HEADER    MEMBRANE PROTEIN/HYDROLASE              24-JUN-13   4LDL              
TITLE     STRUCTURE OF BETA2 ADRENOCEPTOR BOUND TO HYDROXYBENZYLISOPROTERENOL   
TITLE    2 AND AN ENGINEERED NANOBODY                                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: LYSOZYME, BETA-2 ADRENERGIC RECEPTOR;                      
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: ENDOLYSIN, LYSIS PROTEIN, MURAMIDASE, BETA-2 ADRENORECEPTOR,
COMPND   5 BETA-2 ADRENOCEPTOR;                                                 
COMPND   6 EC: 3.2.1.17;                                                        
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MUTATION: YES;                                                       
COMPND   9 MOL_ID: 2;                                                           
COMPND  10 MOLECULE: CAMELID ANTIBODY FRAGMENT;                                 
COMPND  11 CHAIN: B;                                                            
COMPND  12 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ENTEROBACTERIA PHAGE T4, HOMO SAPIENS;          
SOURCE   3 ORGANISM_TAXID: 10665, 9606;                                         
SOURCE   4 GENE: ADRB2;                                                         
SOURCE   5 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   6 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: SF9;                                       
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PVL1392;                                  
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: LAMA GLAMA;                                     
SOURCE  13 ORGANISM_COMMON: LLAMA;                                              
SOURCE  14 ORGANISM_TAXID: 9844;                                                
SOURCE  15 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  16 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  17 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE  18 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  19 EXPRESSION_SYSTEM_PLASMID: PET26B                                    
KEYWDS    G PROTEIN COUPLED RECEPTOR, MEMBRANE PROTEIN-HYDROLASE COMPLEX        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.M.RING,A.MANGLIK,A.C.KRUSE,M.D.ENOS,W.I.WEIS,K.C.GARCIA,B.K.KOBILKA 
REVDAT   3   09-AUG-17 4LDL    1       SOURCE REMARK                            
REVDAT   2   30-OCT-13 4LDL    1       JRNL                                     
REVDAT   1   25-SEP-13 4LDL    0                                                
JRNL        AUTH   A.M.RING,A.MANGLIK,A.C.KRUSE,M.D.ENOS,W.I.WEIS,K.C.GARCIA,   
JRNL        AUTH 2 B.K.KOBILKA                                                  
JRNL        TITL   ADRENALINE-ACTIVATED STRUCTURE OF BETA 2-ADRENOCEPTOR        
JRNL        TITL 2 STABILIZED BY AN ENGINEERED NANOBODY.                        
JRNL        REF    NATURE                        V. 502   575 2013              
JRNL        REFN                   ISSN 0028-0836                               
JRNL        PMID   24056936                                                     
JRNL        DOI    10.1038/NATURE12572                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: DEV_1243)                     
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 33.27                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.380                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 90.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 18053                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.230                           
REMARK   3   R VALUE            (WORKING SET) : 0.229                           
REMARK   3   FREE R VALUE                     : 0.254                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 876                             
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 33.2665 -  7.0764    0.91     2496   143  0.1827 0.2116        
REMARK   3     2  7.0764 -  5.6256    0.90     2529   135  0.2317 0.2299        
REMARK   3     3  5.6256 -  4.9170    0.90     2488   134  0.1989 0.2384        
REMARK   3     4  4.9170 -  4.4686    0.92     2551   143  0.1843 0.2583        
REMARK   3     5  4.4686 -  4.1490    0.93     2533   136  0.1830 0.1846        
REMARK   3     6  4.1490 -  3.9048    0.92     2587   147  0.2139 0.2410        
REMARK   3     7  3.9048 -  3.7095    0.91     2557   127  0.2386 0.2539        
REMARK   3     8  3.7095 -  3.5482    0.94     2583   135  0.2581 0.2996        
REMARK   3     9  3.5482 -  3.4117    0.91     2572   139  0.2925 0.2963        
REMARK   3    10  3.4117 -  3.2941    0.91     2515   131  0.3192 0.3789        
REMARK   3    11  3.2941 -  3.1912    0.84     2361   122  0.3451 0.3319        
REMARK   3    12  3.1912 -  3.1000    0.86     2379   128  0.3632 0.3914        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.450            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.170           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.003           4622                                  
REMARK   3   ANGLE     :  0.590           6274                                  
REMARK   3   CHIRALITY :  0.042            722                                  
REMARK   3   PLANARITY :  0.002            781                                  
REMARK   3   DIHEDRAL  :  9.281           1604                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 8                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 858 THROUGH 1023 )                
REMARK   3    ORIGIN FOR THE GROUP (A): -16.0277 -29.5091 -77.6583              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4733 T22:   0.3899                                     
REMARK   3      T33:   0.5518 T12:   0.0483                                     
REMARK   3      T13:  -0.0236 T23:  -0.0085                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.0774 L22:   6.9243                                     
REMARK   3      L33:   2.5219 L12:   5.4055                                     
REMARK   3      L13:   0.6478 L23:   1.6548                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0293 S12:   0.2568 S13:  -0.2740                       
REMARK   3      S21:   0.2155 S22:   0.1828 S23:  -0.2279                       
REMARK   3      S31:   0.0858 S32:   0.1006 S33:  -0.2349                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 1024 THROUGH 1231 )               
REMARK   3    ORIGIN FOR THE GROUP (A):  -3.4208 -10.9940 -40.5645              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4704 T22:   0.4905                                     
REMARK   3      T33:   0.3481 T12:   0.0289                                     
REMARK   3      T13:   0.0285 T23:  -0.0744                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1447 L22:   1.2527                                     
REMARK   3      L33:   5.2329 L12:   0.1270                                     
REMARK   3      L13:   0.8674 L23:  -1.0026                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0288 S12:  -0.2786 S13:   0.1274                       
REMARK   3      S21:   0.1520 S22:  -0.0910 S23:   0.0126                       
REMARK   3      S31:  -0.2591 S32:   0.1187 S33:   0.0553                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 1263 THROUGH 1298 )               
REMARK   3    ORIGIN FOR THE GROUP (A):   0.0598 -25.3169 -35.7801              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5409 T22:   0.9991                                     
REMARK   3      T33:   0.5749 T12:  -0.0037                                     
REMARK   3      T13:  -0.0233 T23:  -0.2430                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.1644 L22:   4.0982                                     
REMARK   3      L33:   0.7526 L12:  -0.1757                                     
REMARK   3      L13:  -0.6487 L23:  -0.6843                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1014 S12:  -0.5535 S13:  -0.2791                       
REMARK   3      S21:  -0.0702 S22:  -0.2211 S23:  -0.7285                       
REMARK   3      S31:   0.0580 S32:  -0.4834 S33:   0.3258                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 1299 THROUGH 1304 )               
REMARK   3    ORIGIN FOR THE GROUP (A):   1.3955 -24.7169 -60.2710              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0530 T22:   1.6877                                     
REMARK   3      T33:   0.9354 T12:  -0.0893                                     
REMARK   3      T13:  -0.2586 T23:  -0.0523                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.7266 L22:   5.0315                                     
REMARK   3      L33:   2.0013 L12:  -4.5322                                     
REMARK   3      L13:  -5.1272 L23:  -1.3931                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.7207 S12:   1.1542 S13:   1.0556                       
REMARK   3      S21:  -0.8506 S22:   0.3387 S23:  -0.3431                       
REMARK   3      S31:   0.4019 S32:   0.5600 S33:   0.3812                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 1305 THROUGH 1342 )               
REMARK   3    ORIGIN FOR THE GROUP (A): -12.2479 -17.1836 -33.7019              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5458 T22:   0.8207                                     
REMARK   3      T33:   0.4203 T12:  -0.1992                                     
REMARK   3      T13:   0.0007 T23:  -0.1170                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.7363 L22:   3.5730                                     
REMARK   3      L33:   8.4024 L12:  -1.0201                                     
REMARK   3      L13:  -3.4053 L23:   1.0232                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2031 S12:   0.1277 S13:  -0.1575                       
REMARK   3      S21:   0.4691 S22:  -0.4627 S23:   0.3525                       
REMARK   3      S31:   0.6228 S32:  -1.8624 S33:   0.6485                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 1 THROUGH 52 )                    
REMARK   3    ORIGIN FOR THE GROUP (A):  -1.1181 -17.4581   1.8390              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4557 T22:   1.0324                                     
REMARK   3      T33:   0.4648 T12:  -0.0805                                     
REMARK   3      T13:  -0.0443 T23:   0.0279                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8306 L22:   2.8639                                     
REMARK   3      L33:   8.0049 L12:  -0.6207                                     
REMARK   3      L13:  -1.3245 L23:   2.8446                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0730 S12:   0.1073 S13:  -0.0547                       
REMARK   3      S21:   0.1243 S22:   0.0709 S23:  -0.0536                       
REMARK   3      S31:   0.0474 S32:   0.1429 S33:  -0.0745                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 53 THROUGH 76 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):   8.2045 -16.1964  -0.1657              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8515 T22:   1.2072                                     
REMARK   3      T33:   0.5406 T12:  -0.0929                                     
REMARK   3      T13:  -0.1367 T23:  -0.1836                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.7921 L22:   0.8659                                     
REMARK   3      L33:   5.0293 L12:   0.3587                                     
REMARK   3      L13:  -0.4368 L23:   0.1421                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0569 S12:   0.5008 S13:  -0.3482                       
REMARK   3      S21:   0.0752 S22:  -0.0677 S23:  -0.0114                       
REMARK   3      S31:   0.3263 S32:   0.6221 S33:   0.0520                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 77 THROUGH 120 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  -1.8949 -15.6956   1.1580              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5909 T22:   1.1065                                     
REMARK   3      T33:   0.5391 T12:   0.0682                                     
REMARK   3      T13:  -0.0275 T23:  -0.0265                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.8177 L22:   3.2179                                     
REMARK   3      L33:   2.7920 L12:  -2.0715                                     
REMARK   3      L13:  -2.0214 L23:   0.8187                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2609 S12:  -0.5220 S13:   0.0939                       
REMARK   3      S21:   0.5546 S22:   0.2709 S23:   0.0219                       
REMARK   3      S31:   0.0760 S32:  -1.0733 S33:   0.0804                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4LDL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-JUL-13.                  
REMARK 100 THE DEPOSITION ID IS D_1000080495.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 13-DEC-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 78                                 
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 9                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 23-ID-B                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.033                              
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL CRYO-COOLED         
REMARK 200                                   SI(111)                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 300 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : PHENIX (PHENIX.REFINE: DEV_1241)   
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 18053                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 33.300                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.5                               
REMARK 200  DATA REDUNDANCY                : 4.600                              
REMARK 200  R MERGE                    (I) : 0.17700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 6.2000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.20                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.65900                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.900                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 4LDE                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 67.35                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.77                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM MES PH 6.2-6.7, 40-100 MM         
REMARK 280  AMMONIUM PHOSPHATE DIBASIC, 18-24% PEG400, LIPIDIC CUBIC PHASE,     
REMARK 280  TEMPERATURE 293K, PH 6.5                                            
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       24.83500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      151.55000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       33.24000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      151.55000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       24.83500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       33.24000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2310 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 28200 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -19.0 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 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     ASP A   852                                                      
REMARK 465     TYR A   853                                                      
REMARK 465     LYS A   854                                                      
REMARK 465     ASP A   855                                                      
REMARK 465     ASP A   856                                                      
REMARK 465     ASP A   857                                                      
REMARK 465     LYS A  1260                                                      
REMARK 465     ILE A  1261                                                      
REMARK 465     ASP A  1262                                                      
REMARK 465     ARG A  1343                                                      
REMARK 465     ARG A  1344                                                      
REMARK 465     SER A  1345                                                      
REMARK 465     SER A  1346                                                      
REMARK 465     LEU A  1347                                                      
REMARK 465     LYS A  1348                                                      
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     ASP A 858    CG   OD1  OD2                                       
REMARK 470     LYS A1060    CG   CD   CE   NZ                                   
REMARK 470     GLU A1062    CG   CD   OE1  OE2                                  
REMARK 470     ARG A1063    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A1149    CG   CD   CE   NZ                                   
REMARK 470     PHE A1223    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     GLN A1224    CG   CD   OE1  NE2                                  
REMARK 470     LYS A1227    CG   CD   CE   NZ                                   
REMARK 470     GLN A1231    CG   CD   OE1  NE2                                  
REMARK 470     LYS A1263    CG   CD   CE   NZ                                   
REMARK 470     PHE A1264    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LEU A1266    CG   CD1  CD2                                       
REMARK 470     LYS A1270    CG   CD   CE   NZ                                   
REMARK 470     GLN A1299    CD   OE1  NE2                                       
REMARK 470     GLN B   1    CG   CD   OE1  NE2                                  
REMARK 470     GLN B  13    CG   CD   OE1  NE2                                  
REMARK 470     SER B  25    OG                                                  
REMARK 470     LYS B  64    CG   CD   CE   NZ                                   
REMARK 470     SER B 120    OG                                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OE2  GLU A   876     NH1  ARG A  1010              2.02            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASN A 861       27.59   -140.23                                   
REMARK 500    PHE A 864       83.39     72.92                                   
REMARK 500    ILE A 894       77.55   -100.88                                   
REMARK 500    SER A 955       32.07    -93.41                                   
REMARK 500    ARG A 990       79.66   -101.99                                   
REMARK 500    LYS A1097      -21.47     65.54                                   
REMARK 500    THR A1098     -163.99   -128.86                                   
REMARK 500    THR A1100       55.60   -118.11                                   
REMARK 500    PHE A1101       -8.16   -145.64                                   
REMARK 500    SER A1165      -79.84   -121.80                                   
REMARK 500    PHE A1208      -56.91   -123.11                                   
REMARK 500    ALA A1265     -159.71    -90.98                                   
REMARK 500    ILE A1298      -74.58    -89.67                                   
REMARK 500    CYS A1327       43.30   -141.04                                   
REMARK 500    PRO B  41      102.72    -56.12                                   
REMARK 500    ALA B  74       -2.12   -140.40                                   
REMARK 500    PHE B 100       50.20    -95.80                                   
REMARK 500    ILE B 103      -52.02     63.06                                   
REMARK 500    TYR B 105     -168.54   -126.24                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     1WV A 1403                                                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA A1402  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A1184   O                                                      
REMARK 620 2 ASN A1103   OD1 138.5                                              
REMARK 620 3 HOH A1501   O   101.9 101.8                                        
REMARK 620 4 CYS A1190   O    98.5 111.9  96.8                                  
REMARK 620 5 GLU A1187   O    79.1  71.3 168.4  94.4                            
REMARK 620 N                    1     2     3     4                             
REMARK 650                                                                      
REMARK 650 HELIX                                                                
REMARK 650 DETERMINATION METHOD: AUTHOR DETERMINED                              
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE XQC A 1401                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 1402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1WV A 1403                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4LDE   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN COMPLEXED TO BI167107                               
REMARK 900 RELATED ID: 4LDO   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN BOUND TO ADRENALINE AND AN ENGINEERED NANOBODY      
DBREF  4LDL A  867  1026  UNP    P00720   LYS_BPT4         2    161             
DBREF  4LDL A 1029  1263  UNP    P07550   ADRB2_HUMAN     29    235             
DBREF  4LDL A 1264  1348  UNP    P07550   ADRB2_HUMAN    264    348             
DBREF  4LDL B    1   120  PDB    4LDL     4LDL             1    120             
SEQADV 4LDL ASP A  852  UNP  P00720              EXPRESSION TAG                 
SEQADV 4LDL TYR A  853  UNP  P00720              EXPRESSION TAG                 
SEQADV 4LDL LYS A  854  UNP  P00720              EXPRESSION TAG                 
SEQADV 4LDL ASP A  855  UNP  P00720              EXPRESSION TAG                 
SEQADV 4LDL ASP A  856  UNP  P00720              EXPRESSION TAG                 
SEQADV 4LDL ASP A  857  UNP  P00720              EXPRESSION TAG                 
SEQADV 4LDL ASP A  858  UNP  P00720              EXPRESSION TAG                 
SEQADV 4LDL ALA A  859  UNP  P00720              EXPRESSION TAG                 
SEQADV 4LDL GLU A  860  UNP  P00720              EXPRESSION TAG                 
SEQADV 4LDL ASN A  861  UNP  P00720              EXPRESSION TAG                 
SEQADV 4LDL LEU A  862  UNP  P00720              EXPRESSION TAG                 
SEQADV 4LDL TYR A  863  UNP  P00720              EXPRESSION TAG                 
SEQADV 4LDL PHE A  864  UNP  P00720              EXPRESSION TAG                 
SEQADV 4LDL GLN A  865  UNP  P00720              EXPRESSION TAG                 
SEQADV 4LDL GLY A  866  UNP  P00720              EXPRESSION TAG                 
SEQADV 4LDL THR A  919  UNP  P00720    CYS    54 ENGINEERED MUTATION            
SEQADV 4LDL ALA A  962  UNP  P00720    CYS    97 ENGINEERED MUTATION            
SEQADV 4LDL ALA A 1027  UNP  P00720              LINKER                         
SEQADV 4LDL ALA A 1028  UNP  P00720              LINKER                         
SEQADV 4LDL THR A 1096  UNP  P07550    MET    96 ENGINEERED MUTATION            
SEQADV 4LDL THR A 1098  UNP  P07550    MET    98 ENGINEERED MUTATION            
SEQADV 4LDL GLU A 1187  UNP  P07550    ASN   187 ENGINEERED MUTATION            
SEQADV 4LDL ALA A 1265  UNP  P07550    CYS   265 ENGINEERED MUTATION            
SEQRES   1 A  469  ASP TYR LYS ASP ASP ASP ASP ALA GLU ASN LEU TYR PHE          
SEQRES   2 A  469  GLN GLY ASN ILE PHE GLU MET LEU ARG ILE ASP GLU GLY          
SEQRES   3 A  469  LEU ARG LEU LYS ILE TYR LYS ASP THR GLU GLY TYR TYR          
SEQRES   4 A  469  THR ILE GLY ILE GLY HIS LEU LEU THR LYS SER PRO SER          
SEQRES   5 A  469  LEU ASN ALA ALA LYS SER GLU LEU ASP LYS ALA ILE GLY          
SEQRES   6 A  469  ARG ASN THR ASN GLY VAL ILE THR LYS ASP GLU ALA GLU          
SEQRES   7 A  469  LYS LEU PHE ASN GLN ASP VAL ASP ALA ALA VAL ARG GLY          
SEQRES   8 A  469  ILE LEU ARG ASN ALA LYS LEU LYS PRO VAL TYR ASP SER          
SEQRES   9 A  469  LEU ASP ALA VAL ARG ARG ALA ALA LEU ILE ASN MET VAL          
SEQRES  10 A  469  PHE GLN MET GLY GLU THR GLY VAL ALA GLY PHE THR ASN          
SEQRES  11 A  469  SER LEU ARG MET LEU GLN GLN LYS ARG TRP ASP GLU ALA          
SEQRES  12 A  469  ALA VAL ASN LEU ALA LYS SER ARG TRP TYR ASN GLN THR          
SEQRES  13 A  469  PRO ASN ARG ALA LYS ARG VAL ILE THR THR PHE ARG THR          
SEQRES  14 A  469  GLY THR TRP ASP ALA TYR ALA ALA ASP GLU VAL TRP VAL          
SEQRES  15 A  469  VAL GLY MET GLY ILE VAL MET SER LEU ILE VAL LEU ALA          
SEQRES  16 A  469  ILE VAL PHE GLY ASN VAL LEU VAL ILE THR ALA ILE ALA          
SEQRES  17 A  469  LYS PHE GLU ARG LEU GLN THR VAL THR ASN TYR PHE ILE          
SEQRES  18 A  469  THR SER LEU ALA CYS ALA ASP LEU VAL MET GLY LEU ALA          
SEQRES  19 A  469  VAL VAL PRO PHE GLY ALA ALA HIS ILE LEU THR LYS THR          
SEQRES  20 A  469  TRP THR PHE GLY ASN PHE TRP CYS GLU PHE TRP THR SER          
SEQRES  21 A  469  ILE ASP VAL LEU CYS VAL THR ALA SER ILE GLU THR LEU          
SEQRES  22 A  469  CYS VAL ILE ALA VAL ASP ARG TYR PHE ALA ILE THR SER          
SEQRES  23 A  469  PRO PHE LYS TYR GLN SER LEU LEU THR LYS ASN LYS ALA          
SEQRES  24 A  469  ARG VAL ILE ILE LEU MET VAL TRP ILE VAL SER GLY LEU          
SEQRES  25 A  469  THR SER PHE LEU PRO ILE GLN MET HIS TRP TYR ARG ALA          
SEQRES  26 A  469  THR HIS GLN GLU ALA ILE ASN CYS TYR ALA GLU GLU THR          
SEQRES  27 A  469  CYS CYS ASP PHE PHE THR ASN GLN ALA TYR ALA ILE ALA          
SEQRES  28 A  469  SER SER ILE VAL SER PHE TYR VAL PRO LEU VAL ILE MET          
SEQRES  29 A  469  VAL PHE VAL TYR SER ARG VAL PHE GLN GLU ALA LYS ARG          
SEQRES  30 A  469  GLN LEU GLN LYS ILE ASP LYS PHE ALA LEU LYS GLU HIS          
SEQRES  31 A  469  LYS ALA LEU LYS THR LEU GLY ILE ILE MET GLY THR PHE          
SEQRES  32 A  469  THR LEU CYS TRP LEU PRO PHE PHE ILE VAL ASN ILE VAL          
SEQRES  33 A  469  HIS VAL ILE GLN ASP ASN LEU ILE ARG LYS GLU VAL TYR          
SEQRES  34 A  469  ILE LEU LEU ASN TRP ILE GLY TYR VAL ASN SER GLY PHE          
SEQRES  35 A  469  ASN PRO LEU ILE TYR CYS ARG SER PRO ASP PHE ARG ILE          
SEQRES  36 A  469  ALA PHE GLN GLU LEU LEU CYS LEU ARG ARG SER SER LEU          
SEQRES  37 A  469  LYS                                                          
SEQRES   1 B  120  GLN VAL GLN LEU GLN GLU SER GLY GLY GLY LEU VAL GLN          
SEQRES   2 B  120  ALA GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY          
SEQRES   3 B  120  SER ILE PHE ALA LEU ASN ILE MET GLY TRP TYR ARG GLN          
SEQRES   4 B  120  ALA PRO GLY LYS GLN ARG GLU LEU VAL ALA ALA ILE HIS          
SEQRES   5 B  120  SER GLY GLY THR THR ASN TYR ALA ASN SER VAL LYS GLY          
SEQRES   6 B  120  ARG PHE THR ILE SER ARG ASP ASN ALA ALA ASN THR VAL          
SEQRES   7 B  120  TYR LEU GLN MET ASN SER LEU LYS PRO GLU ASP THR ALA          
SEQRES   8 B  120  VAL TYR TYR CYS ASN VAL LYS ASP PHE GLY ALA ILE ILE          
SEQRES   9 B  120  TYR ASP TYR ASP TYR TRP GLY GLN GLY THR GLN VAL THR          
SEQRES  10 B  120  VAL SER SER                                                  
HET    XQC  A1401      23                                                       
HET     NA  A1402       1                                                       
HET    1WV  A1403      15                                                       
HETNAM     XQC 4-[(1R)-1-HYDROXY-2-{[1-(4-HYDROXYPHENYL)-2-                     
HETNAM   2 XQC  METHYLPROPAN-2-YL]AMINO}ETHYL]BENZENE-1,2-DIOL                  
HETNAM      NA SODIUM ION                                                       
HETNAM     1WV (2S)-2,3-DIHYDROXYPROPYL (7Z)-TETRADEC-7-ENOATE                  
FORMUL   3  XQC    C18 H23 N O4                                                 
FORMUL   4   NA    NA 1+                                                        
FORMUL   5  1WV    C17 H32 O4                                                   
FORMUL   6  HOH   *2(H2 O)                                                      
HELIX    1   1 ASN A  867  GLU A  876  1                                  10    
HELIX    2   2 SER A  903  GLY A  916  1                                  14    
HELIX    3   3 THR A  924  ASN A  946  1                                  23    
HELIX    4   4 LEU A  949  SER A  955  1                                   7    
HELIX    5   5 ASP A  957  MET A  971  1                                  15    
HELIX    6   6 GLU A  973  GLY A  978  1                                   6    
HELIX    7   7 THR A  980  GLN A  988  1                                   9    
HELIX    8   8 ARG A  990  ALA A  999  1                                  10    
HELIX    9   9 ARG A 1002  GLN A 1006  1                                   5    
HELIX   10  10 PRO A 1008  GLY A 1021  1                                  14    
HELIX   11  11 ASP A 1029  PHE A 1061  1                                  33    
HELIX   12  12 THR A 1066  ALA A 1085  1                                  20    
HELIX   13  13 ALA A 1085  THR A 1096  1                                  12    
HELIX   14  14 GLY A 1102  THR A 1136  1                                  35    
HELIX   15  15 PRO A 1138  LEU A 1144  1                                   7    
HELIX   16  16 LYS A 1147  THR A 1164  1                                  18    
HELIX   17  17 SER A 1165  MET A 1171  1                                   7    
HELIX   18  18 HIS A 1178  GLU A 1187  1                                  10    
HELIX   19  19 ASN A 1196  PHE A 1208  1                                  13    
HELIX   20  20 PHE A 1208  ALA A 1226  1                                  19    
HELIX   21  21 LYS A 1227  GLN A 1229  5                                   3    
HELIX   22  22 LEU A 1266  GLN A 1299  1                                  34    
HELIX   23  23 ARG A 1304  VAL A 1317  1                                  14    
HELIX   24  24 VAL A 1317  ASN A 1322  1                                   6    
HELIX   25  25 PRO A 1323  ILE A 1325  5                                   3    
HELIX   26  26 SER A 1329  LEU A 1340  1                                  12    
HELIX   27  27 LYS B   86  THR B   90  5                                   5    
SHEET    1   A 3 ARG A 879  LYS A 884  0                                        
SHEET    2   A 3 TYR A 890  GLY A 893 -1  O  THR A 891   N  TYR A 883           
SHEET    3   A 3 HIS A 896  THR A 899 -1  O  LEU A 898   N  TYR A 890           
SHEET    1   B 4 GLN B   3  SER B   7  0                                        
SHEET    2   B 4 LEU B  18  SER B  25 -1  O  ALA B  23   N  GLN B   5           
SHEET    3   B 4 THR B  77  MET B  82 -1  O  MET B  82   N  LEU B  18           
SHEET    4   B 4 PHE B  67  ARG B  71 -1  N  THR B  68   O  GLN B  81           
SHEET    1   C 6 GLY B  10  GLN B  13  0                                        
SHEET    2   C 6 THR B 114  SER B 119  1  O  SER B 119   N  VAL B  12           
SHEET    3   C 6 ALA B  91  ASP B  99 -1  N  TYR B  93   O  THR B 114           
SHEET    4   C 6 ASN B  32  GLN B  39 -1  N  TYR B  37   O  TYR B  94           
SHEET    5   C 6 ARG B  45  HIS B  52 -1  O  GLU B  46   N  ARG B  38           
SHEET    6   C 6 THR B  57  TYR B  59 -1  O  ASN B  58   N  ALA B  50           
SHEET    1   D 4 GLY B  10  GLN B  13  0                                        
SHEET    2   D 4 THR B 114  SER B 119  1  O  SER B 119   N  VAL B  12           
SHEET    3   D 4 ALA B  91  ASP B  99 -1  N  TYR B  93   O  THR B 114           
SHEET    4   D 4 TYR B 107  TRP B 110 -1  O  TYR B 107   N  ASP B  99           
SSBOND   1 CYS A 1106    CYS A 1191                          1555   1555  2.03  
SSBOND   2 CYS A 1184    CYS A 1190                          1555   1555  2.03  
SSBOND   3 CYS B   22    CYS B   95                          1555   1555  2.03  
LINK         O   CYS A1184                NA    NA A1402     1555   1555  2.38  
LINK         OD1 ASN A1103                NA    NA A1402     1555   1555  2.39  
LINK        NA    NA A1402                 O   HOH A1501     1555   1555  2.39  
LINK         O   CYS A1190                NA    NA A1402     1555   1555  2.40  
LINK         O   GLU A1187                NA    NA A1402     1555   1555  2.41  
SITE     1 AC1 11 ASP A1113  CYS A1191  ASP A1192  PHE A1193                    
SITE     2 AC1 11 SER A1203  SER A1207  PHE A1289  ASN A1293                    
SITE     3 AC1 11 ILE A1309  ASN A1312  TYR A1316                               
SITE     1 AC2  6 ASN A1103  CYS A1184  TYR A1185  GLU A1187                    
SITE     2 AC2  6 CYS A1190  HOH A1501                                          
SITE     1 AC3  2 GLU A1306  TRP A1313                                          
CRYST1   49.670   66.480  303.100  90.00  90.00  90.00 P 21 21 21    4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.020133  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.015042  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003299        0.00000                         
ATOM      1  N   ASP A 858     -38.706 -16.950 -74.761  1.00146.84           N  
ANISOU    1  N   ASP A 858    12718  13716  29357    968    773  -2455       N  
ATOM      2  CA  ASP A 858     -38.554 -18.082 -73.854  1.00141.65           C  
ANISOU    2  CA  ASP A 858    12300  13413  28109    786   1360  -2806       C  
ATOM      3  C   ASP A 858     -38.762 -17.661 -72.401  1.00149.48           C  
ANISOU    3  C   ASP A 858    13225  14316  29256    507   2084  -3465       C  
ATOM      4  O   ASP A 858     -39.062 -18.494 -71.544  1.00149.13           O  
ANISOU    4  O   ASP A 858    13282  14471  28909    248   2607  -3870       O  
ATOM      5  CB  ASP A 858     -37.176 -18.723 -74.023  1.00128.16           C  
ANISOU    5  CB  ASP A 858    11118  12083  25494    843   1312  -2478       C  
ATOM      6  N   ALA A 859     -38.600 -16.364 -72.141  1.00155.74           N  
ANISOU    6  N   ALA A 859    13863  14815  30497    514   2107  -3566       N  
ATOM      7  CA  ALA A 859     -38.741 -15.793 -70.801  1.00157.52           C  
ANISOU    7  CA  ALA A 859    14010  14934  30906    207   2776  -4182       C  
ATOM      8  C   ALA A 859     -37.829 -16.466 -69.775  1.00152.87           C  
ANISOU    8  C   ALA A 859    13943  14743  29397    -67   3320  -4385       C  
ATOM      9  O   ALA A 859     -38.195 -16.619 -68.609  1.00155.47           O  
ANISOU    9  O   ALA A 859    14293  15118  29663   -462   3941  -4938       O  
ATOM     10  CB  ALA A 859     -40.198 -15.836 -70.342  1.00160.89           C  
ANISOU   10  CB  ALA A 859    13969  15108  32055      9   3075  -4716       C  
ATOM     11  N   GLU A 860     -36.640 -16.861 -70.218  1.00143.60           N  
ANISOU   11  N   GLU A 860    13207  13841  27514    101   3069  -3938       N  
ATOM     12  CA  GLU A 860     -35.677 -17.530 -69.351  1.00135.70           C  
ANISOU   12  CA  GLU A 860    12738  13195  25628   -139   3489  -4057       C  
ATOM     13  C   GLU A 860     -34.508 -16.611 -69.018  1.00127.74           C  
ANISOU   13  C   GLU A 860    11993  12168  24375   -131   3538  -3979       C  
ATOM     14  O   GLU A 860     -33.651 -16.354 -69.863  1.00117.72           O  
ANISOU   14  O   GLU A 860    10881  10901  22946    172   3076  -3507       O  
ATOM     15  CB  GLU A 860     -35.155 -18.805 -70.017  1.00132.64           C  
ANISOU   15  CB  GLU A 860    12670  13122  24606     16   3219  -3667       C  
ATOM     16  CG  GLU A 860     -36.237 -19.797 -70.409  1.00136.93           C  
ANISOU   16  CG  GLU A 860    12981  13726  25320     11   3154  -3706       C  
ATOM     17  CD  GLU A 860     -35.680 -21.009 -71.132  1.00131.69           C  
ANISOU   17  CD  GLU A 860    12594  13365  24076    167   2878  -3309       C  
ATOM     18  OE1 GLU A 860     -34.442 -21.099 -71.276  1.00123.55           O  
ANISOU   18  OE1 GLU A 860    11946  12473  22524    269   2761  -3038       O  
ATOM     19  OE2 GLU A 860     -36.479 -21.871 -71.558  1.00133.32           O  
ANISOU   19  OE2 GLU A 860    12624  13656  24375    175   2784  -3286       O  
ATOM     20  N   ASN A 861     -34.474 -16.121 -67.783  1.00130.66           N  
ANISOU   20  N   ASN A 861    12425  12522  24697   -507   4103  -4450       N  
ATOM     21  CA  ASN A 861     -33.380 -15.265 -67.339  1.00128.35           C  
ANISOU   21  CA  ASN A 861    12400  12232  24137   -558   4210  -4428       C  
ATOM     22  C   ASN A 861     -32.948 -15.571 -65.906  1.00129.62           C  
ANISOU   22  C   ASN A 861    12971  12640  23639  -1091   4840  -4827       C  
ATOM     23  O   ASN A 861     -32.443 -14.699 -65.199  1.00130.45           O  
ANISOU   23  O   ASN A 861    13174  12697  23695  -1294   5108  -5016       O  
ATOM     24  CB  ASN A 861     -33.754 -13.787 -67.483  1.00132.45           C  
ANISOU   24  CB  ASN A 861    12473  12359  25492   -444   4127  -4523       C  
ATOM     25  CG  ASN A 861     -32.641 -12.963 -68.108  1.00129.92           C  
ANISOU   25  CG  ASN A 861    12330  11967  25065   -150   3730  -4103       C  
ATOM     26  OD1 ASN A 861     -31.705 -12.544 -67.427  1.00129.33           O  
ANISOU   26  OD1 ASN A 861    12580  11988  24570   -314   3990  -4200       O  
ATOM     27  ND2 ASN A 861     -32.741 -12.724 -69.411  1.00126.97           N  
ANISOU   27  ND2 ASN A 861    11772  11426  25045    239   3084  -3630       N  
ATOM     28  N   LEU A 862     -33.152 -16.816 -65.486  1.00130.61           N  
ANISOU   28  N   LEU A 862    13358  13033  23234  -1360   5054  -4935       N  
ATOM     29  CA  LEU A 862     -32.685 -17.275 -64.182  1.00130.42           C  
ANISOU   29  CA  LEU A 862    13834  13282  22437  -1939   5553  -5213       C  
ATOM     30  C   LEU A 862     -31.514 -18.238 -64.360  1.00128.82           C  
ANISOU   30  C   LEU A 862    14233  13377  21334  -1882   5326  -4836       C  
ATOM     31  O   LEU A 862     -31.438 -18.945 -65.364  1.00123.42           O  
ANISOU   31  O   LEU A 862    13535  12730  20629  -1496   4924  -4489       O  
ATOM     32  CB  LEU A 862     -33.822 -17.930 -63.399  1.00130.56           C  
ANISOU   32  CB  LEU A 862    13760  13355  22491  -2427   5996  -5664       C  
ATOM     33  CG  LEU A 862     -35.031 -17.020 -63.162  1.00139.17           C  
ANISOU   33  CG  LEU A 862    14245  14101  24533  -2535   6254  -6125       C  
ATOM     34  CD1 LEU A 862     -36.047 -17.679 -62.238  1.00145.21           C  
ANISOU   34  CD1 LEU A 862    15009  14920  25245  -3125   6752  -6641       C  
ATOM     35  CD2 LEU A 862     -34.591 -15.670 -62.612  1.00141.92           C  
ANISOU   35  CD2 LEU A 862    14510  14285  25129  -2661   6475  -6311       C  
ATOM     36  N   TYR A 863     -30.612 -18.253 -63.380  1.00133.79           N  
ANISOU   36  N   TYR A 863    15389  14201  21243  -2302   5568  -4910       N  
ATOM     37  CA  TYR A 863     -29.314 -18.929 -63.484  1.00131.01           C  
ANISOU   37  CA  TYR A 863    15643  14057  20078  -2274   5297  -4563       C  
ATOM     38  C   TYR A 863     -29.371 -20.352 -64.052  1.00132.48           C  
ANISOU   38  C   TYR A 863    16024  14407  19907  -2153   5023  -4296       C  
ATOM     39  O   TYR A 863     -30.250 -21.142 -63.701  1.00134.43           O  
ANISOU   39  O   TYR A 863    16239  14747  20091  -2426   5279  -4516       O  
ATOM     40  CB  TYR A 863     -28.603 -18.928 -62.123  1.00133.56           C  
ANISOU   40  CB  TYR A 863    16527  14597  19625  -2924   5605  -4714       C  
ATOM     41  CG  TYR A 863     -27.089 -18.827 -62.191  1.00132.81           C  
ANISOU   41  CG  TYR A 863    16931  14571  18959  -2861   5276  -4399       C  
ATOM     42  CD1 TYR A 863     -26.402 -19.073 -63.374  1.00126.20           C  
ANISOU   42  CD1 TYR A 863    16059  13748  18143  -2308   4632  -3828       C  
ATOM     43  CD2 TYR A 863     -26.346 -18.483 -61.068  1.00136.85           C  
ANISOU   43  CD2 TYR A 863    17872  15237  18886  -3389   5461  -4478       C  
ATOM     44  CE1 TYR A 863     -25.025 -18.984 -63.438  1.00121.80           C  
ANISOU   44  CE1 TYR A 863    15857  13325  17098  -2262   4232  -3422       C  
ATOM     45  CE2 TYR A 863     -24.966 -18.389 -61.123  1.00132.85           C  
ANISOU   45  CE2 TYR A 863    17783  14804  17891  -3355   5083  -4148       C  
ATOM     46  CZ  TYR A 863     -24.311 -18.642 -62.311  1.00125.49           C  
ANISOU   46  CZ  TYR A 863    16743  13892  17047  -2763   4442  -3575       C  
ATOM     47  OH  TYR A 863     -22.939 -18.551 -62.373  1.00124.37           O  
ANISOU   47  OH  TYR A 863    16908  13875  16471  -2715   4021  -3178       O  
ATOM     48  N   PHE A 864     -28.426 -20.637 -64.946  1.00133.03           N  
ANISOU   48  N   PHE A 864    16250  14577  19717  -1776   4389  -3684       N  
ATOM     49  CA  PHE A 864     -28.229 -21.946 -65.575  1.00135.11           C  
ANISOU   49  CA  PHE A 864    16701  15059  19576  -1643   3943  -3226       C  
ATOM     50  C   PHE A 864     -29.281 -22.318 -66.618  1.00138.24           C  
ANISOU   50  C   PHE A 864    16627  15367  20531  -1289   3790  -3168       C  
ATOM     51  O   PHE A 864     -30.244 -23.028 -66.327  1.00139.79           O  
ANISOU   51  O   PHE A 864    16734  15611  20768  -1498   4048  -3408       O  
ATOM     52  CB  PHE A 864     -28.061 -23.065 -64.539  1.00135.73           C  
ANISOU   52  CB  PHE A 864    17309  15383  18881  -2192   4084  -3253       C  
ATOM     53  CG  PHE A 864     -27.627 -24.376 -65.134  1.00132.36           C  
ANISOU   53  CG  PHE A 864    17115  15133  18043  -2048   3584  -2758       C  
ATOM     54  CD1 PHE A 864     -26.342 -24.533 -65.629  1.00126.05           C  
ANISOU   54  CD1 PHE A 864    16535  14410  16947  -1809   3076  -2288       C  
ATOM     55  CD2 PHE A 864     -28.501 -25.449 -65.199  1.00131.61           C  
ANISOU   55  CD2 PHE A 864    16996  15110  17899  -2165   3649  -2801       C  
ATOM     56  CE1 PHE A 864     -25.936 -25.735 -66.179  1.00117.40           C  
ANISOU   56  CE1 PHE A 864    15608  13435  15565  -1677   2658  -1897       C  
ATOM     57  CE2 PHE A 864     -28.100 -26.655 -65.748  1.00125.43           C  
ANISOU   57  CE2 PHE A 864    16420  14453  16785  -2036   3209  -2375       C  
ATOM     58  CZ  PHE A 864     -26.816 -26.797 -66.239  1.00117.98           C  
ANISOU   58  CZ  PHE A 864    15670  13558  15598  -1786   2721  -1936       C  
ATOM     59  N   GLN A 865     -29.077 -21.829 -67.838  1.00138.25           N  
ANISOU   59  N   GLN A 865    16349  15247  20932   -799   3354  -2838       N  
ATOM     60  CA  GLN A 865     -29.878 -22.241 -68.981  1.00140.46           C  
ANISOU   60  CA  GLN A 865    16258  15479  21632   -479   3059  -2652       C  
ATOM     61  C   GLN A 865     -29.103 -23.305 -69.750  1.00137.94           C  
ANISOU   61  C   GLN A 865    16252  15410  20748   -360   2580  -2145       C  
ATOM     62  O   GLN A 865     -27.905 -23.156 -69.988  1.00138.76           O  
ANISOU   62  O   GLN A 865    16627  15595  20499   -275   2307  -1850       O  
ATOM     63  CB  GLN A 865     -30.175 -21.045 -69.889  1.00143.73           C  
ANISOU   63  CB  GLN A 865    16197  15583  22829    -88   2827  -2576       C  
ATOM     64  CG  GLN A 865     -30.861 -19.883 -69.187  1.00150.28           C  
ANISOU   64  CG  GLN A 865    16654  16083  24363   -152   3284  -3099       C  
ATOM     65  CD  GLN A 865     -31.101 -18.703 -70.110  1.00154.00           C  
ANISOU   65  CD  GLN A 865    16679  16202  25634    233   2939  -2938       C  
ATOM     66  OE1 GLN A 865     -30.877 -18.787 -71.317  1.00153.73           O  
ANISOU   66  OE1 GLN A 865    16599  16161  25649    528   2379  -2458       O  
ATOM     67  NE2 GLN A 865     -31.556 -17.592 -69.542  1.00157.56           N  
ANISOU   67  NE2 GLN A 865    16873  16447  26547    108   3165  -3229       N  
ATOM     68  N   GLY A 866     -29.784 -24.381 -70.130  1.00132.56           N  
ANISOU   68  N   GLY A 866    15514  14840  20015   -372   2506  -2084       N  
ATOM     69  CA  GLY A 866     -29.134 -25.492 -70.801  1.00122.98           C  
ANISOU   69  CA  GLY A 866    14578  13837  18310   -298   2123  -1684       C  
ATOM     70  C   GLY A 866     -28.617 -25.159 -72.188  1.00116.45           C  
ANISOU   70  C   GLY A 866    13630  12997  17619     48   1645  -1299       C  
ATOM     71  O   GLY A 866     -29.397 -24.998 -73.127  1.00120.64           O  
ANISOU   71  O   GLY A 866    13812  13443  18585    231   1455  -1215       O  
ATOM     72  N   ASN A 867     -27.297 -25.056 -72.318  1.00106.58           N  
ANISOU   72  N   ASN A 867    12671  11834  15990     93   1441  -1067       N  
ATOM     73  CA  ASN A 867     -26.670 -24.802 -73.614  1.00 98.78           C  
ANISOU   73  CA  ASN A 867    11638  10874  15021    327   1030   -729       C  
ATOM     74  C   ASN A 867     -25.252 -25.363 -73.729  1.00 92.88           C  
ANISOU   74  C   ASN A 867    11239  10300  13750    307    850   -523       C  
ATOM     75  O   ASN A 867     -24.734 -25.973 -72.794  1.00 90.61           O  
ANISOU   75  O   ASN A 867    11230  10088  13109    138    971   -589       O  
ATOM     76  CB  ASN A 867     -26.686 -23.307 -73.949  1.00 97.97           C  
ANISOU   76  CB  ASN A 867    11301  10555  15367    479    955   -714       C  
ATOM     77  CG  ASN A 867     -26.068 -22.454 -72.857  1.00103.73           C  
ANISOU   77  CG  ASN A 867    12173  11201  16038    375   1223   -916       C  
ATOM     78  OD1 ASN A 867     -25.381 -22.958 -71.967  1.00105.24           O  
ANISOU   78  OD1 ASN A 867    12691  11532  15764    181   1374   -986       O  
ATOM     79  ND2 ASN A 867     -26.311 -21.150 -72.921  1.00107.93           N  
ANISOU   79  ND2 ASN A 867    12466  11481  17060    481   1252   -998       N  
ATOM     80  N   ILE A 868     -24.633 -25.144 -74.885  1.00 89.51           N  
ANISOU   80  N   ILE A 868    10788   9921  13302    446    548   -280       N  
ATOM     81  CA  ILE A 868     -23.302 -25.672 -75.170  1.00 82.44           C  
ANISOU   81  CA  ILE A 868    10133   9175  12017    439    391   -135       C  
ATOM     82  C   ILE A 868     -22.193 -24.843 -74.517  1.00 78.23           C  
ANISOU   82  C   ILE A 868     9750   8615  11361    415    434   -158       C  
ATOM     83  O   ILE A 868     -21.167 -25.382 -74.099  1.00 76.05           O  
ANISOU   83  O   ILE A 868     9682   8426  10789    356    392   -132       O  
ATOM     84  CB  ILE A 868     -23.064 -25.773 -76.700  1.00 63.20           C  
ANISOU   84  CB  ILE A 868     7622   6825   9566    507    112     73       C  
ATOM     85  CG1 ILE A 868     -21.643 -26.245 -77.009  1.00 62.38           C  
ANISOU   85  CG1 ILE A 868     7703   6856   9143    485     18    134       C  
ATOM     86  CG2 ILE A 868     -23.339 -24.438 -77.378  1.00 68.98           C  
ANISOU   86  CG2 ILE A 868     8183   7433  10594    571    -33    186       C  
ATOM     87  CD1 ILE A 868     -21.327 -27.619 -76.477  1.00 66.83           C  
ANISOU   87  CD1 ILE A 868     8410   7479   9504    441     68     68       C  
ATOM     88  N   PHE A 869     -22.415 -23.537 -74.411  1.00 78.06           N  
ANISOU   88  N   PHE A 869     9603   8445  11612    456    499   -210       N  
ATOM     89  CA  PHE A 869     -21.393 -22.615 -73.922  1.00 78.51           C  
ANISOU   89  CA  PHE A 869     9787   8471  11572    424    533   -229       C  
ATOM     90  C   PHE A 869     -20.990 -22.862 -72.467  1.00 80.12           C  
ANISOU   90  C   PHE A 869    10222   8704  11514    232    746   -395       C  
ATOM     91  O   PHE A 869     -19.800 -22.938 -72.152  1.00 82.92           O  
ANISOU   91  O   PHE A 869    10771   9147  11588    173    653   -328       O  
ATOM     92  CB  PHE A 869     -21.848 -21.166 -74.111  1.00 77.74           C  
ANISOU   92  CB  PHE A 869     9493   8154  11889    501    563   -264       C  
ATOM     93  CG  PHE A 869     -22.182 -20.820 -75.534  1.00 77.01           C  
ANISOU   93  CG  PHE A 869     9224   8007  12028    624    261    -30       C  
ATOM     94  CD1 PHE A 869     -21.186 -20.461 -76.425  1.00 77.04           C  
ANISOU   94  CD1 PHE A 869     9336   8093  11841    616     26    178       C  
ATOM     95  CD2 PHE A 869     -23.492 -20.859 -75.981  1.00 82.32           C  
ANISOU   95  CD2 PHE A 869     9630   8549  13098    697    195    -18       C  
ATOM     96  CE1 PHE A 869     -21.489 -20.145 -77.735  1.00 80.01           C  
ANISOU   96  CE1 PHE A 869     9618   8432  12349    627   -276    418       C  
ATOM     97  CE2 PHE A 869     -23.803 -20.543 -77.290  1.00 85.21           C  
ANISOU   97  CE2 PHE A 869     9869   8861  13647    748   -159    250       C  
ATOM     98  CZ  PHE A 869     -22.799 -20.185 -78.168  1.00 83.92           C  
ANISOU   98  CZ  PHE A 869     9877   8789  13219    688   -400    480       C  
ATOM     99  N   GLU A 870     -21.976 -22.986 -71.585  1.00 77.63           N  
ANISOU   99  N   GLU A 870     9888   8318  11292     91   1022   -616       N  
ATOM    100  CA  GLU A 870     -21.697 -23.238 -70.175  1.00 80.33           C  
ANISOU  100  CA  GLU A 870    10508   8699  11315   -205   1226   -770       C  
ATOM    101  C   GLU A 870     -21.100 -24.630 -69.979  1.00 80.79           C  
ANISOU  101  C   GLU A 870    10818   8900  10978   -298   1022   -601       C  
ATOM    102  O   GLU A 870     -20.187 -24.819 -69.170  1.00 89.73           O  
ANISOU  102  O   GLU A 870    12222  10082  11790   -484    943   -548       O  
ATOM    103  CB  GLU A 870     -22.963 -23.075 -69.333  1.00 85.90           C  
ANISOU  103  CB  GLU A 870    11132   9304  12202   -409   1626  -1101       C  
ATOM    104  CG  GLU A 870     -22.723 -23.182 -67.835  1.00 96.99           C  
ANISOU  104  CG  GLU A 870    12876  10757  13218   -837   1880  -1293       C  
ATOM    105  CD  GLU A 870     -21.792 -22.102 -67.314  1.00103.31           C  
ANISOU  105  CD  GLU A 870    13807  11526  13919   -934   1926  -1339       C  
ATOM    106  OE1 GLU A 870     -21.205 -22.294 -66.228  1.00104.45           O  
ANISOU  106  OE1 GLU A 870    14306  11758  13623  -1298   1976  -1370       O  
ATOM    107  OE2 GLU A 870     -21.651 -21.059 -67.987  1.00106.60           O  
ANISOU  107  OE2 GLU A 870    13992  11826  14686   -680   1886  -1327       O  
ATOM    108  N   MET A 871     -21.619 -25.597 -70.731  1.00 67.95           N  
ANISOU  108  N   MET A 871     9090   7313   9413   -177    906   -508       N  
ATOM    109  CA  MET A 871     -21.118 -26.967 -70.702  1.00 65.45           C  
ANISOU  109  CA  MET A 871     8962   7074   8833   -221    694   -353       C  
ATOM    110  C   MET A 871     -19.630 -27.011 -71.045  1.00 69.42           C  
ANISOU  110  C   MET A 871     9529   7619   9229   -109    407   -177       C  
ATOM    111  O   MET A 871     -18.830 -27.628 -70.334  1.00 68.03           O  
ANISOU  111  O   MET A 871     9572   7440   8835   -240    245    -87       O  
ATOM    112  CB  MET A 871     -21.911 -27.831 -71.685  1.00 62.64           C  
ANISOU  112  CB  MET A 871     8436   6744   8619    -83    635   -307       C  
ATOM    113  CG  MET A 871     -21.472 -29.284 -71.754  1.00 64.22           C  
ANISOU  113  CG  MET A 871     8795   6974   8632   -108    432   -175       C  
ATOM    114  SD  MET A 871     -22.367 -30.195 -73.029  1.00 55.96           S  
ANISOU  114  SD  MET A 871     7543   5971   7746     31    391   -151       S  
ATOM    115  CE  MET A 871     -21.702 -31.844 -72.814  1.00 90.85           C  
ANISOU  115  CE  MET A 871    12185  10351  11984    -31    183    -39       C  
ATOM    116  N   LEU A 872     -19.267 -26.341 -72.134  1.00 72.99           N  
ANISOU  116  N   LEU A 872     9781   8096   9856    104    329   -128       N  
ATOM    117  CA  LEU A 872     -17.876 -26.269 -72.564  1.00 74.29           C  
ANISOU  117  CA  LEU A 872     9951   8312   9963    191    120    -27       C  
ATOM    118  C   LEU A 872     -17.020 -25.461 -71.597  1.00 76.42           C  
ANISOU  118  C   LEU A 872    10366   8565  10104     66    126    -47       C  
ATOM    119  O   LEU A 872     -15.834 -25.737 -71.438  1.00 80.75           O  
ANISOU  119  O   LEU A 872    10974   9139  10567     60    -73     28       O  
ATOM    120  CB  LEU A 872     -17.774 -25.678 -73.970  1.00 70.93           C  
ANISOU  120  CB  LEU A 872     9322   7935   9694    349     72     12       C  
ATOM    121  CG  LEU A 872     -18.091 -26.620 -75.129  1.00 62.77           C  
ANISOU  121  CG  LEU A 872     8176   6966   8707    424    -13     54       C  
ATOM    122  CD1 LEU A 872     -17.974 -25.886 -76.452  1.00 59.45           C  
ANISOU  122  CD1 LEU A 872     7626   6607   8356    462    -72    110       C  
ATOM    123  CD2 LEU A 872     -17.165 -27.823 -75.096  1.00 60.91           C  
ANISOU  123  CD2 LEU A 872     7991   6751   8401    432   -141     54       C  
ATOM    124  N   ARG A 873     -17.616 -24.456 -70.963  1.00 72.61           N  
ANISOU  124  N   ARG A 873     9914   8026   9649    -45    357   -173       N  
ATOM    125  CA  ARG A 873     -16.895 -23.679 -69.961  1.00 72.37           C  
ANISOU  125  CA  ARG A 873    10054   7985   9459   -229    404   -223       C  
ATOM    126  C   ARG A 873     -16.530 -24.565 -68.774  1.00 77.74           C  
ANISOU  126  C   ARG A 873    11022   8685   9831   -499    293   -169       C  
ATOM    127  O   ARG A 873     -15.444 -24.445 -68.205  1.00 80.60           O  
ANISOU  127  O   ARG A 873    11528   9071  10024   -619    112    -86       O  
ATOM    128  CB  ARG A 873     -17.713 -22.468 -69.504  1.00 69.20           C  
ANISOU  128  CB  ARG A 873     9610   7483   9199   -324    733   -433       C  
ATOM    129  CG  ARG A 873     -17.133 -21.755 -68.290  1.00 75.22           C  
ANISOU  129  CG  ARG A 873    10599   8241   9740   -611    854   -542       C  
ATOM    130  CD  ARG A 873     -17.735 -20.372 -68.098  1.00 83.95           C  
ANISOU  130  CD  ARG A 873    11591   9207  11100   -644   1185   -784       C  
ATOM    131  NE  ARG A 873     -17.145 -19.386 -69.000  1.00 82.70           N  
ANISOU  131  NE  ARG A 873    11272   8997  11152   -414   1069   -696       N  
ATOM    132  CZ  ARG A 873     -17.680 -19.014 -70.158  1.00 82.01           C  
ANISOU  132  CZ  ARG A 873    10927   8813  11421   -149   1008   -629       C  
ATOM    133  NH1 ARG A 873     -17.067 -18.110 -70.911  1.00 80.66           N  
ANISOU  133  NH1 ARG A 873    10682   8598  11369    -25    880   -525       N  
ATOM    134  NH2 ARG A 873     -18.827 -19.540 -70.564  1.00 83.24           N  
ANISOU  134  NH2 ARG A 873    10914   8916  11798    -46   1050   -651       N  
ATOM    135  N   ILE A 874     -17.437 -25.468 -68.416  1.00 73.61           N  
ANISOU  135  N   ILE A 874    10591   8142   9235   -622    366   -193       N  
ATOM    136  CA  ILE A 874     -17.185 -26.404 -67.327  1.00 67.42           C  
ANISOU  136  CA  ILE A 874    10130   7351   8136   -933    207    -91       C  
ATOM    137  C   ILE A 874     -16.153 -27.461 -67.719  1.00 71.43           C  
ANISOU  137  C   ILE A 874    10626   7832   8682   -778   -230    153       C  
ATOM    138  O   ILE A 874     -15.237 -27.757 -66.953  1.00 73.64           O  
ANISOU  138  O   ILE A 874    11105   8078   8796   -958   -523    307       O  
ATOM    139  CB  ILE A 874     -18.484 -27.090 -66.859  1.00 61.20           C  
ANISOU  139  CB  ILE A 874     9459   6544   7250  -1153    427   -199       C  
ATOM    140  CG1 ILE A 874     -19.452 -26.052 -66.286  1.00 60.42           C  
ANISOU  140  CG1 ILE A 874     9344   6439   7173  -1365    901   -517       C  
ATOM    141  CG2 ILE A 874     -18.182 -28.164 -65.824  1.00 59.39           C  
ANISOU  141  CG2 ILE A 874     9614   6288   6663  -1516    185    -28       C  
ATOM    142  CD1 ILE A 874     -20.793 -26.620 -65.884  1.00 63.04           C  
ANISOU  142  CD1 ILE A 874     9723   6761   7470  -1596   1195   -705       C  
ATOM    143  N   ASP A 875     -16.297 -28.017 -68.919  1.00 77.38           N  
ANISOU  143  N   ASP A 875    11128   8583   9690   -464   -283    174       N  
ATOM    144  CA  ASP A 875     -15.410 -29.088 -69.374  1.00 73.81           C  
ANISOU  144  CA  ASP A 875    10602   8067   9374   -308   -629    322       C  
ATOM    145  C   ASP A 875     -13.990 -28.621 -69.704  1.00 65.91           C  
ANISOU  145  C   ASP A 875     9450   7079   8511   -168   -828    355       C  
ATOM    146  O   ASP A 875     -13.039 -29.394 -69.597  1.00 61.79           O  
ANISOU  146  O   ASP A 875     8897   6459   8122   -125  -1158    468       O  
ATOM    147  CB  ASP A 875     -16.013 -29.810 -70.582  1.00 73.20           C  
ANISOU  147  CB  ASP A 875    10310   7996   9507    -78   -562    273       C  
ATOM    148  CG  ASP A 875     -17.243 -30.619 -70.224  1.00 72.67           C  
ANISOU  148  CG  ASP A 875    10384   7892   9334   -223   -451    266       C  
ATOM    149  OD1 ASP A 875     -17.321 -31.108 -69.078  1.00 79.79           O  
ANISOU  149  OD1 ASP A 875    11579   8721  10017   -502   -550    354       O  
ATOM    150  OD2 ASP A 875     -18.131 -30.766 -71.089  1.00 67.81           O  
ANISOU  150  OD2 ASP A 875     9603   7325   8835   -100   -280    179       O  
ATOM    151  N   GLU A 876     -13.850 -27.361 -70.105  1.00 69.21           N  
ANISOU  151  N   GLU A 876     9755   7595   8947   -103   -637    249       N  
ATOM    152  CA  GLU A 876     -12.556 -26.834 -70.529  1.00 81.39           C  
ANISOU  152  CA  GLU A 876    11137   9176  10612      6   -768    242       C  
ATOM    153  C   GLU A 876     -11.933 -25.913 -69.487  1.00 86.28           C  
ANISOU  153  C   GLU A 876    11926   9814  11044   -202   -810    267       C  
ATOM    154  O   GLU A 876     -10.780 -26.092 -69.096  1.00 93.95           O  
ANISOU  154  O   GLU A 876    12888  10756  12052   -242  -1099    353       O  
ATOM    155  CB  GLU A 876     -12.687 -26.083 -71.859  1.00 87.92           C  
ANISOU  155  CB  GLU A 876    11739  10099  11570    183   -565    127       C  
ATOM    156  CG  GLU A 876     -13.198 -26.928 -73.016  1.00 94.23           C  
ANISOU  156  CG  GLU A 876    12377  10912  12515    331   -527     91       C  
ATOM    157  CD  GLU A 876     -12.171 -27.926 -73.516  1.00 98.77           C  
ANISOU  157  CD  GLU A 876    12782  11449  13295    430   -715     56       C  
ATOM    158  OE1 GLU A 876     -10.977 -27.781 -73.177  1.00101.48           O  
ANISOU  158  OE1 GLU A 876    13063  11768  13728    426   -879     51       O  
ATOM    159  OE2 GLU A 876     -12.561 -28.856 -74.251  1.00 99.34           O  
ANISOU  159  OE2 GLU A 876    12759  11504  13481    505   -690      7       O  
ATOM    160  N   GLY A 877     -12.700 -24.922 -69.046  1.00 79.16           N  
ANISOU  160  N   GLY A 877    11151   8943   9981   -345   -523    172       N  
ATOM    161  CA  GLY A 877     -12.197 -23.930 -68.116  1.00 71.77           C  
ANISOU  161  CA  GLY A 877    10384   8032   8854   -578   -487    143       C  
ATOM    162  C   GLY A 877     -11.561 -22.770 -68.855  1.00 66.57           C  
ANISOU  162  C   GLY A 877     9543   7427   8325   -435   -399     64       C  
ATOM    163  O   GLY A 877     -11.201 -22.894 -70.024  1.00 74.66           O  
ANISOU  163  O   GLY A 877    10330   8484   9551   -198   -449     64       O  
ATOM    164  N   LEU A 878     -11.421 -21.640 -68.173  1.00 63.54           N  
ANISOU  164  N   LEU A 878     9289   7050   7802   -627   -248    -20       N  
ATOM    165  CA  LEU A 878     -10.866 -20.443 -68.793  1.00 63.21           C  
ANISOU  165  CA  LEU A 878     9117   7035   7864   -535   -154    -90       C  
ATOM    166  C   LEU A 878      -9.447 -20.151 -68.313  1.00 74.51           C  
ANISOU  166  C   LEU A 878    10589   8533   9187   -665   -372    -42       C  
ATOM    167  O   LEU A 878      -9.235 -19.796 -67.154  1.00 85.29           O  
ANISOU  167  O   LEU A 878    12185   9904  10318   -960   -377    -52       O  
ATOM    168  CB  LEU A 878     -11.768 -19.238 -68.518  1.00 62.88           C  
ANISOU  168  CB  LEU A 878     9138   6906   7848   -625    200   -254       C  
ATOM    169  CG  LEU A 878     -11.254 -17.883 -69.009  1.00 67.06           C  
ANISOU  169  CG  LEU A 878     9588   7411   8480   -581    290   -312       C  
ATOM    170  CD1 LEU A 878     -11.063 -17.897 -70.517  1.00 70.91           C  
ANISOU  170  CD1 LEU A 878     9852   7925   9164   -322    187   -224       C  
ATOM    171  CD2 LEU A 878     -12.200 -16.767 -68.595  1.00 69.11           C  
ANISOU  171  CD2 LEU A 878     9890   7508   8860   -672    631   -498       C  
ATOM    172  N   ARG A 879      -8.481 -20.306 -69.213  1.00 70.91           N  
ANISOU  172  N   ARG A 879     9904   8136   8903   -486   -538    -15       N  
ATOM    173  CA  ARG A 879      -7.090 -19.985 -68.913  1.00 65.18           C  
ANISOU  173  CA  ARG A 879     9132   7473   8159   -582   -741     -1       C  
ATOM    174  C   ARG A 879      -6.528 -19.036 -69.969  1.00 60.86           C  
ANISOU  174  C   ARG A 879     8405   6992   7726   -485   -602   -107       C  
ATOM    175  O   ARG A 879      -6.444 -19.385 -71.146  1.00 66.03           O  
ANISOU  175  O   ARG A 879     8852   7682   8555   -309   -580   -146       O  
ATOM    176  CB  ARG A 879      -6.245 -21.259 -68.832  1.00 64.55           C  
ANISOU  176  CB  ARG A 879     8906   7375   8246   -512  -1126    104       C  
ATOM    177  CG  ARG A 879      -6.777 -22.292 -67.847  1.00 72.96           C  
ANISOU  177  CG  ARG A 879    10186   8346   9190   -643  -1332    264       C  
ATOM    178  CD  ARG A 879      -5.809 -23.453 -67.660  1.00 83.19           C  
ANISOU  178  CD  ARG A 879    11328   9551  10729   -587  -1805    406       C  
ATOM    179  NE  ARG A 879      -4.555 -23.029 -67.043  1.00 91.10           N  
ANISOU  179  NE  ARG A 879    12296  10576  11741   -743  -2094    464       N  
ATOM    180  CZ  ARG A 879      -3.594 -23.860 -66.654  1.00 91.84           C  
ANISOU  180  CZ  ARG A 879    12249  10554  12094   -744  -2590    615       C  
ATOM    181  NH1 ARG A 879      -3.741 -25.168 -66.814  1.00 94.93           N  
ANISOU  181  NH1 ARG A 879    12532  10773  12763   -589  -2839    716       N  
ATOM    182  NH2 ARG A 879      -2.485 -23.385 -66.101  1.00 88.77           N  
ANISOU  182  NH2 ARG A 879    11809  10193  11725   -902  -2864    668       N  
ATOM    183  N   LEU A 880      -6.144 -17.836 -69.542  1.00 57.74           N  
ANISOU  183  N   LEU A 880     8120   6617   7203   -653   -497   -164       N  
ATOM    184  CA  LEU A 880      -5.705 -16.792 -70.466  1.00 56.14           C  
ANISOU  184  CA  LEU A 880     7817   6454   7061   -625   -352   -248       C  
ATOM    185  C   LEU A 880      -4.286 -16.996 -71.000  1.00 61.07           C  
ANISOU  185  C   LEU A 880     8207   7200   7797   -614   -517   -302       C  
ATOM    186  O   LEU A 880      -3.958 -16.539 -72.094  1.00 66.27           O  
ANISOU  186  O   LEU A 880     8742   7918   8518   -589   -401   -382       O  
ATOM    187  CB  LEU A 880      -5.826 -15.416 -69.809  1.00 48.74           C  
ANISOU  187  CB  LEU A 880     7079   5458   5982   -818   -161   -311       C  
ATOM    188  CG  LEU A 880      -7.222 -15.051 -69.304  1.00 48.73           C  
ANISOU  188  CG  LEU A 880     7246   5301   5970   -848     80   -351       C  
ATOM    189  CD1 LEU A 880      -7.257 -13.616 -68.800  1.00 54.75           C  
ANISOU  189  CD1 LEU A 880     8151   5963   6687  -1030    310   -475       C  
ATOM    190  CD2 LEU A 880      -8.260 -15.268 -70.392  1.00 49.71           C  
ANISOU  190  CD2 LEU A 880     7244   5340   6304   -612    162   -313       C  
ATOM    191  N   LYS A 881      -3.448 -17.675 -70.224  1.00 58.94           N  
ANISOU  191  N   LYS A 881     7871   6954   7568   -670   -798   -263       N  
ATOM    192  CA  LYS A 881      -2.074 -17.941 -70.635  1.00 57.11           C  
ANISOU  192  CA  LYS A 881     7338   6804   7556   -649   -969   -356       C  
ATOM    193  C   LYS A 881      -1.981 -19.304 -71.320  1.00 65.73           C  
ANISOU  193  C   LYS A 881     8151   7861   8963   -437  -1091   -396       C  
ATOM    194  O   LYS A 881      -2.723 -20.226 -70.979  1.00 69.92           O  
ANISOU  194  O   LYS A 881     8761   8292   9514   -346  -1202   -275       O  
ATOM    195  CB  LYS A 881      -1.141 -17.885 -69.423  1.00 64.05           C  
ANISOU  195  CB  LYS A 881     8248   7691   8396   -832  -1275   -282       C  
ATOM    196  CG  LYS A 881       0.341 -17.920 -69.761  1.00 71.72           C  
ANISOU  196  CG  LYS A 881     8863   8737   9652   -835  -1443   -413       C  
ATOM    197  CD  LYS A 881       1.198 -17.798 -68.510  1.00 72.27           C  
ANISOU  197  CD  LYS A 881     8979   8805   9675  -1048  -1807   -294       C  
ATOM    198  CE  LYS A 881       2.679 -17.819 -68.852  1.00 77.57           C  
ANISOU  198  CE  LYS A 881     9224   9535  10713  -1039  -1983   -451       C  
ATOM    199  NZ  LYS A 881       3.530 -17.706 -67.636  1.00 86.91           N  
ANISOU  199  NZ  LYS A 881    10437  10713  11874  -1266  -2412   -300       N  
ATOM    200  N   ILE A 882      -1.077 -19.423 -72.290  1.00 68.05           N  
ANISOU  200  N   ILE A 882     8120   8230   9507   -393  -1035   -599       N  
ATOM    201  CA  ILE A 882      -0.896 -20.671 -73.029  1.00 66.90           C  
ANISOU  201  CA  ILE A 882     7664   8037   9719   -220  -1082   -726       C  
ATOM    202  C   ILE A 882      -0.531 -21.826 -72.102  1.00 67.07           C  
ANISOU  202  C   ILE A 882     7557   7889  10036   -119  -1503   -603       C  
ATOM    203  O   ILE A 882       0.437 -21.744 -71.345  1.00 65.00           O  
ANISOU  203  O   ILE A 882     7181   7595   9921   -191  -1798   -563       O  
ATOM    204  CB  ILE A 882       0.198 -20.544 -74.114  1.00 67.95           C  
ANISOU  204  CB  ILE A 882     7435   8283  10100   -272   -908  -1051       C  
ATOM    205  CG1 ILE A 882      -0.179 -19.479 -75.143  1.00 66.61           C  
ANISOU  205  CG1 ILE A 882     7439   8265   9604   -437   -537  -1132       C  
ATOM    206  CG2 ILE A 882       0.425 -21.882 -74.804  1.00 69.45           C  
ANISOU  206  CG2 ILE A 882     7270   8392  10726   -117   -917  -1253       C  
ATOM    207  CD1 ILE A 882       0.782 -19.399 -76.312  1.00 51.39           C  
ANISOU  207  CD1 ILE A 882     5217   6477   7833   -587   -301  -1482       C  
ATOM    208  N   TYR A 883      -1.314 -22.899 -72.164  1.00 73.86           N  
ANISOU  208  N   TYR A 883     8448   8627  10990     26  -1568   -520       N  
ATOM    209  CA  TYR A 883      -1.058 -24.079 -71.348  1.00 86.44           C  
ANISOU  209  CA  TYR A 883     9951  10009  12881    109  -2009   -363       C  
ATOM    210  C   TYR A 883      -1.042 -25.344 -72.201  1.00 91.80           C  
ANISOU  210  C   TYR A 883    10307  10554  14017    324  -1997   -531       C  
ATOM    211  O   TYR A 883      -1.397 -25.313 -73.380  1.00 90.85           O  
ANISOU  211  O   TYR A 883    10100  10540  13877    365  -1616   -757       O  
ATOM    212  CB  TYR A 883      -2.106 -24.206 -70.237  1.00 86.52           C  
ANISOU  212  CB  TYR A 883    10411   9953  12508     -2  -2154    -49       C  
ATOM    213  CG  TYR A 883      -3.517 -24.447 -70.734  1.00 82.07           C  
ANISOU  213  CG  TYR A 883    10045   9407  11729     68  -1854    -42       C  
ATOM    214  CD1 TYR A 883      -4.353 -23.386 -71.050  1.00 86.28           C  
ANISOU  214  CD1 TYR A 883    10794  10080  11908     -4  -1480    -82       C  
ATOM    215  CD2 TYR A 883      -4.014 -25.737 -70.877  1.00 82.60           C  
ANISOU  215  CD2 TYR A 883    10063   9323  11997    204  -1973     10       C  
ATOM    216  CE1 TYR A 883      -5.643 -23.601 -71.503  1.00 89.36           C  
ANISOU  216  CE1 TYR A 883    11315  10469  12169     62  -1253    -68       C  
ATOM    217  CE2 TYR A 883      -5.301 -25.963 -71.328  1.00 84.58           C  
ANISOU  217  CE2 TYR A 883    10476   9601  12059    250  -1710     12       C  
ATOM    218  CZ  TYR A 883      -6.111 -24.892 -71.639  1.00 87.61           C  
ANISOU  218  CZ  TYR A 883    11043  10135  12109    181  -1361    -25       C  
ATOM    219  OH  TYR A 883      -7.394 -25.114 -72.088  1.00 85.29           O  
ANISOU  219  OH  TYR A 883    10862   9851  11692    230  -1145    -17       O  
ATOM    220  N   LYS A 884      -0.626 -26.453 -71.600  1.00 95.86           N  
ANISOU  220  N   LYS A 884    10657  10818  14949    425  -2435   -416       N  
ATOM    221  CA  LYS A 884      -0.665 -27.748 -72.269  1.00 99.68           C  
ANISOU  221  CA  LYS A 884    10843  11107  15923    632  -2450   -571       C  
ATOM    222  C   LYS A 884      -1.794 -28.605 -71.708  1.00102.47           C  
ANISOU  222  C   LYS A 884    11525  11308  16099    656  -2623   -280       C  
ATOM    223  O   LYS A 884      -1.936 -28.739 -70.492  1.00103.87           O  
ANISOU  223  O   LYS A 884    11984  11375  16109    537  -3020     62       O  
ATOM    224  CB  LYS A 884       0.669 -28.481 -72.113  1.00105.89           C  
ANISOU  224  CB  LYS A 884    11117  11638  17478    760  -2837   -689       C  
ATOM    225  CG  LYS A 884       1.843 -27.808 -72.800  1.00111.97           C  
ANISOU  225  CG  LYS A 884    11463  12546  18536    733  -2612  -1074       C  
ATOM    226  CD  LYS A 884       3.106 -28.647 -72.668  1.00120.57           C  
ANISOU  226  CD  LYS A 884    11954  13327  20532    892  -2997  -1239       C  
ATOM    227  CE  LYS A 884       4.291 -27.979 -73.347  1.00123.04           C  
ANISOU  227  CE  LYS A 884    11804  13787  21157    830  -2726  -1683       C  
ATOM    228  NZ  LYS A 884       5.532 -28.793 -73.229  1.00127.74           N  
ANISOU  228  NZ  LYS A 884    11724  14049  22762   1003  -3093  -1896       N  
ATOM    229  N   ASP A 885      -2.594 -29.185 -72.596  1.00104.83           N  
ANISOU  229  N   ASP A 885    11813  11615  16404    757  -2321   -424       N  
ATOM    230  CA  ASP A 885      -3.677 -30.070 -72.184  1.00113.28           C  
ANISOU  230  CA  ASP A 885    13160  12543  17338    775  -2443   -196       C  
ATOM    231  C   ASP A 885      -3.133 -31.415 -71.704  1.00126.61           C  
ANISOU  231  C   ASP A 885    14641  13853  19612    900  -2937    -90       C  
ATOM    232  O   ASP A 885      -1.922 -31.586 -71.556  1.00134.72           O  
ANISOU  232  O   ASP A 885    15303  14714  21169    977  -3235   -162       O  
ATOM    233  CB  ASP A 885      -4.679 -30.270 -73.325  1.00114.58           C  
ANISOU  233  CB  ASP A 885    13356  12835  17345    825  -1988   -384       C  
ATOM    234  CG  ASP A 885      -4.024 -30.771 -74.600  1.00121.97           C  
ANISOU  234  CG  ASP A 885    13845  13748  18752    938  -1754   -792       C  
ATOM    235  OD1 ASP A 885      -3.093 -31.599 -74.513  1.00131.12           O  
ANISOU  235  OD1 ASP A 885    14639  14647  20532   1067  -2005   -913       O  
ATOM    236  OD2 ASP A 885      -4.442 -30.336 -75.694  1.00119.19           O  
ANISOU  236  OD2 ASP A 885    13500  13622  18167    865  -1325  -1004       O  
ATOM    237  N   THR A 886      -4.029 -32.366 -71.462  1.00130.23           N  
ANISOU  237  N   THR A 886    15314  14150  20016    913  -3044     83       N  
ATOM    238  CA  THR A 886      -3.629 -33.693 -71.003  1.00134.69           C  
ANISOU  238  CA  THR A 886    15730  14299  21147   1019  -3553    230       C  
ATOM    239  C   THR A 886      -2.819 -34.435 -72.064  1.00137.71           C  
ANISOU  239  C   THR A 886    15515  14483  22327   1277  -3451   -179       C  
ATOM    240  O   THR A 886      -2.011 -35.307 -71.744  1.00140.44           O  
ANISOU  240  O   THR A 886    15549  14439  23373   1408  -3909   -141       O  
ATOM    241  CB  THR A 886      -4.847 -34.545 -70.591  1.00131.58           C  
ANISOU  241  CB  THR A 886    15729  13785  20479    939  -3634    481       C  
ATOM    242  OG1 THR A 886      -5.828 -34.520 -71.636  1.00128.61           O  
ANISOU  242  OG1 THR A 886    15384  13620  19861    992  -3068    232       O  
ATOM    243  CG2 THR A 886      -5.466 -34.007 -69.310  1.00127.00           C  
ANISOU  243  CG2 THR A 886    15709  13317  19228    617  -3820    869       C  
ATOM    244  N   GLU A 887      -3.038 -34.081 -73.327  1.00137.62           N  
ANISOU  244  N   GLU A 887    15345  14724  22220   1310  -2850   -581       N  
ATOM    245  CA  GLU A 887      -2.305 -34.688 -74.431  1.00141.05           C  
ANISOU  245  CA  GLU A 887    15228  15027  23336   1464  -2614  -1071       C  
ATOM    246  C   GLU A 887      -0.882 -34.142 -74.510  1.00141.36           C  
ANISOU  246  C   GLU A 887    14815  15061  23833   1495  -2673  -1316       C  
ATOM    247  O   GLU A 887       0.087 -34.901 -74.483  1.00149.20           O  
ANISOU  247  O   GLU A 887    15404  15746  25538   1583  -2887  -1481       O  
ATOM    248  CB  GLU A 887      -3.032 -34.449 -75.756  1.00138.88           C  
ANISOU  248  CB  GLU A 887    15005  15063  22701   1375  -1956  -1404       C  
ATOM    249  CG  GLU A 887      -4.431 -35.040 -75.815  1.00136.72           C  
ANISOU  249  CG  GLU A 887    15102  14797  22047   1347  -1868  -1221       C  
ATOM    250  CD  GLU A 887      -5.077 -34.868 -77.176  1.00135.75           C  
ANISOU  250  CD  GLU A 887    14997  14959  21624   1228  -1290  -1539       C  
ATOM    251  OE1 GLU A 887      -4.393 -34.381 -78.101  1.00137.40           O  
ANISOU  251  OE1 GLU A 887    14939  15338  21927   1137   -951  -1920       O  
ATOM    252  OE2 GLU A 887      -6.267 -35.219 -77.321  1.00134.55           O  
ANISOU  252  OE2 GLU A 887    15135  14865  21123   1181  -1187  -1404       O  
ATOM    253  N   GLY A 888      -0.765 -32.821 -74.609  1.00129.06           N  
ANISOU  253  N   GLY A 888    13406  13873  21759   1333  -2428  -1336       N  
ATOM    254  CA  GLY A 888       0.531 -32.173 -74.689  1.00120.76           C  
ANISOU  254  CA  GLY A 888    11966  12872  21045   1314  -2439  -1572       C  
ATOM    255  C   GLY A 888       0.563 -31.034 -75.689  1.00110.70           C  
ANISOU  255  C   GLY A 888    10722  12015  19324   1120  -1842  -1887       C  
ATOM    256  O   GLY A 888       1.591 -30.378 -75.861  1.00114.16           O  
ANISOU  256  O   GLY A 888    10870  12552  19953   1050  -1762  -2122       O  
ATOM    257  N   TYR A 889      -0.566 -30.797 -76.350  1.00 99.97           N  
ANISOU  257  N   TYR A 889     9717  10889  17377   1009  -1456  -1874       N  
ATOM    258  CA  TYR A 889      -0.666 -29.729 -77.339  1.00 94.17           C  
ANISOU  258  CA  TYR A 889     9087  10524  16171    778   -953  -2096       C  
ATOM    259  C   TYR A 889      -0.950 -28.385 -76.676  1.00 88.00           C  
ANISOU  259  C   TYR A 889     8703   9954  14778    656  -1029  -1759       C  
ATOM    260  O   TYR A 889      -1.659 -28.317 -75.671  1.00 81.69           O  
ANISOU  260  O   TYR A 889     8251   9093  13694    703  -1310  -1354       O  
ATOM    261  CB  TYR A 889      -1.756 -30.045 -78.365  1.00 90.78           C  
ANISOU  261  CB  TYR A 889     8856  10227  15409    681   -577  -2195       C  
ATOM    262  CG  TYR A 889      -1.499 -31.296 -79.175  1.00 96.16           C  
ANISOU  262  CG  TYR A 889     9161  10731  16644    732   -389  -2611       C  
ATOM    263  CD1 TYR A 889      -0.207 -31.758 -79.387  1.00104.08           C  
ANISOU  263  CD1 TYR A 889     9602  11555  18390    789   -360  -3040       C  
ATOM    264  CD2 TYR A 889      -2.551 -32.015 -79.728  1.00 93.98           C  
ANISOU  264  CD2 TYR A 889     9062  10452  16193    711   -224  -2610       C  
ATOM    265  CE1 TYR A 889       0.030 -32.902 -80.127  1.00108.23           C  
ANISOU  265  CE1 TYR A 889     9747  11880  19496    827   -139  -3488       C  
ATOM    266  CE2 TYR A 889      -2.323 -33.159 -80.469  1.00 95.52           C  
ANISOU  266  CE2 TYR A 889     8922  10474  16898    729    -16  -3026       C  
ATOM    267  CZ  TYR A 889      -1.031 -33.598 -80.665  1.00104.10           C  
ANISOU  267  CZ  TYR A 889     9446  11361  18745    787     42  -3480       C  
ATOM    268  OH  TYR A 889      -0.800 -34.736 -81.402  1.00109.96           O  
ANISOU  268  OH  TYR A 889     9818  11894  20066    796    296  -3960       O  
ATOM    269  N   TYR A 890      -0.396 -27.319 -77.246  1.00 90.13           N  
ANISOU  269  N   TYR A 890     8929  10464  14852    462   -751  -1957       N  
ATOM    270  CA  TYR A 890      -0.569 -25.977 -76.696  1.00 87.69           C  
ANISOU  270  CA  TYR A 890     8963  10329  14028    335   -787  -1693       C  
ATOM    271  C   TYR A 890      -1.993 -25.463 -76.870  1.00 83.07           C  
ANISOU  271  C   TYR A 890     8845   9867  12852    267   -635  -1438       C  
ATOM    272  O   TYR A 890      -2.455 -25.238 -77.988  1.00 77.35           O  
ANISOU  272  O   TYR A 890     8192   9295  11904    127   -314  -1573       O  
ATOM    273  CB  TYR A 890       0.422 -25.001 -77.332  1.00 88.45           C  
ANISOU  273  CB  TYR A 890     8886  10626  14095    121   -525  -1985       C  
ATOM    274  CG  TYR A 890       1.862 -25.278 -76.976  1.00 90.03           C  
ANISOU  274  CG  TYR A 890     8602  10709  14897    180   -708  -2221       C  
ATOM    275  CD1 TYR A 890       2.389 -24.861 -75.761  1.00 91.25           C  
ANISOU  275  CD1 TYR A 890     8781  10790  15099    224  -1107  -1969       C  
ATOM    276  CD2 TYR A 890       2.697 -25.953 -77.854  1.00 92.54           C  
ANISOU  276  CD2 TYR A 890     8416  10981  15765    162   -479  -2720       C  
ATOM    277  CE1 TYR A 890       3.705 -25.112 -75.429  1.00 94.99           C  
ANISOU  277  CE1 TYR A 890     8777  11139  16175    277  -1339  -2159       C  
ATOM    278  CE2 TYR A 890       4.015 -26.207 -77.531  1.00 99.73           C  
ANISOU  278  CE2 TYR A 890     8804  11748  17340    235   -658  -2967       C  
ATOM    279  CZ  TYR A 890       4.514 -25.784 -76.318  1.00 99.93           C  
ANISOU  279  CZ  TYR A 890     8849  11694  17424    306  -1122  -2660       C  
ATOM    280  OH  TYR A 890       5.827 -26.035 -75.993  1.00107.24           O  
ANISOU  280  OH  TYR A 890     9223  12461  19061    377  -1363  -2881       O  
ATOM    281  N   THR A 891      -2.679 -25.272 -75.749  1.00 87.63           N  
ANISOU  281  N   THR A 891     9730  10368  13196    329   -877  -1080       N  
ATOM    282  CA  THR A 891      -4.056 -24.802 -75.753  1.00 89.15           C  
ANISOU  282  CA  THR A 891    10304  10628  12943    290   -753   -861       C  
ATOM    283  C   THR A 891      -4.154 -23.495 -74.973  1.00 90.26           C  
ANISOU  283  C   THR A 891    10709  10830  12756    180   -777   -679       C  
ATOM    284  O   THR A 891      -3.432 -23.293 -73.997  1.00 96.94           O  
ANISOU  284  O   THR A 891    11543  11627  13662    153  -1000   -609       O  
ATOM    285  CB  THR A 891      -4.997 -25.851 -75.129  1.00 91.12           C  
ANISOU  285  CB  THR A 891    10689  10713  13221    421   -932   -665       C  
ATOM    286  OG1 THR A 891      -4.768 -27.126 -75.742  1.00 93.25           O  
ANISOU  286  OG1 THR A 891    10686  10873  13870    532   -940   -850       O  
ATOM    287  CG2 THR A 891      -6.455 -25.459 -75.316  1.00 90.20           C  
ANISOU  287  CG2 THR A 891    10870  10662  12739    386   -755   -517       C  
ATOM    288  N   ILE A 892      -5.036 -22.605 -75.413  1.00 81.31           N  
ANISOU  288  N   ILE A 892     9802   9782  11309     99   -566   -607       N  
ATOM    289  CA  ILE A 892      -5.249 -21.339 -74.724  1.00 75.89           C  
ANISOU  289  CA  ILE A 892     9356   9109  10371     -2   -541   -474       C  
ATOM    290  C   ILE A 892      -6.742 -21.021 -74.674  1.00 68.73           C  
ANISOU  290  C   ILE A 892     8687   8146   9281     21   -432   -322       C  
ATOM    291  O   ILE A 892      -7.527 -21.588 -75.434  1.00 68.68           O  
ANISOU  291  O   ILE A 892     8656   8139   9299     85   -366   -316       O  
ATOM    292  CB  ILE A 892      -4.481 -20.188 -75.412  1.00 76.66           C  
ANISOU  292  CB  ILE A 892     9413   9330  10385   -162   -389   -595       C  
ATOM    293  CG1 ILE A 892      -4.278 -19.016 -74.448  1.00 74.02           C  
ANISOU  293  CG1 ILE A 892     9264   8975   9884   -267   -415   -504       C  
ATOM    294  CG2 ILE A 892      -5.188 -19.751 -76.689  1.00 73.45           C  
ANISOU  294  CG2 ILE A 892     9088   8986   9833   -246   -191   -595       C  
ATOM    295  CD1 ILE A 892      -3.630 -17.813 -75.082  1.00 74.93           C  
ANISOU  295  CD1 ILE A 892     9389   9186   9894   -444   -268   -595       C  
ATOM    296  N   GLY A 893      -7.131 -20.127 -73.771  1.00 63.98           N  
ANISOU  296  N   GLY A 893     8292   7488   8531    -48   -404   -230       N  
ATOM    297  CA  GLY A 893      -8.520 -19.725 -73.639  1.00 60.75           C  
ANISOU  297  CA  GLY A 893     8043   6987   8052    -28   -274   -146       C  
ATOM    298  C   GLY A 893      -9.400 -20.854 -73.139  1.00 60.29           C  
ANISOU  298  C   GLY A 893     8028   6864   8017     49   -324    -91       C  
ATOM    299  O   GLY A 893      -9.035 -21.572 -72.209  1.00 67.76           O  
ANISOU  299  O   GLY A 893     9024   7785   8938     12   -480    -58       O  
ATOM    300  N   ILE A 894     -10.565 -21.009 -73.759  1.00 52.17           N  
ANISOU  300  N   ILE A 894     6989   5797   7034    126   -224    -59       N  
ATOM    301  CA  ILE A 894     -11.484 -22.078 -73.397  1.00 47.72           C  
ANISOU  301  CA  ILE A 894     6461   5182   6489    180   -241    -24       C  
ATOM    302  C   ILE A 894     -11.383 -23.230 -74.391  1.00 57.24           C  
ANISOU  302  C   ILE A 894     7513   6441   7793    280   -318    -39       C  
ATOM    303  O   ILE A 894     -12.227 -23.379 -75.276  1.00 58.14           O  
ANISOU  303  O   ILE A 894     7578   6570   7941    323   -248    -24       O  
ATOM    304  CB  ILE A 894     -12.940 -21.575 -73.335  1.00 46.83           C  
ANISOU  304  CB  ILE A 894     6398   4975   6419    189    -70    -15       C  
ATOM    305  CG1 ILE A 894     -13.015 -20.257 -72.565  1.00 41.94           C  
ANISOU  305  CG1 ILE A 894     5882   4271   5784     83     72    -71       C  
ATOM    306  CG2 ILE A 894     -13.844 -22.622 -72.695  1.00 52.41           C  
ANISOU  306  CG2 ILE A 894     7171   5637   7104    179    -50    -12       C  
ATOM    307  CD1 ILE A 894     -14.418 -19.704 -72.444  1.00 43.40           C  
ANISOU  307  CD1 ILE A 894     6040   4307   6143    102    263   -126       C  
ATOM    308  N   GLY A 895     -10.334 -24.033 -74.247  1.00 68.10           N  
ANISOU  308  N   GLY A 895     8796   7828   9251    302   -471    -82       N  
ATOM    309  CA  GLY A 895     -10.150 -25.212 -75.073  1.00 73.86           C  
ANISOU  309  CA  GLY A 895     9355   8567  10143    386   -514   -160       C  
ATOM    310  C   GLY A 895      -9.862 -24.921 -76.533  1.00 70.44           C  
ANISOU  310  C   GLY A 895     8777   8259   9727    343   -374   -289       C  
ATOM    311  O   GLY A 895     -10.285 -25.669 -77.416  1.00 72.31           O  
ANISOU  311  O   GLY A 895     8941   8527  10005    349   -311   -353       O  
ATOM    312  N   HIS A 896      -9.141 -23.835 -76.792  1.00 66.78           N  
ANISOU  312  N   HIS A 896     8303   7876   9196    246   -318   -334       N  
ATOM    313  CA  HIS A 896      -8.768 -23.480 -78.157  1.00 71.02           C  
ANISOU  313  CA  HIS A 896     8756   8548   9679    103   -183   -458       C  
ATOM    314  C   HIS A 896      -7.398 -24.040 -78.524  1.00 76.88           C  
ANISOU  314  C   HIS A 896     9251   9346  10614     62   -149   -720       C  
ATOM    315  O   HIS A 896      -6.374 -23.593 -78.009  1.00 82.90           O  
ANISOU  315  O   HIS A 896     9932  10110  11457     49   -201   -784       O  
ATOM    316  CB  HIS A 896      -8.779 -21.963 -78.348  1.00 71.66           C  
ANISOU  316  CB  HIS A 896     8977   8668   9583    -30   -135   -364       C  
ATOM    317  CG  HIS A 896      -8.330 -21.526 -79.708  1.00 72.59           C  
ANISOU  317  CG  HIS A 896     9077   8930   9574   -271    -24   -462       C  
ATOM    318  ND1 HIS A 896      -9.134 -21.620 -80.822  1.00 73.15           N  
ANISOU  318  ND1 HIS A 896     9225   9056   9512   -411      2   -393       N  
ATOM    319  CD2 HIS A 896      -7.157 -21.001 -80.132  1.00 73.90           C  
ANISOU  319  CD2 HIS A 896     9178   9206   9693   -458     67   -627       C  
ATOM    320  CE1 HIS A 896      -8.477 -21.167 -81.876  1.00 77.90           C  
ANISOU  320  CE1 HIS A 896     9851   9801   9946   -713    101   -500       C  
ATOM    321  NE2 HIS A 896      -7.275 -20.787 -81.484  1.00 78.51           N  
ANISOU  321  NE2 HIS A 896     9834   9917  10079   -743    167   -662       N  
ATOM    322  N   LEU A 897      -7.389 -25.019 -79.423  1.00 76.52           N  
ANISOU  322  N   LEU A 897     9060   9336  10678     27    -47   -904       N  
ATOM    323  CA  LEU A 897      -6.152 -25.651 -79.864  1.00 77.16           C  
ANISOU  323  CA  LEU A 897     8834   9434  11048    -18     46  -1241       C  
ATOM    324  C   LEU A 897      -5.373 -24.751 -80.819  1.00 82.46           C  
ANISOU  324  C   LEU A 897     9469  10296  11567   -311    265  -1443       C  
ATOM    325  O   LEU A 897      -5.822 -24.470 -81.930  1.00 87.34           O  
ANISOU  325  O   LEU A 897    10220  11057  11907   -568    433  -1471       O  
ATOM    326  CB  LEU A 897      -6.453 -26.991 -80.536  1.00 76.28           C  
ANISOU  326  CB  LEU A 897     8582   9279  11122      1    143  -1428       C  
ATOM    327  CG  LEU A 897      -5.280 -27.705 -81.205  1.00 76.75           C  
ANISOU  327  CG  LEU A 897     8274   9333  11556    -80    330  -1878       C  
ATOM    328  CD1 LEU A 897      -4.171 -27.976 -80.202  1.00 81.23           C  
ANISOU  328  CD1 LEU A 897     8561   9714  12590    134    111  -1944       C  
ATOM    329  CD2 LEU A 897      -5.751 -28.997 -81.853  1.00 76.64           C  
ANISOU  329  CD2 LEU A 897     8159   9252  11708    -79    455  -2065       C  
ATOM    330  N   LEU A 898      -4.202 -24.305 -80.378  1.00 81.19           N  
ANISOU  330  N   LEU A 898     9144  10138  11568   -317    242  -1571       N  
ATOM    331  CA  LEU A 898      -3.351 -23.449 -81.196  1.00 75.48           C  
ANISOU  331  CA  LEU A 898     8378   9597  10705   -629    467  -1792       C  
ATOM    332  C   LEU A 898      -2.645 -24.254 -82.280  1.00 82.99           C  
ANISOU  332  C   LEU A 898     9034  10632  11867   -832    763  -2263       C  
ATOM    333  O   LEU A 898      -2.882 -24.051 -83.471  1.00 90.23           O  
ANISOU  333  O   LEU A 898    10084  11723  12475  -1186   1011  -2387       O  
ATOM    334  CB  LEU A 898      -2.324 -22.725 -80.324  1.00 65.63           C  
ANISOU  334  CB  LEU A 898     7027   8328   9583   -580    352  -1798       C  
ATOM    335  CG  LEU A 898      -2.877 -21.673 -79.363  1.00 59.41           C  
ANISOU  335  CG  LEU A 898     6551   7489   8532   -499    158  -1419       C  
ATOM    336  CD1 LEU A 898      -1.776 -21.134 -78.466  1.00 58.00           C  
ANISOU  336  CD1 LEU A 898     6248   7293   8495   -480     36  -1459       C  
ATOM    337  CD2 LEU A 898      -3.538 -20.546 -80.138  1.00 46.65           C  
ANISOU  337  CD2 LEU A 898     5249   5975   6501   -740    280  -1267       C  
ATOM    338  N   THR A 899      -1.776 -25.167 -81.861  1.00 82.51           N  
ANISOU  338  N   THR A 899     8568  10426  12355   -639    726  -2534       N  
ATOM    339  CA  THR A 899      -1.041 -26.009 -82.797  1.00 85.03           C  
ANISOU  339  CA  THR A 899     8519  10768  13020   -806   1049  -3073       C  
ATOM    340  C   THR A 899      -0.619 -27.325 -82.152  1.00 86.48           C  
ANISOU  340  C   THR A 899     8294  10655  13911   -450    869  -3226       C  
ATOM    341  O   THR A 899      -0.602 -27.452 -80.927  1.00 84.30           O  
ANISOU  341  O   THR A 899     8006  10181  13843   -130    463  -2918       O  
ATOM    342  CB  THR A 899       0.209 -25.293 -83.340  1.00 90.05           C  
ANISOU  342  CB  THR A 899     8946  11574  13696  -1128   1332  -3463       C  
ATOM    343  OG1 THR A 899       0.902 -26.157 -84.248  1.00 95.56           O  
ANISOU  343  OG1 THR A 899     9247  12283  14780  -1323   1715  -4072       O  
ATOM    344  CG2 THR A 899       1.141 -24.912 -82.201  1.00 92.94           C  
ANISOU  344  CG2 THR A 899     9082  11820  14410   -889   1056  -3396       C  
ATOM    345  N   LYS A 900      -0.282 -28.303 -82.987  1.00 89.14           N  
ANISOU  345  N   LYS A 900     8308  10941  14619   -549   1166  -3705       N  
ATOM    346  CA  LYS A 900       0.180 -29.598 -82.505  1.00 88.69           C  
ANISOU  346  CA  LYS A 900     7808  10539  15350   -223   1001  -3900       C  
ATOM    347  C   LYS A 900       1.703 -29.648 -82.464  1.00 94.61           C  
ANISOU  347  C   LYS A 900     7982  11186  16781   -216   1081  -4365       C  
ATOM    348  O   LYS A 900       2.295 -30.686 -82.164  1.00 97.17           O  
ANISOU  348  O   LYS A 900     7828  11178  17915     37    945  -4606       O  
ATOM    349  CB  LYS A 900      -0.362 -30.725 -83.384  1.00 82.92           C  
ANISOU  349  CB  LYS A 900     7011   9748  14747   -305   1284  -4193       C  
ATOM    350  CG  LYS A 900      -1.876 -30.844 -83.378  1.00 81.05           C  
ANISOU  350  CG  LYS A 900     7273   9575  13948   -280   1164  -3747       C  
ATOM    351  CD  LYS A 900      -2.331 -32.044 -84.191  1.00 83.91           C  
ANISOU  351  CD  LYS A 900     7537   9857  14487   -364   1426  -4059       C  
ATOM    352  CE  LYS A 900      -3.840 -32.206 -84.152  1.00 77.03           C  
ANISOU  352  CE  LYS A 900     7122   9042  13102   -334   1283  -3620       C  
ATOM    353  NZ  LYS A 900      -4.280 -33.407 -84.914  1.00 78.36           N  
ANISOU  353  NZ  LYS A 900     7205   9131  13439   -430   1529  -3924       N  
ATOM    354  N   SER A 901       2.332 -28.518 -82.769  1.00 93.98           N  
ANISOU  354  N   SER A 901     7930  11367  16411   -501   1284  -4493       N  
ATOM    355  CA  SER A 901       3.785 -28.418 -82.743  1.00100.88           C  
ANISOU  355  CA  SER A 901     8249  12183  17897   -538   1385  -4952       C  
ATOM    356  C   SER A 901       4.289 -28.285 -81.310  1.00105.49           C  
ANISOU  356  C   SER A 901     8688  12538  18857   -163    785  -4582       C  
ATOM    357  O   SER A 901       3.734 -27.520 -80.523  1.00108.85           O  
ANISOU  357  O   SER A 901     9564  13044  18748    -96    468  -4028       O  
ATOM    358  CB  SER A 901       4.252 -27.225 -83.579  1.00101.33           C  
ANISOU  358  CB  SER A 901     8436  12618  17444  -1038   1819  -5207       C  
ATOM    359  OG  SER A 901       5.664 -27.103 -83.555  1.00104.04           O  
ANISOU  359  OG  SER A 901     8244  12918  18370  -1096   1942  -5676       O  
ATOM    360  N   PRO A 902       5.346 -29.038 -80.967  1.00107.78           N  
ANISOU  360  N   PRO A 902     8400  12509  20044     47    609  -4873       N  
ATOM    361  CA  PRO A 902       5.953 -29.009 -79.632  1.00108.86           C  
ANISOU  361  CA  PRO A 902     8404  12391  20567    344    -25  -4513       C  
ATOM    362  C   PRO A 902       6.599 -27.663 -79.310  1.00108.58           C  
ANISOU  362  C   PRO A 902     8346  12631  20279    168    -40  -4473       C  
ATOM    363  O   PRO A 902       6.900 -27.394 -78.147  1.00108.27           O  
ANISOU  363  O   PRO A 902     8322  12474  20340    336   -578  -4083       O  
ATOM    364  CB  PRO A 902       7.032 -30.096 -79.714  1.00116.12           C  
ANISOU  364  CB  PRO A 902     8951  12874  22296    453   -107  -4854       C  
ATOM    365  CG  PRO A 902       6.610 -30.975 -80.842  1.00117.01           C  
ANISOU  365  CG  PRO A 902     9057  12937  22464    312    347  -5256       C  
ATOM    366  CD  PRO A 902       5.963 -30.059 -81.829  1.00113.80           C  
ANISOU  366  CD  PRO A 902     8920  13031  21287    -50    914  -5418       C  
ATOM    367  N   SER A 903       6.811 -26.835 -80.328  1.00109.98           N  
ANISOU  367  N   SER A 903     8588  13157  20040   -229    531  -4837       N  
ATOM    368  CA  SER A 903       7.434 -25.530 -80.139  1.00114.53           C  
ANISOU  368  CA  SER A 903     9263  13983  20270   -459    571  -4799       C  
ATOM    369  C   SER A 903       6.433 -24.498 -79.628  1.00109.14           C  
ANISOU  369  C   SER A 903     9322  13486  18661   -512    394  -4170       C  
ATOM    370  O   SER A 903       5.339 -24.357 -80.175  1.00105.11           O  
ANISOU  370  O   SER A 903     9274  13108  17556   -627    595  -3998       O  
ATOM    371  CB  SER A 903       8.066 -25.044 -81.445  1.00121.80           C  
ANISOU  371  CB  SER A 903    10078  15172  21029   -918   1243  -5404       C  
ATOM    372  OG  SER A 903       8.673 -23.775 -81.276  1.00124.76           O  
ANISOU  372  OG  SER A 903    10515  15792  21096  -1171   1292  -5387       O  
ATOM    373  N   LEU A 904       6.816 -23.777 -78.578  1.00109.49           N  
ANISOU  373  N   LEU A 904     9451  13523  18626   -446     17  -3850       N  
ATOM    374  CA  LEU A 904       5.959 -22.748 -77.998  1.00103.88           C  
ANISOU  374  CA  LEU A 904     9387  12951  17134   -505   -124  -3320       C  
ATOM    375  C   LEU A 904       5.904 -21.508 -78.889  1.00105.98           C  
ANISOU  375  C   LEU A 904     9952  13532  16783   -903    327  -3444       C  
ATOM    376  O   LEU A 904       4.895 -20.804 -78.925  1.00106.17           O  
ANISOU  376  O   LEU A 904    10517  13652  16171   -984    362  -3097       O  
ATOM    377  CB  LEU A 904       6.439 -22.376 -76.591  1.00 96.93           C  
ANISOU  377  CB  LEU A 904     8511  11965  16352   -380   -642  -2985       C  
ATOM    378  CG  LEU A 904       5.670 -21.277 -75.850  1.00 83.04           C  
ANISOU  378  CG  LEU A 904     7370  10319  13861   -468   -761  -2509       C  
ATOM    379  CD1 LEU A 904       4.191 -21.614 -75.756  1.00 74.22           C  
ANISOU  379  CD1 LEU A 904     6701   9141  12359   -345   -783  -2172       C  
ATOM    380  CD2 LEU A 904       6.254 -21.044 -74.465  1.00 83.50           C  
ANISOU  380  CD2 LEU A 904     7405  10278  14042   -418  -1264  -2238       C  
ATOM    381  N   ASN A 905       6.992 -21.251 -79.609  1.00106.04           N  
ANISOU  381  N   ASN A 905     9594  13678  17020  -1170    660  -3946       N  
ATOM    382  CA  ASN A 905       7.067 -20.102 -80.504  1.00103.96           C  
ANISOU  382  CA  ASN A 905     9616  13705  16179  -1628   1078  -4084       C  
ATOM    383  C   ASN A 905       6.057 -20.194 -81.645  1.00 98.88           C  
ANISOU  383  C   ASN A 905     9339  13181  15049  -1856   1405  -4083       C  
ATOM    384  O   ASN A 905       5.465 -19.191 -82.046  1.00 95.64           O  
ANISOU  384  O   ASN A 905     9431  12922  13985  -2124   1505  -3838       O  
ATOM    385  CB  ASN A 905       8.481 -19.953 -81.063  1.00117.40           C  
ANISOU  385  CB  ASN A 905    10808  15531  18267  -1919   1409  -4695       C  
ATOM    386  CG  ASN A 905       9.533 -19.885 -79.973  1.00125.78           C  
ANISOU  386  CG  ASN A 905    11449  16469  19873  -1709   1042  -4703       C  
ATOM    387  OD1 ASN A 905       9.829 -18.813 -79.445  1.00126.58           O  
ANISOU  387  OD1 ASN A 905    11760  16678  19659  -1831    923  -4499       O  
ATOM    388  ND2 ASN A 905      10.104 -21.034 -79.630  1.00130.89           N  
ANISOU  388  ND2 ASN A 905    11496  16866  21371  -1405    829  -4929       N  
ATOM    389  N   ALA A 906       5.870 -21.405 -82.164  1.00 98.05           N  
ANISOU  389  N   ALA A 906     8976  12982  15294  -1765   1540  -4350       N  
ATOM    390  CA  ALA A 906       4.887 -21.650 -83.214  1.00 92.68           C  
ANISOU  390  CA  ALA A 906     8626  12408  14180  -1990   1807  -4345       C  
ATOM    391  C   ALA A 906       3.479 -21.406 -82.683  1.00 97.28           C  
ANISOU  391  C   ALA A 906     9738  12913  14310  -1758   1470  -3698       C  
ATOM    392  O   ALA A 906       2.624 -20.860 -83.384  1.00102.93           O  
ANISOU  392  O   ALA A 906    10901  13760  14450  -2016   1580  -3494       O  
ATOM    393  CB  ALA A 906       5.019 -23.069 -83.740  1.00 85.60           C  
ANISOU  393  CB  ALA A 906     7306  11392  13827  -1913   2010  -4790       C  
ATOM    394  N   ALA A 907       3.251 -21.813 -81.438  1.00 93.65           N  
ANISOU  394  N   ALA A 907     9218  12229  14135  -1303   1045  -3384       N  
ATOM    395  CA  ALA A 907       1.973 -21.585 -80.776  1.00 82.35           C  
ANISOU  395  CA  ALA A 907     8237  10711  12341  -1089    754  -2830       C  
ATOM    396  C   ALA A 907       1.718 -20.091 -80.611  1.00 72.94           C  
ANISOU  396  C   ALA A 907     7458   9631  10624  -1272    733  -2537       C  
ATOM    397  O   ALA A 907       0.600 -19.619 -80.809  1.00 65.99           O  
ANISOU  397  O   ALA A 907     6983   8757   9332  -1311    706  -2219       O  
ATOM    398  CB  ALA A 907       1.944 -22.285 -79.426  1.00 57.70           C  
ANISOU  398  CB  ALA A 907     4979   7343   9601   -674    326  -2599       C  
ATOM    399  N   LYS A 908       2.764 -19.353 -80.251  1.00 75.21           N  
ANISOU  399  N   LYS A 908     7615   9981  10982  -1384    733  -2656       N  
ATOM    400  CA  LYS A 908       2.668 -17.904 -80.112  1.00 78.73           C  
ANISOU  400  CA  LYS A 908     8424  10509  10981  -1585    737  -2429       C  
ATOM    401  C   LYS A 908       2.386 -17.250 -81.459  1.00 85.30           C  
ANISOU  401  C   LYS A 908     9527  11509  11372  -2014   1039  -2494       C  
ATOM    402  O   LYS A 908       1.685 -16.243 -81.534  1.00 88.43           O  
ANISOU  402  O   LYS A 908    10341  11891  11369  -2128    978  -2169       O  
ATOM    403  CB  LYS A 908       3.952 -17.328 -79.513  1.00 78.42           C  
ANISOU  403  CB  LYS A 908     8153  10517  11127  -1658    694  -2594       C  
ATOM    404  CG  LYS A 908       4.206 -17.722 -78.069  1.00 76.30           C  
ANISOU  404  CG  LYS A 908     7724  10081  11186  -1322    298  -2420       C  
ATOM    405  CD  LYS A 908       5.527 -17.154 -77.579  1.00 84.03           C  
ANISOU  405  CD  LYS A 908     8446  11125  12356  -1443    239  -2597       C  
ATOM    406  CE  LYS A 908       5.799 -17.543 -76.138  1.00 91.06           C  
ANISOU  406  CE  LYS A 908     9213  11853  13532  -1185   -225  -2379       C  
ATOM    407  NZ  LYS A 908       4.792 -16.963 -75.211  1.00 95.47           N  
ANISOU  407  NZ  LYS A 908    10276  12341  13659  -1122   -408  -1934       N  
ATOM    408  N   SER A 909       2.939 -17.829 -82.521  1.00 86.72           N  
ANISOU  408  N   SER A 909     9472  11829  11647  -2286   1355  -2924       N  
ATOM    409  CA  SER A 909       2.720 -17.320 -83.870  1.00 87.00           C  
ANISOU  409  CA  SER A 909     9798  12049  11209  -2807   1638  -3004       C  
ATOM    410  C   SER A 909       1.270 -17.519 -84.303  1.00 79.56           C  
ANISOU  410  C   SER A 909     9222  11046   9962  -2771   1512  -2641       C  
ATOM    411  O   SER A 909       0.623 -16.586 -84.787  1.00 74.68           O  
ANISOU  411  O   SER A 909     9034  10448   8893  -3028   1443  -2327       O  
ATOM    412  CB  SER A 909       3.664 -18.004 -84.860  1.00 96.98           C  
ANISOU  412  CB  SER A 909    10702  13486  12660  -3163   2067  -3631       C  
ATOM    413  OG  SER A 909       3.443 -17.537 -86.180  1.00103.90           O  
ANISOU  413  OG  SER A 909    11923  14565  12988  -3775   2342  -3704       O  
ATOM    414  N   GLU A 910       0.768 -18.738 -84.124  1.00 79.95           N  
ANISOU  414  N   GLU A 910     9085  10996  10297  -2457   1450  -2674       N  
ATOM    415  CA  GLU A 910      -0.617 -19.058 -84.459  1.00 82.99           C  
ANISOU  415  CA  GLU A 910     9757  11320  10457  -2389   1318  -2353       C  
ATOM    416  C   GLU A 910      -1.585 -18.222 -83.629  1.00 82.07           C  
ANISOU  416  C   GLU A 910     9956  11036  10190  -2127    982  -1820       C  
ATOM    417  O   GLU A 910      -2.632 -17.799 -84.119  1.00 81.42           O  
ANISOU  417  O   GLU A 910    10201  10922   9812  -2239    871  -1506       O  
ATOM    418  CB  GLU A 910      -0.893 -20.547 -84.241  1.00 91.39           C  
ANISOU  418  CB  GLU A 910    10533  12281  11910  -2065   1306  -2502       C  
ATOM    419  CG  GLU A 910      -0.094 -21.472 -85.144  1.00106.86           C  
ANISOU  419  CG  GLU A 910    12153  14357  14094  -2323   1680  -3079       C  
ATOM    420  CD  GLU A 910      -0.528 -21.395 -86.594  1.00118.32           C  
ANISOU  420  CD  GLU A 910    13881  16014  15062  -2880   1944  -3181       C  
ATOM    421  OE1 GLU A 910      -1.703 -21.055 -86.849  1.00120.01           O  
ANISOU  421  OE1 GLU A 910    14494  16220  14886  -2929   1741  -2748       O  
ATOM    422  OE2 GLU A 910       0.307 -21.673 -87.481  1.00123.75           O  
ANISOU  422  OE2 GLU A 910    14381  16867  15770  -3306   2351  -3707       O  
ATOM    423  N   LEU A 911      -1.226 -17.991 -82.370  1.00 82.80           N  
ANISOU  423  N   LEU A 911     9934  11008  10519  -1806    819  -1740       N  
ATOM    424  CA  LEU A 911      -2.043 -17.188 -81.467  1.00 76.58           C  
ANISOU  424  CA  LEU A 911     9407  10053   9636  -1588    576  -1333       C  
ATOM    425  C   LEU A 911      -2.083 -15.729 -81.906  1.00 79.99           C  
ANISOU  425  C   LEU A 911    10152  10498   9742  -1894    586  -1160       C  
ATOM    426  O   LEU A 911      -3.148 -15.112 -81.937  1.00 82.64           O  
ANISOU  426  O   LEU A 911    10762  10692   9947  -1860    436   -826       O  
ATOM    427  CB  LEU A 911      -1.510 -17.287 -80.037  1.00 70.35           C  
ANISOU  427  CB  LEU A 911     8448   9165   9117  -1290    427  -1335       C  
ATOM    428  CG  LEU A 911      -2.211 -16.421 -78.989  1.00 59.50           C  
ANISOU  428  CG  LEU A 911     7330   7630   7647  -1134    255  -1012       C  
ATOM    429  CD1 LEU A 911      -3.667 -16.832 -78.839  1.00 52.78           C  
ANISOU  429  CD1 LEU A 911     6628   6640   6786   -928    155   -769       C  
ATOM    430  CD2 LEU A 911      -1.481 -16.507 -77.659  1.00 56.78           C  
ANISOU  430  CD2 LEU A 911     6847   7240   7486   -980    119  -1050       C  
ATOM    431  N   ASP A 912      -0.919 -15.181 -82.239  1.00 83.49           N  
ANISOU  431  N   ASP A 912    10534  11085  10105  -2199    754  -1397       N  
ATOM    432  CA  ASP A 912      -0.829 -13.802 -82.707  1.00 90.52           C  
ANISOU  432  CA  ASP A 912    11738  11980  10675  -2549    763  -1246       C  
ATOM    433  C   ASP A 912      -1.563 -13.626 -84.031  1.00 99.92           C  
ANISOU  433  C   ASP A 912    13225  13209  11531  -2913    756  -1081       C  
ATOM    434  O   ASP A 912      -2.098 -12.555 -84.316  1.00104.62           O  
ANISOU  434  O   ASP A 912    14156  13678  11917  -3087    593   -755       O  
ATOM    435  CB  ASP A 912       0.632 -13.369 -82.852  1.00 94.27           C  
ANISOU  435  CB  ASP A 912    12066  12632  11120  -2854    980  -1585       C  
ATOM    436  CG  ASP A 912       1.333 -13.227 -81.515  1.00 98.38           C  
ANISOU  436  CG  ASP A 912    12368  13093  11920  -2563    897  -1652       C  
ATOM    437  OD1 ASP A 912       0.644 -12.970 -80.505  1.00101.55           O  
ANISOU  437  OD1 ASP A 912    12888  13305  12393  -2247    685  -1369       O  
ATOM    438  OD2 ASP A 912       2.573 -13.372 -81.473  1.00100.91           O  
ANISOU  438  OD2 ASP A 912    12390  13557  12395  -2687   1048  -2005       O  
ATOM    439  N   LYS A 913      -1.588 -14.683 -84.836  1.00104.10           N  
ANISOU  439  N   LYS A 913    13632  13891  12031  -3052    907  -1301       N  
ATOM    440  CA  LYS A 913      -2.303 -14.647 -86.106  1.00106.36           C  
ANISOU  440  CA  LYS A 913    14215  14241  11956  -3459    876  -1143       C  
ATOM    441  C   LYS A 913      -3.812 -14.706 -85.887  1.00 99.87           C  
ANISOU  441  C   LYS A 913    13551  13196  11197  -3150    546   -699       C  
ATOM    442  O   LYS A 913      -4.575 -14.019 -86.566  1.00102.35           O  
ANISOU  442  O   LYS A 913    14194  13424  11270  -3403    324   -346       O  
ATOM    443  CB  LYS A 913      -1.848 -15.790 -87.017  1.00108.57           C  
ANISOU  443  CB  LYS A 913    14309  14761  12183  -3751   1194  -1579       C  
ATOM    444  CG  LYS A 913      -2.537 -15.809 -88.372  1.00105.49           C  
ANISOU  444  CG  LYS A 913    14262  14479  11339  -4280   1173  -1438       C  
ATOM    445  CD  LYS A 913      -2.413 -14.465 -89.072  1.00102.57           C  
ANISOU  445  CD  LYS A 913    14324  14135  10511  -4840   1068  -1189       C  
ATOM    446  CE  LYS A 913      -3.280 -14.414 -90.318  1.00107.47           C  
ANISOU  446  CE  LYS A 913    15352  14811  10669  -5367    893   -904       C  
ATOM    447  NZ  LYS A 913      -3.281 -13.063 -90.942  1.00112.41           N  
ANISOU  447  NZ  LYS A 913    16449  15389  10872  -5907    667   -546       N  
ATOM    448  N   ALA A 914      -4.236 -15.528 -84.932  1.00 94.52           N  
ANISOU  448  N   ALA A 914    12632  12412  10869  -2626    493   -714       N  
ATOM    449  CA  ALA A 914      -5.655 -15.691 -84.632  1.00 92.40           C  
ANISOU  449  CA  ALA A 914    12449  11943  10715  -2319    235   -369       C  
ATOM    450  C   ALA A 914      -6.248 -14.437 -83.993  1.00 88.50           C  
ANISOU  450  C   ALA A 914    12134  11186  10307  -2163      4    -22       C  
ATOM    451  O   ALA A 914      -7.341 -14.005 -84.356  1.00 89.93           O  
ANISOU  451  O   ALA A 914    12490  11193  10487  -2178   -238    313       O  
ATOM    452  CB  ALA A 914      -5.871 -16.899 -83.732  1.00 91.66           C  
ANISOU  452  CB  ALA A 914    12075  11811  10942  -1864    269   -505       C  
ATOM    453  N   ILE A 915      -5.522 -13.859 -83.042  1.00 85.62           N  
ANISOU  453  N   ILE A 915    11702  10770  10059  -2025     73   -118       N  
ATOM    454  CA  ILE A 915      -5.987 -12.664 -82.347  1.00 81.85           C  
ANISOU  454  CA  ILE A 915    11369  10025   9705  -1890    -77    128       C  
ATOM    455  C   ILE A 915      -5.885 -11.425 -83.232  1.00 78.29           C  
ANISOU  455  C   ILE A 915    11208   9501   9036  -2293   -192    335       C  
ATOM    456  O   ILE A 915      -6.875 -10.726 -83.451  1.00 77.05           O  
ANISOU  456  O   ILE A 915    11217   9079   8980  -2279   -446    669       O  
ATOM    457  CB  ILE A 915      -5.206 -12.426 -81.039  1.00 79.75           C  
ANISOU  457  CB  ILE A 915    10973   9744   9583  -1686     38    -51       C  
ATOM    458  CG1 ILE A 915      -5.386 -13.611 -80.090  1.00 74.76           C  
ANISOU  458  CG1 ILE A 915    10114   9138   9155  -1330     68   -179       C  
ATOM    459  CG2 ILE A 915      -5.664 -11.140 -80.369  1.00 78.46           C  
ANISOU  459  CG2 ILE A 915    10970   9298   9544  -1608    -53    142       C  
ATOM    460  CD1 ILE A 915      -6.827 -13.874 -79.710  1.00 69.34           C  
ANISOU  460  CD1 ILE A 915     9455   8250   8639  -1062    -49     20       C  
ATOM    461  N   GLY A 916      -4.685 -11.157 -83.736  1.00 75.22           N  
ANISOU  461  N   GLY A 916    10869   9326   8386  -2669    -21    133       N  
ATOM    462  CA  GLY A 916      -4.467 -10.017 -84.606  1.00 76.52           C  
ANISOU  462  CA  GLY A 916    11355   9444   8275  -3141   -122    320       C  
ATOM    463  C   GLY A 916      -3.499  -9.008 -84.021  1.00 75.03           C  
ANISOU  463  C   GLY A 916    11207   9225   8077  -3224    -11    214       C  
ATOM    464  O   GLY A 916      -3.475  -7.847 -84.429  1.00 80.49           O  
ANISOU  464  O   GLY A 916    12186   9763   8633  -3521   -147    436       O  
ATOM    465  N   ARG A 917      -2.698  -9.454 -83.059  1.00 72.28           N  
ANISOU  465  N   ARG A 917    10577   9005   7880  -2980    201   -106       N  
ATOM    466  CA  ARG A 917      -1.702  -8.597 -82.427  1.00 76.35           C  
ANISOU  466  CA  ARG A 917    11094   9529   8387  -3063    314   -243       C  
ATOM    467  C   ARG A 917      -0.634  -9.444 -81.752  1.00 80.38           C  
ANISOU  467  C   ARG A 917    11242  10279   9022  -2919    522   -638       C  
ATOM    468  O   ARG A 917      -0.760 -10.666 -81.670  1.00 77.07           O  
ANISOU  468  O   ARG A 917    10578   9958   8747  -2700    554   -776       O  
ATOM    469  CB  ARG A 917      -2.356  -7.688 -81.387  1.00 75.60           C  
ANISOU  469  CB  ARG A 917    11099   9094   8531  -2772    171    -23       C  
ATOM    470  CG  ARG A 917      -2.961  -8.445 -80.218  1.00 74.15           C  
ANISOU  470  CG  ARG A 917    10699   8831   8642  -2283    161    -65       C  
ATOM    471  CD  ARG A 917      -3.441  -7.512 -79.120  1.00 73.32           C  
ANISOU  471  CD  ARG A 917    10681   8425   8754  -2087    125     34       C  
ATOM    472  NE  ARG A 917      -4.113  -8.249 -78.054  1.00 74.73           N  
ANISOU  472  NE  ARG A 917    10702   8539   9151  -1715    138    -14       N  
ATOM    473  CZ  ARG A 917      -3.485  -8.836 -77.040  1.00 77.50           C  
ANISOU  473  CZ  ARG A 917    10899   9044   9505  -1603    226   -217       C  
ATOM    474  NH1 ARG A 917      -2.164  -8.771 -76.949  1.00 82.17           N  
ANISOU  474  NH1 ARG A 917    11414   9850   9958  -1785    299   -403       N  
ATOM    475  NH2 ARG A 917      -4.177  -9.490 -76.117  1.00 74.71           N  
ANISOU  475  NH2 ARG A 917    10468   8622   9296  -1342    219   -226       N  
ATOM    476  N   ASN A 918       0.417  -8.791 -81.270  1.00 86.13           N  
ANISOU  476  N   ASN A 918    11927  11073   9728  -3047    629   -807       N  
ATOM    477  CA  ASN A 918       1.445  -9.478 -80.501  1.00 81.41           C  
ANISOU  477  CA  ASN A 918    10960  10647   9326  -2896    737  -1135       C  
ATOM    478  C   ASN A 918       0.960  -9.705 -79.075  1.00 71.43           C  
ANISOU  478  C   ASN A 918     9622   9216   8301  -2457    578  -1016       C  
ATOM    479  O   ASN A 918       0.935  -8.780 -78.264  1.00 68.39           O  
ANISOU  479  O   ASN A 918     9388   8691   7907  -2433    534   -913       O  
ATOM    480  CB  ASN A 918       2.747  -8.680 -80.504  1.00 85.33           C  
ANISOU  480  CB  ASN A 918    11423  11284   9714  -3230    889  -1358       C  
ATOM    481  CG  ASN A 918       3.894  -9.437 -79.868  1.00 91.08           C  
ANISOU  481  CG  ASN A 918    11705  12188  10712  -3114    957  -1711       C  
ATOM    482  OD1 ASN A 918       4.162  -9.296 -78.676  1.00 95.04           O  
ANISOU  482  OD1 ASN A 918    12117  12626  11368  -2903    829  -1683       O  
ATOM    483  ND2 ASN A 918       4.575 -10.253 -80.663  1.00 93.79           N  
ANISOU  483  ND2 ASN A 918    11755  12740  11142  -3280   1147  -2057       N  
ATOM    484  N   THR A 919       0.570 -10.940 -78.778  1.00 68.78           N  
ANISOU  484  N   THR A 919     9080   8894   8160  -2159    510  -1046       N  
ATOM    485  CA  THR A 919      -0.055 -11.266 -77.501  1.00 67.79           C  
ANISOU  485  CA  THR A 919     8946   8615   8196  -1813    359   -912       C  
ATOM    486  C   THR A 919       0.937 -11.743 -76.445  1.00 68.44           C  
ANISOU  486  C   THR A 919     8776   8784   8442  -1723    280  -1078       C  
ATOM    487  O   THR A 919       0.627 -11.743 -75.254  1.00 70.58           O  
ANISOU  487  O   THR A 919     9116   8948   8751  -1572    154   -967       O  
ATOM    488  CB  THR A 919      -1.139 -12.346 -77.673  1.00 64.57           C  
ANISOU  488  CB  THR A 919     8499   8142   7893  -1560    284   -804       C  
ATOM    489  OG1 THR A 919      -0.570 -13.494 -78.316  1.00 59.35           O  
ANISOU  489  OG1 THR A 919     7559   7652   7340  -1572    339  -1027       O  
ATOM    490  CG2 THR A 919      -2.290 -11.817 -78.517  1.00 66.53           C  
ANISOU  490  CG2 THR A 919     9000   8254   8025  -1622    271   -571       C  
ATOM    491  N   ASN A 920       2.123 -12.152 -76.889  1.00 71.37           N  
ANISOU  491  N   ASN A 920     8852   9341   8925  -1854    346  -1352       N  
ATOM    492  CA  ASN A 920       3.143 -12.707 -76.001  1.00 81.05           C  
ANISOU  492  CA  ASN A 920     9762  10625  10409  -1768    196  -1503       C  
ATOM    493  C   ASN A 920       2.659 -13.931 -75.224  1.00 87.29           C  
ANISOU  493  C   ASN A 920    10434  11308  11424  -1450    -45  -1391       C  
ATOM    494  O   ASN A 920       3.138 -14.210 -74.125  1.00 91.60           O  
ANISOU  494  O   ASN A 920    10874  11820  12109  -1378   -288  -1350       O  
ATOM    495  CB  ASN A 920       3.685 -11.642 -75.040  1.00 83.08           C  
ANISOU  495  CB  ASN A 920    10150  10873  10543  -1904    133  -1454       C  
ATOM    496  CG  ASN A 920       4.421 -10.529 -75.758  1.00 91.57           C  
ANISOU  496  CG  ASN A 920    11289  12063  11442  -2247    351  -1604       C  
ATOM    497  OD1 ASN A 920       4.052  -9.359 -75.657  1.00 94.36           O  
ANISOU  497  OD1 ASN A 920    11978  12326  11549  -2388    421  -1461       O  
ATOM    498  ND2 ASN A 920       5.471 -10.888 -76.488  1.00 96.33           N  
ANISOU  498  ND2 ASN A 920    11559  12844  12199  -2407    474  -1920       N  
ATOM    499  N   GLY A 921       1.705 -14.656 -75.801  1.00 85.92           N  
ANISOU  499  N   GLY A 921    10302  11079  11265  -1303     -3  -1322       N  
ATOM    500  CA  GLY A 921       1.196 -15.874 -75.198  1.00 79.86           C  
ANISOU  500  CA  GLY A 921     9442  10203  10698  -1031   -211  -1221       C  
ATOM    501  C   GLY A 921       0.055 -15.645 -74.227  1.00 73.11           C  
ANISOU  501  C   GLY A 921     8919   9205   9655   -927   -313   -935       C  
ATOM    502  O   GLY A 921      -0.472 -16.591 -73.643  1.00 76.72           O  
ANISOU  502  O   GLY A 921     9371   9570  10211   -754   -480   -825       O  
ATOM    503  N   VAL A 922      -0.331 -14.386 -74.052  1.00 65.76           N  
ANISOU  503  N   VAL A 922     8272   8237   8477  -1059   -193   -842       N  
ATOM    504  CA  VAL A 922      -1.394 -14.043 -73.114  1.00 60.29           C  
ANISOU  504  CA  VAL A 922     7863   7394   7653  -1006   -208   -659       C  
ATOM    505  C   VAL A 922      -2.483 -13.189 -73.761  1.00 60.22           C  
ANISOU  505  C   VAL A 922     8066   7265   7549  -1013    -24   -566       C  
ATOM    506  O   VAL A 922      -2.215 -12.097 -74.266  1.00 64.92           O  
ANISOU  506  O   VAL A 922     8756   7851   8058  -1174     85   -583       O  
ATOM    507  CB  VAL A 922      -0.840 -13.303 -71.879  1.00 57.82           C  
ANISOU  507  CB  VAL A 922     7679   7074   7217  -1173   -273   -655       C  
ATOM    508  CG1 VAL A 922      -1.979 -12.823 -70.992  1.00 59.36           C  
ANISOU  508  CG1 VAL A 922     8171   7110   7272  -1194   -179   -554       C  
ATOM    509  CG2 VAL A 922       0.108 -14.202 -71.100  1.00 55.43           C  
ANISOU  509  CG2 VAL A 922     7180   6842   7037  -1175   -568   -668       C  
ATOM    510  N   ILE A 923      -3.711 -13.696 -73.740  1.00 51.27           N  
ANISOU  510  N   ILE A 923     7000   6018   6465   -848    -22   -456       N  
ATOM    511  CA  ILE A 923      -4.851 -12.958 -74.269  1.00 51.33           C  
ANISOU  511  CA  ILE A 923     7156   5858   6488   -823     84   -346       C  
ATOM    512  C   ILE A 923      -5.768 -12.501 -73.139  1.00 67.24           C  
ANISOU  512  C   ILE A 923     9327   7681   8541   -786    164   -321       C  
ATOM    513  O   ILE A 923      -5.663 -12.979 -72.009  1.00 78.87           O  
ANISOU  513  O   ILE A 923    10833   9183   9951   -805    135   -367       O  
ATOM    514  CB  ILE A 923      -5.657 -13.803 -75.270  1.00 45.05           C  
ANISOU  514  CB  ILE A 923     6282   5069   5764   -695     49   -269       C  
ATOM    515  CG1 ILE A 923      -6.262 -15.023 -74.576  1.00 42.44           C  
ANISOU  515  CG1 ILE A 923     5893   4726   5508   -514    -13   -259       C  
ATOM    516  CG2 ILE A 923      -4.777 -14.232 -76.431  1.00 55.83           C  
ANISOU  516  CG2 ILE A 923     7507   6629   7076   -810     46   -364       C  
ATOM    517  CD1 ILE A 923      -7.062 -15.911 -75.502  1.00 43.76           C  
ANISOU  517  CD1 ILE A 923     5981   4903   5742   -399    -40   -199       C  
ATOM    518  N   THR A 924      -6.665 -11.571 -73.450  1.00 69.13           N  
ANISOU  518  N   THR A 924     9658   7704   8905   -770    257   -259       N  
ATOM    519  CA  THR A 924      -7.596 -11.043 -72.460  1.00 68.62           C  
ANISOU  519  CA  THR A 924     9689   7416   8966   -753    409   -318       C  
ATOM    520  C   THR A 924      -8.860 -11.897 -72.380  1.00 76.34           C  
ANISOU  520  C   THR A 924    10598   8316  10091   -578    423   -289       C  
ATOM    521  O   THR A 924      -9.017 -12.859 -73.134  1.00 76.49           O  
ANISOU  521  O   THR A 924    10514   8446  10102   -462    294   -195       O  
ATOM    522  CB  THR A 924      -7.981  -9.583 -72.777  1.00 63.14           C  
ANISOU  522  CB  THR A 924     9069   6448   8473   -800    497   -299       C  
ATOM    523  OG1 THR A 924      -8.583  -9.513 -74.076  1.00 58.70           O  
ANISOU  523  OG1 THR A 924     8447   5782   8073   -703    353   -109       O  
ATOM    524  CG2 THR A 924      -6.751  -8.693 -72.753  1.00 48.29           C  
ANISOU  524  CG2 THR A 924     7285   4638   6423  -1011    511   -345       C  
ATOM    525  N   LYS A 925      -9.754 -11.546 -71.460  1.00 80.34           N  
ANISOU  525  N   LYS A 925    11155   8634  10737   -592    615   -410       N  
ATOM    526  CA  LYS A 925     -11.021 -12.254 -71.309  1.00 79.24           C  
ANISOU  526  CA  LYS A 925    10937   8406  10766   -461    679   -429       C  
ATOM    527  C   LYS A 925     -11.888 -12.120 -72.556  1.00 79.93           C  
ANISOU  527  C   LYS A 925    10875   8339  11154   -271    564   -274       C  
ATOM    528  O   LYS A 925     -12.441 -13.105 -73.042  1.00 79.19           O  
ANISOU  528  O   LYS A 925    10689   8321  11078   -150    464   -187       O  
ATOM    529  CB  LYS A 925     -11.788 -11.737 -70.090  1.00 81.27           C  
ANISOU  529  CB  LYS A 925    11257   8475  11148   -580    983   -670       C  
ATOM    530  CG  LYS A 925     -11.722 -12.644 -68.874  1.00 84.36           C  
ANISOU  530  CG  LYS A 925    11790   9032  11230   -769   1065   -781       C  
ATOM    531  CD  LYS A 925     -12.639 -12.136 -67.771  1.00 93.73           C  
ANISOU  531  CD  LYS A 925    13041  10036  12535   -959   1443  -1080       C  
ATOM    532  CE  LYS A 925     -12.691 -13.101 -66.599  1.00 98.66           C  
ANISOU  532  CE  LYS A 925    13867  10832  12786  -1236   1509  -1164       C  
ATOM    533  NZ  LYS A 925     -13.603 -12.617 -65.526  1.00101.14           N  
ANISOU  533  NZ  LYS A 925    14261  10993  13176  -1514   1954  -1525       N  
ATOM    534  N   ASP A 926     -12.001 -10.894 -73.061  1.00 81.62           N  
ANISOU  534  N   ASP A 926    11082   8322  11607   -275    546   -220       N  
ATOM    535  CA  ASP A 926     -12.792 -10.603 -74.254  1.00 83.55           C  
ANISOU  535  CA  ASP A 926    11216   8375  12154   -153    347    -11       C  
ATOM    536  C   ASP A 926     -12.346 -11.466 -75.431  1.00 88.44           C  
ANISOU  536  C   ASP A 926    11842   9259  12501   -168    109    190       C  
ATOM    537  O   ASP A 926     -13.164 -12.117 -76.087  1.00 98.12           O  
ANISOU  537  O   ASP A 926    12969  10481  13833    -68    -20    309       O  
ATOM    538  CB  ASP A 926     -12.669  -9.118 -74.612  1.00 85.67           C  
ANISOU  538  CB  ASP A 926    11533   8351  12667   -217    290     63       C  
ATOM    539  CG  ASP A 926     -13.597  -8.704 -75.741  1.00 97.96           C  
ANISOU  539  CG  ASP A 926    12986   9628  14608   -122      7    326       C  
ATOM    540  OD1 ASP A 926     -13.933  -9.556 -76.592  1.00104.32           O  
ANISOU  540  OD1 ASP A 926    13744  10580  15311    -83   -196    505       O  
ATOM    541  OD2 ASP A 926     -13.990  -7.519 -75.780  1.00101.41           O  
ANISOU  541  OD2 ASP A 926    13388   9674  15469   -104    -40    362       O  
ATOM    542  N   GLU A 927     -11.040 -11.470 -75.682  1.00 77.71           N  
ANISOU  542  N   GLU A 927    10587   8133  10808   -321     79    188       N  
ATOM    543  CA  GLU A 927     -10.461 -12.235 -76.780  1.00 70.93           C  
ANISOU  543  CA  GLU A 927     9722   7531   9697   -401    -63    283       C  
ATOM    544  C   GLU A 927     -10.681 -13.735 -76.592  1.00 66.26           C  
ANISOU  544  C   GLU A 927     9025   7124   9028   -279    -47    215       C  
ATOM    545  O   GLU A 927     -10.923 -14.464 -77.557  1.00 67.12           O  
ANISOU  545  O   GLU A 927     9084   7338   9078   -285   -151    299       O  
ATOM    546  CB  GLU A 927      -8.970 -11.919 -76.910  1.00 70.14           C  
ANISOU  546  CB  GLU A 927     9698   7629   9325   -603    -29    202       C  
ATOM    547  CG  GLU A 927      -8.684 -10.453 -77.213  1.00 71.61           C  
ANISOU  547  CG  GLU A 927    10023   7640   9544   -770    -57    286       C  
ATOM    548  CD  GLU A 927      -7.209 -10.106 -77.135  1.00 66.78           C  
ANISOU  548  CD  GLU A 927     9470   7229   8676   -982     22    156       C  
ATOM    549  OE1 GLU A 927      -6.449 -10.857 -76.488  1.00 58.61           O  
ANISOU  549  OE1 GLU A 927     8338   6407   7524   -953     99    -19       O  
ATOM    550  OE2 GLU A 927      -6.808  -9.079 -77.721  1.00 71.65           O  
ANISOU  550  OE2 GLU A 927    10222   7770   9230  -1192    -20    239       O  
ATOM    551  N   ALA A 928     -10.606 -14.183 -75.343  1.00 61.11           N  
ANISOU  551  N   ALA A 928     8364   6497   8357   -212     75     68       N  
ATOM    552  CA  ALA A 928     -10.821 -15.588 -75.015  1.00 59.14           C  
ANISOU  552  CA  ALA A 928     8046   6373   8050   -115     63     23       C  
ATOM    553  C   ALA A 928     -12.257 -16.009 -75.313  1.00 61.27           C  
ANISOU  553  C   ALA A 928     8244   6523   8512     15     53     95       C  
ATOM    554  O   ALA A 928     -12.497 -17.082 -75.873  1.00 57.88           O  
ANISOU  554  O   ALA A 928     7747   6205   8040     70    -22    134       O  
ATOM    555  CB  ALA A 928     -10.479 -15.851 -73.558  1.00 51.96           C  
ANISOU  555  CB  ALA A 928     7209   5486   7046   -156    144   -100       C  
ATOM    556  N   GLU A 929     -13.207 -15.157 -74.937  1.00 64.04           N  
ANISOU  556  N   GLU A 929     8583   6630   9121     57    140     85       N  
ATOM    557  CA  GLU A 929     -14.618 -15.425 -75.184  1.00 67.36           C  
ANISOU  557  CA  GLU A 929     8876   6900   9817    182    127    129       C  
ATOM    558  C   GLU A 929     -14.927 -15.405 -76.677  1.00 68.86           C  
ANISOU  558  C   GLU A 929     9011   7088  10067    186   -120    357       C  
ATOM    559  O   GLU A 929     -15.693 -16.237 -77.170  1.00 69.36           O  
ANISOU  559  O   GLU A 929     8986   7192  10177    249   -202    424       O  
ATOM    560  CB  GLU A 929     -15.502 -14.416 -74.445  1.00 73.80           C  
ANISOU  560  CB  GLU A 929     9624   7407  11008    218    297      6       C  
ATOM    561  CG  GLU A 929     -15.328 -14.419 -72.932  1.00 80.12           C  
ANISOU  561  CG  GLU A 929    10522   8220  11700    112    585   -254       C  
ATOM    562  CD  GLU A 929     -15.648 -15.761 -72.302  1.00 84.78           C  
ANISOU  562  CD  GLU A 929    11145   8975  12094     89    658   -331       C  
ATOM    563  OE1 GLU A 929     -16.519 -16.482 -72.834  1.00 92.24           O  
ANISOU  563  OE1 GLU A 929    11962   9916  13170    204    591   -267       O  
ATOM    564  OE2 GLU A 929     -15.027 -16.096 -71.271  1.00 81.61           O  
ANISOU  564  OE2 GLU A 929    10912   8696  11399    -75    752   -436       O  
ATOM    565  N   LYS A 930     -14.328 -14.456 -77.393  1.00 65.91           N  
ANISOU  565  N   LYS A 930     8719   6672   9653     67   -246    484       N  
ATOM    566  CA  LYS A 930     -14.492 -14.389 -78.843  1.00 61.91           C  
ANISOU  566  CA  LYS A 930     8239   6187   9097    -49   -510    727       C  
ATOM    567  C   LYS A 930     -13.971 -15.654 -79.517  1.00 65.43           C  
ANISOU  567  C   LYS A 930     8705   6959   9197   -144   -518    696       C  
ATOM    568  O   LYS A 930     -14.643 -16.223 -80.378  1.00 73.32           O  
ANISOU  568  O   LYS A 930     9671   8000  10188   -184   -663    822       O  
ATOM    569  CB  LYS A 930     -13.800 -13.154 -79.423  1.00 63.03           C  
ANISOU  569  CB  LYS A 930     8528   6243   9179   -244   -632    861       C  
ATOM    570  CG  LYS A 930     -14.517 -11.845 -79.134  1.00 74.94           C  
ANISOU  570  CG  LYS A 930     9994   7340  11140   -163   -715    955       C  
ATOM    571  CD  LYS A 930     -13.930 -10.687 -79.936  1.00 83.17           C  
ANISOU  571  CD  LYS A 930    11219   8268  12115   -398   -921   1166       C  
ATOM    572  CE  LYS A 930     -14.265 -10.791 -81.422  1.00 85.66           C  
ANISOU  572  CE  LYS A 930    11631   8609  12308   -618  -1292   1500       C  
ATOM    573  NZ  LYS A 930     -13.592 -11.935 -82.100  1.00 83.33           N  
ANISOU  573  NZ  LYS A 930    11420   8748  11496   -816  -1221   1431       N  
ATOM    574  N   LEU A 931     -12.779 -16.094 -79.122  1.00 62.87           N  
ANISOU  574  N   LEU A 931     8413   6843   8631   -191   -368    513       N  
ATOM    575  CA  LEU A 931     -12.224 -17.340 -79.644  1.00 59.58           C  
ANISOU  575  CA  LEU A 931     7954   6683   7999   -253   -334    410       C  
ATOM    576  C   LEU A 931     -13.142 -18.512 -79.325  1.00 64.48           C  
ANISOU  576  C   LEU A 931     8476   7301   8723    -78   -319    383       C  
ATOM    577  O   LEU A 931     -13.354 -19.389 -80.160  1.00 66.51           O  
ANISOU  577  O   LEU A 931     8700   7680   8892   -142   -359    390       O  
ATOM    578  CB  LEU A 931     -10.828 -17.606 -79.075  1.00 54.65           C  
ANISOU  578  CB  LEU A 931     7304   6209   7251   -279   -207    200       C  
ATOM    579  CG  LEU A 931      -9.666 -16.784 -79.634  1.00 53.67           C  
ANISOU  579  CG  LEU A 931     7247   6184   6964   -517   -181    155       C  
ATOM    580  CD1 LEU A 931      -8.354 -17.236 -79.013  1.00 51.01           C  
ANISOU  580  CD1 LEU A 931     6800   5984   6598   -507    -82    -76       C  
ATOM    581  CD2 LEU A 931      -9.609 -16.890 -81.148  1.00 55.97           C  
ANISOU  581  CD2 LEU A 931     7594   6607   7064   -794   -224    201       C  
ATOM    582  N   PHE A 932     -13.684 -18.515 -78.111  1.00 70.54           N  
ANISOU  582  N   PHE A 932     9215   7934   9653     92   -236    331       N  
ATOM    583  CA  PHE A 932     -14.586 -19.575 -77.675  1.00 73.95           C  
ANISOU  583  CA  PHE A 932     9579   8352  10167    219   -199    294       C  
ATOM    584  C   PHE A 932     -15.812 -19.671 -78.578  1.00 75.35           C  
ANISOU  584  C   PHE A 932     9683   8464  10484    230   -319    439       C  
ATOM    585  O   PHE A 932     -16.110 -20.738 -79.121  1.00 75.85           O  
ANISOU  585  O   PHE A 932     9709   8643  10470    219   -354    442       O  
ATOM    586  CB  PHE A 932     -15.009 -19.350 -76.222  1.00 73.86           C  
ANISOU  586  CB  PHE A 932     9590   8204  10270    296    -53    192       C  
ATOM    587  CG  PHE A 932     -16.009 -20.349 -75.721  1.00 72.28           C  
ANISOU  587  CG  PHE A 932     9347   7982  10134    366     11    143       C  
ATOM    588  CD1 PHE A 932     -15.714 -21.701 -75.719  1.00 71.69           C  
ANISOU  588  CD1 PHE A 932     9288   8041   9909    375    -27    119       C  
ATOM    589  CD2 PHE A 932     -17.240 -19.936 -75.242  1.00 72.94           C  
ANISOU  589  CD2 PHE A 932     9356   7887  10471    410    124     94       C  
ATOM    590  CE1 PHE A 932     -16.631 -22.623 -75.257  1.00 70.66           C  
ANISOU  590  CE1 PHE A 932     9150   7884   9814    404     29     84       C  
ATOM    591  CE2 PHE A 932     -18.161 -20.854 -74.777  1.00 70.19           C  
ANISOU  591  CE2 PHE A 932     8970   7534  10164    429    217     19       C  
ATOM    592  CZ  PHE A 932     -17.856 -22.199 -74.785  1.00 66.84           C  
ANISOU  592  CZ  PHE A 932     8614   7262   9522    415    161     32       C  
ATOM    593  N   ASN A 933     -16.511 -18.551 -78.742  1.00 74.12           N  
ANISOU  593  N   ASN A 933     9492   8099  10571    244   -408    563       N  
ATOM    594  CA  ASN A 933     -17.683 -18.503 -79.610  1.00 69.86           C  
ANISOU  594  CA  ASN A 933     8854   7453  10236    244   -610    747       C  
ATOM    595  C   ASN A 933     -17.357 -18.855 -81.057  1.00 65.45           C  
ANISOU  595  C   ASN A 933     8387   7080   9401     20   -807    905       C  
ATOM    596  O   ASN A 933     -18.125 -19.552 -81.721  1.00 66.97           O  
ANISOU  596  O   ASN A 933     8527   7325   9594    -22   -927    992       O  
ATOM    597  CB  ASN A 933     -18.359 -17.134 -79.536  1.00 72.77           C  
ANISOU  597  CB  ASN A 933     9138   7496  11015    301   -728    864       C  
ATOM    598  CG  ASN A 933     -19.215 -16.978 -78.298  1.00 84.88           C  
ANISOU  598  CG  ASN A 933    10505   8821  12926    486   -505    660       C  
ATOM    599  OD1 ASN A 933     -20.419 -17.234 -78.327  1.00 85.99           O  
ANISOU  599  OD1 ASN A 933    10448   8831  13391    582   -544    662       O  
ATOM    600  ND2 ASN A 933     -18.598 -16.560 -77.199  1.00 94.74           N  
ANISOU  600  ND2 ASN A 933    11830  10044  14123    492   -253    457       N  
ATOM    601  N   GLN A 934     -16.215 -18.375 -81.540  1.00 57.66           N  
ANISOU  601  N   GLN A 934     7546   6204   8159   -173   -816    915       N  
ATOM    602  CA  GLN A 934     -15.771 -18.695 -82.891  1.00 55.76           C  
ANISOU  602  CA  GLN A 934     7427   6171   7588   -487   -923    992       C  
ATOM    603  C   GLN A 934     -15.580 -20.196 -83.066  1.00 57.48           C  
ANISOU  603  C   GLN A 934     7594   6618   7627   -499   -764    793       C  
ATOM    604  O   GLN A 934     -15.971 -20.761 -84.085  1.00 59.22           O  
ANISOU  604  O   GLN A 934     7852   6956   7693   -704   -860    861       O  
ATOM    605  CB  GLN A 934     -14.471 -17.961 -83.226  1.00 59.66           C  
ANISOU  605  CB  GLN A 934     8071   6761   7836   -721   -871    950       C  
ATOM    606  CG  GLN A 934     -14.652 -16.494 -83.559  1.00 67.32           C  
ANISOU  606  CG  GLN A 934     9161   7513   8905   -847  -1108   1215       C  
ATOM    607  CD  GLN A 934     -13.344 -15.823 -83.920  1.00 75.83           C  
ANISOU  607  CD  GLN A 934    10410   8711   9691  -1130  -1032   1156       C  
ATOM    608  OE1 GLN A 934     -13.292 -14.611 -84.133  1.00 88.47           O  
ANISOU  608  OE1 GLN A 934    12142  10132  11341  -1260  -1206   1355       O  
ATOM    609  NE2 GLN A 934     -12.277 -16.610 -83.991  1.00 69.81           N  
ANISOU  609  NE2 GLN A 934     9626   8229   8668  -1235   -774    866       N  
ATOM    610  N   ASP A 935     -14.981 -20.837 -82.066  1.00 58.24           N  
ANISOU  610  N   ASP A 935     7613   6756   7758   -305   -547    559       N  
ATOM    611  CA  ASP A 935     -14.725 -22.272 -82.121  1.00 58.83           C  
ANISOU  611  CA  ASP A 935     7618   6978   7755   -283   -416    363       C  
ATOM    612  C   ASP A 935     -16.018 -23.076 -82.018  1.00 64.31           C  
ANISOU  612  C   ASP A 935     8246   7616   8574   -160   -466    427       C  
ATOM    613  O   ASP A 935     -16.154 -24.129 -82.645  1.00 68.14           O  
ANISOU  613  O   ASP A 935     8710   8220   8961   -252   -432    349       O  
ATOM    614  CB  ASP A 935     -13.753 -22.691 -81.018  1.00 58.07           C  
ANISOU  614  CB  ASP A 935     7460   6882   7722   -116   -270    159       C  
ATOM    615  CG  ASP A 935     -12.365 -22.119 -81.215  1.00 65.70           C  
ANISOU  615  CG  ASP A 935     8439   7940   8583   -257   -202     39       C  
ATOM    616  OD1 ASP A 935     -11.977 -21.880 -82.378  1.00 71.19           O  
ANISOU  616  OD1 ASP A 935     9186   8767   9097   -537   -184     13       O  
ATOM    617  OD2 ASP A 935     -11.661 -21.910 -80.205  1.00 67.82           O  
ANISOU  617  OD2 ASP A 935     8678   8160   8930   -135   -165    -37       O  
ATOM    618  N   VAL A 936     -16.962 -22.581 -81.222  1.00 62.10           N  
ANISOU  618  N   VAL A 936     7916   7149   8529     24   -513    529       N  
ATOM    619  CA  VAL A 936     -18.261 -23.234 -81.093  1.00 63.14           C  
ANISOU  619  CA  VAL A 936     7955   7219   8816    122   -545    570       C  
ATOM    620  C   VAL A 936     -19.027 -23.166 -82.412  1.00 68.48           C  
ANISOU  620  C   VAL A 936     8625   7932   9462    -63   -769    766       C  
ATOM    621  O   VAL A 936     -19.539 -24.178 -82.898  1.00 70.91           O  
ANISOU  621  O   VAL A 936     8907   8341   9695   -128   -779    745       O  
ATOM    622  CB  VAL A 936     -19.107 -22.608 -79.962  1.00 60.18           C  
ANISOU  622  CB  VAL A 936     7492   6625   8751    311   -492    567       C  
ATOM    623  CG1 VAL A 936     -20.528 -23.146 -79.992  1.00 50.73           C  
ANISOU  623  CG1 VAL A 936     6154   5360   7760    372   -526    596       C  
ATOM    624  CG2 VAL A 936     -18.465 -22.873 -78.609  1.00 61.27           C  
ANISOU  624  CG2 VAL A 936     7690   6755   8835    403   -284    383       C  
ATOM    625  N   ASP A 937     -19.091 -21.971 -82.990  1.00 71.30           N  
ANISOU  625  N   ASP A 937     9025   8194   9869   -180   -980    975       N  
ATOM    626  CA  ASP A 937     -19.770 -21.766 -84.265  1.00 81.57           C  
ANISOU  626  CA  ASP A 937    10364   9507  11120   -426  -1293   1236       C  
ATOM    627  C   ASP A 937     -19.107 -22.565 -85.385  1.00 78.37           C  
ANISOU  627  C   ASP A 937    10120   9391  10265   -776  -1251   1169       C  
ATOM    628  O   ASP A 937     -19.786 -23.126 -86.244  1.00 84.42           O  
ANISOU  628  O   ASP A 937    10908  10250  10919   -978  -1399   1271       O  
ATOM    629  CB  ASP A 937     -19.808 -20.278 -84.621  1.00 96.38           C  
ANISOU  629  CB  ASP A 937    12295  11183  13141   -518  -1575   1504       C  
ATOM    630  CG  ASP A 937     -20.688 -19.475 -83.679  1.00103.93           C  
ANISOU  630  CG  ASP A 937    13036  11801  14653   -201  -1625   1545       C  
ATOM    631  OD1 ASP A 937     -20.920 -19.934 -82.541  1.00101.43           O  
ANISOU  631  OD1 ASP A 937    12584  11450  14506     56  -1341   1301       O  
ATOM    632  OD2 ASP A 937     -21.146 -18.383 -84.077  1.00110.45           O  
ANISOU  632  OD2 ASP A 937    13829  12376  15762   -243  -1947   1808       O  
ATOM    633  N   ALA A 938     -17.779 -22.615 -85.365  1.00 72.05           N  
ANISOU  633  N   ALA A 938     9414   8731   9231   -872  -1028    962       N  
ATOM    634  CA  ALA A 938     -17.027 -23.395 -86.341  1.00 67.08           C  
ANISOU  634  CA  ALA A 938     8890   8362   8235  -1216   -882    779       C  
ATOM    635  C   ALA A 938     -17.309 -24.882 -86.167  1.00 63.21           C  
ANISOU  635  C   ALA A 938     8288   7951   7780  -1102   -700    559       C  
ATOM    636  O   ALA A 938     -17.317 -25.637 -87.138  1.00 64.60           O  
ANISOU  636  O   ALA A 938     8526   8299   7719  -1407   -644    461       O  
ATOM    637  CB  ALA A 938     -15.537 -23.116 -86.220  1.00 63.21           C  
ANISOU  637  CB  ALA A 938     8439   7966   7610  -1299   -653    545       C  
ATOM    638  N   ALA A 939     -17.535 -25.297 -84.924  1.00 61.68           N  
ANISOU  638  N   ALA A 939     7952   7621   7861   -708   -601    474       N  
ATOM    639  CA  ALA A 939     -17.884 -26.683 -84.642  1.00 60.90           C  
ANISOU  639  CA  ALA A 939     7768   7545   7825   -589   -468    307       C  
ATOM    640  C   ALA A 939     -19.266 -27.003 -85.199  1.00 65.13           C  
ANISOU  640  C   ALA A 939     8291   8087   8369   -677   -640    482       C  
ATOM    641  O   ALA A 939     -19.473 -28.060 -85.795  1.00 69.77           O  
ANISOU  641  O   ALA A 939     8887   8790   8831   -829   -566    367       O  
ATOM    642  CB  ALA A 939     -17.833 -26.956 -83.147  1.00 54.65           C  
ANISOU  642  CB  ALA A 939     6892   6601   7273   -230   -371    227       C  
ATOM    643  N   VAL A 940     -20.206 -26.082 -85.005  1.00 61.88           N  
ANISOU  643  N   VAL A 940     7831   7530   8151   -585   -870    741       N  
ATOM    644  CA  VAL A 940     -21.566 -26.255 -85.507  1.00 63.13           C  
ANISOU  644  CA  VAL A 940     7919   7660   8407   -655  -1094    931       C  
ATOM    645  C   VAL A 940     -21.592 -26.331 -87.032  1.00 69.29           C  
ANISOU  645  C   VAL A 940     8853   8624   8852  -1110  -1285   1064       C  
ATOM    646  O   VAL A 940     -22.210 -27.229 -87.609  1.00 68.66           O  
ANISOU  646  O   VAL A 940     8774   8656   8660  -1275  -1311   1047       O  
ATOM    647  CB  VAL A 940     -22.492 -25.119 -85.031  1.00 62.89           C  
ANISOU  647  CB  VAL A 940     7742   7381   8773   -465  -1324   1157       C  
ATOM    648  CG1 VAL A 940     -23.841 -25.198 -85.732  1.00 64.32           C  
ANISOU  648  CG1 VAL A 940     7807   7519   9111   -574  -1638   1383       C  
ATOM    649  CG2 VAL A 940     -22.664 -25.173 -83.522  1.00 60.41           C  
ANISOU  649  CG2 VAL A 940     7292   6912   8747   -109  -1081    973       C  
ATOM    650  N   ARG A 941     -20.912 -25.387 -87.678  1.00 71.44           N  
ANISOU  650  N   ARG A 941     9284   8932   8928  -1367  -1412   1192       N  
ATOM    651  CA  ARG A 941     -20.810 -25.375 -89.134  1.00 66.51           C  
ANISOU  651  CA  ARG A 941     8881   8503   7888  -1920  -1583   1315       C  
ATOM    652  C   ARG A 941     -20.098 -26.627 -89.634  1.00 61.69           C  
ANISOU  652  C   ARG A 941     8346   8146   6947  -2166  -1217    940       C  
ATOM    653  O   ARG A 941     -20.415 -27.152 -90.703  1.00 66.51           O  
ANISOU  653  O   ARG A 941     9091   8936   7245  -2601  -1278    955       O  
ATOM    654  CB  ARG A 941     -20.080 -24.119 -89.615  1.00 67.05           C  
ANISOU  654  CB  ARG A 941     9142   8556   7777  -2184  -1742   1491       C  
ATOM    655  CG  ARG A 941     -20.823 -22.823 -89.325  1.00 72.61           C  
ANISOU  655  CG  ARG A 941     9778   8959   8852  -2005  -2161   1886       C  
ATOM    656  CD  ARG A 941     -20.116 -21.615 -89.925  1.00 80.16           C  
ANISOU  656  CD  ARG A 941    10977   9887   9592  -2339  -2361   2097       C  
ATOM    657  NE  ARG A 941     -18.791 -21.402 -89.350  1.00 82.55           N  
ANISOU  657  NE  ARG A 941    11313  10254   9797  -2236  -1976   1796       N  
ATOM    658  CZ  ARG A 941     -17.653 -21.756 -89.940  1.00 83.41           C  
ANISOU  658  CZ  ARG A 941    11595  10632   9463  -2606  -1690   1534       C  
ATOM    659  NH1 ARG A 941     -17.674 -22.341 -91.130  1.00 85.90           N  
ANISOU  659  NH1 ARG A 941    12103  11191   9344  -3143  -1702   1510       N  
ATOM    660  NH2 ARG A 941     -16.493 -21.522 -89.340  1.00 79.05           N  
ANISOU  660  NH2 ARG A 941    11011  10108   8918  -2472  -1376   1265       N  
ATOM    661  N   GLY A 942     -19.140 -27.104 -88.847  1.00 59.69           N  
ANISOU  661  N   GLY A 942     7994   7884   6800  -1901   -849    596       N  
ATOM    662  CA  GLY A 942     -18.440 -28.337 -89.153  1.00 65.54           C  
ANISOU  662  CA  GLY A 942     8720   8777   7405  -2040   -487    189       C  
ATOM    663  C   GLY A 942     -19.374 -29.530 -89.100  1.00 68.98           C  
ANISOU  663  C   GLY A 942     9072   9207   7929  -1953   -459    133       C  
ATOM    664  O   GLY A 942     -19.237 -30.472 -89.880  1.00 75.03           O  
ANISOU  664  O   GLY A 942     9890  10125   8494  -2263   -270   -107       O  
ATOM    665  N   ILE A 943     -20.328 -29.490 -88.176  1.00 64.87           N  
ANISOU  665  N   ILE A 943     8423   8512   7714  -1564   -614    319       N  
ATOM    666  CA  ILE A 943     -21.326 -30.547 -88.067  1.00 68.41           C  
ANISOU  666  CA  ILE A 943     8794   8948   8252  -1490   -605    292       C  
ATOM    667  C   ILE A 943     -22.282 -30.506 -89.253  1.00 82.15           C  
ANISOU  667  C   ILE A 943    10628  10823   9762  -1896   -871    513       C  
ATOM    668  O   ILE A 943     -22.560 -31.532 -89.875  1.00 91.35           O  
ANISOU  668  O   ILE A 943    11837  12118  10753  -2140   -767    366       O  
ATOM    669  CB  ILE A 943     -22.133 -30.437 -86.760  1.00 60.89           C  
ANISOU  669  CB  ILE A 943     7680   7784   7670  -1040   -671    404       C  
ATOM    670  CG1 ILE A 943     -21.229 -30.683 -85.553  1.00 56.91           C  
ANISOU  670  CG1 ILE A 943     7131   7159   7333   -714   -438    198       C  
ATOM    671  CG2 ILE A 943     -23.286 -31.426 -86.760  1.00 57.69           C  
ANISOU  671  CG2 ILE A 943     7204   7384   7333  -1032   -686    399       C  
ATOM    672  CD1 ILE A 943     -21.948 -30.620 -84.222  1.00 54.38           C  
ANISOU  672  CD1 ILE A 943     6714   6658   7292   -379   -445    262       C  
ATOM    673  N   LEU A 944     -22.774 -29.312 -89.566  1.00 82.61           N  
ANISOU  673  N   LEU A 944    10719  10828   9841  -1986  -1245    877       N  
ATOM    674  CA  LEU A 944     -23.732 -29.136 -90.653  1.00 81.43           C  
ANISOU  674  CA  LEU A 944    10656  10765   9519  -2383  -1628   1181       C  
ATOM    675  C   LEU A 944     -23.146 -29.478 -92.023  1.00 86.48           C  
ANISOU  675  C   LEU A 944    11578  11684   9596  -3037  -1562   1082       C  
ATOM    676  O   LEU A 944     -23.848 -30.006 -92.885  1.00 95.39           O  
ANISOU  676  O   LEU A 944    12799  12956  10490  -3422  -1715   1166       O  
ATOM    677  CB  LEU A 944     -24.289 -27.710 -90.652  1.00 79.84           C  
ANISOU  677  CB  LEU A 944    10409  10371   9554  -2324  -2100   1615       C  
ATOM    678  CG  LEU A 944     -25.098 -27.318 -89.413  1.00 76.04           C  
ANISOU  678  CG  LEU A 944     9615   9603   9673  -1762  -2163   1683       C  
ATOM    679  CD1 LEU A 944     -25.612 -25.890 -89.527  1.00 75.76           C  
ANISOU  679  CD1 LEU A 944     9502   9327   9958  -1728  -2632   2078       C  
ATOM    680  CD2 LEU A 944     -26.248 -28.289 -89.199  1.00 77.89           C  
ANISOU  680  CD2 LEU A 944     9660   9840  10094  -1649  -2152   1626       C  
ATOM    681  N   ARG A 945     -21.865 -29.181 -92.223  1.00 83.44           N  
ANISOU  681  N   ARG A 945    11330  11386   8986  -3208  -1312    874       N  
ATOM    682  CA  ARG A 945     -21.211 -29.482 -93.495  1.00 86.58           C  
ANISOU  682  CA  ARG A 945    11999  12061   8838  -3897  -1150    685       C  
ATOM    683  C   ARG A 945     -20.997 -30.980 -93.700  1.00 84.93           C  
ANISOU  683  C   ARG A 945    11743  11983   8544  -4004   -704    211       C  
ATOM    684  O   ARG A 945     -21.076 -31.478 -94.823  1.00 86.16           O  
ANISOU  684  O   ARG A 945    12099  12366   8271  -4617   -635     97       O  
ATOM    685  CB  ARG A 945     -19.874 -28.744 -93.614  1.00 93.01           C  
ANISOU  685  CB  ARG A 945    12931  12927   9481  -4063   -952    531       C  
ATOM    686  CG  ARG A 945     -20.005 -27.251 -93.865  1.00106.27           C  
ANISOU  686  CG  ARG A 945    14776  14524  11077  -4219  -1411   1004       C  
ATOM    687  CD  ARG A 945     -18.657 -26.607 -94.161  1.00117.00           C  
ANISOU  687  CD  ARG A 945    16302  15986  12165  -4520  -1177    815       C  
ATOM    688  NE  ARG A 945     -17.741 -26.670 -93.024  1.00122.00           N  
ANISOU  688  NE  ARG A 945    16687  16499  13170  -3965   -813    491       N  
ATOM    689  CZ  ARG A 945     -16.780 -27.578 -92.885  1.00125.79           C  
ANISOU  689  CZ  ARG A 945    17037  17075  13683  -3933   -301    -45       C  
ATOM    690  NH1 ARG A 945     -16.605 -28.509 -93.813  1.00128.34           N  
ANISOU  690  NH1 ARG A 945    17447  17613  13703  -4419    -18   -378       N  
ATOM    691  NH2 ARG A 945     -15.994 -27.557 -91.818  1.00126.92           N  
ANISOU  691  NH2 ARG A 945    16951  17077  14196  -3434    -84   -257       N  
ATOM    692  N   ASN A 946     -20.725 -31.693 -92.612  1.00 85.16           N  
ANISOU  692  N   ASN A 946    11523  11851   8981  -3445   -414    -62       N  
ATOM    693  CA  ASN A 946     -20.430 -33.120 -92.689  1.00 85.50           C  
ANISOU  693  CA  ASN A 946    11490  11935   9062  -3477      1   -524       C  
ATOM    694  C   ASN A 946     -21.665 -33.950 -93.035  1.00 91.42           C  
ANISOU  694  C   ASN A 946    12257  12736   9743  -3607   -126   -428       C  
ATOM    695  O   ASN A 946     -22.790 -33.574 -92.706  1.00 91.80           O  
ANISOU  695  O   ASN A 946    12250  12703   9925  -3410   -505    -37       O  
ATOM    696  CB  ASN A 946     -19.807 -33.608 -91.379  1.00 75.31           C  
ANISOU  696  CB  ASN A 946     9951  10407   8255  -2856    240   -761       C  
ATOM    697  CG  ASN A 946     -19.095 -34.937 -91.533  1.00 73.49           C  
ANISOU  697  CG  ASN A 946     9622  10160   8143  -2916    681  -1291       C  
ATOM    698  OD1 ASN A 946     -19.702 -35.999 -91.396  1.00 80.94           O  
ANISOU  698  OD1 ASN A 946    10510  11036   9209  -2827    748  -1386       O  
ATOM    699  ND2 ASN A 946     -17.798 -34.885 -91.818  1.00 63.19           N  
ANISOU  699  ND2 ASN A 946     8270   8889   6849  -3071    992  -1661       N  
ATOM    700  N   ALA A 947     -21.447 -35.079 -93.702  1.00 93.28           N  
ANISOU  700  N   ALA A 947    12542  13093   9808  -3950    213   -823       N  
ATOM    701  CA  ALA A 947     -22.545 -35.931 -94.149  1.00 90.41           C  
ANISOU  701  CA  ALA A 947    12221  12808   9321  -4161    132   -779       C  
ATOM    702  C   ALA A 947     -22.938 -36.969 -93.101  1.00 88.94           C  
ANISOU  702  C   ALA A 947    11816  12400   9578  -3619    272   -916       C  
ATOM    703  O   ALA A 947     -24.025 -37.544 -93.166  1.00 93.35           O  
ANISOU  703  O   ALA A 947    12365  12975  10128  -3652    139   -798       O  
ATOM    704  CB  ALA A 947     -22.187 -36.612 -95.462  1.00 92.45           C  
ANISOU  704  CB  ALA A 947    12683  13317   9125  -4897    440  -1149       C  
ATOM    705  N   LYS A 948     -22.052 -37.208 -92.140  1.00 83.08           N  
ANISOU  705  N   LYS A 948    10911  11445   9212  -3158    512  -1149       N  
ATOM    706  CA  LYS A 948     -22.315 -38.180 -91.084  1.00 84.48           C  
ANISOU  706  CA  LYS A 948    10928  11380   9789  -2687    609  -1249       C  
ATOM    707  C   LYS A 948     -22.848 -37.514 -89.819  1.00 85.13           C  
ANISOU  707  C   LYS A 948    10913  11291  10141  -2173    332   -892       C  
ATOM    708  O   LYS A 948     -23.565 -38.136 -89.035  1.00 86.81           O  
ANISOU  708  O   LYS A 948    11057  11363  10561  -1904    301   -838       O  
ATOM    709  CB  LYS A 948     -21.049 -38.976 -90.753  1.00 86.92           C  
ANISOU  709  CB  LYS A 948    11114  11509  10404  -2523    985  -1709       C  
ATOM    710  CG  LYS A 948     -20.714 -40.080 -91.743  1.00 92.48           C  
ANISOU  710  CG  LYS A 948    11837  12279  11022  -2944   1359  -2187       C  
ATOM    711  CD  LYS A 948     -19.448 -40.817 -91.327  1.00 96.54           C  
ANISOU  711  CD  LYS A 948    12140  12530  12010  -2709   1692  -2648       C  
ATOM    712  CE  LYS A 948     -19.226 -42.066 -92.165  1.00107.86           C  
ANISOU  712  CE  LYS A 948    13536  13942  13502  -3062   2101  -3180       C  
ATOM    713  NZ  LYS A 948     -20.307 -43.072 -91.965  1.00112.61           N  
ANISOU  713  NZ  LYS A 948    14190  14448  14148  -2997   2033  -3097       N  
ATOM    714  N   LEU A 949     -22.496 -36.247 -89.626  1.00 81.51           N  
ANISOU  714  N   LEU A 949    10460  10844   9667  -2082    162   -678       N  
ATOM    715  CA  LEU A 949     -22.841 -35.537 -88.400  1.00 72.12           C  
ANISOU  715  CA  LEU A 949     9172   9481   8748  -1630    -26   -418       C  
ATOM    716  C   LEU A 949     -24.221 -34.888 -88.466  1.00 78.95           C  
ANISOU  716  C   LEU A 949    10005  10377   9617  -1646   -360    -55       C  
ATOM    717  O   LEU A 949     -24.948 -34.864 -87.474  1.00 82.73           O  
ANISOU  717  O   LEU A 949    10365  10709  10358  -1328   -424     51       O  
ATOM    718  CB  LEU A 949     -21.782 -34.479 -88.082  1.00 66.00           C  
ANISOU  718  CB  LEU A 949     8396   8668   8014  -1506    -30   -393       C  
ATOM    719  CG  LEU A 949     -20.341 -34.982 -87.986  1.00 66.25           C  
ANISOU  719  CG  LEU A 949     8388   8648   8135  -1469    269   -759       C  
ATOM    720  CD1 LEU A 949     -19.388 -33.843 -87.652  1.00 64.07           C  
ANISOU  720  CD1 LEU A 949     8101   8352   7891  -1363    235   -705       C  
ATOM    721  CD2 LEU A 949     -20.235 -36.093 -86.959  1.00 64.71           C  
ANISOU  721  CD2 LEU A 949     8093   8227   8268  -1128    386   -916       C  
ATOM    722  N   LYS A 950     -24.576 -34.364 -89.635  1.00 86.31           N  
ANISOU  722  N   LYS A 950    11034  11484  10278  -2053   -583    126       N  
ATOM    723  CA  LYS A 950     -25.833 -33.630 -89.796  1.00 88.55           C  
ANISOU  723  CA  LYS A 950    11239  11752  10655  -2079   -991    506       C  
ATOM    724  C   LYS A 950     -27.120 -34.458 -89.620  1.00 85.46           C  
ANISOU  724  C   LYS A 950    10721  11346  10406  -2031  -1046    529       C  
ATOM    725  O   LYS A 950     -28.035 -34.017 -88.921  1.00 86.93           O  
ANISOU  725  O   LYS A 950    10707  11389  10934  -1757  -1218    701       O  
ATOM    726  CB  LYS A 950     -25.858 -32.853 -91.119  1.00 90.84           C  
ANISOU  726  CB  LYS A 950    11699  12207  10610  -2584  -1310    759       C  
ATOM    727  CG  LYS A 950     -27.048 -31.918 -91.252  1.00 96.43           C  
ANISOU  727  CG  LYS A 950    12282  12818  11537  -2570  -1832   1204       C  
ATOM    728  CD  LYS A 950     -26.987 -31.116 -92.538  1.00108.79           C  
ANISOU  728  CD  LYS A 950    14070  14511  12754  -3115  -2229   1519       C  
ATOM    729  CE  LYS A 950     -28.150 -30.142 -92.629  1.00116.47           C  
ANISOU  729  CE  LYS A 950    14871  15304  14078  -3058  -2833   1998       C  
ATOM    730  NZ  LYS A 950     -29.464 -30.839 -92.553  1.00119.25           N  
ANISOU  730  NZ  LYS A 950    14996  15641  14674  -2989  -2976   2046       N  
ATOM    731  N   PRO A 951     -27.208 -35.647 -90.254  1.00 79.28           N  
ANISOU  731  N   PRO A 951    10036  10704   9385  -2320   -874    322       N  
ATOM    732  CA  PRO A 951     -28.416 -36.452 -90.033  1.00 73.68           C  
ANISOU  732  CA  PRO A 951     9206   9978   8810  -2279   -909    330       C  
ATOM    733  C   PRO A 951     -28.587 -36.828 -88.566  1.00 75.52           C  
ANISOU  733  C   PRO A 951     9299   9998   9399  -1797   -706    210       C  
ATOM    734  O   PRO A 951     -29.716 -36.951 -88.089  1.00 79.57           O  
ANISOU  734  O   PRO A 951     9648  10451  10135  -1679   -797    293       O  
ATOM    735  CB  PRO A 951     -28.155 -37.711 -90.864  1.00 71.36           C  
ANISOU  735  CB  PRO A 951     9078   9841   8195  -2658   -659     44       C  
ATOM    736  CG  PRO A 951     -27.210 -37.276 -91.917  1.00 78.90           C  
ANISOU  736  CG  PRO A 951    10231  10963   8785  -3069   -638     -5       C  
ATOM    737  CD  PRO A 951     -26.321 -36.271 -91.254  1.00 81.13           C  
ANISOU  737  CD  PRO A 951    10475  11115   9235  -2747   -633     51       C  
ATOM    738  N   VAL A 952     -27.473 -37.006 -87.863  1.00 73.48           N  
ANISOU  738  N   VAL A 952     9105   9626   9189  -1569   -445     11       N  
ATOM    739  CA  VAL A 952     -27.511 -37.291 -86.436  1.00 70.22           C  
ANISOU  739  CA  VAL A 952     8627   9008   9044  -1190   -294    -65       C  
ATOM    740  C   VAL A 952     -27.889 -36.035 -85.659  1.00 68.98           C  
ANISOU  740  C   VAL A 952     8330   8748   9129   -944   -449    134       C  
ATOM    741  O   VAL A 952     -28.740 -36.077 -84.773  1.00 76.29           O  
ANISOU  741  O   VAL A 952     9137   9572  10277   -782   -420    143       O  
ATOM    742  CB  VAL A 952     -26.155 -37.823 -85.927  1.00 65.40           C  
ANISOU  742  CB  VAL A 952     8121   8280   8448  -1044    -53   -294       C  
ATOM    743  CG1 VAL A 952     -26.179 -37.985 -84.416  1.00 44.12           C  
ANISOU  743  CG1 VAL A 952     5416   5375   5973   -724     19   -298       C  
ATOM    744  CG2 VAL A 952     -25.814 -39.143 -86.603  1.00 47.05           C  
ANISOU  744  CG2 VAL A 952     5880   5985   6012  -1256    143   -559       C  
ATOM    745  N   TYR A 953     -27.258 -34.919 -86.012  1.00 62.83           N  
ANISOU  745  N   TYR A 953     7568   7991   8315   -953   -585    262       N  
ATOM    746  CA  TYR A 953     -27.475 -33.645 -85.333  1.00 65.94           C  
ANISOU  746  CA  TYR A 953     7830   8253   8970   -728   -716    423       C  
ATOM    747  C   TYR A 953     -28.936 -33.206 -85.373  1.00 82.50           C  
ANISOU  747  C   TYR A 953     9692  10300  11355   -719   -941    591       C  
ATOM    748  O   TYR A 953     -29.477 -32.732 -84.373  1.00 88.69           O  
ANISOU  748  O   TYR A 953    10303  10925  12472   -488   -884    565       O  
ATOM    749  CB  TYR A 953     -26.590 -32.564 -85.954  1.00 63.03           C  
ANISOU  749  CB  TYR A 953     7544   7923   8481   -818   -862    553       C  
ATOM    750  CG  TYR A 953     -26.719 -31.204 -85.309  1.00 68.59           C  
ANISOU  750  CG  TYR A 953     8123   8459   9478   -596   -993    706       C  
ATOM    751  CD1 TYR A 953     -26.016 -30.893 -84.151  1.00 70.49           C  
ANISOU  751  CD1 TYR A 953     8385   8578   9820   -338   -786    582       C  
ATOM    752  CD2 TYR A 953     -27.534 -30.226 -85.863  1.00 72.13           C  
ANISOU  752  CD2 TYR A 953     8430   8845  10130   -665  -1347    978       C  
ATOM    753  CE1 TYR A 953     -26.128 -29.649 -83.559  1.00 73.52           C  
ANISOU  753  CE1 TYR A 953     8660   8800  10474   -166   -861    676       C  
ATOM    754  CE2 TYR A 953     -27.653 -28.979 -85.278  1.00 79.50           C  
ANISOU  754  CE2 TYR A 953     9223   9572  11413   -453  -1451   1084       C  
ATOM    755  CZ  TYR A 953     -26.948 -28.696 -84.127  1.00 82.01           C  
ANISOU  755  CZ  TYR A 953     9572   9789  11799   -209  -1173    909       C  
ATOM    756  OH  TYR A 953     -27.064 -27.455 -83.544  1.00 87.02           O  
ANISOU  756  OH  TYR A 953    10071  10211  12782    -29  -1234    971       O  
ATOM    757  N   ASP A 954     -29.567 -33.365 -86.531  1.00 90.62           N  
ANISOU  757  N   ASP A 954    10698  11458  12275  -1005  -1195    740       N  
ATOM    758  CA  ASP A 954     -30.961 -32.969 -86.704  1.00 91.87           C  
ANISOU  758  CA  ASP A 954    10581  11553  12772  -1016  -1487    922       C  
ATOM    759  C   ASP A 954     -31.909 -33.854 -85.900  1.00 96.54           C  
ANISOU  759  C   ASP A 954    11012  12104  13563   -902  -1266    724       C  
ATOM    760  O   ASP A 954     -32.970 -33.406 -85.463  1.00 98.36           O  
ANISOU  760  O   ASP A 954    10933  12204  14234   -775  -1359    752       O  
ATOM    761  CB  ASP A 954     -31.346 -32.999 -88.186  1.00 88.20           C  
ANISOU  761  CB  ASP A 954    10177  11255  12081  -1425  -1868   1164       C  
ATOM    762  CG  ASP A 954     -30.615 -31.949 -88.998  1.00 88.21           C  
ANISOU  762  CG  ASP A 954    10336  11278  11903  -1615  -2155   1413       C  
ATOM    763  OD1 ASP A 954     -30.421 -30.828 -88.483  1.00 90.84           O  
ANISOU  763  OD1 ASP A 954    10563  11417  12535  -1372  -2252   1521       O  
ATOM    764  OD2 ASP A 954     -30.232 -32.246 -90.149  1.00 88.34           O  
ANISOU  764  OD2 ASP A 954    10599  11503  11462  -2050  -2263   1481       O  
ATOM    765  N   SER A 955     -31.520 -35.110 -85.706  1.00 96.03           N  
ANISOU  765  N   SER A 955    11147  12128  13211   -964   -967    505       N  
ATOM    766  CA  SER A 955     -32.352 -36.068 -84.987  1.00 94.55           C  
ANISOU  766  CA  SER A 955    10880  11912  13131   -927   -750    323       C  
ATOM    767  C   SER A 955     -32.002 -36.122 -83.503  1.00 87.68           C  
ANISOU  767  C   SER A 955    10063  10887  12365   -684   -433    138       C  
ATOM    768  O   SER A 955     -32.115 -37.171 -82.869  1.00 91.26           O  
ANISOU  768  O   SER A 955    10633  11320  12721   -709   -195    -32       O  
ATOM    769  CB  SER A 955     -32.221 -37.460 -85.606  1.00102.27           C  
ANISOU  769  CB  SER A 955    12060  13032  13765  -1170   -633    203       C  
ATOM    770  OG  SER A 955     -30.893 -37.943 -85.497  1.00105.41           O  
ANISOU  770  OG  SER A 955    12718  13414  13921  -1139   -426     64       O  
ATOM    771  N   LEU A 956     -31.577 -34.988 -82.955  1.00 78.58           N  
ANISOU  771  N   LEU A 956     8852   9617  11387   -494   -449    185       N  
ATOM    772  CA  LEU A 956     -31.242 -34.899 -81.538  1.00 70.63           C  
ANISOU  772  CA  LEU A 956     7918   8476  10441   -333   -171     24       C  
ATOM    773  C   LEU A 956     -31.933 -33.715 -80.876  1.00 67.19           C  
ANISOU  773  C   LEU A 956     7202   7897  10429   -200   -156     -4       C  
ATOM    774  O   LEU A 956     -32.129 -32.671 -81.499  1.00 67.82           O  
ANISOU  774  O   LEU A 956     7078   7928  10761   -143   -414    159       O  
ATOM    775  CB  LEU A 956     -29.728 -34.773 -81.346  1.00 64.31           C  
ANISOU  775  CB  LEU A 956     7375   7659   9403   -251   -126     34       C  
ATOM    776  CG  LEU A 956     -28.864 -35.998 -81.644  1.00 60.98           C  
ANISOU  776  CG  LEU A 956     7201   7291   8678   -335    -52    -37       C  
ATOM    777  CD1 LEU A 956     -27.391 -35.663 -81.467  1.00 62.44           C  
ANISOU  777  CD1 LEU A 956     7537   7432   8755   -232    -40    -39       C  
ATOM    778  CD2 LEU A 956     -29.261 -37.165 -80.760  1.00 58.00           C  
ANISOU  778  CD2 LEU A 956     6939   6840   8258   -379    139   -174       C  
ATOM    779  N   ASP A 957     -32.299 -33.882 -79.609  1.00 66.22           N  
ANISOU  779  N   ASP A 957     7076   7688  10398   -189    150   -223       N  
ATOM    780  CA  ASP A 957     -32.823 -32.776 -78.819  1.00 78.18           C  
ANISOU  780  CA  ASP A 957     8336   9044  12323    -92    277   -353       C  
ATOM    781  C   ASP A 957     -31.696 -31.793 -78.517  1.00 83.78           C  
ANISOU  781  C   ASP A 957     9179   9676  12978     41    256   -285       C  
ATOM    782  O   ASP A 957     -30.524 -32.114 -78.712  1.00 90.13           O  
ANISOU  782  O   ASP A 957    10280  10556  13409     47    194   -177       O  
ATOM    783  CB  ASP A 957     -33.456 -33.286 -77.524  1.00 83.98           C  
ANISOU  783  CB  ASP A 957     9093   9739  13075   -226    677   -657       C  
ATOM    784  CG  ASP A 957     -32.548 -34.230 -76.761  1.00 86.13           C  
ANISOU  784  CG  ASP A 957     9825  10058  12841   -344    839   -685       C  
ATOM    785  OD1 ASP A 957     -31.756 -33.751 -75.922  1.00 88.83           O  
ANISOU  785  OD1 ASP A 957    10356  10335  13061   -328    950   -720       O  
ATOM    786  OD2 ASP A 957     -32.627 -35.453 -77.002  1.00 87.12           O  
ANISOU  786  OD2 ASP A 957    10121  10264  12716   -465    826   -659       O  
ATOM    787  N   ALA A 958     -32.055 -30.604 -78.041  1.00 84.07           N  
ANISOU  787  N   ALA A 958     8967   9544  13430    142    322   -378       N  
ATOM    788  CA  ALA A 958     -31.086 -29.534 -77.803  1.00 89.97           C  
ANISOU  788  CA  ALA A 958     9806  10200  14177    260    291   -316       C  
ATOM    789  C   ALA A 958     -29.931 -29.955 -76.894  1.00 88.65           C  
ANISOU  789  C   ALA A 958    10038  10095  13549    199    496   -385       C  
ATOM    790  O   ALA A 958     -28.785 -29.554 -77.104  1.00 90.10           O  
ANISOU  790  O   ALA A 958    10398  10299  13537    268    372   -247       O  
ATOM    791  CB  ALA A 958     -31.785 -28.304 -77.240  1.00 96.46           C  
ANISOU  791  CB  ALA A 958    10283  10789  15580    352    415   -492       C  
ATOM    792  N   VAL A 959     -30.241 -30.769 -75.890  1.00 85.29           N  
ANISOU  792  N   VAL A 959     9757   9693  12957     37    781   -585       N  
ATOM    793  CA  VAL A 959     -29.237 -31.236 -74.941  1.00 83.65           C  
ANISOU  793  CA  VAL A 959     9939   9511  12332    -71    904   -610       C  
ATOM    794  C   VAL A 959     -28.220 -32.156 -75.615  1.00 81.38           C  
ANISOU  794  C   VAL A 959     9890   9320  11710    -31    669   -403       C  
ATOM    795  O   VAL A 959     -27.010 -31.913 -75.562  1.00 87.07           O  
ANISOU  795  O   VAL A 959    10778  10038  12266     37    566   -305       O  
ATOM    796  CB  VAL A 959     -29.891 -31.976 -73.763  1.00 83.91           C  
ANISOU  796  CB  VAL A 959    10117   9540  12226   -341   1218   -838       C  
ATOM    797  CG1 VAL A 959     -28.851 -32.325 -72.714  1.00 88.47           C  
ANISOU  797  CG1 VAL A 959    11121  10111  12384   -504   1263   -809       C  
ATOM    798  CG2 VAL A 959     -30.998 -31.129 -73.157  1.00 76.94           C  
ANISOU  798  CG2 VAL A 959     8930   8560  11741   -420   1531  -1143       C  
ATOM    799  N   ARG A 960     -28.719 -33.211 -76.251  1.00 73.64           N  
ANISOU  799  N   ARG A 960     8896   8412  10672    -84    606   -372       N  
ATOM    800  CA  ARG A 960     -27.858 -34.150 -76.960  1.00 73.80           C  
ANISOU  800  CA  ARG A 960     9091   8494  10456    -65    435   -249       C  
ATOM    801  C   ARG A 960     -27.147 -33.472 -78.129  1.00 76.66           C  
ANISOU  801  C   ARG A 960     9359   8919  10848     56    226   -112       C  
ATOM    802  O   ARG A 960     -26.014 -33.828 -78.471  1.00 78.09           O  
ANISOU  802  O   ARG A 960     9680   9122  10866     85    145    -70       O  
ATOM    803  CB  ARG A 960     -28.659 -35.362 -77.434  1.00 73.48           C  
ANISOU  803  CB  ARG A 960     9039   8509  10370   -181    446   -280       C  
ATOM    804  CG  ARG A 960     -29.203 -36.211 -76.294  1.00 77.79           C  
ANISOU  804  CG  ARG A 960     9759   8993  10806   -364    645   -402       C  
ATOM    805  CD  ARG A 960     -29.915 -37.447 -76.814  1.00 82.39           C  
ANISOU  805  CD  ARG A 960    10349   9623  11334   -485    649   -430       C  
ATOM    806  NE  ARG A 960     -30.296 -38.353 -75.734  1.00 84.47           N  
ANISOU  806  NE  ARG A 960    10850   9812  11434   -707    813   -518       N  
ATOM    807  CZ  ARG A 960     -31.468 -38.321 -75.110  1.00 89.76           C  
ANISOU  807  CZ  ARG A 960    11435  10502  12169   -894   1045   -686       C  
ATOM    808  NH1 ARG A 960     -32.381 -37.425 -75.457  1.00 96.56           N  
ANISOU  808  NH1 ARG A 960    11919  11423  13346   -832   1121   -791       N  
ATOM    809  NH2 ARG A 960     -31.728 -39.184 -74.138  1.00 91.42           N  
ANISOU  809  NH2 ARG A 960    11928  10651  12156  -1169   1190   -755       N  
ATOM    810  N   ARG A 961     -27.813 -32.491 -78.732  1.00 76.30           N  
ANISOU  810  N   ARG A 961     9068   8882  11042    100    130    -51       N  
ATOM    811  CA  ARG A 961     -27.182 -31.661 -79.749  1.00 74.48           C  
ANISOU  811  CA  ARG A 961     8792   8695  10812    146    -86    108       C  
ATOM    812  C   ARG A 961     -25.970 -30.964 -79.156  1.00 72.31           C  
ANISOU  812  C   ARG A 961     8652   8366  10455    235    -44    103       C  
ATOM    813  O   ARG A 961     -24.906 -30.931 -79.767  1.00 74.66           O  
ANISOU  813  O   ARG A 961     9053   8733  10583    227   -135    161       O  
ATOM    814  CB  ARG A 961     -28.157 -30.620 -80.296  1.00 76.96           C  
ANISOU  814  CB  ARG A 961     8823   8949  11467    172   -260    217       C  
ATOM    815  CG  ARG A 961     -29.048 -31.125 -81.415  1.00 80.11           C  
ANISOU  815  CG  ARG A 961     9094   9444  11899     42   -463    325       C  
ATOM    816  CD  ARG A 961     -29.905 -30.001 -81.969  1.00 82.42           C  
ANISOU  816  CD  ARG A 961     9092   9625  12599     71   -747    496       C  
ATOM    817  NE  ARG A 961     -30.734 -30.447 -83.083  1.00 87.94           N  
ANISOU  817  NE  ARG A 961     9680  10422  13311   -100  -1019    648       N  
ATOM    818  CZ  ARG A 961     -31.561 -29.658 -83.758  1.00 95.30           C  
ANISOU  818  CZ  ARG A 961    10351  11252  14607   -124  -1385    863       C  
ATOM    819  NH1 ARG A 961     -31.671 -28.378 -83.432  1.00 97.17           N  
ANISOU  819  NH1 ARG A 961    10390  11253  15277     44  -1498    927       N  
ATOM    820  NH2 ARG A 961     -32.278 -30.148 -84.760  1.00100.09           N  
ANISOU  820  NH2 ARG A 961    10890  11969  15172   -332  -1664   1020       N  
ATOM    821  N   ALA A 962     -26.137 -30.416 -77.957  1.00 69.63           N  
ANISOU  821  N   ALA A 962     8310   7912  10235    280    122      2       N  
ATOM    822  CA  ALA A 962     -25.037 -29.758 -77.263  1.00 67.43           C  
ANISOU  822  CA  ALA A 962     8172   7584   9862    329    166    -11       C  
ATOM    823  C   ALA A 962     -23.921 -30.747 -76.931  1.00 68.57           C  
ANISOU  823  C   ALA A 962     8558   7767   9727    299    157    -18       C  
ATOM    824  O   ALA A 962     -22.746 -30.385 -76.925  1.00 73.33           O  
ANISOU  824  O   ALA A 962     9242   8376  10242    345     90     18       O  
ATOM    825  CB  ALA A 962     -25.533 -29.064 -76.006  1.00 63.72           C  
ANISOU  825  CB  ALA A 962     7673   6993   9546    304    387   -162       C  
ATOM    826  N   ALA A 963     -24.288 -31.996 -76.660  1.00 61.12           N  
ANISOU  826  N   ALA A 963     7709   6824   8690    219    205    -65       N  
ATOM    827  CA  ALA A 963     -23.290 -33.033 -76.406  1.00 57.01           C  
ANISOU  827  CA  ALA A 963     7378   6269   8012    205    134    -54       C  
ATOM    828  C   ALA A 963     -22.454 -33.312 -77.658  1.00 57.63           C  
ANISOU  828  C   ALA A 963     7388   6420   8091    266     18    -39       C  
ATOM    829  O   ALA A 963     -21.221 -33.416 -77.593  1.00 56.18           O  
ANISOU  829  O   ALA A 963     7254   6198   7895    318    -53    -50       O  
ATOM    830  CB  ALA A 963     -23.957 -34.306 -75.912  1.00 52.61           C  
ANISOU  830  CB  ALA A 963     6944   5659   7386     84    189    -92       C  
ATOM    831  N   LEU A 964     -23.133 -33.425 -78.796  1.00 54.36           N  
ANISOU  831  N   LEU A 964     6847   6110   7696    218      4    -34       N  
ATOM    832  CA  LEU A 964     -22.456 -33.654 -80.069  1.00 47.44           C  
ANISOU  832  CA  LEU A 964     5929   5334   6762    168    -50    -64       C  
ATOM    833  C   LEU A 964     -21.549 -32.477 -80.425  1.00 49.87           C  
ANISOU  833  C   LEU A 964     6207   5692   7049    191   -105    -23       C  
ATOM    834  O   LEU A 964     -20.396 -32.666 -80.824  1.00 48.26           O  
ANISOU  834  O   LEU A 964     6013   5512   6812    174    -92   -118       O  
ATOM    835  CB  LEU A 964     -23.477 -33.893 -81.181  1.00 39.63           C  
ANISOU  835  CB  LEU A 964     4853   4468   5737     25    -84    -35       C  
ATOM    836  CG  LEU A 964     -22.921 -34.315 -82.542  1.00 40.39           C  
ANISOU  836  CG  LEU A 964     4953   4695   5698   -148    -89   -112       C  
ATOM    837  CD1 LEU A 964     -22.154 -35.621 -82.422  1.00 57.60           C  
ANISOU  837  CD1 LEU A 964     7186   6791   7908   -135     30   -313       C  
ATOM    838  CD2 LEU A 964     -24.044 -34.442 -83.556  1.00 49.29           C  
ANISOU  838  CD2 LEU A 964     6027   5954   6745   -350   -174    -35       C  
ATOM    839  N   ILE A 965     -22.077 -31.265 -80.269  1.00 50.54           N  
ANISOU  839  N   ILE A 965     6234   5768   7199    221   -153     92       N  
ATOM    840  CA  ILE A 965     -21.312 -30.047 -80.512  1.00 54.86           C  
ANISOU  840  CA  ILE A 965     6777   6334   7734    231   -215    154       C  
ATOM    841  C   ILE A 965     -20.090 -30.005 -79.602  1.00 59.72           C  
ANISOU  841  C   ILE A 965     7475   6886   8330    323   -158     74       C  
ATOM    842  O   ILE A 965     -19.029 -29.530 -79.998  1.00 64.06           O  
ANISOU  842  O   ILE A 965     8028   7485   8826    297   -178     48       O  
ATOM    843  CB  ILE A 965     -22.170 -28.782 -80.295  1.00 61.01           C  
ANISOU  843  CB  ILE A 965     7461   7031   8690    278   -281    279       C  
ATOM    844  CG1 ILE A 965     -23.313 -28.733 -81.309  1.00 66.65           C  
ANISOU  844  CG1 ILE A 965     8055   7785   9485    178   -438    405       C  
ATOM    845  CG2 ILE A 965     -21.327 -27.522 -80.422  1.00 60.90           C  
ANISOU  845  CG2 ILE A 965     7473   6997   8668    285   -344    346       C  
ATOM    846  CD1 ILE A 965     -24.234 -27.547 -81.130  1.00 67.50           C  
ANISOU  846  CD1 ILE A 965     7992   7740   9915    253   -549    521       C  
ATOM    847  N   ASN A 966     -20.245 -30.517 -78.385  1.00 60.21           N  
ANISOU  847  N   ASN A 966     7613   6841   8423    386   -104     40       N  
ATOM    848  CA  ASN A 966     -19.133 -30.625 -77.449  1.00 58.37           C  
ANISOU  848  CA  ASN A 966     7477   6531   8169    433   -127      8       C  
ATOM    849  C   ASN A 966     -18.049 -31.561 -77.989  1.00 61.29           C  
ANISOU  849  C   ASN A 966     7808   6899   8579    448   -182    -86       C  
ATOM    850  O   ASN A 966     -16.868 -31.198 -78.029  1.00 62.12           O  
ANISOU  850  O   ASN A 966     7873   7008   8724    476   -221   -135       O  
ATOM    851  CB  ASN A 966     -19.635 -31.100 -76.080  1.00 53.92           C  
ANISOU  851  CB  ASN A 966     7060   5855   7571    397    -95     21       C  
ATOM    852  CG  ASN A 966     -18.591 -30.961 -74.986  1.00 58.25           C  
ANISOU  852  CG  ASN A 966     7747   6321   8066    381   -182     49       C  
ATOM    853  OD1 ASN A 966     -17.455 -31.412 -75.127  1.00 68.17           O  
ANISOU  853  OD1 ASN A 966     8979   7538   9384    435   -321     44       O  
ATOM    854  ND2 ASN A 966     -18.977 -30.329 -73.884  1.00 57.18           N  
ANISOU  854  ND2 ASN A 966     7739   6148   7837    278    -99     57       N  
ATOM    855  N   MET A 967     -18.455 -32.759 -78.409  1.00 55.69           N  
ANISOU  855  N   MET A 967     7084   6169   7905    420   -165   -146       N  
ATOM    856  CA  MET A 967     -17.511 -33.721 -78.980  1.00 48.85           C  
ANISOU  856  CA  MET A 967     6131   5256   7173    430   -172   -303       C  
ATOM    857  C   MET A 967     -16.756 -33.144 -80.179  1.00 53.57           C  
ANISOU  857  C   MET A 967     6605   6004   7746    345    -88   -435       C  
ATOM    858  O   MET A 967     -15.533 -33.264 -80.272  1.00 55.45           O  
ANISOU  858  O   MET A 967     6736   6197   8136    374    -81   -586       O  
ATOM    859  CB  MET A 967     -18.221 -35.013 -79.390  1.00 44.26           C  
ANISOU  859  CB  MET A 967     5555   4632   6630    379   -126   -372       C  
ATOM    860  CG  MET A 967     -18.735 -35.847 -78.229  1.00 44.64           C  
ANISOU  860  CG  MET A 967     5750   4501   6711    410   -215   -271       C  
ATOM    861  SD  MET A 967     -19.412 -37.432 -78.770  1.00 53.66           S  
ANISOU  861  SD  MET A 967     6897   5563   7927    340   -160   -374       S  
ATOM    862  CE  MET A 967     -17.956 -38.208 -79.462  1.00 42.90           C  
ANISOU  862  CE  MET A 967     5350   4058   6893    406   -161   -619       C  
ATOM    863  N   VAL A 968     -17.492 -32.519 -81.094  1.00 53.70           N  
ANISOU  863  N   VAL A 968     6632   6187   7583    204    -41   -378       N  
ATOM    864  CA  VAL A 968     -16.891 -31.903 -82.274  1.00 52.36           C  
ANISOU  864  CA  VAL A 968     6419   6181   7294     16     25   -468       C  
ATOM    865  C   VAL A 968     -15.945 -30.769 -81.889  1.00 51.62           C  
ANISOU  865  C   VAL A 968     6320   6090   7205     65     -7   -437       C  
ATOM    866  O   VAL A 968     -14.887 -30.594 -82.494  1.00 55.60           O  
ANISOU  866  O   VAL A 968     6754   6669   7703    -53     84   -613       O  
ATOM    867  CB  VAL A 968     -17.974 -31.394 -83.248  1.00 53.13           C  
ANISOU  867  CB  VAL A 968     6576   6428   7185   -187    -26   -319       C  
ATOM    868  CG1 VAL A 968     -17.352 -30.595 -84.387  1.00 47.05           C  
ANISOU  868  CG1 VAL A 968     5839   5823   6214   -464     -5   -350       C  
ATOM    869  CG2 VAL A 968     -18.782 -32.564 -83.785  1.00 51.13           C  
ANISOU  869  CG2 VAL A 968     6321   6206   6901   -292     21   -387       C  
ATOM    870  N   PHE A 969     -16.332 -30.011 -80.868  1.00 46.54           N  
ANISOU  870  N   PHE A 969     5743   5365   6576    206   -102   -253       N  
ATOM    871  CA  PHE A 969     -15.515 -28.921 -80.351  1.00 43.15           C  
ANISOU  871  CA  PHE A 969     5328   4921   6148    249   -132   -217       C  
ATOM    872  C   PHE A 969     -14.195 -29.468 -79.834  1.00 45.97           C  
ANISOU  872  C   PHE A 969     5601   5205   6661    330   -135   -376       C  
ATOM    873  O   PHE A 969     -13.150 -28.835 -79.973  1.00 39.09           O  
ANISOU  873  O   PHE A 969     4671   4380   5801    289   -114   -458       O  
ATOM    874  CB  PHE A 969     -16.254 -28.201 -79.222  1.00 43.33           C  
ANISOU  874  CB  PHE A 969     5435   4841   6186    359   -183    -52       C  
ATOM    875  CG  PHE A 969     -15.478 -27.072 -78.599  1.00 50.38           C  
ANISOU  875  CG  PHE A 969     6364   5708   7071    382   -198    -25       C  
ATOM    876  CD1 PHE A 969     -14.660 -27.293 -77.501  1.00 57.82           C  
ANISOU  876  CD1 PHE A 969     7340   6573   8058    449   -239    -64       C  
ATOM    877  CD2 PHE A 969     -15.582 -25.787 -79.099  1.00 46.98           C  
ANISOU  877  CD2 PHE A 969     5947   5310   6592    310   -209     61       C  
ATOM    878  CE1 PHE A 969     -13.952 -26.256 -76.923  1.00 53.63           C  
ANISOU  878  CE1 PHE A 969     6850   6032   7495    436   -253    -47       C  
ATOM    879  CE2 PHE A 969     -14.879 -24.747 -78.522  1.00 48.71           C  
ANISOU  879  CE2 PHE A 969     6208   5494   6805    317   -206     71       C  
ATOM    880  CZ  PHE A 969     -14.062 -24.983 -77.435  1.00 50.05           C  
ANISOU  880  CZ  PHE A 969     6406   5620   6991    376   -209      2       C  
ATOM    881  N   GLN A 970     -14.251 -30.650 -79.233  1.00 46.55           N  
ANISOU  881  N   GLN A 970     5658   5141   6887    436   -189   -410       N  
ATOM    882  CA  GLN A 970     -13.053 -31.260 -78.677  1.00 44.71           C  
ANISOU  882  CA  GLN A 970     5314   4768   6906    532   -285   -520       C  
ATOM    883  C   GLN A 970     -12.166 -31.885 -79.752  1.00 41.91           C  
ANISOU  883  C   GLN A 970     4732   4436   6757    472   -155   -822       C  
ATOM    884  O   GLN A 970     -11.077 -31.385 -80.027  1.00 47.69           O  
ANISOU  884  O   GLN A 970     5322   5217   7580    431   -102   -977       O  
ATOM    885  CB  GLN A 970     -13.420 -32.299 -77.616  1.00 47.63           C  
ANISOU  885  CB  GLN A 970     5775   4932   7390    629   -453   -407       C  
ATOM    886  CG  GLN A 970     -12.224 -32.907 -76.905  1.00 48.95           C  
ANISOU  886  CG  GLN A 970     5835   4890   7872    727   -674   -437       C  
ATOM    887  CD  GLN A 970     -12.630 -33.895 -75.833  1.00 60.34           C  
ANISOU  887  CD  GLN A 970     7440   6109   9379    754   -908   -256       C  
ATOM    888  OE1 GLN A 970     -13.818 -34.090 -75.571  1.00 63.86           O  
ANISOU  888  OE1 GLN A 970     8083   6582   9600    684   -849   -141       O  
ATOM    889  NE2 GLN A 970     -11.645 -34.527 -75.204  1.00 68.77           N  
ANISOU  889  NE2 GLN A 970     8420   6938  10773    827  -1198   -223       N  
ATOM    890  N   MET A 971     -12.635 -32.967 -80.368  1.00 42.68           N  
ANISOU  890  N   MET A 971     4785   4499   6933    436    -66   -947       N  
ATOM    891  CA  MET A 971     -11.774 -33.758 -81.248  1.00 69.02           C  
ANISOU  891  CA  MET A 971     7877   7799  10549    368    101  -1311       C  
ATOM    892  C   MET A 971     -11.971 -33.518 -82.750  1.00 73.57           C  
ANISOU  892  C   MET A 971     8453   8625  10874     60    385  -1518       C  
ATOM    893  O   MET A 971     -11.465 -34.281 -83.574  1.00 79.25           O  
ANISOU  893  O   MET A 971     8996   9333  11782    -73    603  -1879       O  
ATOM    894  CB  MET A 971     -11.902 -35.250 -80.921  1.00 46.53           C  
ANISOU  894  CB  MET A 971     4948   4684   8045    501     22  -1385       C  
ATOM    895  CG  MET A 971     -13.247 -35.857 -81.264  1.00 45.63           C  
ANISOU  895  CG  MET A 971     5005   4619   7714    419     85  -1298       C  
ATOM    896  SD  MET A 971     -13.770 -37.065 -80.035  1.00 77.13           S  
ANISOU  896  SD  MET A 971     9103   8284  11918    608   -180  -1096       S  
ATOM    897  CE  MET A 971     -14.034 -35.991 -78.629  1.00 74.27           C  
ANISOU  897  CE  MET A 971     8974   7949  11297    677   -417   -714       C  
ATOM    898  N   GLY A 972     -12.697 -32.462 -83.103  1.00 71.57           N  
ANISOU  898  N   GLY A 972     8399   8576  10216    -89    371  -1296       N  
ATOM    899  CA  GLY A 972     -12.835 -32.066 -84.497  1.00 73.92           C  
ANISOU  899  CA  GLY A 972     8761   9117  10208   -460    555  -1412       C  
ATOM    900  C   GLY A 972     -13.912 -32.794 -85.285  1.00 75.54           C  
ANISOU  900  C   GLY A 972     9062   9402  10239   -646    613  -1411       C  
ATOM    901  O   GLY A 972     -14.372 -33.863 -84.891  1.00 79.51           O  
ANISOU  901  O   GLY A 972     9524   9756  10928   -488    592  -1436       O  
ATOM    902  N   GLU A 973     -14.300 -32.204 -86.413  1.00 75.22           N  
ANISOU  902  N   GLU A 973     9168   9590   9820  -1024    658  -1365       N  
ATOM    903  CA  GLU A 973     -15.375 -32.720 -87.260  1.00 80.93           C  
ANISOU  903  CA  GLU A 973    10012  10429  10307  -1279    660  -1313       C  
ATOM    904  C   GLU A 973     -15.077 -34.118 -87.786  1.00 82.81           C  
ANISOU  904  C   GLU A 973    10132  10639  10694  -1408    939  -1726       C  
ATOM    905  O   GLU A 973     -15.902 -35.027 -87.666  1.00 87.74           O  
ANISOU  905  O   GLU A 973    10768  11187  11383  -1330    910  -1695       O  
ATOM    906  CB  GLU A 973     -15.609 -31.770 -88.436  1.00 93.19           C  
ANISOU  906  CB  GLU A 973    11765  12227  11414  -1750    609  -1181       C  
ATOM    907  CG  GLU A 973     -16.459 -32.343 -89.560  1.00106.99           C  
ANISOU  907  CG  GLU A 973    13650  14141  12861  -2164    629  -1192       C  
ATOM    908  CD  GLU A 973     -16.470 -31.453 -90.793  1.00112.85           C  
ANISOU  908  CD  GLU A 973    14631  15125  13121  -2743    555  -1073       C  
ATOM    909  OE1 GLU A 973     -15.919 -30.334 -90.724  1.00111.81           O  
ANISOU  909  OE1 GLU A 973    14562  15010  12910  -2780    467   -944       O  
ATOM    910  OE2 GLU A 973     -17.026 -31.872 -91.830  1.00116.11           O  
ANISOU  910  OE2 GLU A 973    15196  15709  13211  -3203    568  -1096       O  
ATOM    911  N   THR A 974     -13.896 -34.277 -88.377  1.00 79.37           N  
ANISOU  911  N   THR A 974     9567  10251  10340  -1626   1234  -2146       N  
ATOM    912  CA  THR A 974     -13.470 -35.559 -88.925  1.00 83.97           C  
ANISOU  912  CA  THR A 974     9980  10768  11156  -1772   1564  -2638       C  
ATOM    913  C   THR A 974     -13.410 -36.634 -87.841  1.00 86.58           C  
ANISOU  913  C   THR A 974    10110  10749  12036  -1285   1478  -2678       C  
ATOM    914  O   THR A 974     -13.929 -37.741 -88.019  1.00 91.93           O  
ANISOU  914  O   THR A 974    10772  11328  12830  -1301   1561  -2807       O  
ATOM    915  CB  THR A 974     -12.094 -35.448 -89.606  1.00 89.85           C  
ANISOU  915  CB  THR A 974    10545  11587  12007  -2064   1934  -3149       C  
ATOM    916  OG1 THR A 974     -12.093 -34.344 -90.523  1.00 87.86           O  
ANISOU  916  OG1 THR A 974    10538  11653  11192  -2561   1972  -3059       O  
ATOM    917  CG2 THR A 974     -11.760 -36.738 -90.351  1.00 98.97           C  
ANISOU  917  CG2 THR A 974    11518  12681  13406  -2304   2346  -3731       C  
ATOM    918  N   GLY A 975     -12.789 -36.300 -86.714  1.00 85.39           N  
ANISOU  918  N   GLY A 975     9837  10407  12202   -892   1284  -2543       N  
ATOM    919  CA  GLY A 975     -12.689 -37.230 -85.604  1.00 84.33           C  
ANISOU  919  CA  GLY A 975     9565   9922  12555   -480   1109  -2500       C  
ATOM    920  C   GLY A 975     -14.020 -37.766 -85.105  1.00 74.63           C  
ANISOU  920  C   GLY A 975     8536   8627  11195   -357    915  -2180       C  
ATOM    921  O   GLY A 975     -14.174 -38.970 -84.912  1.00 73.83           O  
ANISOU  921  O   GLY A 975     8363   8294  11392   -256    926  -2300       O  
ATOM    922  N   VAL A 976     -14.977 -36.870 -84.886  1.00 62.95           N  
ANISOU  922  N   VAL A 976     7283   7322   9314   -374    742  -1791       N  
ATOM    923  CA  VAL A 976     -16.310 -37.263 -84.447  1.00 58.43           C  
ANISOU  923  CA  VAL A 976     6873   6718   8612   -299    595  -1520       C  
ATOM    924  C   VAL A 976     -17.027 -38.049 -85.541  1.00 67.29           C  
ANISOU  924  C   VAL A 976     8037   7957   9573   -590    771  -1686       C  
ATOM    925  O   VAL A 976     -17.748 -39.008 -85.258  1.00 68.44           O  
ANISOU  925  O   VAL A 976     8223   7977   9803   -525    742  -1658       O  
ATOM    926  CB  VAL A 976     -17.146 -36.036 -84.033  1.00 49.97           C  
ANISOU  926  CB  VAL A 976     5958   5785   7243   -262    405  -1135       C  
ATOM    927  CG1 VAL A 976     -18.587 -36.432 -83.749  1.00 49.58           C  
ANISOU  927  CG1 VAL A 976     6021   5730   7086   -244    312   -930       C  
ATOM    928  CG2 VAL A 976     -16.535 -35.377 -82.821  1.00 48.49           C  
ANISOU  928  CG2 VAL A 976     5760   5466   7198     -1    251   -986       C  
ATOM    929  N   ALA A 977     -16.816 -37.647 -86.792  1.00 74.24           N  
ANISOU  929  N   ALA A 977     8937   9084  10188   -964    954  -1862       N  
ATOM    930  CA  ALA A 977     -17.408 -38.349 -87.925  1.00 74.58           C  
ANISOU  930  CA  ALA A 977     9048   9274  10015  -1341   1135  -2047       C  
ATOM    931  C   ALA A 977     -16.860 -39.769 -88.000  1.00 74.24           C  
ANISOU  931  C   ALA A 977     8835   9000  10373  -1306   1385  -2477       C  
ATOM    932  O   ALA A 977     -17.484 -40.659 -88.587  1.00 75.91           O  
ANISOU  932  O   ALA A 977     9098   9236  10510  -1518   1519  -2624       O  
ATOM    933  CB  ALA A 977     -17.130 -37.600 -89.221  1.00 77.81           C  
ANISOU  933  CB  ALA A 977     9554   9992  10018  -1841   1277  -2162       C  
ATOM    934  N   GLY A 978     -15.693 -39.973 -87.393  1.00 73.09           N  
ANISOU  934  N   GLY A 978     8468   8603  10698  -1037   1423  -2676       N  
ATOM    935  CA  GLY A 978     -15.088 -41.290 -87.318  1.00 73.89           C  
ANISOU  935  CA  GLY A 978     8345   8382  11348   -926   1592  -3066       C  
ATOM    936  C   GLY A 978     -15.948 -42.261 -86.532  1.00 65.60           C  
ANISOU  936  C   GLY A 978     7383   7084  10459   -690   1389  -2850       C  
ATOM    937  O   GLY A 978     -15.926 -43.466 -86.785  1.00 60.58           O  
ANISOU  937  O   GLY A 978     6650   6229  10138   -722   1546  -3142       O  
ATOM    938  N   PHE A 979     -16.716 -41.735 -85.582  1.00 64.45           N  
ANISOU  938  N   PHE A 979     7423   6962  10102   -486   1067  -2366       N  
ATOM    939  CA  PHE A 979     -17.597 -42.571 -84.767  1.00 69.79           C  
ANISOU  939  CA  PHE A 979     8227   7434  10855   -324    882  -2143       C  
ATOM    940  C   PHE A 979     -18.814 -43.068 -85.548  1.00 74.54           C  
ANISOU  940  C   PHE A 979     8968   8220  11132   -606   1014  -2164       C  
ATOM    941  O   PHE A 979     -19.898 -42.497 -85.444  1.00 71.31           O  
ANISOU  941  O   PHE A 979     8720   8023  10351   -668    887  -1857       O  
ATOM    942  CB  PHE A 979     -18.077 -41.816 -83.522  1.00 66.95           C  
ANISOU  942  CB  PHE A 979     8027   7074  10338   -106    570  -1687       C  
ATOM    943  CG  PHE A 979     -16.986 -41.477 -82.545  1.00 65.38           C  
ANISOU  943  CG  PHE A 979     7738   6660  10443    156    374  -1609       C  
ATOM    944  CD1 PHE A 979     -16.634 -42.357 -81.532  1.00 64.46           C  
ANISOU  944  CD1 PHE A 979     7619   6160  10713    359    145  -1529       C  
ATOM    945  CD2 PHE A 979     -16.330 -40.264 -82.626  1.00 67.13           C  
ANISOU  945  CD2 PHE A 979     7898   7056  10553    165    375  -1583       C  
ATOM    946  CE1 PHE A 979     -15.633 -42.031 -80.629  1.00 64.69           C  
ANISOU  946  CE1 PHE A 979     7573   5994  11011    559   -102  -1417       C  
ATOM    947  CE2 PHE A 979     -15.333 -39.932 -81.730  1.00 63.64           C  
ANISOU  947  CE2 PHE A 979     7371   6435  10375    378    181  -1508       C  
ATOM    948  CZ  PHE A 979     -14.983 -40.816 -80.730  1.00 62.66           C  
ANISOU  948  CZ  PHE A 979     7234   5940  10634    571    -71  -1419       C  
ATOM    949  N   THR A 980     -18.642 -44.144 -86.308  1.00 76.85           N  
ANISOU  949  N   THR A 980     9175   8410  11614   -782   1266  -2546       N  
ATOM    950  CA  THR A 980     -19.725 -44.669 -87.137  1.00 77.69           C  
ANISOU  950  CA  THR A 980     9414   8703  11400  -1107   1407  -2605       C  
ATOM    951  C   THR A 980     -20.829 -45.329 -86.310  1.00 84.79           C  
ANISOU  951  C   THR A 980    10463   9462  12290   -968   1212  -2326       C  
ATOM    952  O   THR A 980     -21.996 -44.936 -86.389  1.00 85.95           O  
ANISOU  952  O   THR A 980    10751   9853  12053  -1093   1114  -2067       O  
ATOM    953  CB  THR A 980     -19.201 -45.675 -88.179  1.00 81.17           C  
ANISOU  953  CB  THR A 980     9728   9063  12052  -1383   1790  -3157       C  
ATOM    954  OG1 THR A 980     -18.214 -45.041 -89.001  1.00 83.62           O  
ANISOU  954  OG1 THR A 980     9910   9542  12318  -1604   2033  -3469       O  
ATOM    955  CG2 THR A 980     -20.337 -46.175 -89.057  1.00 84.66           C  
ANISOU  955  CG2 THR A 980    10339   9732  12097  -1780   1923  -3206       C  
ATOM    956  N   ASN A 981     -20.452 -46.331 -85.523  1.00 90.36           N  
ANISOU  956  N   ASN A 981    11127   9755  13451   -733   1139  -2381       N  
ATOM    957  CA  ASN A 981     -21.399 -47.072 -84.695  1.00 88.99           C  
ANISOU  957  CA  ASN A 981    11128   9409  13273   -655    969  -2142       C  
ATOM    958  C   ASN A 981     -22.133 -46.202 -83.683  1.00 81.80           C  
ANISOU  958  C   ASN A 981    10376   8631  12073   -535    715  -1700       C  
ATOM    959  O   ASN A 981     -23.349 -46.308 -83.531  1.00 80.97           O  
ANISOU  959  O   ASN A 981    10409   8657  11701   -650    689  -1535       O  
ATOM    960  CB  ASN A 981     -20.692 -48.222 -83.977  1.00 91.86           C  
ANISOU  960  CB  ASN A 981    11437   9248  14217   -438    859  -2234       C  
ATOM    961  CG  ASN A 981     -20.485 -49.424 -84.872  1.00 97.76           C  
ANISOU  961  CG  ASN A 981    12064   9800  15279   -594   1138  -2679       C  
ATOM    962  OD1 ASN A 981     -20.886 -50.538 -84.537  1.00104.62           O  
ANISOU  962  OD1 ASN A 981    13025  10368  16359   -585   1083  -2676       O  
ATOM    963  ND2 ASN A 981     -19.871 -49.201 -86.027  1.00 97.11           N  
ANISOU  963  ND2 ASN A 981    11793   9888  15218   -786   1465  -3087       N  
ATOM    964  N   SER A 982     -21.389 -45.345 -82.993  1.00 78.29           N  
ANISOU  964  N   SER A 982     9892   8147  11706   -327    555  -1549       N  
ATOM    965  CA  SER A 982     -21.967 -44.474 -81.977  1.00 75.37           C  
ANISOU  965  CA  SER A 982     9661   7878  11100   -236    363  -1194       C  
ATOM    966  C   SER A 982     -23.014 -43.533 -82.573  1.00 70.19           C  
ANISOU  966  C   SER A 982     9011   7609  10051   -399    434  -1092       C  
ATOM    967  O   SER A 982     -24.110 -43.389 -82.030  1.00 70.62           O  
ANISOU  967  O   SER A 982     9162   7735   9937   -435    380   -907       O  
ATOM    968  CB  SER A 982     -20.868 -43.678 -81.271  1.00 73.92           C  
ANISOU  968  CB  SER A 982     9422   7601  11064    -27    206  -1096       C  
ATOM    969  OG  SER A 982     -19.896 -44.546 -80.710  1.00 70.66           O  
ANISOU  969  OG  SER A 982     8967   6791  11089    126     58  -1154       O  
ATOM    970  N   LEU A 983     -22.675 -42.906 -83.695  1.00 65.14           N  
ANISOU  970  N   LEU A 983     8259   7197   9292   -527    543  -1221       N  
ATOM    971  CA  LEU A 983     -23.601 -42.007 -84.376  1.00 65.93           C  
ANISOU  971  CA  LEU A 983     8357   7622   9070   -708    523  -1085       C  
ATOM    972  C   LEU A 983     -24.790 -42.760 -84.961  1.00 70.25           C  
ANISOU  972  C   LEU A 983     8947   8276   9469   -943    579  -1115       C  
ATOM    973  O   LEU A 983     -25.897 -42.222 -85.039  1.00 71.02           O  
ANISOU  973  O   LEU A 983     9035   8548   9403  -1024    475   -924       O  
ATOM    974  CB  LEU A 983     -22.884 -41.217 -85.471  1.00 64.57           C  
ANISOU  974  CB  LEU A 983     8116   7654   8762   -875    589  -1193       C  
ATOM    975  CG  LEU A 983     -21.922 -40.128 -84.996  1.00 62.90           C  
ANISOU  975  CG  LEU A 983     7857   7420   8622   -686    511  -1111       C  
ATOM    976  CD1 LEU A 983     -21.205 -39.500 -86.179  1.00 62.12           C  
ANISOU  976  CD1 LEU A 983     7721   7525   8358   -937    616  -1260       C  
ATOM    977  CD2 LEU A 983     -22.660 -39.074 -84.188  1.00 65.85           C  
ANISOU  977  CD2 LEU A 983     8262   7839   8921   -538    320   -786       C  
ATOM    978  N   ARG A 984     -24.560 -44.003 -85.375  1.00 68.42           N  
ANISOU  978  N   ARG A 984     8735   7918   9344  -1054    739  -1372       N  
ATOM    979  CA  ARG A 984     -25.640 -44.835 -85.894  1.00 71.99           C  
ANISOU  979  CA  ARG A 984     9242   8453   9657  -1297    808  -1425       C  
ATOM    980  C   ARG A 984     -26.628 -45.157 -84.778  1.00 69.87           C  
ANISOU  980  C   ARG A 984     9051   8072   9424  -1173    702  -1225       C  
ATOM    981  O   ARG A 984     -27.839 -45.185 -84.995  1.00 73.03           O  
ANISOU  981  O   ARG A 984     9449   8639   9659  -1335    674  -1135       O  
ATOM    982  CB  ARG A 984     -25.095 -46.129 -86.504  1.00 81.11           C  
ANISOU  982  CB  ARG A 984    10401   9443  10975  -1440   1039  -1791       C  
ATOM    983  CG  ARG A 984     -26.138 -46.929 -87.274  1.00 87.52           C  
ANISOU  983  CG  ARG A 984    11278  10391  11583  -1774   1145  -1890       C  
ATOM    984  CD  ARG A 984     -25.637 -48.316 -87.649  1.00 96.26           C  
ANISOU  984  CD  ARG A 984    12390  11248  12936  -1878   1396  -2276       C  
ATOM    985  NE  ARG A 984     -25.552 -49.202 -86.491  1.00104.59           N  
ANISOU  985  NE  ARG A 984    13498  11896  14347  -1599   1316  -2224       N  
ATOM    986  CZ  ARG A 984     -24.427 -49.475 -85.838  1.00111.42           C  
ANISOU  986  CZ  ARG A 984    14296  12396  15644  -1317   1271  -2298       C  
ATOM    987  NH1 ARG A 984     -23.282 -48.934 -86.233  1.00115.74           N  
ANISOU  987  NH1 ARG A 984    14682  12950  16346  -1253   1353  -2479       N  
ATOM    988  NH2 ARG A 984     -24.444 -50.293 -84.794  1.00111.91           N  
ANISOU  988  NH2 ARG A 984    14455  12077  15990  -1129   1118  -2181       N  
ATOM    989  N   MET A 985     -26.100 -45.394 -83.582  1.00 65.40           N  
ANISOU  989  N   MET A 985     8555   7224   9072   -929    633  -1158       N  
ATOM    990  CA  MET A 985     -26.929 -45.681 -82.418  1.00 58.39           C  
ANISOU  990  CA  MET A 985     7793   6224   8167   -887    558   -985       C  
ATOM    991  C   MET A 985     -27.694 -44.440 -81.972  1.00 56.90           C  
ANISOU  991  C   MET A 985     7544   6243   7834   -853    487   -786       C  
ATOM    992  O   MET A 985     -28.872 -44.521 -81.624  1.00 61.10           O  
ANISOU  992  O   MET A 985     8082   6848   8283   -959    512   -727       O  
ATOM    993  CB  MET A 985     -26.074 -46.222 -81.270  1.00 53.29           C  
ANISOU  993  CB  MET A 985     7286   5215   7749   -710    446   -931       C  
ATOM    994  CG  MET A 985     -25.466 -47.587 -81.547  1.00 53.89           C  
ANISOU  994  CG  MET A 985     7394   4981   8103   -721    480  -1123       C  
ATOM    995  SD  MET A 985     -24.220 -48.063 -80.334  1.00 77.23           S  
ANISOU  995  SD  MET A 985    10448   7456  11441   -490    218  -1009       S  
ATOM    996  CE  MET A 985     -23.636 -49.601 -81.040  1.00 56.48           C  
ANISOU  996  CE  MET A 985     7738   4455   9265   -502    299  -1319       C  
ATOM    997  N   LEU A 986     -27.019 -43.293 -81.986  1.00 53.53           N  
ANISOU  997  N   LEU A 986     7032   5889   7418   -715    418   -714       N  
ATOM    998  CA  LEU A 986     -27.656 -42.028 -81.635  1.00 54.17           C  
ANISOU  998  CA  LEU A 986     7017   6120   7445   -666    357   -557       C  
ATOM    999  C   LEU A 986     -28.745 -41.670 -82.640  1.00 59.21           C  
ANISOU  999  C   LEU A 986     7497   7001   8001   -836    325   -526       C  
ATOM   1000  O   LEU A 986     -29.727 -41.011 -82.297  1.00 62.67           O  
ANISOU 1000  O   LEU A 986     7811   7507   8494   -831    285   -432       O  
ATOM   1001  CB  LEU A 986     -26.622 -40.901 -81.563  1.00 53.50           C  
ANISOU 1001  CB  LEU A 986     6884   6045   7398   -502    283   -495       C  
ATOM   1002  CG  LEU A 986     -25.600 -40.946 -80.426  1.00 52.68           C  
ANISOU 1002  CG  LEU A 986     6905   5719   7392   -333    242   -468       C  
ATOM   1003  CD1 LEU A 986     -24.549 -39.860 -80.605  1.00 48.59           C  
ANISOU 1003  CD1 LEU A 986     6310   5247   6904   -206    183   -440       C  
ATOM   1004  CD2 LEU A 986     -26.285 -40.807 -79.076  1.00 53.22           C  
ANISOU 1004  CD2 LEU A 986     7089   5710   7423   -343    250   -367       C  
ATOM   1005  N   GLN A 987     -28.565 -42.107 -83.882  1.00 63.72           N  
ANISOU 1005  N   GLN A 987     8059   7686   8466  -1017    338   -620       N  
ATOM   1006  CA  GLN A 987     -29.527 -41.824 -84.941  1.00 74.88           C  
ANISOU 1006  CA  GLN A 987     9357   9333   9760  -1251    236   -552       C  
ATOM   1007  C   GLN A 987     -30.817 -42.618 -84.748  1.00 73.87           C  
ANISOU 1007  C   GLN A 987     9199   9222   9646  -1376    274   -575       C  
ATOM   1008  O   GLN A 987     -31.910 -42.126 -85.034  1.00 73.60           O  
ANISOU 1008  O   GLN A 987     8992   9323   9650  -1467    138   -458       O  
ATOM   1009  CB  GLN A 987     -28.918 -42.132 -86.310  1.00 84.09           C  
ANISOU 1009  CB  GLN A 987    10582  10636  10731  -1514    270   -677       C  
ATOM   1010  CG  GLN A 987     -29.796 -41.742 -87.484  1.00 92.20           C  
ANISOU 1010  CG  GLN A 987    11544  11921  11569  -1837     86   -550       C  
ATOM   1011  CD  GLN A 987     -29.134 -42.029 -88.815  1.00106.35           C  
ANISOU 1011  CD  GLN A 987    13455  13871  13082  -2204    162   -705       C  
ATOM   1012  OE1 GLN A 987     -27.971 -42.427 -88.868  1.00106.82           O  
ANISOU 1012  OE1 GLN A 987    13593  13839  13156  -2178    387   -949       O  
ATOM   1013  NE2 GLN A 987     -29.874 -41.831 -89.899  1.00118.15           N  
ANISOU 1013  NE2 GLN A 987    14955  15599  14337  -2587    -27   -582       N  
ATOM   1014  N   GLN A 988     -30.681 -43.847 -84.259  1.00 68.42           N  
ANISOU 1014  N   GLN A 988     8661   8369   8965  -1386    438   -722       N  
ATOM   1015  CA  GLN A 988     -31.833 -44.702 -83.996  1.00 62.09           C  
ANISOU 1015  CA  GLN A 988     7870   7566   8154  -1533    508   -767       C  
ATOM   1016  C   GLN A 988     -32.317 -44.525 -82.561  1.00 54.76           C  
ANISOU 1016  C   GLN A 988     6960   6510   7337  -1406    561   -715       C  
ATOM   1017  O   GLN A 988     -33.137 -45.301 -82.069  1.00 50.65           O  
ANISOU 1017  O   GLN A 988     6498   5945   6802  -1538    665   -777       O  
ATOM   1018  CB  GLN A 988     -31.485 -46.168 -84.261  1.00 68.96           C  
ANISOU 1018  CB  GLN A 988     8923   8300   8979  -1665    655   -957       C  
ATOM   1019  CG  GLN A 988     -31.064 -46.459 -85.693  1.00 77.39           C  
ANISOU 1019  CG  GLN A 988     9986   9503   9916  -1885    693  -1100       C  
ATOM   1020  CD  GLN A 988     -30.656 -47.905 -85.895  1.00 87.89           C  
ANISOU 1020  CD  GLN A 988    11462  10636  11295  -1996    885  -1352       C  
ATOM   1021  OE1 GLN A 988     -30.902 -48.757 -85.042  1.00 91.68           O  
ANISOU 1021  OE1 GLN A 988    12058  10889  11886  -1938    935  -1368       O  
ATOM   1022  NE2 GLN A 988     -30.023 -48.187 -87.028  1.00 91.10           N  
ANISOU 1022  NE2 GLN A 988    11874  11111  11629  -2193   1003  -1568       N  
ATOM   1023  N   LYS A 989     -31.790 -43.498 -81.900  1.00 53.52           N  
ANISOU 1023  N   LYS A 989     6771   6302   7262  -1201    514   -624       N  
ATOM   1024  CA  LYS A 989     -32.194 -43.135 -80.543  1.00 57.32           C  
ANISOU 1024  CA  LYS A 989     7277   6690   7813  -1143    598   -608       C  
ATOM   1025  C   LYS A 989     -31.957 -44.242 -79.517  1.00 55.36           C  
ANISOU 1025  C   LYS A 989     7333   6226   7475  -1222    698   -652       C  
ATOM   1026  O   LYS A 989     -32.772 -44.460 -78.622  1.00 55.60           O  
ANISOU 1026  O   LYS A 989     7426   6228   7470  -1370    825   -695       O  
ATOM   1027  CB  LYS A 989     -33.650 -42.658 -80.519  1.00 57.86           C  
ANISOU 1027  CB  LYS A 989     7077   6894   8012  -1243    638   -637       C  
ATOM   1028  CG  LYS A 989     -33.887 -41.418 -81.364  1.00 57.92           C  
ANISOU 1028  CG  LYS A 989     6779   7039   8188  -1152    447   -529       C  
ATOM   1029  CD  LYS A 989     -35.310 -40.914 -81.241  1.00 70.89           C  
ANISOU 1029  CD  LYS A 989     8083   8745  10108  -1210    452   -571       C  
ATOM   1030  CE  LYS A 989     -35.492 -39.626 -82.023  1.00 79.54           C  
ANISOU 1030  CE  LYS A 989     8873   9899  11450  -1104    176   -410       C  
ATOM   1031  NZ  LYS A 989     -34.529 -38.582 -81.581  1.00 50.98           N  
ANISOU 1031  NZ  LYS A 989     5308   6182   7880   -887    158   -343       N  
ATOM   1032  N   ARG A 990     -30.831 -44.932 -79.654  1.00 58.06           N  
ANISOU 1032  N   ARG A 990     7856   6396   7808  -1152    630   -647       N  
ATOM   1033  CA  ARG A 990     -30.419 -45.934 -78.682  1.00 65.94           C  
ANISOU 1033  CA  ARG A 990     9154   7115   8783  -1208    615   -621       C  
ATOM   1034  C   ARG A 990     -29.337 -45.344 -77.784  1.00 68.58           C  
ANISOU 1034  C   ARG A 990     9607   7300   9151  -1050    491   -500       C  
ATOM   1035  O   ARG A 990     -28.147 -45.600 -77.972  1.00 65.77           O  
ANISOU 1035  O   ARG A 990     9288   6772   8930   -898    358   -481       O  
ATOM   1036  CB  ARG A 990     -29.919 -47.192 -79.393  1.00 67.87           C  
ANISOU 1036  CB  ARG A 990     9481   7193   9114  -1234    590   -711       C  
ATOM   1037  CG  ARG A 990     -30.950 -47.797 -80.334  1.00 71.89           C  
ANISOU 1037  CG  ARG A 990     9895   7867   9552  -1435    714   -840       C  
ATOM   1038  CD  ARG A 990     -30.467 -49.095 -80.955  1.00 77.66           C  
ANISOU 1038  CD  ARG A 990    10724   8396  10388  -1496    741   -981       C  
ATOM   1039  NE  ARG A 990     -29.331 -48.890 -81.845  1.00 89.27           N  
ANISOU 1039  NE  ARG A 990    12069   9850  11998  -1360    730  -1095       N  
ATOM   1040  CZ  ARG A 990     -28.751 -49.859 -82.545  1.00107.71           C  
ANISOU 1040  CZ  ARG A 990    14412  12012  14500  -1404    809  -1304       C  
ATOM   1041  NH1 ARG A 990     -29.203 -51.103 -82.458  1.00110.93           N  
ANISOU 1041  NH1 ARG A 990    14962  12227  14960  -1555    869  -1385       N  
ATOM   1042  NH2 ARG A 990     -27.720 -49.585 -83.332  1.00116.64           N  
ANISOU 1042  NH2 ARG A 990    15403  13152  15764  -1324    858  -1466       N  
ATOM   1043  N   TRP A 991     -29.766 -44.552 -76.806  1.00 70.72           N  
ANISOU 1043  N   TRP A 991     9915   7632   9324  -1111    551   -451       N  
ATOM   1044  CA  TRP A 991     -28.853 -43.748 -75.998  1.00 72.22           C  
ANISOU 1044  CA  TRP A 991    10192   7743   9505  -1000    452   -345       C  
ATOM   1045  C   TRP A 991     -27.926 -44.571 -75.110  1.00 70.95           C  
ANISOU 1045  C   TRP A 991    10359   7277   9322  -1049    246   -206       C  
ATOM   1046  O   TRP A 991     -26.756 -44.232 -74.952  1.00 74.93           O  
ANISOU 1046  O   TRP A 991    10875   7667   9927   -878     65   -116       O  
ATOM   1047  CB  TRP A 991     -29.633 -42.750 -75.138  1.00 77.30           C  
ANISOU 1047  CB  TRP A 991    10803   8517  10052  -1122    624   -386       C  
ATOM   1048  CG  TRP A 991     -30.767 -42.077 -75.854  1.00 78.95           C  
ANISOU 1048  CG  TRP A 991    10665   8952  10382  -1106    783   -514       C  
ATOM   1049  CD1 TRP A 991     -32.080 -42.080 -75.486  1.00 83.61           C  
ANISOU 1049  CD1 TRP A 991    11161   9630  10977  -1314   1000   -655       C  
ATOM   1050  CD2 TRP A 991     -30.690 -41.309 -77.061  1.00 72.98           C  
ANISOU 1050  CD2 TRP A 991     9599   8341   9790   -901    702   -502       C  
ATOM   1051  NE1 TRP A 991     -32.825 -41.357 -76.385  1.00 82.88           N  
ANISOU 1051  NE1 TRP A 991    10677   9700  11112  -1207   1017   -718       N  
ATOM   1052  CE2 TRP A 991     -31.994 -40.874 -77.363  1.00 73.34           C  
ANISOU 1052  CE2 TRP A 991     9363   8530   9974   -972    810   -596       C  
ATOM   1053  CE3 TRP A 991     -29.645 -40.944 -77.916  1.00 71.39           C  
ANISOU 1053  CE3 TRP A 991     9333   8156   9636   -704    540   -426       C  
ATOM   1054  CZ2 TRP A 991     -32.283 -40.095 -78.479  1.00 72.21           C  
ANISOU 1054  CZ2 TRP A 991     8907   8520  10008   -854    686   -552       C  
ATOM   1055  CZ3 TRP A 991     -29.933 -40.174 -79.025  1.00 68.45           C  
ANISOU 1055  CZ3 TRP A 991     8694   7950   9364   -634    472   -407       C  
ATOM   1056  CH2 TRP A 991     -31.241 -39.757 -79.297  1.00 70.38           C  
ANISOU 1056  CH2 TRP A 991     8690   8312   9740   -709    508   -438       C  
ATOM   1057  N   ASP A 992     -28.449 -45.642 -74.525  1.00 68.38           N  
ANISOU 1057  N   ASP A 992    10297   6802   8883  -1301    242   -171       N  
ATOM   1058  CA  ASP A 992     -27.665 -46.452 -73.600  1.00 76.17           C  
ANISOU 1058  CA  ASP A 992    11633   7449   9858  -1403    -36     25       C  
ATOM   1059  C   ASP A 992     -26.601 -47.282 -74.317  1.00 84.15           C  
ANISOU 1059  C   ASP A 992    12566   8187  11221  -1162   -266     42       C  
ATOM   1060  O   ASP A 992     -25.491 -47.453 -73.807  1.00 91.54           O  
ANISOU 1060  O   ASP A 992    13609   8848  12324  -1070   -571    202       O  
ATOM   1061  CB  ASP A 992     -28.578 -47.343 -72.757  1.00 84.96           C  
ANISOU 1061  CB  ASP A 992    13093   8468  10722  -1808     13     73       C  
ATOM   1062  CG  ASP A 992     -29.505 -46.542 -71.861  1.00 87.51           C  
ANISOU 1062  CG  ASP A 992    13504   9021  10725  -2111    277     -2       C  
ATOM   1063  OD1 ASP A 992     -29.109 -46.235 -70.717  1.00 93.87           O  
ANISOU 1063  OD1 ASP A 992    14602   9745  11318  -2323    171    134       O  
ATOM   1064  OD2 ASP A 992     -30.629 -46.218 -72.301  1.00 80.08           O  
ANISOU 1064  OD2 ASP A 992    12324   8331   9771  -2162    592   -218       O  
ATOM   1065  N   GLU A 993     -26.939 -47.791 -75.498  1.00 81.46           N  
ANISOU 1065  N   GLU A 993    12018   7912  11021  -1086   -115   -145       N  
ATOM   1066  CA  GLU A 993     -25.982 -48.544 -76.302  1.00 77.40           C  
ANISOU 1066  CA  GLU A 993    11371   7154  10884   -887   -229   -238       C  
ATOM   1067  C   GLU A 993     -24.846 -47.639 -76.763  1.00 74.55           C  
ANISOU 1067  C   GLU A 993    10755   6855  10715   -611   -277   -293       C  
ATOM   1068  O   GLU A 993     -23.682 -48.039 -76.765  1.00 80.60           O  
ANISOU 1068  O   GLU A 993    11460   7323  11841   -443   -477   -296       O  
ATOM   1069  CB  GLU A 993     -26.661 -49.179 -77.514  1.00 79.21           C  
ANISOU 1069  CB  GLU A 993    11448   7501  11148   -946      8   -475       C  
ATOM   1070  CG  GLU A 993     -27.704 -50.224 -77.171  1.00 89.28           C  
ANISOU 1070  CG  GLU A 993    12958   8683  12282  -1221     61   -453       C  
ATOM   1071  CD  GLU A 993     -28.181 -50.982 -78.392  1.00 94.21           C  
ANISOU 1071  CD  GLU A 993    13441   9371  12984  -1287    261   -696       C  
ATOM   1072  OE1 GLU A 993     -29.262 -51.604 -78.323  1.00102.69           O  
ANISOU 1072  OE1 GLU A 993    14641  10496  13879  -1532    376   -719       O  
ATOM   1073  OE2 GLU A 993     -27.471 -50.957 -79.421  1.00 86.51           O  
ANISOU 1073  OE2 GLU A 993    12237   8405  12229  -1138    326   -888       O  
ATOM   1074  N   ALA A 994     -25.194 -46.418 -77.155  1.00 65.42           N  
ANISOU 1074  N   ALA A 994     9430   6064   9362   -574   -104   -343       N  
ATOM   1075  CA  ALA A 994     -24.201 -45.434 -77.559  1.00 65.11           C  
ANISOU 1075  CA  ALA A 994     9183   6120   9437   -363   -131   -384       C  
ATOM   1076  C   ALA A 994     -23.367 -45.003 -76.358  1.00 70.51           C  
ANISOU 1076  C   ALA A 994    10008   6632  10151   -296   -379   -180       C  
ATOM   1077  O   ALA A 994     -22.190 -44.670 -76.494  1.00 76.74           O  
ANISOU 1077  O   ALA A 994    10658   7330  11168   -111   -502   -200       O  
ATOM   1078  CB  ALA A 994     -24.875 -44.233 -78.200  1.00 47.07           C  
ANISOU 1078  CB  ALA A 994     6725   4223   6937   -377     58   -434       C  
ATOM   1079  N   ALA A 995     -23.986 -45.017 -75.182  1.00 67.48           N  
ANISOU 1079  N   ALA A 995     9906   6215   9518   -497   -441     -1       N  
ATOM   1080  CA  ALA A 995     -23.300 -44.667 -73.946  1.00 65.18           C  
ANISOU 1080  CA  ALA A 995     9826   5774   9165   -543   -694    216       C  
ATOM   1081  C   ALA A 995     -22.244 -45.710 -73.605  1.00 70.49           C  
ANISOU 1081  C   ALA A 995    10594   6013  10177   -477  -1075    352       C  
ATOM   1082  O   ALA A 995     -21.121 -45.371 -73.228  1.00 74.62           O  
ANISOU 1082  O   ALA A 995    11075   6393  10886   -347  -1335    458       O  
ATOM   1083  CB  ALA A 995     -24.298 -44.529 -72.807  1.00 62.74           C  
ANISOU 1083  CB  ALA A 995     9835   5544   8461   -886   -616    326       C  
ATOM   1084  N   VAL A 996     -22.611 -46.981 -73.740  1.00 65.50           N  
ANISOU 1084  N   VAL A 996    10068   5147   9671   -565  -1129    348       N  
ATOM   1085  CA  VAL A 996     -21.679 -48.075 -73.499  1.00 65.88           C  
ANISOU 1085  CA  VAL A 996    10163   4703  10164   -484  -1519    467       C  
ATOM   1086  C   VAL A 996     -20.576 -48.079 -74.553  1.00 66.23           C  
ANISOU 1086  C   VAL A 996     9778   4645  10741   -137  -1498    219       C  
ATOM   1087  O   VAL A 996     -19.405 -48.299 -74.245  1.00 73.66           O  
ANISOU 1087  O   VAL A 996    10619   5249  12120     25  -1842    304       O  
ATOM   1088  CB  VAL A 996     -22.399 -49.440 -73.510  1.00 69.01           C  
ANISOU 1088  CB  VAL A 996    10760   4855  10606   -664  -1542    483       C  
ATOM   1089  CG1 VAL A 996     -21.397 -50.579 -73.398  1.00 66.22           C  
ANISOU 1089  CG1 VAL A 996    10383   3921  10855   -530  -1962    579       C  
ATOM   1090  CG2 VAL A 996     -23.420 -49.508 -72.386  1.00 75.10           C  
ANISOU 1090  CG2 VAL A 996    11985   5704  10847  -1079  -1560    710       C  
ATOM   1091  N   ASN A 997     -20.961 -47.815 -75.797  1.00 63.61           N  
ANISOU 1091  N   ASN A 997     9187   4610  10373    -65  -1095    -96       N  
ATOM   1092  CA  ASN A 997     -20.031 -47.864 -76.918  1.00 69.19           C  
ANISOU 1092  CA  ASN A 997     9507   5267  11516    157   -969   -412       C  
ATOM   1093  C   ASN A 997     -18.994 -46.742 -76.901  1.00 70.65           C  
ANISOU 1093  C   ASN A 997     9490   5571  11785    330  -1024   -426       C  
ATOM   1094  O   ASN A 997     -17.826 -46.962 -77.219  1.00 73.29           O  
ANISOU 1094  O   ASN A 997     9550   5667  12630    515  -1117   -590       O  
ATOM   1095  CB  ASN A 997     -20.798 -47.859 -78.242  1.00 66.76           C  
ANISOU 1095  CB  ASN A 997     9054   5282  11028     69   -537   -717       C  
ATOM   1096  CG  ASN A 997     -19.886 -47.981 -79.442  1.00 67.50           C  
ANISOU 1096  CG  ASN A 997     8794   5345  11508    183   -338  -1103       C  
ATOM   1097  OD1 ASN A 997     -19.577 -46.990 -80.104  1.00 71.61           O  
ANISOU 1097  OD1 ASN A 997     9145   6178  11886    199   -154  -1237       O  
ATOM   1098  ND2 ASN A 997     -19.445 -49.201 -79.728  1.00 65.57           N  
ANISOU 1098  ND2 ASN A 997     8438   4705  11770    229   -357  -1306       N  
ATOM   1099  N   LEU A 998     -19.424 -45.541 -76.528  1.00 67.34           N  
ANISOU 1099  N   LEU A 998     9181   5500  10905    261   -951   -284       N  
ATOM   1100  CA  LEU A 998     -18.528 -44.388 -76.489  1.00 66.27           C  
ANISOU 1100  CA  LEU A 998     8887   5502  10789    393   -986   -287       C  
ATOM   1101  C   LEU A 998     -17.469 -44.516 -75.396  1.00 74.85           C  
ANISOU 1101  C   LEU A 998    10033   6254  12154    475  -1423    -62       C  
ATOM   1102  O   LEU A 998     -16.433 -43.853 -75.446  1.00 79.91           O  
ANISOU 1102  O   LEU A 998    10469   6903  12989    618  -1501   -112       O  
ATOM   1103  CB  LEU A 998     -19.321 -43.091 -76.306  1.00 60.47           C  
ANISOU 1103  CB  LEU A 998     8262   5170   9543    290   -808   -192       C  
ATOM   1104  CG  LEU A 998     -20.006 -42.497 -77.539  1.00 56.08           C  
ANISOU 1104  CG  LEU A 998     7545   4974   8788    253   -461   -390       C  
ATOM   1105  CD1 LEU A 998     -20.886 -41.324 -77.146  1.00 45.19           C  
ANISOU 1105  CD1 LEU A 998     6264   3877   7029    167   -363   -258       C  
ATOM   1106  CD2 LEU A 998     -18.976 -42.065 -78.570  1.00 58.96           C  
ANISOU 1106  CD2 LEU A 998     7626   5418   9360    364   -354   -622       C  
ATOM   1107  N   ALA A 999     -17.732 -45.368 -74.410  1.00 76.53           N  
ANISOU 1107  N   ALA A 999    10538   6167  12372    345  -1737    203       N  
ATOM   1108  CA  ALA A 999     -16.803 -45.567 -73.303  1.00 77.77           C  
ANISOU 1108  CA  ALA A 999    10809   5974  12765    352  -2255    496       C  
ATOM   1109  C   ALA A 999     -15.710 -46.572 -73.660  1.00 88.38           C  
ANISOU 1109  C   ALA A 999    11847   6835  14899    585  -2529    387       C  
ATOM   1110  O   ALA A 999     -14.825 -46.852 -72.852  1.00 95.68           O  
ANISOU 1110  O   ALA A 999    12787   7390  16177    628  -3042    632       O  
ATOM   1111  CB  ALA A 999     -17.550 -46.012 -72.056  1.00 77.56           C  
ANISOU 1111  CB  ALA A 999    11283   5828  12357     22  -2513    859       C  
ATOM   1112  N   LYS A1000     -15.780 -47.112 -74.872  1.00 90.01           N  
ANISOU 1112  N   LYS A1000    11761   7028  15411    711  -2194      5       N  
ATOM   1113  CA  LYS A1000     -14.792 -48.078 -75.337  1.00 91.91           C  
ANISOU 1113  CA  LYS A1000    11638   6794  16490    930  -2344   -218       C  
ATOM   1114  C   LYS A1000     -13.838 -47.453 -76.350  1.00 98.71           C  
ANISOU 1114  C   LYS A1000    12014   7812  17680   1120  -2039   -647       C  
ATOM   1115  O   LYS A1000     -13.154 -48.161 -77.089  1.00110.37           O  
ANISOU 1115  O   LYS A1000    13104   9178  19653   1213  -1889   -989       O  
ATOM   1116  CB  LYS A1000     -15.481 -49.297 -75.954  1.00 86.95           C  
ANISOU 1116  CB  LYS A1000    11027   5987  16025    872  -2151   -408       C  
ATOM   1117  CG  LYS A1000     -16.333 -50.094 -74.979  1.00 86.56           C  
ANISOU 1117  CG  LYS A1000    11441   5741  15708    653  -2456    -11       C  
ATOM   1118  CD  LYS A1000     -16.864 -51.367 -75.622  1.00 85.81           C  
ANISOU 1118  CD  LYS A1000    11316   5450  15839    612  -2270   -222       C  
ATOM   1119  CE  LYS A1000     -17.644 -52.210 -74.624  1.00 83.93           C  
ANISOU 1119  CE  LYS A1000    11545   5010  15334    364  -2583    175       C  
ATOM   1120  NZ  LYS A1000     -18.100 -53.497 -75.218  1.00 81.82           N  
ANISOU 1120  NZ  LYS A1000    11249   4520  15318    328  -2423    -23       N  
ATOM   1121  N   SER A1001     -13.793 -46.125 -76.379  1.00 92.07           N  
ANISOU 1121  N   SER A1001    11193   7411  16380   1086  -1874   -623       N  
ATOM   1122  CA  SER A1001     -12.948 -45.412 -77.330  1.00 89.03           C  
ANISOU 1122  CA  SER A1001    10412   7228  16189   1190  -1564  -1010       C  
ATOM   1123  C   SER A1001     -11.698 -44.849 -76.663  1.00100.48           C  
ANISOU 1123  C   SER A1001    11674   8528  17976   1339  -1913   -898       C  
ATOM   1124  O   SER A1001     -11.537 -44.934 -75.446  1.00107.21           O  
ANISOU 1124  O   SER A1001    12740   9201  18792   1318  -2400   -479       O  
ATOM   1125  CB  SER A1001     -13.729 -44.279 -77.995  1.00 77.21           C  
ANISOU 1125  CB  SER A1001     9040   6317  13980   1029  -1133  -1082       C  
ATOM   1126  OG  SER A1001     -14.087 -43.286 -77.050  1.00 73.60           O  
ANISOU 1126  OG  SER A1001     8874   6074  13018    965  -1304   -711       O  
ATOM   1127  N   ARG A1002     -10.818 -44.273 -77.475  1.00103.45           N  
ANISOU 1127  N   ARG A1002    11666   9045  18596   1417  -1642  -1275       N  
ATOM   1128  CA  ARG A1002      -9.603 -43.639 -76.979  1.00105.16           C  
ANISOU 1128  CA  ARG A1002    11663   9260  19033   1500  -1888  -1212       C  
ATOM   1129  C   ARG A1002      -9.958 -42.340 -76.266  1.00 96.05           C  
ANISOU 1129  C   ARG A1002    10843   8402  17251   1424  -1988   -874       C  
ATOM   1130  O   ARG A1002      -9.263 -41.904 -75.346  1.00 97.31           O  
ANISOU 1130  O   ARG A1002    11015   8456  17500   1466  -2379   -623       O  
ATOM   1131  CB  ARG A1002      -8.648 -43.359 -78.140  1.00112.08           C  
ANISOU 1131  CB  ARG A1002    12059  10281  20246   1514  -1476  -1754       C  
ATOM   1132  CG  ARG A1002      -7.298 -42.803 -77.728  1.00123.33           C  
ANISOU 1132  CG  ARG A1002    13190  11684  21984   1578  -1701  -1758       C  
ATOM   1133  CD  ARG A1002      -6.468 -42.441 -78.947  1.00132.56           C  
ANISOU 1133  CD  ARG A1002    13930  13037  23402   1514  -1212  -2333       C  
ATOM   1134  NE  ARG A1002      -7.122 -41.424 -79.766  1.00132.98           N  
ANISOU 1134  NE  ARG A1002    14144  13465  22916   1406   -750  -2519       N  
ATOM   1135  CZ  ARG A1002      -6.638 -40.964 -80.914  1.00134.54           C  
ANISOU 1135  CZ  ARG A1002    14093  13910  23116   1243   -255  -3011       C  
ATOM   1136  NH1 ARG A1002      -5.491 -41.431 -81.388  1.00141.19           N  
ANISOU 1136  NH1 ARG A1002    14491  14655  24500   1173   -126  -3392       N  
ATOM   1137  NH2 ARG A1002      -7.301 -40.037 -81.592  1.00131.11           N  
ANISOU 1137  NH2 ARG A1002    13919  13924  21972   1013     88  -3029       N  
ATOM   1138  N   TRP A1003     -11.057 -41.733 -76.703  1.00 89.50           N  
ANISOU 1138  N   TRP A1003    10276   7993  15737   1260  -1620   -865       N  
ATOM   1139  CA  TRP A1003     -11.558 -40.492 -76.127  1.00 83.06           C  
ANISOU 1139  CA  TRP A1003     9765   7524  14271   1139  -1610   -592       C  
ATOM   1140  C   TRP A1003     -11.945 -40.663 -74.661  1.00 88.44           C  
ANISOU 1140  C   TRP A1003    10825   8042  14736   1049  -2035   -137       C  
ATOM   1141  O   TRP A1003     -11.802 -39.740 -73.860  1.00 92.44           O  
ANISOU 1141  O   TRP A1003    11505   8684  14932    965  -2171     79       O  
ATOM   1142  CB  TRP A1003     -12.753 -39.994 -76.942  1.00 78.34           C  
ANISOU 1142  CB  TRP A1003     9320   7318  13127    995  -1178   -680       C  
ATOM   1143  CG  TRP A1003     -13.523 -38.880 -76.305  1.00 77.72           C  
ANISOU 1143  CG  TRP A1003     9546   7518  12467    877  -1160   -414       C  
ATOM   1144  CD1 TRP A1003     -13.040 -37.665 -75.914  1.00 78.68           C  
ANISOU 1144  CD1 TRP A1003     9684   7799  12413    871  -1193   -330       C  
ATOM   1145  CD2 TRP A1003     -14.923 -38.870 -76.005  1.00 69.52           C  
ANISOU 1145  CD2 TRP A1003     8802   6611  11000    738  -1065   -248       C  
ATOM   1146  NE1 TRP A1003     -14.052 -36.903 -75.382  1.00 68.50           N  
ANISOU 1146  NE1 TRP A1003     8676   6707  10643    743  -1115   -138       N  
ATOM   1147  CE2 TRP A1003     -15.218 -37.621 -75.426  1.00 64.89           C  
ANISOU 1147  CE2 TRP A1003     8374   6239  10043    662  -1031    -96       C  
ATOM   1148  CE3 TRP A1003     -15.955 -39.800 -76.164  1.00 69.56           C  
ANISOU 1148  CE3 TRP A1003     8933   6565  10934    659   -990   -241       C  
ATOM   1149  CZ2 TRP A1003     -16.501 -37.276 -75.007  1.00 66.94           C  
ANISOU 1149  CZ2 TRP A1003     8868   6644   9924    519   -905     25       C  
ATOM   1150  CZ3 TRP A1003     -17.229 -39.456 -75.748  1.00 67.77           C  
ANISOU 1150  CZ3 TRP A1003     8951   6509  10289    509   -882    -97       C  
ATOM   1151  CH2 TRP A1003     -17.491 -38.206 -75.176  1.00 65.82           C  
ANISOU 1151  CH2 TRP A1003     8815   6457   9736    445   -833     18       C  
ATOM   1152  N   TYR A1004     -12.429 -41.851 -74.314  1.00 93.81           N  
ANISOU 1152  N   TYR A1004    11657   8431  15557   1014  -2230     -6       N  
ATOM   1153  CA  TYR A1004     -12.821 -42.143 -72.940  1.00101.41           C  
ANISOU 1153  CA  TYR A1004    13034   9223  16273    831  -2638    425       C  
ATOM   1154  C   TYR A1004     -11.604 -42.445 -72.069  1.00114.29           C  
ANISOU 1154  C   TYR A1004    14591  10465  18369    890  -3236    656       C  
ATOM   1155  O   TYR A1004     -11.636 -42.249 -70.855  1.00119.29           O  
ANISOU 1155  O   TYR A1004    15579  11045  18701    671  -3608   1036       O  
ATOM   1156  CB  TYR A1004     -13.806 -43.313 -72.902  1.00102.44           C  
ANISOU 1156  CB  TYR A1004    13388   9177  16357    721  -2643    497       C  
ATOM   1157  CG  TYR A1004     -14.340 -43.628 -71.522  1.00104.82           C  
ANISOU 1157  CG  TYR A1004    14186   9341  16300    428  -3009    925       C  
ATOM   1158  CD1 TYR A1004     -15.402 -42.911 -70.987  1.00101.60           C  
ANISOU 1158  CD1 TYR A1004    14135   9276  15190    151  -2773   1029       C  
ATOM   1159  CD2 TYR A1004     -13.787 -44.648 -70.757  1.00110.62           C  
ANISOU 1159  CD2 TYR A1004    15031   9579  17419    386  -3593   1213       C  
ATOM   1160  CE1 TYR A1004     -15.895 -43.197 -69.727  1.00103.41           C  
ANISOU 1160  CE1 TYR A1004    14845   9406  15041   -212  -3042   1365       C  
ATOM   1161  CE2 TYR A1004     -14.274 -44.941 -69.497  1.00111.82           C  
ANISOU 1161  CE2 TYR A1004    15691   9650  17145     14  -3924   1612       C  
ATOM   1162  CZ  TYR A1004     -15.328 -44.213 -68.987  1.00107.93           C  
ANISOU 1162  CZ  TYR A1004    15587   9518  15902   -307  -3632   1678       C  
ATOM   1163  OH  TYR A1004     -15.815 -44.503 -67.734  1.00109.42           O  
ANISOU 1163  OH  TYR A1004    16319   9617  15638   -764  -3919   2034       O  
ATOM   1164  N   ASN A1005     -10.531 -42.920 -72.694  1.00119.11           N  
ANISOU 1164  N   ASN A1005    14723  10841  19691   1134  -3306    402       N  
ATOM   1165  CA  ASN A1005      -9.312 -43.257 -71.965  1.00119.97           C  
ANISOU 1165  CA  ASN A1005    14641  10757  20185   1129  -3783    547       C  
ATOM   1166  C   ASN A1005      -8.407 -42.052 -71.728  1.00116.46           C  
ANISOU 1166  C   ASN A1005    14056  10478  19716   1161  -3855    547       C  
ATOM   1167  O   ASN A1005      -7.730 -41.969 -70.703  1.00120.47           O  
ANISOU 1167  O   ASN A1005    14640  10887  20245   1033  -4325    832       O  
ATOM   1168  CB  ASN A1005      -8.538 -44.365 -72.683  1.00120.22           C  
ANISOU 1168  CB  ASN A1005    14178  10542  20959   1294  -3766    228       C  
ATOM   1169  CG  ASN A1005      -9.267 -45.694 -72.660  1.00120.31           C  
ANISOU 1169  CG  ASN A1005    14341  10318  21052   1238  -3837    304       C  
ATOM   1170  OD1 ASN A1005      -9.549 -46.280 -73.705  1.00122.75           O  
ANISOU 1170  OD1 ASN A1005    14439  10599  21601   1341  -3456    -48       O  
ATOM   1171  ND2 ASN A1005      -9.575 -46.179 -71.462  1.00119.40           N  
ANISOU 1171  ND2 ASN A1005    14613  10043  20710   1028  -4317    754       N  
ATOM   1172  N   GLN A1006      -8.396 -41.122 -72.677  1.00109.78           N  
ANISOU 1172  N   GLN A1006    13015   9881  18815   1300  -3400    225       N  
ATOM   1173  CA  GLN A1006      -7.562 -39.930 -72.560  1.00109.10           C  
ANISOU 1173  CA  GLN A1006    12782   9967  18706   1337  -3419    189       C  
ATOM   1174  C   GLN A1006      -8.156 -38.908 -71.595  1.00 99.32           C  
ANISOU 1174  C   GLN A1006    12032   9020  16686   1082  -3470    530       C  
ATOM   1175  O   GLN A1006      -7.454 -38.374 -70.736  1.00103.96           O  
ANISOU 1175  O   GLN A1006    12679   9577  17243    996  -3827    751       O  
ATOM   1176  CB  GLN A1006      -7.334 -39.292 -73.931  1.00117.21           C  
ANISOU 1176  CB  GLN A1006    13461  11295  19779   1439  -2825   -307       C  
ATOM   1177  CG  GLN A1006      -6.480 -40.130 -74.865  1.00132.52           C  
ANISOU 1177  CG  GLN A1006    14866  13025  22459   1589  -2685   -746       C  
ATOM   1178  CD  GLN A1006      -6.188 -39.424 -76.173  1.00141.01           C  
ANISOU 1178  CD  GLN A1006    15635  14374  23568   1617  -2117  -1249       C  
ATOM   1179  OE1 GLN A1006      -6.791 -38.397 -76.484  1.00140.46           O  
ANISOU 1179  OE1 GLN A1006    15815  14738  22815   1463  -1793  -1222       O  
ATOM   1180  NE2 GLN A1006      -5.256 -39.971 -76.946  1.00146.78           N  
ANISOU 1180  NE2 GLN A1006    15900  15016  24854   1631  -1925  -1680       N  
ATOM   1181  N   THR A1007      -9.447 -38.635 -71.743  1.00 90.10           N  
ANISOU 1181  N   THR A1007    11190   8136  14910    936  -3094    541       N  
ATOM   1182  CA  THR A1007     -10.138 -37.704 -70.857  1.00 89.03           C  
ANISOU 1182  CA  THR A1007    11488   8264  14075    668  -3045    778       C  
ATOM   1183  C   THR A1007     -11.403 -38.335 -70.283  1.00 91.65           C  
ANISOU 1183  C   THR A1007    12244   8560  14020    442  -3046    980       C  
ATOM   1184  O   THR A1007     -12.507 -38.043 -70.740  1.00 94.39           O  
ANISOU 1184  O   THR A1007    12693   9161  14011    391  -2610    849       O  
ATOM   1185  CB  THR A1007     -10.505 -36.393 -71.582  1.00 82.79           C  
ANISOU 1185  CB  THR A1007    10638   7898  12922    682  -2517    543       C  
ATOM   1186  OG1 THR A1007     -11.257 -36.691 -72.766  1.00 76.43           O  
ANISOU 1186  OG1 THR A1007     9704   7213  12123    779  -2111    292       O  
ATOM   1187  CG2 THR A1007      -9.250 -35.624 -71.966  1.00 84.26           C  
ANISOU 1187  CG2 THR A1007    10488   8150  13377    813  -2520    375       C  
ATOM   1188  N   PRO A1008     -11.243 -39.201 -69.270  1.00 91.08           N  
ANISOU 1188  N   PRO A1008    12419   8160  14028    275  -3564   1312       N  
ATOM   1189  CA  PRO A1008     -12.362 -39.952 -68.689  1.00 88.75           C  
ANISOU 1189  CA  PRO A1008    12546   7788  13386      4  -3601   1507       C  
ATOM   1190  C   PRO A1008     -13.387 -39.073 -67.974  1.00 89.53           C  
ANISOU 1190  C   PRO A1008    13060   8223  12734   -355  -3301   1563       C  
ATOM   1191  O   PRO A1008     -14.584 -39.301 -68.132  1.00 88.10           O  
ANISOU 1191  O   PRO A1008    13040   8167  12268   -471  -2968   1477       O  
ATOM   1192  CB  PRO A1008     -11.673 -40.889 -67.691  1.00 93.16           C  
ANISOU 1192  CB  PRO A1008    13285   7897  14216   -143  -4332   1901       C  
ATOM   1193  CG  PRO A1008     -10.401 -40.204 -67.346  1.00 99.99           C  
ANISOU 1193  CG  PRO A1008    13957   8737  15299    -79  -4652   1975       C  
ATOM   1194  CD  PRO A1008      -9.968 -39.504 -68.598  1.00 97.40           C  
ANISOU 1194  CD  PRO A1008    13119   8627  15263    296  -4193   1544       C  
ATOM   1195  N   ASN A1009     -12.927 -38.091 -67.205  1.00 92.68           N  
ANISOU 1195  N   ASN A1009    13602   8757  12854   -542  -3395   1668       N  
ATOM   1196  CA  ASN A1009     -13.828 -37.239 -66.432  1.00 91.04           C  
ANISOU 1196  CA  ASN A1009    13772   8829  11990   -924  -3087   1667       C  
ATOM   1197  C   ASN A1009     -14.813 -36.458 -67.297  1.00 84.38           C  
ANISOU 1197  C   ASN A1009    12752   8304  11005   -775  -2434   1324       C  
ATOM   1198  O   ASN A1009     -15.976 -36.290 -66.932  1.00 86.29           O  
ANISOU 1198  O   ASN A1009    13230   8690  10868  -1033  -2114   1254       O  
ATOM   1199  CB  ASN A1009     -13.031 -36.281 -65.545  1.00 94.22           C  
ANISOU 1199  CB  ASN A1009    14319   9311  12169  -1144  -3287   1795       C  
ATOM   1200  CG  ASN A1009     -12.201 -37.006 -64.506  1.00 96.02           C  
ANISOU 1200  CG  ASN A1009    14807   9229  12448  -1410  -4006   2206       C  
ATOM   1201  OD1 ASN A1009     -12.544 -38.111 -64.083  1.00 96.77           O  
ANISOU 1201  OD1 ASN A1009    15163   9080  12524  -1608  -4311   2438       O  
ATOM   1202  ND2 ASN A1009     -11.103 -36.388 -64.087  1.00 96.07           N  
ANISOU 1202  ND2 ASN A1009    14749   9226  12527  -1440  -4321   2321       N  
ATOM   1203  N   ARG A1010     -14.338 -35.987 -68.445  1.00 78.31           N  
ANISOU 1203  N   ARG A1010    11559   7630  10567   -390  -2256   1109       N  
ATOM   1204  CA  ARG A1010     -15.174 -35.240 -69.377  1.00 70.98           C  
ANISOU 1204  CA  ARG A1010    10445   6965   9560   -247  -1742    841       C  
ATOM   1205  C   ARG A1010     -16.034 -36.185 -70.208  1.00 67.80           C  
ANISOU 1205  C   ARG A1010     9947   6529   9284   -137  -1583    740       C  
ATOM   1206  O   ARG A1010     -17.221 -35.928 -70.443  1.00 63.86           O  
ANISOU 1206  O   ARG A1010     9484   6194   8586   -206  -1241    624       O  
ATOM   1207  CB  ARG A1010     -14.300 -34.386 -70.294  1.00 68.95           C  
ANISOU 1207  CB  ARG A1010     9833   6822   9542     32  -1649    680       C  
ATOM   1208  CG  ARG A1010     -15.060 -33.658 -71.385  1.00 67.24           C  
ANISOU 1208  CG  ARG A1010     9428   6837   9285    165  -1223    462       C  
ATOM   1209  CD  ARG A1010     -14.121 -32.785 -72.194  1.00 66.44           C  
ANISOU 1209  CD  ARG A1010     9053   6843   9350    345  -1164    335       C  
ATOM   1210  NE  ARG A1010     -14.809 -32.075 -73.266  1.00 62.68           N  
ANISOU 1210  NE  ARG A1010     8435   6560   8820    420   -840    187       N  
ATOM   1211  CZ  ARG A1010     -14.247 -31.126 -74.006  1.00 57.83           C  
ANISOU 1211  CZ  ARG A1010     7650   6072   8250    497   -738     89       C  
ATOM   1212  NH1 ARG A1010     -12.990 -30.772 -73.782  1.00 48.80           N  
ANISOU 1212  NH1 ARG A1010     6427   4901   7213    526   -884     80       N  
ATOM   1213  NH2 ARG A1010     -14.942 -30.526 -74.964  1.00 59.88           N  
ANISOU 1213  NH2 ARG A1010     7826   6476   8450    515   -521     17       N  
ATOM   1214  N   ALA A1011     -15.423 -37.280 -70.650  1.00 70.23           N  
ANISOU 1214  N   ALA A1011    10108   6603   9972     29  -1835    767       N  
ATOM   1215  CA  ALA A1011     -16.120 -38.290 -71.435  1.00 69.50           C  
ANISOU 1215  CA  ALA A1011     9933   6447  10025    111  -1707    661       C  
ATOM   1216  C   ALA A1011     -17.326 -38.839 -70.682  1.00 79.66           C  
ANISOU 1216  C   ALA A1011    11575   7715  10977   -183  -1659    779       C  
ATOM   1217  O   ALA A1011     -18.371 -39.075 -71.276  1.00 83.63           O  
ANISOU 1217  O   ALA A1011    12038   8336  11400   -187  -1367    643       O  
ATOM   1218  CB  ALA A1011     -15.174 -39.415 -71.823  1.00 62.41           C  
ANISOU 1218  CB  ALA A1011     8833   5227   9654    301  -2008    655       C  
ATOM   1219  N   LYS A1012     -17.178 -39.037 -69.375  1.00 80.06           N  
ANISOU 1219  N   LYS A1012    11983   7626  10811   -478  -1951   1030       N  
ATOM   1220  CA  LYS A1012     -18.283 -39.515 -68.550  1.00 81.59           C  
ANISOU 1220  CA  LYS A1012    12566   7817  10619   -861  -1882   1124       C  
ATOM   1221  C   LYS A1012     -19.449 -38.532 -68.564  1.00 79.17           C  
ANISOU 1221  C   LYS A1012    12266   7837   9980   -991  -1365    904       C  
ATOM   1222  O   LYS A1012     -20.607 -38.935 -68.651  1.00 79.83           O  
ANISOU 1222  O   LYS A1012    12419   7985   9926  -1130  -1112    805       O  
ATOM   1223  CB  LYS A1012     -17.826 -39.764 -67.110  1.00 84.31           C  
ANISOU 1223  CB  LYS A1012    13346   7978  10711  -1256  -2306   1446       C  
ATOM   1224  CG  LYS A1012     -16.981 -41.014 -66.925  1.00 87.66           C  
ANISOU 1224  CG  LYS A1012    13826   7982  11497  -1209  -2900   1727       C  
ATOM   1225  CD  LYS A1012     -16.509 -41.146 -65.484  1.00 94.30           C  
ANISOU 1225  CD  LYS A1012    15133   8649  12049  -1662  -3403   2108       C  
ATOM   1226  CE  LYS A1012     -15.603 -42.354 -65.306  1.00100.14           C  
ANISOU 1226  CE  LYS A1012    15883   8898  13266  -1585  -4098   2433       C  
ATOM   1227  NZ  LYS A1012     -15.103 -42.478 -63.909  1.00106.43           N  
ANISOU 1227  NZ  LYS A1012    17041   9645  13752  -2041  -4602   2760       N  
ATOM   1228  N   ARG A1013     -19.139 -37.242 -68.483  1.00 75.51           N  
ANISOU 1228  N   ARG A1013    11699   7550   9441   -943  -1215    815       N  
ATOM   1229  CA  ARG A1013     -20.171 -36.212 -68.462  1.00 75.18           C  
ANISOU 1229  CA  ARG A1013    11609   7752   9205  -1041   -751    591       C  
ATOM   1230  C   ARG A1013     -20.887 -36.103 -69.805  1.00 80.64           C  
ANISOU 1230  C   ARG A1013    11935   8567  10135   -740   -481    397       C  
ATOM   1231  O   ARG A1013     -22.114 -35.990 -69.856  1.00 88.72           O  
ANISOU 1231  O   ARG A1013    12929   9697  11084   -850   -173    246       O  
ATOM   1232  CB  ARG A1013     -19.583 -34.857 -68.058  1.00 73.02           C  
ANISOU 1232  CB  ARG A1013    11312   7586   8845  -1058   -686    549       C  
ATOM   1233  CG  ARG A1013     -19.084 -34.802 -66.622  1.00 81.61           C  
ANISOU 1233  CG  ARG A1013    12809   8605   9593  -1476   -899    717       C  
ATOM   1234  CD  ARG A1013     -18.709 -33.385 -66.216  1.00 86.43           C  
ANISOU 1234  CD  ARG A1013    13404   9350  10087  -1544   -735    610       C  
ATOM   1235  NE  ARG A1013     -17.588 -32.863 -66.993  1.00 87.72           N  
ANISOU 1235  NE  ARG A1013    13265   9515  10551  -1154   -908    643       N  
ATOM   1236  CZ  ARG A1013     -16.316 -32.950 -66.619  1.00 92.52           C  
ANISOU 1236  CZ  ARG A1013    13934  10020  11200  -1157  -1316    842       C  
ATOM   1237  NH1 ARG A1013     -15.997 -33.540 -65.475  1.00 94.40           N  
ANISOU 1237  NH1 ARG A1013    14549  10130  11190  -1533  -1659   1080       N  
ATOM   1238  NH2 ARG A1013     -15.360 -32.447 -67.389  1.00 94.36           N  
ANISOU 1238  NH2 ARG A1013    13853  10274  11725   -822  -1402    808       N  
ATOM   1239  N   VAL A1014     -20.118 -36.141 -70.890  1.00 77.49           N  
ANISOU 1239  N   VAL A1014    11258   8155  10028   -402   -601    389       N  
ATOM   1240  CA  VAL A1014     -20.699 -36.073 -72.228  1.00 68.11           C  
ANISOU 1240  CA  VAL A1014     9772   7093   9013   -190   -401    238       C  
ATOM   1241  C   VAL A1014     -21.560 -37.304 -72.519  1.00 72.31           C  
ANISOU 1241  C   VAL A1014    10349   7568   9557   -261   -364    218       C  
ATOM   1242  O   VAL A1014     -22.677 -37.189 -73.028  1.00 78.90           O  
ANISOU 1242  O   VAL A1014    11067   8535  10379   -281   -132    103       O  
ATOM   1243  CB  VAL A1014     -19.611 -35.936 -73.308  1.00 58.69           C  
ANISOU 1243  CB  VAL A1014     8322   5907   8071     81   -511    201       C  
ATOM   1244  CG1 VAL A1014     -20.237 -35.903 -74.693  1.00 60.18           C  
ANISOU 1244  CG1 VAL A1014     8274   6242   8350    190   -328     68       C  
ATOM   1245  CG2 VAL A1014     -18.783 -34.685 -73.067  1.00 56.12           C  
ANISOU 1245  CG2 VAL A1014     7948   5649   7724    135   -533    213       C  
ATOM   1246  N   ILE A1015     -21.033 -38.477 -72.184  1.00 64.01           N  
ANISOU 1246  N   ILE A1015     9456   6294   8570   -305   -623    339       N  
ATOM   1247  CA  ILE A1015     -21.750 -39.734 -72.365  1.00 59.91           C  
ANISOU 1247  CA  ILE A1015     9023   5674   8068   -398   -617    334       C  
ATOM   1248  C   ILE A1015     -23.038 -39.762 -71.545  1.00 64.32           C  
ANISOU 1248  C   ILE A1015     9809   6311   8318   -723   -411    317       C  
ATOM   1249  O   ILE A1015     -24.083 -40.182 -72.039  1.00 64.23           O  
ANISOU 1249  O   ILE A1015     9724   6381   8301   -769   -212    203       O  
ATOM   1250  CB  ILE A1015     -20.864 -40.945 -72.000  1.00 60.77           C  
ANISOU 1250  CB  ILE A1015     9277   5447   8365   -397   -995    498       C  
ATOM   1251  CG1 ILE A1015     -19.813 -41.182 -73.086  1.00 54.28           C  
ANISOU 1251  CG1 ILE A1015     8128   4533   7964    -76  -1089    388       C  
ATOM   1252  CG2 ILE A1015     -21.703 -42.197 -71.810  1.00 64.06           C  
ANISOU 1252  CG2 ILE A1015     9899   5722   8718   -593  -1007    540       C  
ATOM   1253  CD1 ILE A1015     -18.845 -42.301 -72.765  1.00 55.78           C  
ANISOU 1253  CD1 ILE A1015     8358   4327   8510    -18  -1484    513       C  
ATOM   1254  N   THR A1016     -22.959 -39.308 -70.298  1.00 67.52           N  
ANISOU 1254  N   THR A1016    10486   6703   8465   -990   -439    402       N  
ATOM   1255  CA  THR A1016     -24.132 -39.237 -69.432  1.00 71.25           C  
ANISOU 1255  CA  THR A1016    11178   7265   8631  -1377   -170    312       C  
ATOM   1256  C   THR A1016     -25.163 -38.280 -70.020  1.00 70.11           C  
ANISOU 1256  C   THR A1016    10706   7351   8581  -1277    234     48       C  
ATOM   1257  O   THR A1016     -26.367 -38.538 -69.971  1.00 68.80           O  
ANISOU 1257  O   THR A1016    10518   7259   8364  -1457    494   -105       O  
ATOM   1258  CB  THR A1016     -23.762 -38.781 -68.005  1.00 72.06           C  
ANISOU 1258  CB  THR A1016    11644   7336   8398  -1751   -238    410       C  
ATOM   1259  OG1 THR A1016     -22.795 -39.681 -67.449  1.00 71.52           O  
ANISOU 1259  OG1 THR A1016    11878   7014   8284  -1860   -718    718       O  
ATOM   1260  CG2 THR A1016     -24.993 -38.756 -67.110  1.00 75.74           C  
ANISOU 1260  CG2 THR A1016    12344   7903   8531  -2237    119    241       C  
ATOM   1261  N   THR A1017     -24.677 -37.178 -70.584  1.00 67.33           N  
ANISOU 1261  N   THR A1017    10087   7089   8405   -999    257      2       N  
ATOM   1262  CA  THR A1017     -25.535 -36.203 -71.246  1.00 65.94           C  
ANISOU 1262  CA  THR A1017     9568   7069   8415   -862    533   -191       C  
ATOM   1263  C   THR A1017     -26.239 -36.825 -72.452  1.00 71.64           C  
ANISOU 1263  C   THR A1017    10055   7848   9318   -712    547   -229       C  
ATOM   1264  O   THR A1017     -27.392 -36.509 -72.744  1.00 75.11           O  
ANISOU 1264  O   THR A1017    10279   8379   9880   -741    760   -379       O  
ATOM   1265  CB  THR A1017     -24.727 -34.971 -71.694  1.00 65.13           C  
ANISOU 1265  CB  THR A1017     9272   7013   8460   -607    474   -173       C  
ATOM   1266  OG1 THR A1017     -24.082 -34.387 -70.556  1.00 69.86           O  
ANISOU 1266  OG1 THR A1017    10098   7572   8875   -778    466   -147       O  
ATOM   1267  CG2 THR A1017     -25.631 -33.938 -72.344  1.00 63.59           C  
ANISOU 1267  CG2 THR A1017     8734   6917   8511   -482    682   -323       C  
ATOM   1268  N   PHE A1018     -25.539 -37.717 -73.145  1.00 75.32           N  
ANISOU 1268  N   PHE A1018    10544   8244   9830   -573    320   -115       N  
ATOM   1269  CA  PHE A1018     -26.117 -38.434 -74.277  1.00 72.00           C  
ANISOU 1269  CA  PHE A1018     9954   7877   9526   -498    335   -162       C  
ATOM   1270  C   PHE A1018     -27.172 -39.444 -73.831  1.00 71.90           C  
ANISOU 1270  C   PHE A1018    10088   7832   9401   -750    452   -215       C  
ATOM   1271  O   PHE A1018     -28.235 -39.558 -74.441  1.00 70.53           O  
ANISOU 1271  O   PHE A1018     9725   7770   9303   -779    592   -321       O  
ATOM   1272  CB  PHE A1018     -25.022 -39.145 -75.075  1.00 65.26           C  
ANISOU 1272  CB  PHE A1018     9086   6933   8778   -329    124   -100       C  
ATOM   1273  CG  PHE A1018     -24.491 -38.340 -76.225  1.00 55.58           C  
ANISOU 1273  CG  PHE A1018     7607   5834   7677   -130    104   -133       C  
ATOM   1274  CD1 PHE A1018     -25.356 -37.687 -77.088  1.00 55.59           C  
ANISOU 1274  CD1 PHE A1018     7389   6015   7717   -119    202   -181       C  
ATOM   1275  CD2 PHE A1018     -23.128 -38.233 -76.442  1.00 46.97           C  
ANISOU 1275  CD2 PHE A1018     6497   4673   6677     10    -37   -111       C  
ATOM   1276  CE1 PHE A1018     -24.872 -36.946 -78.148  1.00 52.20           C  
ANISOU 1276  CE1 PHE A1018     6791   5698   7344    -17    146   -172       C  
ATOM   1277  CE2 PHE A1018     -22.637 -37.491 -77.498  1.00 45.92           C  
ANISOU 1277  CE2 PHE A1018     6168   4673   6606    116    -26   -161       C  
ATOM   1278  CZ  PHE A1018     -23.510 -36.846 -78.354  1.00 49.45           C  
ANISOU 1278  CZ  PHE A1018     6463   5306   7021     81     58   -175       C  
ATOM   1279  N   ARG A1019     -26.868 -40.171 -72.761  1.00 69.81           N  
ANISOU 1279  N   ARG A1019    10170   7406   8950   -964    364   -124       N  
ATOM   1280  CA  ARG A1019     -27.736 -41.236 -72.271  1.00 70.60           C  
ANISOU 1280  CA  ARG A1019    10485   7446   8896  -1262    446   -148       C  
ATOM   1281  C   ARG A1019     -29.016 -40.695 -71.644  1.00 78.47           C  
ANISOU 1281  C   ARG A1019    11443   8587   9784  -1531    796   -346       C  
ATOM   1282  O   ARG A1019     -30.119 -41.031 -72.075  1.00 79.67           O  
ANISOU 1282  O   ARG A1019    11434   8831  10004  -1603    978   -489       O  
ATOM   1283  CB  ARG A1019     -26.987 -42.103 -71.258  1.00 67.22           C  
ANISOU 1283  CB  ARG A1019    10484   6770   8289  -1471    183     58       C  
ATOM   1284  CG  ARG A1019     -27.817 -43.229 -70.669  1.00 71.85           C  
ANISOU 1284  CG  ARG A1019    11370   7264   8666  -1846    235     71       C  
ATOM   1285  CD  ARG A1019     -26.994 -44.061 -69.702  1.00 83.69           C  
ANISOU 1285  CD  ARG A1019    13316   8467  10014  -2068   -135    349       C  
ATOM   1286  NE  ARG A1019     -26.425 -43.244 -68.634  1.00 92.60           N  
ANISOU 1286  NE  ARG A1019    14659   9604  10919  -2253   -216    450       N  
ATOM   1287  CZ  ARG A1019     -27.001 -43.052 -67.452  1.00 97.06           C  
ANISOU 1287  CZ  ARG A1019    15564  10234  11081  -2760    -50    420       C  
ATOM   1288  NH1 ARG A1019     -28.166 -43.625 -67.179  1.00 98.28           N  
ANISOU 1288  NH1 ARG A1019    15865  10447  11032  -3121    215    284       N  
ATOM   1289  NH2 ARG A1019     -26.411 -42.290 -66.541  1.00 95.91           N  
ANISOU 1289  NH2 ARG A1019    15619  10105  10718  -2954   -123    498       N  
ATOM   1290  N   THR A1020     -28.860 -39.859 -70.623  1.00 81.98           N  
ANISOU 1290  N   THR A1020    12016   9047  10087  -1701    906   -388       N  
ATOM   1291  CA  THR A1020     -30.001 -39.307 -69.902  1.00 79.96           C  
ANISOU 1291  CA  THR A1020    11712   8900   9768  -2006   1304   -657       C  
ATOM   1292  C   THR A1020     -30.782 -38.317 -70.761  1.00 79.15           C  
ANISOU 1292  C   THR A1020    11086   8930  10057  -1743   1501   -861       C  
ATOM   1293  O   THR A1020     -32.011 -38.346 -70.796  1.00 79.74           O  
ANISOU 1293  O   THR A1020    10950   9078  10269  -1880   1773  -1092       O  
ATOM   1294  CB  THR A1020     -29.556 -38.605 -68.607  1.00 77.44           C  
ANISOU 1294  CB  THR A1020    11672   8561   9192  -2299   1400   -689       C  
ATOM   1295  OG1 THR A1020     -28.772 -37.450 -68.932  1.00 74.84           O  
ANISOU 1295  OG1 THR A1020    11134   8251   9050  -1974   1314   -654       O  
ATOM   1296  CG2 THR A1020     -28.729 -39.549 -67.748  1.00 78.71           C  
ANISOU 1296  CG2 THR A1020    12370   8562   8973  -2592   1090   -411       C  
ATOM   1297  N   GLY A1021     -30.059 -37.445 -71.454  1.00 80.08           N  
ANISOU 1297  N   GLY A1021    10988   9060  10380  -1383   1335   -765       N  
ATOM   1298  CA  GLY A1021     -30.683 -36.428 -72.279  1.00 82.37           C  
ANISOU 1298  CA  GLY A1021    10812   9424  11060  -1142   1418   -883       C  
ATOM   1299  C   GLY A1021     -30.951 -35.162 -71.491  1.00 82.73           C  
ANISOU 1299  C   GLY A1021    10732   9451  11253  -1220   1687  -1100       C  
ATOM   1300  O   GLY A1021     -31.591 -34.233 -71.983  1.00 84.01           O  
ANISOU 1300  O   GLY A1021    10482   9611  11826  -1050   1769  -1228       O  
ATOM   1301  N   THR A1022     -30.457 -35.129 -70.258  1.00 84.62           N  
ANISOU 1301  N   THR A1022    11329   9651  11173  -1506   1804  -1141       N  
ATOM   1302  CA  THR A1022     -30.631 -33.971 -69.392  1.00 94.69           C  
ANISOU 1302  CA  THR A1022    12542  10905  12532  -1659   2116  -1397       C  
ATOM   1303  C   THR A1022     -29.282 -33.387 -68.992  1.00 91.03           C  
ANISOU 1303  C   THR A1022    12322  10403  11863  -1604   1932  -1222       C  
ATOM   1304  O   THR A1022     -28.235 -33.868 -69.425  1.00 95.22           O  
ANISOU 1304  O   THR A1022    13016  10918  12245  -1421   1561   -917       O  
ATOM   1305  CB  THR A1022     -31.421 -34.332 -68.123  1.00107.51           C  
ANISOU 1305  CB  THR A1022    14394  12548  13907  -2208   2526  -1695       C  
ATOM   1306  OG1 THR A1022     -30.760 -35.404 -67.439  1.00108.57           O  
ANISOU 1306  OG1 THR A1022    15084  12671  13495  -2520   2336  -1466       O  
ATOM   1307  CG2 THR A1022     -32.836 -34.763 -68.483  1.00113.45           C  
ANISOU 1307  CG2 THR A1022    14829  13341  14936  -2274   2767  -1939       C  
ATOM   1308  N   TRP A1023     -29.310 -32.350 -68.162  1.00 85.24           N  
ANISOU 1308  N   TRP A1023    11586   9646  11154  -1779   2215  -1453       N  
ATOM   1309  CA  TRP A1023     -28.086 -31.686 -67.733  1.00 84.21           C  
ANISOU 1309  CA  TRP A1023    11669   9491  10835  -1762   2067  -1318       C  
ATOM   1310  C   TRP A1023     -27.667 -32.120 -66.333  1.00 89.10           C  
ANISOU 1310  C   TRP A1023    12823  10124  10909  -2295   2128  -1314       C  
ATOM   1311  O   TRP A1023     -27.073 -31.339 -65.591  1.00 92.14           O  
ANISOU 1311  O   TRP A1023    13374  10503  11133  -2472   2202  -1370       O  
ATOM   1312  CB  TRP A1023     -28.259 -30.166 -67.772  1.00 86.38           C  
ANISOU 1312  CB  TRP A1023    11615   9710  11495  -1616   2300  -1553       C  
ATOM   1313  CG  TRP A1023     -28.503 -29.621 -69.144  1.00 88.16           C  
ANISOU 1313  CG  TRP A1023    11374   9892  12232  -1128   2124  -1467       C  
ATOM   1314  CD1 TRP A1023     -29.698 -29.218 -69.666  1.00 91.77           C  
ANISOU 1314  CD1 TRP A1023    11378  10285  13205   -998   2289  -1672       C  
ATOM   1315  CD2 TRP A1023     -27.528 -29.421 -70.174  1.00 84.08           C  
ANISOU 1315  CD2 TRP A1023    10806   9384  11756   -761   1722  -1145       C  
ATOM   1316  NE1 TRP A1023     -29.526 -28.777 -70.956  1.00 90.93           N  
ANISOU 1316  NE1 TRP A1023    10986  10144  13420   -594   1959  -1443       N  
ATOM   1317  CE2 TRP A1023     -28.202 -28.891 -71.291  1.00 83.97           C  
ANISOU 1317  CE2 TRP A1023    10362   9323  12221   -467   1643  -1138       C  
ATOM   1318  CE3 TRP A1023     -26.149 -29.638 -70.258  1.00 78.22           C  
ANISOU 1318  CE3 TRP A1023    10328   8679  10713   -684   1418   -875       C  
ATOM   1319  CZ2 TRP A1023     -27.546 -28.576 -72.478  1.00 79.50           C  
ANISOU 1319  CZ2 TRP A1023     9689   8770  11749   -165   1293   -867       C  
ATOM   1320  CZ3 TRP A1023     -25.499 -29.324 -71.437  1.00 77.76           C  
ANISOU 1320  CZ3 TRP A1023    10106   8634  10803   -351   1130   -667       C  
ATOM   1321  CH2 TRP A1023     -26.198 -28.799 -72.530  1.00 80.09           C  
ANISOU 1321  CH2 TRP A1023    10037   8907  11487   -125   1080   -662       C  
ATOM   1322  N   ASP A1024     -27.973 -33.365 -65.980  1.00125.40           N  
ANISOU 1322  N   ASP A1024    19198  16116  12332  -6303  -3613    259       N  
ATOM   1323  CA  ASP A1024     -27.677 -33.884 -64.646  1.00123.41           C  
ANISOU 1323  CA  ASP A1024    19063  15654  12173  -6347  -3580    327       C  
ATOM   1324  C   ASP A1024     -26.188 -33.843 -64.310  1.00111.17           C  
ANISOU 1324  C   ASP A1024    17822  13678  10741  -5896  -3449     73       C  
ATOM   1325  O   ASP A1024     -25.809 -33.629 -63.160  1.00112.64           O  
ANISOU 1325  O   ASP A1024    17894  13853  11052  -5787  -3352    116       O  
ATOM   1326  CB  ASP A1024     -28.201 -35.316 -64.499  1.00133.82           C  
ANISOU 1326  CB  ASP A1024    20782  16698  13366  -6772  -3759    445       C  
ATOM   1327  CG  ASP A1024     -29.712 -35.395 -64.578  1.00140.65           C  
ANISOU 1327  CG  ASP A1024    21309  18026  14104  -7254  -3879    744       C  
ATOM   1328  OD1 ASP A1024     -30.382 -34.435 -64.143  1.00139.79           O  
ANISOU 1328  OD1 ASP A1024    20600  18467  14048  -7267  -3793    925       O  
ATOM   1329  OD2 ASP A1024     -30.229 -36.417 -65.075  1.00146.16           O  
ANISOU 1329  OD2 ASP A1024    22344  18551  14639  -7606  -4058    803       O  
ATOM   1330  N   ALA A1025     -25.348 -34.043 -65.319  1.00100.27           N  
ANISOU 1330  N   ALA A1025    16817  11973   9308  -5625  -3439   -184       N  
ATOM   1331  CA  ALA A1025     -23.906 -34.091 -65.108  1.00 95.76           C  
ANISOU 1331  CA  ALA A1025    16559  11004   8820  -5169  -3307   -425       C  
ATOM   1332  C   ALA A1025     -23.301 -32.703 -64.907  1.00 95.54           C  
ANISOU 1332  C   ALA A1025    16154  11242   8904  -4794  -3123   -497       C  
ATOM   1333  O   ALA A1025     -22.144 -32.579 -64.504  1.00 90.29           O  
ANISOU 1333  O   ALA A1025    15653  10331   8321  -4422  -2991   -654       O  
ATOM   1334  CB  ALA A1025     -23.224 -34.808 -66.264  1.00 98.17           C  
ANISOU 1334  CB  ALA A1025    17376  10916   9008  -4981  -3344   -666       C  
ATOM   1335  N   TYR A1026     -24.084 -31.664 -65.182  1.00104.14           N  
ANISOU 1335  N   TYR A1026    16741  12842   9986  -4882  -3117   -367       N  
ATOM   1336  CA  TYR A1026     -23.593 -30.292 -65.083  1.00107.32           C  
ANISOU 1336  CA  TYR A1026    16789  13520  10466  -4540  -2963   -413       C  
ATOM   1337  C   TYR A1026     -24.434 -29.417 -64.153  1.00118.90           C  
ANISOU 1337  C   TYR A1026    17658  15478  12040  -4638  -2905   -161       C  
ATOM   1338  O   TYR A1026     -23.997 -28.342 -63.742  1.00117.38           O  
ANISOU 1338  O   TYR A1026    17125  15452  12021  -4228  -2669   -141       O  
ATOM   1339  CB  TYR A1026     -23.515 -29.650 -66.471  1.00101.72           C  
ANISOU 1339  CB  TYR A1026    16026  12971   9653  -4376  -2956   -515       C  
ATOM   1340  CG  TYR A1026     -22.586 -30.362 -67.428  1.00102.90           C  
ANISOU 1340  CG  TYR A1026    16696  12694   9708  -4167  -2950   -770       C  
ATOM   1341  CD1 TYR A1026     -21.225 -30.086 -67.440  1.00 96.79           C  
ANISOU 1341  CD1 TYR A1026    16112  11695   8969  -3715  -2788   -978       C  
ATOM   1342  CD2 TYR A1026     -23.070 -31.310 -68.322  1.00111.70           C  
ANISOU 1342  CD2 TYR A1026    18099  13656  10686  -4406  -3098   -798       C  
ATOM   1343  CE1 TYR A1026     -20.372 -30.734 -68.312  1.00 98.84           C  
ANISOU 1343  CE1 TYR A1026    16803  11620   9134  -3480  -2761  -1202       C  
ATOM   1344  CE2 TYR A1026     -22.224 -31.963 -69.198  1.00111.97           C  
ANISOU 1344  CE2 TYR A1026    18596  13327  10623  -4185  -3086  -1036       C  
ATOM   1345  CZ  TYR A1026     -20.876 -31.671 -69.189  1.00108.31           C  
ANISOU 1345  CZ  TYR A1026    18280  12675  10199  -3708  -2910  -1236       C  
ATOM   1346  OH  TYR A1026     -20.030 -32.318 -70.060  1.00113.95           O  
ANISOU 1346  OH  TYR A1026    19411  13078  10806  -3452  -2879  -1463       O  
ATOM   1347  N   ALA A1027     -25.636 -29.880 -63.824  1.00127.36           N  
ANISOU 1347  N   ALA A1027    18562  16772  13057  -5081  -3043     59       N  
ATOM   1348  CA  ALA A1027     -26.544 -29.113 -62.974  1.00124.63           C  
ANISOU 1348  CA  ALA A1027    17629  16955  12771  -5190  -3002    308       C  
ATOM   1349  C   ALA A1027     -26.044 -29.024 -61.537  1.00114.79           C  
ANISOU 1349  C   ALA A1027    16295  15616  11703  -4998  -2825    348       C  
ATOM   1350  O   ALA A1027     -26.270 -28.026 -60.853  1.00106.23           O  
ANISOU 1350  O   ALA A1027    14730  14884  10747  -4766  -2645    469       O  
ATOM   1351  CB  ALA A1027     -27.944 -29.711 -63.011  1.00131.40           C  
ANISOU 1351  CB  ALA A1027    18318  18075  13532  -5649  -3131    559       C  
ATOM   1352  N   ALA A1028     -25.364 -30.072 -61.086  1.00119.61           N  
ANISOU 1352  N   ALA A1028    17387  15744  12317  -5071  -2874    246       N  
ATOM   1353  CA  ALA A1028     -24.876 -30.134 -59.713  1.00127.39           C  
ANISOU 1353  CA  ALA A1028    18334  16615  13455  -4918  -2725    294       C  
ATOM   1354  C   ALA A1028     -23.733 -29.153 -59.469  1.00129.47           C  
ANISOU 1354  C   ALA A1028    18478  16809  13907  -4305  -2443    157       C  
ATOM   1355  O   ALA A1028     -23.481 -28.757 -58.332  1.00129.43           O  
ANISOU 1355  O   ALA A1028    18257  16879  14040  -4121  -2279    225       O  
ATOM   1356  CB  ALA A1028     -24.445 -31.552 -59.367  1.00130.53           C  
ANISOU 1356  CB  ALA A1028    19313  16490  13791  -5154  -2875    231       C  
ATOM   1357  N   ASP A1029     -23.050 -28.761 -60.540  1.00132.70           N  
ANISOU 1357  N   ASP A1029    19025  17091  14305  -4011  -2393    -29       N  
ATOM   1358  CA  ASP A1029     -21.903 -27.865 -60.434  1.00136.13           C  
ANISOU 1358  CA  ASP A1029    19377  17452  14895  -3469  -2146   -157       C  
ATOM   1359  C   ASP A1029     -22.303 -26.468 -59.961  1.00138.09           C  
ANISOU 1359  C   ASP A1029    19058  18139  15271  -3260  -1973    -23       C  
ATOM   1360  O   ASP A1029     -21.519 -25.777 -59.310  1.00139.86           O  
ANISOU 1360  O   ASP A1029    19164  18330  15647  -2899  -1772    -64       O  
ATOM   1361  CB  ASP A1029     -21.167 -27.776 -61.774  1.00136.62           C  
ANISOU 1361  CB  ASP A1029    19697  17333  14880  -3248  -2146   -362       C  
ATOM   1362  CG  ASP A1029     -19.897 -26.947 -61.690  1.00131.85           C  
ANISOU 1362  CG  ASP A1029    19035  16648  14415  -2729  -1905   -483       C  
ATOM   1363  OD1 ASP A1029     -19.255 -26.945 -60.619  1.00132.53           O  
ANISOU 1363  OD1 ASP A1029    19111  16613  14633  -2551  -1778   -480       O  
ATOM   1364  OD2 ASP A1029     -19.542 -26.298 -62.697  1.00126.70           O  
ANISOU 1364  OD2 ASP A1029    18344  16068  13728  -2519  -1850   -568       O  
ATOM   1365  N   GLU A1030     -23.526 -26.061 -60.285  1.00137.26           N  
ANISOU 1365  N   GLU A1030    18615  18445  15092  -3482  -2061    137       N  
ATOM   1366  CA  GLU A1030     -24.006 -24.729 -59.929  1.00134.70           C  
ANISOU 1366  CA  GLU A1030    17773  18542  14867  -3257  -1912    262       C  
ATOM   1367  C   GLU A1030     -24.435 -24.649 -58.464  1.00129.01           C  
ANISOU 1367  C   GLU A1030    16782  18013  14222  -3305  -1828    412       C  
ATOM   1368  O   GLU A1030     -24.437 -23.574 -57.863  1.00124.32           O  
ANISOU 1368  O   GLU A1030    15856  17640  13742  -3004  -1651    457       O  
ATOM   1369  CB  GLU A1030     -25.158 -24.314 -60.850  1.00141.23           C  
ANISOU 1369  CB  GLU A1030    18321  19770  15571  -3435  -2037    387       C  
ATOM   1370  CG  GLU A1030     -25.609 -22.873 -60.676  1.00146.90           C  
ANISOU 1370  CG  GLU A1030    18545  20892  16377  -3130  -1890    499       C  
ATOM   1371  CD  GLU A1030     -24.464 -21.886 -60.806  1.00151.74           C  
ANISOU 1371  CD  GLU A1030    19207  21309  17137  -2641  -1692    355       C  
ATOM   1372  OE1 GLU A1030     -23.661 -22.021 -61.754  1.00153.98           O  
ANISOU 1372  OE1 GLU A1030    19787  21328  17390  -2548  -1710    202       O  
ATOM   1373  OE2 GLU A1030     -24.364 -20.977 -59.956  1.00153.04           O  
ANISOU 1373  OE2 GLU A1030    19120  21595  17434  -2359  -1521    397       O  
ATOM   1374  N   VAL A1031     -24.789 -25.796 -57.893  1.00127.97           N  
ANISOU 1374  N   VAL A1031    16821  17788  14016  -3687  -1959    487       N  
ATOM   1375  CA  VAL A1031     -25.242 -25.857 -56.507  1.00125.67           C  
ANISOU 1375  CA  VAL A1031    16289  17698  13761  -3788  -1895    647       C  
ATOM   1376  C   VAL A1031     -24.113 -25.521 -55.534  1.00124.19           C  
ANISOU 1376  C   VAL A1031    16175  17276  13737  -3411  -1688    543       C  
ATOM   1377  O   VAL A1031     -24.331 -24.846 -54.528  1.00123.55           O  
ANISOU 1377  O   VAL A1031    15766  17452  13726  -3260  -1542    631       O  
ATOM   1378  CB  VAL A1031     -25.817 -27.249 -56.168  1.00125.21           C  
ANISOU 1378  CB  VAL A1031    16451  17553  13569  -4330  -2106    767       C  
ATOM   1379  CG1 VAL A1031     -26.358 -27.277 -54.744  1.00120.80           C  
ANISOU 1379  CG1 VAL A1031    15600  17274  13025  -4454  -2036    961       C  
ATOM   1380  CG2 VAL A1031     -26.906 -27.626 -57.160  1.00128.54           C  
ANISOU 1380  CG2 VAL A1031    16822  18206  13810  -4751  -2336    870       C  
ATOM   1381  N   TRP A1032     -22.907 -25.984 -55.847  1.00124.38           N  
ANISOU 1381  N   TRP A1032    16625  16830  13805  -3250  -1678    354       N  
ATOM   1382  CA  TRP A1032     -21.752 -25.776 -54.978  1.00121.41           C  
ANISOU 1382  CA  TRP A1032    16342  16223  13566  -2918  -1505    258       C  
ATOM   1383  C   TRP A1032     -21.352 -24.306 -54.854  1.00117.09           C  
ANISOU 1383  C   TRP A1032    15487  15856  13146  -2489  -1295    211       C  
ATOM   1384  O   TRP A1032     -20.682 -23.920 -53.895  1.00119.03           O  
ANISOU 1384  O   TRP A1032    15681  16047  13497  -2257  -1146    182       O  
ATOM   1385  CB  TRP A1032     -20.560 -26.612 -55.453  1.00122.71           C  
ANISOU 1385  CB  TRP A1032    17013  15886  13726  -2819  -1548     72       C  
ATOM   1386  CG  TRP A1032     -20.777 -28.088 -55.311  1.00131.28           C  
ANISOU 1386  CG  TRP A1032    18480  16698  14702  -3193  -1745    107       C  
ATOM   1387  CD1 TRP A1032     -21.359 -28.921 -56.220  1.00135.67           C  
ANISOU 1387  CD1 TRP A1032    19290  17151  15106  -3538  -1964    104       C  
ATOM   1388  CD2 TRP A1032     -20.416 -28.906 -54.191  1.00136.00           C  
ANISOU 1388  CD2 TRP A1032    19277  17071  15324  -3273  -1757    157       C  
ATOM   1389  NE1 TRP A1032     -21.384 -30.207 -55.738  1.00138.91           N  
ANISOU 1389  NE1 TRP A1032    20071  17259  15448  -3836  -2117    146       N  
ATOM   1390  CE2 TRP A1032     -20.811 -30.225 -54.494  1.00137.91           C  
ANISOU 1390  CE2 TRP A1032    19915  17055  15430  -3673  -1992    187       C  
ATOM   1391  CE3 TRP A1032     -19.798 -28.653 -52.963  1.00134.02           C  
ANISOU 1391  CE3 TRP A1032    18926  16809  15186  -3056  -1603    184       C  
ATOM   1392  CZ2 TRP A1032     -20.608 -31.286 -53.614  1.00136.84           C  
ANISOU 1392  CZ2 TRP A1032    20083  16634  15276  -3851  -2076    254       C  
ATOM   1393  CZ3 TRP A1032     -19.597 -29.708 -52.090  1.00131.29           C  
ANISOU 1393  CZ3 TRP A1032    18853  16214  14818  -3227  -1680    252       C  
ATOM   1394  CH2 TRP A1032     -20.000 -31.008 -52.420  1.00133.41           C  
ANISOU 1394  CH2 TRP A1032    19521  16212  14958  -3616  -1915    292       C  
ATOM   1395  N   VAL A1033     -21.763 -23.492 -55.821  1.00112.49           N  
ANISOU 1395  N   VAL A1033    14719  15478  12545  -2399  -1296    208       N  
ATOM   1396  CA  VAL A1033     -21.476 -22.061 -55.791  1.00110.79           C  
ANISOU 1396  CA  VAL A1033    14242  15414  12438  -2016  -1123    179       C  
ATOM   1397  C   VAL A1033     -22.151 -21.384 -54.600  1.00119.64           C  
ANISOU 1397  C   VAL A1033    14992  16863  13603  -1951  -1015    307       C  
ATOM   1398  O   VAL A1033     -21.484 -20.819 -53.730  1.00125.54           O  
ANISOU 1398  O   VAL A1033    15701  17546  14455  -1696   -862    256       O  
ATOM   1399  CB  VAL A1033     -21.930 -21.371 -57.088  1.00107.49           C  
ANISOU 1399  CB  VAL A1033    13703  15168  11972  -1962  -1172    185       C  
ATOM   1400  CG1 VAL A1033     -21.692 -19.872 -57.001  1.00104.06           C  
ANISOU 1400  CG1 VAL A1033    13025  14866  11646  -1579  -1008    176       C  
ATOM   1401  CG2 VAL A1033     -21.203 -21.965 -58.284  1.00109.04           C  
ANISOU 1401  CG2 VAL A1033    14266  15062  12103  -1989  -1260     41       C  
ATOM   1402  N   VAL A1034     -23.479 -21.444 -54.567  1.00120.42           N  
ANISOU 1402  N   VAL A1034    14813  17336  13604  -2183  -1097    474       N  
ATOM   1403  CA  VAL A1034     -24.241 -20.910 -53.446  1.00116.22           C  
ANISOU 1403  CA  VAL A1034    13911  17172  13074  -2131   -998    606       C  
ATOM   1404  C   VAL A1034     -23.928 -21.719 -52.189  1.00108.44           C  
ANISOU 1404  C   VAL A1034    13042  16065  12094  -2275   -971    631       C  
ATOM   1405  O   VAL A1034     -23.894 -21.183 -51.076  1.00109.85           O  
ANISOU 1405  O   VAL A1034    13038  16383  12316  -2096   -827    652       O  
ATOM   1406  CB  VAL A1034     -25.755 -20.953 -53.730  1.00121.06           C  
ANISOU 1406  CB  VAL A1034    14183  18263  13550  -2384  -1106    804       C  
ATOM   1407  CG1 VAL A1034     -26.532 -20.295 -52.601  1.00126.05           C  
ANISOU 1407  CG1 VAL A1034    14400  19327  14166  -2258   -978    933       C  
ATOM   1408  CG2 VAL A1034     -26.064 -20.273 -55.055  1.00120.64           C  
ANISOU 1408  CG2 VAL A1034    14042  18319  13475  -2269  -1162    793       C  
ATOM   1409  N   GLY A1035     -23.681 -23.012 -52.388  1.00100.40           N  
ANISOU 1409  N   GLY A1035    12357  14769  11020  -2590  -1118    623       N  
ATOM   1410  CA  GLY A1035     -23.356 -23.921 -51.305  1.00 98.81           C  
ANISOU 1410  CA  GLY A1035    12329  14402  10814  -2757  -1127    661       C  
ATOM   1411  C   GLY A1035     -22.130 -23.499 -50.517  1.00 91.82           C  
ANISOU 1411  C   GLY A1035    11550  13279  10057  -2405   -958    531       C  
ATOM   1412  O   GLY A1035     -22.074 -23.685 -49.301  1.00 92.82           O  
ANISOU 1412  O   GLY A1035    11621  13458  10187  -2430   -893    595       O  
ATOM   1413  N   MET A1036     -21.147 -22.930 -51.209  1.00 86.34           N  
ANISOU 1413  N   MET A1036    11001  12349   9455  -2097   -892    361       N  
ATOM   1414  CA  MET A1036     -19.944 -22.433 -50.553  1.00 83.27           C  
ANISOU 1414  CA  MET A1036    10691  11767   9182  -1772   -741    243       C  
ATOM   1415  C   MET A1036     -20.107 -20.958 -50.196  1.00 92.18           C  
ANISOU 1415  C   MET A1036    11496  13153  10374  -1472   -582    233       C  
ATOM   1416  O   MET A1036     -19.429 -20.445 -49.304  1.00 99.63           O  
ANISOU 1416  O   MET A1036    12418  14048  11387  -1259   -455    179       O  
ATOM   1417  CB  MET A1036     -18.712 -22.639 -51.440  1.00 69.69           C  
ANISOU 1417  CB  MET A1036     9298   9672   7508  -1608   -753     77       C  
ATOM   1418  CG  MET A1036     -18.611 -21.685 -52.619  1.00 66.39           C  
ANISOU 1418  CG  MET A1036     8803   9305   7116  -1414   -723      0       C  
ATOM   1419  SD  MET A1036     -17.080 -21.893 -53.546  1.00120.44           S  
ANISOU 1419  SD  MET A1036    15994  15778  13992  -1202   -708   -183       S  
ATOM   1420  CE  MET A1036     -17.242 -20.577 -54.750  1.00100.82           C  
ANISOU 1420  CE  MET A1036    13327  13456  11522  -1020   -667   -211       C  
ATOM   1421  N   GLY A1037     -21.014 -20.285 -50.899  1.00 88.66           N  
ANISOU 1421  N   GLY A1037    10817  12973   9895  -1455   -601    287       N  
ATOM   1422  CA  GLY A1037     -21.313 -18.891 -50.628  1.00 83.41           C  
ANISOU 1422  CA  GLY A1037     9870  12546   9276  -1159   -469    287       C  
ATOM   1423  C   GLY A1037     -21.884 -18.708 -49.235  1.00 84.38           C  
ANISOU 1423  C   GLY A1037     9756  12941   9363  -1147   -377    372       C  
ATOM   1424  O   GLY A1037     -21.466 -17.817 -48.487  1.00 81.72           O  
ANISOU 1424  O   GLY A1037     9356  12610   9086   -869   -238    303       O  
ATOM   1425  N   ILE A1038     -22.840 -19.560 -48.879  1.00 83.76           N  
ANISOU 1425  N   ILE A1038     9554  13098   9172  -1465   -459    526       N  
ATOM   1426  CA  ILE A1038     -23.424 -19.511 -47.544  1.00 81.00           C  
ANISOU 1426  CA  ILE A1038     8967  13054   8757  -1488   -372    628       C  
ATOM   1427  C   ILE A1038     -22.379 -19.848 -46.482  1.00 80.39           C  
ANISOU 1427  C   ILE A1038     9099  12715   8730  -1440   -301    553       C  
ATOM   1428  O   ILE A1038     -22.438 -19.339 -45.362  1.00 88.15           O  
ANISOU 1428  O   ILE A1038     9927  13872   9694  -1289   -174    557       O  
ATOM   1429  CB  ILE A1038     -24.651 -20.442 -47.408  1.00 79.11           C  
ANISOU 1429  CB  ILE A1038     8547  13146   8365  -1900   -490    840       C  
ATOM   1430  CG1 ILE A1038     -24.278 -21.887 -47.741  1.00 77.86           C  
ANISOU 1430  CG1 ILE A1038     8740  12658   8183  -2284   -663    863       C  
ATOM   1431  CG2 ILE A1038     -25.784 -19.964 -48.305  1.00 76.98           C  
ANISOU 1431  CG2 ILE A1038     7984  13240   8025  -1918   -546    937       C  
ATOM   1432  CD1 ILE A1038     -25.433 -22.855 -47.626  1.00 78.11           C  
ANISOU 1432  CD1 ILE A1038     8644  12977   8059  -2757   -808   1084       C  
ATOM   1433  N   VAL A1039     -21.418 -20.693 -46.844  1.00 72.45           N  
ANISOU 1433  N   VAL A1039     8448  11304   7776  -1547   -384    482       N  
ATOM   1434  CA  VAL A1039     -20.322 -21.034 -45.945  1.00 74.32           C  
ANISOU 1434  CA  VAL A1039     8895  11280   8062  -1477   -331    415       C  
ATOM   1435  C   VAL A1039     -19.456 -19.808 -45.682  1.00 84.01           C  
ANISOU 1435  C   VAL A1039    10101  12430   9390  -1091   -182    265       C  
ATOM   1436  O   VAL A1039     -19.096 -19.526 -44.538  1.00 92.87           O  
ANISOU 1436  O   VAL A1039    11181  13591  10512   -981    -84    246       O  
ATOM   1437  CB  VAL A1039     -19.448 -22.173 -46.511  1.00 65.18           C  
ANISOU 1437  CB  VAL A1039     8130   9703   6931  -1615   -453    364       C  
ATOM   1438  CG1 VAL A1039     -18.213 -22.381 -45.646  1.00 49.70           C  
ANISOU 1438  CG1 VAL A1039     6361   7494   5028  -1472   -389    291       C  
ATOM   1439  CG2 VAL A1039     -20.252 -23.459 -46.613  1.00 67.59           C  
ANISOU 1439  CG2 VAL A1039     8526  10029   7127  -2035   -620    513       C  
ATOM   1440  N   MET A1040     -19.131 -19.077 -46.746  1.00 82.18           N  
ANISOU 1440  N   MET A1040     9906  12091   9229   -907   -177    167       N  
ATOM   1441  CA  MET A1040     -18.383 -17.830 -46.619  1.00 80.91           C  
ANISOU 1441  CA  MET A1040     9733  11856   9153   -578    -57     41       C  
ATOM   1442  C   MET A1040     -19.143 -16.836 -45.748  1.00 81.46           C  
ANISOU 1442  C   MET A1040     9532  12234   9184   -414     55     66       C  
ATOM   1443  O   MET A1040     -18.550 -16.138 -44.921  1.00 85.45           O  
ANISOU 1443  O   MET A1040    10054  12694   9720   -219    156    -18       O  
ATOM   1444  CB  MET A1040     -18.117 -17.217 -47.995  1.00 79.33           C  
ANISOU 1444  CB  MET A1040     9595  11537   9012   -453    -86    -28       C  
ATOM   1445  CG  MET A1040     -17.243 -18.068 -48.897  1.00 79.36           C  
ANISOU 1445  CG  MET A1040     9874  11242   9036   -547   -173    -83       C  
ATOM   1446  SD  MET A1040     -17.072 -17.349 -50.540  1.00 83.30           S  
ANISOU 1446  SD  MET A1040    10412  11672   9568   -423   -205   -142       S  
ATOM   1447  CE  MET A1040     -16.079 -18.599 -51.352  1.00134.41           C  
ANISOU 1447  CE  MET A1040    17218  17831  16020   -535   -295   -212       C  
ATOM   1448  N   SER A1041     -20.459 -16.781 -45.941  1.00 78.37           N  
ANISOU 1448  N   SER A1041     8893  12171   8712   -489     32    180       N  
ATOM   1449  CA  SER A1041     -21.318 -15.929 -45.126  1.00 78.76           C  
ANISOU 1449  CA  SER A1041     8662  12571   8694   -310    141    215       C  
ATOM   1450  C   SER A1041     -21.187 -16.290 -43.650  1.00 79.08           C  
ANISOU 1450  C   SER A1041     8676  12703   8669   -361    216    234       C  
ATOM   1451  O   SER A1041     -21.018 -15.415 -42.796  1.00 82.45           O  
ANISOU 1451  O   SER A1041     9050  13193   9084   -113    337    152       O  
ATOM   1452  CB  SER A1041     -22.775 -16.065 -45.567  1.00 81.85           C  
ANISOU 1452  CB  SER A1041     8760  13359   8981   -429     90    371       C  
ATOM   1453  OG  SER A1041     -22.904 -15.871 -46.963  1.00 85.35           O  
ANISOU 1453  OG  SER A1041     9237  13723   9468   -424     -1    369       O  
ATOM   1454  N   LEU A1042     -21.260 -17.585 -43.359  1.00 72.84           N  
ANISOU 1454  N   LEU A1042     7946  11905   7824   -690    133    343       N  
ATOM   1455  CA  LEU A1042     -21.114 -18.073 -41.993  1.00 64.29           C  
ANISOU 1455  CA  LEU A1042     6857  10903   6669   -782    185    389       C  
ATOM   1456  C   LEU A1042     -19.749 -17.708 -41.422  1.00 66.61           C  
ANISOU 1456  C   LEU A1042     7373  10890   7046   -591    250    236       C  
ATOM   1457  O   LEU A1042     -19.630 -17.390 -40.240  1.00 76.10           O  
ANISOU 1457  O   LEU A1042     8514  12213   8189   -494    347    214       O  
ATOM   1458  CB  LEU A1042     -21.317 -19.588 -41.934  1.00 58.87           C  
ANISOU 1458  CB  LEU A1042     6269  10177   5921  -1191     53    543       C  
ATOM   1459  CG  LEU A1042     -22.711 -20.105 -42.287  1.00 61.65           C  
ANISOU 1459  CG  LEU A1042     6387  10881   6154  -1477    -31    733       C  
ATOM   1460  CD1 LEU A1042     -22.796 -21.606 -42.061  1.00 53.88           C  
ANISOU 1460  CD1 LEU A1042     5566   9802   5103  -1909   -173    884       C  
ATOM   1461  CD2 LEU A1042     -23.778 -19.371 -41.489  1.00 64.82           C  
ANISOU 1461  CD2 LEU A1042     6391  11808   6430  -1353     97    812       C  
ATOM   1462  N   ILE A1043     -18.724 -17.756 -42.267  1.00 58.34           N  
ANISOU 1462  N   ILE A1043     6571   9478   6118   -543    195    137       N  
ATOM   1463  CA  ILE A1043     -17.378 -17.391 -41.846  1.00 55.04           C  
ANISOU 1463  CA  ILE A1043     6341   8798   5773   -377    244      6       C  
ATOM   1464  C   ILE A1043     -17.316 -15.920 -41.445  1.00 60.45           C  
ANISOU 1464  C   ILE A1043     6933   9566   6470    -79    362   -110       C  
ATOM   1465  O   ILE A1043     -16.823 -15.587 -40.365  1.00 69.52           O  
ANISOU 1465  O   ILE A1043     8106  10723   7587     11    434   -168       O  
ATOM   1466  CB  ILE A1043     -16.334 -17.678 -42.943  1.00 46.11           C  
ANISOU 1466  CB  ILE A1043     5451   7318   4748   -369    168    -66       C  
ATOM   1467  CG1 ILE A1043     -16.242 -19.179 -43.209  1.00 42.99           C  
ANISOU 1467  CG1 ILE A1043     5225   6778   4331   -628     48     21       C  
ATOM   1468  CG2 ILE A1043     -14.972 -17.143 -42.537  1.00 39.38           C  
ANISOU 1468  CG2 ILE A1043     4735   6266   3959   -191    224   -186       C  
ATOM   1469  CD1 ILE A1043     -15.263 -19.547 -44.299  1.00 40.47           C  
ANISOU 1469  CD1 ILE A1043     5147   6144   4087   -591    -19    -58       C  
ATOM   1470  N   VAL A1044     -17.826 -15.046 -42.311  1.00 55.81           N  
ANISOU 1470  N   VAL A1044     6260   9031   5916     71    372   -142       N  
ATOM   1471  CA  VAL A1044     -17.859 -13.614 -42.022  1.00 57.20           C  
ANISOU 1471  CA  VAL A1044     6388   9248   6096    369    467   -251       C  
ATOM   1472  C   VAL A1044     -18.616 -13.330 -40.728  1.00 61.98           C  
ANISOU 1472  C   VAL A1044     6812  10166   6571    456    569   -236       C  
ATOM   1473  O   VAL A1044     -18.127 -12.604 -39.857  1.00 66.42           O  
ANISOU 1473  O   VAL A1044     7445  10682   7110    624    646   -348       O  
ATOM   1474  CB  VAL A1044     -18.513 -12.814 -43.165  1.00 61.21           C  
ANISOU 1474  CB  VAL A1044     6815   9800   6642    516    450   -249       C  
ATOM   1475  CG1 VAL A1044     -18.614 -11.340 -42.793  1.00 43.64           C  
ANISOU 1475  CG1 VAL A1044     4580   7592   4410    843    540   -357       C  
ATOM   1476  CG2 VAL A1044     -17.728 -12.991 -44.452  1.00 59.85           C  
ANISOU 1476  CG2 VAL A1044     6824   9340   6578    448    360   -272       C  
ATOM   1477  N   LEU A1045     -19.805 -13.915 -40.609  1.00 64.97           N  
ANISOU 1477  N   LEU A1045     6958  10880   6849    327    565    -94       N  
ATOM   1478  CA  LEU A1045     -20.633 -13.750 -39.418  1.00 72.06           C  
ANISOU 1478  CA  LEU A1045     7636  12152   7591    396    669    -53       C  
ATOM   1479  C   LEU A1045     -19.896 -14.181 -38.152  1.00 73.42           C  
ANISOU 1479  C   LEU A1045     7918  12269   7710    311    707    -81       C  
ATOM   1480  O   LEU A1045     -19.879 -13.454 -37.158  1.00 73.47           O  
ANISOU 1480  O   LEU A1045     7896  12388   7629    512    814   -173       O  
ATOM   1481  CB  LEU A1045     -21.938 -14.537 -39.559  1.00 76.73           C  
ANISOU 1481  CB  LEU A1045     7947  13134   8072    180    635    147       C  
ATOM   1482  CG  LEU A1045     -23.167 -13.805 -40.108  1.00 86.32           C  
ANISOU 1482  CG  LEU A1045     8883  14686   9229    370    670    197       C  
ATOM   1483  CD1 LEU A1045     -22.876 -13.130 -41.440  1.00 86.92           C  
ANISOU 1483  CD1 LEU A1045     9085  14495   9446    521    608    119       C  
ATOM   1484  CD2 LEU A1045     -24.334 -14.772 -40.244  1.00 92.97           C  
ANISOU 1484  CD2 LEU A1045     9447  15924   9953     64    608    423       C  
ATOM   1485  N   ALA A1046     -19.281 -15.359 -38.203  1.00 71.68           N  
ANISOU 1485  N   ALA A1046     7840  11865   7530     29    613     -5       N  
ATOM   1486  CA  ALA A1046     -18.549 -15.899 -37.061  1.00 70.88           C  
ANISOU 1486  CA  ALA A1046     7849  11704   7379    -70    628     -1       C  
ATOM   1487  C   ALA A1046     -17.380 -15.005 -36.654  1.00 74.37           C  
ANISOU 1487  C   ALA A1046     8474  11908   7875    148    676   -185       C  
ATOM   1488  O   ALA A1046     -17.232 -14.665 -35.479  1.00 80.02           O  
ANISOU 1488  O   ALA A1046     9174  12741   8488    230    754   -237       O  
ATOM   1489  CB  ALA A1046     -18.060 -17.309 -37.362  1.00 66.44           C  
ANISOU 1489  CB  ALA A1046     7448  10934   6864   -373    500    113       C  
ATOM   1490  N   ILE A1047     -16.557 -14.630 -37.630  1.00 68.28           N  
ANISOU 1490  N   ILE A1047     7874  10821   7249    222    623   -276       N  
ATOM   1491  CA  ILE A1047     -15.396 -13.779 -37.377  1.00 63.25           C  
ANISOU 1491  CA  ILE A1047     7412   9955   6664    379    646   -431       C  
ATOM   1492  C   ILE A1047     -15.792 -12.430 -36.779  1.00 69.46           C  
ANISOU 1492  C   ILE A1047     8152  10863   7377    639    747   -558       C  
ATOM   1493  O   ILE A1047     -15.297 -12.040 -35.712  1.00 73.26           O  
ANISOU 1493  O   ILE A1047     8703  11351   7781    702    794   -644       O  
ATOM   1494  CB  ILE A1047     -14.582 -13.540 -38.663  1.00 53.11           C  
ANISOU 1494  CB  ILE A1047     6281   8368   5531    404    575   -482       C  
ATOM   1495  CG1 ILE A1047     -13.941 -14.844 -39.139  1.00 53.71           C  
ANISOU 1495  CG1 ILE A1047     6461   8283   5662    200    482   -395       C  
ATOM   1496  CG2 ILE A1047     -13.513 -12.494 -38.426  1.00 47.62           C  
ANISOU 1496  CG2 ILE A1047     5738   7485   4872    546    595   -625       C  
ATOM   1497  CD1 ILE A1047     -13.110 -14.691 -40.396  1.00 47.74           C  
ANISOU 1497  CD1 ILE A1047     5841   7273   5026    233    424   -443       C  
ATOM   1498  N   VAL A1048     -16.688 -11.727 -37.469  1.00 63.86           N  
ANISOU 1498  N   VAL A1048     7338  10246   6678    800    773   -570       N  
ATOM   1499  CA  VAL A1048     -17.165 -10.426 -37.008  1.00 59.79           C  
ANISOU 1499  CA  VAL A1048     6803   9826   6088   1099    864   -694       C  
ATOM   1500  C   VAL A1048     -17.767 -10.505 -35.609  1.00 62.47           C  
ANISOU 1500  C   VAL A1048     7005  10491   6239   1150    967   -695       C  
ATOM   1501  O   VAL A1048     -17.350  -9.775 -34.710  1.00 63.25           O  
ANISOU 1501  O   VAL A1048     7224  10546   6261   1297   1022   -837       O  
ATOM   1502  CB  VAL A1048     -18.203  -9.822 -37.972  1.00 60.58           C  
ANISOU 1502  CB  VAL A1048     6773  10033   6213   1278    873   -667       C  
ATOM   1503  CG1 VAL A1048     -18.820  -8.570 -37.370  1.00 48.92           C  
ANISOU 1503  CG1 VAL A1048     5273   8684   4629   1630    975   -789       C  
ATOM   1504  CG2 VAL A1048     -17.561  -9.510 -39.313  1.00 67.14           C  
ANISOU 1504  CG2 VAL A1048     7763  10538   7209   1264    781   -686       C  
ATOM   1505  N   PHE A1049     -18.737 -11.398 -35.429  1.00 63.40           N  
ANISOU 1505  N   PHE A1049     6877  10944   6268   1008    985   -533       N  
ATOM   1506  CA  PHE A1049     -19.405 -11.554 -34.138  1.00 69.27           C  
ANISOU 1506  CA  PHE A1049     7448  12065   6808   1035   1089   -500       C  
ATOM   1507  C   PHE A1049     -18.411 -11.845 -33.019  1.00 66.32           C  
ANISOU 1507  C   PHE A1049     7235  11587   6378    930   1092   -553       C  
ATOM   1508  O   PHE A1049     -18.414 -11.174 -31.984  1.00 75.00           O  
ANISOU 1508  O   PHE A1049     8357  12804   7336   1109   1185   -673       O  
ATOM   1509  CB  PHE A1049     -20.459 -12.661 -34.206  1.00 77.80           C  
ANISOU 1509  CB  PHE A1049     8248  13505   7809    796   1076   -271       C  
ATOM   1510  CG  PHE A1049     -21.118 -12.955 -32.889  1.00 82.16           C  
ANISOU 1510  CG  PHE A1049     8599  14484   8135    768   1179   -199       C  
ATOM   1511  CD1 PHE A1049     -22.143 -12.151 -32.418  1.00 85.94           C  
ANISOU 1511  CD1 PHE A1049     8854  15353   8446   1059   1315   -239       C  
ATOM   1512  CD2 PHE A1049     -20.720 -14.043 -32.127  1.00 79.43           C  
ANISOU 1512  CD2 PHE A1049     8287  14163   7731    467   1141    -81       C  
ATOM   1513  CE1 PHE A1049     -22.753 -12.421 -31.208  1.00 89.49           C  
ANISOU 1513  CE1 PHE A1049     9099  16242   8663   1041   1422   -168       C  
ATOM   1514  CE2 PHE A1049     -21.326 -14.318 -30.916  1.00 83.55           C  
ANISOU 1514  CE2 PHE A1049     8617  15099   8027    424   1236      3       C  
ATOM   1515  CZ  PHE A1049     -22.344 -13.506 -30.456  1.00 90.25           C  
ANISOU 1515  CZ  PHE A1049     9225  16366   8699    705   1382    -42       C  
ATOM   1516  N   GLY A1050     -17.558 -12.840 -33.241  1.00 58.78           N  
ANISOU 1516  N   GLY A1050     6400  10412   5523    657    988   -468       N  
ATOM   1517  CA  GLY A1050     -16.577 -13.248 -32.251  1.00 59.66           C  
ANISOU 1517  CA  GLY A1050     6649  10434   5586    542    971   -484       C  
ATOM   1518  C   GLY A1050     -15.619 -12.144 -31.844  1.00 55.98           C  
ANISOU 1518  C   GLY A1050     6389   9755   5125    727    990   -693       C  
ATOM   1519  O   GLY A1050     -15.457 -11.853 -30.655  1.00 52.74           O  
ANISOU 1519  O   GLY A1050     6005   9469   4563    783   1049   -766       O  
ATOM   1520  N   ASN A1051     -14.985 -11.518 -32.831  1.00 56.04           N  
ANISOU 1520  N   ASN A1051     6552   9450   5293    804    932   -784       N  
ATOM   1521  CA  ASN A1051     -14.005 -10.479 -32.536  1.00 55.71           C  
ANISOU 1521  CA  ASN A1051     6728   9179   5260    921    922   -963       C  
ATOM   1522  C   ASN A1051     -14.613  -9.201 -31.958  1.00 60.44           C  
ANISOU 1522  C   ASN A1051     7358   9875   5731   1204   1017  -1131       C  
ATOM   1523  O   ASN A1051     -14.016  -8.568 -31.083  1.00 61.98           O  
ANISOU 1523  O   ASN A1051     7713  10005   5831   1262   1028  -1271       O  
ATOM   1524  CB  ASN A1051     -13.139 -10.184 -33.760  1.00 57.43           C  
ANISOU 1524  CB  ASN A1051     7097   9059   5667    893    830   -989       C  
ATOM   1525  CG  ASN A1051     -12.264 -11.362 -34.143  1.00 63.68           C  
ANISOU 1525  CG  ASN A1051     7909   9732   6553    662    741   -865       C  
ATOM   1526  OD1 ASN A1051     -11.214 -11.593 -33.542  1.00 55.87           O  
ANISOU 1526  OD1 ASN A1051     7016   8670   5544    569    703   -876       O  
ATOM   1527  ND2 ASN A1051     -12.698 -12.120 -35.144  1.00 72.89           N  
ANISOU 1527  ND2 ASN A1051     8996  10888   7811    578    704   -747       N  
ATOM   1528  N   VAL A1052     -15.798  -8.829 -32.438  1.00 60.30           N  
ANISOU 1528  N   VAL A1052     7196  10018   5698   1389   1079  -1118       N  
ATOM   1529  CA  VAL A1052     -16.524  -7.700 -31.864  1.00 59.21           C  
ANISOU 1529  CA  VAL A1052     7071  10012   5415   1714   1182  -1270       C  
ATOM   1530  C   VAL A1052     -16.850  -7.995 -30.404  1.00 65.28           C  
ANISOU 1530  C   VAL A1052     7741  11110   5954   1721   1278  -1283       C  
ATOM   1531  O   VAL A1052     -16.730  -7.123 -29.539  1.00 69.75           O  
ANISOU 1531  O   VAL A1052     8454  11671   6377   1915   1334  -1464       O  
ATOM   1532  CB  VAL A1052     -17.822  -7.388 -32.641  1.00 54.27           C  
ANISOU 1532  CB  VAL A1052     6249   9575   4798   1927   1234  -1216       C  
ATOM   1533  CG1 VAL A1052     -18.758  -6.526 -31.809  1.00 56.14           C  
ANISOU 1533  CG1 VAL A1052     6423  10081   4828   2283   1369  -1337       C  
ATOM   1534  CG2 VAL A1052     -17.500  -6.704 -33.958  1.00 51.67           C  
ANISOU 1534  CG2 VAL A1052     6076   8901   4657   2004   1150  -1252       C  
ATOM   1535  N   LEU A1053     -17.242  -9.238 -30.136  1.00 66.93           N  
ANISOU 1535  N   LEU A1053     7722  11593   6117   1493   1287  -1087       N  
ATOM   1536  CA  LEU A1053     -17.527  -9.674 -28.774  1.00 69.61           C  
ANISOU 1536  CA  LEU A1053     7946  12270   6230   1445   1370  -1055       C  
ATOM   1537  C   LEU A1053     -16.288  -9.555 -27.888  1.00 68.74           C  
ANISOU 1537  C   LEU A1053     8077  11968   6074   1355   1326  -1166       C  
ATOM   1538  O   LEU A1053     -16.369  -9.068 -26.759  1.00 67.75           O  
ANISOU 1538  O   LEU A1053     7994  12008   5741   1486   1406  -1288       O  
ATOM   1539  CB  LEU A1053     -18.045 -11.114 -28.769  1.00 67.99           C  
ANISOU 1539  CB  LEU A1053     7496  12330   6008   1147   1352   -792       C  
ATOM   1540  CG  LEU A1053     -18.621 -11.626 -27.448  1.00 72.39           C  
ANISOU 1540  CG  LEU A1053     7869  13325   6310   1082   1448   -704       C  
ATOM   1541  CD1 LEU A1053     -19.855 -10.828 -27.058  1.00 73.54           C  
ANISOU 1541  CD1 LEU A1053     7811  13872   6258   1403   1606   -775       C  
ATOM   1542  CD2 LEU A1053     -18.945 -13.108 -27.542  1.00 75.98           C  
ANISOU 1542  CD2 LEU A1053     8151  13943   6776    718   1386   -422       C  
ATOM   1543  N   VAL A1054     -15.143  -9.993 -28.406  1.00 65.81           N  
ANISOU 1543  N   VAL A1054     7855  11272   5878   1141   1198  -1123       N  
ATOM   1544  CA  VAL A1054     -13.885  -9.909 -27.662  1.00 62.91           C  
ANISOU 1544  CA  VAL A1054     7691  10737   5474   1036   1137  -1203       C  
ATOM   1545  C   VAL A1054     -13.493  -8.467 -27.343  1.00 59.17           C  
ANISOU 1545  C   VAL A1054     7457  10087   4936   1249   1148  -1458       C  
ATOM   1546  O   VAL A1054     -13.245  -8.125 -26.183  1.00 61.79           O  
ANISOU 1546  O   VAL A1054     7883  10517   5079   1283   1180  -1570       O  
ATOM   1547  CB  VAL A1054     -12.725 -10.582 -28.424  1.00 65.47           C  
ANISOU 1547  CB  VAL A1054     8108  10767   6001    810   1000  -1105       C  
ATOM   1548  CG1 VAL A1054     -11.398 -10.290 -27.737  1.00 48.40           C  
ANISOU 1548  CG1 VAL A1054     6140   8452   3798    729    930  -1196       C  
ATOM   1549  CG2 VAL A1054     -12.960 -12.080 -28.533  1.00 67.41           C  
ANISOU 1549  CG2 VAL A1054     8194  11141   6280    586    969   -868       C  
ATOM   1550  N   ILE A1055     -13.440  -7.631 -28.378  1.00 57.14           N  
ANISOU 1550  N   ILE A1055     7322   9560   4827   1378   1113  -1544       N  
ATOM   1551  CA  ILE A1055     -13.083  -6.222 -28.218  1.00 53.36           C  
ANISOU 1551  CA  ILE A1055     7123   8847   4304   1565   1099  -1777       C  
ATOM   1552  C   ILE A1055     -14.026  -5.507 -27.250  1.00 61.16           C  
ANISOU 1552  C   ILE A1055     8119  10067   5052   1860   1229  -1933       C  
ATOM   1553  O   ILE A1055     -13.588  -4.718 -26.410  1.00 65.26           O  
ANISOU 1553  O   ILE A1055     8876  10496   5424   1937   1224  -2125       O  
ATOM   1554  CB  ILE A1055     -13.077  -5.483 -29.572  1.00 52.31           C  
ANISOU 1554  CB  ILE A1055     7101   8411   4364   1667   1044  -1808       C  
ATOM   1555  CG1 ILE A1055     -12.056  -6.117 -30.516  1.00 54.21           C  
ANISOU 1555  CG1 ILE A1055     7348   8436   4814   1395    923  -1673       C  
ATOM   1556  CG2 ILE A1055     -12.768  -4.007 -29.383  1.00 54.12           C  
ANISOU 1556  CG2 ILE A1055     7662   8367   4536   1851   1016  -2039       C  
ATOM   1557  CD1 ILE A1055     -12.010  -5.475 -31.884  1.00 54.83           C  
ANISOU 1557  CD1 ILE A1055     7518   8244   5070   1462    867  -1677       C  
ATOM   1558  N   THR A1056     -15.318  -5.796 -27.365  1.00 57.48           N  
ANISOU 1558  N   THR A1056     7390   9920   4529   2023   1343  -1849       N  
ATOM   1559  CA  THR A1056     -16.305  -5.211 -26.467  1.00 64.23           C  
ANISOU 1559  CA  THR A1056     8194  11076   5134   2338   1488  -1976       C  
ATOM   1560  C   THR A1056     -16.049  -5.663 -25.033  1.00 72.50           C  
ANISOU 1560  C   THR A1056     9220  12370   5957   2218   1531  -1990       C  
ATOM   1561  O   THR A1056     -16.113  -4.862 -24.098  1.00 78.08           O  
ANISOU 1561  O   THR A1056    10092  13039   6537   2360   1558  -2142       O  
ATOM   1562  CB  THR A1056     -17.740  -5.596 -26.872  1.00 65.44           C  
ANISOU 1562  CB  THR A1056     7993  11602   5269   2483   1594  -1824       C  
ATOM   1563  OG1 THR A1056     -17.966  -5.232 -28.239  1.00 67.59           O  
ANISOU 1563  OG1 THR A1056     8274  11666   5742   2582   1544  -1796       O  
ATOM   1564  CG2 THR A1056     -18.754  -4.884 -25.988  1.00 70.60           C  
ANISOU 1564  CG2 THR A1056     8597  12450   5778   2757   1686  -1888       C  
ATOM   1565  N   ALA A1057     -15.748  -6.948 -24.869  1.00 71.81           N  
ANISOU 1565  N   ALA A1057     8951  12434   5899   1893   1495  -1777       N  
ATOM   1566  CA  ALA A1057     -15.489  -7.517 -23.550  1.00 71.92           C  
ANISOU 1566  CA  ALA A1057     8925  12702   5700   1747   1525  -1747       C  
ATOM   1567  C   ALA A1057     -14.289  -6.865 -22.872  1.00 74.71           C  
ANISOU 1567  C   ALA A1057     9605  12796   5986   1699   1442  -1939       C  
ATOM   1568  O   ALA A1057     -14.360  -6.483 -21.705  1.00 80.23           O  
ANISOU 1568  O   ALA A1057    10384  13624   6477   1772   1490  -2048       O  
ATOM   1569  CB  ALA A1057     -15.289  -9.022 -23.651  1.00 67.81           C  
ANISOU 1569  CB  ALA A1057     8202  12298   5266   1395   1466  -1461       C  
ATOM   1570  N   ILE A1058     -13.190  -6.737 -23.609  1.00 71.19           N  
ANISOU 1570  N   ILE A1058     9342  11951   5754   1536   1296  -1944       N  
ATOM   1571  CA  ILE A1058     -11.977  -6.129 -23.067  1.00 70.54           C  
ANISOU 1571  CA  ILE A1058     9556  11628   5619   1437   1191  -2099       C  
ATOM   1572  C   ILE A1058     -12.152  -4.633 -22.799  1.00 74.17           C  
ANISOU 1572  C   ILE A1058    10313  11919   5951   1716   1217  -2395       C  
ATOM   1573  O   ILE A1058     -11.679  -4.117 -21.785  1.00 77.68           O  
ANISOU 1573  O   ILE A1058    10967  12356   6192   1711   1196  -2563       O  
ATOM   1574  CB  ILE A1058     -10.771  -6.342 -24.005  1.00 72.89           C  
ANISOU 1574  CB  ILE A1058     9942  11583   6171   1193   1031  -2011       C  
ATOM   1575  CG1 ILE A1058     -10.546  -7.835 -24.251  1.00 79.63           C  
ANISOU 1575  CG1 ILE A1058    10553  12567   7137    952    997  -1738       C  
ATOM   1576  CG2 ILE A1058      -9.516  -5.706 -23.425  1.00 69.63           C  
ANISOU 1576  CG2 ILE A1058     9801  10972   5681   1055    912  -2150       C  
ATOM   1577  CD1 ILE A1058      -9.408  -8.130 -25.207  1.00 78.80           C  
ANISOU 1577  CD1 ILE A1058    10503  12175   7264    758    859  -1644       C  
ATOM   1578  N   ALA A1059     -12.840  -3.941 -23.702  1.00 74.32           N  
ANISOU 1578  N   ALA A1059    10368  11793   6078   1965   1254  -2457       N  
ATOM   1579  CA  ALA A1059     -13.003  -2.494 -23.586  1.00 74.41           C  
ANISOU 1579  CA  ALA A1059    10694  11524   6054   2204   1247  -2684       C  
ATOM   1580  C   ALA A1059     -13.964  -2.086 -22.471  1.00 79.12           C  
ANISOU 1580  C   ALA A1059    11255  12336   6471   2420   1370  -2754       C  
ATOM   1581  O   ALA A1059     -13.735  -1.092 -21.782  1.00 80.37           O  
ANISOU 1581  O   ALA A1059    11710  12303   6522   2500   1346  -2950       O  
ATOM   1582  CB  ALA A1059     -13.451  -1.899 -24.916  1.00 70.92           C  
ANISOU 1582  CB  ALA A1059    10293  10840   5812   2392   1233  -2684       C  
ATOM   1583  N   LYS A1060     -15.035  -2.853 -22.295  1.00 83.27           N  
ANISOU 1583  N   LYS A1060    11419  13267   6953   2499   1495  -2590       N  
ATOM   1584  CA  LYS A1060     -16.070  -2.507 -21.322  1.00 86.86           C  
ANISOU 1584  CA  LYS A1060    11788  13981   7234   2729   1618  -2634       C  
ATOM   1585  C   LYS A1060     -15.677  -2.852 -19.887  1.00 89.21           C  
ANISOU 1585  C   LYS A1060    12112  14478   7305   2579   1638  -2663       C  
ATOM   1586  O   LYS A1060     -15.812  -2.028 -18.985  1.00 89.34           O  
ANISOU 1586  O   LYS A1060    12324  14458   7164   2730   1672  -2839       O  
ATOM   1587  CB  LYS A1060     -17.394  -3.188 -21.680  1.00 86.41           C  
ANISOU 1587  CB  LYS A1060    11312  14320   7199   2846   1728  -2428       C  
ATOM   1588  N   PHE A1061     -15.195  -4.073 -19.684  1.00 92.82           N  
ANISOU 1588  N   PHE A1061    12382  15143   7741   2282   1612  -2486       N  
ATOM   1589  CA  PHE A1061     -14.849  -4.547 -18.347  1.00 96.93           C  
ANISOU 1589  CA  PHE A1061    12891  15891   8047   2120   1623  -2466       C  
ATOM   1590  C   PHE A1061     -13.466  -4.074 -17.904  1.00102.47           C  
ANISOU 1590  C   PHE A1061    13944  16301   8687   1946   1492  -2631       C  
ATOM   1591  O   PHE A1061     -12.536  -3.996 -18.707  1.00101.79           O  
ANISOU 1591  O   PHE A1061    14001  15932   8743   1808   1369  -2655       O  
ATOM   1592  CB  PHE A1061     -14.944  -6.072 -18.279  1.00 91.66           C  
ANISOU 1592  CB  PHE A1061    11881  15570   7375   1866   1636  -2180       C  
ATOM   1593  CG  PHE A1061     -16.335  -6.600 -18.492  1.00 92.48           C  
ANISOU 1593  CG  PHE A1061    11626  16026   7488   1975   1753  -2000       C  
ATOM   1594  CD1 PHE A1061     -16.808  -6.852 -19.770  1.00 88.24           C  
ANISOU 1594  CD1 PHE A1061    10929  15456   7143   2008   1753  -1891       C  
ATOM   1595  CD2 PHE A1061     -17.171  -6.837 -17.415  1.00 98.80           C  
ANISOU 1595  CD2 PHE A1061    12240  17209   8091   2030   1854  -1933       C  
ATOM   1596  CE1 PHE A1061     -18.089  -7.333 -19.968  1.00 90.82           C  
ANISOU 1596  CE1 PHE A1061    10915  16132   7462   2076   1842  -1714       C  
ATOM   1597  CE2 PHE A1061     -18.452  -7.318 -17.607  1.00101.23           C  
ANISOU 1597  CE2 PHE A1061    12198  17874   8392   2102   1945  -1753       C  
ATOM   1598  CZ  PHE A1061     -18.911  -7.567 -18.884  1.00 97.62           C  
ANISOU 1598  CZ  PHE A1061    11581  17385   8124   2116   1933  -1641       C  
ATOM   1599  N   GLU A1062     -13.341  -3.761 -16.617  1.00108.08           N  
ANISOU 1599  N   GLU A1062    14786  17108   9173   1945   1513  -2739       N  
ATOM   1600  CA  GLU A1062     -12.091  -3.247 -16.066  1.00109.82           C  
ANISOU 1600  CA  GLU A1062    15344  17088   9294   1766   1381  -2901       C  
ATOM   1601  C   GLU A1062     -11.200  -4.364 -15.532  1.00105.01           C  
ANISOU 1601  C   GLU A1062    14613  16678   8609   1437   1297  -2731       C  
ATOM   1602  O   GLU A1062     -10.010  -4.158 -15.293  1.00105.90           O  
ANISOU 1602  O   GLU A1062    14943  16622   8673   1230   1153  -2807       O  
ATOM   1603  CB  GLU A1062     -12.375  -2.228 -14.960  1.00114.46           C  
ANISOU 1603  CB  GLU A1062    16181  17646   9663   1932   1434  -3130       C  
ATOM   1604  N   ARG A1063     -11.780  -5.545 -15.344  1.00 97.95           N  
ANISOU 1604  N   ARG A1063    13367  16149   7702   1377   1376  -2487       N  
ATOM   1605  CA  ARG A1063     -11.033  -6.692 -14.841  1.00 88.19           C  
ANISOU 1605  CA  ARG A1063    11995  15110   6404   1076   1299  -2287       C  
ATOM   1606  C   ARG A1063     -10.300  -7.413 -15.970  1.00 79.62           C  
ANISOU 1606  C   ARG A1063    10822  13904   5528    885   1193  -2141       C  
ATOM   1607  O   ARG A1063      -9.525  -8.338 -15.729  1.00 73.87           O  
ANISOU 1607  O   ARG A1063    10007  13282   4779    634   1105  -1971       O  
ATOM   1608  CB  ARG A1063     -11.963  -7.662 -14.110  1.00 85.69           C  
ANISOU 1608  CB  ARG A1063    11366  15218   5973   1060   1414  -2071       C  
ATOM   1609  N   LEU A1064     -10.553  -6.985 -17.202  1.00 79.95           N  
ANISOU 1609  N   LEU A1064    10889  13724   5765   1016   1202  -2201       N  
ATOM   1610  CA  LEU A1064      -9.899  -7.570 -18.366  1.00 82.59           C  
ANISOU 1610  CA  LEU A1064    11157  13877   6349    850   1101  -2061       C  
ATOM   1611  C   LEU A1064      -8.838  -6.630 -18.930  1.00 91.18           C  
ANISOU 1611  C   LEU A1064    12529  14545   7569    794    956  -2218       C  
ATOM   1612  O   LEU A1064      -8.478  -6.719 -20.104  1.00 95.03           O  
ANISOU 1612  O   LEU A1064    13002  14777   8329    731    886  -2133       O  
ATOM   1613  CB  LEU A1064     -10.929  -7.910 -19.445  1.00 81.16           C  
ANISOU 1613  CB  LEU A1064    10768  13711   6358    976   1188  -1941       C  
ATOM   1614  CG  LEU A1064     -11.777  -9.161 -19.214  1.00 77.02           C  
ANISOU 1614  CG  LEU A1064     9922  13556   5786    898   1277  -1684       C  
ATOM   1615  CD1 LEU A1064     -12.883  -9.261 -20.250  1.00 73.66           C  
ANISOU 1615  CD1 LEU A1064     9313  13164   5510   1038   1360  -1608       C  
ATOM   1616  CD2 LEU A1064     -10.900 -10.400 -19.253  1.00 77.10           C  
ANISOU 1616  CD2 LEU A1064     9859  13523   5913    585   1153  -1433       C  
ATOM   1617  N   GLN A1065      -8.340  -5.732 -18.087  1.00 95.99           N  
ANISOU 1617  N   GLN A1065    13405  15098   7970    800    908  -2442       N  
ATOM   1618  CA  GLN A1065      -7.348  -4.752 -18.512  1.00 97.58           C  
ANISOU 1618  CA  GLN A1065    13905  14916   8256    707    757  -2594       C  
ATOM   1619  C   GLN A1065      -5.928  -5.214 -18.204  1.00 92.64           C  
ANISOU 1619  C   GLN A1065    13282  14277   7640    365    587  -2475       C  
ATOM   1620  O   GLN A1065      -5.212  -4.576 -17.433  1.00 95.46           O  
ANISOU 1620  O   GLN A1065    13866  14594   7812    248    488  -2626       O  
ATOM   1621  CB  GLN A1065      -7.618  -3.400 -17.848  1.00106.56           C  
ANISOU 1621  CB  GLN A1065    15386  15934   9168    896    777  -2915       C  
ATOM   1622  CG  GLN A1065      -8.986  -2.821 -18.163  1.00112.97           C  
ANISOU 1622  CG  GLN A1065    16195  16687  10041   1243    937  -2985       C  
ATOM   1623  CD  GLN A1065      -9.161  -2.511 -19.635  1.00115.75           C  
ANISOU 1623  CD  GLN A1065    16559  16778  10642   1352    917  -2979       C  
ATOM   1624  OE1 GLN A1065      -8.537  -1.593 -20.166  1.00117.64           O  
ANISOU 1624  OE1 GLN A1065    17095  16648  10956   1315    796  -3115       O  
ATOM   1625  NE2 GLN A1065     -10.010  -3.282 -20.306  1.00117.57           N  
ANISOU 1625  NE2 GLN A1065    16475  17199  10998   1464   1025  -2807       N  
ATOM   1626  N   THR A1066      -5.524  -6.326 -18.810  1.00 87.04           N  
ANISOU 1626  N   THR A1066    12326  13609   7136    214    548  -2205       N  
ATOM   1627  CA  THR A1066      -4.178  -6.851 -18.617  1.00 81.12           C  
ANISOU 1627  CA  THR A1066    11536  12877   6410    -67    392  -2061       C  
ATOM   1628  C   THR A1066      -3.383  -6.817 -19.920  1.00 78.96           C  
ANISOU 1628  C   THR A1066    11248  12334   6419   -173    289  -1968       C  
ATOM   1629  O   THR A1066      -3.959  -6.727 -21.005  1.00 79.00           O  
ANISOU 1629  O   THR A1066    11218  12175   6625    -43    349  -1956       O  
ATOM   1630  CB  THR A1066      -4.200  -8.288 -18.060  1.00 75.01           C  
ANISOU 1630  CB  THR A1066    10501  12409   5592   -150    417  -1806       C  
ATOM   1631  OG1 THR A1066      -4.758  -9.178 -19.034  1.00 72.75           O  
ANISOU 1631  OG1 THR A1066    10011  12093   5538    -88    481  -1615       O  
ATOM   1632  CG2 THR A1066      -5.031  -8.350 -16.788  1.00 75.98           C  
ANISOU 1632  CG2 THR A1066    10611  12841   5418    -58    529  -1874       C  
ATOM   1633  N   VAL A1067      -2.059  -6.888 -19.801  1.00 73.14           N  
ANISOU 1633  N   VAL A1067    10521  11587   5680   -409    134  -1895       N  
ATOM   1634  CA  VAL A1067      -1.164  -6.810 -20.952  1.00 69.39           C  
ANISOU 1634  CA  VAL A1067    10019  10914   5431   -528     31  -1802       C  
ATOM   1635  C   VAL A1067      -1.473  -7.887 -21.989  1.00 71.78           C  
ANISOU 1635  C   VAL A1067    10088  11209   5977   -440     96  -1592       C  
ATOM   1636  O   VAL A1067      -1.550  -7.606 -23.193  1.00 80.92           O  
ANISOU 1636  O   VAL A1067    11255  12157   7335   -391    103  -1590       O  
ATOM   1637  CB  VAL A1067       0.312  -6.923 -20.517  1.00 69.91           C  
ANISOU 1637  CB  VAL A1067    10057  11086   5419   -794   -138  -1710       C  
ATOM   1638  CG1 VAL A1067       1.230  -6.908 -21.731  1.00 72.70           C  
ANISOU 1638  CG1 VAL A1067    10334  11299   5989   -904   -227  -1590       C  
ATOM   1639  CG2 VAL A1067       0.669  -5.797 -19.557  1.00 65.64           C  
ANISOU 1639  CG2 VAL A1067     9783  10526   4630   -926   -230  -1928       C  
ATOM   1640  N   THR A1068      -1.654  -9.116 -21.515  1.00 69.63           N  
ANISOU 1640  N   THR A1068     9628  11157   5672   -430    135  -1415       N  
ATOM   1641  CA  THR A1068      -2.029 -10.221 -22.387  1.00 68.88           C  
ANISOU 1641  CA  THR A1068     9352  11044   5777   -355    187  -1222       C  
ATOM   1642  C   THR A1068      -3.298  -9.861 -23.148  1.00 69.28           C  
ANISOU 1642  C   THR A1068     9423  10968   5932   -178    309  -1311       C  
ATOM   1643  O   THR A1068      -3.380 -10.052 -24.359  1.00 73.10           O  
ANISOU 1643  O   THR A1068     9856  11292   6625   -135    315  -1249       O  
ATOM   1644  CB  THR A1068      -2.260 -11.522 -21.594  1.00 69.41           C  
ANISOU 1644  CB  THR A1068     9272  11347   5752   -372    212  -1033       C  
ATOM   1645  OG1 THR A1068      -1.114 -11.803 -20.781  1.00 70.63           O  
ANISOU 1645  OG1 THR A1068     9408  11646   5781   -516     95   -950       O  
ATOM   1646  CG2 THR A1068      -2.502 -12.686 -22.542  1.00 64.86           C  
ANISOU 1646  CG2 THR A1068     8562  10700   5380   -326    232   -834       C  
ATOM   1647  N   ASN A1069      -4.275  -9.313 -22.432  1.00 69.28           N  
ANISOU 1647  N   ASN A1069     9492  11062   5769    -63    405  -1459       N  
ATOM   1648  CA  ASN A1069      -5.519  -8.868 -23.048  1.00 69.05           C  
ANISOU 1648  CA  ASN A1069     9468  10962   5806    137    523  -1549       C  
ATOM   1649  C   ASN A1069      -5.325  -7.643 -23.938  1.00 73.70           C  
ANISOU 1649  C   ASN A1069    10242  11252   6508    197    485  -1710       C  
ATOM   1650  O   ASN A1069      -6.107  -7.409 -24.859  1.00 73.20           O  
ANISOU 1650  O   ASN A1069    10159  11077   6577    344    548  -1728       O  
ATOM   1651  CB  ASN A1069      -6.581  -8.589 -21.983  1.00 64.85           C  
ANISOU 1651  CB  ASN A1069     8944  10660   5037    278    645  -1663       C  
ATOM   1652  CG  ASN A1069      -6.950  -9.828 -21.193  1.00 67.54           C  
ANISOU 1652  CG  ASN A1069     9086  11311   5265    208    693  -1473       C  
ATOM   1653  OD1 ASN A1069      -6.752 -10.953 -21.653  1.00 63.33           O  
ANISOU 1653  OD1 ASN A1069     8411  10782   4869    102    656  -1252       O  
ATOM   1654  ND2 ASN A1069      -7.492  -9.629 -19.996  1.00 74.15           N  
ANISOU 1654  ND2 ASN A1069     9932  12404   5836    270    773  -1557       N  
ATOM   1655  N   TYR A1070      -4.286  -6.860 -23.658  1.00 76.04           N  
ANISOU 1655  N   TYR A1070    10722  11427   6743     65    370  -1814       N  
ATOM   1656  CA  TYR A1070      -3.940  -5.734 -24.518  1.00 80.18           C  
ANISOU 1656  CA  TYR A1070    11443  11647   7373     60    303  -1932       C  
ATOM   1657  C   TYR A1070      -3.446  -6.247 -25.866  1.00 84.83           C  
ANISOU 1657  C   TYR A1070    11898  12121   8214    -12    259  -1759       C  
ATOM   1658  O   TYR A1070      -3.652  -5.606 -26.896  1.00 92.03           O  
ANISOU 1658  O   TYR A1070    12892  12813   9262     54    257  -1802       O  
ATOM   1659  CB  TYR A1070      -2.882  -4.839 -23.866  1.00 86.98           C  
ANISOU 1659  CB  TYR A1070    12535  12422   8090   -129    167  -2059       C  
ATOM   1660  CG  TYR A1070      -3.445  -3.660 -23.102  1.00103.30           C  
ANISOU 1660  CG  TYR A1070    14896  14395   9957     -2    191  -2327       C  
ATOM   1661  CD1 TYR A1070      -3.690  -2.449 -23.738  1.00109.99           C  
ANISOU 1661  CD1 TYR A1070    16010  14923  10858     93    166  -2488       C  
ATOM   1662  CD2 TYR A1070      -3.722  -3.753 -21.743  1.00109.75           C  
ANISOU 1662  CD2 TYR A1070    15747  15438  10517     34    235  -2421       C  
ATOM   1663  CE1 TYR A1070      -4.201  -1.367 -23.043  1.00116.13           C  
ANISOU 1663  CE1 TYR A1070    17101  15581  11443    247    184  -2749       C  
ATOM   1664  CE2 TYR A1070      -4.233  -2.677 -21.040  1.00112.65           C  
ANISOU 1664  CE2 TYR A1070    16405  15718  10677    183    262  -2688       C  
ATOM   1665  CZ  TYR A1070      -4.471  -1.487 -21.695  1.00116.43           C  
ANISOU 1665  CZ  TYR A1070    17168  15852  11218    301    236  -2857       C  
ATOM   1666  OH  TYR A1070      -4.979  -0.413 -20.999  1.00119.64           O  
ANISOU 1666  OH  TYR A1070    17907  16142  11409    486    259  -3136       O  
ATOM   1667  N   PHE A1071      -2.795  -7.407 -25.857  1.00 78.87           N  
ANISOU 1667  N   PHE A1071    10946  11516   7505   -129    224  -1563       N  
ATOM   1668  CA  PHE A1071      -2.380  -8.042 -27.105  1.00 70.59           C  
ANISOU 1668  CA  PHE A1071     9762  10388   6670   -158    199  -1402       C  
ATOM   1669  C   PHE A1071      -3.572  -8.711 -27.788  1.00 70.67           C  
ANISOU 1669  C   PHE A1071     9654  10400   6799      7    310  -1336       C  
ATOM   1670  O   PHE A1071      -3.727  -8.640 -29.014  1.00 74.29           O  
ANISOU 1670  O   PHE A1071    10095  10708   7425     55    316  -1305       O  
ATOM   1671  CB  PHE A1071      -1.269  -9.061 -26.852  1.00 67.59           C  
ANISOU 1671  CB  PHE A1071     9234  10162   6284   -294    122  -1223       C  
ATOM   1672  CG  PHE A1071      -0.011  -8.461 -26.293  1.00 68.59           C  
ANISOU 1672  CG  PHE A1071     9431  10333   6298   -486     -4  -1253       C  
ATOM   1673  CD1 PHE A1071       0.308  -7.137 -26.537  1.00 68.10           C  
ANISOU 1673  CD1 PHE A1071     9560  10098   6219   -575    -68  -1397       C  
ATOM   1674  CD2 PHE A1071       0.851  -9.219 -25.518  1.00 68.15           C  
ANISOU 1674  CD2 PHE A1071     9257  10493   6142   -590    -72  -1125       C  
ATOM   1675  CE1 PHE A1071       1.463  -6.580 -26.023  1.00 69.06           C  
ANISOU 1675  CE1 PHE A1071     9748  10271   6220   -800   -202  -1414       C  
ATOM   1676  CE2 PHE A1071       2.007  -8.667 -25.000  1.00 64.31           C  
ANISOU 1676  CE2 PHE A1071     8811  10087   5536   -787   -200  -1139       C  
ATOM   1677  CZ  PHE A1071       2.313  -7.346 -25.253  1.00 65.15           C  
ANISOU 1677  CZ  PHE A1071     9102  10031   5621   -911   -267  -1284       C  
ATOM   1678  N   ILE A1072      -4.412  -9.358 -26.981  1.00 68.63           N  
ANISOU 1678  N   ILE A1072     9310  10331   6434     70    389  -1304       N  
ATOM   1679  CA  ILE A1072      -5.633  -9.987 -27.472  1.00 64.23           C  
ANISOU 1679  CA  ILE A1072     8628   9825   5950    187    486  -1232       C  
ATOM   1680  C   ILE A1072      -6.497  -8.970 -28.207  1.00 66.67           C  
ANISOU 1680  C   ILE A1072     9013   9998   6321    350    545  -1366       C  
ATOM   1681  O   ILE A1072      -7.122  -9.289 -29.214  1.00 68.11           O  
ANISOU 1681  O   ILE A1072     9108  10129   6640    414    577  -1296       O  
ATOM   1682  CB  ILE A1072      -6.452 -10.620 -26.325  1.00 66.06           C  
ANISOU 1682  CB  ILE A1072     8764  10325   6009    206    564  -1187       C  
ATOM   1683  CG1 ILE A1072      -5.640 -11.708 -25.625  1.00 63.48           C  
ANISOU 1683  CG1 ILE A1072     8373  10123   5625     53    497  -1025       C  
ATOM   1684  CG2 ILE A1072      -7.754 -11.209 -26.846  1.00 69.26           C  
ANISOU 1684  CG2 ILE A1072     9026  10815   6474    289    654  -1099       C  
ATOM   1685  CD1 ILE A1072      -5.103 -12.758 -26.562  1.00 59.07           C  
ANISOU 1685  CD1 ILE A1072     7743   9456   5247     -8    434   -846       C  
ATOM   1686  N   THR A1073      -6.516  -7.741 -27.699  1.00 66.68           N  
ANISOU 1686  N   THR A1073     9195   9931   6211    421    547  -1558       N  
ATOM   1687  CA  THR A1073      -7.256  -6.656 -28.330  1.00 65.77           C  
ANISOU 1687  CA  THR A1073     9198   9653   6139    608    589  -1694       C  
ATOM   1688  C   THR A1073      -6.743  -6.412 -29.744  1.00 68.46           C  
ANISOU 1688  C   THR A1073     9575   9748   6688    556    517  -1641       C  
ATOM   1689  O   THR A1073      -7.526  -6.246 -30.678  1.00 68.98           O  
ANISOU 1689  O   THR A1073     9603   9744   6862    690    561  -1627       O  
ATOM   1690  CB  THR A1073      -7.140  -5.352 -27.521  1.00 62.51           C  
ANISOU 1690  CB  THR A1073     9048   9143   5561    679    573  -1921       C  
ATOM   1691  OG1 THR A1073      -7.582  -5.578 -26.177  1.00 63.03           O  
ANISOU 1691  OG1 THR A1073     9080   9465   5404    732    645  -1978       O  
ATOM   1692  CG2 THR A1073      -7.984  -4.254 -28.153  1.00 61.95           C  
ANISOU 1692  CG2 THR A1073     9122   8887   5527    921    616  -2056       C  
ATOM   1693  N   SER A1074      -5.422  -6.401 -29.890  1.00 70.82           N  
ANISOU 1693  N   SER A1074     9928   9953   7026    358    407  -1599       N  
ATOM   1694  CA  SER A1074      -4.782  -6.190 -31.184  1.00 66.97           C  
ANISOU 1694  CA  SER A1074     9460   9277   6708    283    339  -1534       C  
ATOM   1695  C   SER A1074      -5.119  -7.317 -32.155  1.00 62.44           C  
ANISOU 1695  C   SER A1074     8683   8761   6281    311    377  -1371       C  
ATOM   1696  O   SER A1074      -5.485  -7.070 -33.310  1.00 63.46           O  
ANISOU 1696  O   SER A1074     8813   8764   6536    379    385  -1352       O  
ATOM   1697  CB  SER A1074      -3.266  -6.081 -31.010  1.00 64.88           C  
ANISOU 1697  CB  SER A1074     9240   8994   6420     53    220  -1496       C  
ATOM   1698  OG  SER A1074      -2.613  -5.934 -32.258  1.00 64.80           O  
ANISOU 1698  OG  SER A1074     9214   8855   6552    -27    163  -1413       O  
ATOM   1699  N   LEU A1075      -4.992  -8.553 -31.679  1.00 57.34           N  
ANISOU 1699  N   LEU A1075     7886   8294   5608    254    389  -1253       N  
ATOM   1700  CA  LEU A1075      -5.330  -9.723 -32.483  1.00 57.90           C  
ANISOU 1700  CA  LEU A1075     7807   8399   5793    268    412  -1105       C  
ATOM   1701  C   LEU A1075      -6.784  -9.679 -32.954  1.00 66.30           C  
ANISOU 1701  C   LEU A1075     8818   9481   6893    407    494  -1120       C  
ATOM   1702  O   LEU A1075      -7.084  -9.927 -34.127  1.00 68.91           O  
ANISOU 1702  O   LEU A1075     9103   9731   7348    434    492  -1061       O  
ATOM   1703  CB  LEU A1075      -5.082 -11.001 -31.681  1.00 54.12           C  
ANISOU 1703  CB  LEU A1075     7227   8089   5249    193    405   -983       C  
ATOM   1704  CG  LEU A1075      -5.537 -12.307 -32.333  1.00 54.02           C  
ANISOU 1704  CG  LEU A1075     7109   8091   5325    194    416   -835       C  
ATOM   1705  CD1 LEU A1075      -4.765 -12.563 -33.618  1.00 51.27           C  
ANISOU 1705  CD1 LEU A1075     6767   7598   5117    185    363   -780       C  
ATOM   1706  CD2 LEU A1075      -5.383 -13.468 -31.363  1.00 56.61           C  
ANISOU 1706  CD2 LEU A1075     7384   8562   5563    121    401   -715       C  
ATOM   1707  N   ALA A1076      -7.680  -9.350 -32.029  1.00 66.60           N  
ANISOU 1707  N   ALA A1076     8850   9653   6802    501    565  -1197       N  
ATOM   1708  CA  ALA A1076      -9.104  -9.269 -32.317  1.00 66.25           C  
ANISOU 1708  CA  ALA A1076     8715   9702   6756    649    650  -1202       C  
ATOM   1709  C   ALA A1076      -9.412  -8.125 -33.275  1.00 72.17           C  
ANISOU 1709  C   ALA A1076     9564  10267   7590    790    649  -1296       C  
ATOM   1710  O   ALA A1076     -10.381  -8.185 -34.027  1.00 80.66           O  
ANISOU 1710  O   ALA A1076    10542  11380   8724    892    687  -1254       O  
ATOM   1711  CB  ALA A1076      -9.897  -9.113 -31.027  1.00 63.36           C  
ANISOU 1711  CB  ALA A1076     8307   9567   6199    738    737  -1266       C  
ATOM   1712  N   CYS A1077      -8.588  -7.082 -33.241  1.00 67.04           N  
ANISOU 1712  N   CYS A1077     9113   9422   6937    781    592  -1409       N  
ATOM   1713  CA  CYS A1077      -8.743  -5.965 -34.166  1.00 64.93           C  
ANISOU 1713  CA  CYS A1077     8984   8935   6751    891    568  -1481       C  
ATOM   1714  C   CYS A1077      -8.352  -6.385 -35.576  1.00 67.35           C  
ANISOU 1714  C   CYS A1077     9229   9135   7226    801    516  -1357       C  
ATOM   1715  O   CYS A1077      -9.082  -6.127 -36.538  1.00 77.19           O  
ANISOU 1715  O   CYS A1077    10448  10330   8551    914    532  -1334       O  
ATOM   1716  CB  CYS A1077      -7.903  -4.766 -33.721  1.00 60.08           C  
ANISOU 1716  CB  CYS A1077     8634   8119   6075    853    499  -1622       C  
ATOM   1717  SG  CYS A1077      -8.594  -3.849 -32.328  1.00 78.68           S  
ANISOU 1717  SG  CYS A1077    11154  10521   8220   1051    562  -1830       S  
ATOM   1718  N   ALA A1078      -7.197  -7.036 -35.690  1.00 55.61           N  
ANISOU 1718  N   ALA A1078     7714   7638   5777    612    455  -1275       N  
ATOM   1719  CA  ALA A1078      -6.731  -7.541 -36.976  1.00 51.07           C  
ANISOU 1719  CA  ALA A1078     7077   6994   5333    538    414  -1163       C  
ATOM   1720  C   ALA A1078      -7.753  -8.498 -37.581  1.00 56.50           C  
ANISOU 1720  C   ALA A1078     7609   7784   6074    599    461  -1073       C  
ATOM   1721  O   ALA A1078      -8.078  -8.407 -38.766  1.00 64.52           O  
ANISOU 1721  O   ALA A1078     8609   8726   7180    637    450  -1034       O  
ATOM   1722  CB  ALA A1078      -5.384  -8.227 -36.823  1.00 49.84           C  
ANISOU 1722  CB  ALA A1078     6887   6874   5176    373    357  -1088       C  
ATOM   1723  N   ASP A1079      -8.267  -9.407 -36.758  1.00 58.71           N  
ANISOU 1723  N   ASP A1079     7782   8241   6285    585    502  -1031       N  
ATOM   1724  CA  ASP A1079      -9.273 -10.359 -37.218  1.00 65.32           C  
ANISOU 1724  CA  ASP A1079     8480   9189   7150    591    530   -933       C  
ATOM   1725  C   ASP A1079     -10.605  -9.677 -37.534  1.00 66.51           C  
ANISOU 1725  C   ASP A1079     8576   9405   7291    748    583   -970       C  
ATOM   1726  O   ASP A1079     -11.364 -10.144 -38.382  1.00 69.45           O  
ANISOU 1726  O   ASP A1079     8848   9827   7714    749    581   -891       O  
ATOM   1727  CB  ASP A1079      -9.477 -11.468 -36.187  1.00 80.90           C  
ANISOU 1727  CB  ASP A1079    10366  11338   9033    503    549   -858       C  
ATOM   1728  CG  ASP A1079      -8.215 -12.269 -35.937  1.00 98.82           C  
ANISOU 1728  CG  ASP A1079    12680  13554  11313    382    489   -797       C  
ATOM   1729  OD1 ASP A1079      -7.384 -12.374 -36.864  1.00101.66           O  
ANISOU 1729  OD1 ASP A1079    13086  13776  11763    358    438   -775       O  
ATOM   1730  OD2 ASP A1079      -8.056 -12.794 -34.815  1.00107.48           O  
ANISOU 1730  OD2 ASP A1079    13757  14767  12313    324    495   -764       O  
ATOM   1731  N   LEU A1080     -10.887  -8.573 -36.849  1.00 67.00           N  
ANISOU 1731  N   LEU A1080     8710   9471   7275    890    626  -1091       N  
ATOM   1732  CA  LEU A1080     -12.108  -7.819 -37.106  1.00 65.49           C  
ANISOU 1732  CA  LEU A1080     8474   9347   7061   1100    681  -1134       C  
ATOM   1733  C   LEU A1080     -12.054  -7.169 -38.483  1.00 70.17           C  
ANISOU 1733  C   LEU A1080     9141   9743   7777   1157    630  -1126       C  
ATOM   1734  O   LEU A1080     -12.984  -7.304 -39.278  1.00 74.48           O  
ANISOU 1734  O   LEU A1080     9566  10375   8360   1230    640  -1058       O  
ATOM   1735  CB  LEU A1080     -12.337  -6.756 -36.030  1.00 64.62           C  
ANISOU 1735  CB  LEU A1080     8474   9255   6822   1278    736  -1288       C  
ATOM   1736  CG  LEU A1080     -13.561  -5.864 -36.243  1.00 70.66           C  
ANISOU 1736  CG  LEU A1080     9213  10087   7547   1565    799  -1346       C  
ATOM   1737  CD1 LEU A1080     -14.817  -6.709 -36.386  1.00 71.60           C  
ANISOU 1737  CD1 LEU A1080     9039  10532   7632   1593    861  -1218       C  
ATOM   1738  CD2 LEU A1080     -13.706  -4.868 -35.104  1.00 76.31           C  
ANISOU 1738  CD2 LEU A1080    10080  10803   8112   1766    855  -1522       C  
ATOM   1739  N   VAL A1081     -10.959  -6.466 -38.762  1.00 68.61           N  
ANISOU 1739  N   VAL A1081     9135   9303   7629   1104    567  -1181       N  
ATOM   1740  CA  VAL A1081     -10.771  -5.849 -40.071  1.00 63.64           C  
ANISOU 1740  CA  VAL A1081     8590   8486   7106   1125    511  -1155       C  
ATOM   1741  C   VAL A1081     -10.651  -6.933 -41.144  1.00 63.85           C  
ANISOU 1741  C   VAL A1081     8486   8557   7218    993    481  -1023       C  
ATOM   1742  O   VAL A1081     -10.959  -6.703 -42.314  1.00 67.84           O  
ANISOU 1742  O   VAL A1081     8983   9003   7791   1032    453   -973       O  
ATOM   1743  CB  VAL A1081      -9.538  -4.920 -40.094  1.00 61.24           C  
ANISOU 1743  CB  VAL A1081     8512   7937   6818   1039    441  -1217       C  
ATOM   1744  CG1 VAL A1081      -9.474  -4.144 -41.401  1.00 59.23           C  
ANISOU 1744  CG1 VAL A1081     8357   7496   6652   1068    385  -1179       C  
ATOM   1745  CG2 VAL A1081      -9.580  -3.958 -38.919  1.00 66.39           C  
ANISOU 1745  CG2 VAL A1081     9337   8525   7362   1139    456  -1366       C  
ATOM   1746  N   MET A1082     -10.213  -8.120 -40.734  1.00 64.21           N  
ANISOU 1746  N   MET A1082     8448   8701   7248    847    481   -969       N  
ATOM   1747  CA  MET A1082     -10.207  -9.282 -41.616  1.00 71.25           C  
ANISOU 1747  CA  MET A1082     9248   9630   8195    741    452   -861       C  
ATOM   1748  C   MET A1082     -11.625  -9.661 -42.031  1.00 75.45           C  
ANISOU 1748  C   MET A1082     9638  10312   8719    795    474   -802       C  
ATOM   1749  O   MET A1082     -11.920  -9.803 -43.218  1.00 79.49           O  
ANISOU 1749  O   MET A1082    10122  10794   9285    786    437   -747       O  
ATOM   1750  CB  MET A1082      -9.541 -10.472 -40.927  1.00 75.54           C  
ANISOU 1750  CB  MET A1082     9764  10231   8706    606    444   -817       C  
ATOM   1751  CG  MET A1082      -8.047 -10.570 -41.149  1.00 83.69           C  
ANISOU 1751  CG  MET A1082    10878  11150   9768    524    399   -813       C  
ATOM   1752  SD  MET A1082      -7.670 -11.341 -42.728  1.00111.22           S  
ANISOU 1752  SD  MET A1082    14361  14567  13331    482    355   -735       S  
ATOM   1753  CE  MET A1082      -8.524 -12.900 -42.517  1.00 44.19           C  
ANISOU 1753  CE  MET A1082     5804   6172   4815    423    351   -660       C  
ATOM   1754  N   GLY A1083     -12.500  -9.818 -41.042  1.00 68.92           N  
ANISOU 1754  N   GLY A1083     8705   9676   7806    841    530   -805       N  
ATOM   1755  CA  GLY A1083     -13.867 -10.238 -41.291  1.00 61.15           C  
ANISOU 1755  CA  GLY A1083     7542   8904   6787    862    549   -725       C  
ATOM   1756  C   GLY A1083     -14.764  -9.168 -41.887  1.00 59.22           C  
ANISOU 1756  C   GLY A1083     7253   8699   6550   1069    568   -747       C  
ATOM   1757  O   GLY A1083     -15.813  -9.479 -42.450  1.00 58.02           O  
ANISOU 1757  O   GLY A1083     6940   8722   6384   1076    562   -660       O  
ATOM   1758  N   LEU A1084     -14.360  -7.908 -41.766  1.00 58.75           N  
ANISOU 1758  N   LEU A1084     7345   8473   6502   1233    581   -855       N  
ATOM   1759  CA  LEU A1084     -15.168  -6.802 -42.274  1.00 58.80           C  
ANISOU 1759  CA  LEU A1084     7353   8477   6511   1473    593   -878       C  
ATOM   1760  C   LEU A1084     -14.788  -6.387 -43.691  1.00 66.92           C  
ANISOU 1760  C   LEU A1084     8480   9303   7645   1457    515   -839       C  
ATOM   1761  O   LEU A1084     -15.656  -6.079 -44.507  1.00 78.63           O  
ANISOU 1761  O   LEU A1084     9876  10858   9140   1577    500   -779       O  
ATOM   1762  CB  LEU A1084     -15.075  -5.591 -41.343  1.00 43.67           C  
ANISOU 1762  CB  LEU A1084     5593   6467   4530   1685    640  -1022       C  
ATOM   1763  CG  LEU A1084     -15.797  -5.696 -40.001  1.00 63.92           C  
ANISOU 1763  CG  LEU A1084     8044   9291   6953   1801    737  -1073       C  
ATOM   1764  CD1 LEU A1084     -15.589  -4.428 -39.191  1.00 65.35           C  
ANISOU 1764  CD1 LEU A1084     8447   9322   7061   2022    770  -1244       C  
ATOM   1765  CD2 LEU A1084     -17.277  -5.961 -40.214  1.00 46.75           C  
ANISOU 1765  CD2 LEU A1084     5593   7452   4718   1935    789   -979       C  
ATOM   1766  N   ALA A1085     -13.492  -6.378 -43.983  1.00 65.56           N  
ANISOU 1766  N   ALA A1085     8469   8907   7533   1310    466   -859       N  
ATOM   1767  CA  ALA A1085     -13.014  -5.885 -45.269  1.00 66.56           C  
ANISOU 1767  CA  ALA A1085     8700   8852   7739   1287    398   -819       C  
ATOM   1768  C   ALA A1085     -12.517  -6.996 -46.192  1.00 63.57           C  
ANISOU 1768  C   ALA A1085     8261   8491   7402   1087    355   -733       C  
ATOM   1769  O   ALA A1085     -13.007  -7.149 -47.310  1.00 69.98           O  
ANISOU 1769  O   ALA A1085     9013   9340   8237   1088    319   -660       O  
ATOM   1770  CB  ALA A1085     -11.926  -4.837 -45.064  1.00 66.12           C  
ANISOU 1770  CB  ALA A1085     8879   8543   7701   1277    368   -893       C  
ATOM   1771  N   VAL A1086     -11.546  -7.768 -45.716  1.00 54.03           N  
ANISOU 1771  N   VAL A1086     7078   7262   6190    933    357   -747       N  
ATOM   1772  CA  VAL A1086     -10.887  -8.776 -46.542  1.00 59.13           C  
ANISOU 1772  CA  VAL A1086     7713   7892   6862    785    319   -689       C  
ATOM   1773  C   VAL A1086     -11.824  -9.890 -47.007  1.00 68.08           C  
ANISOU 1773  C   VAL A1086     8722   9167   7977    729    303   -621       C  
ATOM   1774  O   VAL A1086     -12.053 -10.066 -48.207  1.00 65.86           O  
ANISOU 1774  O   VAL A1086     8432   8880   7712    705    259   -572       O  
ATOM   1775  CB  VAL A1086      -9.701  -9.411 -45.794  1.00 56.24           C  
ANISOU 1775  CB  VAL A1086     7391   7497   6480    675    326   -712       C  
ATOM   1776  CG1 VAL A1086      -8.991 -10.421 -46.683  1.00 45.62           C  
ANISOU 1776  CG1 VAL A1086     6052   6132   5148    580    293   -663       C  
ATOM   1777  CG2 VAL A1086      -8.740  -8.333 -45.324  1.00 64.92           C  
ANISOU 1777  CG2 VAL A1086     8607   8480   7581    680    323   -769       C  
ATOM   1778  N   VAL A1087     -12.360 -10.638 -46.047  1.00 70.61           N  
ANISOU 1778  N   VAL A1087     8958   9620   8252    685    329   -611       N  
ATOM   1779  CA  VAL A1087     -13.187 -11.810 -46.337  1.00 61.53           C  
ANISOU 1779  CA  VAL A1087     7711   8599   7070    569    297   -534       C  
ATOM   1780  C   VAL A1087     -14.455 -11.546 -47.172  1.00 56.83           C  
ANISOU 1780  C   VAL A1087     6991   8140   6460    611    270   -473       C  
ATOM   1781  O   VAL A1087     -14.714 -12.278 -48.129  1.00 45.30           O  
ANISOU 1781  O   VAL A1087     5526   6692   4995    496    204   -418       O  
ATOM   1782  CB  VAL A1087     -13.540 -12.588 -45.046  1.00 60.08           C  
ANISOU 1782  CB  VAL A1087     7457   8548   6823    489    326   -512       C  
ATOM   1783  CG1 VAL A1087     -14.308 -13.851 -45.380  1.00 63.79           C  
ANISOU 1783  CG1 VAL A1087     7864   9120   7254    313    268   -415       C  
ATOM   1784  CG2 VAL A1087     -12.276 -12.923 -44.273  1.00 60.42           C  
ANISOU 1784  CG2 VAL A1087     7615   8470   6871    448    338   -554       C  
ATOM   1785  N   PRO A1088     -15.250 -10.513 -46.820  1.00 63.44           N  
ANISOU 1785  N   PRO A1088     7736   9087   7280    786    315   -484       N  
ATOM   1786  CA  PRO A1088     -16.449 -10.285 -47.638  1.00 66.68           C  
ANISOU 1786  CA  PRO A1088     8002   9663   7668    845    284   -407       C  
ATOM   1787  C   PRO A1088     -16.124  -9.911 -49.084  1.00 67.52           C  
ANISOU 1787  C   PRO A1088     8197   9632   7826    855    219   -389       C  
ATOM   1788  O   PRO A1088     -16.714 -10.474 -50.007  1.00 68.93           O  
ANISOU 1788  O   PRO A1088     8301   9908   7980    756    153   -313       O  
ATOM   1789  CB  PRO A1088     -17.136  -9.108 -46.934  1.00 60.09           C  
ANISOU 1789  CB  PRO A1088     7092   8936   6803   1101    355   -443       C  
ATOM   1790  CG  PRO A1088     -16.636  -9.155 -45.541  1.00 57.24           C  
ANISOU 1790  CG  PRO A1088     6783   8555   6412   1105    425   -522       C  
ATOM   1791  CD  PRO A1088     -15.214  -9.608 -45.656  1.00 60.54           C  
ANISOU 1791  CD  PRO A1088     7385   8729   6889    949    391   -563       C  
ATOM   1792  N   PHE A1089     -15.196  -8.977 -49.273  1.00 65.06           N  
ANISOU 1792  N   PHE A1089     8044   9107   7569    952    230   -448       N  
ATOM   1793  CA  PHE A1089     -14.812  -8.539 -50.612  1.00 62.68           C  
ANISOU 1793  CA  PHE A1089     7829   8684   7301    955    174   -417       C  
ATOM   1794  C   PHE A1089     -14.170  -9.668 -51.410  1.00 53.22           C  
ANISOU 1794  C   PHE A1089     6682   7443   6095    762    127   -401       C  
ATOM   1795  O   PHE A1089     -14.311  -9.735 -52.632  1.00 50.26           O  
ANISOU 1795  O   PHE A1089     6315   7076   5707    729     70   -352       O  
ATOM   1796  CB  PHE A1089     -13.876  -7.331 -50.538  1.00 67.43           C  
ANISOU 1796  CB  PHE A1089     8602   9068   7949   1051    188   -469       C  
ATOM   1797  CG  PHE A1089     -14.584  -6.032 -50.277  1.00 74.65           C  
ANISOU 1797  CG  PHE A1089     9532   9964   8867   1282    202   -477       C  
ATOM   1798  CD1 PHE A1089     -15.198  -5.792 -49.058  1.00 71.12           C  
ANISOU 1798  CD1 PHE A1089     9027   9611   8384   1418    265   -534       C  
ATOM   1799  CD2 PHE A1089     -14.633  -5.048 -51.251  1.00 81.67           C  
ANISOU 1799  CD2 PHE A1089    10510  10742   9781   1381    152   -426       C  
ATOM   1800  CE1 PHE A1089     -15.850  -4.599 -48.817  1.00 73.43           C  
ANISOU 1800  CE1 PHE A1089     9359   9877   8663   1679    282   -558       C  
ATOM   1801  CE2 PHE A1089     -15.282  -3.851 -51.016  1.00 84.26           C  
ANISOU 1801  CE2 PHE A1089    10890  11018  10106   1628    157   -435       C  
ATOM   1802  CZ  PHE A1089     -15.892  -3.626 -49.796  1.00 81.00           C  
ANISOU 1802  CZ  PHE A1089    10429  10691   9656   1794    224   -510       C  
ATOM   1803  N   GLY A1090     -13.467 -10.555 -50.713  1.00 50.78           N  
ANISOU 1803  N   GLY A1090     6422   7092   5782    654    149   -443       N  
ATOM   1804  CA  GLY A1090     -12.891 -11.726 -51.347  1.00 46.20           C  
ANISOU 1804  CA  GLY A1090     5915   6462   5179    511    107   -442       C  
ATOM   1805  C   GLY A1090     -13.976 -12.682 -51.802  1.00 51.32           C  
ANISOU 1805  C   GLY A1090     6489   7239   5773    391     43   -385       C  
ATOM   1806  O   GLY A1090     -13.904 -13.252 -52.893  1.00 57.70           O  
ANISOU 1806  O   GLY A1090     7362   8018   6545    310    -19   -374       O  
ATOM   1807  N   ALA A1091     -14.990 -12.851 -50.959  1.00 55.71           N  
ANISOU 1807  N   ALA A1091     6908   7957   6304    368     53   -346       N  
ATOM   1808  CA  ALA A1091     -16.121 -13.711 -51.280  1.00 62.10           C  
ANISOU 1808  CA  ALA A1091     7617   8932   7046    211    -19   -267       C  
ATOM   1809  C   ALA A1091     -16.854 -13.179 -52.503  1.00 64.25           C  
ANISOU 1809  C   ALA A1091     7810   9305   7297    248    -77   -211       C  
ATOM   1810  O   ALA A1091     -17.206 -13.936 -53.407  1.00 73.45           O  
ANISOU 1810  O   ALA A1091     9000  10501   8406     91   -168   -175       O  
ATOM   1811  CB  ALA A1091     -17.067 -13.807 -50.094  1.00 64.87           C  
ANISOU 1811  CB  ALA A1091     7791   9497   7359    190     18   -215       C  
ATOM   1812  N   ALA A1092     -17.074 -11.868 -52.524  1.00 58.43           N  
ANISOU 1812  N   ALA A1092     6999   8606   6596    458    -32   -205       N  
ATOM   1813  CA  ALA A1092     -17.724 -11.216 -53.653  1.00 59.65           C  
ANISOU 1813  CA  ALA A1092     7081   8850   6732    533    -86   -138       C  
ATOM   1814  C   ALA A1092     -16.887 -11.365 -54.918  1.00 67.88           C  
ANISOU 1814  C   ALA A1092     8291   9727   7773    470   -139   -160       C  
ATOM   1815  O   ALA A1092     -17.425 -11.562 -56.008  1.00 71.30           O  
ANISOU 1815  O   ALA A1092     8690  10252   8150    401   -221   -101       O  
ATOM   1816  CB  ALA A1092     -17.967  -9.746 -53.346  1.00 59.75           C  
ANISOU 1816  CB  ALA A1092     7044   8871   6786    804    -29   -135       C  
ATOM   1817  N   HIS A1093     -15.569 -11.275 -54.764  1.00 73.28           N  
ANISOU 1817  N   HIS A1093     9141  10200   8504    492    -90   -239       N  
ATOM   1818  CA  HIS A1093     -14.652 -11.417 -55.890  1.00 74.47           C  
ANISOU 1818  CA  HIS A1093     9434  10227   8633    451   -118   -261       C  
ATOM   1819  C   HIS A1093     -14.706 -12.820 -56.485  1.00 71.06           C  
ANISOU 1819  C   HIS A1093     9073   9806   8121    272   -186   -280       C  
ATOM   1820  O   HIS A1093     -14.682 -12.986 -57.705  1.00 77.52           O  
ANISOU 1820  O   HIS A1093     9948  10633   8875    227   -245   -269       O  
ATOM   1821  CB  HIS A1093     -13.221 -11.086 -55.462  1.00 82.64           C  
ANISOU 1821  CB  HIS A1093    10592  11091   9717    503    -47   -327       C  
ATOM   1822  CG  HIS A1093     -12.211 -11.246 -56.555  1.00 91.47           C  
ANISOU 1822  CG  HIS A1093    11826  12137  10793    473    -58   -342       C  
ATOM   1823  ND1 HIS A1093     -11.573 -12.442 -56.811  1.00 94.50           N  
ANISOU 1823  ND1 HIS A1093    12305  12480  11120    395    -64   -399       N  
ATOM   1824  CD2 HIS A1093     -11.727 -10.362 -57.459  1.00 95.19           C  
ANISOU 1824  CD2 HIS A1093    12334  12579  11254    521    -60   -301       C  
ATOM   1825  CE1 HIS A1093     -10.741 -12.286 -57.825  1.00 97.38           C  
ANISOU 1825  CE1 HIS A1093    12741  12826  11433    415    -58   -402       C  
ATOM   1826  NE2 HIS A1093     -10.815 -11.033 -58.236  1.00 98.24           N  
ANISOU 1826  NE2 HIS A1093    12807  12950  11569    471    -57   -333       N  
ATOM   1827  N   ILE A1094     -14.777 -13.827 -55.621  1.00 59.97           N  
ANISOU 1827  N   ILE A1094     7688   8389   6710    166   -186   -309       N  
ATOM   1828  CA  ILE A1094     -14.817 -15.215 -56.073  1.00 59.21           C  
ANISOU 1828  CA  ILE A1094     7716   8247   6533    -10   -266   -334       C  
ATOM   1829  C   ILE A1094     -16.164 -15.573 -56.698  1.00 67.37           C  
ANISOU 1829  C   ILE A1094     8656   9453   7488   -166   -376   -257       C  
ATOM   1830  O   ILE A1094     -16.221 -16.147 -57.786  1.00 68.14           O  
ANISOU 1830  O   ILE A1094     8865   9527   7499   -270   -462   -273       O  
ATOM   1831  CB  ILE A1094     -14.522 -16.192 -54.921  1.00 56.48           C  
ANISOU 1831  CB  ILE A1094     7444   7816   6199    -90   -249   -366       C  
ATOM   1832  CG1 ILE A1094     -13.120 -15.954 -54.365  1.00 55.77           C  
ANISOU 1832  CG1 ILE A1094     7442   7579   6167     51   -156   -437       C  
ATOM   1833  CG2 ILE A1094     -14.658 -17.631 -55.393  1.00 58.34           C  
ANISOU 1833  CG2 ILE A1094     7857   7964   6344   -278   -353   -388       C  
ATOM   1834  CD1 ILE A1094     -12.823 -16.750 -53.116  1.00 58.86           C  
ANISOU 1834  CD1 ILE A1094     7885   7906   6574      3   -135   -450       C  
ATOM   1835  N   LEU A1095     -17.244 -15.229 -56.004  1.00 73.26           N  
ANISOU 1835  N   LEU A1095     9189  10398   8246   -180   -373   -171       N  
ATOM   1836  CA  LEU A1095     -18.589 -15.572 -56.455  1.00 68.83           C  
ANISOU 1836  CA  LEU A1095     8483  10069   7599   -346   -480    -70       C  
ATOM   1837  C   LEU A1095     -18.962 -14.887 -57.769  1.00 65.46           C  
ANISOU 1837  C   LEU A1095     8001   9740   7131   -286   -537    -24       C  
ATOM   1838  O   LEU A1095     -19.495 -15.524 -58.677  1.00 67.80           O  
ANISOU 1838  O   LEU A1095     8324  10111   7324   -472   -658      7       O  
ATOM   1839  CB  LEU A1095     -19.621 -15.250 -55.369  1.00 61.34           C  
ANISOU 1839  CB  LEU A1095     7274   9372   6660   -330   -442     24       C  
ATOM   1840  CG  LEU A1095     -19.524 -16.092 -54.093  1.00 58.86           C  
ANISOU 1840  CG  LEU A1095     6987   9028   6348   -457   -412     17       C  
ATOM   1841  CD1 LEU A1095     -20.554 -15.656 -53.060  1.00 54.64           C  
ANISOU 1841  CD1 LEU A1095     6167   8796   5798   -412   -357    112       C  
ATOM   1842  CD2 LEU A1095     -19.675 -17.572 -54.415  1.00 64.71           C  
ANISOU 1842  CD2 LEU A1095     7888   9695   7003   -775   -541     30       C  
ATOM   1843  N   THR A1096     -18.673 -13.593 -57.870  1.00 64.97           N  
ANISOU 1843  N   THR A1096     7882   9665   7139    -41   -462    -17       N  
ATOM   1844  CA  THR A1096     -19.043 -12.822 -59.055  1.00 73.23           C  
ANISOU 1844  CA  THR A1096     8871  10806   8148     40   -516     50       C  
ATOM   1845  C   THR A1096     -18.025 -12.950 -60.187  1.00 73.12           C  
ANISOU 1845  C   THR A1096     9073  10614   8097     22   -536    -16       C  
ATOM   1846  O   THR A1096     -18.119 -12.248 -61.195  1.00 74.09           O  
ANISOU 1846  O   THR A1096     9178  10786   8185     95   -571     39       O  
ATOM   1847  CB  THR A1096     -19.249 -11.330 -58.721  1.00 75.93           C  
ANISOU 1847  CB  THR A1096     9089  11193   8570    318   -444    103       C  
ATOM   1848  OG1 THR A1096     -18.023 -10.770 -58.236  1.00 83.73           O  
ANISOU 1848  OG1 THR A1096    10232  11934   9649    447   -344     16       O  
ATOM   1849  CG2 THR A1096     -20.330 -11.165 -57.665  1.00 68.73           C  
ANISOU 1849  CG2 THR A1096     7943  10509   7664    380   -414    166       C  
ATOM   1850  N   LYS A1097     -17.046 -13.834 -60.002  1.00 74.18           N  
ANISOU 1850  N   LYS A1097     9403  10558   8226    -55   -509   -127       N  
ATOM   1851  CA  LYS A1097     -16.040 -14.150 -61.022  1.00 77.78           C  
ANISOU 1851  CA  LYS A1097    10061  10878   8615    -62   -515   -204       C  
ATOM   1852  C   LYS A1097     -15.091 -13.000 -61.390  1.00 76.39           C  
ANISOU 1852  C   LYS A1097     9907  10631   8485    121   -433   -197       C  
ATOM   1853  O   LYS A1097     -14.003 -13.239 -61.914  1.00 78.23           O  
ANISOU 1853  O   LYS A1097    10285  10764   8674    142   -398   -264       O  
ATOM   1854  CB  LYS A1097     -16.696 -14.715 -62.288  1.00 81.29           C  
ANISOU 1854  CB  LYS A1097    10546  11426   8914   -216   -646   -183       C  
ATOM   1855  CG  LYS A1097     -17.535 -15.964 -62.062  1.00 88.38           C  
ANISOU 1855  CG  LYS A1097    11473  12370   9739   -462   -755   -189       C  
ATOM   1856  CD  LYS A1097     -16.694 -17.120 -61.547  1.00 95.21           C  
ANISOU 1856  CD  LYS A1097    12576  13003  10597   -522   -734   -314       C  
ATOM   1857  CE  LYS A1097     -17.515 -18.398 -61.459  1.00106.12           C  
ANISOU 1857  CE  LYS A1097    14047  14387  11885   -806   -872   -311       C  
ATOM   1858  NZ  LYS A1097     -18.723 -18.232 -60.602  1.00113.55           N  
ANISOU 1858  NZ  LYS A1097    14730  15548  12866   -924   -902   -177       N  
ATOM   1859  N   THR A1098     -15.499 -11.763 -61.125  1.00 73.24           N  
ANISOU 1859  N   THR A1098     9373  10290   8164    253   -407   -110       N  
ATOM   1860  CA  THR A1098     -14.686 -10.600 -61.473  1.00 71.07           C  
ANISOU 1860  CA  THR A1098     9143   9931   7929    388   -354    -79       C  
ATOM   1861  C   THR A1098     -14.494  -9.652 -60.291  1.00 68.72           C  
ANISOU 1861  C   THR A1098     8807   9546   7756    524   -276    -74       C  
ATOM   1862  O   THR A1098     -14.729 -10.019 -59.140  1.00 64.33           O  
ANISOU 1862  O   THR A1098     8203   8987   7251    521   -239   -120       O  
ATOM   1863  CB  THR A1098     -15.301  -9.807 -62.644  1.00 75.89           C  
ANISOU 1863  CB  THR A1098     9700  10652   8483    429   -427     38       C  
ATOM   1864  OG1 THR A1098     -16.619  -9.369 -62.289  1.00 78.69           O  
ANISOU 1864  OG1 THR A1098     9883  11147   8867    497   -472    124       O  
ATOM   1865  CG2 THR A1098     -15.375 -10.666 -63.898  1.00 82.16           C  
ANISOU 1865  CG2 THR A1098    10559  11532   9128    291   -507     23       C  
ATOM   1866  N   TRP A1099     -14.061  -8.431 -60.592  1.00 67.22           N  
ANISOU 1866  N   TRP A1099     8659   9279   7602    629   -259    -17       N  
ATOM   1867  CA  TRP A1099     -13.856  -7.404 -59.575  1.00 63.25           C  
ANISOU 1867  CA  TRP A1099     8174   8659   7201    755   -204    -19       C  
ATOM   1868  C   TRP A1099     -14.480  -6.083 -60.019  1.00 69.38           C  
ANISOU 1868  C   TRP A1099     8943   9422   7996    904   -249     91       C  
ATOM   1869  O   TRP A1099     -14.131  -5.544 -61.069  1.00 72.77           O  
ANISOU 1869  O   TRP A1099     9442   9820   8385    891   -289    171       O  
ATOM   1870  CB  TRP A1099     -12.364  -7.216 -59.294  1.00 56.35           C  
ANISOU 1870  CB  TRP A1099     7426   7634   6353    711   -142    -69       C  
ATOM   1871  CG  TRP A1099     -12.066  -6.090 -58.350  1.00 57.01           C  
ANISOU 1871  CG  TRP A1099     7570   7571   6521    804   -108    -73       C  
ATOM   1872  CD1 TRP A1099     -11.756  -4.802 -58.681  1.00 59.39           C  
ANISOU 1872  CD1 TRP A1099     7975   7746   6843    855   -133      2       C  
ATOM   1873  CD2 TRP A1099     -12.052  -6.150 -56.919  1.00 57.70           C  
ANISOU 1873  CD2 TRP A1099     7647   7608   6666    844    -54   -158       C  
ATOM   1874  NE1 TRP A1099     -11.549  -4.058 -57.544  1.00 57.43           N  
ANISOU 1874  NE1 TRP A1099     7806   7352   6663    922   -105    -46       N  
ATOM   1875  CE2 TRP A1099     -11.725  -4.862 -56.450  1.00 56.47           C  
ANISOU 1875  CE2 TRP A1099     7605   7289   6561    924    -50   -148       C  
ATOM   1876  CE3 TRP A1099     -12.285  -7.168 -55.989  1.00 59.22           C  
ANISOU 1876  CE3 TRP A1099     7764   7874   6864    808    -16   -236       C  
ATOM   1877  CZ2 TRP A1099     -11.625  -4.566 -55.092  1.00 56.93           C  
ANISOU 1877  CZ2 TRP A1099     7701   7267   6663    979     -6   -231       C  
ATOM   1878  CZ3 TRP A1099     -12.184  -6.871 -54.641  1.00 58.87           C  
ANISOU 1878  CZ3 TRP A1099     7733   7770   6865    863     35   -300       C  
ATOM   1879  CH2 TRP A1099     -11.857  -5.581 -54.206  1.00 57.95           C  
ANISOU 1879  CH2 TRP A1099     7727   7502   6788    953     41   -306       C  
ATOM   1880  N   THR A1100     -15.399  -5.564 -59.211  1.00 70.94           N  
ANISOU 1880  N   THR A1100     9061   9651   8243   1061   -241    100       N  
ATOM   1881  CA  THR A1100     -16.150  -4.367 -59.577  1.00 72.47           C  
ANISOU 1881  CA  THR A1100     9249   9838   8447   1258   -289    205       C  
ATOM   1882  C   THR A1100     -15.914  -3.204 -58.617  1.00 73.95           C  
ANISOU 1882  C   THR A1100     9565   9820   8712   1435   -247    170       C  
ATOM   1883  O   THR A1100     -16.863  -2.656 -58.056  1.00 80.79           O  
ANISOU 1883  O   THR A1100    10368  10736   9594   1655   -241    179       O  
ATOM   1884  CB  THR A1100     -17.662  -4.656 -59.633  1.00 68.20           C  
ANISOU 1884  CB  THR A1100     8486   9565   7863   1350   -330    266       C  
ATOM   1885  OG1 THR A1100     -18.111  -5.110 -58.350  1.00 59.62           O  
ANISOU 1885  OG1 THR A1100     7287   8567   6799   1384   -264    188       O  
ATOM   1886  CG2 THR A1100     -17.965  -5.721 -60.676  1.00 71.37           C  
ANISOU 1886  CG2 THR A1100     8793  10155   8168   1151   -401    307       C  
ATOM   1887  N   PHE A1101     -14.653  -2.827 -58.432  1.00 67.86           N  
ANISOU 1887  N   PHE A1101     8978   8831   7975   1342   -222    129       N  
ATOM   1888  CA  PHE A1101     -14.315  -1.714 -57.548  1.00 67.40           C  
ANISOU 1888  CA  PHE A1101     9092   8540   7975   1463   -203     87       C  
ATOM   1889  C   PHE A1101     -13.110  -0.919 -58.050  1.00 63.85           C  
ANISOU 1889  C   PHE A1101     8861   7866   7533   1339   -240    141       C  
ATOM   1890  O   PHE A1101     -12.780   0.134 -57.505  1.00 57.50           O  
ANISOU 1890  O   PHE A1101     8254   6827   6765   1403   -256    126       O  
ATOM   1891  CB  PHE A1101     -14.058  -2.211 -56.120  1.00 74.46           C  
ANISOU 1891  CB  PHE A1101     9963   9433   8897   1443   -121    -55       C  
ATOM   1892  CG  PHE A1101     -15.256  -2.845 -55.468  1.00 68.52           C  
ANISOU 1892  CG  PHE A1101     9002   8905   8126   1559    -82    -91       C  
ATOM   1893  CD1 PHE A1101     -16.255  -2.061 -54.912  1.00 61.82           C  
ANISOU 1893  CD1 PHE A1101     8130   8080   7278   1831    -71    -94       C  
ATOM   1894  CD2 PHE A1101     -15.380  -4.223 -55.407  1.00 64.04           C  
ANISOU 1894  CD2 PHE A1101     8271   8532   7527   1398    -60   -115       C  
ATOM   1895  CE1 PHE A1101     -17.357  -2.641 -54.311  1.00 58.87           C  
ANISOU 1895  CE1 PHE A1101     7528   7974   6866   1928    -29   -108       C  
ATOM   1896  CE2 PHE A1101     -16.480  -4.809 -54.807  1.00 60.17           C  
ANISOU 1896  CE2 PHE A1101     7584   8270   7007   1457    -34   -123       C  
ATOM   1897  CZ  PHE A1101     -17.468  -4.017 -54.258  1.00 58.40           C  
ANISOU 1897  CZ  PHE A1101     7292   8121   6775   1716    -14   -112       C  
ATOM   1898  N   GLY A1102     -12.452  -1.429 -59.086  1.00 68.53           N  
ANISOU 1898  N   GLY A1102     9425   8540   8075   1152   -257    204       N  
ATOM   1899  CA  GLY A1102     -11.326  -0.735 -59.683  1.00 73.20           C  
ANISOU 1899  CA  GLY A1102    10177   8989   8646   1005   -290    287       C  
ATOM   1900  C   GLY A1102      -9.977  -1.188 -59.157  1.00 80.23           C  
ANISOU 1900  C   GLY A1102    11086   9868   9531    808   -233    217       C  
ATOM   1901  O   GLY A1102      -9.894  -1.848 -58.122  1.00 81.41           O  
ANISOU 1901  O   GLY A1102    11171  10053   9710    813   -171     93       O  
ATOM   1902  N   ASN A1103      -8.919  -0.822 -59.876  1.00 88.63           N  
ANISOU 1902  N   ASN A1103    12224  10908  10544    635   -255    312       N  
ATOM   1903  CA  ASN A1103      -7.559  -1.208 -59.512  1.00 93.56           C  
ANISOU 1903  CA  ASN A1103    12831  11578  11140    447   -204    277       C  
ATOM   1904  C   ASN A1103      -7.115  -0.629 -58.176  1.00 95.60           C  
ANISOU 1904  C   ASN A1103    13206  11657  11460    419   -202    203       C  
ATOM   1905  O   ASN A1103      -6.432  -1.297 -57.396  1.00 98.28           O  
ANISOU 1905  O   ASN A1103    13472  12072  11798    346   -145    114       O  
ATOM   1906  CB  ASN A1103      -6.570  -0.792 -60.604  1.00 93.64           C  
ANISOU 1906  CB  ASN A1103    12876  11644  11061    263   -232    426       C  
ATOM   1907  CG  ASN A1103      -6.843  -1.474 -61.926  1.00 95.41           C  
ANISOU 1907  CG  ASN A1103    12985  12077  11191    275   -225    483       C  
ATOM   1908  OD1 ASN A1103      -7.415  -2.561 -61.972  1.00 95.36           O  
ANISOU 1908  OD1 ASN A1103    12858  12201  11172    364   -187    387       O  
ATOM   1909  ND2 ASN A1103      -6.430  -0.836 -63.015  1.00100.86           N  
ANISOU 1909  ND2 ASN A1103    13727  12797  11798    168   -269    643       N  
ATOM   1910  N   PHE A1104      -7.501   0.618 -57.922  1.00 92.53           N  
ANISOU 1910  N   PHE A1104    13019  11025  11114    486   -273    238       N  
ATOM   1911  CA  PHE A1104      -7.134   1.293 -56.684  1.00 91.45           C  
ANISOU 1911  CA  PHE A1104    13047  10683  11017    460   -288    156       C  
ATOM   1912  C   PHE A1104      -7.664   0.540 -55.470  1.00 90.63           C  
ANISOU 1912  C   PHE A1104    12838  10647  10951    600   -213    -14       C  
ATOM   1913  O   PHE A1104      -6.907   0.207 -54.557  1.00 98.02           O  
ANISOU 1913  O   PHE A1104    13755  11606  11881    491   -178    -94       O  
ATOM   1914  CB  PHE A1104      -7.649   2.734 -56.677  1.00 92.77           C  
ANISOU 1914  CB  PHE A1104    13493  10542  11213    565   -385    206       C  
ATOM   1915  CG  PHE A1104      -7.424   3.448 -55.376  1.00 97.67           C  
ANISOU 1915  CG  PHE A1104    14329  10923  11858    571   -409     92       C  
ATOM   1916  CD1 PHE A1104      -6.169   3.929 -55.044  1.00100.18           C  
ANISOU 1916  CD1 PHE A1104    14787  11134  12143    287   -460    120       C  
ATOM   1917  CD2 PHE A1104      -8.466   3.635 -54.483  1.00100.58           C  
ANISOU 1917  CD2 PHE A1104    14752  11200  12263    854   -384    -41       C  
ATOM   1918  CE1 PHE A1104      -5.957   4.584 -53.846  1.00102.29           C  
ANISOU 1918  CE1 PHE A1104    15275  11174  12415    271   -497      6       C  
ATOM   1919  CE2 PHE A1104      -8.260   4.289 -53.284  1.00101.86           C  
ANISOU 1919  CE2 PHE A1104    15135  11142  12425    872   -405   -164       C  
ATOM   1920  CZ  PHE A1104      -7.004   4.765 -52.965  1.00102.62           C  
ANISOU 1920  CZ  PHE A1104    15399  11101  12489    572   -468   -147       C  
ATOM   1921  N   TRP A1105      -8.965   0.266 -55.469  1.00 80.14           N  
ANISOU 1921  N   TRP A1105    11423   9378   9648    831   -191    -51       N  
ATOM   1922  CA  TRP A1105      -9.584  -0.459 -54.367  1.00 71.96           C  
ANISOU 1922  CA  TRP A1105    10267   8443   8632    956   -119   -187       C  
ATOM   1923  C   TRP A1105      -9.179  -1.928 -54.363  1.00 64.44           C  
ANISOU 1923  C   TRP A1105     9107   7720   7656    835    -55   -221       C  
ATOM   1924  O   TRP A1105      -9.262  -2.597 -53.335  1.00 65.20           O  
ANISOU 1924  O   TRP A1105     9127   7886   7759    854      0   -321       O  
ATOM   1925  CB  TRP A1105     -11.107  -0.314 -54.403  1.00 75.33           C  
ANISOU 1925  CB  TRP A1105    10630   8920   9072   1224   -118   -191       C  
ATOM   1926  CG  TRP A1105     -11.567   1.091 -54.159  1.00 83.67           C  
ANISOU 1926  CG  TRP A1105    11913   9733  10145   1417   -171   -189       C  
ATOM   1927  CD1 TRP A1105     -12.169   1.925 -55.055  1.00 90.95           C  
ANISOU 1927  CD1 TRP A1105    12928  10561  11070   1559   -242    -77       C  
ATOM   1928  CD2 TRP A1105     -11.443   1.833 -52.940  1.00 83.16           C  
ANISOU 1928  CD2 TRP A1105    12043   9469  10085   1503   -165   -307       C  
ATOM   1929  NE1 TRP A1105     -12.437   3.138 -54.466  1.00 92.18           N  
ANISOU 1929  NE1 TRP A1105    13339  10449  11236   1749   -282   -120       N  
ATOM   1930  CE2 TRP A1105     -12.000   3.107 -53.168  1.00 88.54           C  
ANISOU 1930  CE2 TRP A1105    12953   9916  10772   1715   -235   -271       C  
ATOM   1931  CE3 TRP A1105     -10.920   1.543 -51.676  1.00 80.05           C  
ANISOU 1931  CE3 TRP A1105    11667   9069   9679   1429   -114   -442       C  
ATOM   1932  CZ2 TRP A1105     -12.047   4.089 -52.181  1.00 89.51           C  
ANISOU 1932  CZ2 TRP A1105    13346   9779  10884   1862   -254   -383       C  
ATOM   1933  CZ3 TRP A1105     -10.968   2.518 -50.697  1.00 80.22           C  
ANISOU 1933  CZ3 TRP A1105    11934   8861   9684   1553   -132   -549       C  
ATOM   1934  CH2 TRP A1105     -11.528   3.776 -50.955  1.00 85.89           C  
ANISOU 1934  CH2 TRP A1105    12902   9328  10404   1771   -200   -529       C  
ATOM   1935  N   CYS A1106      -8.739  -2.426 -55.515  1.00 63.50           N  
ANISOU 1935  N   CYS A1106     8917   7712   7498    723    -65   -137       N  
ATOM   1936  CA  CYS A1106      -8.205  -3.779 -55.601  1.00 64.92           C  
ANISOU 1936  CA  CYS A1106     8953   8071   7641    627    -12   -173       C  
ATOM   1937  C   CYS A1106      -6.916  -3.891 -54.791  1.00 76.10           C  
ANISOU 1937  C   CYS A1106    10393   9472   9049    496     18   -216       C  
ATOM   1938  O   CYS A1106      -6.816  -4.703 -53.866  1.00 80.57           O  
ANISOU 1938  O   CYS A1106    10890  10099   9622    503     65   -302       O  
ATOM   1939  CB  CYS A1106      -7.956  -4.170 -57.062  1.00 60.64           C  
ANISOU 1939  CB  CYS A1106     8362   7646   7034    560    -29    -85       C  
ATOM   1940  SG  CYS A1106      -6.881  -5.604 -57.269  1.00 57.31           S  
ANISOU 1940  SG  CYS A1106     7837   7399   6539    458     33   -130       S  
ATOM   1941  N   GLU A1107      -5.936  -3.061 -55.135  1.00 80.21           N  
ANISOU 1941  N   GLU A1107    11004   9926   9544    362    -17   -137       N  
ATOM   1942  CA  GLU A1107      -4.651  -3.063 -54.443  1.00 79.66           C  
ANISOU 1942  CA  GLU A1107    10936   9882   9449    209     -4   -150       C  
ATOM   1943  C   GLU A1107      -4.785  -2.595 -52.997  1.00 76.96           C  
ANISOU 1943  C   GLU A1107    10692   9401   9149    232    -12   -249       C  
ATOM   1944  O   GLU A1107      -3.993  -2.981 -52.135  1.00 76.48           O  
ANISOU 1944  O   GLU A1107    10587   9405   9068    147     11   -295       O  
ATOM   1945  CB  GLU A1107      -3.632  -2.203 -55.191  1.00 81.77           C  
ANISOU 1945  CB  GLU A1107    11269  10139   9662     20    -53    -16       C  
ATOM   1946  CG  GLU A1107      -3.189  -2.797 -56.518  1.00 84.36           C  
ANISOU 1946  CG  GLU A1107    11470  10674   9910    -20    -24     76       C  
ATOM   1947  CD  GLU A1107      -2.162  -1.939 -57.226  1.00 93.53           C  
ANISOU 1947  CD  GLU A1107    12668  11871  10996   -231    -68    232       C  
ATOM   1948  OE1 GLU A1107      -1.462  -2.464 -58.117  1.00 92.83           O  
ANISOU 1948  OE1 GLU A1107    12446  12015  10809   -285    -26    304       O  
ATOM   1949  OE2 GLU A1107      -2.057  -0.740 -56.893  1.00100.38           O  
ANISOU 1949  OE2 GLU A1107    13712  12539  11890   -344   -147    284       O  
ATOM   1950  N   PHE A1108      -5.790  -1.765 -52.735  1.00 74.88           N  
ANISOU 1950  N   PHE A1108    10562   8960   8928    366    -45   -282       N  
ATOM   1951  CA  PHE A1108      -6.070  -1.320 -51.375  1.00 74.75           C  
ANISOU 1951  CA  PHE A1108    10654   8818   8931    434    -44   -397       C  
ATOM   1952  C   PHE A1108      -6.584  -2.491 -50.546  1.00 73.81           C  
ANISOU 1952  C   PHE A1108    10370   8859   8816    534     35   -494       C  
ATOM   1953  O   PHE A1108      -6.174  -2.686 -49.401  1.00 82.04           O  
ANISOU 1953  O   PHE A1108    11417   9915   9841    492     56   -574       O  
ATOM   1954  CB  PHE A1108      -7.098  -0.191 -51.378  1.00 73.45           C  
ANISOU 1954  CB  PHE A1108    10673   8442   8794    616    -88   -413       C  
ATOM   1955  CG  PHE A1108      -7.200   0.534 -50.070  1.00 74.99           C  
ANISOU 1955  CG  PHE A1108    11049   8465   8979    680   -101   -536       C  
ATOM   1956  CD1 PHE A1108      -6.351   1.590 -49.783  1.00 78.98           C  
ANISOU 1956  CD1 PHE A1108    11803   8746   9459    519   -185   -533       C  
ATOM   1957  CD2 PHE A1108      -8.141   0.161 -49.126  1.00 72.76           C  
ANISOU 1957  CD2 PHE A1108    10696   8254   8694    886    -33   -654       C  
ATOM   1958  CE1 PHE A1108      -6.438   2.261 -48.580  1.00 76.89           C  
ANISOU 1958  CE1 PHE A1108    11743   8306   9166    577   -206   -666       C  
ATOM   1959  CE2 PHE A1108      -8.233   0.830 -47.920  1.00 73.96           C  
ANISOU 1959  CE2 PHE A1108    11025   8264   8812    964    -37   -782       C  
ATOM   1960  CZ  PHE A1108      -7.380   1.881 -47.646  1.00 75.19           C  
ANISOU 1960  CZ  PHE A1108    11458   8170   8942    816   -125   -799       C  
ATOM   1961  N   TRP A1109      -7.486  -3.266 -51.140  1.00 64.85           N  
ANISOU 1961  N   TRP A1109     9096   7849   7694    644     67   -476       N  
ATOM   1962  CA  TRP A1109      -8.018  -4.464 -50.503  1.00 60.96           C  
ANISOU 1962  CA  TRP A1109     8451   7512   7198    699    126   -537       C  
ATOM   1963  C   TRP A1109      -6.908  -5.478 -50.244  1.00 65.05           C  
ANISOU 1963  C   TRP A1109     8894   8135   7689    561    153   -542       C  
ATOM   1964  O   TRP A1109      -6.866  -6.109 -49.187  1.00 70.63           O  
ANISOU 1964  O   TRP A1109     9553   8899   8385    561    187   -604       O  
ATOM   1965  CB  TRP A1109      -9.123  -5.074 -51.367  1.00 61.34           C  
ANISOU 1965  CB  TRP A1109     8381   7675   7250    786    129   -493       C  
ATOM   1966  CG  TRP A1109      -9.508  -6.469 -50.989  1.00 68.90           C  
ANISOU 1966  CG  TRP A1109     9199   8790   8191    767    167   -522       C  
ATOM   1967  CD1 TRP A1109     -10.157  -6.864 -49.856  1.00 71.18           C  
ANISOU 1967  CD1 TRP A1109     9423   9150   8472    820    205   -579       C  
ATOM   1968  CD2 TRP A1109      -9.285  -7.655 -51.759  1.00 75.29           C  
ANISOU 1968  CD2 TRP A1109     9940   9693   8974    684    162   -492       C  
ATOM   1969  NE1 TRP A1109     -10.343  -8.226 -49.868  1.00 73.68           N  
ANISOU 1969  NE1 TRP A1109     9641   9587   8767    747    214   -568       N  
ATOM   1970  CE2 TRP A1109      -9.817  -8.735 -51.028  1.00 78.04           C  
ANISOU 1970  CE2 TRP A1109    10207  10135   9309    671    184   -525       C  
ATOM   1971  CE3 TRP A1109      -8.683  -7.910 -52.995  1.00 78.19           C  
ANISOU 1971  CE3 TRP A1109    10322  10074   9313    621    139   -441       C  
ATOM   1972  CZ2 TRP A1109      -9.765 -10.048 -51.489  1.00 83.25           C  
ANISOU 1972  CZ2 TRP A1109    10838  10856   9936    595    171   -516       C  
ATOM   1973  CZ3 TRP A1109      -8.632  -9.214 -53.452  1.00 83.65           C  
ANISOU 1973  CZ3 TRP A1109    10974  10847   9962    575    139   -449       C  
ATOM   1974  CH2 TRP A1109      -9.170 -10.266 -52.701  1.00 85.36           C  
ANISOU 1974  CH2 TRP A1109    11147  11111  10175    561    148   -489       C  
ATOM   1975  N   THR A1110      -6.007  -5.624 -51.211  1.00 66.53           N  
ANISOU 1975  N   THR A1110     9064   8361   7852    460    138   -470       N  
ATOM   1976  CA  THR A1110      -4.861  -6.516 -51.057  1.00 68.30           C  
ANISOU 1976  CA  THR A1110     9212   8704   8037    371    165   -465       C  
ATOM   1977  C   THR A1110      -3.966  -6.046 -49.912  1.00 66.12           C  
ANISOU 1977  C   THR A1110     8976   8401   7745    278    156   -494       C  
ATOM   1978  O   THR A1110      -3.458  -6.853 -49.124  1.00 67.89           O  
ANISOU 1978  O   THR A1110     9131   8718   7947    263    183   -525       O  
ATOM   1979  CB  THR A1110      -4.030  -6.596 -52.352  1.00 68.68           C  
ANISOU 1979  CB  THR A1110     9225   8836   8036    302    159   -377       C  
ATOM   1980  OG1 THR A1110      -4.870  -7.005 -53.440  1.00 66.62           O  
ANISOU 1980  OG1 THR A1110     8943   8599   7769    377    156   -357       O  
ATOM   1981  CG2 THR A1110      -2.893  -7.591 -52.195  1.00 64.60           C  
ANISOU 1981  CG2 THR A1110     8611   8473   7462    271    197   -375       C  
ATOM   1982  N   SER A1111      -3.788  -4.731 -49.825  1.00 66.45           N  
ANISOU 1982  N   SER A1111     9150   8306   7792    209    106   -478       N  
ATOM   1983  CA  SER A1111      -2.998  -4.124 -48.760  1.00 68.86           C  
ANISOU 1983  CA  SER A1111     9533   8563   8069     89     73   -510       C  
ATOM   1984  C   SER A1111      -3.609  -4.415 -47.393  1.00 75.10           C  
ANISOU 1984  C   SER A1111    10336   9337   8864    183    104   -627       C  
ATOM   1985  O   SER A1111      -2.899  -4.765 -46.449  1.00 82.59           O  
ANISOU 1985  O   SER A1111    11246  10365   9771    107    107   -655       O  
ATOM   1986  CB  SER A1111      -2.877  -2.614 -48.973  1.00 63.21           C  
ANISOU 1986  CB  SER A1111     9020   7646   7353     -5     -6   -479       C  
ATOM   1987  OG  SER A1111      -2.246  -2.322 -50.207  1.00 60.32           O  
ANISOU 1987  OG  SER A1111     8634   7320   6964   -127    -37   -347       O  
ATOM   1988  N   ILE A1112      -4.928  -4.272 -47.295  1.00 69.55           N  
ANISOU 1988  N   ILE A1112     9668   8563   8195    352    126   -682       N  
ATOM   1989  CA  ILE A1112      -5.641  -4.588 -46.061  1.00 65.39           C  
ANISOU 1989  CA  ILE A1112     9125   8068   7652    456    169   -781       C  
ATOM   1990  C   ILE A1112      -5.471  -6.064 -45.712  1.00 66.45           C  
ANISOU 1990  C   ILE A1112     9092   8385   7773    439    216   -768       C  
ATOM   1991  O   ILE A1112      -5.277  -6.417 -44.548  1.00 70.02           O  
ANISOU 1991  O   ILE A1112     9525   8895   8184    420    234   -818       O  
ATOM   1992  CB  ILE A1112      -7.141  -4.250 -46.168  1.00 64.63           C  
ANISOU 1992  CB  ILE A1112     9044   7935   7580    659    194   -816       C  
ATOM   1993  CG1 ILE A1112      -7.336  -2.749 -46.378  1.00 69.66           C  
ANISOU 1993  CG1 ILE A1112     9892   8353   8223    722    141   -837       C  
ATOM   1994  CG2 ILE A1112      -7.887  -4.700 -44.922  1.00 61.96           C  
ANISOU 1994  CG2 ILE A1112     8643   7699   7201    761    253   -900       C  
ATOM   1995  CD1 ILE A1112      -8.786  -2.338 -46.507  1.00 73.14           C  
ANISOU 1995  CD1 ILE A1112    10338   8777   8676    970    166   -863       C  
ATOM   1996  N   ASP A1113      -5.533  -6.918 -46.731  1.00 65.45           N  
ANISOU 1996  N   ASP A1113     8867   8333   7668    445    226   -702       N  
ATOM   1997  CA  ASP A1113      -5.332  -8.355 -46.560  1.00 63.29           C  
ANISOU 1997  CA  ASP A1113     8485   8184   7378    436    254   -685       C  
ATOM   1998  C   ASP A1113      -3.982  -8.643 -45.905  1.00 64.42           C  
ANISOU 1998  C   ASP A1113     8606   8391   7479    345    247   -674       C  
ATOM   1999  O   ASP A1113      -3.920  -9.198 -44.799  1.00 65.63           O  
ANISOU 1999  O   ASP A1113     8733   8600   7603    344    261   -702       O  
ATOM   2000  CB  ASP A1113      -5.421  -9.063 -47.916  1.00 64.49           C  
ANISOU 2000  CB  ASP A1113     8591   8370   7542    452    251   -628       C  
ATOM   2001  CG  ASP A1113      -5.552 -10.572 -47.788  1.00 76.08           C  
ANISOU 2001  CG  ASP A1113    10007   9910   8992    467    265   -624       C  
ATOM   2002  OD1 ASP A1113      -5.210 -11.126 -46.723  1.00 78.67           O  
ANISOU 2002  OD1 ASP A1113    10318  10275   9297    452    277   -640       O  
ATOM   2003  OD2 ASP A1113      -5.996 -11.209 -48.766  1.00 86.95           O  
ANISOU 2003  OD2 ASP A1113    11377  11293  10367    487    255   -602       O  
ATOM   2004  N   VAL A1114      -2.909  -8.258 -46.592  1.00 64.81           N  
ANISOU 2004  N   VAL A1114     8652   8461   7512    265    223   -619       N  
ATOM   2005  CA  VAL A1114      -1.555  -8.503 -46.100  1.00 64.00           C  
ANISOU 2005  CA  VAL A1114     8489   8475   7355    178    212   -584       C  
ATOM   2006  C   VAL A1114      -1.328  -7.896 -44.715  1.00 62.15           C  
ANISOU 2006  C   VAL A1114     8307   8219   7086    100    185   -636       C  
ATOM   2007  O   VAL A1114      -0.800  -8.559 -43.817  1.00 60.46           O  
ANISOU 2007  O   VAL A1114     8030   8113   6829     87    188   -634       O  
ATOM   2008  CB  VAL A1114      -0.491  -7.964 -47.075  1.00 68.70           C  
ANISOU 2008  CB  VAL A1114     9050   9137   7918     78    189   -498       C  
ATOM   2009  CG1 VAL A1114       0.905  -8.245 -46.545  1.00 72.31           C  
ANISOU 2009  CG1 VAL A1114     9397   9776   8301     -6    177   -443       C  
ATOM   2010  CG2 VAL A1114      -0.675  -8.583 -48.451  1.00 67.21           C  
ANISOU 2010  CG2 VAL A1114     8814   8989   7734    166    220   -457       C  
ATOM   2011  N   LEU A1115      -1.740  -6.640 -44.548  1.00 62.26           N  
ANISOU 2011  N   LEU A1115     8459   8086   7111     58    152   -684       N  
ATOM   2012  CA  LEU A1115      -1.612  -5.943 -43.269  1.00 60.55           C  
ANISOU 2012  CA  LEU A1115     8344   7818   6845    -10    119   -760       C  
ATOM   2013  C   LEU A1115      -2.274  -6.708 -42.128  1.00 60.65           C  
ANISOU 2013  C   LEU A1115     8317   7894   6834     90    167   -827       C  
ATOM   2014  O   LEU A1115      -1.662  -6.931 -41.083  1.00 57.25           O  
ANISOU 2014  O   LEU A1115     7865   7553   6337     19    151   -842       O  
ATOM   2015  CB  LEU A1115      -2.219  -4.540 -43.357  1.00 56.94           C  
ANISOU 2015  CB  LEU A1115     8091   7143   6402     -5     81   -823       C  
ATOM   2016  CG  LEU A1115      -2.297  -3.771 -42.036  1.00 54.56           C  
ANISOU 2016  CG  LEU A1115     7951   6748   6033    -34     49   -939       C  
ATOM   2017  CD1 LEU A1115      -0.911  -3.345 -41.581  1.00 54.17           C  
ANISOU 2017  CD1 LEU A1115     7938   6737   5908   -281    -35   -907       C  
ATOM   2018  CD2 LEU A1115      -3.226  -2.569 -42.147  1.00 52.14           C  
ANISOU 2018  CD2 LEU A1115     7866   6202   5742     77     31  -1022       C  
ATOM   2019  N   CYS A1116      -3.523  -7.110 -42.337  1.00 64.90           N  
ANISOU 2019  N   CYS A1116     8834   8410   7415    237    219   -853       N  
ATOM   2020  CA  CYS A1116      -4.283  -7.816 -41.311  1.00 64.73           C  
ANISOU 2020  CA  CYS A1116     8763   8471   7359    313    266   -895       C  
ATOM   2021  C   CYS A1116      -3.713  -9.193 -40.986  1.00 62.50           C  
ANISOU 2021  C   CYS A1116     8365   8326   7057    280    273   -827       C  
ATOM   2022  O   CYS A1116      -3.632  -9.569 -39.818  1.00 65.56           O  
ANISOU 2022  O   CYS A1116     8735   8796   7380    261    280   -844       O  
ATOM   2023  CB  CYS A1116      -5.755  -7.936 -41.709  1.00 63.72           C  
ANISOU 2023  CB  CYS A1116     8608   8334   7270    451    312   -908       C  
ATOM   2024  SG  CYS A1116      -6.680  -6.394 -41.597  1.00 97.93           S  
ANISOU 2024  SG  CYS A1116    13083  12533  11595    578    317  -1007       S  
ATOM   2025  N   VAL A1117      -3.326  -9.947 -42.012  1.00 57.79           N  
ANISOU 2025  N   VAL A1117     7706   7751   6502    287    270   -751       N  
ATOM   2026  CA  VAL A1117      -2.753 -11.271 -41.776  1.00 57.65           C  
ANISOU 2026  CA  VAL A1117     7616   7828   6460    296    270   -688       C  
ATOM   2027  C   VAL A1117      -1.437 -11.164 -41.003  1.00 62.23           C  
ANISOU 2027  C   VAL A1117     8162   8508   6974    220    236   -663       C  
ATOM   2028  O   VAL A1117      -1.228 -11.862 -40.001  1.00 65.90           O  
ANISOU 2028  O   VAL A1117     8597   9054   7388    221    232   -643       O  
ATOM   2029  CB  VAL A1117      -2.534 -12.051 -43.090  1.00 53.99           C  
ANISOU 2029  CB  VAL A1117     7125   7354   6033    350    271   -632       C  
ATOM   2030  CG1 VAL A1117      -1.780 -13.345 -42.822  1.00 54.53           C  
ANISOU 2030  CG1 VAL A1117     7159   7496   6065    396    263   -574       C  
ATOM   2031  CG2 VAL A1117      -3.865 -12.342 -43.764  1.00 48.13           C  
ANISOU 2031  CG2 VAL A1117     6410   6541   5338    398    287   -645       C  
ATOM   2032  N   THR A1118      -0.564 -10.272 -41.466  1.00 60.64           N  
ANISOU 2032  N   THR A1118     7960   8316   6764    137    205   -650       N  
ATOM   2033  CA  THR A1118       0.726 -10.046 -40.822  1.00 60.39           C  
ANISOU 2033  CA  THR A1118     7874   8416   6657     27    158   -610       C  
ATOM   2034  C   THR A1118       0.559  -9.610 -39.367  1.00 59.24           C  
ANISOU 2034  C   THR A1118     7790   8274   6444    -43    134   -678       C  
ATOM   2035  O   THR A1118       1.172 -10.186 -38.464  1.00 57.12           O  
ANISOU 2035  O   THR A1118     7454   8142   6106    -65    114   -641       O  
ATOM   2036  CB  THR A1118       1.558  -8.989 -41.578  1.00 57.10           C  
ANISOU 2036  CB  THR A1118     7455   8009   6229   -106    116   -573       C  
ATOM   2037  OG1 THR A1118       1.728  -9.397 -42.941  1.00 63.45           O  
ANISOU 2037  OG1 THR A1118     8194   8843   7072    -33    147   -509       O  
ATOM   2038  CG2 THR A1118       2.924  -8.818 -40.931  1.00 46.46           C  
ANISOU 2038  CG2 THR A1118     6016   6851   4787   -250     57   -509       C  
ATOM   2039  N   ALA A1119      -0.277  -8.599 -39.147  1.00 58.69           N  
ANISOU 2039  N   ALA A1119     7856   8060   6383    -58    137   -779       N  
ATOM   2040  CA  ALA A1119      -0.542  -8.098 -37.801  1.00 59.33           C  
ANISOU 2040  CA  ALA A1119     8028   8136   6380    -98    123   -872       C  
ATOM   2041  C   ALA A1119      -1.105  -9.190 -36.897  1.00 56.28           C  
ANISOU 2041  C   ALA A1119     7573   7853   5956    -10    170   -864       C  
ATOM   2042  O   ALA A1119      -0.706  -9.312 -35.741  1.00 58.10           O  
ANISOU 2042  O   ALA A1119     7798   8189   6089    -70    145   -874       O  
ATOM   2043  CB  ALA A1119      -1.489  -6.905 -37.850  1.00 56.80           C  
ANISOU 2043  CB  ALA A1119     7880   7629   6071    -55    132   -990       C  
ATOM   2044  N   SER A1120      -2.025  -9.985 -37.436  1.00 48.29           N  
ANISOU 2044  N   SER A1120     6515   6820   5013    108    226   -835       N  
ATOM   2045  CA  SER A1120      -2.618 -11.090 -36.692  1.00 46.35           C  
ANISOU 2045  CA  SER A1120     6214   6665   4733    159    261   -799       C  
ATOM   2046  C   SER A1120      -1.568 -12.104 -36.237  1.00 49.02           C  
ANISOU 2046  C   SER A1120     6477   7119   5028    126    222   -698       C  
ATOM   2047  O   SER A1120      -1.450 -12.393 -35.043  1.00 54.03           O  
ANISOU 2047  O   SER A1120     7102   7858   5570     92    212   -687       O  
ATOM   2048  CB  SER A1120      -3.692 -11.787 -37.532  1.00 47.21           C  
ANISOU 2048  CB  SER A1120     6293   6724   4920    244    303   -764       C  
ATOM   2049  OG  SER A1120      -4.197 -12.935 -36.873  1.00 49.52           O  
ANISOU 2049  OG  SER A1120     6544   7097   5174    248    318   -701       O  
ATOM   2050  N   ILE A1121      -0.803 -12.635 -37.187  1.00 44.64           N  
ANISOU 2050  N   ILE A1121     5872   6563   4527    156    202   -621       N  
ATOM   2051  CA  ILE A1121       0.182 -13.667 -36.866  1.00 46.79           C  
ANISOU 2051  CA  ILE A1121     6073   6949   4758    186    169   -516       C  
ATOM   2052  C   ILE A1121       1.303 -13.156 -35.953  1.00 50.40           C  
ANISOU 2052  C   ILE A1121     6477   7557   5115     86    114   -501       C  
ATOM   2053  O   ILE A1121       1.695 -13.829 -34.990  1.00 56.48           O  
ANISOU 2053  O   ILE A1121     7208   8443   5810     90     86   -438       O  
ATOM   2054  CB  ILE A1121       0.776 -14.299 -38.139  1.00 47.97           C  
ANISOU 2054  CB  ILE A1121     6182   7080   4965    284    170   -452       C  
ATOM   2055  CG1 ILE A1121      -0.343 -14.858 -39.019  1.00 46.02           C  
ANISOU 2055  CG1 ILE A1121     6006   6682   4796    356    205   -470       C  
ATOM   2056  CG2 ILE A1121       1.768 -15.394 -37.779  1.00 48.28           C  
ANISOU 2056  CG2 ILE A1121     6159   7236   4950    372    137   -346       C  
ATOM   2057  CD1 ILE A1121       0.144 -15.554 -40.269  1.00 45.24           C  
ANISOU 2057  CD1 ILE A1121     5905   6553   4733    468    208   -429       C  
ATOM   2058  N   GLU A1122       1.810 -11.963 -36.245  1.00 48.62           N  
ANISOU 2058  N   GLU A1122     6259   7333   4881    -24     86   -547       N  
ATOM   2059  CA  GLU A1122       2.843 -11.370 -35.404  1.00 55.94           C  
ANISOU 2059  CA  GLU A1122     7148   8407   5701   -171     15   -535       C  
ATOM   2060  C   GLU A1122       2.322 -11.093 -33.996  1.00 58.34           C  
ANISOU 2060  C   GLU A1122     7536   8722   5909   -231      5   -614       C  
ATOM   2061  O   GLU A1122       3.061 -11.226 -33.020  1.00 58.11           O  
ANISOU 2061  O   GLU A1122     7455   8855   5768   -309    -52   -573       O  
ATOM   2062  CB  GLU A1122       3.405 -10.097 -36.034  1.00 58.42           C  
ANISOU 2062  CB  GLU A1122     7490   8690   6017   -322    -29   -563       C  
ATOM   2063  CG  GLU A1122       4.277 -10.349 -37.249  1.00 63.71           C  
ANISOU 2063  CG  GLU A1122     8027   9454   6727   -297    -29   -454       C  
ATOM   2064  CD  GLU A1122       4.943  -9.088 -37.751  1.00 76.91           C  
ANISOU 2064  CD  GLU A1122     9714  11135   8374   -502    -88   -446       C  
ATOM   2065  OE1 GLU A1122       4.834  -8.049 -37.067  1.00 82.72           O  
ANISOU 2065  OE1 GLU A1122    10588  11785   9057   -671   -147   -529       O  
ATOM   2066  OE2 GLU A1122       5.573  -9.135 -38.829  1.00 81.35           O  
ANISOU 2066  OE2 GLU A1122    10166  11788   8957   -499    -79   -357       O  
ATOM   2067  N   THR A1123       1.051 -10.716 -33.891  1.00 60.22           N  
ANISOU 2067  N   THR A1123     7891   8816   6174   -182     62   -723       N  
ATOM   2068  CA  THR A1123       0.433 -10.535 -32.581  1.00 55.64           C  
ANISOU 2068  CA  THR A1123     7381   8275   5484   -199     75   -803       C  
ATOM   2069  C   THR A1123       0.334 -11.875 -31.855  1.00 53.10           C  
ANISOU 2069  C   THR A1123     6973   8086   5117   -141     90   -698       C  
ATOM   2070  O   THR A1123       0.510 -11.935 -30.643  1.00 48.78           O  
ANISOU 2070  O   THR A1123     6428   7666   4439   -200     64   -701       O  
ATOM   2071  CB  THR A1123      -0.958  -9.878 -32.673  1.00 59.10           C  
ANISOU 2071  CB  THR A1123     7934   8573   5947   -114    148   -933       C  
ATOM   2072  OG1 THR A1123      -0.846  -8.619 -33.348  1.00 65.56           O  
ANISOU 2072  OG1 THR A1123     8870   9235   6807   -157    121  -1020       O  
ATOM   2073  CG2 THR A1123      -1.536  -9.643 -31.287  1.00 41.38           C  
ANISOU 2073  CG2 THR A1123     5753   6412   3556   -112    173  -1024       C  
ATOM   2074  N   LEU A1124       0.063 -12.946 -32.598  1.00 51.99           N  
ANISOU 2074  N   LEU A1124     6776   7903   5073    -37    120   -602       N  
ATOM   2075  CA  LEU A1124       0.078 -14.290 -32.018  1.00 50.36           C  
ANISOU 2075  CA  LEU A1124     6524   7780   4830     10    111   -478       C  
ATOM   2076  C   LEU A1124       1.454 -14.602 -31.432  1.00 51.95           C  
ANISOU 2076  C   LEU A1124     6647   8144   4948    -23     33   -383       C  
ATOM   2077  O   LEU A1124       1.568 -15.143 -30.326  1.00 55.27           O  
ANISOU 2077  O   LEU A1124     7053   8684   5263    -44      5   -318       O  
ATOM   2078  CB  LEU A1124      -0.299 -15.342 -33.063  1.00 44.27           C  
ANISOU 2078  CB  LEU A1124     5755   6892   4173    118    133   -400       C  
ATOM   2079  CG  LEU A1124      -1.734 -15.338 -33.588  1.00 46.59           C  
ANISOU 2079  CG  LEU A1124     6098   7070   4535    139    197   -451       C  
ATOM   2080  CD1 LEU A1124      -1.864 -16.271 -34.782  1.00 49.92           C  
ANISOU 2080  CD1 LEU A1124     6543   7365   5060    217    192   -386       C  
ATOM   2081  CD2 LEU A1124      -2.708 -15.735 -32.491  1.00 46.02           C  
ANISOU 2081  CD2 LEU A1124     6033   7079   4373     96    225   -429       C  
ATOM   2082  N   CYS A1125       2.495 -14.251 -32.183  1.00 51.76           N  
ANISOU 2082  N   CYS A1125     6556   8152   4959    -30     -4   -361       N  
ATOM   2083  CA  CYS A1125       3.873 -14.417 -31.724  1.00 55.71           C  
ANISOU 2083  CA  CYS A1125     6938   8859   5369    -64    -82   -260       C  
ATOM   2084  C   CYS A1125       4.151 -13.632 -30.437  1.00 54.66           C  
ANISOU 2084  C   CYS A1125     6821   8861   5088   -237   -139   -313       C  
ATOM   2085  O   CYS A1125       4.698 -14.172 -29.464  1.00 55.78           O  
ANISOU 2085  O   CYS A1125     6898   9177   5117   -249   -193   -221       O  
ATOM   2086  CB  CYS A1125       4.844 -13.989 -32.827  1.00 56.52           C  
ANISOU 2086  CB  CYS A1125     6944   9012   5519    -70   -101   -231       C  
ATOM   2087  SG  CYS A1125       6.581 -13.949 -32.341  1.00 88.33           S  
ANISOU 2087  SG  CYS A1125    10772  13371   9417   -144   -201    -98       S  
ATOM   2088  N   VAL A1126       3.765 -12.358 -30.442  1.00 51.04           N  
ANISOU 2088  N   VAL A1126     6467   8308   4617   -361   -134   -461       N  
ATOM   2089  CA  VAL A1126       3.922 -11.488 -29.279  1.00 54.34           C  
ANISOU 2089  CA  VAL A1126     6960   8806   4882   -528   -190   -552       C  
ATOM   2090  C   VAL A1126       3.187 -12.047 -28.060  1.00 63.68           C  
ANISOU 2090  C   VAL A1126     8183  10052   5960   -486   -159   -562       C  
ATOM   2091  O   VAL A1126       3.686 -11.970 -26.940  1.00 66.18           O  
ANISOU 2091  O   VAL A1126     8490  10539   6118   -589   -224   -550       O  
ATOM   2092  CB  VAL A1126       3.435 -10.051 -29.580  1.00 51.33           C  
ANISOU 2092  CB  VAL A1126     6752   8238   4514   -623   -184   -729       C  
ATOM   2093  CG1 VAL A1126       3.375  -9.214 -28.308  1.00 50.78           C  
ANISOU 2093  CG1 VAL A1126     6822   8206   4267   -759   -234   -859       C  
ATOM   2094  CG2 VAL A1126       4.336  -9.392 -30.609  1.00 44.85           C  
ANISOU 2094  CG2 VAL A1126     5894   7393   3754   -733   -242   -694       C  
ATOM   2095  N   ILE A1127       2.007 -12.618 -28.284  1.00 61.07           N  
ANISOU 2095  N   ILE A1127     7888   9610   5704   -354    -65   -571       N  
ATOM   2096  CA  ILE A1127       1.246 -13.254 -27.214  1.00 52.73           C  
ANISOU 2096  CA  ILE A1127     6848   8642   4547   -325    -27   -547       C  
ATOM   2097  C   ILE A1127       1.998 -14.461 -26.669  1.00 56.65           C  
ANISOU 2097  C   ILE A1127     7243   9294   4989   -307    -89   -356       C  
ATOM   2098  O   ILE A1127       2.063 -14.662 -25.456  1.00 60.34           O  
ANISOU 2098  O   ILE A1127     7708   9921   5298   -366   -118   -323       O  
ATOM   2099  CB  ILE A1127      -0.156 -13.693 -27.689  1.00 46.16           C  
ANISOU 2099  CB  ILE A1127     6045   7688   3806   -216     76   -560       C  
ATOM   2100  CG1 ILE A1127      -1.020 -12.471 -27.998  1.00 47.85           C  
ANISOU 2100  CG1 ILE A1127     6356   7785   4038   -197    140   -747       C  
ATOM   2101  CG2 ILE A1127      -0.842 -14.541 -26.631  1.00 44.06           C  
ANISOU 2101  CG2 ILE A1127     5762   7552   3426   -215    106   -480       C  
ATOM   2102  CD1 ILE A1127      -2.248 -12.789 -28.821  1.00 50.62           C  
ANISOU 2102  CD1 ILE A1127     6697   8029   4507    -90    227   -745       C  
ATOM   2103  N   ALA A1128       2.571 -15.259 -27.566  1.00 62.30           N  
ANISOU 2103  N   ALA A1128     7886   9963   5821   -208   -109   -231       N  
ATOM   2104  CA  ALA A1128       3.352 -16.424 -27.154  1.00 64.19           C  
ANISOU 2104  CA  ALA A1128     8047  10326   6016   -138   -174    -44       C  
ATOM   2105  C   ALA A1128       4.514 -16.020 -26.250  1.00 71.57           C  
ANISOU 2105  C   ALA A1128     8892  11506   6796   -246   -271     -5       C  
ATOM   2106  O   ALA A1128       4.684 -16.570 -25.156  1.00 81.00           O  
ANISOU 2106  O   ALA A1128    10068  12851   7859   -264   -318     91       O  
ATOM   2107  CB  ALA A1128       3.861 -17.184 -28.369  1.00 63.67           C  
ANISOU 2107  CB  ALA A1128     7936  10167   6087     23   -177     50       C  
ATOM   2108  N   VAL A1129       5.304 -15.051 -26.706  1.00 70.07           N  
ANISOU 2108  N   VAL A1129     8648  11367   6610   -339   -311    -69       N  
ATOM   2109  CA  VAL A1129       6.429 -14.549 -25.917  1.00 71.55           C  
ANISOU 2109  CA  VAL A1129     8742  11804   6639   -492   -421    -34       C  
ATOM   2110  C   VAL A1129       5.962 -13.976 -24.575  1.00 75.99           C  
ANISOU 2110  C   VAL A1129     9414  12434   7027   -645   -441   -140       C  
ATOM   2111  O   VAL A1129       6.544 -14.259 -23.521  1.00 79.79           O  
ANISOU 2111  O   VAL A1129     9833  13139   7346   -710   -521    -52       O  
ATOM   2112  CB  VAL A1129       7.224 -13.480 -26.699  1.00 63.72           C  
ANISOU 2112  CB  VAL A1129     7697  10837   5677   -625   -465    -89       C  
ATOM   2113  CG1 VAL A1129       8.195 -12.749 -25.786  1.00 51.19           C  
ANISOU 2113  CG1 VAL A1129     6054   9494   3902   -861   -592    -83       C  
ATOM   2114  CG2 VAL A1129       7.958 -14.120 -27.864  1.00 48.60           C  
ANISOU 2114  CG2 VAL A1129     5624   8966   3877   -468   -455     46       C  
ATOM   2115  N   ASP A1130       4.897 -13.182 -24.634  1.00 73.10           N  
ANISOU 2115  N   ASP A1130     9208  11884   6681   -680   -364   -328       N  
ATOM   2116  CA  ASP A1130       4.291 -12.572 -23.456  1.00 69.66           C  
ANISOU 2116  CA  ASP A1130     8904  11494   6071   -778   -356   -465       C  
ATOM   2117  C   ASP A1130       3.947 -13.616 -22.404  1.00 61.26           C  
ANISOU 2117  C   ASP A1130     7801  10582   4892   -724   -344   -346       C  
ATOM   2118  O   ASP A1130       4.291 -13.464 -21.234  1.00 61.39           O  
ANISOU 2118  O   ASP A1130     7825  10793   4705   -835   -408   -347       O  
ATOM   2119  CB  ASP A1130       3.028 -11.805 -23.854  1.00 72.79           C  
ANISOU 2119  CB  ASP A1130     9460  11665   6533   -725   -247   -661       C  
ATOM   2120  CG  ASP A1130       2.235 -11.321 -22.657  1.00 73.31           C  
ANISOU 2120  CG  ASP A1130     9655  11791   6406   -754   -207   -805       C  
ATOM   2121  OD1 ASP A1130       1.372 -12.082 -22.171  1.00 74.33           O  
ANISOU 2121  OD1 ASP A1130     9756  11989   6497   -660   -127   -751       O  
ATOM   2122  OD2 ASP A1130       2.468 -10.179 -22.209  1.00 72.78           O  
ANISOU 2122  OD2 ASP A1130     9731  11708   6215   -875   -259   -972       O  
ATOM   2123  N   ARG A1131       3.272 -14.677 -22.831  1.00 56.08           N  
ANISOU 2123  N   ARG A1131     7117   9836   4353   -572   -271   -237       N  
ATOM   2124  CA  ARG A1131       2.889 -15.747 -21.922  1.00 64.55           C  
ANISOU 2124  CA  ARG A1131     8172  11027   5328   -537   -265    -92       C  
ATOM   2125  C   ARG A1131       4.108 -16.506 -21.417  1.00 74.53           C  
ANISOU 2125  C   ARG A1131     9325  12480   6513   -537   -385    108       C  
ATOM   2126  O   ARG A1131       4.121 -16.983 -20.282  1.00 81.12           O  
ANISOU 2126  O   ARG A1131    10152  13490   7181   -579   -423    204       O  
ATOM   2127  CB  ARG A1131       1.899 -16.704 -22.588  1.00 65.94           C  
ANISOU 2127  CB  ARG A1131     8370  11033   5650   -413   -182    -11       C  
ATOM   2128  CG  ARG A1131       0.552 -16.073 -22.892  1.00 65.93           C  
ANISOU 2128  CG  ARG A1131     8444  10916   5688   -406    -61   -176       C  
ATOM   2129  CD  ARG A1131       0.021 -15.319 -21.683  1.00 61.63           C  
ANISOU 2129  CD  ARG A1131     7952  10536   4929   -487    -23   -307       C  
ATOM   2130  NE  ARG A1131      -0.076 -16.172 -20.503  1.00 58.18           N  
ANISOU 2130  NE  ARG A1131     7483  10302   4320   -534    -44   -156       N  
ATOM   2131  CZ  ARG A1131      -0.344 -15.726 -19.280  1.00 58.83           C  
ANISOU 2131  CZ  ARG A1131     7596  10587   4170   -606    -26   -232       C  
ATOM   2132  NH1 ARG A1131      -0.539 -14.430 -19.077  1.00 56.75           N  
ANISOU 2132  NH1 ARG A1131     7420  10323   3819   -624     10   -473       N  
ATOM   2133  NH2 ARG A1131      -0.415 -16.572 -18.261  1.00 59.04           N  
ANISOU 2133  NH2 ARG A1131     7587  10807   4039   -656    -48    -67       N  
ATOM   2134  N   TYR A1132       5.133 -16.615 -22.259  1.00 77.54           N  
ANISOU 2134  N   TYR A1132     9606  12853   7001   -477   -443    180       N  
ATOM   2135  CA  TYR A1132       6.372 -17.253 -21.831  1.00 80.32           C  
ANISOU 2135  CA  TYR A1132     9822  13427   7270   -445   -559    373       C  
ATOM   2136  C   TYR A1132       6.989 -16.506 -20.657  1.00 87.10           C  
ANISOU 2136  C   TYR A1132    10644  14550   7902   -645   -654    336       C  
ATOM   2137  O   TYR A1132       7.336 -17.110 -19.644  1.00 88.52           O  
ANISOU 2137  O   TYR A1132    10776  14930   7928   -654   -725    478       O  
ATOM   2138  CB  TYR A1132       7.385 -17.339 -22.970  1.00 73.96           C  
ANISOU 2138  CB  TYR A1132     8885  12623   6592   -339   -592    440       C  
ATOM   2139  CG  TYR A1132       8.732 -17.855 -22.518  1.00 72.98           C  
ANISOU 2139  CG  TYR A1132     8580  12789   6359   -290   -712    637       C  
ATOM   2140  CD1 TYR A1132       8.921 -19.201 -22.236  1.00 73.44           C  
ANISOU 2140  CD1 TYR A1132     8620  12875   6409    -86   -745    845       C  
ATOM   2141  CD2 TYR A1132       9.812 -16.995 -22.363  1.00 73.90           C  
ANISOU 2141  CD2 TYR A1132     8550  13157   6371   -452   -805    628       C  
ATOM   2142  CE1 TYR A1132      10.147 -19.679 -21.816  1.00 75.00           C  
ANISOU 2142  CE1 TYR A1132     8641  13356   6499     -1   -856   1037       C  
ATOM   2143  CE2 TYR A1132      11.044 -17.464 -21.943  1.00 76.17           C  
ANISOU 2143  CE2 TYR A1132     8633  13764   6545   -404   -920    826       C  
ATOM   2144  CZ  TYR A1132      11.205 -18.807 -21.672  1.00 76.57           C  
ANISOU 2144  CZ  TYR A1132     8653  13849   6592   -156   -940   1029       C  
ATOM   2145  OH  TYR A1132      12.426 -19.282 -21.254  1.00 83.40           O  
ANISOU 2145  OH  TYR A1132     9305  15047   7336    -68  -1055   1237       O  
ATOM   2146  N   PHE A1133       7.125 -15.191 -20.795  1.00 89.80           N  
ANISOU 2146  N   PHE A1133    11030  14880   8212   -816   -666    147       N  
ATOM   2147  CA  PHE A1133       7.694 -14.384 -19.719  1.00 89.93           C  
ANISOU 2147  CA  PHE A1133    11054  15117   7997  -1041   -771     83       C  
ATOM   2148  C   PHE A1133       6.766 -14.298 -18.511  1.00 83.32           C  
ANISOU 2148  C   PHE A1133    10361  14316   6982  -1095   -729    -11       C  
ATOM   2149  O   PHE A1133       7.223 -14.160 -17.378  1.00 85.53           O  
ANISOU 2149  O   PHE A1133    10629  14833   7035  -1230   -822     10       O  
ATOM   2150  CB  PHE A1133       8.057 -12.985 -20.219  1.00 97.91           C  
ANISOU 2150  CB  PHE A1133    12128  16058   9016  -1230   -811    -96       C  
ATOM   2151  CG  PHE A1133       9.340 -12.936 -20.996  1.00106.64           C  
ANISOU 2151  CG  PHE A1133    13037  17296  10184  -1273   -901     33       C  
ATOM   2152  CD1 PHE A1133      10.335 -13.874 -20.772  1.00109.57           C  
ANISOU 2152  CD1 PHE A1133    13180  17944  10506  -1190   -982    274       C  
ATOM   2153  CD2 PHE A1133       9.551 -11.957 -21.952  1.00110.51           C  
ANISOU 2153  CD2 PHE A1133    13564  17654  10770  -1386   -905    -73       C  
ATOM   2154  CE1 PHE A1133      11.518 -13.835 -21.484  1.00111.38           C  
ANISOU 2154  CE1 PHE A1133    13193  18355  10772  -1205  -1053    402       C  
ATOM   2155  CE2 PHE A1133      10.732 -11.913 -22.669  1.00112.35           C  
ANISOU 2155  CE2 PHE A1133    13588  18061  11040  -1440   -981     63       C  
ATOM   2156  CZ  PHE A1133      11.717 -12.853 -22.434  1.00112.31           C  
ANISOU 2156  CZ  PHE A1133    13327  18371  10975  -1342  -1050    299       C  
ATOM   2157  N   ALA A1134       5.464 -14.388 -18.755  1.00 74.06           N  
ANISOU 2157  N   ALA A1134     9306  12941   5895   -989   -590   -107       N  
ATOM   2158  CA  ALA A1134       4.482 -14.315 -17.680  1.00 66.92           C  
ANISOU 2158  CA  ALA A1134     8512  12103   4812  -1015   -524   -193       C  
ATOM   2159  C   ALA A1134       4.478 -15.587 -16.840  1.00 63.22           C  
ANISOU 2159  C   ALA A1134     7963  11818   4242   -969   -548     41       C  
ATOM   2160  O   ALA A1134       4.172 -15.551 -15.649  1.00 69.85           O  
ANISOU 2160  O   ALA A1134     8845  12842   4851  -1047   -550     26       O  
ATOM   2161  CB  ALA A1134       3.095 -14.049 -18.244  1.00 68.20           C  
ANISOU 2161  CB  ALA A1134     8780  12043   5089   -909   -366   -339       C  
ATOM   2162  N   ILE A1135       4.819 -16.710 -17.465  1.00 63.33           N  
ANISOU 2162  N   ILE A1135     7878  11770   4414   -834   -570    259       N  
ATOM   2163  CA  ILE A1135       4.800 -17.997 -16.778  1.00 72.11           C  
ANISOU 2163  CA  ILE A1135     8952  12995   5452   -774   -604    505       C  
ATOM   2164  C   ILE A1135       6.160 -18.369 -16.184  1.00 77.48           C  
ANISOU 2164  C   ILE A1135     9506  13923   6009   -793   -762    687       C  
ATOM   2165  O   ILE A1135       6.248 -18.794 -15.032  1.00 74.06           O  
ANISOU 2165  O   ILE A1135     9063  13702   5372   -851   -820    808       O  
ATOM   2166  CB  ILE A1135       4.322 -19.126 -17.716  1.00 77.86           C  
ANISOU 2166  CB  ILE A1135     9698  13485   6400   -600   -552    649       C  
ATOM   2167  CG1 ILE A1135       2.871 -18.894 -18.135  1.00 75.92           C  
ANISOU 2167  CG1 ILE A1135     9551  13058   6238   -602   -407    511       C  
ATOM   2168  CG2 ILE A1135       4.441 -20.470 -17.031  1.00 89.09           C  
ANISOU 2168  CG2 ILE A1135    11119  14985   7745   -543   -619    923       C  
ATOM   2169  CD1 ILE A1135       2.353 -19.924 -19.114  1.00 78.10           C  
ANISOU 2169  CD1 ILE A1135     9867  13088   6721   -476   -369    632       C  
ATOM   2170  N   THR A1136       7.216 -18.203 -16.975  1.00 83.00           N  
ANISOU 2170  N   THR A1136    10091  14627   6818   -745   -830    717       N  
ATOM   2171  CA  THR A1136       8.566 -18.565 -16.552  1.00 89.21           C  
ANISOU 2171  CA  THR A1136    10711  15687   7498   -734   -979    908       C  
ATOM   2172  C   THR A1136       9.106 -17.635 -15.467  1.00 87.23           C  
ANISOU 2172  C   THR A1136    10430  15726   6987   -983  -1080    825       C  
ATOM   2173  O   THR A1136       9.548 -18.090 -14.412  1.00 83.10           O  
ANISOU 2173  O   THR A1136     9846  15460   6267  -1021  -1178    980       O  
ATOM   2174  CB  THR A1136       9.545 -18.563 -17.741  1.00 94.26           C  
ANISOU 2174  CB  THR A1136    11203  16307   8305   -615  -1013    960       C  
ATOM   2175  OG1 THR A1136       9.182 -19.601 -18.660  1.00 90.89           O  
ANISOU 2175  OG1 THR A1136    10817  15633   8084   -358   -942   1061       O  
ATOM   2176  CG2 THR A1136      10.969 -18.793 -17.262  1.00105.97           C  
ANISOU 2176  CG2 THR A1136    12470  18147   9648   -613  -1168   1154       C  
ATOM   2177  N   SER A1137       9.075 -16.334 -15.738  1.00 85.29           N  
ANISOU 2177  N   SER A1137    10248  15426   6734  -1157  -1068    584       N  
ATOM   2178  CA  SER A1137       9.551 -15.340 -14.784  1.00 81.67           C  
ANISOU 2178  CA  SER A1137     9816  15191   6023  -1423  -1174    467       C  
ATOM   2179  C   SER A1137       8.513 -14.238 -14.592  1.00 82.58           C  
ANISOU 2179  C   SER A1137    10172  15121   6082  -1540  -1081    158       C  
ATOM   2180  O   SER A1137       8.639 -13.155 -15.164  1.00 82.04           O  
ANISOU 2180  O   SER A1137    10187  14919   6066  -1657  -1090    -29       O  
ATOM   2181  CB  SER A1137      10.874 -14.740 -15.256  1.00 83.29           C  
ANISOU 2181  CB  SER A1137     9863  15555   6230  -1559  -1308    499       C  
ATOM   2182  OG  SER A1137      11.332 -13.754 -14.350  1.00 93.11           O  
ANISOU 2182  OG  SER A1137    11162  16996   7219  -1858  -1432    380       O  
ATOM   2183  N   PRO A1138       7.486 -14.513 -13.773  1.00 80.15           N  
ANISOU 2183  N   PRO A1138     9982  14818   5654  -1499   -992    113       N  
ATOM   2184  CA  PRO A1138       6.325 -13.630 -13.605  1.00 80.87           C  
ANISOU 2184  CA  PRO A1138    10289  14747   5691  -1523   -869   -167       C  
ATOM   2185  C   PRO A1138       6.643 -12.328 -12.874  1.00 85.58           C  
ANISOU 2185  C   PRO A1138    11043  15427   6046  -1749   -955   -404       C  
ATOM   2186  O   PRO A1138       6.079 -11.286 -13.209  1.00 93.11           O  
ANISOU 2186  O   PRO A1138    12189  16164   7024  -1767   -892   -664       O  
ATOM   2187  CB  PRO A1138       5.366 -14.477 -12.766  1.00 79.17           C  
ANISOU 2187  CB  PRO A1138    10088  14634   5357  -1430   -775    -76       C  
ATOM   2188  CG  PRO A1138       6.254 -15.396 -12.000  1.00 67.59           C  
ANISOU 2188  CG  PRO A1138     8476  13446   3759  -1468   -908    195       C  
ATOM   2189  CD  PRO A1138       7.398 -15.711 -12.918  1.00 76.16           C  
ANISOU 2189  CD  PRO A1138     9400  14501   5035  -1421  -1009    350       C  
ATOM   2190  N   PHE A1139       7.532 -12.392 -11.889  1.00 82.39           N  
ANISOU 2190  N   PHE A1139    10574  15298   5432  -1906  -1100   -310       N  
ATOM   2191  CA  PHE A1139       7.865 -11.226 -11.080  1.00 85.43           C  
ANISOU 2191  CA  PHE A1139    11123  15670   5665  -2106  -1178   -517       C  
ATOM   2192  C   PHE A1139       8.606 -10.172 -11.896  1.00 92.31           C  
ANISOU 2192  C   PHE A1139    12054  16401   6620  -2282  -1280   -636       C  
ATOM   2193  O   PHE A1139       8.440  -8.973 -11.674  1.00 74.17           O  
ANISOU 2193  O   PHE A1139    10004  13927   4250  -2405  -1299   -892       O  
ATOM   2194  CB  PHE A1139       8.690 -11.646  -9.864  1.00 88.00           C  
ANISOU 2194  CB  PHE A1139    11332  16269   5835  -2211  -1298   -350       C  
ATOM   2195  CG  PHE A1139       8.022 -12.689  -9.014  1.00 83.87           C  
ANISOU 2195  CG  PHE A1139    10758  15884   5224  -2068  -1215   -207       C  
ATOM   2196  CD1 PHE A1139       6.649 -12.678  -8.835  1.00 86.40           C  
ANISOU 2196  CD1 PHE A1139    11222  16100   5508  -1936  -1043   -343       C  
ATOM   2197  CD2 PHE A1139       8.763 -13.688  -8.407  1.00 81.71           C  
ANISOU 2197  CD2 PHE A1139    10285  15853   4906  -2063  -1307     79       C  
ATOM   2198  CE1 PHE A1139       6.029 -13.637  -8.059  1.00 90.03           C  
ANISOU 2198  CE1 PHE A1139    11623  16699   5883  -1839   -968   -188       C  
ATOM   2199  CE2 PHE A1139       8.147 -14.651  -7.631  1.00 85.50           C  
ANISOU 2199  CE2 PHE A1139    10739  16441   5307  -1954  -1241    229       C  
ATOM   2200  CZ  PHE A1139       6.779 -14.625  -7.456  1.00 89.85           C  
ANISOU 2200  CZ  PHE A1139    11430  16891   5818  -1860  -1073    100       C  
ATOM   2201  N   LYS A1140       9.421 -10.628 -12.842  1.00 92.95           N  
ANISOU 2201  N   LYS A1140    11915  16555   6847  -2284  -1347   -442       N  
ATOM   2202  CA  LYS A1140      10.113  -9.726 -13.756  1.00 89.87           C  
ANISOU 2202  CA  LYS A1140    11542  16053   6552  -2457  -1435   -512       C  
ATOM   2203  C   LYS A1140       9.159  -9.248 -14.846  1.00 87.51           C  
ANISOU 2203  C   LYS A1140    11409  15397   6445  -2329  -1295   -692       C  
ATOM   2204  O   LYS A1140       9.226  -8.100 -15.283  1.00 88.38           O  
ANISOU 2204  O   LYS A1140    11707  15303   6570  -2485  -1338   -879       O  
ATOM   2205  CB  LYS A1140      11.324 -10.420 -14.386  1.00 94.41           C  
ANISOU 2205  CB  LYS A1140    11784  16862   7226  -2462  -1534   -221       C  
ATOM   2206  CG  LYS A1140      12.509 -10.601 -13.447  1.00107.42           C  
ANISOU 2206  CG  LYS A1140    13249  18811   8755  -2611  -1679    -45       C  
ATOM   2207  CD  LYS A1140      13.587 -11.471 -14.084  1.00119.85           C  
ANISOU 2207  CD  LYS A1140    14464  20641  10432  -2515  -1741    261       C  
ATOM   2208  CE  LYS A1140      13.961 -10.969 -15.473  1.00129.67           C  
ANISOU 2208  CE  LYS A1140    15640  21803  11828  -2570  -1751    249       C  
ATOM   2209  NZ  LYS A1140      14.919 -11.878 -16.163  1.00132.11           N  
ANISOU 2209  NZ  LYS A1140    15590  22370  12235  -2404  -1781    541       N  
ATOM   2210  N   TYR A1141       8.271 -10.141 -15.273  1.00 87.28           N  
ANISOU 2210  N   TYR A1141    11316  15253   6594  -2039  -1127   -619       N  
ATOM   2211  CA  TYR A1141       7.290  -9.835 -16.309  1.00 87.40           C  
ANISOU 2211  CA  TYR A1141    11449  14922   6837  -1871   -975   -754       C  
ATOM   2212  C   TYR A1141       6.337  -8.723 -15.885  1.00 94.87           C  
ANISOU 2212  C   TYR A1141    12709  15675   7660  -1891   -911  -1067       C  
ATOM   2213  O   TYR A1141       5.973  -7.865 -16.688  1.00101.41           O  
ANISOU 2213  O   TYR A1141    13699  16219   8613  -1877   -873  -1231       O  
ATOM   2214  CB  TYR A1141       6.495 -11.093 -16.673  1.00 81.84           C  
ANISOU 2214  CB  TYR A1141    10619  14176   6301  -1592   -827   -601       C  
ATOM   2215  CG  TYR A1141       5.241 -10.831 -17.480  1.00 77.59           C  
ANISOU 2215  CG  TYR A1141    10206  13334   5940  -1418   -661   -749       C  
ATOM   2216  CD1 TYR A1141       5.304 -10.627 -18.852  1.00 79.77           C  
ANISOU 2216  CD1 TYR A1141    10457  13388   6465  -1358   -631   -750       C  
ATOM   2217  CD2 TYR A1141       3.993 -10.801 -16.871  1.00 72.87           C  
ANISOU 2217  CD2 TYR A1141     9730  12712   5246  -1310   -534   -873       C  
ATOM   2218  CE1 TYR A1141       4.160 -10.391 -19.592  1.00 76.39           C  
ANISOU 2218  CE1 TYR A1141    10131  12706   6190  -1200   -490   -871       C  
ATOM   2219  CE2 TYR A1141       2.844 -10.565 -17.602  1.00 69.67           C  
ANISOU 2219  CE2 TYR A1141     9405  12076   4989  -1143   -387   -990       C  
ATOM   2220  CZ  TYR A1141       2.933 -10.363 -18.962  1.00 71.38           C  
ANISOU 2220  CZ  TYR A1141     9603  12061   5459  -1091   -372   -988       C  
ATOM   2221  OH  TYR A1141       1.790 -10.129 -19.693  1.00 70.94           O  
ANISOU 2221  OH  TYR A1141     9615  11796   5542   -926   -236  -1092       O  
ATOM   2222  N   GLN A1142       5.933  -8.747 -14.620  1.00 95.15           N  
ANISOU 2222  N   GLN A1142    12838  15874   7439  -1906   -900  -1145       N  
ATOM   2223  CA  GLN A1142       4.981  -7.770 -14.106  1.00 95.83           C  
ANISOU 2223  CA  GLN A1142    13225  15817   7370  -1867   -824  -1449       C  
ATOM   2224  C   GLN A1142       5.612  -6.387 -13.970  1.00 88.27           C  
ANISOU 2224  C   GLN A1142    12529  14725   6284  -2114   -974  -1664       C  
ATOM   2225  O   GLN A1142       4.957  -5.370 -14.196  1.00 86.42           O  
ANISOU 2225  O   GLN A1142    12577  14205   6055  -2051   -923  -1919       O  
ATOM   2226  CB  GLN A1142       4.425  -8.230 -12.757  1.00106.28           C  
ANISOU 2226  CB  GLN A1142    14556  17390   8436  -1807   -766  -1456       C  
ATOM   2227  CG  GLN A1142       3.331  -7.341 -12.195  1.00116.48           C  
ANISOU 2227  CG  GLN A1142    16121  18530   9607  -1668   -648  -1745       C  
ATOM   2228  CD  GLN A1142       2.837  -7.815 -10.844  1.00128.74           C  
ANISOU 2228  CD  GLN A1142    17646  20312  10958  -1590   -582  -1710       C  
ATOM   2229  OE1 GLN A1142       1.835  -7.321 -10.328  1.00136.13           O  
ANISOU 2229  OE1 GLN A1142    18747  21197  11780  -1423   -458  -1902       O  
ATOM   2230  NE2 GLN A1142       3.543  -8.777 -10.262  1.00131.22           N  
ANISOU 2230  NE2 GLN A1142    17746  20888  11223  -1695   -665  -1453       N  
ATOM   2231  N   SER A1143       6.890  -6.356 -13.606  1.00 88.91           N  
ANISOU 2231  N   SER A1143    12508  14960   6314  -2359  -1156  -1530       N  
ATOM   2232  CA  SER A1143       7.583  -5.097 -13.363  1.00 98.37           C  
ANISOU 2232  CA  SER A1143    13932  16000   7444  -2609  -1312  -1678       C  
ATOM   2233  C   SER A1143       8.085  -4.452 -14.653  1.00103.41           C  
ANISOU 2233  C   SER A1143    14607  16428   8257  -2756  -1386  -1681       C  
ATOM   2234  O   SER A1143       7.935  -3.246 -14.850  1.00103.62           O  
ANISOU 2234  O   SER A1143    14945  16139   8286  -2839  -1428  -1893       O  
ATOM   2235  CB  SER A1143       8.748  -5.309 -12.393  1.00104.06           C  
ANISOU 2235  CB  SER A1143    14507  17005   8027  -2834  -1475  -1519       C  
ATOM   2236  OG  SER A1143       9.392  -4.083 -12.091  1.00109.38           O  
ANISOU 2236  OG  SER A1143    15410  17531   8620  -3098  -1630  -1660       O  
ATOM   2237  N   LEU A1144       8.678  -5.261 -15.526  1.00106.57           N  
ANISOU 2237  N   LEU A1144    14695  17002   8797  -2773  -1403  -1436       N  
ATOM   2238  CA  LEU A1144       9.264  -4.759 -16.767  1.00104.80           C  
ANISOU 2238  CA  LEU A1144    14444  16641   8735  -2921  -1474  -1390       C  
ATOM   2239  C   LEU A1144       8.211  -4.368 -17.802  1.00 95.45           C  
ANISOU 2239  C   LEU A1144    13425  15059   7783  -2689  -1316  -1528       C  
ATOM   2240  O   LEU A1144       8.117  -3.205 -18.197  1.00 93.51           O  
ANISOU 2240  O   LEU A1144    13469  14518   7544  -2816  -1370  -1707       O  
ATOM   2241  CB  LEU A1144      10.229  -5.787 -17.368  1.00106.18           C  
ANISOU 2241  CB  LEU A1144    14193  17103   9049  -2910  -1507  -1059       C  
ATOM   2242  CG  LEU A1144      11.691  -5.754 -16.909  1.00110.96           C  
ANISOU 2242  CG  LEU A1144    14596  18038   9524  -3210  -1705   -876       C  
ATOM   2243  CD1 LEU A1144      11.826  -6.058 -15.423  1.00117.23           C  
ANISOU 2243  CD1 LEU A1144    15384  19027  10133  -3224  -1741   -859       C  
ATOM   2244  CD2 LEU A1144      12.528  -6.723 -17.734  1.00107.36           C  
ANISOU 2244  CD2 LEU A1144    13729  17873   9189  -3140  -1721   -573       C  
ATOM   2245  N   LEU A1145       7.425  -5.346 -18.240  1.00 89.53           N  
ANISOU 2245  N   LEU A1145    12502  14299   7215  -2361  -1133  -1435       N  
ATOM   2246  CA  LEU A1145       6.415  -5.114 -19.266  1.00 87.48           C  
ANISOU 2246  CA  LEU A1145    12344  13714   7180  -2129   -982  -1530       C  
ATOM   2247  C   LEU A1145       5.210  -4.359 -18.711  1.00 93.41           C  
ANISOU 2247  C   LEU A1145    13425  14250   7817  -1986   -890  -1818       C  
ATOM   2248  O   LEU A1145       4.327  -4.950 -18.089  1.00 93.59           O  
ANISOU 2248  O   LEU A1145    13410  14376   7774  -1771   -758  -1844       O  
ATOM   2249  CB  LEU A1145       5.964  -6.443 -19.877  1.00 83.80           C  
ANISOU 2249  CB  LEU A1145    11595  13323   6923  -1853   -835  -1333       C  
ATOM   2250  CG  LEU A1145       5.879  -6.510 -21.404  1.00 83.39           C  
ANISOU 2250  CG  LEU A1145    11458  13075   7153  -1749   -773  -1258       C  
ATOM   2251  CD1 LEU A1145       5.359  -7.869 -21.849  1.00 79.90           C  
ANISOU 2251  CD1 LEU A1145    10788  12696   6876  -1484   -639  -1089       C  
ATOM   2252  CD2 LEU A1145       5.010  -5.393 -21.960  1.00 87.72           C  
ANISOU 2252  CD2 LEU A1145    12293  13267   7770  -1688   -716  -1484       C  
ATOM   2253  N   THR A1146       5.181  -3.051 -18.944  1.00100.31           N  
ANISOU 2253  N   THR A1146    14626  14833   8656  -2101   -961  -2025       N  
ATOM   2254  CA  THR A1146       4.054  -2.224 -18.530  1.00108.30           C  
ANISOU 2254  CA  THR A1146    15983  15606   9559  -1917   -873  -2316       C  
ATOM   2255  C   THR A1146       3.012  -2.172 -19.642  1.00108.23           C  
ANISOU 2255  C   THR A1146    15980  15345   9797  -1619   -712  -2344       C  
ATOM   2256  O   THR A1146       3.132  -2.875 -20.644  1.00106.90           O  
ANISOU 2256  O   THR A1146    15549  15202   9867  -1565   -665  -2142       O  
ATOM   2257  CB  THR A1146       4.501  -0.790 -18.191  1.00115.23           C  
ANISOU 2257  CB  THR A1146    17280  16245  10258  -2169  -1045  -2544       C  
ATOM   2258  OG1 THR A1146       5.058  -0.171 -19.357  1.00121.21           O  
ANISOU 2258  OG1 THR A1146    18098  16757  11198  -2341  -1144  -2484       O  
ATOM   2259  CG2 THR A1146       5.544  -0.804 -17.084  1.00114.58           C  
ANISOU 2259  CG2 THR A1146    17157  16406   9974  -2453  -1213  -2487       C  
ATOM   2260  N   LYS A1147       1.989  -1.343 -19.463  1.00111.69           N  
ANISOU 2260  N   LYS A1147    16722  15551  10163  -1412   -631  -2598       N  
ATOM   2261  CA  LYS A1147       0.959  -1.184 -20.483  1.00110.59           C  
ANISOU 2261  CA  LYS A1147    16602  15184  10235  -1121   -489  -2632       C  
ATOM   2262  C   LYS A1147       1.443  -0.281 -21.612  1.00112.41           C  
ANISOU 2262  C   LYS A1147    17010  15077  10626  -1264   -601  -2638       C  
ATOM   2263  O   LYS A1147       1.142  -0.520 -22.781  1.00115.87           O  
ANISOU 2263  O   LYS A1147    17308  15412  11305  -1146   -531  -2523       O  
ATOM   2264  CB  LYS A1147      -0.336  -0.639 -19.875  1.00110.39           C  
ANISOU 2264  CB  LYS A1147    16809  15075  10059   -801   -353  -2887       C  
ATOM   2265  CG  LYS A1147      -1.034  -1.612 -18.936  1.00109.34           C  
ANISOU 2265  CG  LYS A1147    16450  15304   9789   -625   -205  -2847       C  
ATOM   2266  CD  LYS A1147      -2.346  -1.044 -18.420  1.00108.54           C  
ANISOU 2266  CD  LYS A1147    16542  15168   9529   -279    -53  -3091       C  
ATOM   2267  CE  LYS A1147      -3.046  -2.023 -17.487  1.00102.20           C  
ANISOU 2267  CE  LYS A1147    15490  14770   8572   -135     98  -3024       C  
ATOM   2268  NZ  LYS A1147      -2.239  -2.318 -16.270  1.00 97.39           N  
ANISOU 2268  NZ  LYS A1147    14882  14408   7715   -375     -2  -3010       N  
ATOM   2269  N   ASN A1148       2.199   0.754 -21.254  1.00110.29           N  
ANISOU 2269  N   ASN A1148    17057  14640  10207  -1541   -783  -2764       N  
ATOM   2270  CA  ASN A1148       2.775   1.658 -22.243  1.00109.99           C  
ANISOU 2270  CA  ASN A1148    17211  14291  10290  -1750   -919  -2748       C  
ATOM   2271  C   ASN A1148       3.747   0.937 -23.167  1.00107.84           C  
ANISOU 2271  C   ASN A1148    16567  14200  10208  -1959   -969  -2445       C  
ATOM   2272  O   ASN A1148       3.678   1.082 -24.388  1.00112.09           O  
ANISOU 2272  O   ASN A1148    17062  14569  10956  -1923   -948  -2353       O  
ATOM   2273  CB  ASN A1148       3.475   2.834 -21.561  1.00116.35           C  
ANISOU 2273  CB  ASN A1148    18427  14907  10874  -2066  -1130  -2919       C  
ATOM   2274  CG  ASN A1148       2.502   3.787 -20.899  1.00127.21           C  
ANISOU 2274  CG  ASN A1148    20147  16012  12174  -1764  -1071  -3191       C  
ATOM   2275  OD1 ASN A1148       1.984   4.703 -21.536  1.00132.32           O  
ANISOU 2275  OD1 ASN A1148    21054  16286  12935  -1618  -1064  -3291       O  
ATOM   2276  ND2 ASN A1148       2.250   3.576 -19.612  1.00131.52           N  
ANISOU 2276  ND2 ASN A1148    20683  16766  12522  -1658  -1027  -3305       N  
ATOM   2277  N   LYS A1149       4.648   0.157 -22.577  1.00 99.76           N  
ANISOU 2277  N   LYS A1149    15273  13537   9096  -2156  -1034  -2289       N  
ATOM   2278  CA  LYS A1149       5.613  -0.619 -23.346  1.00 92.75           C  
ANISOU 2278  CA  LYS A1149    14006  12881   8356  -2306  -1073  -2000       C  
ATOM   2279  C   LYS A1149       4.911  -1.628 -24.252  1.00 83.26           C  
ANISOU 2279  C   LYS A1149    12521  11720   7395  -1981   -885  -1867       C  
ATOM   2280  O   LYS A1149       5.341  -1.865 -25.380  1.00 86.95           O  
ANISOU 2280  O   LYS A1149    12807  12188   8040  -2018   -886  -1700       O  
ATOM   2281  CB  LYS A1149       6.590  -1.338 -22.412  1.00 65.83           C  
ANISOU 2281  CB  LYS A1149    10355   9875   4783  -2503  -1164  -1863       C  
ATOM   2282  N   ALA A1150       3.826  -2.212 -23.754  1.00 78.13           N  
ANISOU 2282  N   ALA A1150    11838  11117   6732  -1678   -727  -1941       N  
ATOM   2283  CA  ALA A1150       3.045  -3.168 -24.530  1.00 74.56           C  
ANISOU 2283  CA  ALA A1150    11151  10695   6485  -1392   -560  -1827       C  
ATOM   2284  C   ALA A1150       2.381  -2.482 -25.719  1.00 83.38           C  
ANISOU 2284  C   ALA A1150    12411  11492   7779  -1262   -508  -1892       C  
ATOM   2285  O   ALA A1150       2.329  -3.036 -26.819  1.00 85.70           O  
ANISOU 2285  O   ALA A1150    12509  11781   8271  -1178   -450  -1746       O  
ATOM   2286  CB  ALA A1150       2.002  -3.840 -23.651  1.00 68.52           C  
ANISOU 2286  CB  ALA A1150    10336  10068   5632  -1148   -420  -1886       C  
ATOM   2287  N   ARG A1151       1.873  -1.275 -25.491  1.00 84.11           N  
ANISOU 2287  N   ARG A1151    12862  11311   7785  -1232   -534  -2116       N  
ATOM   2288  CA  ARG A1151       1.259  -0.492 -26.557  1.00 80.35           C  
ANISOU 2288  CA  ARG A1151    12565  10508   7456  -1104   -504  -2181       C  
ATOM   2289  C   ARG A1151       2.305  -0.079 -27.589  1.00 79.99           C  
ANISOU 2289  C   ARG A1151    12512  10359   7521  -1381   -637  -2042       C  
ATOM   2290  O   ARG A1151       2.008   0.037 -28.780  1.00 83.67           O  
ANISOU 2290  O   ARG A1151    12949  10673   8167  -1292   -596  -1974       O  
ATOM   2291  CB  ARG A1151       0.541   0.732 -25.982  1.00 86.04           C  
ANISOU 2291  CB  ARG A1151    13712  10947   8033   -985   -516  -2457       C  
ATOM   2292  CG  ARG A1151      -0.764   0.390 -25.274  1.00 93.18           C  
ANISOU 2292  CG  ARG A1151    14595  11956   8854   -623   -341  -2587       C  
ATOM   2293  CD  ARG A1151      -1.289   1.546 -24.436  1.00108.31           C  
ANISOU 2293  CD  ARG A1151    16936  13659  10560   -502   -359  -2880       C  
ATOM   2294  NE  ARG A1151      -1.547   2.744 -25.229  1.00122.68           N  
ANISOU 2294  NE  ARG A1151    19098  15059  12454   -433   -417  -2990       N  
ATOM   2295  CZ  ARG A1151      -0.780   3.830 -25.212  1.00136.31           C  
ANISOU 2295  CZ  ARG A1151    21198  16490  14106   -696   -605  -3083       C  
ATOM   2296  NH1 ARG A1151       0.296   3.873 -24.438  1.00138.31           N  
ANISOU 2296  NH1 ARG A1151    21504  16849  14199  -1055   -754  -3082       N  
ATOM   2297  NH2 ARG A1151      -1.091   4.875 -25.966  1.00143.25           N  
ANISOU 2297  NH2 ARG A1151    22403  16967  15060   -614   -656  -3165       N  
ATOM   2298  N   VAL A1152       3.533   0.133 -27.124  1.00 78.98           N  
ANISOU 2298  N   VAL A1152    12391  10348   7269  -1730   -797  -1987       N  
ATOM   2299  CA  VAL A1152       4.651   0.408 -28.018  1.00 80.66           C  
ANISOU 2299  CA  VAL A1152    12525  10568   7556  -2034   -924  -1815       C  
ATOM   2300  C   VAL A1152       4.947  -0.821 -28.873  1.00 83.87           C  
ANISOU 2300  C   VAL A1152    12499  11238   8131  -1939   -831  -1576       C  
ATOM   2301  O   VAL A1152       5.197  -0.706 -30.073  1.00 93.62           O  
ANISOU 2301  O   VAL A1152    13657  12407   9506  -1980   -834  -1457       O  
ATOM   2302  CB  VAL A1152       5.912   0.838 -27.238  1.00 84.41           C  
ANISOU 2302  CB  VAL A1152    13057  11182   7831  -2449  -1123  -1791       C  
ATOM   2303  CG1 VAL A1152       7.139   0.809 -28.134  1.00 63.11           C  
ANISOU 2303  CG1 VAL A1152    10138   8645   5198  -2753  -1230  -1551       C  
ATOM   2304  CG2 VAL A1152       5.716   2.224 -26.644  1.00 66.44           C  
ANISOU 2304  CG2 VAL A1152    11287   8562   5395  -2591  -1249  -2031       C  
ATOM   2305  N   ILE A1153       4.905  -1.997 -28.250  1.00 75.51           N  
ANISOU 2305  N   ILE A1153    11181  10465   7044  -1804   -752  -1508       N  
ATOM   2306  CA  ILE A1153       5.082  -3.256 -28.971  1.00 72.29           C  
ANISOU 2306  CA  ILE A1153    10413  10272   6782  -1663   -661  -1305       C  
ATOM   2307  C   ILE A1153       4.016  -3.419 -30.054  1.00 72.76           C  
ANISOU 2307  C   ILE A1153    10477  10133   7035  -1393   -525  -1320       C  
ATOM   2308  O   ILE A1153       4.327  -3.765 -31.195  1.00 66.92           O  
ANISOU 2308  O   ILE A1153     9574   9421   6433  -1376   -502  -1180       O  
ATOM   2309  CB  ILE A1153       5.040  -4.471 -28.020  1.00 69.68           C  
ANISOU 2309  CB  ILE A1153     9875  10220   6378  -1539   -604  -1244       C  
ATOM   2310  CG1 ILE A1153       6.220  -4.427 -27.049  1.00 78.31           C  
ANISOU 2310  CG1 ILE A1153    10904  11568   7280  -1809   -750  -1185       C  
ATOM   2311  CG2 ILE A1153       5.061  -5.773 -28.807  1.00 62.88           C  
ANISOU 2311  CG2 ILE A1153     8716   9501   5672  -1350   -509  -1059       C  
ATOM   2312  CD1 ILE A1153       7.569  -4.414 -27.732  1.00 86.91           C  
ANISOU 2312  CD1 ILE A1153    11792  12841   8390  -2037   -858   -993       C  
ATOM   2313  N   ILE A1154       2.763  -3.160 -29.689  1.00 77.76           N  
ANISOU 2313  N   ILE A1154    11289  10595   7661  -1179   -435  -1488       N  
ATOM   2314  CA  ILE A1154       1.651  -3.225 -30.633  1.00 77.89           C  
ANISOU 2314  CA  ILE A1154    11316  10442   7838   -925   -315  -1509       C  
ATOM   2315  C   ILE A1154       1.859  -2.266 -31.801  1.00 78.85           C  
ANISOU 2315  C   ILE A1154    11578  10322   8059  -1017   -376  -1498       C  
ATOM   2316  O   ILE A1154       1.692  -2.641 -32.966  1.00 80.09           O  
ANISOU 2316  O   ILE A1154    11599  10461   8369   -928   -321  -1390       O  
ATOM   2317  CB  ILE A1154       0.311  -2.902 -29.944  1.00 80.47           C  
ANISOU 2317  CB  ILE A1154    11816  10659   8099   -688   -221  -1698       C  
ATOM   2318  CG1 ILE A1154      -0.016  -3.969 -28.901  1.00 82.85           C  
ANISOU 2318  CG1 ILE A1154    11946  11225   8307   -593   -144  -1676       C  
ATOM   2319  CG2 ILE A1154      -0.810  -2.814 -30.965  1.00 79.25           C  
ANISOU 2319  CG2 ILE A1154    11669  10343   8098   -444   -118  -1712       C  
ATOM   2320  CD1 ILE A1154      -0.086  -5.362 -29.474  1.00 84.96           C  
ANISOU 2320  CD1 ILE A1154    11913  11661   8706   -505    -70  -1486       C  
ATOM   2321  N   LEU A1155       2.233  -1.030 -31.480  1.00 77.23           N  
ANISOU 2321  N   LEU A1155    11664   9926   7752  -1211   -499  -1605       N  
ATOM   2322  CA  LEU A1155       2.507  -0.019 -32.495  1.00 71.18           C  
ANISOU 2322  CA  LEU A1155    11077   8911   7056  -1349   -584  -1580       C  
ATOM   2323  C   LEU A1155       3.602  -0.483 -33.451  1.00 68.52           C  
ANISOU 2323  C   LEU A1155    10470   8767   6797  -1546   -626  -1350       C  
ATOM   2324  O   LEU A1155       3.486  -0.317 -34.665  1.00 73.76           O  
ANISOU 2324  O   LEU A1155    11110   9330   7587  -1515   -605  -1265       O  
ATOM   2325  CB  LEU A1155       2.906   1.307 -31.846  1.00 69.34           C  
ANISOU 2325  CB  LEU A1155    11227   8449   6672  -1589   -742  -1719       C  
ATOM   2326  CG  LEU A1155       3.229   2.446 -32.815  1.00 67.74           C  
ANISOU 2326  CG  LEU A1155    11268   7951   6521  -1782   -859  -1682       C  
ATOM   2327  CD1 LEU A1155       2.029   2.748 -33.699  1.00 64.62           C  
ANISOU 2327  CD1 LEU A1155    10990   7294   6269  -1463   -759  -1733       C  
ATOM   2328  CD2 LEU A1155       3.675   3.694 -32.069  1.00 62.02           C  
ANISOU 2328  CD2 LEU A1155    10960   6981   5624  -2057  -1040  -1821       C  
ATOM   2329  N   MET A1156       4.657  -1.073 -32.897  1.00 62.19           N  
ANISOU 2329  N   MET A1156     9454   8270   5904  -1730   -682  -1243       N  
ATOM   2330  CA  MET A1156       5.766  -1.577 -33.701  1.00 60.48           C  
ANISOU 2330  CA  MET A1156     8944   8308   5729  -1884   -713  -1021       C  
ATOM   2331  C   MET A1156       5.331  -2.721 -34.614  1.00 66.42           C  
ANISOU 2331  C   MET A1156     9437   9165   6635  -1599   -564   -921       C  
ATOM   2332  O   MET A1156       5.740  -2.786 -35.773  1.00 72.13           O  
ANISOU 2332  O   MET A1156    10032   9936   7437  -1633   -556   -790       O  
ATOM   2333  CB  MET A1156       6.929  -2.019 -32.811  1.00 57.07           C  
ANISOU 2333  CB  MET A1156     8318   8217   5150  -2092   -801   -928       C  
ATOM   2334  CG  MET A1156       7.723  -0.870 -32.208  1.00 56.70           C  
ANISOU 2334  CG  MET A1156     8480   8123   4938  -2486   -989   -964       C  
ATOM   2335  SD  MET A1156       9.116  -1.436 -31.211  1.00181.10           S  
ANISOU 2335  SD  MET A1156    23956  24346  20509  -2737  -1103   -824       S  
ATOM   2336  CE  MET A1156       9.860   0.126 -30.745  1.00138.92           C  
ANISOU 2336  CE  MET A1156    18938  18863  14984  -3248  -1344   -883       C  
ATOM   2337  N   VAL A1157       4.502  -3.618 -34.088  1.00 61.62           N  
ANISOU 2337  N   VAL A1157     8763   8596   6053  -1336   -454   -981       N  
ATOM   2338  CA  VAL A1157       3.987  -4.731 -34.879  1.00 56.22           C  
ANISOU 2338  CA  VAL A1157     7884   7974   5502  -1081   -328   -904       C  
ATOM   2339  C   VAL A1157       3.133  -4.230 -36.043  1.00 60.97           C  
ANISOU 2339  C   VAL A1157     8603   8331   6234   -966   -276   -939       C  
ATOM   2340  O   VAL A1157       3.285  -4.690 -37.174  1.00 67.56           O  
ANISOU 2340  O   VAL A1157     9293   9215   7161   -907   -235   -829       O  
ATOM   2341  CB  VAL A1157       3.171  -5.717 -34.020  1.00 49.82           C  
ANISOU 2341  CB  VAL A1157     7019   7231   4679   -867   -237   -955       C  
ATOM   2342  CG1 VAL A1157       2.461  -6.735 -34.901  1.00 45.95           C  
ANISOU 2342  CG1 VAL A1157     6399   6734   4325   -633   -126   -893       C  
ATOM   2343  CG2 VAL A1157       4.075  -6.415 -33.019  1.00 45.63           C  
ANISOU 2343  CG2 VAL A1157     6336   6973   4031   -953   -287   -876       C  
ATOM   2344  N   TRP A1158       2.245  -3.280 -35.767  1.00 59.30           N  
ANISOU 2344  N   TRP A1158     8656   7862   6014   -918   -280  -1093       N  
ATOM   2345  CA  TRP A1158       1.418  -2.705 -36.825  1.00 62.78           C  
ANISOU 2345  CA  TRP A1158     9220   8068   6565   -798   -245  -1119       C  
ATOM   2346  C   TRP A1158       2.243  -1.909 -37.835  1.00 67.21           C  
ANISOU 2346  C   TRP A1158     9834   8552   7150  -1017   -337  -1018       C  
ATOM   2347  O   TRP A1158       1.875  -1.815 -39.006  1.00 72.91           O  
ANISOU 2347  O   TRP A1158    10545   9184   7974   -936   -303   -960       O  
ATOM   2348  CB  TRP A1158       0.294  -1.843 -36.243  1.00 68.90           C  
ANISOU 2348  CB  TRP A1158    10272   8600   7308   -652   -229  -1306       C  
ATOM   2349  CG  TRP A1158      -0.850  -2.651 -35.713  1.00 74.36           C  
ANISOU 2349  CG  TRP A1158    10867   9380   8008   -384   -103  -1372       C  
ATOM   2350  CD1 TRP A1158      -1.046  -3.045 -34.422  1.00 80.15           C  
ANISOU 2350  CD1 TRP A1158    11582  10244   8627   -342    -72  -1450       C  
ATOM   2351  CD2 TRP A1158      -1.953  -3.174 -36.464  1.00 72.87           C  
ANISOU 2351  CD2 TRP A1158    10573   9186   7930   -148      2  -1347       C  
ATOM   2352  NE1 TRP A1158      -2.204  -3.777 -34.321  1.00 78.77           N  
ANISOU 2352  NE1 TRP A1158    11292  10151   8485   -105     48  -1465       N  
ATOM   2353  CE2 TRP A1158      -2.779  -3.871 -35.561  1.00 75.04           C  
ANISOU 2353  CE2 TRP A1158    10762   9598   8151     10     91  -1403       C  
ATOM   2354  CE3 TRP A1158      -2.322  -3.118 -37.811  1.00 70.39           C  
ANISOU 2354  CE3 TRP A1158    10224   8782   7740    -74     22  -1273       C  
ATOM   2355  CZ2 TRP A1158      -3.952  -4.507 -35.960  1.00 75.62           C  
ANISOU 2355  CZ2 TRP A1158    10712   9729   8293    216    191  -1381       C  
ATOM   2356  CZ3 TRP A1158      -3.487  -3.750 -38.206  1.00 70.04           C  
ANISOU 2356  CZ3 TRP A1158    10064   8786   7764    144    120  -1264       C  
ATOM   2357  CH2 TRP A1158      -4.287  -4.436 -37.284  1.00 72.91           C  
ANISOU 2357  CH2 TRP A1158    10337   9293   8072    276    200  -1314       C  
ATOM   2358  N   ILE A1159       3.358  -1.342 -37.382  1.00 62.68           N  
ANISOU 2358  N   ILE A1159     9312   8035   6469  -1316   -461   -982       N  
ATOM   2359  CA  ILE A1159       4.261  -0.624 -38.279  1.00 61.10           C  
ANISOU 2359  CA  ILE A1159     9133   7818   6264  -1584   -560   -852       C  
ATOM   2360  C   ILE A1159       4.979  -1.589 -39.218  1.00 66.54           C  
ANISOU 2360  C   ILE A1159     9472   8812   6999  -1575   -503   -661       C  
ATOM   2361  O   ILE A1159       5.047  -1.357 -40.426  1.00 70.96           O  
ANISOU 2361  O   ILE A1159    10003   9338   7621  -1597   -494   -563       O  
ATOM   2362  CB  ILE A1159       5.290   0.222 -37.503  1.00 58.05           C  
ANISOU 2362  CB  ILE A1159     8883   7445   5728  -1953   -724   -849       C  
ATOM   2363  CG1 ILE A1159       4.635   1.503 -36.983  1.00 59.26           C  
ANISOU 2363  CG1 ILE A1159     9482   7199   5837  -1989   -807  -1033       C  
ATOM   2364  CG2 ILE A1159       6.472   0.580 -38.390  1.00 53.40           C  
ANISOU 2364  CG2 ILE A1159     8173   7003   5112  -2270   -816   -646       C  
ATOM   2365  CD1 ILE A1159       5.577   2.401 -36.216  1.00 65.67           C  
ANISOU 2365  CD1 ILE A1159    10496   7970   6487  -2380   -991  -1052       C  
ATOM   2366  N   VAL A1160       5.508  -2.672 -38.658  1.00 61.88           N  
ANISOU 2366  N   VAL A1160     8627   8519   6365  -1523   -465   -610       N  
ATOM   2367  CA  VAL A1160       6.153  -3.711 -39.454  1.00 58.13           C  
ANISOU 2367  CA  VAL A1160     7834   8335   5918  -1441   -400   -452       C  
ATOM   2368  C   VAL A1160       5.166  -4.316 -40.450  1.00 62.62           C  
ANISOU 2368  C   VAL A1160     8381   8793   6619  -1155   -278   -470       C  
ATOM   2369  O   VAL A1160       5.504  -4.550 -41.612  1.00 66.85           O  
ANISOU 2369  O   VAL A1160     8785   9428   7187  -1132   -244   -360       O  
ATOM   2370  CB  VAL A1160       6.739  -4.824 -38.562  1.00 49.24           C  
ANISOU 2370  CB  VAL A1160     6483   7502   4722  -1370   -381   -409       C  
ATOM   2371  CG1 VAL A1160       7.229  -5.988 -39.406  1.00 44.95           C  
ANISOU 2371  CG1 VAL A1160     5658   7210   4212  -1193   -298   -275       C  
ATOM   2372  CG2 VAL A1160       7.867  -4.275 -37.706  1.00 48.29           C  
ANISOU 2372  CG2 VAL A1160     6332   7564   4452  -1680   -514   -357       C  
ATOM   2373  N   SER A1161       3.941  -4.552 -39.993  1.00 63.40           N  
ANISOU 2373  N   SER A1161     8603   8710   6776   -948   -216   -605       N  
ATOM   2374  CA  SER A1161       2.896  -5.095 -40.851  1.00 66.85           C  
ANISOU 2374  CA  SER A1161     9028   9046   7327   -706   -117   -625       C  
ATOM   2375  C   SER A1161       2.532  -4.111 -41.958  1.00 73.92           C  
ANISOU 2375  C   SER A1161    10063   9744   8280   -747   -139   -613       C  
ATOM   2376  O   SER A1161       2.225  -4.512 -43.079  1.00 82.55           O  
ANISOU 2376  O   SER A1161    11079  10846   9439   -634    -83   -558       O  
ATOM   2377  CB  SER A1161       1.655  -5.449 -40.030  1.00 65.90           C  
ANISOU 2377  CB  SER A1161     8993   8815   7232   -516    -57   -756       C  
ATOM   2378  OG  SER A1161       1.956  -6.416 -39.041  1.00 65.14           O  
ANISOU 2378  OG  SER A1161     8774   8898   7078   -481    -40   -746       O  
ATOM   2379  N   GLY A1162       2.568  -2.822 -41.635  1.00 71.18           N  
ANISOU 2379  N   GLY A1162     9945   9205   7896   -913   -229   -664       N  
ATOM   2380  CA  GLY A1162       2.274  -1.785 -42.607  1.00 69.14           C  
ANISOU 2380  CA  GLY A1162     9861   8728   7682   -968   -272   -639       C  
ATOM   2381  C   GLY A1162       3.366  -1.659 -43.651  1.00 70.60           C  
ANISOU 2381  C   GLY A1162     9912   9071   7840  -1172   -311   -460       C  
ATOM   2382  O   GLY A1162       3.098  -1.340 -44.809  1.00 67.58           O  
ANISOU 2382  O   GLY A1162     9561   8609   7509  -1151   -303   -392       O  
ATOM   2383  N   LEU A1163       4.602  -1.919 -43.235  1.00 75.68           N  
ANISOU 2383  N   LEU A1163    10389   9977   8390  -1368   -354   -373       N  
ATOM   2384  CA  LEU A1163       5.755  -1.831 -44.125  1.00 76.09           C  
ANISOU 2384  CA  LEU A1163    10262  10267   8383  -1573   -387   -186       C  
ATOM   2385  C   LEU A1163       5.813  -2.994 -45.110  1.00 76.48           C  
ANISOU 2385  C   LEU A1163    10047  10545   8466  -1352   -265   -109       C  
ATOM   2386  O   LEU A1163       6.484  -2.912 -46.137  1.00 85.68           O  
ANISOU 2386  O   LEU A1163    11078  11886   9590  -1448   -261     35       O  
ATOM   2387  CB  LEU A1163       7.053  -1.774 -43.315  1.00 75.92           C  
ANISOU 2387  CB  LEU A1163    10108  10509   8231  -1839   -472   -107       C  
ATOM   2388  CG  LEU A1163       7.682  -0.400 -43.070  1.00 79.73           C  
ANISOU 2388  CG  LEU A1163    10788  10882   8624  -2243   -637    -57       C  
ATOM   2389  CD1 LEU A1163       6.684   0.570 -42.456  1.00 82.12           C  
ANISOU 2389  CD1 LEU A1163    11502  10733   8965  -2231   -701   -238       C  
ATOM   2390  CD2 LEU A1163       8.909  -0.539 -42.183  1.00 80.64           C  
ANISOU 2390  CD2 LEU A1163    10725  11316   8598  -2491   -720     21       C  
ATOM   2391  N   THR A1164       5.112  -4.078 -44.792  1.00 69.12           N  
ANISOU 2391  N   THR A1164     9056   9614   7594  -1066   -172   -203       N  
ATOM   2392  CA  THR A1164       5.104  -5.253 -45.656  1.00 70.53           C  
ANISOU 2392  CA  THR A1164     9041   9962   7795   -844    -68   -157       C  
ATOM   2393  C   THR A1164       3.789  -5.374 -46.420  1.00 72.72           C  
ANISOU 2393  C   THR A1164     9439  10014   8176   -648    -11   -230       C  
ATOM   2394  O   THR A1164       3.575  -6.340 -47.155  1.00 65.76           O  
ANISOU 2394  O   THR A1164     8455   9217   7316   -462     65   -219       O  
ATOM   2395  CB  THR A1164       5.352  -6.547 -44.857  1.00 68.04           C  
ANISOU 2395  CB  THR A1164     8573   9822   7457   -674    -18   -182       C  
ATOM   2396  OG1 THR A1164       4.263  -6.773 -43.954  1.00 66.00           O  
ANISOU 2396  OG1 THR A1164     8457   9358   7261   -555     -3   -319       O  
ATOM   2397  CG2 THR A1164       6.645  -6.445 -44.067  1.00 74.12           C  
ANISOU 2397  CG2 THR A1164     9198  10851   8114   -856    -83    -98       C  
ATOM   2398  N   SER A1165       2.914  -4.389 -46.248  1.00 78.57           N  
ANISOU 2398  N   SER A1165    10408  10474   8971   -684    -55   -305       N  
ATOM   2399  CA  SER A1165       1.605  -4.411 -46.891  1.00 79.14           C  
ANISOU 2399  CA  SER A1165    10580  10357   9133   -498    -11   -365       C  
ATOM   2400  C   SER A1165       1.380  -3.194 -47.781  1.00 80.81           C  
ANISOU 2400  C   SER A1165    10951  10392   9362   -599    -69   -311       C  
ATOM   2401  O   SER A1165       1.522  -3.276 -48.999  1.00 89.28           O  
ANISOU 2401  O   SER A1165    11953  11539  10430   -598    -50   -215       O  
ATOM   2402  CB  SER A1165       0.493  -4.502 -45.846  1.00 82.47           C  
ANISOU 2402  CB  SER A1165    11113  10622   9599   -355      8   -508       C  
ATOM   2403  OG  SER A1165       0.505  -3.376 -44.987  1.00 88.68           O  
ANISOU 2403  OG  SER A1165    12093  11243  10358   -474    -65   -572       O  
ATOM   2404  N   PHE A1166       1.027  -2.068 -47.170  1.00 75.70           N  
ANISOU 2404  N   PHE A1166    10537   9502   8723   -675   -142   -374       N  
ATOM   2405  CA  PHE A1166       0.716  -0.857 -47.923  1.00 76.54           C  
ANISOU 2405  CA  PHE A1166    10852   9381   8850   -748   -213   -324       C  
ATOM   2406  C   PHE A1166       1.930  -0.268 -48.637  1.00 81.01           C  
ANISOU 2406  C   PHE A1166    11392  10044   9343  -1043   -285   -155       C  
ATOM   2407  O   PHE A1166       1.821   0.209 -49.767  1.00 83.99           O  
ANISOU 2407  O   PHE A1166    11816  10366   9728  -1082   -307    -50       O  
ATOM   2408  CB  PHE A1166       0.068   0.195 -47.019  1.00 70.47           C  
ANISOU 2408  CB  PHE A1166    10382   8302   8092   -726   -279   -448       C  
ATOM   2409  CG  PHE A1166      -1.401  -0.021 -46.802  1.00 69.42           C  
ANISOU 2409  CG  PHE A1166    10298   8051   8028   -410   -211   -572       C  
ATOM   2410  CD1 PHE A1166      -1.850  -0.938 -45.867  1.00 68.97           C  
ANISOU 2410  CD1 PHE A1166    10119   8115   7972   -257   -131   -679       C  
ATOM   2411  CD2 PHE A1166      -2.334   0.690 -47.537  1.00 74.47           C  
ANISOU 2411  CD2 PHE A1166    11092   8485   8719   -270   -230   -562       C  
ATOM   2412  CE1 PHE A1166      -3.202  -1.140 -45.669  1.00 69.92           C  
ANISOU 2412  CE1 PHE A1166    10250   8180   8136      8    -68   -770       C  
ATOM   2413  CE2 PHE A1166      -3.687   0.493 -47.342  1.00 75.96           C  
ANISOU 2413  CE2 PHE A1166    11283   8623   8954     25   -166   -658       C  
ATOM   2414  CZ  PHE A1166      -4.122  -0.424 -46.407  1.00 72.60           C  
ANISOU 2414  CZ  PHE A1166    10714   8347   8522    153    -83   -760       C  
ATOM   2415  N   LEU A1167       3.083  -0.311 -47.981  1.00 81.43           N  
ANISOU 2415  N   LEU A1167    11353  10273   9312  -1262   -327   -113       N  
ATOM   2416  CA  LEU A1167       4.302   0.254 -48.555  1.00 82.58           C  
ANISOU 2416  CA  LEU A1167    11440  10572   9365  -1584   -402     68       C  
ATOM   2417  C   LEU A1167       4.730  -0.383 -49.888  1.00 83.60           C  
ANISOU 2417  C   LEU A1167    11315  10988   9463  -1546   -324    213       C  
ATOM   2418  O   LEU A1167       4.939   0.333 -50.864  1.00 89.27           O  
ANISOU 2418  O   LEU A1167    12088  11681  10148  -1704   -371    350       O  
ATOM   2419  CB  LEU A1167       5.451   0.246 -47.539  1.00 78.23           C  
ANISOU 2419  CB  LEU A1167    10794  10217   8713  -1826   -464     93       C  
ATOM   2420  CG  LEU A1167       6.780   0.814 -48.037  1.00 73.19           C  
ANISOU 2420  CG  LEU A1167    10050   9806   7954  -2202   -551    303       C  
ATOM   2421  CD1 LEU A1167       6.621   2.271 -48.440  1.00 68.69           C  
ANISOU 2421  CD1 LEU A1167     9812   8908   7380  -2457   -687    366       C  
ATOM   2422  CD2 LEU A1167       7.853   0.660 -46.973  1.00 77.69           C  
ANISOU 2422  CD2 LEU A1167    10480  10621   8417  -2415   -610    328       C  
ATOM   2423  N   PRO A1168       4.858  -1.723 -49.944  1.00 76.92           N  
ANISOU 2423  N   PRO A1168    10210  10404   8611  -1331   -208    185       N  
ATOM   2424  CA  PRO A1168       5.292  -2.273 -51.233  1.00 74.21           C  
ANISOU 2424  CA  PRO A1168     9659  10327   8212  -1280   -135    306       C  
ATOM   2425  C   PRO A1168       4.181  -2.263 -52.278  1.00 81.66           C  
ANISOU 2425  C   PRO A1168    10709  11091   9225  -1100    -97    280       C  
ATOM   2426  O   PRO A1168       4.462  -2.110 -53.467  1.00 90.47           O  
ANISOU 2426  O   PRO A1168    11759  12335  10282  -1154    -83    406       O  
ATOM   2427  CB  PRO A1168       5.665  -3.723 -50.892  1.00 67.83           C  
ANISOU 2427  CB  PRO A1168     8607   9788   7376  -1062    -34    256       C  
ATOM   2428  CG  PRO A1168       5.747  -3.780 -49.397  1.00 71.65           C  
ANISOU 2428  CG  PRO A1168     9135  10212   7879  -1096    -75    163       C  
ATOM   2429  CD  PRO A1168       4.758  -2.775 -48.919  1.00 73.69           C  
ANISOU 2429  CD  PRO A1168     9696  10082   8222  -1148   -148     64       C  
ATOM   2430  N   ILE A1169       2.937  -2.424 -51.838  1.00 80.14           N  
ANISOU 2430  N   ILE A1169    10664  10643   9143   -894    -83    130       N  
ATOM   2431  CA  ILE A1169       1.815  -2.542 -52.764  1.00 79.01           C  
ANISOU 2431  CA  ILE A1169    10588  10372   9061   -708    -50    105       C  
ATOM   2432  C   ILE A1169       1.414  -1.216 -53.406  1.00 85.18           C  
ANISOU 2432  C   ILE A1169    11582  10923   9860   -823   -137    188       C  
ATOM   2433  O   ILE A1169       1.285  -1.130 -54.628  1.00 90.37           O  
ANISOU 2433  O   ILE A1169    12214  11633  10489   -815   -129    285       O  
ATOM   2434  CB  ILE A1169       0.592  -3.199 -52.096  1.00 71.75           C  
ANISOU 2434  CB  ILE A1169     9715   9311   8235   -459     -7    -59       C  
ATOM   2435  CG1 ILE A1169       0.896  -4.662 -51.774  1.00 66.54           C  
ANISOU 2435  CG1 ILE A1169     8864   8864   7552   -327     76   -114       C  
ATOM   2436  CG2 ILE A1169      -0.625  -3.107 -53.002  1.00 73.98           C  
ANISOU 2436  CG2 ILE A1169    10074   9464   8572   -305      0    -67       C  
ATOM   2437  CD1 ILE A1169      -0.202  -5.359 -51.005  1.00 71.72           C  
ANISOU 2437  CD1 ILE A1169     9556   9411   8284   -139    110   -249       C  
ATOM   2438  N   GLN A1170       1.224  -0.185 -52.588  1.00 83.87           N  
ANISOU 2438  N   GLN A1170    11645  10492   9728   -922   -227    147       N  
ATOM   2439  CA  GLN A1170       0.840   1.127 -53.104  1.00 84.24           C  
ANISOU 2439  CA  GLN A1170    11951  10263   9792  -1015   -327    223       C  
ATOM   2440  C   GLN A1170       1.933   1.724 -53.989  1.00 89.31           C  
ANISOU 2440  C   GLN A1170    12564  11034  10335  -1322   -388    434       C  
ATOM   2441  O   GLN A1170       1.655   2.529 -54.877  1.00 91.61           O  
ANISOU 2441  O   GLN A1170    13005  11179  10623  -1384   -451    548       O  
ATOM   2442  CB  GLN A1170       0.496   2.083 -51.960  1.00 77.33           C  
ANISOU 2442  CB  GLN A1170    11367   9061   8955  -1045   -416    116       C  
ATOM   2443  CG  GLN A1170      -0.710   1.655 -51.141  1.00 70.68           C  
ANISOU 2443  CG  GLN A1170    10561   8103   8193   -730   -354    -76       C  
ATOM   2444  CD  GLN A1170      -1.989   1.645 -51.951  1.00 72.95           C  
ANISOU 2444  CD  GLN A1170    10877   8295   8546   -468   -323    -80       C  
ATOM   2445  OE1 GLN A1170      -2.188   2.484 -52.829  1.00 78.89           O  
ANISOU 2445  OE1 GLN A1170    11778   8896   9301   -503   -390     29       O  
ATOM   2446  NE2 GLN A1170      -2.865   0.690 -51.662  1.00 72.75           N  
ANISOU 2446  NE2 GLN A1170    10706   8371   8566   -221   -230   -188       N  
ATOM   2447  N   MET A1171       3.174   1.316 -53.743  1.00 87.82           N  
ANISOU 2447  N   MET A1171    12168  11146  10055  -1513   -370    500       N  
ATOM   2448  CA  MET A1171       4.307   1.780 -54.535  1.00 86.80           C  
ANISOU 2448  CA  MET A1171    11944  11234   9803  -1824   -415    719       C  
ATOM   2449  C   MET A1171       4.585   0.845 -55.709  1.00 86.73           C  
ANISOU 2449  C   MET A1171    11647  11586   9721  -1704   -296    801       C  
ATOM   2450  O   MET A1171       5.570   1.016 -56.428  1.00 93.43           O  
ANISOU 2450  O   MET A1171    12342  12719  10440  -1921   -299    987       O  
ATOM   2451  CB  MET A1171       5.552   1.910 -53.658  1.00 84.65           C  
ANISOU 2451  CB  MET A1171    11573  11148   9441  -2110   -468    769       C  
ATOM   2452  CG  MET A1171       5.439   2.971 -52.579  1.00 83.48           C  
ANISOU 2452  CG  MET A1171    11749  10645   9326  -2296   -610    702       C  
ATOM   2453  SD  MET A1171       5.362   4.634 -53.261  1.00 88.40           S  
ANISOU 2453  SD  MET A1171    12747  10914   9928  -2600   -783    864       S  
ATOM   2454  CE  MET A1171       6.985   4.760 -54.009  1.00 68.14           C  
ANISOU 2454  CE  MET A1171     9903   8810   7178  -3042   -817   1160       C  
ATOM   2455  N   HIS A1172       3.713  -0.145 -55.886  1.00 79.16           N  
ANISOU 2455  N   HIS A1172    10623  10626   8829  -1368   -196    663       N  
ATOM   2456  CA  HIS A1172       3.800  -1.103 -56.990  1.00 75.15           C  
ANISOU 2456  CA  HIS A1172     9901  10404   8249  -1209    -88    696       C  
ATOM   2457  C   HIS A1172       5.108  -1.900 -57.010  1.00 71.44           C  
ANISOU 2457  C   HIS A1172     9131  10367   7646  -1249     -9    757       C  
ATOM   2458  O   HIS A1172       5.522  -2.396 -58.059  1.00 69.16           O  
ANISOU 2458  O   HIS A1172     8670  10364   7242  -1191     68    835       O  
ATOM   2459  CB  HIS A1172       3.579  -0.408 -58.340  1.00 75.04           C  
ANISOU 2459  CB  HIS A1172     9960  10369   8182  -1296   -122    850       C  
ATOM   2460  CG  HIS A1172       2.256   0.289 -58.453  1.00 78.42           C  
ANISOU 2460  CG  HIS A1172    10660  10408   8730  -1195   -194    804       C  
ATOM   2461  ND1 HIS A1172       1.218   0.060 -57.581  1.00 78.76           N  
ANISOU 2461  ND1 HIS A1172    10816  10206   8905   -979   -191    620       N  
ATOM   2462  CD2 HIS A1172       1.812   1.212 -59.339  1.00 79.80           C  
ANISOU 2462  CD2 HIS A1172    11000  10422   8897  -1268   -269    931       C  
ATOM   2463  CE1 HIS A1172       0.184   0.812 -57.924  1.00 77.57           C  
ANISOU 2463  CE1 HIS A1172    10875   9777   8822   -901   -257    631       C  
ATOM   2464  NE2 HIS A1172       0.519   1.519 -58.985  1.00 78.32           N  
ANISOU 2464  NE2 HIS A1172    11018   9901   8841  -1068   -310    818       N  
ATOM   2465  N   TRP A1173       5.748  -2.024 -55.850  1.00 64.19           N  
ANISOU 2465  N   TRP A1173     8148   9512   6729  -1327    -26    720       N  
ATOM   2466  CA  TRP A1173       6.981  -2.796 -55.731  1.00 57.42           C  
ANISOU 2466  CA  TRP A1173     6990   9082   5745  -1329     44    779       C  
ATOM   2467  C   TRP A1173       6.688  -4.294 -55.753  1.00 56.32           C  
ANISOU 2467  C   TRP A1173     6732   9048   5619   -958    165    634       C  
ATOM   2468  O   TRP A1173       7.520  -5.096 -56.175  1.00 49.46           O  
ANISOU 2468  O   TRP A1173     5627   8539   4625   -846    253    680       O  
ATOM   2469  CB  TRP A1173       7.720  -2.436 -54.440  1.00 57.32           C  
ANISOU 2469  CB  TRP A1173     6952   9104   5724  -1538    -32    793       C  
ATOM   2470  CG  TRP A1173       8.134  -0.998 -54.350  1.00 63.44           C  
ANISOU 2470  CG  TRP A1173     7870   9772   6464  -1944   -173    937       C  
ATOM   2471  CD1 TRP A1173       8.165  -0.087 -55.365  1.00 66.23           C  
ANISOU 2471  CD1 TRP A1173     8312  10084   6767  -2153   -227   1096       C  
ATOM   2472  CD2 TRP A1173       8.574  -0.304 -53.176  1.00 65.11           C  
ANISOU 2472  CD2 TRP A1173     8181   9882   6674  -2211   -292    937       C  
ATOM   2473  NE1 TRP A1173       8.598   1.130 -54.898  1.00 67.11           N  
ANISOU 2473  NE1 TRP A1173     8593  10051   6853  -2541   -380   1201       N  
ATOM   2474  CE2 TRP A1173       8.856   1.023 -53.556  1.00 62.83           C  
ANISOU 2474  CE2 TRP A1173     8065   9469   6337  -2586   -424   1097       C  
ATOM   2475  CE3 TRP A1173       8.758  -0.677 -51.840  1.00 64.96           C  
ANISOU 2475  CE3 TRP A1173     8140   9863   6680  -2180   -309    822       C  
ATOM   2476  CZ2 TRP A1173       9.310   1.979 -52.650  1.00 63.43           C  
ANISOU 2476  CZ2 TRP A1173     8313   9402   6386  -2936   -578   1130       C  
ATOM   2477  CZ3 TRP A1173       9.210   0.274 -50.941  1.00 61.77           C  
ANISOU 2477  CZ3 TRP A1173     7882   9347   6243  -2518   -454    853       C  
ATOM   2478  CH2 TRP A1173       9.481   1.586 -51.350  1.00 63.37           C  
ANISOU 2478  CH2 TRP A1173     8276   9408   6395  -2895   -590    998       C  
ATOM   2479  N   TYR A1174       5.495  -4.659 -55.294  1.00 64.32           N  
ANISOU 2479  N   TYR A1174     7920   9747   6772   -767    165    464       N  
ATOM   2480  CA  TYR A1174       5.085  -6.057 -55.220  1.00 66.23           C  
ANISOU 2480  CA  TYR A1174     8110  10018   7036   -454    253    325       C  
ATOM   2481  C   TYR A1174       4.770  -6.617 -56.602  1.00 65.43           C  
ANISOU 2481  C   TYR A1174     7985  10006   6870   -292    321    326       C  
ATOM   2482  O   TYR A1174       4.720  -7.832 -56.791  1.00 62.48           O  
ANISOU 2482  O   TYR A1174     7559   9718   6463    -49    394    235       O  
ATOM   2483  CB  TYR A1174       3.845  -6.197 -54.332  1.00 65.03           C  
ANISOU 2483  CB  TYR A1174     8145   9526   7038   -349    223    169       C  
ATOM   2484  CG  TYR A1174       2.543  -5.936 -55.063  1.00 64.85           C  
ANISOU 2484  CG  TYR A1174     8283   9268   7088   -274    207    125       C  
ATOM   2485  CD1 TYR A1174       2.195  -4.654 -55.467  1.00 67.95           C  
ANISOU 2485  CD1 TYR A1174     8813   9499   7508   -432    134    204       C  
ATOM   2486  CD2 TYR A1174       1.664  -6.974 -55.350  1.00 63.84           C  
ANISOU 2486  CD2 TYR A1174     8180   9083   6994    -53    253     17       C  
ATOM   2487  CE1 TYR A1174       1.008  -4.412 -56.136  1.00 74.27           C  
ANISOU 2487  CE1 TYR A1174     9740  10112   8366   -341    115    180       C  
ATOM   2488  CE2 TYR A1174       0.476  -6.741 -56.020  1.00 69.68           C  
ANISOU 2488  CE2 TYR A1174     9037   9654   7786      2    229     -7       C  
ATOM   2489  CZ  TYR A1174       0.153  -5.459 -56.410  1.00 75.97           C  
ANISOU 2489  CZ  TYR A1174     9939  10319   8609   -127    164     77       C  
ATOM   2490  OH  TYR A1174      -1.028  -5.221 -57.076  1.00 77.27           O  
ANISOU 2490  OH  TYR A1174    10201  10341   8817    -50    135     67       O  
ATOM   2491  N   ARG A1175       4.553  -5.722 -57.562  1.00 62.55           N  
ANISOU 2491  N   ARG A1175     7684   9606   6478   -430    286    429       N  
ATOM   2492  CA  ARG A1175       4.084  -6.112 -58.887  1.00 64.38           C  
ANISOU 2492  CA  ARG A1175     7926   9890   6645   -298    332    426       C  
ATOM   2493  C   ARG A1175       5.049  -7.037 -59.625  1.00 68.96           C  
ANISOU 2493  C   ARG A1175     8304  10850   7048   -158    438    451       C  
ATOM   2494  O   ARG A1175       6.262  -6.979 -59.424  1.00 73.95           O  
ANISOU 2494  O   ARG A1175     8743  11780   7574   -237    469    552       O  
ATOM   2495  CB  ARG A1175       3.777  -4.876 -59.736  1.00 66.35           C  
ANISOU 2495  CB  ARG A1175     8277  10049   6883   -495    264    564       C  
ATOM   2496  CG  ARG A1175       2.552  -4.102 -59.274  1.00 65.36           C  
ANISOU 2496  CG  ARG A1175     8386   9525   6922   -523    170    513       C  
ATOM   2497  CD  ARG A1175       2.084  -3.115 -60.331  1.00 71.38           C  
ANISOU 2497  CD  ARG A1175     9266  10190   7664   -631    108    642       C  
ATOM   2498  NE  ARG A1175       0.828  -2.471 -59.958  1.00 74.15           N  
ANISOU 2498  NE  ARG A1175     9833  10179   8161   -582     28    585       N  
ATOM   2499  CZ  ARG A1175       0.167  -1.618 -60.732  1.00 73.84           C  
ANISOU 2499  CZ  ARG A1175     9933   9990   8132   -618    -42    680       C  
ATOM   2500  NH1 ARG A1175       0.639  -1.302 -61.930  1.00 76.77           N  
ANISOU 2500  NH1 ARG A1175    10258  10535   8376   -735    -44    842       N  
ATOM   2501  NH2 ARG A1175      -0.969  -1.080 -60.308  1.00 68.71           N  
ANISOU 2501  NH2 ARG A1175     9463   9036   7609   -522   -106    621       N  
ATOM   2502  N   ALA A1176       4.492  -7.893 -60.476  1.00 65.05           N  
ANISOU 2502  N   ALA A1176     7856  10356   6505     57    490    358       N  
ATOM   2503  CA  ALA A1176       5.292  -8.812 -61.272  1.00 67.49           C  
ANISOU 2503  CA  ALA A1176     8020  10998   6626    246    596    350       C  
ATOM   2504  C   ALA A1176       5.696  -8.156 -62.588  1.00 74.52           C  
ANISOU 2504  C   ALA A1176     8827  12133   7354    127    619    504       C  
ATOM   2505  O   ALA A1176       5.476  -6.961 -62.789  1.00 75.41           O  
ANISOU 2505  O   ALA A1176     8993  12153   7508   -128    543    637       O  
ATOM   2506  CB  ALA A1176       4.524 -10.098 -61.527  1.00 67.45           C  
ANISOU 2506  CB  ALA A1176     8149  10854   6627    525    627    161       C  
ATOM   2507  N   THR A1177       6.284  -8.941 -63.484  1.00 75.09           N  
ANISOU 2507  N   THR A1177     8786  12515   7229    321    723    487       N  
ATOM   2508  CA  THR A1177       6.788  -8.405 -64.741  1.00 77.35           C  
ANISOU 2508  CA  THR A1177     8959  13109   7320    221    765    642       C  
ATOM   2509  C   THR A1177       6.241  -9.139 -65.962  1.00 80.59           C  
ANISOU 2509  C   THR A1177     9469  13550   7602    435    816    534       C  
ATOM   2510  O   THR A1177       6.331  -8.635 -67.082  1.00 94.41           O  
ANISOU 2510  O   THR A1177    11181  15487   9205    340    831    651       O  
ATOM   2511  CB  THR A1177       8.327  -8.445 -64.791  1.00 88.44           C  
ANISOU 2511  CB  THR A1177    10058  15016   8531    214    858    778       C  
ATOM   2512  OG1 THR A1177       8.778  -9.791 -64.593  1.00 94.09           O  
ANISOU 2512  OG1 THR A1177    10704  15883   9162    577    960    626       O  
ATOM   2513  CG2 THR A1177       8.919  -7.554 -63.711  1.00 91.23           C  
ANISOU 2513  CG2 THR A1177    10308  15376   8979    -78    784    920       C  
ATOM   2514  N   HIS A1178       5.678 -10.325 -65.752  1.00 68.06           N  
ANISOU 2514  N   HIS A1178     8025  11780   6056    703    832    317       N  
ATOM   2515  CA  HIS A1178       5.185 -11.124 -66.870  1.00 61.95           C  
ANISOU 2515  CA  HIS A1178     7378  11021   5140    903    868    190       C  
ATOM   2516  C   HIS A1178       3.930 -10.520 -67.495  1.00 63.61           C  
ANISOU 2516  C   HIS A1178     7760  10985   5424    745    767    209       C  
ATOM   2517  O   HIS A1178       3.273  -9.669 -66.893  1.00 62.38           O  
ANISOU 2517  O   HIS A1178     7664  10573   5463    546    669    276       O  
ATOM   2518  CB  HIS A1178       4.954 -12.581 -66.458  1.00 57.34           C  
ANISOU 2518  CB  HIS A1178     6938  10280   4569   1208    892    -41       C  
ATOM   2519  CG  HIS A1178       3.948 -12.752 -65.365  1.00 47.76           C  
ANISOU 2519  CG  HIS A1178     5892   8648   3607   1153    790   -134       C  
ATOM   2520  ND1 HIS A1178       4.280 -12.676 -64.031  1.00 51.79           N  
ANISOU 2520  ND1 HIS A1178     6333   9078   4265   1116    775   -116       N  
ATOM   2521  CD2 HIS A1178       2.619 -13.008 -65.410  1.00 56.44           C  
ANISOU 2521  CD2 HIS A1178     7206   9423   4816   1123    700   -238       C  
ATOM   2522  CE1 HIS A1178       3.198 -12.871 -63.298  1.00 50.08           C  
ANISOU 2522  CE1 HIS A1178     6285   8507   4236   1075    689   -207       C  
ATOM   2523  NE2 HIS A1178       2.177 -13.075 -64.110  1.00 53.14           N  
ANISOU 2523  NE2 HIS A1178     6836   8751   4606   1075    642   -276       N  
ATOM   2524  N   GLN A1179       3.609 -10.969 -68.705  1.00 67.55           N  
ANISOU 2524  N   GLN A1179     8341  11576   5750    852    790    148       N  
ATOM   2525  CA  GLN A1179       2.550 -10.361 -69.507  1.00 71.16           C  
ANISOU 2525  CA  GLN A1179     8920  11895   6222    706    699    200       C  
ATOM   2526  C   GLN A1179       1.165 -10.431 -68.864  1.00 73.59           C  
ANISOU 2526  C   GLN A1179     9412  11790   6761    665    578    105       C  
ATOM   2527  O   GLN A1179       0.416  -9.453 -68.888  1.00 77.76           O  
ANISOU 2527  O   GLN A1179     9977  12164   7404    488    485    217       O  
ATOM   2528  CB  GLN A1179       2.511 -10.987 -70.903  1.00 71.52           C  
ANISOU 2528  CB  GLN A1179     9023  12143   6007    848    747    128       C  
ATOM   2529  CG  GLN A1179       1.537 -10.312 -71.848  1.00 72.40           C  
ANISOU 2529  CG  GLN A1179     9229  12185   6095    690    652    214       C  
ATOM   2530  CD  GLN A1179       1.869  -8.852 -72.076  1.00 76.97           C  
ANISOU 2530  CD  GLN A1179     9680  12878   6685    431    626    486       C  
ATOM   2531  OE1 GLN A1179       3.033  -8.486 -72.240  1.00 76.27           O  
ANISOU 2531  OE1 GLN A1179     9408  13105   6465    376    712    621       O  
ATOM   2532  NE2 GLN A1179       0.845  -8.007 -72.081  1.00 83.28           N  
ANISOU 2532  NE2 GLN A1179    10581  13428   7634    268    499    578       N  
ATOM   2533  N   GLU A1180       0.828 -11.584 -68.295  1.00 70.53           N  
ANISOU 2533  N   GLU A1180     9136  11235   6426    835    577    -89       N  
ATOM   2534  CA  GLU A1180      -0.477 -11.769 -67.665  1.00 65.82           C  
ANISOU 2534  CA  GLU A1180     8687  10300   6023    790    469   -173       C  
ATOM   2535  C   GLU A1180      -0.673 -10.802 -66.499  1.00 64.56           C  
ANISOU 2535  C   GLU A1180     8467   9973   6091    639    422    -74       C  
ATOM   2536  O   GLU A1180      -1.763 -10.258 -66.305  1.00 68.95           O  
ANISOU 2536  O   GLU A1180     9087  10330   6781    542    330    -45       O  
ATOM   2537  CB  GLU A1180      -0.649 -13.215 -67.192  1.00 64.49           C  
ANISOU 2537  CB  GLU A1180     8655   9994   5855    972    476   -378       C  
ATOM   2538  CG  GLU A1180      -2.042 -13.529 -66.671  1.00 74.45           C  
ANISOU 2538  CG  GLU A1180    10058  10957   7274    902    362   -453       C  
ATOM   2539  CD  GLU A1180      -2.213 -14.988 -66.296  1.00 84.82           C  
ANISOU 2539  CD  GLU A1180    11541  12120   8566   1043    350   -637       C  
ATOM   2540  OE1 GLU A1180      -1.208 -15.730 -66.322  1.00 93.77           O  
ANISOU 2540  OE1 GLU A1180    12692  13353   9582   1233    434   -714       O  
ATOM   2541  OE2 GLU A1180      -3.352 -15.393 -65.979  1.00 81.36           O  
ANISOU 2541  OE2 GLU A1180    11221  11473   8219    964    252   -695       O  
ATOM   2542  N   ALA A1181       0.394 -10.585 -65.736  1.00 59.86           N  
ANISOU 2542  N   ALA A1181     7746   9477   5520    631    483    -24       N  
ATOM   2543  CA  ALA A1181       0.367  -9.650 -64.618  1.00 56.01           C  
ANISOU 2543  CA  ALA A1181     7219   8843   5217    481    438     60       C  
ATOM   2544  C   ALA A1181       0.121  -8.229 -65.105  1.00 55.92           C  
ANISOU 2544  C   ALA A1181     7209   8810   5229    282    376    236       C  
ATOM   2545  O   ALA A1181      -0.689  -7.503 -64.531  1.00 65.19           O  
ANISOU 2545  O   ALA A1181     8462   9743   6563    199    295    261       O  
ATOM   2546  CB  ALA A1181       1.664  -9.723 -63.831  1.00 63.38           C  
ANISOU 2546  CB  ALA A1181     8009   9941   6133    490    507     91       C  
ATOM   2547  N   ILE A1182       0.825  -7.840 -66.166  1.00 52.39           N  
ANISOU 2547  N   ILE A1182     6680   8617   4608    219    414    361       N  
ATOM   2548  CA  ILE A1182       0.651  -6.522 -66.771  1.00 61.67           C  
ANISOU 2548  CA  ILE A1182     7878   9776   5778     21    346    553       C  
ATOM   2549  C   ILE A1182      -0.787  -6.323 -67.247  1.00 67.24           C  
ANISOU 2549  C   ILE A1182     8729  10267   6551     45    254    533       C  
ATOM   2550  O   ILE A1182      -1.393  -5.272 -67.015  1.00 70.74           O  
ANISOU 2550  O   ILE A1182     9256  10507   7117    -60    163    631       O  
ATOM   2551  CB  ILE A1182       1.605  -6.322 -67.964  1.00 65.13           C  
ANISOU 2551  CB  ILE A1182     8194  10574   5978    -44    410    694       C  
ATOM   2552  CG1 ILE A1182       3.060  -6.459 -67.513  1.00 67.12           C  
ANISOU 2552  CG1 ILE A1182     8254  11107   6143    -73    502    745       C  
ATOM   2553  CG2 ILE A1182       1.374  -4.968 -68.615  1.00 66.39           C  
ANISOU 2553  CG2 ILE A1182     8407  10691   6128   -267    324    914       C  
ATOM   2554  CD1 ILE A1182       3.476  -5.436 -66.482  1.00 71.86           C  
ANISOU 2554  CD1 ILE A1182     8835  11589   6879   -301    440    865       C  
ATOM   2555  N   ASN A1183      -1.326  -7.343 -67.908  1.00 64.19           N  
ANISOU 2555  N   ASN A1183     8382   9933   6075    191    269    406       N  
ATOM   2556  CA  ASN A1183      -2.698  -7.303 -68.398  1.00 65.83           C  
ANISOU 2556  CA  ASN A1183     8697   9994   6321    210    176    387       C  
ATOM   2557  C   ASN A1183      -3.711  -7.166 -67.266  1.00 69.37           C  
ANISOU 2557  C   ASN A1183     9207  10158   6993    229    107    324       C  
ATOM   2558  O   ASN A1183      -4.660  -6.388 -67.364  1.00 75.06           O  
ANISOU 2558  O   ASN A1183     9979  10744   7796    196     19    403       O  
ATOM   2559  CB  ASN A1183      -3.009  -8.544 -69.238  1.00 63.13           C  
ANISOU 2559  CB  ASN A1183     8402   9763   5821    336    195    243       C  
ATOM   2560  CG  ASN A1183      -2.236  -8.576 -70.544  1.00 63.22           C  
ANISOU 2560  CG  ASN A1183     8366  10074   5579    336    256    308       C  
ATOM   2561  OD1 ASN A1183      -1.270  -7.834 -70.727  1.00 66.11           O  
ANISOU 2561  OD1 ASN A1183     8628  10610   5879    243    306    460       O  
ATOM   2562  ND2 ASN A1183      -2.658  -9.439 -71.460  1.00 62.02           N  
ANISOU 2562  ND2 ASN A1183     8295  10004   5266    425    249    197       N  
ATOM   2563  N   CYS A1184      -3.503  -7.920 -66.190  1.00 64.27           N  
ANISOU 2563  N   CYS A1184     8549   9439   6431    300    150    189       N  
ATOM   2564  CA  CYS A1184      -4.404  -7.873 -65.043  1.00 67.65           C  
ANISOU 2564  CA  CYS A1184     9016   9640   7047    323    101    125       C  
ATOM   2565  C   CYS A1184      -4.321  -6.538 -64.308  1.00 74.64           C  
ANISOU 2565  C   CYS A1184     9913  10386   8063    235     68    234       C  
ATOM   2566  O   CYS A1184      -5.324  -6.046 -63.792  1.00 82.71           O  
ANISOU 2566  O   CYS A1184    10985  11234   9209    261      6    235       O  
ATOM   2567  CB  CYS A1184      -4.118  -9.026 -64.080  1.00 68.01           C  
ANISOU 2567  CB  CYS A1184     9055   9654   7131    407    153    -29       C  
ATOM   2568  SG  CYS A1184      -5.214  -9.101 -62.643  1.00111.44           S  
ANISOU 2568  SG  CYS A1184    14584  14928  12829    427    106   -104       S  
ATOM   2569  N   TYR A1185      -3.126  -5.957 -64.257  1.00 71.59           N  
ANISOU 2569  N   TYR A1185     9485  10083   7633    132    104    327       N  
ATOM   2570  CA  TYR A1185      -2.951  -4.649 -63.638  1.00 72.53           C  
ANISOU 2570  CA  TYR A1185     9661  10048   7851     12     54    434       C  
ATOM   2571  C   TYR A1185      -3.628  -3.578 -64.483  1.00 82.31           C  
ANISOU 2571  C   TYR A1185    10994  11194   9084    -36    -34    578       C  
ATOM   2572  O   TYR A1185      -4.197  -2.624 -63.954  1.00 85.96           O  
ANISOU 2572  O   TYR A1185    11570  11428   9663    -41   -105    619       O  
ATOM   2573  CB  TYR A1185      -1.467  -4.315 -63.461  1.00 68.35           C  
ANISOU 2573  CB  TYR A1185     9055   9666   7250   -137     97    520       C  
ATOM   2574  CG  TYR A1185      -0.736  -5.238 -62.514  1.00 65.43           C  
ANISOU 2574  CG  TYR A1185     8586   9386   6888    -79    173    401       C  
ATOM   2575  CD1 TYR A1185      -1.414  -5.915 -61.508  1.00 75.10           C  
ANISOU 2575  CD1 TYR A1185     9844  10460   8230     46    176    246       C  
ATOM   2576  CD2 TYR A1185       0.633  -5.436 -62.629  1.00 62.75           C  
ANISOU 2576  CD2 TYR A1185     8106   9311   6426   -146    240    461       C  
ATOM   2577  CE1 TYR A1185      -0.747  -6.762 -60.643  1.00 79.20           C  
ANISOU 2577  CE1 TYR A1185    10286  11054   8752    104    235    154       C  
ATOM   2578  CE2 TYR A1185       1.307  -6.283 -61.771  1.00 66.83           C  
ANISOU 2578  CE2 TYR A1185     8525   9923   6943    -66    302    366       C  
ATOM   2579  CZ  TYR A1185       0.614  -6.941 -60.780  1.00 72.80           C  
ANISOU 2579  CZ  TYR A1185     9344  10492   7825     59    296    213       C  
ATOM   2580  OH  TYR A1185       1.283  -7.783 -59.922  1.00 71.77           O  
ANISOU 2580  OH  TYR A1185     9131  10448   7692    143    349    134       O  
ATOM   2581  N   ALA A1186      -3.566  -3.747 -65.800  1.00 87.23           N  
ANISOU 2581  N   ALA A1186    11584  11999   9561    -51    -29    654       N  
ATOM   2582  CA  ALA A1186      -4.205  -2.811 -66.719  1.00 89.23           C  
ANISOU 2582  CA  ALA A1186    11922  12194   9788    -88   -118    809       C  
ATOM   2583  C   ALA A1186      -5.723  -2.955 -66.685  1.00 79.00           C  
ANISOU 2583  C   ALA A1186    10670  10767   8579     66   -183    746       C  
ATOM   2584  O   ALA A1186      -6.452  -1.966 -66.772  1.00 79.76           O  
ANISOU 2584  O   ALA A1186    10862  10702   8742     90   -272    851       O  
ATOM   2585  CB  ALA A1186      -3.681  -3.014 -68.133  1.00 95.77           C  
ANISOU 2585  CB  ALA A1186    12688  13295  10408   -152    -90    908       C  
ATOM   2586  N   GLU A1187      -6.192  -4.192 -66.555  1.00 71.84           N  
ANISOU 2586  N   GLU A1187     9696   9938   7662    169   -147    585       N  
ATOM   2587  CA  GLU A1187      -7.622  -4.477 -66.515  1.00 71.47           C  
ANISOU 2587  CA  GLU A1187     9650   9832   7675    283   -209    532       C  
ATOM   2588  C   GLU A1187      -8.256  -3.972 -65.222  1.00 80.09           C  
ANISOU 2588  C   GLU A1187    10772  10714   8944    362   -231    492       C  
ATOM   2589  O   GLU A1187      -7.795  -4.296 -64.127  1.00 87.40           O  
ANISOU 2589  O   GLU A1187    11686  11577   9944    361   -173    389       O  
ATOM   2590  CB  GLU A1187      -7.867  -5.980 -66.664  1.00 70.96           C  
ANISOU 2590  CB  GLU A1187     9531   9892   7538    324   -176    375       C  
ATOM   2591  CG  GLU A1187      -9.331  -6.382 -66.628  1.00 72.02           C  
ANISOU 2591  CG  GLU A1187     9641  10012   7711    389   -250    333       C  
ATOM   2592  CD  GLU A1187     -10.093  -5.922 -67.853  1.00 76.18           C  
ANISOU 2592  CD  GLU A1187    10166  10632   8145    386   -341    459       C  
ATOM   2593  OE1 GLU A1187     -11.338  -5.856 -67.788  1.00 76.57           O  
ANISOU 2593  OE1 GLU A1187    10170  10683   8239    444   -417    481       O  
ATOM   2594  OE2 GLU A1187      -9.446  -5.631 -68.882  1.00 82.72           O  
ANISOU 2594  OE2 GLU A1187    11024  11564   8844    325   -336    547       O  
ATOM   2595  N   GLU A1188      -9.318  -3.183 -65.357  1.00 79.06           N  
ANISOU 2595  N   GLU A1188    10677  10494   8868    451   -312    576       N  
ATOM   2596  CA  GLU A1188     -10.018  -2.626 -64.204  1.00 75.28           C  
ANISOU 2596  CA  GLU A1188    10231   9837   8533    573   -329    538       C  
ATOM   2597  C   GLU A1188     -10.878  -3.666 -63.493  1.00 71.84           C  
ANISOU 2597  C   GLU A1188     9680   9477   8139    655   -303    399       C  
ATOM   2598  O   GLU A1188     -11.243  -3.488 -62.332  1.00 71.79           O  
ANISOU 2598  O   GLU A1188     9672   9371   8232    743   -282    331       O  
ATOM   2599  CB  GLU A1188     -10.886  -1.437 -64.625  1.00 80.48           C  
ANISOU 2599  CB  GLU A1188    10967  10392   9218    689   -424    680       C  
ATOM   2600  CG  GLU A1188     -10.107  -0.168 -64.930  1.00 90.68           C  
ANISOU 2600  CG  GLU A1188    12436  11511  10507    606   -467    824       C  
ATOM   2601  CD  GLU A1188      -9.619   0.534 -63.676  1.00 97.09           C  
ANISOU 2601  CD  GLU A1188    13384  12080  11425    605   -451    768       C  
ATOM   2602  OE1 GLU A1188     -10.142   0.235 -62.582  1.00 95.40           O  
ANISOU 2602  OE1 GLU A1188    13131  11821  11295    731   -414    631       O  
ATOM   2603  OE2 GLU A1188      -8.713   1.387 -63.785  1.00103.36           O  
ANISOU 2603  OE2 GLU A1188    14328  12738  12205    458   -483    867       O  
ATOM   2604  N   THR A1189     -11.201  -4.748 -64.193  1.00 73.67           N  
ANISOU 2604  N   THR A1189     9828   9887   8278    613   -310    361       N  
ATOM   2605  CA  THR A1189     -12.044  -5.793 -63.623  1.00 77.40           C  
ANISOU 2605  CA  THR A1189    10203  10438   8770    639   -307    254       C  
ATOM   2606  C   THR A1189     -11.228  -6.966 -63.088  1.00 80.42           C  
ANISOU 2606  C   THR A1189    10592  10826   9136    558   -234    116       C  
ATOM   2607  O   THR A1189     -11.778  -7.885 -62.482  1.00 83.97           O  
ANISOU 2607  O   THR A1189    10992  11309   9604    550   -231     29       O  
ATOM   2608  CB  THR A1189     -13.075  -6.317 -64.643  1.00 81.12           C  
ANISOU 2608  CB  THR A1189    10599  11084   9141    620   -390    297       C  
ATOM   2609  OG1 THR A1189     -12.395  -6.943 -65.738  1.00 84.26           O  
ANISOU 2609  OG1 THR A1189    11047  11570   9399    512   -390    282       O  
ATOM   2610  CG2 THR A1189     -13.935  -5.177 -65.164  1.00 82.49           C  
ANISOU 2610  CG2 THR A1189    10747  11273   9324    731   -469    450       C  
ATOM   2611  N   CYS A1190      -9.917  -6.934 -63.315  1.00 78.50           N  
ANISOU 2611  N   CYS A1190    10409  10567   8850    499   -179    110       N  
ATOM   2612  CA  CYS A1190      -9.039  -7.981 -62.803  1.00 76.87           C  
ANISOU 2612  CA  CYS A1190    10209  10373   8623    466   -108     -9       C  
ATOM   2613  C   CYS A1190      -8.416  -7.568 -61.476  1.00 80.74           C  
ANISOU 2613  C   CYS A1190    10705  10749   9223    477    -54    -40       C  
ATOM   2614  O   CYS A1190      -7.945  -6.440 -61.325  1.00 85.14           O  
ANISOU 2614  O   CYS A1190    11299  11231   9820    458    -54     37       O  
ATOM   2615  CB  CYS A1190      -7.936  -8.327 -63.810  1.00 71.79           C  
ANISOU 2615  CB  CYS A1190     9594   9843   7839    423    -69     -2       C  
ATOM   2616  SG  CYS A1190      -6.979  -9.801 -63.361  1.00 97.87           S  
ANISOU 2616  SG  CYS A1190    12917  13184  11086    449     11   -154       S  
ATOM   2617  N   CYS A1191      -8.422  -8.485 -60.516  1.00 75.37           N  
ANISOU 2617  N   CYS A1191    10006  10049   8581    490    -20   -148       N  
ATOM   2618  CA  CYS A1191      -7.767  -8.252 -59.236  1.00 70.25           C  
ANISOU 2618  CA  CYS A1191     9360   9320   8013    491     30   -187       C  
ATOM   2619  C   CYS A1191      -7.049  -9.521 -58.782  1.00 71.25           C  
ANISOU 2619  C   CYS A1191     9482   9486   8105    488     80   -281       C  
ATOM   2620  O   CYS A1191      -6.955  -9.810 -57.590  1.00 72.97           O  
ANISOU 2620  O   CYS A1191     9688   9653   8384    498    106   -336       O  
ATOM   2621  CB  CYS A1191      -8.775  -7.780 -58.183  1.00 67.80           C  
ANISOU 2621  CB  CYS A1191     9032   8925   7806    550     13   -203       C  
ATOM   2622  SG  CYS A1191      -8.024  -7.165 -56.656  1.00 97.19           S  
ANISOU 2622  SG  CYS A1191    12788  12533  11607    546     58   -246       S  
ATOM   2623  N   ASP A1192      -6.547 -10.282 -59.748  1.00 72.32           N  
ANISOU 2623  N   ASP A1192     9638   9712   8127    491     93   -300       N  
ATOM   2624  CA  ASP A1192      -5.766 -11.472 -59.445  1.00 76.77           C  
ANISOU 2624  CA  ASP A1192    10227  10303   8640    533    139   -386       C  
ATOM   2625  C   ASP A1192      -4.448 -11.069 -58.796  1.00 80.47           C  
ANISOU 2625  C   ASP A1192    10641  10813   9120    535    201   -361       C  
ATOM   2626  O   ASP A1192      -3.953  -9.962 -59.012  1.00 89.15           O  
ANISOU 2626  O   ASP A1192    11702  11949  10221    474    206   -271       O  
ATOM   2627  CB  ASP A1192      -5.513 -12.292 -60.712  1.00 83.36           C  
ANISOU 2627  CB  ASP A1192    11121  11226   9326    572    140   -423       C  
ATOM   2628  CG  ASP A1192      -6.792 -12.849 -61.311  1.00 81.81           C  
ANISOU 2628  CG  ASP A1192    10992  10995   9098    536     59   -456       C  
ATOM   2629  OD1 ASP A1192      -7.763 -13.060 -60.553  1.00 83.85           O  
ANISOU 2629  OD1 ASP A1192    11243  11175   9443    493     14   -470       O  
ATOM   2630  OD2 ASP A1192      -6.824 -13.079 -62.538  1.00 75.03           O  
ANISOU 2630  OD2 ASP A1192    10183  10213   8112    538     38   -462       O  
ATOM   2631  N   PHE A1193      -3.884 -11.968 -57.999  1.00 75.37           N  
ANISOU 2631  N   PHE A1193     9998  10164   8474    590    236   -428       N  
ATOM   2632  CA  PHE A1193      -2.695 -11.653 -57.217  1.00 69.14           C  
ANISOU 2632  CA  PHE A1193     9135   9441   7695    584    283   -399       C  
ATOM   2633  C   PHE A1193      -1.415 -12.155 -57.880  1.00 68.98           C  
ANISOU 2633  C   PHE A1193     9064   9606   7541    665    344   -388       C  
ATOM   2634  O   PHE A1193      -1.179 -13.360 -57.961  1.00 71.18           O  
ANISOU 2634  O   PHE A1193     9392   9899   7755    796    367   -465       O  
ATOM   2635  CB  PHE A1193      -2.827 -12.239 -55.812  1.00 62.07           C  
ANISOU 2635  CB  PHE A1193     8250   8459   6875    607    283   -457       C  
ATOM   2636  CG  PHE A1193      -1.751 -11.798 -54.866  1.00 57.04           C  
ANISOU 2636  CG  PHE A1193     7532   7888   6251    575    312   -422       C  
ATOM   2637  CD1 PHE A1193      -1.783 -10.533 -54.303  1.00 52.37           C  
ANISOU 2637  CD1 PHE A1193     6922   7252   5725    460    289   -375       C  
ATOM   2638  CD2 PHE A1193      -0.716 -12.653 -54.525  1.00 58.51           C  
ANISOU 2638  CD2 PHE A1193     7675   8181   6376    666    351   -436       C  
ATOM   2639  CE1 PHE A1193      -0.797 -10.125 -53.427  1.00 54.55           C  
ANISOU 2639  CE1 PHE A1193     7136   7592   5997    395    297   -343       C  
ATOM   2640  CE2 PHE A1193       0.272 -12.251 -53.648  1.00 60.95           C  
ANISOU 2640  CE2 PHE A1193     7885   8587   6685    621    366   -390       C  
ATOM   2641  CZ  PHE A1193       0.230 -10.985 -53.098  1.00 59.56           C  
ANISOU 2641  CZ  PHE A1193     7691   8371   6569    464    335   -345       C  
ATOM   2642  N   PHE A1194      -0.592 -11.221 -58.349  1.00 68.34           N  
ANISOU 2642  N   PHE A1194     8889   9669   7406    590    367   -285       N  
ATOM   2643  CA  PHE A1194       0.688 -11.558 -58.965  1.00 76.41           C  
ANISOU 2643  CA  PHE A1194     9811  10940   8280    664    437   -249       C  
ATOM   2644  C   PHE A1194       1.836 -10.836 -58.267  1.00 79.14           C  
ANISOU 2644  C   PHE A1194    10012  11434   8623    561    457   -149       C  
ATOM   2645  O   PHE A1194       1.800  -9.617 -58.103  1.00 90.97           O  
ANISOU 2645  O   PHE A1194    11500  12889  10175    374    413    -57       O  
ATOM   2646  CB  PHE A1194       0.688 -11.190 -60.452  1.00 77.47           C  
ANISOU 2646  CB  PHE A1194     9940  11201   8294    643    449   -190       C  
ATOM   2647  CG  PHE A1194      -0.313 -11.953 -61.273  1.00 68.12           C  
ANISOU 2647  CG  PHE A1194     8893   9917   7072    732    422   -287       C  
ATOM   2648  CD1 PHE A1194      -0.065 -13.262 -61.650  1.00 62.42           C  
ANISOU 2648  CD1 PHE A1194     8239   9240   6236    917    461   -401       C  
ATOM   2649  CD2 PHE A1194      -1.493 -11.355 -61.684  1.00 62.09           C  
ANISOU 2649  CD2 PHE A1194     8201   9019   6372    634    349   -262       C  
ATOM   2650  CE1 PHE A1194      -0.982 -13.964 -62.411  1.00 58.94           C  
ANISOU 2650  CE1 PHE A1194     7955   8697   5744    962    416   -494       C  
ATOM   2651  CE2 PHE A1194      -2.411 -12.051 -62.447  1.00 55.63           C  
ANISOU 2651  CE2 PHE A1194     7494   8140   5501    683    309   -339       C  
ATOM   2652  CZ  PHE A1194      -2.156 -13.356 -62.810  1.00 52.70           C  
ANISOU 2652  CZ  PHE A1194     7209   7801   5015    827    338   -458       C  
ATOM   2653  N   THR A1195       2.854 -11.589 -57.860  1.00 73.05           N  
ANISOU 2653  N   THR A1195     9140  10836   7780    682    512   -162       N  
ATOM   2654  CA  THR A1195       4.030 -11.002 -57.220  1.00 77.35           C  
ANISOU 2654  CA  THR A1195     9513  11581   8294    574    524    -54       C  
ATOM   2655  C   THR A1195       5.331 -11.621 -57.718  1.00 82.43           C  
ANISOU 2655  C   THR A1195     9978  12582   8759    726    611     -7       C  
ATOM   2656  O   THR A1195       5.328 -12.672 -58.357  1.00 88.73           O  
ANISOU 2656  O   THR A1195    10821  13425   9467    966    666    -94       O  
ATOM   2657  CB  THR A1195       3.986 -11.141 -55.682  1.00 80.77           C  
ANISOU 2657  CB  THR A1195     9962  11888   8839    550    487    -96       C  
ATOM   2658  OG1 THR A1195       3.630 -12.484 -55.329  1.00 85.46           O  
ANISOU 2658  OG1 THR A1195    10641  12382   9449    769    506   -215       O  
ATOM   2659  CG2 THR A1195       2.975 -10.184 -55.084  1.00 79.11           C  
ANISOU 2659  CG2 THR A1195     9878  11406   8773    375    411   -110       C  
ATOM   2660  N   ASN A1196       6.442 -10.956 -57.418  1.00 81.90           N  
ANISOU 2660  N   ASN A1196     9713  12778   8629    585    619    130       N  
ATOM   2661  CA  ASN A1196       7.766 -11.479 -57.732  1.00 81.26           C  
ANISOU 2661  CA  ASN A1196     9401  13107   8366    733    705    199       C  
ATOM   2662  C   ASN A1196       8.286 -12.353 -56.597  1.00 87.25           C  
ANISOU 2662  C   ASN A1196    10099  13912   9141    908    715    153       C  
ATOM   2663  O   ASN A1196       7.641 -12.474 -55.556  1.00 89.64           O  
ANISOU 2663  O   ASN A1196    10534  13932   9592    872    652     78       O  
ATOM   2664  CB  ASN A1196       8.741 -10.334 -58.007  1.00 73.35           C  
ANISOU 2664  CB  ASN A1196     8182  12425   7263    462    699    403       C  
ATOM   2665  CG  ASN A1196       8.652  -9.233 -56.969  1.00 65.77           C  
ANISOU 2665  CG  ASN A1196     7257  11302   6430    135    589    471       C  
ATOM   2666  OD1 ASN A1196       9.205  -9.348 -55.875  1.00 72.83           O  
ANISOU 2666  OD1 ASN A1196     8059  12268   7343    106    564    485       O  
ATOM   2667  ND2 ASN A1196       7.952  -8.157 -57.307  1.00 55.41           N  
ANISOU 2667  ND2 ASN A1196     6096   9763   5193   -101    518    511       N  
ATOM   2668  N   GLN A1197       9.451 -12.961 -56.799  1.00 90.43           N  
ANISOU 2668  N   GLN A1197    10292  14691   9378   1112    796    206       N  
ATOM   2669  CA  GLN A1197      10.037 -13.828 -55.782  1.00 86.64           C  
ANISOU 2669  CA  GLN A1197     9739  14289   8892   1315    804    183       C  
ATOM   2670  C   GLN A1197      10.428 -13.045 -54.535  1.00 78.99           C  
ANISOU 2670  C   GLN A1197     8652  13363   7998   1042    723    285       C  
ATOM   2671  O   GLN A1197      10.252 -13.523 -53.415  1.00 71.86           O  
ANISOU 2671  O   GLN A1197     7818  12303   7183   1102    680    229       O  
ATOM   2672  CB  GLN A1197      11.252 -14.577 -56.334  1.00 91.06           C  
ANISOU 2672  CB  GLN A1197    10074  15290   9235   1627    913    233       C  
ATOM   2673  CG  GLN A1197      10.920 -15.590 -57.415  1.00 97.02           C  
ANISOU 2673  CG  GLN A1197    10994  15977   9893   1972    991     92       C  
ATOM   2674  CD  GLN A1197      12.091 -16.496 -57.739  1.00109.43           C  
ANISOU 2674  CD  GLN A1197    12381  17948  11250   2371   1101    109       C  
ATOM   2675  OE1 GLN A1197      13.049 -16.589 -56.972  1.00109.35           O  
ANISOU 2675  OE1 GLN A1197    12135  18223  11191   2436   1109    214       O  
ATOM   2676  NE2 GLN A1197      12.020 -17.171 -58.881  1.00118.90           N  
ANISOU 2676  NE2 GLN A1197    13688  19185  12305   2655   1184      4       N  
ATOM   2677  N   ALA A1198      10.953 -11.841 -54.739  1.00 80.12           N  
ANISOU 2677  N   ALA A1198     8636  13714   8091    724    694    438       N  
ATOM   2678  CA  ALA A1198      11.411 -11.000 -53.640  1.00 77.13           C  
ANISOU 2678  CA  ALA A1198     8161  13394   7753    420    603    539       C  
ATOM   2679  C   ALA A1198      10.295 -10.700 -52.643  1.00 72.58           C  
ANISOU 2679  C   ALA A1198     7852  12351   7374    291    511    421       C  
ATOM   2680  O   ALA A1198      10.427 -10.985 -51.450  1.00 69.49           O  
ANISOU 2680  O   ALA A1198     7453  11922   7026    303    468    396       O  
ATOM   2681  CB  ALA A1198      12.013  -9.706 -54.173  1.00 76.24           C  
ANISOU 2681  CB  ALA A1198     7901  13515   7551     56    567    721       C  
ATOM   2682  N   TYR A1199       9.195 -10.134 -53.132  1.00 69.35           N  
ANISOU 2682  N   TYR A1199     7666  11614   7069    185    483    355       N  
ATOM   2683  CA  TYR A1199       8.089  -9.768 -52.254  1.00 68.35           C  
ANISOU 2683  CA  TYR A1199     7776  11084   7112     83    407    247       C  
ATOM   2684  C   TYR A1199       7.413 -10.986 -51.637  1.00 67.47           C  
ANISOU 2684  C   TYR A1199     7780  10778   7076    348    430    104       C  
ATOM   2685  O   TYR A1199       7.000 -10.950 -50.479  1.00 74.75           O  
ANISOU 2685  O   TYR A1199     8789  11526   8085    293    379     48       O  
ATOM   2686  CB  TYR A1199       7.051  -8.908 -52.979  1.00 66.97           C  
ANISOU 2686  CB  TYR A1199     7794  10634   7018    -47    375    222       C  
ATOM   2687  CG  TYR A1199       5.890  -8.527 -52.087  1.00 68.02           C  
ANISOU 2687  CG  TYR A1199     8149  10390   7305   -107    310    110       C  
ATOM   2688  CD1 TYR A1199       5.992  -7.464 -51.201  1.00 69.38           C  
ANISOU 2688  CD1 TYR A1199     8384  10465   7514   -354    224    137       C  
ATOM   2689  CD2 TYR A1199       4.700  -9.243 -52.117  1.00 72.13           C  
ANISOU 2689  CD2 TYR A1199     8818  10671   7918     82    332    -21       C  
ATOM   2690  CE1 TYR A1199       4.938  -7.119 -50.376  1.00 72.61           C  
ANISOU 2690  CE1 TYR A1199     8993  10557   8040   -368    178     24       C  
ATOM   2691  CE2 TYR A1199       3.641  -8.905 -51.295  1.00 69.75           C  
ANISOU 2691  CE2 TYR A1199     8680  10086   7734     43    285   -110       C  
ATOM   2692  CZ  TYR A1199       3.766  -7.842 -50.427  1.00 68.85           C  
ANISOU 2692  CZ  TYR A1199     8620   9891   7648   -159    217    -93       C  
ATOM   2693  OH  TYR A1199       2.717  -7.497 -49.607  1.00 65.78           O  
ANISOU 2693  OH  TYR A1199     8392   9246   7354   -160    183   -192       O  
ATOM   2694  N   ALA A1200       7.292 -12.058 -52.413  1.00 60.62           N  
ANISOU 2694  N   ALA A1200     6933   9937   6164    623    502     46       N  
ATOM   2695  CA  ALA A1200       6.674 -13.283 -51.922  1.00 63.25           C  
ANISOU 2695  CA  ALA A1200     7408  10070   6554    855    509    -75       C  
ATOM   2696  C   ALA A1200       7.471 -13.857 -50.756  1.00 70.69           C  
ANISOU 2696  C   ALA A1200     8241  11152   7467    942    498    -41       C  
ATOM   2697  O   ALA A1200       6.920 -14.129 -49.689  1.00 74.32           O  
ANISOU 2697  O   ALA A1200     8808  11415   8015    926    453    -95       O  
ATOM   2698  CB  ALA A1200       6.552 -14.305 -53.040  1.00 67.36           C  
ANISOU 2698  CB  ALA A1200     7997  10598   7000   1123    574   -141       C  
ATOM   2699  N   ILE A1201       8.773 -14.024 -50.966  1.00 75.35           N  
ANISOU 2699  N   ILE A1201     8599  12115   7917   1036    541     62       N  
ATOM   2700  CA  ILE A1201       9.659 -14.562 -49.939  1.00 76.23           C  
ANISOU 2700  CA  ILE A1201     8565  12423   7975   1141    527    120       C  
ATOM   2701  C   ILE A1201       9.727 -13.662 -48.708  1.00 78.06           C  
ANISOU 2701  C   ILE A1201     8757  12639   8264    838    439    170       C  
ATOM   2702  O   ILE A1201       9.582 -14.134 -47.580  1.00 76.41           O  
ANISOU 2702  O   ILE A1201     8601  12334   8099    881    398    141       O  
ATOM   2703  CB  ILE A1201      11.080 -14.808 -50.490  1.00 72.92           C  
ANISOU 2703  CB  ILE A1201     7855  12480   7371   1303    595    243       C  
ATOM   2704  CG1 ILE A1201      11.058 -15.942 -51.518  1.00 67.68           C  
ANISOU 2704  CG1 ILE A1201     7269  11818   6627   1689    685    162       C  
ATOM   2705  CG2 ILE A1201      12.046 -15.138 -49.363  1.00 66.97           C  
ANISOU 2705  CG2 ILE A1201     6907  11981   6556   1363    563    337       C  
ATOM   2706  CD1 ILE A1201      12.394 -16.194 -52.176  1.00 70.63           C  
ANISOU 2706  CD1 ILE A1201     7353  12690   6795   1904    774    270       C  
ATOM   2707  N   ALA A1202       9.936 -12.367 -48.930  1.00 81.33           N  
ANISOU 2707  N   ALA A1202     9101  13134   8666    525    402    244       N  
ATOM   2708  CA  ALA A1202      10.029 -11.408 -47.832  1.00 80.58           C  
ANISOU 2708  CA  ALA A1202     9009  13006   8604    216    305    277       C  
ATOM   2709  C   ALA A1202       8.755 -11.386 -46.991  1.00 73.90           C  
ANISOU 2709  C   ALA A1202     8425  11753   7902    187    263    137       C  
ATOM   2710  O   ALA A1202       8.808 -11.500 -45.765  1.00 72.76           O  
ANISOU 2710  O   ALA A1202     8291  11588   7767    145    214    121       O  
ATOM   2711  CB  ALA A1202      10.340 -10.017 -48.363  1.00 45.95           C  
ANISOU 2711  CB  ALA A1202     4580   8699   4182   -121    260    371       C  
ATOM   2712  N   SER A1203       7.613 -11.247 -47.656  1.00 68.91           N  
ANISOU 2712  N   SER A1203     7986  10832   7365    212    285     43       N  
ATOM   2713  CA  SER A1203       6.333 -11.187 -46.961  1.00 68.39           C  
ANISOU 2713  CA  SER A1203     8137  10426   7420    194    257    -79       C  
ATOM   2714  C   SER A1203       6.003 -12.500 -46.259  1.00 75.26           C  
ANISOU 2714  C   SER A1203     9054  11228   8312    413    276   -136       C  
ATOM   2715  O   SER A1203       5.426 -12.494 -45.175  1.00 87.33           O  
ANISOU 2715  O   SER A1203    10674  12616   9890    363    241   -189       O  
ATOM   2716  CB  SER A1203       5.206 -10.799 -47.920  1.00 66.24           C  
ANISOU 2716  CB  SER A1203     8024   9916   7228    191    275   -143       C  
ATOM   2717  OG  SER A1203       5.119 -11.712 -48.998  1.00 71.59           O  
ANISOU 2717  OG  SER A1203     8691  10629   7880    400    338   -155       O  
ATOM   2718  N   SER A1204       6.367 -13.623 -46.870  1.00 66.95           N  
ANISOU 2718  N   SER A1204     7955  10271   7211    660    329   -122       N  
ATOM   2719  CA  SER A1204       6.126 -14.920 -46.242  1.00 60.83           C  
ANISOU 2719  CA  SER A1204     7260   9406   6449    867    331   -159       C  
ATOM   2720  C   SER A1204       6.977 -15.082 -44.987  1.00 64.90           C  
ANISOU 2720  C   SER A1204     7651  10100   6908    854    291    -87       C  
ATOM   2721  O   SER A1204       6.509 -15.599 -43.973  1.00 73.65           O  
ANISOU 2721  O   SER A1204     8853  11079   8050    876    259   -115       O  
ATOM   2722  CB  SER A1204       6.395 -16.067 -47.217  1.00 62.61           C  
ANISOU 2722  CB  SER A1204     7507   9665   6616   1155    385   -170       C  
ATOM   2723  OG  SER A1204       5.455 -16.069 -48.278  1.00 66.00           O  
ANISOU 2723  OG  SER A1204     8084   9900   7091   1162    408   -249       O  
ATOM   2724  N   ILE A1205       8.225 -14.631 -45.059  1.00 61.57           N  
ANISOU 2724  N   ILE A1205     7006  10002   6386    802    287     19       N  
ATOM   2725  CA  ILE A1205       9.141 -14.736 -43.927  1.00 61.46           C  
ANISOU 2725  CA  ILE A1205     6838  10218   6296    776    238    107       C  
ATOM   2726  C   ILE A1205       8.720 -13.827 -42.775  1.00 60.51           C  
ANISOU 2726  C   ILE A1205     6788   9989   6215    490    163     75       C  
ATOM   2727  O   ILE A1205       8.696 -14.248 -41.616  1.00 65.16           O  
ANISOU 2727  O   ILE A1205     7397  10569   6791    507    122     78       O  
ATOM   2728  CB  ILE A1205      10.595 -14.426 -44.344  1.00 59.66           C  
ANISOU 2728  CB  ILE A1205     6315  10423   5930    763    247    249       C  
ATOM   2729  CG1 ILE A1205      11.148 -15.556 -45.216  1.00 53.89           C  
ANISOU 2729  CG1 ILE A1205     5501   9852   5123   1136    329    278       C  
ATOM   2730  CG2 ILE A1205      11.479 -14.237 -43.122  1.00 58.17           C  
ANISOU 2730  CG2 ILE A1205     5953  10491   5658    642    171    350       C  
ATOM   2731  CD1 ILE A1205      12.575 -15.343 -45.655  1.00 49.21           C  
ANISOU 2731  CD1 ILE A1205     4576   9751   4370   1169    356    429       C  
ATOM   2732  N   VAL A1206       8.375 -12.585 -43.098  1.00 59.24           N  
ANISOU 2732  N   VAL A1206     6685   9734   6089    240    142     42       N  
ATOM   2733  CA  VAL A1206       7.968 -11.619 -42.080  1.00 64.44           C  
ANISOU 2733  CA  VAL A1206     7451  10266   6768    -13     70    -11       C  
ATOM   2734  C   VAL A1206       6.612 -11.960 -41.458  1.00 68.90           C  
ANISOU 2734  C   VAL A1206     8227  10525   7425     58     84   -137       C  
ATOM   2735  O   VAL A1206       6.466 -11.965 -40.236  1.00 73.82           O  
ANISOU 2735  O   VAL A1206     8891  11132   8024     -3     43   -164       O  
ATOM   2736  CB  VAL A1206       7.937 -10.181 -42.643  1.00 63.17           C  
ANISOU 2736  CB  VAL A1206     7344  10043   6616   -279     34    -14       C  
ATOM   2737  CG1 VAL A1206       7.333  -9.219 -41.631  1.00 42.03           C  
ANISOU 2737  CG1 VAL A1206     4851   7158   3959   -486    -37   -108       C  
ATOM   2738  CG2 VAL A1206       9.338  -9.737 -43.032  1.00 44.24           C  
ANISOU 2738  CG2 VAL A1206     4717   7995   4099   -432     -1    138       C  
ATOM   2739  N   SER A1207       5.626 -12.257 -42.298  1.00 66.03           N  
ANISOU 2739  N   SER A1207     7984   9954   7152    177    140   -203       N  
ATOM   2740  CA  SER A1207       4.266 -12.483 -41.816  1.00 68.12           C  
ANISOU 2740  CA  SER A1207     8421   9969   7494    215    153   -304       C  
ATOM   2741  C   SER A1207       4.078 -13.814 -41.089  1.00 71.98           C  
ANISOU 2741  C   SER A1207     8926  10451   7973    372    160   -290       C  
ATOM   2742  O   SER A1207       3.343 -13.884 -40.107  1.00 79.46           O  
ANISOU 2742  O   SER A1207     9956  11307   8929    332    148   -335       O  
ATOM   2743  CB  SER A1207       3.254 -12.373 -42.962  1.00 65.09           C  
ANISOU 2743  CB  SER A1207     8140   9396   7194    268    196   -362       C  
ATOM   2744  OG  SER A1207       3.315 -11.101 -43.581  1.00 63.47           O  
ANISOU 2744  OG  SER A1207     7953   9162   7001    121    180   -365       O  
ATOM   2745  N   PHE A1208       4.737 -14.867 -41.564  1.00 64.11           N  
ANISOU 2745  N   PHE A1208     7863   9552   6944    560    178   -224       N  
ATOM   2746  CA  PHE A1208       4.470 -16.206 -41.042  1.00 54.56           C  
ANISOU 2746  CA  PHE A1208     6728   8270   5732    724    174   -206       C  
ATOM   2747  C   PHE A1208       5.683 -16.945 -40.475  1.00 65.31           C  
ANISOU 2747  C   PHE A1208     7969   9844   7002    859    147   -100       C  
ATOM   2748  O   PHE A1208       5.669 -17.364 -39.317  1.00 74.95           O  
ANISOU 2748  O   PHE A1208     9208  11079   8192    851    107    -64       O  
ATOM   2749  CB  PHE A1208       3.793 -17.067 -42.112  1.00 47.47           C  
ANISOU 2749  CB  PHE A1208     5960   7190   4885    877    208   -244       C  
ATOM   2750  CG  PHE A1208       3.590 -18.498 -41.700  1.00 52.06           C  
ANISOU 2750  CG  PHE A1208     6663   7662   5455   1036    185   -215       C  
ATOM   2751  CD1 PHE A1208       2.522 -18.856 -40.895  1.00 57.28           C  
ANISOU 2751  CD1 PHE A1208     7449   8165   6151    948    160   -229       C  
ATOM   2752  CD2 PHE A1208       4.464 -19.487 -42.125  1.00 54.10           C  
ANISOU 2752  CD2 PHE A1208     6920   7979   5655   1280    188   -164       C  
ATOM   2753  CE1 PHE A1208       2.332 -20.172 -40.516  1.00 59.70           C  
ANISOU 2753  CE1 PHE A1208     7893   8350   6440   1058    123   -181       C  
ATOM   2754  CE2 PHE A1208       4.280 -20.804 -41.749  1.00 54.38           C  
ANISOU 2754  CE2 PHE A1208     7118   7865   5677   1431    151   -133       C  
ATOM   2755  CZ  PHE A1208       3.212 -21.146 -40.944  1.00 57.70           C  
ANISOU 2755  CZ  PHE A1208     7680   8105   6140   1299    111   -135       C  
ATOM   2756  N   TYR A1209       6.718 -17.112 -41.294  1.00 62.12           N  
ANISOU 2756  N   TYR A1209     7432   9629   6542    996    170    -42       N  
ATOM   2757  CA  TYR A1209       7.837 -17.993 -40.951  1.00 61.68           C  
ANISOU 2757  CA  TYR A1209     7256   9786   6392   1209    155     65       C  
ATOM   2758  C   TYR A1209       8.610 -17.610 -39.685  1.00 67.02           C  
ANISOU 2758  C   TYR A1209     7774  10701   6989   1084     91    153       C  
ATOM   2759  O   TYR A1209       8.881 -18.465 -38.838  1.00 65.88           O  
ANISOU 2759  O   TYR A1209     7635  10595   6800   1216     53    221       O  
ATOM   2760  CB  TYR A1209       8.780 -18.161 -42.145  1.00 56.70           C  
ANISOU 2760  CB  TYR A1209     6485   9363   5695   1401    209    108       C  
ATOM   2761  CG  TYR A1209       8.194 -19.022 -43.242  1.00 56.34           C  
ANISOU 2761  CG  TYR A1209     6628   9093   5686   1622    259     29       C  
ATOM   2762  CD1 TYR A1209       8.083 -20.399 -43.085  1.00 55.23           C  
ANISOU 2762  CD1 TYR A1209     6654   8796   5534   1890    245     29       C  
ATOM   2763  CD2 TYR A1209       7.745 -18.461 -44.430  1.00 59.11           C  
ANISOU 2763  CD2 TYR A1209     7014   9372   6071   1551    307    -42       C  
ATOM   2764  CE1 TYR A1209       7.545 -21.192 -44.079  1.00 55.17           C  
ANISOU 2764  CE1 TYR A1209     6859   8558   5543   2068    273    -55       C  
ATOM   2765  CE2 TYR A1209       7.205 -19.247 -45.432  1.00 62.36           C  
ANISOU 2765  CE2 TYR A1209     7609   9588   6498   1734    341   -120       C  
ATOM   2766  CZ  TYR A1209       7.107 -20.612 -45.250  1.00 63.25           C  
ANISOU 2766  CZ  TYR A1209     7901   9538   6593   1986    322   -134       C  
ATOM   2767  OH  TYR A1209       6.570 -21.401 -46.242  1.00 67.32           O  
ANISOU 2767  OH  TYR A1209     8638   9834   7108   2146    338   -223       O  
ATOM   2768  N   VAL A1210       8.963 -16.335 -39.554  1.00 70.67           N  
ANISOU 2768  N   VAL A1210     8113  11314   7424    820     66    158       N  
ATOM   2769  CA  VAL A1210       9.617 -15.860 -38.334  1.00 74.50           C  
ANISOU 2769  CA  VAL A1210     8474  12012   7820    646    -12    225       C  
ATOM   2770  C   VAL A1210       8.728 -15.998 -37.083  1.00 74.95           C  
ANISOU 2770  C   VAL A1210     8699  11879   7902    560    -49    167       C  
ATOM   2771  O   VAL A1210       9.178 -16.551 -36.071  1.00 77.57           O  
ANISOU 2771  O   VAL A1210     8974  12344   8156    610   -101    247       O  
ATOM   2772  CB  VAL A1210      10.186 -14.420 -38.486  1.00 50.43           C  
ANISOU 2772  CB  VAL A1210     5301   9137   4723    338    -51    239       C  
ATOM   2773  CG1 VAL A1210      10.502 -13.820 -37.124  1.00 46.30           C  
ANISOU 2773  CG1 VAL A1210     4744   8730   4116     97   -148    259       C  
ATOM   2774  CG2 VAL A1210      11.419 -14.427 -39.378  1.00 47.13           C  
ANISOU 2774  CG2 VAL A1210     4625   9062   4219    411    -31    364       C  
ATOM   2775  N   PRO A1211       7.467 -15.515 -37.143  1.00 66.30           N  
ANISOU 2775  N   PRO A1211     7794  10499   6897    444    -22     38       N  
ATOM   2776  CA  PRO A1211       6.582 -15.755 -35.996  1.00 65.54           C  
ANISOU 2776  CA  PRO A1211     7835  10264   6802    394    -40     -8       C  
ATOM   2777  C   PRO A1211       6.384 -17.241 -35.714  1.00 64.18           C  
ANISOU 2777  C   PRO A1211     7728  10022   6633    616    -38     62       C  
ATOM   2778  O   PRO A1211       6.258 -17.622 -34.552  1.00 73.24           O  
ANISOU 2778  O   PRO A1211     8905  11198   7723    589    -78    102       O  
ATOM   2779  CB  PRO A1211       5.259 -15.127 -36.441  1.00 63.12           C  
ANISOU 2779  CB  PRO A1211     7692   9698   6595    307      9   -143       C  
ATOM   2780  CG  PRO A1211       5.656 -14.067 -37.392  1.00 63.12           C  
ANISOU 2780  CG  PRO A1211     7638   9730   6615    203     15   -170       C  
ATOM   2781  CD  PRO A1211       6.827 -14.631 -38.137  1.00 60.75           C  
ANISOU 2781  CD  PRO A1211     7171   9634   6277    343     20    -58       C  
ATOM   2782  N   LEU A1212       6.358 -18.062 -36.760  1.00 51.50           N  
ANISOU 2782  N   LEU A1212     6169   8317   5082    825      2     76       N  
ATOM   2783  CA  LEU A1212       6.268 -19.509 -36.588  1.00 51.71           C  
ANISOU 2783  CA  LEU A1212     6304   8239   5104   1046    -14    145       C  
ATOM   2784  C   LEU A1212       7.448 -20.039 -35.774  1.00 59.16           C  
ANISOU 2784  C   LEU A1212     7114   9425   5938   1169    -72    284       C  
ATOM   2785  O   LEU A1212       7.259 -20.738 -34.774  1.00 64.44           O  
ANISOU 2785  O   LEU A1212     7861  10055   6570   1195   -120    352       O  
ATOM   2786  CB  LEU A1212       6.209 -20.217 -37.943  1.00 47.78           C  
ANISOU 2786  CB  LEU A1212     5896   7600   4658   1262     29    119       C  
ATOM   2787  CG  LEU A1212       6.323 -21.743 -37.896  1.00 51.79           C  
ANISOU 2787  CG  LEU A1212     6555   7978   5145   1527     -1    190       C  
ATOM   2788  CD1 LEU A1212       5.117 -22.364 -37.201  1.00 48.58           C  
ANISOU 2788  CD1 LEU A1212     6367   7313   4778   1422    -38    189       C  
ATOM   2789  CD2 LEU A1212       6.506 -22.323 -39.292  1.00 52.51           C  
ANISOU 2789  CD2 LEU A1212     6729   7972   5252   1764     41    146       C  
ATOM   2790  N   VAL A1213       8.660 -19.698 -36.204  1.00 55.18           N  
ANISOU 2790  N   VAL A1213     6395   9200   5372   1239    -70    341       N  
ATOM   2791  CA  VAL A1213       9.870 -20.146 -35.519  1.00 57.22           C  
ANISOU 2791  CA  VAL A1213     6475   9755   5511   1374   -127    489       C  
ATOM   2792  C   VAL A1213       9.891 -19.688 -34.063  1.00 59.01           C  
ANISOU 2792  C   VAL A1213     6654  10103   5665   1146   -202    528       C  
ATOM   2793  O   VAL A1213      10.149 -20.485 -33.156  1.00 63.10           O  
ANISOU 2793  O   VAL A1213     7182  10678   6117   1256   -259    635       O  
ATOM   2794  CB  VAL A1213      11.152 -19.659 -36.234  1.00 55.81           C  
ANISOU 2794  CB  VAL A1213     6017   9931   5257   1433   -110    555       C  
ATOM   2795  CG1 VAL A1213      12.386 -19.975 -35.400  1.00 51.74           C  
ANISOU 2795  CG1 VAL A1213     5270   9788   4602   1533   -180    723       C  
ATOM   2796  CG2 VAL A1213      11.264 -20.294 -37.610  1.00 49.93           C  
ANISOU 2796  CG2 VAL A1213     5312   9114   4544   1724    -32    529       C  
ATOM   2797  N   ILE A1214       9.605 -18.408 -33.843  1.00 55.56           N  
ANISOU 2797  N   ILE A1214     6190   9691   5230    836   -207    437       N  
ATOM   2798  CA  ILE A1214       9.596 -17.861 -32.489  1.00 58.22           C  
ANISOU 2798  CA  ILE A1214     6509  10136   5477    606   -277    442       C  
ATOM   2799  C   ILE A1214       8.564 -18.554 -31.597  1.00 60.23           C  
ANISOU 2799  C   ILE A1214     6961  10181   5744    622   -280    428       C  
ATOM   2800  O   ILE A1214       8.862 -18.903 -30.458  1.00 48.35           O  
ANISOU 2800  O   ILE A1214     5424   8813   4134    605   -346    518       O  
ATOM   2801  CB  ILE A1214       9.357 -16.340 -32.484  1.00 57.00           C  
ANISOU 2801  CB  ILE A1214     6362   9975   5320    287   -283    318       C  
ATOM   2802  CG1 ILE A1214      10.445 -15.628 -33.290  1.00 59.48           C  
ANISOU 2802  CG1 ILE A1214     6473  10528   5600    213   -299    366       C  
ATOM   2803  CG2 ILE A1214       9.333 -15.809 -31.062  1.00 54.62           C  
ANISOU 2803  CG2 ILE A1214     6080   9772   4902     66   -359    300       C  
ATOM   2804  CD1 ILE A1214      10.304 -14.122 -33.311  1.00 47.69           C  
ANISOU 2804  CD1 ILE A1214     5025   8999   4097   -118   -329    262       C  
ATOM   2805  N   MET A1215       7.359 -18.762 -32.122  1.00 58.79           N  
ANISOU 2805  N   MET A1215     6968   9695   5675    642   -214    331       N  
ATOM   2806  CA  MET A1215       6.297 -19.426 -31.368  1.00 60.08           C  
ANISOU 2806  CA  MET A1215     7304   9679   5843    628   -212    334       C  
ATOM   2807  C   MET A1215       6.660 -20.866 -31.008  1.00 71.76           C  
ANISOU 2807  C   MET A1215     8832  11147   7286    845   -262    494       C  
ATOM   2808  O   MET A1215       6.469 -21.294 -29.865  1.00 82.08           O  
ANISOU 2808  O   MET A1215    10183  12491   8512    797   -310    573       O  
ATOM   2809  CB  MET A1215       4.973 -19.389 -32.138  1.00 58.35           C  
ANISOU 2809  CB  MET A1215     7247   9178   5746    600   -139    219       C  
ATOM   2810  CG  MET A1215       4.283 -18.032 -32.121  1.00 64.10           C  
ANISOU 2810  CG  MET A1215     7981   9880   6492    391    -97     67       C  
ATOM   2811  SD  MET A1215       2.809 -17.965 -33.160  1.00 71.77           S  
ANISOU 2811  SD  MET A1215     9094  10575   7601    391    -15    -45       S  
ATOM   2812  CE  MET A1215       1.783 -19.208 -32.382  1.00127.99           C  
ANISOU 2812  CE  MET A1215    16344  17588  14697    401    -24     37       C  
ATOM   2813  N   VAL A1216       7.182 -21.605 -31.984  1.00 71.10           N  
ANISOU 2813  N   VAL A1216     8756  11008   7250   1097   -252    540       N  
ATOM   2814  CA  VAL A1216       7.625 -22.978 -31.751  1.00 67.82           C  
ANISOU 2814  CA  VAL A1216     8421  10550   6798   1357   -307    688       C  
ATOM   2815  C   VAL A1216       8.702 -23.029 -30.671  1.00 67.91           C  
ANISOU 2815  C   VAL A1216     8255  10877   6671   1390   -386    832       C  
ATOM   2816  O   VAL A1216       8.607 -23.811 -29.723  1.00 68.45           O  
ANISOU 2816  O   VAL A1216     8413  10917   6676   1431   -450    952       O  
ATOM   2817  CB  VAL A1216       8.173 -23.630 -33.038  1.00 64.38           C  
ANISOU 2817  CB  VAL A1216     8012  10040   6408   1665   -277    691       C  
ATOM   2818  CG1 VAL A1216       8.881 -24.937 -32.714  1.00 52.10           C  
ANISOU 2818  CG1 VAL A1216     6526   8483   4786   1984   -344    849       C  
ATOM   2819  CG2 VAL A1216       7.052 -23.862 -34.033  1.00 60.25           C  
ANISOU 2819  CG2 VAL A1216     7712   9176   6003   1646   -223    570       C  
ATOM   2820  N   PHE A1217       9.715 -22.181 -30.818  1.00 66.88           N  
ANISOU 2820  N   PHE A1217     7869  11059   6482   1350   -390    835       N  
ATOM   2821  CA  PHE A1217      10.816 -22.121 -29.863  1.00 73.73           C  
ANISOU 2821  CA  PHE A1217     8525  12286   7204   1353   -475    977       C  
ATOM   2822  C   PHE A1217      10.334 -21.784 -28.453  1.00 71.79           C  
ANISOU 2822  C   PHE A1217     8323  12081   6872   1092   -531    983       C  
ATOM   2823  O   PHE A1217      10.734 -22.427 -27.483  1.00 79.58           O  
ANISOU 2823  O   PHE A1217     9287  13197   7753   1165   -611   1132       O  
ATOM   2824  CB  PHE A1217      11.861 -21.101 -30.321  1.00 80.32           C  
ANISOU 2824  CB  PHE A1217     9073  13458   7985   1263   -475    970       C  
ATOM   2825  CG  PHE A1217      13.007 -20.934 -29.365  1.00 84.12           C  
ANISOU 2825  CG  PHE A1217     9306  14357   8300   1216   -576   1120       C  
ATOM   2826  CD1 PHE A1217      14.023 -21.874 -29.309  1.00 89.79           C  
ANISOU 2826  CD1 PHE A1217     9877  15300   8938   1543   -620   1304       C  
ATOM   2827  CD2 PHE A1217      13.074 -19.833 -28.528  1.00 82.01           C  
ANISOU 2827  CD2 PHE A1217     8958  14260   7942    855   -635   1076       C  
ATOM   2828  CE1 PHE A1217      15.079 -21.722 -28.431  1.00 93.27           C  
ANISOU 2828  CE1 PHE A1217    10061  16164   9215   1498   -722   1460       C  
ATOM   2829  CE2 PHE A1217      14.127 -19.675 -27.649  1.00 83.64           C  
ANISOU 2829  CE2 PHE A1217     8934  14866   7979    781   -744   1218       C  
ATOM   2830  CZ  PHE A1217      15.131 -20.621 -27.601  1.00 89.80           C  
ANISOU 2830  CZ  PHE A1217     9533  15903   8683   1096   -788   1419       C  
ATOM   2831  N   VAL A1218       9.469 -20.780 -28.352  1.00 67.36           N  
ANISOU 2831  N   VAL A1218     7832  11416   6344    810   -488    820       N  
ATOM   2832  CA  VAL A1218       8.940 -20.325 -27.069  1.00 71.18           C  
ANISOU 2832  CA  VAL A1218     8367  11950   6728    567   -522    789       C  
ATOM   2833  C   VAL A1218       8.092 -21.390 -26.371  1.00 64.25           C  
ANISOU 2833  C   VAL A1218     7676  10896   5840    628   -530    869       C  
ATOM   2834  O   VAL A1218       8.314 -21.699 -25.196  1.00 61.11           O  
ANISOU 2834  O   VAL A1218     7257  10654   5307    584   -601    981       O  
ATOM   2835  CB  VAL A1218       8.127 -19.016 -27.231  1.00 78.64           C  
ANISOU 2835  CB  VAL A1218     9376  12792   7712    309   -462    579       C  
ATOM   2836  CG1 VAL A1218       7.089 -18.875 -26.129  1.00 81.22           C  
ANISOU 2836  CG1 VAL A1218     9838  13055   7965    151   -451    519       C  
ATOM   2837  CG2 VAL A1218       9.057 -17.810 -27.259  1.00 50.58           C  
ANISOU 2837  CG2 VAL A1218     5656   9477   4086    128   -509    532       C  
ATOM   2838  N   TYR A1219       7.128 -21.957 -27.092  1.00 64.95           N  
ANISOU 2838  N   TYR A1219     7946  10673   6058    706   -465    825       N  
ATOM   2839  CA  TYR A1219       6.262 -22.977 -26.509  1.00 69.45           C  
ANISOU 2839  CA  TYR A1219     8706  11065   6616    718   -481    917       C  
ATOM   2840  C   TYR A1219       7.042 -24.242 -26.157  1.00 78.64           C  
ANISOU 2840  C   TYR A1219     9903  12253   7725    954   -573   1132       C  
ATOM   2841  O   TYR A1219       6.732 -24.921 -25.174  1.00 80.87           O  
ANISOU 2841  O   TYR A1219    10283  12523   7922    915   -629   1264       O  
ATOM   2842  CB  TYR A1219       5.085 -23.289 -27.435  1.00 67.21           C  
ANISOU 2842  CB  TYR A1219     8604  10457   6474    717   -409    831       C  
ATOM   2843  CG  TYR A1219       4.037 -22.200 -27.454  1.00 73.32           C  
ANISOU 2843  CG  TYR A1219     9375  11210   7275    489   -325    655       C  
ATOM   2844  CD1 TYR A1219       3.830 -21.392 -26.342  1.00 71.63           C  
ANISOU 2844  CD1 TYR A1219     9094  11187   6935    297   -322    606       C  
ATOM   2845  CD2 TYR A1219       3.259 -21.974 -28.580  1.00 81.77           C  
ANISOU 2845  CD2 TYR A1219    10514  12075   8478    485   -253    535       C  
ATOM   2846  CE1 TYR A1219       2.875 -20.392 -26.352  1.00 69.94           C  
ANISOU 2846  CE1 TYR A1219     8894  10949   6731    141   -242    437       C  
ATOM   2847  CE2 TYR A1219       2.301 -20.975 -28.599  1.00 80.39           C  
ANISOU 2847  CE2 TYR A1219    10332  11891   8322    317   -179    384       C  
ATOM   2848  CZ  TYR A1219       2.115 -20.188 -27.483  1.00 73.56           C  
ANISOU 2848  CZ  TYR A1219     9410  11207   7333    162   -171    333       C  
ATOM   2849  OH  TYR A1219       1.164 -19.194 -27.499  1.00 74.28           O  
ANISOU 2849  OH  TYR A1219     9510  11285   7429     46    -93    174       O  
ATOM   2850  N   SER A1220       8.062 -24.546 -26.954  1.00 83.24           N  
ANISOU 2850  N   SER A1220    10401  12883   8343   1210   -589   1176       N  
ATOM   2851  CA  SER A1220       8.955 -25.654 -26.641  1.00 88.24           C  
ANISOU 2851  CA  SER A1220    11042  13575   8909   1493   -678   1378       C  
ATOM   2852  C   SER A1220       9.726 -25.356 -25.360  1.00 87.72           C  
ANISOU 2852  C   SER A1220    10784  13872   8672   1407   -763   1500       C  
ATOM   2853  O   SER A1220       9.948 -26.246 -24.540  1.00 89.59           O  
ANISOU 2853  O   SER A1220    11089  14130   8821   1516   -850   1685       O  
ATOM   2854  CB  SER A1220       9.925 -25.916 -27.794  1.00 92.40           C  
ANISOU 2854  CB  SER A1220    11480  14144   9486   1815   -659   1383       C  
ATOM   2855  OG  SER A1220       9.224 -26.222 -28.986  1.00 94.08           O  
ANISOU 2855  OG  SER A1220    11888  14021   9837   1895   -588   1265       O  
ATOM   2856  N   ARG A1221      10.127 -24.098 -25.193  1.00 85.14           N  
ANISOU 2856  N   ARG A1221    10236  13823   8290   1197   -749   1401       N  
ATOM   2857  CA  ARG A1221      10.821 -23.669 -23.983  1.00 84.82           C  
ANISOU 2857  CA  ARG A1221    10016  14141   8069   1055   -838   1491       C  
ATOM   2858  C   ARG A1221       9.930 -23.816 -22.757  1.00 83.77           C  
ANISOU 2858  C   ARG A1221    10032  13953   7845    855   -863   1516       C  
ATOM   2859  O   ARG A1221      10.398 -24.206 -21.690  1.00 86.70           O  
ANISOU 2859  O   ARG A1221    10350  14527   8063    860   -959   1679       O  
ATOM   2860  CB  ARG A1221      11.311 -22.224 -24.111  1.00 85.44           C  
ANISOU 2860  CB  ARG A1221     9886  14472   8106    815   -829   1356       C  
ATOM   2861  CG  ARG A1221      12.611 -22.070 -24.884  1.00 95.32           C  
ANISOU 2861  CG  ARG A1221    10882  15984   9351    974   -850   1422       C  
ATOM   2862  CD  ARG A1221      13.772 -22.730 -24.153  1.00107.00           C  
ANISOU 2862  CD  ARG A1221    12173  17806  10678   1153   -966   1658       C  
ATOM   2863  NE  ARG A1221      14.039 -22.102 -22.861  1.00111.44           N  
ANISOU 2863  NE  ARG A1221    12630  18653  11058    866  -1064   1692       N  
ATOM   2864  CZ  ARG A1221      14.914 -21.120 -22.672  1.00112.17           C  
ANISOU 2864  CZ  ARG A1221    12476  19110  11034    651  -1129   1687       C  
ATOM   2865  NH1 ARG A1221      15.616 -20.647 -23.694  1.00109.30           N  
ANISOU 2865  NH1 ARG A1221    11921  18891  10718    683  -1100   1668       N  
ATOM   2866  NH2 ARG A1221      15.091 -20.610 -21.461  1.00115.24           N  
ANISOU 2866  NH2 ARG A1221    12815  19729  11242    383  -1229   1706       N  
ATOM   2867  N   VAL A1222       8.647 -23.502 -22.910  1.00 80.54           N  
ANISOU 2867  N   VAL A1222     9790  13299   7511    685   -774   1365       N  
ATOM   2868  CA  VAL A1222       7.691 -23.683 -21.820  1.00 73.62           C  
ANISOU 2868  CA  VAL A1222     9045  12390   6538    505   -777   1392       C  
ATOM   2869  C   VAL A1222       7.527 -25.161 -21.477  1.00 76.67           C  
ANISOU 2869  C   VAL A1222     9596  12624   6913    667   -840   1616       C  
ATOM   2870  O   VAL A1222       7.658 -25.559 -20.315  1.00 68.21           O  
ANISOU 2870  O   VAL A1222     8527  11704   5684    615   -918   1772       O  
ATOM   2871  CB  VAL A1222       6.311 -23.090 -22.162  1.00 63.19           C  
ANISOU 2871  CB  VAL A1222     7843  10865   5299    325   -659   1196       C  
ATOM   2872  CG1 VAL A1222       5.298 -23.456 -21.090  1.00 61.12           C  
ANISOU 2872  CG1 VAL A1222     7699  10600   4924    171   -651   1258       C  
ATOM   2873  CG2 VAL A1222       6.404 -21.584 -22.317  1.00 62.93           C  
ANISOU 2873  CG2 VAL A1222     7699  10959   5253    154   -612    979       C  
ATOM   2874  N   PHE A1223       7.250 -25.971 -22.497  1.00 88.04           N  
ANISOU 2874  N   PHE A1223    11194  13751   8508    856   -816   1635       N  
ATOM   2875  CA  PHE A1223       7.039 -27.404 -22.310  1.00 95.77           C  
ANISOU 2875  CA  PHE A1223    12398  14500   9489   1007   -889   1839       C  
ATOM   2876  C   PHE A1223       8.264 -28.102 -21.721  1.00101.45           C  
ANISOU 2876  C   PHE A1223    13051  15397  10098   1246  -1012   2061       C  
ATOM   2877  O   PHE A1223       8.138 -29.099 -21.010  1.00 97.62           O  
ANISOU 2877  O   PHE A1223    12729  14822   9540   1295  -1100   2266       O  
ATOM   2878  CB  PHE A1223       6.648 -28.065 -23.635  1.00 93.52           C  
ANISOU 2878  CB  PHE A1223    12313  13837   9381   1178   -853   1788       C  
ATOM   2879  N   GLN A1224       9.446 -27.569 -22.015  1.00109.19           N  
ANISOU 2879  N   GLN A1224    13783  16647  11058   1388  -1024   2036       N  
ATOM   2880  CA  GLN A1224      10.694 -28.155 -21.535  1.00114.09           C  
ANISOU 2880  CA  GLN A1224    14283  17502  11566   1646  -1138   2250       C  
ATOM   2881  C   GLN A1224      11.049 -27.676 -20.130  1.00112.55           C  
ANISOU 2881  C   GLN A1224    13915  17683  11167   1435  -1215   2342       C  
ATOM   2882  O   GLN A1224      11.576 -28.441 -19.321  1.00111.46           O  
ANISOU 2882  O   GLN A1224    13782  17660  10906   1572  -1329   2573       O  
ATOM   2883  CB  GLN A1224      11.841 -27.841 -22.500  1.00113.02           C  
ANISOU 2883  CB  GLN A1224    13919  17551  11475   1896  -1117   2208       C  
ATOM   2884  N   GLU A1225      10.761 -26.410 -19.844  1.00110.14           N  
ANISOU 2884  N   GLU A1225    13477  17557  10813   1111  -1161   2160       N  
ATOM   2885  CA  GLU A1225      11.088 -25.828 -18.547  1.00110.99           C  
ANISOU 2885  CA  GLU A1225    13438  18026  10708    884  -1235   2207       C  
ATOM   2886  C   GLU A1225      10.075 -26.238 -17.480  1.00105.80           C  
ANISOU 2886  C   GLU A1225    12972  17280   9948    704  -1244   2276       C  
ATOM   2887  O   GLU A1225      10.357 -26.174 -16.283  1.00103.43           O  
ANISOU 2887  O   GLU A1225    12600  17255   9444    583  -1328   2387       O  
ATOM   2888  CB  GLU A1225      11.186 -24.303 -18.645  1.00113.52           C  
ANISOU 2888  CB  GLU A1225    13591  18542  10998    610  -1186   1973       C  
ATOM   2889  CG  GLU A1225      11.806 -23.637 -17.428  1.00122.86           C  
ANISOU 2889  CG  GLU A1225    14606  20131  11943    391  -1287   2010       C  
ATOM   2890  CD  GLU A1225      12.177 -22.190 -17.679  1.00129.29           C  
ANISOU 2890  CD  GLU A1225    15271  21124  12730    151  -1273   1802       C  
ATOM   2891  OE1 GLU A1225      12.672 -21.532 -16.739  1.00135.54           O  
ANISOU 2891  OE1 GLU A1225    15950  22231  13317    -69  -1364   1800       O  
ATOM   2892  OE2 GLU A1225      11.979 -21.712 -18.816  1.00125.97           O  
ANISOU 2892  OE2 GLU A1225    14863  20520  12480    169  -1181   1645       O  
ATOM   2893  N   ALA A1226       8.897 -26.670 -17.918  1.00 98.17           N  
ANISOU 2893  N   ALA A1226    12238  15956   9106    673  -1162   2224       N  
ATOM   2894  CA  ALA A1226       7.884 -27.173 -16.997  1.00 83.15           C  
ANISOU 2894  CA  ALA A1226    10509  13978   7105    500  -1166   2321       C  
ATOM   2895  C   ALA A1226       8.305 -28.514 -16.400  1.00 83.96           C  
ANISOU 2895  C   ALA A1226    10729  14042   7130    681  -1300   2636       C  
ATOM   2896  O   ALA A1226       7.778 -28.940 -15.374  1.00 79.44           O  
ANISOU 2896  O   ALA A1226    10254  13515   6413    530  -1341   2782       O  
ATOM   2897  CB  ALA A1226       6.543 -27.304 -17.700  1.00 74.56           C  
ANISOU 2897  CB  ALA A1226     9613  12548   6166    405  -1054   2205       C  
ATOM   2898  N   LYS A1227       9.259 -29.176 -17.048  1.00 94.19           N  
ANISOU 2898  N   LYS A1227    12018  15260   8510   1021  -1367   2746       N  
ATOM   2899  CA  LYS A1227       9.703 -30.498 -16.619  1.00102.36           C  
ANISOU 2899  CA  LYS A1227    13203  16201   9489   1263  -1500   3045       C  
ATOM   2900  C   LYS A1227      10.939 -30.436 -15.725  1.00112.01           C  
ANISOU 2900  C   LYS A1227    14191  17846  10522   1369  -1622   3217       C  
ATOM   2901  O   LYS A1227      11.485 -31.470 -15.338  1.00115.88           O  
ANISOU 2901  O   LYS A1227    14770  18310  10949   1617  -1746   3481       O  
ATOM   2902  CB  LYS A1227       9.978 -31.387 -17.836  1.00 97.16           C  
ANISOU 2902  CB  LYS A1227    12721  15183   9013   1631  -1508   3072       C  
ATOM   2903  N   ARG A1228      11.377 -29.224 -15.398  1.00114.85           N  
ANISOU 2903  N   ARG A1228    14266  18588  10782   1177  -1599   3075       N  
ATOM   2904  CA  ARG A1228      12.571 -29.046 -14.576  1.00120.72           C  
ANISOU 2904  CA  ARG A1228    14753  19784  11331   1228  -1724   3227       C  
ATOM   2905  C   ARG A1228      12.344 -28.083 -13.412  1.00116.52           C  
ANISOU 2905  C   ARG A1228    14103  19584  10585    838  -1736   3148       C  
ATOM   2906  O   ARG A1228      13.262 -27.380 -12.988  1.00114.32           O  
ANISOU 2906  O   ARG A1228    13568  19687  10182    758  -1798   3129       O  
ATOM   2907  CB  ARG A1228      13.750 -28.578 -15.434  1.00124.93           C  
ANISOU 2907  CB  ARG A1228    15011  20530  11926   1434  -1725   3167       C  
ATOM   2908  CG  ARG A1228      13.496 -27.288 -16.198  1.00125.61           C  
ANISOU 2908  CG  ARG A1228    14987  20629  12112   1208  -1602   2857       C  
ATOM   2909  CD  ARG A1228      14.686 -26.911 -17.067  1.00131.63           C  
ANISOU 2909  CD  ARG A1228    15470  21623  12920   1402  -1609   2839       C  
ATOM   2910  NE  ARG A1228      14.448 -25.678 -17.811  1.00133.76           N  
ANISOU 2910  NE  ARG A1228    15658  21884  13281   1167  -1503   2563       N  
ATOM   2911  CZ  ARG A1228      15.308 -25.143 -18.673  1.00133.07           C  
ANISOU 2911  CZ  ARG A1228    15335  21986  13241   1245  -1486   2511       C  
ATOM   2912  NH1 ARG A1228      16.471 -25.734 -18.905  1.00132.15           N  
ANISOU 2912  NH1 ARG A1228    15012  22119  13081   1575  -1556   2709       N  
ATOM   2913  NH2 ARG A1228      15.003 -24.017 -19.302  1.00131.80           N  
ANISOU 2913  NH2 ARG A1228    15140  21779  13157   1003  -1399   2272       N  
ATOM   2914  N   GLN A1229      11.120 -28.057 -12.895  1.00113.91           N  
ANISOU 2914  N   GLN A1229    13964  19101  10214    589  -1670   3089       N  
ATOM   2915  CA  GLN A1229      10.791 -27.207 -11.755  1.00116.30           C  
ANISOU 2915  CA  GLN A1229    14198  19701  10290    247  -1668   3001       C  
ATOM   2916  C   GLN A1229      11.122 -27.908 -10.441  1.00128.04           C  
ANISOU 2916  C   GLN A1229    15698  21332  11619    233  -1777   3232       C  
ATOM   2917  O   GLN A1229      11.788 -28.944 -10.432  1.00137.74           O  
ANISOU 2917  O   GLN A1229    16953  22489  12892    502  -1876   3470       O  
ATOM   2918  CB  GLN A1229       9.316 -26.809 -11.790  1.00113.56           C  
ANISOU 2918  CB  GLN A1229    14021  19143   9983      8  -1518   2803       C  
ATOM   2919  CG  GLN A1229       8.934 -25.966 -12.995  1.00114.03           C  
ANISOU 2919  CG  GLN A1229    14070  19002  10255    -12  -1382   2507       C  
ATOM   2920  CD  GLN A1229       9.624 -24.616 -13.004  1.00112.33           C  
ANISOU 2920  CD  GLN A1229    13654  19056   9972   -146  -1386   2296       C  
ATOM   2921  OE1 GLN A1229       9.607 -23.892 -12.009  1.00108.43           O  
ANISOU 2921  OE1 GLN A1229    13110  18831   9257   -376  -1411   2220       O  
ATOM   2922  NE2 GLN A1229      10.238 -24.272 -14.130  1.00114.45           N  
ANISOU 2922  NE2 GLN A1229    13819  19253  10414    -16  -1368   2202       N  
ATOM   2923  N   LEU A1230      10.654 -27.342  -9.333  1.00125.61           N  
ANISOU 2923  N   LEU A1230    15386  21194  11145    -62  -1748   3137       N  
ATOM   2924  CA  LEU A1230      10.912 -27.910  -8.013  1.00124.19           C  
ANISOU 2924  CA  LEU A1230    15215  21152  10819   -109  -1834   3323       C  
ATOM   2925  C   LEU A1230       9.925 -29.025  -7.677  1.00131.00           C  
ANISOU 2925  C   LEU A1230    16332  21772  11669   -111  -1827   3524       C  
ATOM   2926  O   LEU A1230       9.278 -28.998  -6.630  1.00126.31           O  
ANISOU 2926  O   LEU A1230    15793  21273  10927   -330  -1797   3534       O  
ATOM   2927  CB  LEU A1230      10.857 -26.820  -6.940  1.00118.14           C  
ANISOU 2927  CB  LEU A1230    14343  20678   9866   -416  -1806   3130       C  
ATOM   2928  CG  LEU A1230      11.878 -25.686  -7.060  1.00115.44           C  
ANISOU 2928  CG  LEU A1230    13773  20584   9504   -489  -1840   2948       C  
ATOM   2929  CD1 LEU A1230      11.658 -24.643  -5.975  1.00115.30           C  
ANISOU 2929  CD1 LEU A1230    13732  20784   9293   -800  -1814   2746       C  
ATOM   2930  CD2 LEU A1230      13.295 -26.232  -7.000  1.00115.99           C  
ANISOU 2930  CD2 LEU A1230    13661  20814   9597   -280  -1979   3160       C  
ATOM   2931  N   GLN A1231       9.816 -30.005  -8.569  1.00141.65           N  
ANISOU 2931  N   GLN A1231    17843  22805  13171    128  -1856   3687       N  
ATOM   2932  CA  GLN A1231       8.891 -31.118  -8.381  1.00146.36           C  
ANISOU 2932  CA  GLN A1231    18719  23118  13774    105  -1868   3896       C  
ATOM   2933  C   GLN A1231       9.574 -32.455  -8.648  1.00148.07           C  
ANISOU 2933  C   GLN A1231    19093  23086  14082    444  -2009   4182       C  
ATOM   2934  O   GLN A1231       9.521 -32.979  -9.761  1.00145.97           O  
ANISOU 2934  O   GLN A1231    18971  22514  13977    666  -2016   4224       O  
ATOM   2935  CB  GLN A1231       7.672 -30.960  -9.293  1.00142.24           C  
ANISOU 2935  CB  GLN A1231    18335  22360  13350     -7  -1745   3779       C  
ATOM   2936  N   LYS A1263       4.881 -36.927 -11.062  1.00150.36           N  
ANISOU 2936  N   LYS A1263    15380  27691  14059   -710  -3409   4963       N  
ATOM   2937  CA  LYS A1263       4.179 -38.186 -10.845  1.00153.04           C  
ANISOU 2937  CA  LYS A1263    15575  28052  14523   -728  -3073   5552       C  
ATOM   2938  C   LYS A1263       3.295 -38.534 -12.037  1.00151.45           C  
ANISOU 2938  C   LYS A1263    15357  27361  14826   -756  -2591   5312       C  
ATOM   2939  O   LYS A1263       2.484 -39.459 -11.968  1.00152.61           O  
ANISOU 2939  O   LYS A1263    15401  27501  15083   -776  -2258   5673       O  
ATOM   2940  CB  LYS A1263       3.338 -38.117  -9.568  1.00155.58           C  
ANISOU 2940  CB  LYS A1263    16034  29129  13950   -683  -3060   5732       C  
ATOM   2941  N   PHE A1264       3.466 -37.786 -13.125  1.00149.57           N  
ANISOU 2941  N   PHE A1264    15214  26720  14897   -758  -2565   4712       N  
ATOM   2942  CA  PHE A1264       2.686 -37.971 -14.349  1.00146.06           C  
ANISOU 2942  CA  PHE A1264    14782  25823  14891   -785  -2161   4402       C  
ATOM   2943  C   PHE A1264       1.182 -37.914 -14.089  1.00150.20           C  
ANISOU 2943  C   PHE A1264    15427  26689  14955   -768  -1860   4266       C  
ATOM   2944  O   PHE A1264       0.483 -38.920 -14.208  1.00150.27           O  
ANISOU 2944  O   PHE A1264    15298  26577  15221   -808  -1543   4598       O  
ATOM   2945  CB  PHE A1264       3.062 -39.285 -15.043  1.00142.53           C  
ANISOU 2945  CB  PHE A1264    14068  24799  15287   -849  -1948   4839       C  
ATOM   2946  N   ALA A1265       0.695 -36.730 -13.732  1.00154.28           N  
ANISOU 2946  N   ALA A1265    16180  27609  14831   -709  -1952   3773       N  
ATOM   2947  CA  ALA A1265      -0.717 -36.542 -13.417  1.00156.16           C  
ANISOU 2947  CA  ALA A1265    16531  28200  14601   -679  -1673   3612       C  
ATOM   2948  C   ALA A1265      -1.524 -36.144 -14.649  1.00150.17           C  
ANISOU 2948  C   ALA A1265    15841  27080  14136   -686  -1402   3083       C  
ATOM   2949  O   ALA A1265      -1.095 -36.363 -15.782  1.00145.15           O  
ANISOU 2949  O   ALA A1265    15134  25893  14122   -729  -1351   2966       O  
ATOM   2950  CB  ALA A1265      -0.883 -35.508 -12.311  1.00158.13           C  
ANISOU 2950  CB  ALA A1265    16991  29098  13992   -605  -1885   3365       C  
ATOM   2951  N   LEU A1266      -2.693 -35.553 -14.418  1.00149.52           N  
ANISOU 2951  N   LEU A1266    15893  27322  13594   -640  -1226   2770       N  
ATOM   2952  CA  LEU A1266      -3.607 -35.206 -15.500  1.00145.06           C  
ANISOU 2952  CA  LEU A1266    15375  26475  13266   -644   -971   2316       C  
ATOM   2953  C   LEU A1266      -3.501 -33.740 -15.913  1.00142.17           C  
ANISOU 2953  C   LEU A1266    15209  26113  12695   -578  -1129   1651       C  
ATOM   2954  O   LEU A1266      -3.943 -33.361 -16.999  1.00140.43           O  
ANISOU 2954  O   LEU A1266    15024  25574  12758   -578   -995   1269       O  
ATOM   2955  CB  LEU A1266      -5.049 -35.534 -15.102  1.00142.28           C  
ANISOU 2955  CB  LEU A1266    14995  26407  12659   -636   -639   2411       C  
ATOM   2956  N   LYS A1267      -2.915 -32.920 -15.046  1.00136.00           N  
ANISOU 2956  N   LYS A1267    14550  25691  11431   -523  -1422   1519       N  
ATOM   2957  CA  LYS A1267      -2.816 -31.486 -15.297  1.00126.10           C  
ANISOU 2957  CA  LYS A1267    13471  24461   9980   -458  -1575    892       C  
ATOM   2958  C   LYS A1267      -1.859 -31.186 -16.448  1.00122.53           C  
ANISOU 2958  C   LYS A1267    12995  23460  10102   -480  -1712    687       C  
ATOM   2959  O   LYS A1267      -2.150 -30.355 -17.313  1.00125.17           O  
ANISOU 2959  O   LYS A1267    13411  23571  10575   -444  -1649    220       O  
ATOM   2960  CB  LYS A1267      -2.367 -30.753 -14.032  1.00124.22           C  
ANISOU 2960  CB  LYS A1267    13355  24738   9104   -408  -1873    798       C  
ATOM   2961  CG  LYS A1267      -2.783 -29.292 -13.981  1.00120.86           C  
ANISOU 2961  CG  LYS A1267    13147  24176   8600   -318  -1821    133       C  
ATOM   2962  CD  LYS A1267      -4.296 -29.156 -14.024  1.00120.18           C  
ANISOU 2962  CD  LYS A1267    13097  24209   8356   -273  -1453    -39       C  
ATOM   2963  CE  LYS A1267      -4.732 -27.719 -13.789  1.00120.13           C  
ANISOU 2963  CE  LYS A1267    13277  24083   8285   -176  -1409   -616       C  
ATOM   2964  NZ  LYS A1267      -4.395 -27.258 -12.412  1.00124.28           N  
ANISOU 2964  NZ  LYS A1267    13945  24847   8430   -138  -1555   -655       N  
ATOM   2965  N   GLU A1268      -0.719 -31.872 -16.451  1.00120.12           N  
ANISOU 2965  N   GLU A1268    12564  22937  10140   -532  -1885   1063       N  
ATOM   2966  CA  GLU A1268       0.281 -31.702 -17.501  1.00119.15           C  
ANISOU 2966  CA  GLU A1268    12394  22284  10594   -551  -1986    935       C  
ATOM   2967  C   GLU A1268      -0.253 -32.165 -18.854  1.00120.80           C  
ANISOU 2967  C   GLU A1268    12562  22029  11307   -583  -1666    849       C  
ATOM   2968  O   GLU A1268       0.053 -31.570 -19.888  1.00115.81           O  
ANISOU 2968  O   GLU A1268    11981  21042  10979   -565  -1659    511       O  
ATOM   2969  CB  GLU A1268       1.566 -32.458 -17.156  1.00120.62           C  
ANISOU 2969  CB  GLU A1268    12418  22336  11076   -599  -2210   1413       C  
ATOM   2970  CG  GLU A1268       2.399 -31.825 -16.047  1.00127.68           C  
ANISOU 2970  CG  GLU A1268    13349  23598  11565   -574  -2624   1419       C  
ATOM   2971  CD  GLU A1268       1.800 -32.021 -14.666  1.00133.40           C  
ANISOU 2971  CD  GLU A1268    14126  24963  11598   -558  -2670   1648       C  
ATOM   2972  OE1 GLU A1268       0.892 -32.867 -14.521  1.00139.92           O  
ANISOU 2972  OE1 GLU A1268    14906  25901  12357   -573  -2376   1943       O  
ATOM   2973  OE2 GLU A1268       2.239 -31.327 -13.724  1.00128.47           O  
ANISOU 2973  OE2 GLU A1268    13586  24731  10495   -531  -2996   1527       O  
ATOM   2974  N   HIS A1269      -1.049 -33.231 -18.837  1.00124.83           N  
ANISOU 2974  N   HIS A1269    12977  22551  11903   -632  -1403   1160       N  
ATOM   2975  CA  HIS A1269      -1.696 -33.728 -20.045  1.00117.68           C  
ANISOU 2975  CA  HIS A1269    12031  21257  11426   -675  -1108   1056       C  
ATOM   2976  C   HIS A1269      -2.646 -32.673 -20.603  1.00101.99           C  
ANISOU 2976  C   HIS A1269    10197  19335   9219   -618  -1013    517       C  
ATOM   2977  O   HIS A1269      -2.664 -32.412 -21.807  1.00 96.89           O  
ANISOU 2977  O   HIS A1269     9590  18329   8894   -620   -930    235       O  
ATOM   2978  CB  HIS A1269      -2.474 -35.015 -19.754  1.00131.54           C  
ANISOU 2978  CB  HIS A1269    13635  23058  13284   -743   -859   1479       C  
ATOM   2979  CG  HIS A1269      -1.623 -36.146 -19.264  1.00145.32           C  
ANISOU 2979  CG  HIS A1269    15197  24699  15321   -797   -916   2059       C  
ATOM   2980  ND1 HIS A1269      -2.158 -37.330 -18.803  1.00151.58           N  
ANISOU 2980  ND1 HIS A1269    15821  25548  16222   -853   -721   2533       N  
ATOM   2981  CD2 HIS A1269      -0.279 -36.276 -19.166  1.00149.96           C  
ANISOU 2981  CD2 HIS A1269    15715  25108  16155   -801  -1141   2266       C  
ATOM   2982  CE1 HIS A1269      -1.179 -38.140 -18.439  1.00156.11           C  
ANISOU 2982  CE1 HIS A1269    16235  25987  17094   -885   -825   3017       C  
ATOM   2983  NE2 HIS A1269      -0.030 -37.525 -18.649  1.00155.09           N  
ANISOU 2983  NE2 HIS A1269    16159  25716  17051   -855  -1085   2864       N  
ATOM   2984  N   LYS A1270      -3.433 -32.071 -19.714  1.00 99.07           N  
ANISOU 2984  N   LYS A1270     9910  19435   8298   -562  -1019    390       N  
ATOM   2985  CA  LYS A1270      -4.404 -31.052 -20.099  1.00 97.87           C  
ANISOU 2985  CA  LYS A1270     9876  19377   7932   -497   -923    -93       C  
ATOM   2986  C   LYS A1270      -3.717 -29.819 -20.681  1.00100.67           C  
ANISOU 2986  C   LYS A1270    10349  19549   8352   -434  -1113   -522       C  
ATOM   2987  O   LYS A1270      -4.159 -29.265 -21.690  1.00100.99           O  
ANISOU 2987  O   LYS A1270    10441  19369   8561   -405  -1016   -851       O  
ATOM   2988  CB  LYS A1270      -5.267 -30.657 -18.897  1.00 95.54           C  
ANISOU 2988  CB  LYS A1270     9636  19630   7033   -441   -882   -128       C  
ATOM   2989  N   ALA A1271      -2.633 -29.398 -20.037  1.00104.17           N  
ANISOU 2989  N   ALA A1271    10819  20084   8676   -415  -1392   -497       N  
ATOM   2990  CA  ALA A1271      -1.843 -28.267 -20.514  1.00105.71           C  
ANISOU 2990  CA  ALA A1271    11092  20077   8997   -363  -1587   -861       C  
ATOM   2991  C   ALA A1271      -1.223 -28.555 -21.881  1.00 99.90           C  
ANISOU 2991  C   ALA A1271    10309  18793   8856   -394  -1517   -849       C  
ATOM   2992  O   ALA A1271      -1.201 -27.690 -22.766  1.00 95.90           O  
ANISOU 2992  O   ALA A1271     9873  18058   8508   -343  -1501  -1194       O  
ATOM   2993  CB  ALA A1271      -0.761 -27.928 -19.507  1.00112.97           C  
ANISOU 2993  CB  ALA A1271    12012  21192   9718   -357  -1920   -790       C  
ATOM   2994  N   LEU A1272      -0.719 -29.777 -22.042  1.00 99.80           N  
ANISOU 2994  N   LEU A1272    10175  18570   9176   -472  -1461   -440       N  
ATOM   2995  CA  LEU A1272      -0.103 -30.198 -23.297  1.00 93.80           C  
ANISOU 2995  CA  LEU A1272     9367  17293   8979   -505  -1358   -408       C  
ATOM   2996  C   LEU A1272      -1.133 -30.218 -24.419  1.00 83.05           C  
ANISOU 2996  C   LEU A1272     8064  15767   7725   -506  -1095   -642       C  
ATOM   2997  O   LEU A1272      -0.826 -29.874 -25.562  1.00 75.19           O  
ANISOU 2997  O   LEU A1272     7118  14433   7019   -487  -1035   -845       O  
ATOM   2998  CB  LEU A1272       0.545 -31.576 -23.150  1.00 99.00           C  
ANISOU 2998  CB  LEU A1272     9863  17769   9984   -588  -1320     83       C  
ATOM   2999  CG  LEU A1272       1.391 -32.060 -24.330  1.00 95.81           C  
ANISOU 2999  CG  LEU A1272     9397  16819  10186   -620  -1214    133       C  
ATOM   3000  CD1 LEU A1272       2.604 -31.165 -24.533  1.00 92.91           C  
ANISOU 3000  CD1 LEU A1272     9051  16268   9984   -568  -1422    -14       C  
ATOM   3001  CD2 LEU A1272       1.821 -33.504 -24.136  1.00100.53           C  
ANISOU 3001  CD2 LEU A1272     9812  17239  11147   -702  -1128    619       C  
ATOM   3002  N   LYS A1273      -2.355 -30.624 -24.088  1.00 86.21           N  
ANISOU 3002  N   LYS A1273     8450  16417   7889   -528   -942   -599       N  
ATOM   3003  CA  LYS A1273      -3.449 -30.605 -25.053  1.00 90.49           C  
ANISOU 3003  CA  LYS A1273     9028  16856   8496   -533   -732   -828       C  
ATOM   3004  C   LYS A1273      -3.814 -29.170 -25.410  1.00 90.33           C  
ANISOU 3004  C   LYS A1273     9138  16911   8271   -432   -793  -1268       C  
ATOM   3005  O   LYS A1273      -4.125 -28.866 -26.562  1.00 86.51           O  
ANISOU 3005  O   LYS A1273     8707  16202   7963   -415   -700  -1493       O  
ATOM   3006  CB  LYS A1273      -4.676 -31.332 -24.498  1.00 93.79           C  
ANISOU 3006  CB  LYS A1273     9367  17536   8734   -580   -565   -662       C  
ATOM   3007  CG  LYS A1273      -5.840 -31.407 -25.476  1.00 96.61           C  
ANISOU 3007  CG  LYS A1273     9726  17785   9196   -601   -374   -878       C  
ATOM   3008  CD  LYS A1273      -7.065 -32.039 -24.839  1.00102.01           C  
ANISOU 3008  CD  LYS A1273    10303  18733   9722   -643   -212   -714       C  
ATOM   3009  CE  LYS A1273      -7.624 -31.163 -23.732  1.00104.03           C  
ANISOU 3009  CE  LYS A1273    10610  19449   9469   -553   -259   -815       C  
ATOM   3010  NZ  LYS A1273      -8.850 -31.758 -23.135  1.00107.73           N  
ANISOU 3010  NZ  LYS A1273    10964  20172   9799   -585    -61   -643       N  
ATOM   3011  N   THR A1274      -3.773 -28.292 -24.410  1.00 92.34           N  
ANISOU 3011  N   THR A1274     9441  17487   8156   -364   -949  -1389       N  
ATOM   3012  CA  THR A1274      -4.068 -26.878 -24.620  1.00 91.84           C  
ANISOU 3012  CA  THR A1274     9479  17484   7933   -261  -1011  -1806       C  
ATOM   3013  C   THR A1274      -3.097 -26.258 -25.619  1.00 93.54           C  
ANISOU 3013  C   THR A1274     9738  17315   8487   -227  -1093  -1961       C  
ATOM   3014  O   THR A1274      -3.515 -25.664 -26.613  1.00 86.22           O  
ANISOU 3014  O   THR A1274     8864  16224   7673   -177  -1008  -2197       O  
ATOM   3015  CB  THR A1274      -4.022 -26.079 -23.307  1.00 89.61           C  
ANISOU 3015  CB  THR A1274     9238  17589   7221   -202  -1177  -1931       C  
ATOM   3016  OG1 THR A1274      -4.945 -26.641 -22.367  1.00 89.89           O  
ANISOU 3016  OG1 THR A1274     9240  18006   6910   -224  -1064  -1769       O  
ATOM   3017  CG2 THR A1274      -4.384 -24.621 -23.556  1.00 71.28           C  
ANISOU 3017  CG2 THR A1274     7010  15194   4880    -90  -1180  -2343       C  
ATOM   3018  N   LEU A1275      -1.800 -26.401 -25.358  1.00104.71           N  
ANISOU 3018  N   LEU A1275    11118  18590  10077   -249  -1254  -1803       N  
ATOM   3019  CA  LEU A1275      -0.801 -25.864 -26.280  1.00109.65           C  
ANISOU 3019  CA  LEU A1275    11763  18831  11068   -216  -1306  -1909       C  
ATOM   3020  C   LEU A1275      -0.851 -26.586 -27.625  1.00103.88           C  
ANISOU 3020  C   LEU A1275    11035  17748  10687   -255  -1088  -1830       C  
ATOM   3021  O   LEU A1275      -0.512 -26.014 -28.664  1.00103.77           O  
ANISOU 3021  O   LEU A1275    11074  17457  10897   -206  -1039  -1990       O  
ATOM   3022  CB  LEU A1275       0.608 -25.912 -25.675  1.00114.55           C  
ANISOU 3022  CB  LEU A1275    12312  19368  11844   -237  -1532  -1735       C  
ATOM   3023  CG  LEU A1275       1.200 -27.251 -25.226  1.00122.10           C  
ANISOU 3023  CG  LEU A1275    13153  20290  12950   -329  -1545  -1299       C  
ATOM   3024  CD1 LEU A1275       1.890 -27.976 -26.377  1.00123.78           C  
ANISOU 3024  CD1 LEU A1275    13313  20031  13687   -367  -1387  -1141       C  
ATOM   3025  CD2 LEU A1275       2.166 -27.038 -24.071  1.00124.60           C  
ANISOU 3025  CD2 LEU A1275    13405  20776  13164   -335  -1852  -1173       C  
ATOM   3026  N   GLY A1276      -1.278 -27.845 -27.594  1.00 99.28           N  
ANISOU 3026  N   GLY A1276    10391  17180  10149   -343   -950  -1585       N  
ATOM   3027  CA  GLY A1276      -1.473 -28.614 -28.808  1.00 94.77           C  
ANISOU 3027  CA  GLY A1276     9826  16310   9872   -394   -737  -1555       C  
ATOM   3028  C   GLY A1276      -2.549 -27.996 -29.681  1.00 91.66           C  
ANISOU 3028  C   GLY A1276     9527  15948   9353   -348   -635  -1856       C  
ATOM   3029  O   GLY A1276      -2.450 -28.013 -30.906  1.00 92.39           O  
ANISOU 3029  O   GLY A1276     9680  15773   9651   -343   -524  -1957       O  
ATOM   3030  N   ILE A1277      -3.583 -27.451 -29.046  1.00 83.86           N  
ANISOU 3030  N   ILE A1277     8547  15296   8019   -309   -669  -1990       N  
ATOM   3031  CA  ILE A1277      -4.634 -26.747 -29.770  1.00 72.08           C  
ANISOU 3031  CA  ILE A1277     7115  13857   6414   -251   -602  -2261       C  
ATOM   3032  C   ILE A1277      -4.124 -25.394 -30.255  1.00 71.80           C  
ANISOU 3032  C   ILE A1277     7162  13701   6419   -137   -693  -2495       C  
ATOM   3033  O   ILE A1277      -4.334 -25.017 -31.411  1.00 69.79           O  
ANISOU 3033  O   ILE A1277     6969  13275   6273    -97   -622  -2630       O  
ATOM   3034  CB  ILE A1277      -5.879 -26.528 -28.887  1.00 74.71           C  
ANISOU 3034  CB  ILE A1277     7406  14571   6408   -233   -589  -2328       C  
ATOM   3035  CG1 ILE A1277      -6.499 -27.869 -28.489  1.00 77.48           C  
ANISOU 3035  CG1 ILE A1277     7655  15024   6759   -345   -466  -2076       C  
ATOM   3036  CG2 ILE A1277      -6.904 -25.666 -29.610  1.00 73.42           C  
ANISOU 3036  CG2 ILE A1277     7279  14446   6170   -157   -544  -2603       C  
ATOM   3037  CD1 ILE A1277      -7.724 -27.737 -27.605  1.00 78.36           C  
ANISOU 3037  CD1 ILE A1277     7707  15507   6558   -327   -411  -2102       C  
ATOM   3038  N   ILE A1278      -3.446 -24.678 -29.361  1.00 78.23           N  
ANISOU 3038  N   ILE A1278     7967  14606   7149    -87   -855  -2534       N  
ATOM   3039  CA  ILE A1278      -2.929 -23.341 -29.652  1.00 78.18           C  
ANISOU 3039  CA  ILE A1278     8006  14477   7223     19   -953  -2756       C  
ATOM   3040  C   ILE A1278      -2.019 -23.316 -30.874  1.00 79.60           C  
ANISOU 3040  C   ILE A1278     8221  14260   7761     32   -891  -2713       C  
ATOM   3041  O   ILE A1278      -2.185 -22.484 -31.767  1.00 84.79           O  
ANISOU 3041  O   ILE A1278     8932  14786   8496    115   -845  -2872       O  
ATOM   3042  CB  ILE A1278      -2.149 -22.767 -28.453  1.00 76.25           C  
ANISOU 3042  CB  ILE A1278     7729  14359   6884     41  -1164  -2793       C  
ATOM   3043  CG1 ILE A1278      -3.069 -22.613 -27.241  1.00 79.07           C  
ANISOU 3043  CG1 ILE A1278     8077  15132   6833     50  -1200  -2879       C  
ATOM   3044  CG2 ILE A1278      -1.517 -21.430 -28.814  1.00 74.87           C  
ANISOU 3044  CG2 ILE A1278     7571  13987   6890    139  -1260  -3019       C  
ATOM   3045  CD1 ILE A1278      -2.357 -22.154 -25.993  1.00 66.37           C  
ANISOU 3045  CD1 ILE A1278     6472  13624   5122     63  -1384  -2880       C  
ATOM   3046  N   MET A1279      -1.057 -24.233 -30.910  1.00 77.62           N  
ANISOU 3046  N   MET A1279     7934  13821   7738    -42   -876  -2479       N  
ATOM   3047  CA  MET A1279      -0.109 -24.291 -32.015  1.00 74.18           C  
ANISOU 3047  CA  MET A1279     7525  13002   7657    -29   -781  -2422       C  
ATOM   3048  C   MET A1279      -0.676 -25.095 -33.185  1.00 76.79           C  
ANISOU 3048  C   MET A1279     7923  13212   8043    -73   -564  -2401       C  
ATOM   3049  O   MET A1279      -0.400 -24.801 -34.353  1.00 78.34           O  
ANISOU 3049  O   MET A1279     8196  13178   8392    -27   -449  -2464       O  
ATOM   3050  CB  MET A1279       1.214 -24.897 -31.545  1.00 73.18           C  
ANISOU 3050  CB  MET A1279     7307  12697   7800    -84   -851  -2183       C  
ATOM   3051  CG  MET A1279       2.407 -24.487 -32.386  1.00 75.68           C  
ANISOU 3051  CG  MET A1279     7621  12631   8502    -35   -801  -2163       C  
ATOM   3052  SD  MET A1279       2.771 -22.729 -32.230  1.00 96.26           S  
ANISOU 3052  SD  MET A1279    10224  15216  11135     87   -969  -2398       S  
ATOM   3053  CE  MET A1279       3.730 -22.453 -33.717  1.00188.76           C  
ANISOU 3053  CE  MET A1279    21968  26469  23283    149   -766  -2347       C  
ATOM   3054  N   GLY A1280      -1.479 -26.104 -32.859  1.00 75.74           N  
ANISOU 3054  N   GLY A1280     7756  13241   7780   -164   -509  -2316       N  
ATOM   3055  CA  GLY A1280      -2.074 -26.972 -33.858  1.00 70.16           C  
ANISOU 3055  CA  GLY A1280     7093  12434   7131   -230   -330  -2324       C  
ATOM   3056  C   GLY A1280      -3.012 -26.254 -34.808  1.00 68.22           C  
ANISOU 3056  C   GLY A1280     6945  12252   6725   -166   -291  -2554       C  
ATOM   3057  O   GLY A1280      -2.938 -26.454 -36.019  1.00 75.01           O  
ANISOU 3057  O   GLY A1280     7892  12925   7683   -168   -169  -2609       O  
ATOM   3058  N   THR A1281      -3.894 -25.420 -34.264  1.00 64.60           N  
ANISOU 3058  N   THR A1281     6467  12064   6015   -105   -392  -2684       N  
ATOM   3059  CA  THR A1281      -4.843 -24.676 -35.086  1.00 67.50           C  
ANISOU 3059  CA  THR A1281     6892  12506   6248    -34   -379  -2872       C  
ATOM   3060  C   THR A1281      -4.124 -23.695 -36.008  1.00 73.38           C  
ANISOU 3060  C   THR A1281     7726  13036   7119     76   -367  -2939       C  
ATOM   3061  O   THR A1281      -4.396 -23.640 -37.211  1.00 79.57           O  
ANISOU 3061  O   THR A1281     8597  13734   7901     99   -287  -2994       O  
ATOM   3062  CB  THR A1281      -5.859 -23.908 -34.224  1.00 69.23           C  
ANISOU 3062  CB  THR A1281     7046  13032   6226     25   -472  -2992       C  
ATOM   3063  OG1 THR A1281      -6.577 -24.829 -33.394  1.00 74.15           O  
ANISOU 3063  OG1 THR A1281     7581  13864   6729    -72   -449  -2902       O  
ATOM   3064  CG2 THR A1281      -6.845 -23.154 -35.104  1.00 67.42           C  
ANISOU 3064  CG2 THR A1281     6846  12857   5914    103   -465  -3150       C  
ATOM   3065  N   PHE A1282      -3.202 -22.929 -35.432  1.00 71.36           N  
ANISOU 3065  N   PHE A1282     7441  12701   6972    143   -453  -2928       N  
ATOM   3066  CA  PHE A1282      -2.409 -21.959 -36.181  1.00 71.71           C  
ANISOU 3066  CA  PHE A1282     7535  12512   7200    249   -433  -2958       C  
ATOM   3067  C   PHE A1282      -1.643 -22.619 -37.324  1.00 73.03           C  
ANISOU 3067  C   PHE A1282     7785  12398   7563    220   -264  -2848       C  
ATOM   3068  O   PHE A1282      -1.675 -22.142 -38.461  1.00 77.14           O  
ANISOU 3068  O   PHE A1282     8398  12814   8099    293   -170  -2883       O  
ATOM   3069  CB  PHE A1282      -1.439 -21.237 -35.244  1.00 75.64           C  
ANISOU 3069  CB  PHE A1282     7953  12943   7843    292   -567  -2957       C  
ATOM   3070  CG  PHE A1282      -0.386 -20.440 -35.957  1.00 83.43           C  
ANISOU 3070  CG  PHE A1282     8955  13622   9124    380   -526  -2934       C  
ATOM   3071  CD1 PHE A1282      -0.707 -19.248 -36.583  1.00 86.76           C  
ANISOU 3071  CD1 PHE A1282     9398  14000   9565    503   -512  -3041       C  
ATOM   3072  CD2 PHE A1282       0.928 -20.879 -35.992  1.00 84.85           C  
ANISOU 3072  CD2 PHE A1282     9102  13541   9597    344   -490  -2778       C  
ATOM   3073  CE1 PHE A1282       0.260 -18.511 -37.238  1.00 83.74           C  
ANISOU 3073  CE1 PHE A1282     9012  13322   9482    588   -451  -2986       C  
ATOM   3074  CE2 PHE A1282       1.900 -20.145 -36.646  1.00 83.90           C  
ANISOU 3074  CE2 PHE A1282     8974  13123   9783    427   -428  -2737       C  
ATOM   3075  CZ  PHE A1282       1.565 -18.959 -37.269  1.00 81.69           C  
ANISOU 3075  CZ  PHE A1282     8722  12805   9512    548   -402  -2838       C  
ATOM   3076  N   THR A1283      -0.963 -23.718 -37.016  1.00 72.75           N  
ANISOU 3076  N   THR A1283     7715  12248   7677    119   -213  -2706       N  
ATOM   3077  CA  THR A1283      -0.201 -24.448 -38.022  1.00 77.96           C  
ANISOU 3077  CA  THR A1283     8444  12624   8552     86    -19  -2617       C  
ATOM   3078  C   THR A1283      -1.109 -24.999 -39.116  1.00 79.23           C  
ANISOU 3078  C   THR A1283     8722  12840   8542     48    106  -2716       C  
ATOM   3079  O   THR A1283      -0.879 -24.765 -40.301  1.00 84.58           O  
ANISOU 3079  O   THR A1283     9519  13381   9237    103    240  -2753       O  
ATOM   3080  CB  THR A1283       0.593 -25.611 -37.398  1.00 83.37           C  
ANISOU 3080  CB  THR A1283     9036  13174   9465    -20     12  -2436       C  
ATOM   3081  OG1 THR A1283       1.554 -25.093 -36.470  1.00 90.68           O  
ANISOU 3081  OG1 THR A1283     9853  14040  10562     13   -131  -2336       O  
ATOM   3082  CG2 THR A1283       1.315 -26.403 -38.478  1.00 76.98           C  
ANISOU 3082  CG2 THR A1283     8293  12053   8901    -51    252  -2376       C  
ATOM   3083  N   LEU A1284      -2.147 -25.721 -38.708  1.00 80.20           N  
ANISOU 3083  N   LEU A1284     8805  13173   8495    -46     60  -2757       N  
ATOM   3084  CA  LEU A1284      -3.074 -26.344 -39.646  1.00 83.61           C  
ANISOU 3084  CA  LEU A1284     9318  13667   8783   -107    138  -2871       C  
ATOM   3085  C   LEU A1284      -3.741 -25.322 -40.567  1.00 83.80           C  
ANISOU 3085  C   LEU A1284     9443  13803   8594     -2    102  -3003       C  
ATOM   3086  O   LEU A1284      -4.051 -25.625 -41.721  1.00 87.34           O  
ANISOU 3086  O   LEU A1284    10009  14227   8948    -19    187  -3089       O  
ATOM   3087  CB  LEU A1284      -4.137 -27.144 -38.888  1.00 88.31           C  
ANISOU 3087  CB  LEU A1284     9807  14475   9273   -220     71  -2878       C  
ATOM   3088  CG  LEU A1284      -5.129 -27.954 -39.724  1.00 99.66           C  
ANISOU 3088  CG  LEU A1284    11284  15964  10619   -316    124  -3005       C  
ATOM   3089  CD1 LEU A1284      -4.399 -29.004 -40.546  1.00106.50           C  
ANISOU 3089  CD1 LEU A1284    12226  16547  11692   -398    309  -3008       C  
ATOM   3090  CD2 LEU A1284      -6.181 -28.599 -38.835  1.00101.98           C  
ANISOU 3090  CD2 LEU A1284    11430  16462  10856   -415     57  -2981       C  
ATOM   3091  N   CYS A1285      -3.948 -24.110 -40.061  1.00 75.05           N  
ANISOU 3091  N   CYS A1285     8284  12817   7415    109    -25  -3020       N  
ATOM   3092  CA  CYS A1285      -4.633 -23.076 -40.834  1.00 68.73           C  
ANISOU 3092  CA  CYS A1285     7541  12123   6451    221    -72  -3106       C  
ATOM   3093  C   CYS A1285      -3.715 -22.252 -41.739  1.00 68.41           C  
ANISOU 3093  C   CYS A1285     7599  11874   6521    342     23  -3047       C  
ATOM   3094  O   CYS A1285      -4.080 -21.943 -42.873  1.00 70.34           O  
ANISOU 3094  O   CYS A1285     7951  12148   6628    399     66  -3070       O  
ATOM   3095  CB  CYS A1285      -5.430 -22.147 -39.913  1.00 65.11           C  
ANISOU 3095  CB  CYS A1285     6963  11882   5895    289   -229  -3167       C  
ATOM   3096  SG  CYS A1285      -6.917 -22.895 -39.209  1.00 88.50           S  
ANISOU 3096  SG  CYS A1285     9815  15141   8669    180   -309  -3238       S  
ATOM   3097  N   TRP A1286      -2.532 -21.893 -41.247  1.00 68.40           N  
ANISOU 3097  N   TRP A1286     7551  11669   6770    383     52  -2954       N  
ATOM   3098  CA  TRP A1286      -1.669 -20.977 -41.995  1.00 67.67           C  
ANISOU 3098  CA  TRP A1286     7510  11363   6836    510    148  -2876       C  
ATOM   3099  C   TRP A1286      -0.452 -21.601 -42.683  1.00 70.00           C  
ANISOU 3099  C   TRP A1286     7887  11372   7340    488    365  -2768       C  
ATOM   3100  O   TRP A1286       0.070 -21.036 -43.644  1.00 71.51           O  
ANISOU 3100  O   TRP A1286     8160  11414   7595    588    505  -2696       O  
ATOM   3101  CB  TRP A1286      -1.231 -19.800 -41.120  1.00 64.05           C  
ANISOU 3101  CB  TRP A1286     6922  10847   6566    602     27  -2868       C  
ATOM   3102  CG  TRP A1286      -2.219 -18.673 -41.081  1.00 64.05           C  
ANISOU 3102  CG  TRP A1286     6879  11022   6435    705    -92  -2958       C  
ATOM   3103  CD1 TRP A1286      -2.848 -18.174 -39.979  1.00 68.25           C  
ANISOU 3103  CD1 TRP A1286     7291  11728   6912    715   -255  -3076       C  
ATOM   3104  CD2 TRP A1286      -2.692 -17.905 -42.196  1.00 65.01           C  
ANISOU 3104  CD2 TRP A1286     7067  11160   6474    820    -43  -2925       C  
ATOM   3105  NE1 TRP A1286      -3.681 -17.140 -40.336  1.00 69.93           N  
ANISOU 3105  NE1 TRP A1286     7478  12033   7061    829   -301  -3130       N  
ATOM   3106  CE2 TRP A1286      -3.604 -16.955 -41.692  1.00 69.46           C  
ANISOU 3106  CE2 TRP A1286     7523  11881   6986    896   -187  -3019       C  
ATOM   3107  CE3 TRP A1286      -2.434 -17.926 -43.571  1.00 61.68           C  
ANISOU 3107  CE3 TRP A1286     6786  10646   6006    872    115  -2815       C  
ATOM   3108  CZ2 TRP A1286      -4.256 -16.035 -42.513  1.00 56.51           C  
ANISOU 3108  CZ2 TRP A1286     5889  10289   5293   1022   -192  -2978       C  
ATOM   3109  CZ3 TRP A1286      -3.083 -17.013 -44.384  1.00 61.10           C  
ANISOU 3109  CZ3 TRP A1286     6738  10655   5823    995     99  -2768       C  
ATOM   3110  CH2 TRP A1286      -3.984 -16.081 -43.852  1.00 61.34           C  
ANISOU 3110  CH2 TRP A1286     6637  10824   5846   1069    -61  -2836       C  
ATOM   3111  N   LEU A1287       0.010 -22.749 -42.198  1.00 67.76           N  
ANISOU 3111  N   LEU A1287     7565  10999   7180    367    411  -2736       N  
ATOM   3112  CA  LEU A1287       1.166 -23.404 -42.816  1.00 65.04           C  
ANISOU 3112  CA  LEU A1287     7275  10358   7081    347    641  -2638       C  
ATOM   3113  C   LEU A1287       0.958 -23.851 -44.273  1.00 66.53           C  
ANISOU 3113  C   LEU A1287     7659  10523   7098    349    853  -2701       C  
ATOM   3114  O   LEU A1287       1.813 -23.578 -45.115  1.00 66.95           O  
ANISOU 3114  O   LEU A1287     7793  10368   7278    428   1060  -2622       O  
ATOM   3115  CB  LEU A1287       1.694 -24.566 -41.962  1.00 64.28           C  
ANISOU 3115  CB  LEU A1287     7069  10153   7200    220    645  -2567       C  
ATOM   3116  CG  LEU A1287       2.924 -25.300 -42.507  1.00 63.09           C  
ANISOU 3116  CG  LEU A1287     6935   9660   7376    198    897  -2458       C  
ATOM   3117  CD1 LEU A1287       4.141 -24.386 -42.524  1.00 57.02           C  
ANISOU 3117  CD1 LEU A1287     6099   8644   6922    309    947  -2320       C  
ATOM   3118  CD2 LEU A1287       3.209 -26.564 -41.710  1.00 57.07           C  
ANISOU 3118  CD2 LEU A1287     6053   8816   6816     65    893  -2377       C  
ATOM   3119  N   PRO A1288      -0.164 -24.538 -44.579  1.00 65.16           N  
ANISOU 3119  N   PRO A1288     7557  10564   6636    261    806  -2848       N  
ATOM   3120  CA  PRO A1288      -0.310 -25.009 -45.963  1.00 70.26           C  
ANISOU 3120  CA  PRO A1288     8400  11199   7095    252    990  -2943       C  
ATOM   3121  C   PRO A1288      -0.312 -23.889 -47.004  1.00 78.50           C  
ANISOU 3121  C   PRO A1288     9574  12293   7958    405   1046  -2899       C  
ATOM   3122  O   PRO A1288       0.058 -24.131 -48.151  1.00 85.12           O  
ANISOU 3122  O   PRO A1288    10586  13054   8700    432   1263  -2916       O  
ATOM   3123  CB  PRO A1288      -1.668 -25.716 -45.952  1.00 58.92           C  
ANISOU 3123  CB  PRO A1288     6975  10022   5389    133    846  -3119       C  
ATOM   3124  CG  PRO A1288      -1.863 -26.129 -44.543  1.00 62.78           C  
ANISOU 3124  CG  PRO A1288     7270  10545   6037     46    702  -3077       C  
ATOM   3125  CD  PRO A1288      -1.268 -25.022 -43.728  1.00 62.28           C  
ANISOU 3125  CD  PRO A1288     7097  10439   6126    158    610  -2936       C  
ATOM   3126  N   PHE A1289      -0.715 -22.686 -46.611  1.00 82.26           N  
ANISOU 3126  N   PHE A1289     9967  12894   8395    509    869  -2836       N  
ATOM   3127  CA  PHE A1289      -0.752 -21.569 -47.548  1.00 82.71           C  
ANISOU 3127  CA  PHE A1289    10116  12990   8321    665    915  -2746       C  
ATOM   3128  C   PHE A1289       0.632 -20.991 -47.822  1.00 81.28           C  
ANISOU 3128  C   PHE A1289     9930  12501   8452    774   1131  -2561       C  
ATOM   3129  O   PHE A1289       1.038 -20.860 -48.976  1.00 85.63           O  
ANISOU 3129  O   PHE A1289    10635  12986   8912    851   1350  -2485       O  
ATOM   3130  CB  PHE A1289      -1.686 -20.464 -47.055  1.00 80.95           C  
ANISOU 3130  CB  PHE A1289     9778  12970   8010    745    668  -2740       C  
ATOM   3131  CG  PHE A1289      -1.585 -19.194 -47.850  1.00 75.27           C  
ANISOU 3131  CG  PHE A1289     9098  12233   7268    920    715  -2588       C  
ATOM   3132  CD1 PHE A1289      -2.110 -19.119 -49.129  1.00 76.20           C  
ANISOU 3132  CD1 PHE A1289     9387  12515   7051    972    766  -2562       C  
ATOM   3133  CD2 PHE A1289      -0.958 -18.078 -47.321  1.00 69.29           C  
ANISOU 3133  CD2 PHE A1289     8198  11295   6833   1033    703  -2463       C  
ATOM   3134  CE1 PHE A1289      -2.014 -17.955 -49.865  1.00 76.26           C  
ANISOU 3134  CE1 PHE A1289     9421  12513   7042   1142    818  -2369       C  
ATOM   3135  CE2 PHE A1289      -0.860 -16.909 -48.052  1.00 69.20           C  
ANISOU 3135  CE2 PHE A1289     8198  11238   6857   1198    764  -2293       C  
ATOM   3136  CZ  PHE A1289      -1.389 -16.847 -49.325  1.00 73.24           C  
ANISOU 3136  CZ  PHE A1289     8879  11920   7030   1258    829  -2222       C  
ATOM   3137  N   PHE A1290       1.353 -20.643 -46.761  1.00 79.30           N  
ANISOU 3137  N   PHE A1290     9496  12067   8565    781   1069  -2487       N  
ATOM   3138  CA  PHE A1290       2.664 -20.016 -46.907  1.00 76.25           C  
ANISOU 3138  CA  PHE A1290     9053  11366   8551    880   1242  -2307       C  
ATOM   3139  C   PHE A1290       3.706 -20.953 -47.509  1.00 81.27           C  
ANISOU 3139  C   PHE A1290     9773  11753   9351    840   1546  -2252       C  
ATOM   3140  O   PHE A1290       4.714 -20.501 -48.049  1.00 90.44           O  
ANISOU 3140  O   PHE A1290    10937  12666  10762    937   1772  -2090       O  
ATOM   3141  CB  PHE A1290       3.146 -19.439 -45.576  1.00 65.03           C  
ANISOU 3141  CB  PHE A1290     7403   9825   7479    881   1054  -2276       C  
ATOM   3142  CG  PHE A1290       2.507 -18.129 -45.225  1.00 61.91           C  
ANISOU 3142  CG  PHE A1290     6918   9553   7052    981    857  -2294       C  
ATOM   3143  CD1 PHE A1290       3.063 -16.937 -45.658  1.00 59.14           C  
ANISOU 3143  CD1 PHE A1290     6516   9015   6941   1126    941  -2148       C  
ATOM   3144  CD2 PHE A1290       1.344 -18.088 -44.477  1.00 63.31           C  
ANISOU 3144  CD2 PHE A1290     7047  10014   6994    934    611  -2450       C  
ATOM   3145  CE1 PHE A1290       2.475 -15.728 -45.343  1.00 69.88           C  
ANISOU 3145  CE1 PHE A1290     7773  10451   8327   1221    774  -2171       C  
ATOM   3146  CE2 PHE A1290       0.751 -16.881 -44.158  1.00 57.27           C  
ANISOU 3146  CE2 PHE A1290     6188   9338   6235   1032    455  -2483       C  
ATOM   3147  CZ  PHE A1290       1.316 -15.700 -44.591  1.00 65.48           C  
ANISOU 3147  CZ  PHE A1290     7173  10173   7535   1175    532  -2350       C  
ATOM   3148  N   ILE A1291       3.462 -22.255 -47.414  1.00 78.10           N  
ANISOU 3148  N   ILE A1291     9425  11399   8850    700   1571  -2384       N  
ATOM   3149  CA  ILE A1291       4.285 -23.220 -48.127  1.00 76.47           C  
ANISOU 3149  CA  ILE A1291     9318  10970   8765    662   1889  -2378       C  
ATOM   3150  C   ILE A1291       3.987 -23.099 -49.614  1.00 80.15           C  
ANISOU 3150  C   ILE A1291    10035  11547   8871    735   2096  -2419       C  
ATOM   3151  O   ILE A1291       4.894 -22.960 -50.430  1.00 81.43           O  
ANISOU 3151  O   ILE A1291    10281  11507   9153    821   2405  -2305       O  
ATOM   3152  CB  ILE A1291       4.016 -24.661 -47.665  1.00 71.96           C  
ANISOU 3152  CB  ILE A1291     8727  10408   8205    489   1865  -2521       C  
ATOM   3153  CG1 ILE A1291       4.577 -24.884 -46.260  1.00 73.28           C  
ANISOU 3153  CG1 ILE A1291     8652  10434   8758    426   1713  -2418       C  
ATOM   3154  CG2 ILE A1291       4.636 -25.655 -48.633  1.00 69.23           C  
ANISOU 3154  CG2 ILE A1291     8524   9862   7920    455   2218  -2579       C  
ATOM   3155  CD1 ILE A1291       4.411 -26.302 -45.760  1.00 74.75           C  
ANISOU 3155  CD1 ILE A1291     8785  10592   9023    266   1710  -2491       C  
ATOM   3156  N   VAL A1292       2.703 -23.143 -49.953  1.00 85.01           N  
ANISOU 3156  N   VAL A1292    10764  12496   9039    702   1922  -2571       N  
ATOM   3157  CA  VAL A1292       2.254 -22.989 -51.332  1.00 82.60           C  
ANISOU 3157  CA  VAL A1292    10702  12375   8309    767   2045  -2616       C  
ATOM   3158  C   VAL A1292       2.637 -21.621 -51.888  1.00 78.30           C  
ANISOU 3158  C   VAL A1292    10175  11801   7776    958   2131  -2373       C  
ATOM   3159  O   VAL A1292       3.064 -21.505 -53.038  1.00 82.39           O  
ANISOU 3159  O   VAL A1292    10873  12293   8137   1046   2403  -2295       O  
ATOM   3160  CB  VAL A1292       0.729 -23.203 -51.446  1.00 66.19           C  
ANISOU 3160  CB  VAL A1292     8686  10672   5791    690   1765  -2809       C  
ATOM   3161  CG1 VAL A1292       0.166 -22.510 -52.676  1.00 75.35           C  
ANISOU 3161  CG1 VAL A1292    10037  12080   6514    803   1772  -2767       C  
ATOM   3162  CG2 VAL A1292       0.409 -24.690 -51.462  1.00 69.45           C  
ANISOU 3162  CG2 VAL A1292     9158  11097   6132    509   1793  -3064       C  
ATOM   3163  N   ASN A1293       2.506 -20.592 -51.059  1.00 65.45           N  
ANISOU 3163  N   ASN A1293     8352  10165   6350   1024   1916  -2253       N  
ATOM   3164  CA  ASN A1293       2.845 -19.234 -51.467  1.00 87.84           C  
ANISOU 3164  CA  ASN A1293    11155  12932   9287   1204   1980  -2010       C  
ATOM   3165  C   ASN A1293       4.326 -19.085 -51.800  1.00 96.04           C  
ANISOU 3165  C   ASN A1293    12172  13605  10714   1282   2323  -1815       C  
ATOM   3166  O   ASN A1293       4.718 -18.181 -52.539  1.00104.71           O  
ANISOU 3166  O   ASN A1293    13303  14631  11850   1435   2497  -1591       O  
ATOM   3167  CB  ASN A1293       2.451 -18.234 -50.378  1.00 84.48           C  
ANISOU 3167  CB  ASN A1293    10497  12525   9076   1242   1683  -1975       C  
ATOM   3168  CG  ASN A1293       2.529 -16.796 -50.852  1.00 89.49           C  
ANISOU 3168  CG  ASN A1293    11085  13116   9801   1426   1716  -1741       C  
ATOM   3169  OD1 ASN A1293       2.421 -16.519 -52.047  1.00 95.24           O  
ANISOU 3169  OD1 ASN A1293    11979  13939  10267   1525   1879  -1606       O  
ATOM   3170  ND2 ASN A1293       2.718 -15.872 -49.917  1.00 88.61           N  
ANISOU 3170  ND2 ASN A1293    10744  12860  10061   1473   1563  -1693       N  
ATOM   3171  N   ILE A1294       5.145 -19.981 -51.257  1.00 95.24           N  
ANISOU 3171  N   ILE A1294    11996  13264  10927   1181   2429  -1875       N  
ATOM   3172  CA  ILE A1294       6.585 -19.923 -51.475  1.00 96.54           C  
ANISOU 3172  CA  ILE A1294    12098  13050  11535   1244   2752  -1690       C  
ATOM   3173  C   ILE A1294       7.027 -20.848 -52.611  1.00 96.57           C  
ANISOU 3173  C   ILE A1294    12329  12997  11368   1235   3140  -1735       C  
ATOM   3174  O   ILE A1294       8.110 -20.686 -53.168  1.00100.29           O  
ANISOU 3174  O   ILE A1294    12803  13199  12105   1325   3489  -1557       O  
ATOM   3175  CB  ILE A1294       7.372 -20.240 -50.176  1.00 85.64           C  
ANISOU 3175  CB  ILE A1294    10457  11400  10683   1155   2638  -1684       C  
ATOM   3176  CG1 ILE A1294       8.586 -19.319 -50.049  1.00 90.94           C  
ANISOU 3176  CG1 ILE A1294    10939  11719  11895   1268   2771  -1433       C  
ATOM   3177  CG2 ILE A1294       7.777 -21.709 -50.115  1.00 82.02           C  
ANISOU 3177  CG2 ILE A1294    10036  10821  10308   1024   2794  -1802       C  
ATOM   3178  CD1 ILE A1294       8.223 -17.859 -49.951  1.00 66.85           C  
ANISOU 3178  CD1 ILE A1294     7799   8731   8871   1388   2601  -1323       C  
ATOM   3179  N   VAL A1295       6.175 -21.809 -52.957  1.00 92.51           N  
ANISOU 3179  N   VAL A1295    11996  12730  10422   1126   3090  -1985       N  
ATOM   3180  CA  VAL A1295       6.480 -22.763 -54.019  1.00 87.39           C  
ANISOU 3180  CA  VAL A1295    11581  12053   9572   1101   3441  -2107       C  
ATOM   3181  C   VAL A1295       5.950 -22.281 -55.367  1.00 87.19           C  
ANISOU 3181  C   VAL A1295    11829  12311   8988   1210   3558  -2084       C  
ATOM   3182  O   VAL A1295       6.610 -22.437 -56.396  1.00 94.72           O  
ANISOU 3182  O   VAL A1295    12961  13182   9848   1286   3950  -2032       O  
ATOM   3183  CB  VAL A1295       5.913 -24.164 -53.699  1.00 72.61           C  
ANISOU 3183  CB  VAL A1295     9750  10257   7581    909   3341  -2419       C  
ATOM   3184  CG1 VAL A1295       6.065 -25.095 -54.891  1.00 75.75           C  
ANISOU 3184  CG1 VAL A1295    10415  10660   7707    881   3687  -2612       C  
ATOM   3185  CG2 VAL A1295       6.603 -24.747 -52.478  1.00 70.70           C  
ANISOU 3185  CG2 VAL A1295     9248   9714   7901    813   3290  -2387       C  
ATOM   3186  N   HIS A1296       4.767 -21.674 -55.354  1.00 85.44           N  
ANISOU 3186  N   HIS A1296    11633  12432   8397   1225   3223  -2105       N  
ATOM   3187  CA  HIS A1296       4.133 -21.198 -56.581  1.00 94.47           C  
ANISOU 3187  CA  HIS A1296    13020  13897   8977   1325   3259  -2060       C  
ATOM   3188  C   HIS A1296       4.894 -20.024 -57.193  1.00 99.22           C  
ANISOU 3188  C   HIS A1296    13622  14376   9702   1532   3512  -1689       C  
ATOM   3189  O   HIS A1296       4.597 -19.590 -58.307  1.00104.65           O  
ANISOU 3189  O   HIS A1296    14517  15300   9946   1642   3619  -1574       O  
ATOM   3190  CB  HIS A1296       2.677 -20.804 -56.319  1.00101.72           C  
ANISOU 3190  CB  HIS A1296    13910  15184   9556   1293   2813  -2140       C  
ATOM   3191  CG  HIS A1296       2.470 -19.331 -56.142  1.00116.61           C  
ANISOU 3191  CG  HIS A1296    15652  17108  11546   1449   2661  -1844       C  
ATOM   3192  ND1 HIS A1296       2.066 -18.508 -57.172  1.00124.17           N  
ANISOU 3192  ND1 HIS A1296    16749  18300  12132   1595   2685  -1644       N  
ATOM   3193  CD2 HIS A1296       2.611 -18.533 -55.057  1.00121.57           C  
ANISOU 3193  CD2 HIS A1296    16005  17565  12623   1484   2486  -1719       C  
ATOM   3194  CE1 HIS A1296       1.966 -17.267 -56.728  1.00125.87           C  
ANISOU 3194  CE1 HIS A1296    16762  18455  12609   1715   2543  -1396       C  
ATOM   3195  NE2 HIS A1296       2.292 -17.255 -55.449  1.00124.31           N  
ANISOU 3195  NE2 HIS A1296    16316  18009  12907   1647   2423  -1462       N  
ATOM   3196  N   VAL A1297       5.877 -19.514 -56.458  1.00 98.23           N  
ANISOU 3196  N   VAL A1297    13252  13882  10190   1582   3600  -1490       N  
ATOM   3197  CA  VAL A1297       6.693 -18.406 -56.931  1.00100.41           C  
ANISOU 3197  CA  VAL A1297    13471  13969  10712   1770   3855  -1122       C  
ATOM   3198  C   VAL A1297       8.048 -18.909 -57.437  1.00102.67           C  
ANISOU 3198  C   VAL A1297    13806  13926  11279   1805   4353  -1038       C  
ATOM   3199  O   VAL A1297       8.774 -18.187 -58.121  1.00108.07           O  
ANISOU 3199  O   VAL A1297    14503  14468  12092   1964   4674   -734       O  
ATOM   3200  CB  VAL A1297       6.888 -17.343 -55.827  1.00 96.47           C  
ANISOU 3200  CB  VAL A1297    12640  13259  10755   1815   3616   -951       C  
ATOM   3201  CG1 VAL A1297       7.999 -17.759 -54.872  1.00 94.66           C  
ANISOU 3201  CG1 VAL A1297    12183  12623  11161   1738   3690   -973       C  
ATOM   3202  CG2 VAL A1297       7.179 -15.982 -56.439  1.00 97.69           C  
ANISOU 3202  CG2 VAL A1297    12749  13346  11023   2018   3763   -575       C  
ATOM   3203  N   ILE A1298       8.377 -20.154 -57.104  1.00 96.51           N  
ANISOU 3203  N   ILE A1298    13037  13011  10622   1660   4434  -1292       N  
ATOM   3204  CA  ILE A1298       9.613 -20.773 -57.573  1.00 95.13           C  
ANISOU 3204  CA  ILE A1298    12901  12513  10733   1682   4921  -1250       C  
ATOM   3205  C   ILE A1298       9.386 -21.483 -58.904  1.00104.98           C  
ANISOU 3205  C   ILE A1298    14517  13989  11383   1692   5232  -1421       C  
ATOM   3206  O   ILE A1298       9.801 -20.996 -59.956  1.00109.47           O  
ANISOU 3206  O   ILE A1298    15248  14588  11759   1844   5586  -1217       O  
ATOM   3207  CB  ILE A1298      10.180 -21.776 -56.546  1.00 88.18           C  
ANISOU 3207  CB  ILE A1298    11819  11327  10359   1530   4882  -1411       C  
ATOM   3208  CG1 ILE A1298      10.475 -21.075 -55.219  1.00 85.01           C  
ANISOU 3208  CG1 ILE A1298    11062  10719  10517   1518   4568  -1254       C  
ATOM   3209  CG2 ILE A1298      11.443 -22.437 -57.080  1.00 83.90           C  
ANISOU 3209  CG2 ILE A1298    11300  10432  10147   1560   5410  -1365       C  
ATOM   3210  CD1 ILE A1298      11.495 -19.961 -55.325  1.00 87.28           C  
ANISOU 3210  CD1 ILE A1298    11174  10708  11281   1675   4772   -896       C  
ATOM   3211  N   GLN A1299       8.723 -22.635 -58.851  1.00132.00           N  
ANISOU 3211  N   GLN A1299    13057  21595  15503   -476  -2181   -534       N  
ATOM   3212  CA  GLN A1299       8.393 -23.384 -60.057  1.00134.24           C  
ANISOU 3212  CA  GLN A1299    13785  21996  15224   -560  -1855   -206       C  
ATOM   3213  C   GLN A1299       7.015 -22.973 -60.559  1.00132.68           C  
ANISOU 3213  C   GLN A1299    13818  21667  14927   -767  -2032    -61       C  
ATOM   3214  O   GLN A1299       6.014 -23.140 -59.862  1.00123.46           O  
ANISOU 3214  O   GLN A1299    12816  20413  13680   -708  -2258   -310       O  
ATOM   3215  CB  GLN A1299       8.435 -24.889 -59.790  1.00130.39           C  
ANISOU 3215  CB  GLN A1299    13679  21737  14125   -296  -1582   -409       C  
ATOM   3216  CG  GLN A1299       8.187 -25.744 -61.022  1.00126.97           C  
ANISOU 3216  CG  GLN A1299    13704  21426  13112   -395  -1222   -183       C  
ATOM   3217  N   ASP A1300       6.973 -22.434 -61.773  1.00141.87           N  
ANISOU 3217  N   ASP A1300    14975  22835  16095   -960  -1904    385       N  
ATOM   3218  CA  ASP A1300       5.737 -21.904 -62.335  1.00147.82           C  
ANISOU 3218  CA  ASP A1300    15858  23537  16768  -1132  -2070    606       C  
ATOM   3219  C   ASP A1300       4.715 -22.999 -62.626  1.00147.88           C  
ANISOU 3219  C   ASP A1300    16365  23736  16087  -1125  -2085    443       C  
ATOM   3220  O   ASP A1300       5.060 -24.066 -63.137  1.00151.33           O  
ANISOU 3220  O   ASP A1300    17098  24391  16010  -1057  -1812    373       O  
ATOM   3221  CB  ASP A1300       6.030 -21.105 -63.607  1.00152.56           C  
ANISOU 3221  CB  ASP A1300    16305  24180  17481  -1232  -1857   1181       C  
ATOM   3222  CG  ASP A1300       4.817 -20.353 -64.116  1.00152.43           C  
ANISOU 3222  CG  ASP A1300    16307  24151  17459  -1360  -2020   1483       C  
ATOM   3223  OD1 ASP A1300       3.974 -19.955 -63.285  1.00151.46           O  
ANISOU 3223  OD1 ASP A1300    16126  23820  17604  -1427  -2320   1293       O  
ATOM   3224  OD2 ASP A1300       4.708 -20.160 -65.345  1.00153.42           O  
ANISOU 3224  OD2 ASP A1300    16506  24500  17287  -1349  -1830   1942       O  
ATOM   3225  N   ASN A1301       3.459 -22.719 -62.289  1.00142.46           N  
ANISOU 3225  N   ASN A1301    15746  22929  15454  -1205  -2379    373       N  
ATOM   3226  CA  ASN A1301       2.343 -23.628 -62.544  1.00138.13           C  
ANISOU 3226  CA  ASN A1301    15580  22500  14401  -1241  -2438    198       C  
ATOM   3227  C   ASN A1301       2.522 -25.020 -61.938  1.00128.50           C  
ANISOU 3227  C   ASN A1301    14627  21295  12901  -1052  -2236   -244       C  
ATOM   3228  O   ASN A1301       2.513 -26.025 -62.648  1.00125.07           O  
ANISOU 3228  O   ASN A1301    14490  21058  11972  -1077  -1995   -349       O  
ATOM   3229  CB  ASN A1301       2.052 -23.726 -64.045  1.00147.63           C  
ANISOU 3229  CB  ASN A1301    16956  24038  15097  -1380  -2351    491       C  
ATOM   3230  CG  ASN A1301       0.682 -24.309 -64.336  1.00152.40           C  
ANISOU 3230  CG  ASN A1301    17822  24760  15324  -1491  -2545    308       C  
ATOM   3231  OD1 ASN A1301      -0.189 -24.343 -63.467  1.00150.52           O  
ANISOU 3231  OD1 ASN A1301    17581  24276  15334  -1490  -2758    107       O  
ATOM   3232  ND2 ASN A1301       0.485 -24.771 -65.566  1.00156.64           N  
ANISOU 3232  ND2 ASN A1301    18572  25677  15268  -1569  -2472    364       N  
ATOM   3233  N   LEU A1302       2.691 -25.066 -60.622  1.00126.18           N  
ANISOU 3233  N   LEU A1302    14217  20800  12926   -829  -2296   -501       N  
ATOM   3234  CA  LEU A1302       2.736 -26.329 -59.896  1.00118.99           C  
ANISOU 3234  CA  LEU A1302    13520  19880  11811   -550  -2049   -858       C  
ATOM   3235  C   LEU A1302       1.529 -26.405 -58.968  1.00110.66           C  
ANISOU 3235  C   LEU A1302    12541  18560  10945   -419  -2246  -1049       C  
ATOM   3236  O   LEU A1302       1.065 -27.489 -58.614  1.00108.03           O  
ANISOU 3236  O   LEU A1302    12436  18152  10460   -233  -2013  -1287       O  
ATOM   3237  CB  LEU A1302       4.036 -26.452 -59.097  1.00114.73           C  
ANISOU 3237  CB  LEU A1302    12771  19415  11405   -256  -1884   -963       C  
ATOM   3238  CG  LEU A1302       4.262 -27.770 -58.353  1.00110.65           C  
ANISOU 3238  CG  LEU A1302    12433  18953  10656    133  -1509  -1236       C  
ATOM   3239  CD1 LEU A1302       4.216 -28.947 -59.315  1.00110.60           C  
ANISOU 3239  CD1 LEU A1302    12779  19047  10197     32  -1066  -1252       C  
ATOM   3240  CD2 LEU A1302       5.581 -27.743 -57.596  1.00112.10           C  
ANISOU 3240  CD2 LEU A1302    12330  19315  10947    446  -1406  -1286       C  
ATOM   3241  N   ILE A1303       1.023 -25.237 -58.587  1.00103.84           N  
ANISOU 3241  N   ILE A1303    11477  17509  10467   -503  -2617   -914       N  
ATOM   3242  CA  ILE A1303      -0.160 -25.147 -57.744  1.00 96.86           C  
ANISOU 3242  CA  ILE A1303    10666  16333   9805   -375  -2810  -1007       C  
ATOM   3243  C   ILE A1303      -1.290 -24.441 -58.482  1.00 95.11           C  
ANISOU 3243  C   ILE A1303    10447  16033   9658   -717  -3074   -720       C  
ATOM   3244  O   ILE A1303      -1.162 -23.275 -58.859  1.00 96.22           O  
ANISOU 3244  O   ILE A1303    10363  16176  10020   -919  -3252   -425       O  
ATOM   3245  CB  ILE A1303       0.122 -24.384 -56.434  1.00 95.22           C  
ANISOU 3245  CB  ILE A1303    10239  15943   9996    -99  -3008  -1122       C  
ATOM   3246  CG1 ILE A1303       1.176 -25.111 -55.596  1.00 95.22           C  
ANISOU 3246  CG1 ILE A1303    10197  16112   9868    329  -2780  -1409       C  
ATOM   3247  CG2 ILE A1303      -1.159 -24.211 -55.634  1.00 97.04           C  
ANISOU 3247  CG2 ILE A1303    10583  15835  10454     54  -3182  -1139       C  
ATOM   3248  CD1 ILE A1303       2.593 -24.656 -55.861  1.00102.17           C  
ANISOU 3248  CD1 ILE A1303    10779  17232  10810    242  -2769  -1388       C  
ATOM   3249  N   ARG A1304      -2.393 -25.154 -58.691  1.00 94.36           N  
ANISOU 3249  N   ARG A1304    10566  15869   9419   -763  -3062   -797       N  
ATOM   3250  CA  ARG A1304      -3.572 -24.578 -59.325  1.00 98.30           C  
ANISOU 3250  CA  ARG A1304    11041  16345   9965  -1046  -3334   -529       C  
ATOM   3251  C   ARG A1304      -4.145 -23.452 -58.467  1.00102.01           C  
ANISOU 3251  C   ARG A1304    11355  16477  10929   -977  -3583   -319       C  
ATOM   3252  O   ARG A1304      -4.039 -23.485 -57.240  1.00102.64           O  
ANISOU 3252  O   ARG A1304    11447  16283  11268   -655  -3558   -505       O  
ATOM   3253  CB  ARG A1304      -4.624 -25.661 -59.582  1.00 99.99           C  
ANISOU 3253  CB  ARG A1304    11460  16519  10012  -1096  -3277   -748       C  
ATOM   3254  CG  ARG A1304      -4.533 -26.845 -58.630  1.00104.37           C  
ANISOU 3254  CG  ARG A1304    12178  16828  10650   -742  -2940  -1130       C  
ATOM   3255  CD  ARG A1304      -5.500 -27.959 -59.009  1.00111.49           C  
ANISOU 3255  CD  ARG A1304    13229  17641  11491   -840  -2802  -1392       C  
ATOM   3256  NE  ARG A1304      -6.896 -27.570 -58.827  1.00120.48           N  
ANISOU 3256  NE  ARG A1304    14299  18519  12959   -929  -3087  -1242       N  
ATOM   3257  CZ  ARG A1304      -7.930 -28.386 -59.009  1.00125.42           C  
ANISOU 3257  CZ  ARG A1304    14968  18977  13710  -1020  -3031  -1459       C  
ATOM   3258  NH1 ARG A1304      -7.729 -29.643 -59.380  1.00129.92           N  
ANISOU 3258  NH1 ARG A1304    15661  19588  14115  -1047  -2672  -1882       N  
ATOM   3259  NH2 ARG A1304      -9.166 -27.945 -58.820  1.00122.71           N  
ANISOU 3259  NH2 ARG A1304    14522  18392  13709  -1091  -3302  -1258       N  
ATOM   3260  N   LYS A1305      -4.739 -22.457 -59.118  1.00 73.24           N  
ANISOU 3260  N   LYS A1305    10994  10938   5896   -702    454  -1205       N  
ATOM   3261  CA  LYS A1305      -5.243 -21.269 -58.431  1.00 77.27           C  
ANISOU 3261  CA  LYS A1305    11123  11750   6484   -393    187  -1029       C  
ATOM   3262  C   LYS A1305      -6.306 -21.599 -57.381  1.00 78.01           C  
ANISOU 3262  C   LYS A1305    10900  12175   6567   -817     60  -1340       C  
ATOM   3263  O   LYS A1305      -6.364 -20.965 -56.320  1.00 71.94           O  
ANISOU 3263  O   LYS A1305     9954  11315   6065   -699    -31  -1154       O  
ATOM   3264  CB  LYS A1305      -5.784 -20.255 -59.445  1.00 81.89           C  
ANISOU 3264  CB  LYS A1305    11511  12951   6653    108    -39   -980       C  
ATOM   3265  CG  LYS A1305      -6.274 -18.951 -58.832  1.00 88.21           C  
ANISOU 3265  CG  LYS A1305    11991  14017   7509    526   -265   -764       C  
ATOM   3266  CD  LYS A1305      -6.549 -17.904 -59.901  1.00 94.99           C  
ANISOU 3266  CD  LYS A1305    12794  15318   7978   1158   -403   -593       C  
ATOM   3267  CE  LYS A1305      -7.529 -18.416 -60.945  1.00101.99           C  
ANISOU 3267  CE  LYS A1305    13493  17024   8234   1061   -576  -1009       C  
ATOM   3268  NZ  LYS A1305      -7.752 -17.423 -62.032  1.00104.22           N  
ANISOU 3268  NZ  LYS A1305    13766  17756   8076   1758   -705   -802       N  
ATOM   3269  N   GLU A1306      -7.134 -22.597 -57.679  1.00 81.11           N  
ANISOU 3269  N   GLU A1306    11231  12944   6641  -1343     83  -1833       N  
ATOM   3270  CA  GLU A1306      -8.187 -23.031 -56.766  1.00 84.19           C  
ANISOU 3270  CA  GLU A1306    11323  13674   6991  -1836     23  -2184       C  
ATOM   3271  C   GLU A1306      -7.611 -23.421 -55.409  1.00 81.45           C  
ANISOU 3271  C   GLU A1306    11190  12635   7122  -2045    226  -1988       C  
ATOM   3272  O   GLU A1306      -8.133 -23.023 -54.368  1.00 85.83           O  
ANISOU 3272  O   GLU A1306    11472  13342   7799  -2081    114  -1971       O  
ATOM   3273  CB  GLU A1306      -8.974 -24.208 -57.354  1.00 89.61           C  
ANISOU 3273  CB  GLU A1306    12005  14744   7297  -2485    116  -2777       C  
ATOM   3274  CG  GLU A1306      -9.697 -23.910 -58.662  1.00101.32           C  
ANISOU 3274  CG  GLU A1306    13188  16972   8337  -2279   -124  -2980       C  
ATOM   3275  CD  GLU A1306      -8.774 -23.939 -59.868  1.00110.34           C  
ANISOU 3275  CD  GLU A1306    14752  17913   9258  -2007    -22  -2871       C  
ATOM   3276  OE1 GLU A1306      -9.247 -24.273 -60.975  1.00114.03           O  
ANISOU 3276  OE1 GLU A1306    15142  18731   9454  -2042    -93  -3096       O  
ATOM   3277  OE2 GLU A1306      -7.575 -23.626 -59.706  1.00110.48           O  
ANISOU 3277  OE2 GLU A1306    15122  17206   9648  -1644    140  -2393       O  
ATOM   3278  N   VAL A1307      -6.530 -24.194 -55.431  1.00 74.54           N  
ANISOU 3278  N   VAL A1307    10808  11027   6486  -2139    529  -1831       N  
ATOM   3279  CA  VAL A1307      -5.872 -24.637 -54.206  1.00 67.25           C  
ANISOU 3279  CA  VAL A1307    10130   9452   5970  -2262    730  -1611       C  
ATOM   3280  C   VAL A1307      -5.275 -23.460 -53.439  1.00 60.39           C  
ANISOU 3280  C   VAL A1307     9103   8412   5431  -1763    559  -1159       C  
ATOM   3281  O   VAL A1307      -5.375 -23.391 -52.215  1.00 67.94           O  
ANISOU 3281  O   VAL A1307     9982   9240   6591  -1855    541  -1081       O  
ATOM   3282  CB  VAL A1307      -4.773 -25.677 -54.505  1.00 66.42           C  
ANISOU 3282  CB  VAL A1307    10585   8636   6016  -2345   1097  -1502       C  
ATOM   3283  CG1 VAL A1307      -3.986 -26.006 -53.246  1.00 69.93           C  
ANISOU 3283  CG1 VAL A1307    11258   8459   6854  -2315   1268  -1194       C  
ATOM   3284  CG2 VAL A1307      -5.387 -26.935 -55.097  1.00 65.30           C  
ANISOU 3284  CG2 VAL A1307    10683   8562   5566  -2933   1335  -1995       C  
ATOM   3285  N   TYR A1308      -4.662 -22.536 -54.171  1.00 57.77           N  
ANISOU 3285  N   TYR A1308     8747   8075   5130  -1259    459   -881       N  
ATOM   3286  CA  TYR A1308      -4.077 -21.336 -53.582  1.00 65.46           C  
ANISOU 3286  CA  TYR A1308     9595   8879   6399   -818    329   -491       C  
ATOM   3287  C   TYR A1308      -5.126 -20.540 -52.810  1.00 72.01           C  
ANISOU 3287  C   TYR A1308    10034  10172   7155   -786     82   -585       C  
ATOM   3288  O   TYR A1308      -4.947 -20.235 -51.625  1.00 82.54           O  
ANISOU 3288  O   TYR A1308    11313  11297   8752   -784     51   -444       O  
ATOM   3289  CB  TYR A1308      -3.458 -20.468 -54.679  1.00 66.75           C  
ANISOU 3289  CB  TYR A1308     9812   9027   6525   -336    310   -241       C  
ATOM   3290  CG  TYR A1308      -2.668 -19.279 -54.179  1.00 60.78           C  
ANISOU 3290  CG  TYR A1308     9009   7983   6103     57    266    151       C  
ATOM   3291  CD1 TYR A1308      -1.324 -19.402 -53.851  1.00 59.33           C  
ANISOU 3291  CD1 TYR A1308     9020   7224   6297    120    442    433       C  
ATOM   3292  CD2 TYR A1308      -3.260 -18.029 -54.055  1.00 57.41           C  
ANISOU 3292  CD2 TYR A1308     8343   7872   5597    366     68    221       C  
ATOM   3293  CE1 TYR A1308      -0.594 -18.318 -53.401  1.00 58.21           C  
ANISOU 3293  CE1 TYR A1308     8810   6853   6455    396    414    731       C  
ATOM   3294  CE2 TYR A1308      -2.540 -16.937 -53.606  1.00 59.61           C  
ANISOU 3294  CE2 TYR A1308     8632   7838   6178    664     77    538       C  
ATOM   3295  CZ  TYR A1308      -1.207 -17.088 -53.281  1.00 60.17           C  
ANISOU 3295  CZ  TYR A1308     8873   7358   6630    637    246    771       C  
ATOM   3296  OH  TYR A1308      -0.486 -16.004 -52.833  1.00 57.63           O  
ANISOU 3296  OH  TYR A1308     8535   6757   6604    852    265   1028       O  
ATOM   3297  N   ILE A1309      -6.226 -20.217 -53.484  1.00 68.82           N  
ANISOU 3297  N   ILE A1309     9349  10434   6364   -737    -94   -832       N  
ATOM   3298  CA  ILE A1309      -7.307 -19.461 -52.860  1.00 63.47           C  
ANISOU 3298  CA  ILE A1309     8266  10282   5569   -646   -317   -936       C  
ATOM   3299  C   ILE A1309      -7.918 -20.225 -51.685  1.00 66.76           C  
ANISOU 3299  C   ILE A1309     8581  10729   6055  -1163   -260  -1182       C  
ATOM   3300  O   ILE A1309      -8.179 -19.649 -50.624  1.00 71.00           O  
ANISOU 3300  O   ILE A1309     8952  11286   6740  -1085   -342  -1097       O  
ATOM   3301  CB  ILE A1309      -8.410 -19.111 -53.877  1.00 54.91           C  
ANISOU 3301  CB  ILE A1309     6857  10015   3993   -477   -519  -1183       C  
ATOM   3302  CG1 ILE A1309      -7.810 -18.387 -55.083  1.00 55.28           C  
ANISOU 3302  CG1 ILE A1309     7071  10014   3920     63   -538   -915       C  
ATOM   3303  CG2 ILE A1309      -9.481 -18.255 -53.227  1.00 55.89           C  
ANISOU 3303  CG2 ILE A1309     6542  10692   3999   -279   -732  -1249       C  
ATOM   3304  CD1 ILE A1309      -8.813 -18.080 -56.171  1.00 59.84           C  
ANISOU 3304  CD1 ILE A1309     7364  11423   3948    307   -744  -1125       C  
ATOM   3305  N   LEU A1310      -8.133 -21.524 -51.880  1.00 69.92           N  
ANISOU 3305  N   LEU A1310     9128  11100   6339  -1699    -81  -1489       N  
ATOM   3306  CA  LEU A1310      -8.697 -22.382 -50.839  1.00 71.60           C  
ANISOU 3306  CA  LEU A1310     9329  11279   6596  -2248     59  -1730       C  
ATOM   3307  C   LEU A1310      -7.863 -22.353 -49.561  1.00 68.27           C  
ANISOU 3307  C   LEU A1310     9145  10225   6569  -2182    165  -1400       C  
ATOM   3308  O   LEU A1310      -8.394 -22.139 -48.472  1.00 67.05           O  
ANISOU 3308  O   LEU A1310     8813  10191   6473  -2284    122  -1432       O  
ATOM   3309  CB  LEU A1310      -8.832 -23.822 -51.339  1.00 57.36           C  
ANISOU 3309  CB  LEU A1310     7797   9362   4635  -2834    327  -2077       C  
ATOM   3310  CG  LEU A1310      -9.329 -24.843 -50.314  1.00 77.30           C  
ANISOU 3310  CG  LEU A1310    10437  11725   7208  -3453    579  -2315       C  
ATOM   3311  CD1 LEU A1310     -10.713 -24.465 -49.808  1.00 80.93           C  
ANISOU 3311  CD1 LEU A1310    10352  12925   7472  -3663    415  -2622       C  
ATOM   3312  CD2 LEU A1310      -9.335 -26.246 -50.901  1.00 62.62           C  
ANISOU 3312  CD2 LEU A1310     8962   9625   5205  -4019    915  -2642       C  
ATOM   3313  N   LEU A1311      -6.558 -22.565 -49.702  1.00 64.58           N  
ANISOU 3313  N   LEU A1311     9057   9133   6348  -1995    301  -1090       N  
ATOM   3314  CA  LEU A1311      -5.654 -22.551 -48.557  1.00 64.22           C  
ANISOU 3314  CA  LEU A1311     9209   8549   6642  -1887    374   -771       C  
ATOM   3315  C   LEU A1311      -5.552 -21.157 -47.945  1.00 63.29           C  
ANISOU 3315  C   LEU A1311     8827   8544   6677  -1483    128   -543       C  
ATOM   3316  O   LEU A1311      -5.357 -21.015 -46.736  1.00 67.81           O  
ANISOU 3316  O   LEU A1311     9409   8932   7424  -1492    114   -420       O  
ATOM   3317  CB  LEU A1311      -4.269 -23.068 -48.950  1.00 65.91           C  
ANISOU 3317  CB  LEU A1311     9816   8169   7057  -1732    566   -503       C  
ATOM   3318  CG  LEU A1311      -4.202 -24.523 -49.427  1.00 67.14           C  
ANISOU 3318  CG  LEU A1311    10360   8054   7097  -2102    887   -691       C  
ATOM   3319  CD1 LEU A1311      -2.765 -24.931 -49.703  1.00 59.66           C  
ANISOU 3319  CD1 LEU A1311     9774   6524   6368  -1837   1081   -372       C  
ATOM   3320  CD2 LEU A1311      -4.846 -25.465 -48.418  1.00 67.64           C  
ANISOU 3320  CD2 LEU A1311    10568   8024   7109  -2574   1079   -885       C  
ATOM   3321  N   ASN A1312      -5.684 -20.132 -48.783  1.00 61.95           N  
ANISOU 3321  N   ASN A1312     8462   8661   6416  -1121    -42   -490       N  
ATOM   3322  CA  ASN A1312      -5.730 -18.758 -48.295  1.00 57.64           C  
ANISOU 3322  CA  ASN A1312     7709   8218   5974   -744   -228   -315       C  
ATOM   3323  C   ASN A1312      -6.933 -18.559 -47.374  1.00 65.59           C  
ANISOU 3323  C   ASN A1312     8426   9646   6849   -895   -331   -530       C  
ATOM   3324  O   ASN A1312      -6.842 -17.876 -46.351  1.00 69.16           O  
ANISOU 3324  O   ASN A1312     8823   9993   7462   -767   -398   -408       O  
ATOM   3325  CB  ASN A1312      -5.800 -17.775 -49.465  1.00 54.12           C  
ANISOU 3325  CB  ASN A1312     7170   8010   5383   -313   -332   -227       C  
ATOM   3326  CG  ASN A1312      -5.068 -16.474 -49.186  1.00 56.30           C  
ANISOU 3326  CG  ASN A1312     7487   7999   5906    103   -376     91       C  
ATOM   3327  OD1 ASN A1312      -4.427 -15.912 -50.073  1.00 59.80           O  
ANISOU 3327  OD1 ASN A1312     8058   8280   6384    409   -327    290       O  
ATOM   3328  ND2 ASN A1312      -5.156 -15.992 -47.950  1.00 39.04           N  
ANISOU 3328  ND2 ASN A1312     5218   5733   3881     88   -437    124       N  
ATOM   3329  N   TRP A1313      -8.058 -19.169 -47.739  1.00 64.88           N  
ANISOU 3329  N   TRP A1313     8139  10056   6456  -1192   -330   -878       N  
ATOM   3330  CA  TRP A1313      -9.275 -19.079 -46.935  1.00 65.60           C  
ANISOU 3330  CA  TRP A1313     7901  10624   6399  -1379   -393  -1123       C  
ATOM   3331  C   TRP A1313      -9.207 -19.951 -45.681  1.00 70.78           C  
ANISOU 3331  C   TRP A1313     8732  10961   7199  -1814   -213  -1168       C  
ATOM   3332  O   TRP A1313      -9.785 -19.611 -44.642  1.00 79.92           O  
ANISOU 3332  O   TRP A1313     9717  12287   8364  -1852   -246  -1215       O  
ATOM   3333  CB  TRP A1313     -10.503 -19.429 -47.776  1.00 68.43           C  
ANISOU 3333  CB  TRP A1313     7919  11713   6367  -1583   -452  -1516       C  
ATOM   3334  CG  TRP A1313     -10.992 -18.284 -48.611  1.00 72.15           C  
ANISOU 3334  CG  TRP A1313     8085  12717   6611  -1040   -685  -1476       C  
ATOM   3335  CD1 TRP A1313     -10.406 -17.777 -49.735  1.00 66.50           C  
ANISOU 3335  CD1 TRP A1313     7506  11920   5839   -622   -748  -1277       C  
ATOM   3336  CD2 TRP A1313     -12.171 -17.503 -48.387  1.00 81.98           C  
ANISOU 3336  CD2 TRP A1313     8861  14660   7629   -803   -855  -1616       C  
ATOM   3337  NE1 TRP A1313     -11.146 -16.728 -50.223  1.00 68.41           N  
ANISOU 3337  NE1 TRP A1313     7433  12744   5817   -118   -943  -1264       N  
ATOM   3338  CE2 TRP A1313     -12.236 -16.540 -49.414  1.00 82.69           C  
ANISOU 3338  CE2 TRP A1313     8851  15051   7516   -198  -1020  -1470       C  
ATOM   3339  CE3 TRP A1313     -13.179 -17.525 -47.418  1.00 82.86           C  
ANISOU 3339  CE3 TRP A1313     8633  15177   7674  -1014   -860  -1837       C  
ATOM   3340  CZ2 TRP A1313     -13.269 -15.607 -49.499  1.00 91.08           C  
ANISOU 3340  CZ2 TRP A1313     9496  16808   8304    251  -1198  -1524       C  
ATOM   3341  CZ3 TRP A1313     -14.203 -16.600 -47.504  1.00 86.18           C  
ANISOU 3341  CZ3 TRP A1313     8596  16308   7842   -600  -1038  -1913       C  
ATOM   3342  CH2 TRP A1313     -14.240 -15.654 -48.536  1.00 90.00           C  
ANISOU 3342  CH2 TRP A1313     9011  17032   8154     53  -1186  -1733       C  
ATOM   3343  N   ILE A1314      -8.500 -21.073 -45.780  1.00 67.96           N  
ANISOU 3343  N   ILE A1314     8753  10135   6935  -2103      5  -1137       N  
ATOM   3344  CA  ILE A1314      -8.230 -21.905 -44.613  1.00 70.43           C  
ANISOU 3344  CA  ILE A1314     9342  10039   7378  -2411    212  -1088       C  
ATOM   3345  C   ILE A1314      -7.351 -21.109 -43.649  1.00 67.29           C  
ANISOU 3345  C   ILE A1314     9020   9305   7241  -2042     98   -735       C  
ATOM   3346  O   ILE A1314      -7.397 -21.301 -42.433  1.00 67.93           O  
ANISOU 3346  O   ILE A1314     9181   9252   7375  -2164    160   -690       O  
ATOM   3347  CB  ILE A1314      -7.557 -23.241 -45.004  1.00 73.99           C  
ANISOU 3347  CB  ILE A1314    10249  10001   7861  -2690    503  -1080       C  
ATOM   3348  CG1 ILE A1314      -8.475 -24.045 -45.925  1.00 80.28           C  
ANISOU 3348  CG1 ILE A1314    10988  11139   8377  -3145    636  -1503       C  
ATOM   3349  CG2 ILE A1314      -7.223 -24.068 -43.772  1.00 72.59           C  
ANISOU 3349  CG2 ILE A1314    10421   9370   7792  -2903    739   -962       C  
ATOM   3350  CD1 ILE A1314      -7.917 -25.395 -46.317  1.00 83.86           C  
ANISOU 3350  CD1 ILE A1314    11954  11076   8835  -3458    983  -1546       C  
ATOM   3351  N   GLY A1315      -6.560 -20.197 -44.203  1.00 64.49           N  
ANISOU 3351  N   GLY A1315     8641   8833   7029  -1610    -55   -503       N  
ATOM   3352  CA  GLY A1315      -5.838 -19.239 -43.391  1.00 64.34           C  
ANISOU 3352  CA  GLY A1315     8617   8596   7233  -1295   -185   -245       C  
ATOM   3353  C   GLY A1315      -6.793 -18.211 -42.814  1.00 63.80           C  
ANISOU 3353  C   GLY A1315     8245   8926   7072  -1170   -339   -356       C  
ATOM   3354  O   GLY A1315      -6.630 -17.764 -41.679  1.00 69.67           O  
ANISOU 3354  O   GLY A1315     8997   9558   7916  -1115   -389   -274       O  
ATOM   3355  N   TYR A1316      -7.802 -17.843 -43.599  1.00 61.75           N  
ANISOU 3355  N   TYR A1316     7712   9160   6588  -1099   -412   -550       N  
ATOM   3356  CA  TYR A1316      -8.778 -16.839 -43.180  1.00 64.94           C  
ANISOU 3356  CA  TYR A1316     7807   9997   6871   -893   -539   -650       C  
ATOM   3357  C   TYR A1316      -9.618 -17.266 -41.973  1.00 66.03           C  
ANISOU 3357  C   TYR A1316     7828  10336   6924  -1214   -470   -841       C  
ATOM   3358  O   TYR A1316      -9.927 -16.442 -41.112  1.00 68.82           O  
ANISOU 3358  O   TYR A1316     8074  10779   7296  -1033   -536   -819       O  
ATOM   3359  CB  TYR A1316      -9.705 -16.461 -44.340  1.00 70.04           C  
ANISOU 3359  CB  TYR A1316     8153  11221   7238   -698   -636   -813       C  
ATOM   3360  CG  TYR A1316      -9.053 -15.640 -45.430  1.00 66.27           C  
ANISOU 3360  CG  TYR A1316     7777  10606   6797   -239   -706   -589       C  
ATOM   3361  CD1 TYR A1316      -7.840 -14.999 -45.218  1.00 59.51           C  
ANISOU 3361  CD1 TYR A1316     7193   9181   6239    -12   -683   -286       C  
ATOM   3362  CD2 TYR A1316      -9.658 -15.499 -46.672  1.00 70.25           C  
ANISOU 3362  CD2 TYR A1316     8098  11581   7013    -42   -782   -692       C  
ATOM   3363  CE1 TYR A1316      -7.246 -14.244 -46.213  1.00 59.30           C  
ANISOU 3363  CE1 TYR A1316     7286   8998   6249    371   -687    -81       C  
ATOM   3364  CE2 TYR A1316      -9.073 -14.748 -47.673  1.00 70.30           C  
ANISOU 3364  CE2 TYR A1316     8246  11442   7020    402   -808   -461       C  
ATOM   3365  CZ  TYR A1316      -7.868 -14.123 -47.439  1.00 65.13           C  
ANISOU 3365  CZ  TYR A1316     7897  10160   6691    594   -736   -150       C  
ATOM   3366  OH  TYR A1316      -7.284 -13.375 -48.435  1.00 67.42           O  
ANISOU 3366  OH  TYR A1316     8356  10275   6987    998   -704     80       O  
ATOM   3367  N   VAL A1317      -9.991 -18.543 -41.909  1.00 58.87           N  
ANISOU 3367  N   VAL A1317     6978   9476   5914  -1702   -300  -1035       N  
ATOM   3368  CA  VAL A1317     -10.858 -19.013 -40.823  1.00 57.70           C  
ANISOU 3368  CA  VAL A1317     6732   9528   5661  -2056   -173  -1230       C  
ATOM   3369  C   VAL A1317     -10.169 -19.005 -39.455  1.00 54.70           C  
ANISOU 3369  C   VAL A1317     6636   8696   5453  -2043   -121  -1016       C  
ATOM   3370  O   VAL A1317     -10.829 -19.075 -38.411  1.00 57.61           O  
ANISOU 3370  O   VAL A1317     6935   9219   5737  -2214    -38  -1121       O  
ATOM   3371  CB  VAL A1317     -11.434 -20.418 -41.099  1.00 53.17           C  
ANISOU 3371  CB  VAL A1317     6207   9065   4932  -2649     68  -1514       C  
ATOM   3372  CG1 VAL A1317     -12.226 -20.422 -42.395  1.00 54.92           C  
ANISOU 3372  CG1 VAL A1317     6082   9863   4924  -2704    -15  -1796       C  
ATOM   3373  CG2 VAL A1317     -10.327 -21.455 -41.134  1.00 53.08           C  
ANISOU 3373  CG2 VAL A1317     6712   8388   5069  -2827    261  -1335       C  
ATOM   3374  N   ASN A1318      -8.844 -18.916 -39.462  1.00 52.85           N  
ANISOU 3374  N   ASN A1318     6698   7949   5434  -1834   -168   -724       N  
ATOM   3375  CA  ASN A1318      -8.086 -18.844 -38.220  1.00 56.60           C  
ANISOU 3375  CA  ASN A1318     7403   8065   6036  -1770   -171   -521       C  
ATOM   3376  C   ASN A1318      -8.430 -17.586 -37.430  1.00 58.44           C  
ANISOU 3376  C   ASN A1318     7445   8491   6269  -1516   -327   -532       C  
ATOM   3377  O   ASN A1318      -8.360 -17.575 -36.202  1.00 56.75           O  
ANISOU 3377  O   ASN A1318     7337   8184   6040  -1565   -306   -494       O  
ATOM   3378  CB  ASN A1318      -6.583 -18.910 -38.495  1.00 60.21           C  
ANISOU 3378  CB  ASN A1318     8115   8049   6714  -1569   -219   -233       C  
ATOM   3379  CG  ASN A1318      -5.754 -18.771 -37.235  1.00 61.37           C  
ANISOU 3379  CG  ASN A1318     8432   7929   6956  -1469   -275    -41       C  
ATOM   3380  OD1 ASN A1318      -4.953 -17.845 -37.103  1.00 58.27           O  
ANISOU 3380  OD1 ASN A1318     7995   7422   6722  -1201   -446     94       O  
ATOM   3381  ND2 ASN A1318      -5.952 -19.687 -36.293  1.00 64.73           N  
ANISOU 3381  ND2 ASN A1318     9061   8272   7260  -1697   -115    -40       N  
ATOM   3382  N   SER A1319      -8.811 -16.532 -38.148  1.00 61.56           N  
ANISOU 3382  N   SER A1319     7595   9143   6653  -1218   -460   -581       N  
ATOM   3383  CA  SER A1319      -9.234 -15.283 -37.525  1.00 67.33           C  
ANISOU 3383  CA  SER A1319     8177  10039   7364   -935   -560   -609       C  
ATOM   3384  C   SER A1319     -10.485 -15.497 -36.678  1.00 66.78           C  
ANISOU 3384  C   SER A1319     7914  10374   7087  -1129   -465   -834       C  
ATOM   3385  O   SER A1319     -10.683 -14.830 -35.662  1.00 70.82           O  
ANISOU 3385  O   SER A1319     8423  10905   7579  -1012   -482   -847       O  
ATOM   3386  CB  SER A1319      -9.496 -14.216 -38.588  1.00 74.38           C  
ANISOU 3386  CB  SER A1319     8894  11127   8239   -533   -661   -598       C  
ATOM   3387  OG  SER A1319      -8.315 -13.912 -39.308  1.00 77.48           O  
ANISOU 3387  OG  SER A1319     9484  11121   8833   -357   -708   -381       O  
ATOM   3388  N   GLY A1320     -11.327 -16.429 -37.108  1.00 60.13           N  
ANISOU 3388  N   GLY A1320     6906   9861   6080  -1457   -342  -1037       N  
ATOM   3389  CA  GLY A1320     -12.518 -16.779 -36.361  1.00 60.39           C  
ANISOU 3389  CA  GLY A1320     6725  10301   5918  -1731   -199  -1277       C  
ATOM   3390  C   GLY A1320     -12.203 -17.790 -35.277  1.00 63.34           C  
ANISOU 3390  C   GLY A1320     7427  10340   6299  -2114      0  -1229       C  
ATOM   3391  O   GLY A1320     -12.850 -17.814 -34.228  1.00 64.00           O  
ANISOU 3391  O   GLY A1320     7465  10585   6266  -2249    121  -1327       O  
ATOM   3392  N   PHE A1321     -11.203 -18.628 -35.530  1.00 64.94           N  
ANISOU 3392  N   PHE A1321     7983  10073   6617  -2249     58  -1059       N  
ATOM   3393  CA  PHE A1321     -10.800 -19.641 -34.558  1.00 74.80           C  
ANISOU 3393  CA  PHE A1321     9619  10957   7846  -2527    267   -953       C  
ATOM   3394  C   PHE A1321     -10.073 -19.055 -33.346  1.00 81.34           C  
ANISOU 3394  C   PHE A1321    10641  11538   8726  -2266    152   -741       C  
ATOM   3395  O   PHE A1321     -10.086 -19.645 -32.266  1.00 88.17           O  
ANISOU 3395  O   PHE A1321    11751  12268   9481  -2433    315   -689       O  
ATOM   3396  CB  PHE A1321      -9.935 -20.713 -35.225  1.00 75.95           C  
ANISOU 3396  CB  PHE A1321    10102  10677   8077  -2669    385   -818       C  
ATOM   3397  CG  PHE A1321     -10.718 -21.709 -36.031  1.00 77.00           C  
ANISOU 3397  CG  PHE A1321    10191  10976   8091  -3117    622  -1078       C  
ATOM   3398  CD1 PHE A1321     -11.971 -22.126 -35.613  1.00 81.35           C  
ANISOU 3398  CD1 PHE A1321    10569  11887   8453  -3535    842  -1370       C  
ATOM   3399  CD2 PHE A1321     -10.201 -22.226 -37.209  1.00 78.08           C  
ANISOU 3399  CD2 PHE A1321    10449  10926   8293  -3153    643  -1061       C  
ATOM   3400  CE1 PHE A1321     -12.694 -23.044 -36.352  1.00 88.95           C  
ANISOU 3400  CE1 PHE A1321    11466  13034   9298  -4027   1073  -1670       C  
ATOM   3401  CE2 PHE A1321     -10.920 -23.143 -37.954  1.00 84.38           C  
ANISOU 3401  CE2 PHE A1321    11222  11883   8957  -3613    867  -1352       C  
ATOM   3402  CZ  PHE A1321     -12.167 -23.553 -37.525  1.00 90.66           C  
ANISOU 3402  CZ  PHE A1321    11829  13052   9568  -4075   1078  -1672       C  
ATOM   3403  N   ASN A1322      -9.442 -17.898 -33.525  1.00 77.01           N  
ANISOU 3403  N   ASN A1322    10003  10934   8322  -1873   -109   -632       N  
ATOM   3404  CA  ASN A1322      -8.678 -17.263 -32.447  1.00 68.22           C  
ANISOU 3404  CA  ASN A1322     9049   9618   7255  -1659   -245   -484       C  
ATOM   3405  C   ASN A1322      -9.456 -16.899 -31.170  1.00 73.21           C  
ANISOU 3405  C   ASN A1322     9647  10467   7702  -1696   -185   -607       C  
ATOM   3406  O   ASN A1322      -8.994 -17.204 -30.070  1.00 81.04           O  
ANISOU 3406  O   ASN A1322    10894  11289   8611  -1729   -161   -498       O  
ATOM   3407  CB  ASN A1322      -7.885 -16.052 -32.962  1.00 61.40           C  
ANISOU 3407  CB  ASN A1322     8103   8634   6592  -1306   -485   -396       C  
ATOM   3408  CG  ASN A1322      -6.707 -16.452 -33.827  1.00 65.06           C  
ANISOU 3408  CG  ASN A1322     8693   8782   7246  -1251   -539   -201       C  
ATOM   3409  OD1 ASN A1322      -6.176 -17.556 -33.704  1.00 72.33           O  
ANISOU 3409  OD1 ASN A1322     9832   9493   8155  -1395   -439    -74       O  
ATOM   3410  ND2 ASN A1322      -6.288 -15.550 -34.709  1.00 60.84           N  
ANISOU 3410  ND2 ASN A1322     8047   8193   6876  -1015   -662   -162       N  
ATOM   3411  N   PRO A1323     -10.629 -16.244 -31.300  1.00 70.52           N  
ANISOU 3411  N   PRO A1323     8990  10532   7271  -1651   -155   -826       N  
ATOM   3412  CA  PRO A1323     -11.350 -15.883 -30.070  1.00 71.83           C  
ANISOU 3412  CA  PRO A1323     9130  10902   7258  -1663    -69   -943       C  
ATOM   3413  C   PRO A1323     -11.828 -17.082 -29.246  1.00 69.89           C  
ANISOU 3413  C   PRO A1323     9054  10679   6822  -2053    210   -975       C  
ATOM   3414  O   PRO A1323     -12.241 -16.900 -28.101  1.00 72.07           O  
ANISOU 3414  O   PRO A1323     9393  11056   6933  -2071    304  -1027       O  
ATOM   3415  CB  PRO A1323     -12.555 -15.092 -30.592  1.00 73.40           C  
ANISOU 3415  CB  PRO A1323     8911  11583   7394  -1510    -60  -1163       C  
ATOM   3416  CG  PRO A1323     -12.117 -14.564 -31.908  1.00 72.52           C  
ANISOU 3416  CG  PRO A1323     8691  11411   7450  -1254   -235  -1095       C  
ATOM   3417  CD  PRO A1323     -11.262 -15.646 -32.490  1.00 70.06           C  
ANISOU 3417  CD  PRO A1323     8591  10782   7247  -1489   -222   -952       C  
ATOM   3418  N   LEU A1324     -11.775 -18.281 -29.816  1.00 66.91           N  
ANISOU 3418  N   LEU A1324     8791  10178   6454  -2363    378   -947       N  
ATOM   3419  CA  LEU A1324     -12.162 -19.485 -29.090  1.00 68.15           C  
ANISOU 3419  CA  LEU A1324     9205  10254   6435  -2757    716   -956       C  
ATOM   3420  C   LEU A1324     -10.971 -20.086 -28.352  1.00 70.00           C  
ANISOU 3420  C   LEU A1324     9944  10003   6651  -2672    722   -647       C  
ATOM   3421  O   LEU A1324     -11.134 -20.963 -27.503  1.00 76.74           O  
ANISOU 3421  O   LEU A1324    11122  10716   7320  -2888   1003   -580       O  
ATOM   3422  CB  LEU A1324     -12.756 -20.525 -30.041  1.00 53.63           C  
ANISOU 3422  CB  LEU A1324     7292   8495   4589  -3179    960  -1118       C  
ATOM   3423  CG  LEU A1324     -13.990 -20.105 -30.838  1.00 60.38           C  
ANISOU 3423  CG  LEU A1324     7589   9946   5406  -3294    954  -1451       C  
ATOM   3424  CD1 LEU A1324     -14.541 -21.284 -31.621  1.00 57.72           C  
ANISOU 3424  CD1 LEU A1324     7222   9690   5018  -3822   1227  -1658       C  
ATOM   3425  CD2 LEU A1324     -15.048 -19.520 -29.919  1.00 57.38           C  
ANISOU 3425  CD2 LEU A1324     6936  10003   4864  -3291   1043  -1629       C  
ATOM   3426  N   ILE A1325      -9.773 -19.610 -28.680  1.00 63.44           N  
ANISOU 3426  N   ILE A1325     9173   8940   5992  -2342    427   -456       N  
ATOM   3427  CA  ILE A1325      -8.548 -20.149 -28.099  1.00 62.54           C  
ANISOU 3427  CA  ILE A1325     9455   8454   5855  -2192    382   -158       C  
ATOM   3428  C   ILE A1325      -7.957 -19.217 -27.044  1.00 67.85           C  
ANISOU 3428  C   ILE A1325    10146   9172   6463  -1897    121    -89       C  
ATOM   3429  O   ILE A1325      -7.484 -19.666 -25.999  1.00 66.39           O  
ANISOU 3429  O   ILE A1325    10270   8872   6084  -1830    155     80       O  
ATOM   3430  CB  ILE A1325      -7.481 -20.409 -29.184  1.00 55.73           C  
ANISOU 3430  CB  ILE A1325     8633   7322   5218  -2051    255      8       C  
ATOM   3431  CG1 ILE A1325      -8.035 -21.322 -30.278  1.00 47.29           C  
ANISOU 3431  CG1 ILE A1325     7573   6203   4192  -2359    511    -97       C  
ATOM   3432  CG2 ILE A1325      -6.229 -21.019 -28.573  1.00 61.21           C  
ANISOU 3432  CG2 ILE A1325     9690   7705   5863  -1844    217    325       C  
ATOM   3433  CD1 ILE A1325      -7.042 -21.612 -31.381  1.00 46.71           C  
ANISOU 3433  CD1 ILE A1325     7565   5864   4319  -2219    427     54       C  
ATOM   3434  N   TYR A1326      -7.992 -17.918 -27.321  1.00 72.88           N  
ANISOU 3434  N   TYR A1326    10479   9977   7234  -1717   -122   -228       N  
ATOM   3435  CA  TYR A1326      -7.331 -16.935 -26.468  1.00 76.87           C  
ANISOU 3435  CA  TYR A1326    11003  10495   7709  -1481   -376   -217       C  
ATOM   3436  C   TYR A1326      -8.294 -16.169 -25.565  1.00 78.99           C  
ANISOU 3436  C   TYR A1326    11194  11023   7795  -1483   -322   -430       C  
ATOM   3437  O   TYR A1326      -7.954 -15.101 -25.057  1.00 86.38           O  
ANISOU 3437  O   TYR A1326    12100  11989   8732  -1307   -515   -511       O  
ATOM   3438  CB  TYR A1326      -6.532 -15.948 -27.322  1.00 79.99           C  
ANISOU 3438  CB  TYR A1326    11205  10800   8386  -1280   -639   -220       C  
ATOM   3439  CG  TYR A1326      -5.411 -16.580 -28.117  1.00 82.57           C  
ANISOU 3439  CG  TYR A1326    11596  10884   8893  -1230   -710     -2       C  
ATOM   3440  CD1 TYR A1326      -5.639 -17.100 -29.384  1.00 84.79           C  
ANISOU 3440  CD1 TYR A1326    11803  11095   9318  -1313   -591     17       C  
ATOM   3441  CD2 TYR A1326      -4.123 -16.651 -27.601  1.00 79.42           C  
ANISOU 3441  CD2 TYR A1326    11309  10370   8497  -1086   -896    168       C  
ATOM   3442  CE1 TYR A1326      -4.619 -17.677 -30.114  1.00 84.33           C  
ANISOU 3442  CE1 TYR A1326    11823  10804   9416  -1245   -623    213       C  
ATOM   3443  CE2 TYR A1326      -3.095 -17.227 -28.325  1.00 77.56           C  
ANISOU 3443  CE2 TYR A1326    11099   9946   8423   -999   -941    372       C  
ATOM   3444  CZ  TYR A1326      -3.349 -17.738 -29.580  1.00 81.19           C  
ANISOU 3444  CZ  TYR A1326    11526  10284   9038  -1074   -788    400       C  
ATOM   3445  OH  TYR A1326      -2.330 -18.313 -30.305  1.00 82.88           O  
ANISOU 3445  OH  TYR A1326    11787  10300   9404   -967   -801    600       O  
ATOM   3446  N   CYS A1327      -9.491 -16.710 -25.362  1.00 77.49           N  
ANISOU 3446  N   CYS A1327    10975  11022   7447  -1702    -33   -541       N  
ATOM   3447  CA  CYS A1327     -10.484 -16.052 -24.518  1.00 80.35           C  
ANISOU 3447  CA  CYS A1327    11240  11665   7622  -1695     67   -744       C  
ATOM   3448  C   CYS A1327     -11.262 -17.050 -23.666  1.00 78.63           C  
ANISOU 3448  C   CYS A1327    11206  11541   7131  -1969    412   -748       C  
ATOM   3449  O   CYS A1327     -12.481 -16.943 -23.532  1.00 78.44           O  
ANISOU 3449  O   CYS A1327    10972  11823   7007  -2109    634   -951       O  
ATOM   3450  CB  CYS A1327     -11.458 -15.232 -25.369  1.00 81.87           C  
ANISOU 3450  CB  CYS A1327    11029  12143   7936  -1621     81   -966       C  
ATOM   3451  SG  CYS A1327     -10.718 -13.828 -26.235  1.00 84.89           S  
ANISOU 3451  SG  CYS A1327    11270  12391   8595  -1255   -237   -970       S  
ATOM   3452  N   ARG A1328     -10.557 -18.014 -23.084  1.00 75.04           N  
ANISOU 3452  N   ARG A1328    11144  10831   6538  -2025    483   -514       N  
ATOM   3453  CA  ARG A1328     -11.210 -19.052 -22.296  1.00 70.92           C  
ANISOU 3453  CA  ARG A1328    10898  10306   5745  -2291    875   -472       C  
ATOM   3454  C   ARG A1328     -11.069 -18.823 -20.793  1.00 70.65           C  
ANISOU 3454  C   ARG A1328    11145  10315   5384  -2147    875   -411       C  
ATOM   3455  O   ARG A1328     -11.457 -19.672 -19.988  1.00 68.00           O  
ANISOU 3455  O   ARG A1328    11131   9931   4775  -2313   1210   -320       O  
ATOM   3456  CB  ARG A1328     -10.676 -20.434 -22.677  1.00 65.18           C  
ANISOU 3456  CB  ARG A1328    10512   9225   5028  -2443   1066   -231       C  
ATOM   3457  CG  ARG A1328     -10.781 -20.748 -24.159  1.00 63.03           C  
ANISOU 3457  CG  ARG A1328    10011   8897   5041  -2610   1084   -307       C  
ATOM   3458  CD  ARG A1328     -10.885 -22.244 -24.394  1.00 67.62           C  
ANISOU 3458  CD  ARG A1328    10953   9181   5560  -2936   1488   -197       C  
ATOM   3459  NE  ARG A1328     -12.165 -22.772 -23.930  1.00 76.00           N  
ANISOU 3459  NE  ARG A1328    12036  10405   6436  -3364   1932   -386       N  
ATOM   3460  CZ  ARG A1328     -12.468 -24.065 -23.885  1.00 93.19           C  
ANISOU 3460  CZ  ARG A1328    14591  12313   8504  -3742   2402   -337       C  
ATOM   3461  NH1 ARG A1328     -11.578 -24.969 -24.271  1.00 98.53           N  
ANISOU 3461  NH1 ARG A1328    15688  12522   9226  -3686   2485    -84       N  
ATOM   3462  NH2 ARG A1328     -13.658 -24.455 -23.449  1.00102.60           N  
ANISOU 3462  NH2 ARG A1328    15755  13689   9538  -4180   2826   -547       N  
ATOM   3463  N   SER A1329     -10.513 -17.672 -20.422  1.00 68.01           N  
ANISOU 3463  N   SER A1329    10718  10063   5060  -1855    526   -473       N  
ATOM   3464  CA  SER A1329     -10.346 -17.319 -19.016  1.00 69.04           C  
ANISOU 3464  CA  SER A1329    11094  10284   4855  -1710    477   -468       C  
ATOM   3465  C   SER A1329     -11.705 -17.091 -18.364  1.00 78.33           C  
ANISOU 3465  C   SER A1329    12200  11727   5833  -1856    798   -683       C  
ATOM   3466  O   SER A1329     -12.660 -16.709 -19.042  1.00 86.17           O  
ANISOU 3466  O   SER A1329    12826  12916   7000  -1965    917   -897       O  
ATOM   3467  CB  SER A1329      -9.476 -16.066 -18.875  1.00 63.65           C  
ANISOU 3467  CB  SER A1329    10300   9631   4253  -1439     47   -564       C  
ATOM   3468  OG  SER A1329     -10.194 -14.895 -19.218  1.00 60.81           O  
ANISOU 3468  OG  SER A1329     9632   9427   4047  -1400     25   -848       O  
ATOM   3469  N   PRO A1330     -11.799 -17.337 -17.047  1.00 80.64           N  
ANISOU 3469  N   PRO A1330    12834  12069   5737  -1834    945   -621       N  
ATOM   3470  CA  PRO A1330     -13.040 -17.120 -16.295  1.00 84.92           C  
ANISOU 3470  CA  PRO A1330    13336  12875   6053  -1957   1280   -818       C  
ATOM   3471  C   PRO A1330     -13.575 -15.699 -16.452  1.00 86.10           C  
ANISOU 3471  C   PRO A1330    13110  13273   6331  -1797   1138  -1130       C  
ATOM   3472  O   PRO A1330     -14.787 -15.511 -16.581  1.00 98.10           O  
ANISOU 3472  O   PRO A1330    14348  15061   7865  -1913   1415  -1329       O  
ATOM   3473  CB  PRO A1330     -12.612 -17.369 -14.849  1.00 87.82           C  
ANISOU 3473  CB  PRO A1330    14184  13216   5966  -1828   1311   -668       C  
ATOM   3474  CG  PRO A1330     -11.492 -18.342 -14.964  1.00 85.65           C  
ANISOU 3474  CG  PRO A1330    14235  12651   5655  -1752   1198   -322       C  
ATOM   3475  CD  PRO A1330     -10.750 -17.948 -16.209  1.00 78.46           C  
ANISOU 3475  CD  PRO A1330    13008  11627   5174  -1669    836   -336       C  
ATOM   3476  N   ASP A1331     -12.680 -14.716 -16.451  1.00 71.88           N  
ANISOU 3476  N   ASP A1331    11307  11387   4616  -1531    738  -1177       N  
ATOM   3477  CA  ASP A1331     -13.074 -13.324 -16.634  1.00 72.36           C  
ANISOU 3477  CA  ASP A1331    11110  11579   4804  -1340    633  -1453       C  
ATOM   3478  C   ASP A1331     -13.706 -13.108 -18.006  1.00 75.49           C  
ANISOU 3478  C   ASP A1331    11070  12059   5553  -1354    678  -1537       C  
ATOM   3479  O   ASP A1331     -14.724 -12.425 -18.130  1.00 83.93           O  
ANISOU 3479  O   ASP A1331    11871  13381   6638  -1253    834  -1744       O  
ATOM   3480  CB  ASP A1331     -11.872 -12.398 -16.455  1.00 69.86           C  
ANISOU 3480  CB  ASP A1331    10920  11087   4536  -1134    228  -1494       C  
ATOM   3481  CG  ASP A1331     -11.281 -12.474 -15.065  1.00 74.92           C  
ANISOU 3481  CG  ASP A1331    11942  11753   4770  -1092    136  -1468       C  
ATOM   3482  OD1 ASP A1331     -10.446 -13.371 -14.825  1.00 78.38           O  
ANISOU 3482  OD1 ASP A1331    12590  12107   5083  -1121     21  -1218       O  
ATOM   3483  OD2 ASP A1331     -11.649 -11.637 -14.214  1.00 78.03           O  
ANISOU 3483  OD2 ASP A1331    12436  12269   4944   -996    183  -1695       O  
ATOM   3484  N   PHE A1332     -13.097 -13.696 -19.032  1.00 68.19           N  
ANISOU 3484  N   PHE A1332    10075  10953   4882  -1440    544  -1372       N  
ATOM   3485  CA  PHE A1332     -13.642 -13.624 -20.382  1.00 66.37           C  
ANISOU 3485  CA  PHE A1332     9451  10829   4939  -1461    572  -1436       C  
ATOM   3486  C   PHE A1332     -14.998 -14.320 -20.471  1.00 67.18           C  
ANISOU 3486  C   PHE A1332     9314  11269   4942  -1720    951  -1545       C  
ATOM   3487  O   PHE A1332     -15.890 -13.854 -21.171  1.00 66.19           O  
ANISOU 3487  O   PHE A1332     8776  11453   4920  -1650   1016  -1718       O  
ATOM   3488  CB  PHE A1332     -12.668 -14.223 -21.404  1.00 67.93           C  
ANISOU 3488  CB  PHE A1332     9673  10752   5386  -1524    380  -1235       C  
ATOM   3489  CG  PHE A1332     -11.773 -13.207 -22.059  1.00 65.60           C  
ANISOU 3489  CG  PHE A1332     9316  10267   5344  -1265     48  -1233       C  
ATOM   3490  CD1 PHE A1332     -12.287 -12.298 -22.968  1.00 66.10           C  
ANISOU 3490  CD1 PHE A1332     9077  10442   5595  -1076     19  -1368       C  
ATOM   3491  CD2 PHE A1332     -10.420 -13.167 -21.774  1.00 65.64           C  
ANISOU 3491  CD2 PHE A1332     9559  10002   5381  -1202   -214  -1092       C  
ATOM   3492  CE1 PHE A1332     -11.469 -11.363 -23.574  1.00 61.07           C  
ANISOU 3492  CE1 PHE A1332     8445   9574   5185   -858   -220  -1353       C  
ATOM   3493  CE2 PHE A1332      -9.597 -12.235 -22.379  1.00 60.69           C  
ANISOU 3493  CE2 PHE A1332     8865   9197   4997  -1033   -470  -1116       C  
ATOM   3494  CZ  PHE A1332     -10.123 -11.332 -23.279  1.00 54.91           C  
ANISOU 3494  CZ  PHE A1332     7900   8501   4464   -875   -450  -1241       C  
ATOM   3495  N   ARG A1333     -15.145 -15.432 -19.757  1.00 69.03           N  
ANISOU 3495  N   ARG A1333     9806  11461   4960  -2014   1217  -1445       N  
ATOM   3496  CA  ARG A1333     -16.409 -16.163 -19.713  1.00 77.70           C  
ANISOU 3496  CA  ARG A1333    10709  12866   5947  -2359   1641  -1574       C  
ATOM   3497  C   ARG A1333     -17.528 -15.308 -19.118  1.00 78.95           C  
ANISOU 3497  C   ARG A1333    10595  13448   5953  -2226   1811  -1824       C  
ATOM   3498  O   ARG A1333     -18.600 -15.149 -19.718  1.00 81.59           O  
ANISOU 3498  O   ARG A1333    10439  14206   6355  -2288   1960  -2031       O  
ATOM   3499  CB  ARG A1333     -16.246 -17.442 -18.890  1.00 87.19           C  
ANISOU 3499  CB  ARG A1333    12374  13845   6911  -2671   1945  -1389       C  
ATOM   3500  CG  ARG A1333     -15.394 -18.517 -19.545  1.00 89.10           C  
ANISOU 3500  CG  ARG A1333    12876  13697   7282  -2836   1913  -1152       C  
ATOM   3501  CD  ARG A1333     -16.233 -19.395 -20.454  1.00102.93           C  
ANISOU 3501  CD  ARG A1333    14382  15572   9153  -3285   2228  -1284       C  
ATOM   3502  NE  ARG A1333     -15.583 -20.671 -20.737  1.00114.20           N  
ANISOU 3502  NE  ARG A1333    16227  16563  10601  -3516   2380  -1055       N  
ATOM   3503  CZ  ARG A1333     -16.177 -21.690 -21.350  1.00124.53           C  
ANISOU 3503  CZ  ARG A1333    17503  17852  11959  -3996   2739  -1153       C  
ATOM   3504  NH1 ARG A1333     -17.439 -21.583 -21.745  1.00129.09           N  
ANISOU 3504  NH1 ARG A1333    17578  18904  12565  -4316   2946  -1491       N  
ATOM   3505  NH2 ARG A1333     -15.512 -22.816 -21.567  1.00125.33           N  
ANISOU 3505  NH2 ARG A1333    18074  17478  12068  -4154   2905   -928       N  
ATOM   3506  N   ILE A1334     -17.269 -14.765 -17.932  1.00 75.79           N  
ANISOU 3506  N   ILE A1334    10502  12971   5322  -2024   1788  -1813       N  
ATOM   3507  CA  ILE A1334     -18.230 -13.907 -17.246  1.00 79.40           C  
ANISOU 3507  CA  ILE A1334    10785  13777   5607  -1845   1967  -2039       C  
ATOM   3508  C   ILE A1334     -18.578 -12.686 -18.093  1.00 85.62           C  
ANISOU 3508  C   ILE A1334    11156  14763   6611  -1475   1782  -2209       C  
ATOM   3509  O   ILE A1334     -19.744 -12.293 -18.187  1.00 91.76           O  
ANISOU 3509  O   ILE A1334    11529  15989   7347  -1383   1998  -2408       O  
ATOM   3510  CB  ILE A1334     -17.690 -13.452 -15.879  1.00 79.34           C  
ANISOU 3510  CB  ILE A1334    11247  13595   5304  -1663   1914  -2006       C  
ATOM   3511  CG1 ILE A1334     -17.387 -14.668 -15.001  1.00 79.50           C  
ANISOU 3511  CG1 ILE A1334    11717  13445   5044  -1950   2122  -1797       C  
ATOM   3512  CG2 ILE A1334     -18.685 -12.534 -15.187  1.00 90.14           C  
ANISOU 3512  CG2 ILE A1334    12465  15294   6488  -1452   2129  -2254       C  
ATOM   3513  CD1 ILE A1334     -16.709 -14.325 -13.695  1.00 82.84           C  
ANISOU 3513  CD1 ILE A1334    12621  13728   5124  -1755   2009  -1739       C  
ATOM   3514  N   ALA A1335     -17.560 -12.097 -18.715  1.00 86.38           N  
ANISOU 3514  N   ALA A1335    11356  14538   6928  -1244   1407  -2119       N  
ATOM   3515  CA  ALA A1335     -17.757 -10.953 -19.597  1.00 84.46           C  
ANISOU 3515  CA  ALA A1335    10817  14382   6890   -861   1250  -2226       C  
ATOM   3516  C   ALA A1335     -18.668 -11.311 -20.767  1.00 80.23           C  
ANISOU 3516  C   ALA A1335     9742  14253   6489   -928   1346  -2292       C  
ATOM   3517  O   ALA A1335     -19.607 -10.580 -21.081  1.00 72.77           O  
ANISOU 3517  O   ALA A1335     8420  13701   5529   -632   1438  -2450       O  
ATOM   3518  CB  ALA A1335     -16.419 -10.439 -20.105  1.00 66.82           C  
ANISOU 3518  CB  ALA A1335     8823  11686   4878   -702    879  -2098       C  
ATOM   3519  N   PHE A1336     -18.386 -12.446 -21.399  1.00 74.47           N  
ANISOU 3519  N   PHE A1336     8982  13450   5863  -1302   1331  -2180       N  
ATOM   3520  CA  PHE A1336     -19.156 -12.907 -22.550  1.00 69.70           C  
ANISOU 3520  CA  PHE A1336     7879  13240   5362  -1450   1398  -2275       C  
ATOM   3521  C   PHE A1336     -20.610 -13.182 -22.183  1.00 78.26           C  
ANISOU 3521  C   PHE A1336     8547  14937   6252  -1631   1761  -2508       C  
ATOM   3522  O   PHE A1336     -21.514 -12.917 -22.975  1.00 79.05           O  
ANISOU 3522  O   PHE A1336     8091  15569   6375  -1513   1784  -2675       O  
ATOM   3523  CB  PHE A1336     -18.521 -14.157 -23.167  1.00 67.66           C  
ANISOU 3523  CB  PHE A1336     7769  12716   5223  -1873   1366  -2132       C  
ATOM   3524  CG  PHE A1336     -17.210 -13.896 -23.856  1.00 65.89           C  
ANISOU 3524  CG  PHE A1336     7791  12019   5227  -1678   1013  -1928       C  
ATOM   3525  CD1 PHE A1336     -16.863 -12.615 -24.255  1.00 61.98           C  
ANISOU 3525  CD1 PHE A1336     7249  11443   4858  -1203    765  -1921       C  
ATOM   3526  CD2 PHE A1336     -16.324 -14.932 -24.104  1.00 61.57           C  
ANISOU 3526  CD2 PHE A1336     7538  11092   4762  -1962    973  -1740       C  
ATOM   3527  CE1 PHE A1336     -15.657 -12.373 -24.887  1.00 58.60           C  
ANISOU 3527  CE1 PHE A1336     7030  10589   4646  -1070    483  -1748       C  
ATOM   3528  CE2 PHE A1336     -15.117 -14.697 -24.735  1.00 58.18           C  
ANISOU 3528  CE2 PHE A1336     7289  10274   4544  -1780    669  -1559       C  
ATOM   3529  CZ  PHE A1336     -14.784 -13.415 -25.127  1.00 56.61           C  
ANISOU 3529  CZ  PHE A1336     7005  10024   4480  -1361    425  -1571       C  
ATOM   3530  N   GLN A1337     -20.838 -13.713 -20.985  1.00 76.56           N  
ANISOU 3530  N   GLN A1337     8579  14688   5824  -1906   2050  -2519       N  
ATOM   3531  CA  GLN A1337     -22.206 -13.964 -20.542  1.00 87.68           C  
ANISOU 3531  CA  GLN A1337     9592  16678   7042  -2113   2446  -2750       C  
ATOM   3532  C   GLN A1337     -22.950 -12.670 -20.218  1.00 90.72           C  
ANISOU 3532  C   GLN A1337     9687  17452   7331  -1578   2471  -2907       C  
ATOM   3533  O   GLN A1337     -24.120 -12.511 -20.569  1.00 96.94           O  
ANISOU 3533  O   GLN A1337     9873  18880   8080  -1522   2628  -3113       O  
ATOM   3534  CB  GLN A1337     -22.236 -14.901 -19.335  1.00 86.45           C  
ANISOU 3534  CB  GLN A1337     9844  16340   6664  -2549   2806  -2694       C  
ATOM   3535  CG  GLN A1337     -23.637 -15.127 -18.788  1.00 90.40           C  
ANISOU 3535  CG  GLN A1337     9972  17288   7088  -2743   3169  -2876       C  
ATOM   3536  CD  GLN A1337     -23.664 -16.100 -17.632  1.00 99.51           C  
ANISOU 3536  CD  GLN A1337    11589  18119   8101  -3135   3498  -2753       C  
ATOM   3537  OE1 GLN A1337     -24.617 -16.129 -16.855  1.00102.20           O  
ANISOU 3537  OE1 GLN A1337    11794  18685   8352  -3204   3780  -2848       O  
ATOM   3538  NE2 GLN A1337     -22.619 -16.909 -17.514  1.00107.53           N  
ANISOU 3538  NE2 GLN A1337    13171  18599   9086  -3353   3474  -2520       N  
ATOM   3539  N   GLU A1338     -22.267 -11.747 -19.549  1.00 89.67           N  
ANISOU 3539  N   GLU A1338     9983  16929   7159  -1178   2315  -2816       N  
ATOM   3540  CA  GLU A1338     -22.885 -10.489 -19.141  1.00 96.94           C  
ANISOU 3540  CA  GLU A1338    10763  18099   7972   -644   2385  -2958       C  
ATOM   3541  C   GLU A1338     -23.184  -9.574 -20.331  1.00100.27           C  
ANISOU 3541  C   GLU A1338    10771  18768   8558   -138   2188  -3000       C  
ATOM   3542  O   GLU A1338     -24.161  -8.823 -20.314  1.00102.42           O  
ANISOU 3542  O   GLU A1338    10672  19516   8727    272   2341  -3150       O  
ATOM   3543  CB  GLU A1338     -22.001  -9.768 -18.118  1.00 96.87           C  
ANISOU 3543  CB  GLU A1338    11386  17556   7864   -414   2280  -2887       C  
ATOM   3544  CG  GLU A1338     -22.575  -8.460 -17.597  1.00101.57           C  
ANISOU 3544  CG  GLU A1338    11961  18301   8328    128   2403  -3047       C  
ATOM   3545  CD  GLU A1338     -21.721  -7.846 -16.507  1.00108.16           C  
ANISOU 3545  CD  GLU A1338    13442  18631   9024    244   2327  -3039       C  
ATOM   3546  OE1 GLU A1338     -20.872  -8.567 -15.941  1.00107.31           O  
ANISOU 3546  OE1 GLU A1338    13732  18198   8842   -116   2229  -2916       O  
ATOM   3547  OE2 GLU A1338     -21.895  -6.644 -16.216  1.00115.44           O  
ANISOU 3547  OE2 GLU A1338    14483  19493   9887    709   2373  -3164       O  
ATOM   3548  N   LEU A1339     -22.346  -9.646 -21.362  1.00 98.45           N  
ANISOU 3548  N   LEU A1339    10618  18227   8561   -130   1870  -2852       N  
ATOM   3549  CA  LEU A1339     -22.497  -8.787 -22.536  1.00 97.34           C  
ANISOU 3549  CA  LEU A1339    10181  18249   8556    378   1677  -2841       C  
ATOM   3550  C   LEU A1339     -23.817  -9.000 -23.275  1.00101.88           C  
ANISOU 3550  C   LEU A1339     9994  19666   9049    438   1802  -3011       C  
ATOM   3551  O   LEU A1339     -24.499  -8.039 -23.628  1.00106.60           O  
ANISOU 3551  O   LEU A1339    10275  20645   9582   1035   1819  -3073       O  
ATOM   3552  CB  LEU A1339     -21.324  -8.974 -23.501  1.00 75.73           C  
ANISOU 3552  CB  LEU A1339     7680  15025   6069    301   1347  -2644       C  
ATOM   3553  CG  LEU A1339     -20.048  -8.196 -23.182  1.00 72.77           C  
ANISOU 3553  CG  LEU A1339     7909  13924   5814    507   1149  -2501       C  
ATOM   3554  CD1 LEU A1339     -18.990  -8.449 -24.244  1.00 68.68           C  
ANISOU 3554  CD1 LEU A1339     7520  13028   5550    416    862  -2317       C  
ATOM   3555  CD2 LEU A1339     -20.343  -6.710 -23.060  1.00 75.01           C  
ANISOU 3555  CD2 LEU A1339     8270  14175   6058   1148   1201  -2564       C  
ATOM   3556  N   LEU A1340     -24.172 -10.259 -23.506  1.00104.80           N  
ANISOU 3556  N   LEU A1340    10075  20339   9404   -174   1904  -3097       N  
ATOM   3557  CA  LEU A1340     -25.382 -10.578 -24.256  1.00115.72           C  
ANISOU 3557  CA  LEU A1340    10711  22512  10744   -240   1958  -3280       C  
ATOM   3558  C   LEU A1340     -26.541 -11.019 -23.361  1.00134.82           C  
ANISOU 3558  C   LEU A1340    12873  25276  13078   -550   2230  -3425       C  
ATOM   3559  O   LEU A1340     -27.575 -11.471 -23.856  1.00145.73           O  
ANISOU 3559  O   LEU A1340    13700  27215  14457   -760   2225  -3580       O  
ATOM   3560  CB  LEU A1340     -25.085 -11.624 -25.336  1.00111.12           C  
ANISOU 3560  CB  LEU A1340     9967  21987  10266   -732   1828  -3297       C  
ATOM   3561  CG  LEU A1340     -24.102 -12.746 -24.986  1.00103.46           C  
ANISOU 3561  CG  LEU A1340     9548  20381   9382  -1374   1886  -3178       C  
ATOM   3562  CD1 LEU A1340     -24.770 -13.814 -24.137  1.00102.18           C  
ANISOU 3562  CD1 LEU A1340     9355  20340   9127  -2020   2243  -3309       C  
ATOM   3563  CD2 LEU A1340     -23.490 -13.355 -26.244  1.00 80.57           C  
ANISOU 3563  CD2 LEU A1340     6650  17312   6651  -1590   1648  -3106       C  
ATOM   3564  N   CYS A1341     -26.358 -10.875 -22.049  1.00139.37           N  
ANISOU 3564  N   CYS A1341    13876  25524  13554   -578   2456  -3389       N  
ATOM   3565  CA  CYS A1341     -27.389 -11.197 -21.058  1.00143.42           C  
ANISOU 3565  CA  CYS A1341    14230  26296  13968   -817   2763  -3502       C  
ATOM   3566  C   CYS A1341     -27.962 -12.604 -21.219  1.00147.37           C  
ANISOU 3566  C   CYS A1341    14476  27007  14512  -1588   2909  -3622       C  
ATOM   3567  O   CYS A1341     -29.163 -12.773 -21.427  1.00152.87           O  
ANISOU 3567  O   CYS A1341    14613  28281  15188  -1692   2971  -3806       O  
ATOM   3568  CB  CYS A1341     -28.519 -10.164 -21.092  1.00144.57           C  
ANISOU 3568  CB  CYS A1341    13902  26972  14056   -220   2769  -3593       C  
ATOM   3569  SG  CYS A1341     -28.029  -8.500 -20.584  1.00118.79           S  
ANISOU 3569  SG  CYS A1341    11072  23343  10720    661   2737  -3481       S  
ATOM   3570  N   LEU A1342     -27.097 -13.607 -21.116  1.00141.03           N  
ANISOU 3570  N   LEU A1342    14125  25709  13751  -2121   2968  -3523       N  
ATOM   3571  CA  LEU A1342     -27.512 -14.995 -21.285  1.00135.44           C  
ANISOU 3571  CA  LEU A1342    13325  25040  13096  -2872   3141  -3629       C  
ATOM   3572  C   LEU A1342     -28.186 -15.527 -20.022  1.00137.67           C  
ANISOU 3572  C   LEU A1342    13752  25284  13272  -3215   3539  -3673       C  
ATOM   3573  O   LEU A1342     -29.065 -14.878 -19.450  1.00132.22           O  
ANISOU 3573  O   LEU A1342    12777  24970  12490  -2930   3658  -3767       O  
ATOM   3574  CB  LEU A1342     -26.310 -15.868 -21.652  1.00119.57           C  
ANISOU 3574  CB  LEU A1342    11821  22438  11170  -3250   3087  -3467       C  
ATOM   3575  CG  LEU A1342     -26.604 -17.260 -22.211  1.00118.70           C  
ANISOU 3575  CG  LEU A1342    11653  22297  11150  -3970   3207  -3593       C  
ATOM   3576  CD1 LEU A1342     -27.414 -17.163 -23.497  1.00117.54           C  
ANISOU 3576  CD1 LEU A1342    10813  22795  11051  -3964   2975  -3854       C  
ATOM   3577  CD2 LEU A1342     -25.311 -18.026 -22.445  1.00116.43           C  
ANISOU 3577  CD2 LEU A1342    11975  21329  10934  -4228   3184  -3373       C  
TER    3578      LEU A1342                                                      
ATOM   3579  N   GLN B   1     -10.490 -28.667  -8.635  1.00116.18           N  
ANISOU 3579  N   GLN B   1    12115  19636  12392  -2576   -227  -1704       N  
ATOM   3580  CA  GLN B   1     -10.993 -29.538  -7.581  1.00112.40           C  
ANISOU 3580  CA  GLN B   1    11835  18934  11936  -2976     -2  -1803       C  
ATOM   3581  C   GLN B   1      -9.897 -29.888  -6.579  1.00107.08           C  
ANISOU 3581  C   GLN B   1    11628  17731  11327  -2873     82  -1536       C  
ATOM   3582  O   GLN B   1      -9.804 -31.027  -6.118  1.00105.20           O  
ANISOU 3582  O   GLN B   1    11790  17123  11059  -3126    263  -1587       O  
ATOM   3583  CB  GLN B   1     -11.591 -30.815  -8.177  1.00114.94           C  
ANISOU 3583  CB  GLN B   1    12242  19249  12180  -3407    136  -2133       C  
ATOM   3584  N   VAL B   2      -9.067 -28.902  -6.249  1.00104.09           N  
ANISOU 3584  N   VAL B   2    11221  17320  11009  -2493    -48  -1266       N  
ATOM   3585  CA  VAL B   2      -8.006 -29.087  -5.264  1.00100.01           C  
ANISOU 3585  CA  VAL B   2    11068  16400  10533  -2336    -11  -1035       C  
ATOM   3586  C   VAL B   2      -8.292 -28.271  -4.008  1.00103.40           C  
ANISOU 3586  C   VAL B   2    11425  16859  11004  -2311     16   -901       C  
ATOM   3587  O   VAL B   2      -9.075 -27.321  -4.037  1.00106.00           O  
ANISOU 3587  O   VAL B   2    11401  17528  11347  -2300    -34   -940       O  
ATOM   3588  CB  VAL B   2      -6.626 -28.687  -5.824  1.00 94.55           C  
ANISOU 3588  CB  VAL B   2    10410  15648   9865  -1946   -163   -870       C  
ATOM   3589  CG1 VAL B   2      -6.353 -29.413  -7.131  1.00100.59           C  
ANISOU 3589  CG1 VAL B   2    11221  16422  10578  -1947   -192  -1011       C  
ATOM   3590  CG2 VAL B   2      -6.543 -27.183  -6.019  1.00 87.37           C  
ANISOU 3590  CG2 VAL B   2     9173  15030   8992  -1713   -298   -749       C  
ATOM   3591  N   GLN B   3      -7.651 -28.645  -2.905  1.00105.88           N  
ANISOU 3591  N   GLN B   3    12093  16821  11315  -2263     87   -750       N  
ATOM   3592  CA  GLN B   3      -7.894 -27.991  -1.626  1.00103.48           C  
ANISOU 3592  CA  GLN B   3    11776  16510  11030  -2258    130   -631       C  
ATOM   3593  C   GLN B   3      -6.639 -27.296  -1.108  1.00 92.21           C  
ANISOU 3593  C   GLN B   3    10420  14977   9638  -1888     -4   -402       C  
ATOM   3594  O   GLN B   3      -5.521 -27.678  -1.450  1.00 80.89           O  
ANISOU 3594  O   GLN B   3     9152  13388   8193  -1672    -82   -343       O  
ATOM   3595  CB  GLN B   3      -8.387 -29.009  -0.594  1.00112.11           C  
ANISOU 3595  CB  GLN B   3    13248  17304  12043  -2572    358   -674       C  
ATOM   3596  CG  GLN B   3      -9.364 -30.042  -1.144  1.00118.94           C  
ANISOU 3596  CG  GLN B   3    14168  18175  12847  -3010    540   -939       C  
ATOM   3597  CD  GLN B   3     -10.655 -29.426  -1.652  1.00123.21           C  
ANISOU 3597  CD  GLN B   3    14171  19227  13415  -3224    541  -1165       C  
ATOM   3598  OE1 GLN B   3     -11.062 -28.351  -1.212  1.00127.49           O  
ANISOU 3598  OE1 GLN B   3    14398  20045  13999  -3109    479  -1118       O  
ATOM   3599  NE2 GLN B   3     -11.305 -30.109  -2.587  1.00123.76           N  
ANISOU 3599  NE2 GLN B   3    14135  19444  13443  -3513    604  -1435       N  
ATOM   3600  N   LEU B   4      -6.834 -26.274  -0.281  1.00 95.56           N  
ANISOU 3600  N   LEU B   4    10698  15514  10095  -1822    -24   -305       N  
ATOM   3601  CA  LEU B   4      -5.721 -25.566   0.344  1.00 88.89           C  
ANISOU 3601  CA  LEU B   4     9903  14599   9274  -1535   -131   -129       C  
ATOM   3602  C   LEU B   4      -5.876 -25.535   1.862  1.00 97.88           C  
ANISOU 3602  C   LEU B   4    11234  15586  10369  -1580    -48    -43       C  
ATOM   3603  O   LEU B   4      -6.778 -24.886   2.393  1.00 97.44           O  
ANISOU 3603  O   LEU B   4    11020  15676  10327  -1702     15    -61       O  
ATOM   3604  CB  LEU B   4      -5.607 -24.142  -0.203  1.00 71.84           C  
ANISOU 3604  CB  LEU B   4     7412  12709   7174  -1374   -245    -86       C  
ATOM   3605  CG  LEU B   4      -5.290 -24.008  -1.693  1.00 65.60           C  
ANISOU 3605  CG  LEU B   4     6469  12064   6392  -1283   -330   -139       C  
ATOM   3606  CD1 LEU B   4      -5.114 -22.548  -2.072  1.00 61.82           C  
ANISOU 3606  CD1 LEU B   4     5790  11770   5930  -1121   -406    -65       C  
ATOM   3607  CD2 LEU B   4      -4.050 -24.808  -2.053  1.00 62.49           C  
ANISOU 3607  CD2 LEU B   4     6256  11502   5984  -1158   -370   -128       C  
ATOM   3608  N   GLN B   5      -4.990 -26.244   2.553  1.00101.36           N  
ANISOU 3608  N   GLN B   5    12028  15750  10733  -1445    -56     40       N  
ATOM   3609  CA  GLN B   5      -5.023 -26.306   4.010  1.00100.71           C  
ANISOU 3609  CA  GLN B   5    12202  15499  10566  -1447     12    132       C  
ATOM   3610  C   GLN B   5      -4.088 -25.285   4.650  1.00 95.86           C  
ANISOU 3610  C   GLN B   5    11472  14982   9969  -1171   -138    239       C  
ATOM   3611  O   GLN B   5      -2.866 -25.412   4.576  1.00 87.46           O  
ANISOU 3611  O   GLN B   5    10468  13887   8874   -900   -273    270       O  
ATOM   3612  CB  GLN B   5      -4.682 -27.716   4.495  1.00 99.81           C  
ANISOU 3612  CB  GLN B   5    12624  15002  10296  -1430     96    158       C  
ATOM   3613  CG  GLN B   5      -5.893 -28.613   4.674  1.00 98.42           C  
ANISOU 3613  CG  GLN B   5    12697  14651  10046  -1841    353     66       C  
ATOM   3614  CD  GLN B   5      -6.750 -28.194   5.853  1.00 99.87           C  
ANISOU 3614  CD  GLN B   5    12897  14863  10186  -2051    503     92       C  
ATOM   3615  OE1 GLN B   5      -6.250 -28.012   6.964  1.00 96.93           O  
ANISOU 3615  OE1 GLN B   5    12747  14363   9720  -1867    471    227       O  
ATOM   3616  NE2 GLN B   5      -8.046 -28.034   5.617  1.00105.53           N  
ANISOU 3616  NE2 GLN B   5    13353  15789  10953  -2425    661    -62       N  
ATOM   3617  N   GLU B   6      -4.676 -24.274   5.280  1.00 96.52           N  
ANISOU 3617  N   GLU B   6    11376  15208  10088  -1246   -108    264       N  
ATOM   3618  CA  GLU B   6      -3.910 -23.243   5.968  1.00 95.55           C  
ANISOU 3618  CA  GLU B   6    11161  15173   9972  -1050   -220    337       C  
ATOM   3619  C   GLU B   6      -3.768 -23.582   7.446  1.00 96.56           C  
ANISOU 3619  C   GLU B   6    11601  15124   9963  -1003   -184    411       C  
ATOM   3620  O   GLU B   6      -4.654 -24.199   8.036  1.00 97.95           O  
ANISOU 3620  O   GLU B   6    12001  15155  10060  -1198    -20    414       O  
ATOM   3621  CB  GLU B   6      -4.596 -21.887   5.818  1.00 96.60           C  
ANISOU 3621  CB  GLU B   6    10980  15528  10196  -1119   -206    322       C  
ATOM   3622  CG  GLU B   6      -4.818 -21.452   4.383  1.00 99.72           C  
ANISOU 3622  CG  GLU B   6    11114  16097  10678  -1125   -244    264       C  
ATOM   3623  CD  GLU B   6      -5.614 -20.167   4.289  1.00105.89           C  
ANISOU 3623  CD  GLU B   6    11672  17063  11497  -1130   -227    254       C  
ATOM   3624  OE1 GLU B   6      -5.741 -19.622   3.172  1.00109.67           O  
ANISOU 3624  OE1 GLU B   6    11984  17679  12007  -1072   -272    227       O  
ATOM   3625  OE2 GLU B   6      -6.115 -19.703   5.333  1.00107.55           O  
ANISOU 3625  OE2 GLU B   6    11907  17276  11682  -1162   -168    273       O  
ATOM   3626  N   SER B   7      -2.653 -23.170   8.041  1.00 97.65           N  
ANISOU 3626  N   SER B   7    11753  15298  10052   -758   -326    449       N  
ATOM   3627  CA  SER B   7      -2.404 -23.416   9.457  1.00 97.98           C  
ANISOU 3627  CA  SER B   7    12092  15207   9927   -649   -331    515       C  
ATOM   3628  C   SER B   7      -1.292 -22.519   9.988  1.00 89.00           C  
ANISOU 3628  C   SER B   7    10795  14252   8770   -425   -506    498       C  
ATOM   3629  O   SER B   7      -0.363 -22.176   9.260  1.00 83.52           O  
ANISOU 3629  O   SER B   7     9864  13727   8145   -303   -631    427       O  
ATOM   3630  CB  SER B   7      -2.037 -24.883   9.689  1.00 99.54           C  
ANISOU 3630  CB  SER B   7    12747  15125   9948   -507   -323    553       C  
ATOM   3631  OG  SER B   7      -0.868 -25.232   8.967  1.00 97.80           O  
ANISOU 3631  OG  SER B   7    12468  14965   9728   -229   -493    505       O  
ATOM   3632  N   GLY B   8      -1.392 -22.141  11.258  1.00 88.26           N  
ANISOU 3632  N   GLY B   8    10825  14142   8569   -402   -497    537       N  
ATOM   3633  CA  GLY B   8      -0.340 -21.374  11.898  1.00 93.10           C  
ANISOU 3633  CA  GLY B   8    11308  14939   9128   -212   -661    484       C  
ATOM   3634  C   GLY B   8      -0.797 -20.076  12.533  1.00 93.75           C  
ANISOU 3634  C   GLY B   8    11234  15127   9260   -361   -606    472       C  
ATOM   3635  O   GLY B   8      -0.189 -19.605  13.494  1.00100.24           O  
ANISOU 3635  O   GLY B   8    12071  16042   9974   -248   -699    435       O  
ATOM   3636  N   GLY B   9      -1.868 -19.498  12.000  1.00 87.55           N  
ANISOU 3636  N   GLY B   9    10303  14344   8617   -588   -463    485       N  
ATOM   3637  CA  GLY B   9      -2.368 -18.223  12.483  1.00 84.78           C  
ANISOU 3637  CA  GLY B   9     9826  14077   8311   -692   -402    466       C  
ATOM   3638  C   GLY B   9      -2.847 -18.246  13.924  1.00 83.62           C  
ANISOU 3638  C   GLY B   9     9900  13855   8017   -704   -334    506       C  
ATOM   3639  O   GLY B   9      -2.966 -19.308  14.537  1.00 85.39           O  
ANISOU 3639  O   GLY B   9    10419  13933   8094   -666   -299    567       O  
ATOM   3640  N   GLY B  10      -3.119 -17.064  14.465  1.00 78.97           N  
ANISOU 3640  N   GLY B  10     9216  13343   7445   -754   -298    471       N  
ATOM   3641  CA  GLY B  10      -3.613 -16.940  15.823  1.00 81.57           C  
ANISOU 3641  CA  GLY B  10     9733  13627   7633   -774   -220    493       C  
ATOM   3642  C   GLY B  10      -3.263 -15.599  16.436  1.00 78.76           C  
ANISOU 3642  C   GLY B  10     9285  13371   7270   -755   -262    418       C  
ATOM   3643  O   GLY B  10      -2.856 -14.673  15.733  1.00 75.81           O  
ANISOU 3643  O   GLY B  10     8717  13072   7014   -776   -303    352       O  
ATOM   3644  N   LEU B  11      -3.424 -15.495  17.751  1.00 76.35           N  
ANISOU 3644  N   LEU B  11     9162  13044   6804   -734   -230    422       N  
ATOM   3645  CA  LEU B  11      -3.082 -14.274  18.470  1.00 83.32           C  
ANISOU 3645  CA  LEU B  11    10001  14008   7650   -728   -264    329       C  
ATOM   3646  C   LEU B  11      -1.575 -14.197  18.709  1.00 83.58           C  
ANISOU 3646  C   LEU B  11     9991  14167   7600   -610   -474    230       C  
ATOM   3647  O   LEU B  11      -0.917 -15.218  18.913  1.00 61.20           O  
ANISOU 3647  O   LEU B  11     7264  11349   4639   -450   -600    255       O  
ATOM   3648  CB  LEU B  11      -3.837 -14.194  19.801  1.00 93.95           C  
ANISOU 3648  CB  LEU B  11    11550  15310   8835   -749   -147    351       C  
ATOM   3649  CG  LEU B  11      -5.338 -13.885  19.785  1.00102.06           C  
ANISOU 3649  CG  LEU B  11    12540  16314   9924   -874     76    368       C  
ATOM   3650  CD1 LEU B  11      -6.167 -15.079  19.326  1.00104.57           C  
ANISOU 3650  CD1 LEU B  11    12902  16572  10258   -974    203    442       C  
ATOM   3651  CD2 LEU B  11      -5.794 -13.412  21.158  1.00105.32           C  
ANISOU 3651  CD2 LEU B  11    13110  16733  10175   -883    173    336       C  
ATOM   3652  N   VAL B  12      -1.033 -12.984  18.681  1.00 81.78           N  
ANISOU 3652  N   VAL B  12     9615  14036   7422   -687   -504     96       N  
ATOM   3653  CA  VAL B  12       0.404 -12.783  18.834  1.00 82.20           C  
ANISOU 3653  CA  VAL B  12     9541  14287   7404   -639   -684    -69       C  
ATOM   3654  C   VAL B  12       0.712 -11.371  19.336  1.00 80.26           C  
ANISOU 3654  C   VAL B  12     9244  14107   7144   -793   -651   -237       C  
ATOM   3655  O   VAL B  12       0.077 -10.402  18.918  1.00 85.76           O  
ANISOU 3655  O   VAL B  12     9953  14671   7959   -941   -494   -228       O  
ATOM   3656  CB  VAL B  12       1.147 -13.056  17.501  1.00 84.20           C  
ANISOU 3656  CB  VAL B  12     9576  14624   7792   -652   -747   -110       C  
ATOM   3657  CG1 VAL B  12       0.551 -12.225  16.374  1.00 84.00           C  
ANISOU 3657  CG1 VAL B  12     9470  14481   7966   -837   -586    -76       C  
ATOM   3658  CG2 VAL B  12       2.641 -12.796  17.643  1.00 91.22           C  
ANISOU 3658  CG2 VAL B  12    10259  15798   8602   -633   -914   -340       C  
ATOM   3659  N   GLN B  13       1.675 -11.262  20.246  1.00 70.49           N  
ANISOU 3659  N   GLN B  13     7974  13074   5735   -739   -801   -405       N  
ATOM   3660  CA  GLN B  13       2.060  -9.968  20.797  1.00 72.46           C  
ANISOU 3660  CA  GLN B  13     8188  13399   5946   -924   -767   -608       C  
ATOM   3661  C   GLN B  13       2.797  -9.128  19.759  1.00 76.73           C  
ANISOU 3661  C   GLN B  13     8525  14001   6628  -1169   -712   -770       C  
ATOM   3662  O   GLN B  13       3.236  -9.643  18.730  1.00 82.39           O  
ANISOU 3662  O   GLN B  13     9079  14782   7442  -1156   -749   -753       O  
ATOM   3663  CB  GLN B  13       2.929 -10.151  22.043  1.00 77.28           C  
ANISOU 3663  CB  GLN B  13     8786  14273   6305   -798   -964   -782       C  
ATOM   3664  N   ALA B  14       2.930  -7.834  20.033  1.00 78.24           N  
ANISOU 3664  N   ALA B  14     8765  14150   6813  -1411   -599   -934       N  
ATOM   3665  CA  ALA B  14       3.611  -6.927  19.116  1.00 83.70           C  
ANISOU 3665  CA  ALA B  14     9353  14847   7603  -1711   -486  -1100       C  
ATOM   3666  C   ALA B  14       5.112  -7.192  19.092  1.00 87.55           C  
ANISOU 3666  C   ALA B  14     9510  15739   8014  -1796   -644  -1383       C  
ATOM   3667  O   ALA B  14       5.781  -7.127  20.123  1.00 96.35           O  
ANISOU 3667  O   ALA B  14    10524  17125   8959  -1787   -782  -1604       O  
ATOM   3668  CB  ALA B  14       3.333  -5.481  19.493  1.00 88.33           C  
ANISOU 3668  CB  ALA B  14    10167  15229   8167  -1956   -296  -1209       C  
ATOM   3669  N   GLY B  15       5.636  -7.490  17.908  1.00 79.11           N  
ANISOU 3669  N   GLY B  15     8252  14750   7054  -1863   -628  -1399       N  
ATOM   3670  CA  GLY B  15       7.049  -7.777  17.751  1.00 78.97           C  
ANISOU 3670  CA  GLY B  15     7863  15173   6970  -1929   -764  -1696       C  
ATOM   3671  C   GLY B  15       7.338  -9.265  17.775  1.00 78.63           C  
ANISOU 3671  C   GLY B  15     7658  15351   6866  -1514  -1017  -1615       C  
ATOM   3672  O   GLY B  15       8.474  -9.689  17.559  1.00 78.78           O  
ANISOU 3672  O   GLY B  15     7341  15772   6820  -1461  -1161  -1849       O  
ATOM   3673  N   GLY B  16       6.305 -10.060  18.037  1.00 77.23           N  
ANISOU 3673  N   GLY B  16     7736  14916   6692  -1219  -1054  -1301       N  
ATOM   3674  CA  GLY B  16       6.444 -11.503  18.093  1.00 79.68           C  
ANISOU 3674  CA  GLY B  16     8030  15326   6917   -821  -1256  -1187       C  
ATOM   3675  C   GLY B  16       6.519 -12.133  16.716  1.00 86.10           C  
ANISOU 3675  C   GLY B  16     8737  16094   7884   -788  -1221  -1092       C  
ATOM   3676  O   GLY B  16       6.250 -11.480  15.708  1.00 88.97           O  
ANISOU 3676  O   GLY B  16     9081  16302   8420  -1058  -1029  -1057       O  
ATOM   3677  N   SER B  17       6.883 -13.411  16.674  1.00 89.49           N  
ANISOU 3677  N   SER B  17     9141  16641   8221   -433  -1404  -1048       N  
ATOM   3678  CA  SER B  17       7.012 -14.124  15.408  1.00 89.03           C  
ANISOU 3678  CA  SER B  17     8989  16555   8283   -365  -1388   -977       C  
ATOM   3679  C   SER B  17       5.889 -15.137  15.208  1.00 86.12           C  
ANISOU 3679  C   SER B  17     8949  15819   7952   -182  -1345   -654       C  
ATOM   3680  O   SER B  17       5.371 -15.707  16.168  1.00 91.91           O  
ANISOU 3680  O   SER B  17     9962  16414   8545     15  -1399   -521       O  
ATOM   3681  CB  SER B  17       8.373 -14.819  15.318  1.00 90.14           C  
ANISOU 3681  CB  SER B  17     8831  17130   8290    -99  -1613  -1221       C  
ATOM   3682  OG  SER B  17       9.430 -13.874  15.339  1.00 88.87           O  
ANISOU 3682  OG  SER B  17     8292  17367   8106   -351  -1617  -1576       O  
ATOM   3683  N   LEU B  18       5.520 -15.355  13.950  1.00 79.91           N  
ANISOU 3683  N   LEU B  18     8138  14887   7338   -276  -1232   -547       N  
ATOM   3684  CA  LEU B  18       4.443 -16.273  13.609  1.00 80.25           C  
ANISOU 3684  CA  LEU B  18     8447  14613   7430   -181  -1164   -291       C  
ATOM   3685  C   LEU B  18       4.788 -16.979  12.301  1.00 80.38           C  
ANISOU 3685  C   LEU B  18     8347  14657   7536   -119  -1174   -292       C  
ATOM   3686  O   LEU B  18       5.424 -16.394  11.427  1.00 76.64           O  
ANISOU 3686  O   LEU B  18     7608  14354   7156   -274  -1136   -429       O  
ATOM   3687  CB  LEU B  18       3.124 -15.505  13.481  1.00 78.61           C  
ANISOU 3687  CB  LEU B  18     8366  14148   7355   -432   -957   -142       C  
ATOM   3688  CG  LEU B  18       1.802 -16.238  13.722  1.00 77.71           C  
ANISOU 3688  CG  LEU B  18     8530  13761   7236   -393   -865     71       C  
ATOM   3689  CD1 LEU B  18       0.726 -15.245  14.129  1.00 73.50           C  
ANISOU 3689  CD1 LEU B  18     8063  13108   6757   -577   -708    128       C  
ATOM   3690  CD2 LEU B  18       1.363 -17.010  12.488  1.00 81.47           C  
ANISOU 3690  CD2 LEU B  18     9003  14125   7825   -402   -809    162       C  
ATOM   3691  N   ARG B  19       4.378 -18.236  12.173  1.00 84.56           N  
ANISOU 3691  N   ARG B  19     9107  15004   8019     87  -1203   -150       N  
ATOM   3692  CA  ARG B  19       4.671 -19.011  10.972  1.00 81.91           C  
ANISOU 3692  CA  ARG B  19     8703  14671   7749    171  -1216   -155       C  
ATOM   3693  C   ARG B  19       3.401 -19.538  10.311  1.00 76.50           C  
ANISOU 3693  C   ARG B  19     8227  13670   7170     49  -1064     38       C  
ATOM   3694  O   ARG B  19       2.715 -20.397  10.864  1.00 80.23           O  
ANISOU 3694  O   ARG B  19     9020  13911   7552    132  -1036    167       O  
ATOM   3695  CB  ARG B  19       5.601 -20.179  11.304  1.00 86.29           C  
ANISOU 3695  CB  ARG B  19     9339  15337   8110    585  -1415   -228       C  
ATOM   3696  CG  ARG B  19       6.088 -20.951  10.089  1.00 90.96           C  
ANISOU 3696  CG  ARG B  19     9837  15974   8749    713  -1442   -278       C  
ATOM   3697  CD  ARG B  19       6.834 -22.210  10.500  1.00100.17           C  
ANISOU 3697  CD  ARG B  19    11195  17177   9688   1202  -1636   -322       C  
ATOM   3698  NE  ARG B  19       7.847 -21.935  11.515  1.00109.81           N  
ANISOU 3698  NE  ARG B  19    12262  18745  10717   1459  -1839   -505       N  
ATOM   3699  CZ  ARG B  19       9.096 -21.573  11.245  1.00114.06           C  
ANISOU 3699  CZ  ARG B  19    12353  19758  11227   1560  -1969   -792       C  
ATOM   3700  NH1 ARG B  19       9.493 -21.440   9.987  1.00115.53           N  
ANISOU 3700  NH1 ARG B  19    12237  20094  11566   1415  -1895   -903       N  
ATOM   3701  NH2 ARG B  19       9.950 -21.343  12.234  1.00114.77           N  
ANISOU 3701  NH2 ARG B  19    12283  20205  11119   1792  -2167   -990       N  
ATOM   3702  N   LEU B  20       3.091 -19.018   9.128  1.00 69.31           N  
ANISOU 3702  N   LEU B  20     7146  12764   6427   -162   -955     40       N  
ATOM   3703  CA  LEU B  20       1.955 -19.509   8.356  1.00 68.76           C  
ANISOU 3703  CA  LEU B  20     7198  12482   6447   -269   -836    168       C  
ATOM   3704  C   LEU B  20       2.375 -20.687   7.485  1.00 73.08           C  
ANISOU 3704  C   LEU B  20     7785  13002   6978   -118   -887    146       C  
ATOM   3705  O   LEU B  20       3.559 -20.859   7.189  1.00 75.80           O  
ANISOU 3705  O   LEU B  20     7979  13538   7282     49   -998     20       O  
ATOM   3706  CB  LEU B  20       1.359 -18.394   7.494  1.00 66.84           C  
ANISOU 3706  CB  LEU B  20     6793  12259   6345   -503   -714    182       C  
ATOM   3707  CG  LEU B  20       0.689 -17.237   8.236  1.00 68.45           C  
ANISOU 3707  CG  LEU B  20     7018  12429   6561   -636   -634    217       C  
ATOM   3708  CD1 LEU B  20       0.068 -16.253   7.255  1.00 63.06           C  
ANISOU 3708  CD1 LEU B  20     6252  11732   5975   -777   -524    242       C  
ATOM   3709  CD2 LEU B  20      -0.357 -17.758   9.208  1.00 75.29           C  
ANISOU 3709  CD2 LEU B  20     8093  13145   7370   -628   -586    313       C  
ATOM   3710  N   SER B  21       1.403 -21.495   7.076  1.00 71.59           N  
ANISOU 3710  N   SER B  21     7787  12601   6814   -186   -797    238       N  
ATOM   3711  CA  SER B  21       1.681 -22.684   6.279  1.00 72.73           C  
ANISOU 3711  CA  SER B  21     8041  12664   6931    -58   -824    216       C  
ATOM   3712  C   SER B  21       0.472 -23.082   5.441  1.00 78.92           C  
ANISOU 3712  C   SER B  21     8890  13297   7798   -279   -686    265       C  
ATOM   3713  O   SER B  21      -0.650 -23.132   5.943  1.00 88.20           O  
ANISOU 3713  O   SER B  21    10198  14342   8971   -454   -572    330       O  
ATOM   3714  CB  SER B  21       2.091 -23.848   7.183  1.00 77.03           C  
ANISOU 3714  CB  SER B  21     8942  13044   7281    219   -903    242       C  
ATOM   3715  OG  SER B  21       2.321 -25.021   6.425  1.00 84.85           O  
ANISOU 3715  OG  SER B  21    10107  13904   8228    361   -914    218       O  
ATOM   3716  N   CYS B  22       0.706 -23.367   4.165  1.00 80.43           N  
ANISOU 3716  N   CYS B  22     8965  13546   8050   -278   -692    206       N  
ATOM   3717  CA  CYS B  22      -0.367 -23.775   3.263  1.00 83.17           C  
ANISOU 3717  CA  CYS B  22     9335  13807   8458   -476   -584    209       C  
ATOM   3718  C   CYS B  22      -0.013 -25.034   2.479  1.00 78.57           C  
ANISOU 3718  C   CYS B  22     8913  13109   7829   -376   -598    151       C  
ATOM   3719  O   CYS B  22       0.956 -25.052   1.724  1.00 79.06           O  
ANISOU 3719  O   CYS B  22     8837  13303   7900   -220   -678     80       O  
ATOM   3720  CB  CYS B  22      -0.717 -22.647   2.292  1.00 85.04           C  
ANISOU 3720  CB  CYS B  22     9267  14239   8804   -610   -559    191       C  
ATOM   3721  SG  CYS B  22      -2.053 -23.057   1.146  1.00149.94           S  
ANISOU 3721  SG  CYS B  22    17447  22459  17066   -810   -470    151       S  
ATOM   3722  N   ALA B  23      -0.809 -26.082   2.655  1.00 78.92           N  
ANISOU 3722  N   ALA B  23     9266  12907   7814   -491   -496    163       N  
ATOM   3723  CA  ALA B  23      -0.593 -27.333   1.940  1.00 85.69           C  
ANISOU 3723  CA  ALA B  23    10357  13591   8610   -423   -480     99       C  
ATOM   3724  C   ALA B  23      -1.596 -27.478   0.800  1.00 90.74           C  
ANISOU 3724  C   ALA B  23    10874  14273   9329   -711   -380     19       C  
ATOM   3725  O   ALA B  23      -2.804 -27.359   1.008  1.00 91.93           O  
ANISOU 3725  O   ALA B  23    11003  14421   9505   -998   -261      9       O  
ATOM   3726  CB  ALA B  23      -0.688 -28.512   2.891  1.00 89.03           C  
ANISOU 3726  CB  ALA B  23    11309  13654   8866   -357   -411    148       C  
ATOM   3727  N   ALA B  24      -1.090 -27.741  -0.401  1.00 89.99           N  
ANISOU 3727  N   ALA B  24    10676  14260   9256   -624   -431    -63       N  
ATOM   3728  CA  ALA B  24      -1.939 -27.876  -1.579  1.00 88.14           C  
ANISOU 3728  CA  ALA B  24    10307  14110   9070   -856   -368   -162       C  
ATOM   3729  C   ALA B  24      -2.269 -29.335  -1.872  1.00 94.14           C  
ANISOU 3729  C   ALA B  24    11432  14592   9746   -965   -266   -256       C  
ATOM   3730  O   ALA B  24      -1.441 -30.075  -2.402  1.00 96.67           O  
ANISOU 3730  O   ALA B  24    11916  14804  10010   -761   -310   -304       O  
ATOM   3731  CB  ALA B  24      -1.278 -27.229  -2.785  1.00 86.65           C  
ANISOU 3731  CB  ALA B  24     9812  14177   8933   -734   -460   -202       C  
ATOM   3732  N   SER B  25      -3.485 -29.742  -1.526  1.00101.52           N  
ANISOU 3732  N   SER B  25    12497  15417  10660  -1302   -112   -306       N  
ATOM   3733  CA  SER B  25      -3.929 -31.110  -1.758  1.00108.07           C  
ANISOU 3733  CA  SER B  25    13718  15950  11394  -1508     38   -422       C  
ATOM   3734  C   SER B  25      -4.609 -31.238  -3.116  1.00113.57           C  
ANISOU 3734  C   SER B  25    14171  16849  12133  -1740     60   -608       C  
ATOM   3735  O   SER B  25      -5.741 -30.791  -3.298  1.00123.01           O  
ANISOU 3735  O   SER B  25    15077  18291  13372  -2032    115   -707       O  
ATOM   3736  CB  SER B  25      -4.883 -31.557  -0.648  1.00107.55           C  
ANISOU 3736  CB  SER B  25    13951  15660  11255  -1826    242   -418       C  
ATOM   3737  N   GLY B  26      -3.912 -31.847  -4.069  1.00107.04           N  
ANISOU 3737  N   GLY B  26    13445  15951  11272  -1581      7   -677       N  
ATOM   3738  CA  GLY B  26      -4.457 -32.042  -5.400  1.00103.92           C  
ANISOU 3738  CA  GLY B  26    12853  15744  10887  -1771     14   -865       C  
ATOM   3739  C   GLY B  26      -3.410 -31.904  -6.487  1.00101.03           C  
ANISOU 3739  C   GLY B  26    12356  15503  10528  -1457   -128   -871       C  
ATOM   3740  O   GLY B  26      -2.222 -31.751  -6.201  1.00106.35           O  
ANISOU 3740  O   GLY B  26    13087  16121  11199  -1104   -219   -756       O  
ATOM   3741  N   SER B  27      -3.851 -31.954  -7.740  1.00 94.12           N  
ANISOU 3741  N   SER B  27    11283  14835   9644  -1588   -143  -1030       N  
ATOM   3742  CA  SER B  27      -2.938 -31.870  -8.874  1.00 95.11           C  
ANISOU 3742  CA  SER B  27    11297  15089   9752  -1333   -246  -1057       C  
ATOM   3743  C   SER B  27      -2.827 -30.447  -9.418  1.00 89.46           C  
ANISOU 3743  C   SER B  27    10140  14765   9086  -1216   -364   -974       C  
ATOM   3744  O   SER B  27      -3.788 -29.898  -9.957  1.00 88.30           O  
ANISOU 3744  O   SER B  27     9739  14881   8931  -1378   -386  -1040       O  
ATOM   3745  CB  SER B  27      -3.371 -32.828  -9.986  1.00102.44           C  
ANISOU 3745  CB  SER B  27    12338  15983  10602  -1518   -189  -1285       C  
ATOM   3746  OG  SER B  27      -4.661 -32.500 -10.469  1.00109.22           O  
ANISOU 3746  OG  SER B  27    12916  17125  11456  -1836   -177  -1426       O  
ATOM   3747  N   ILE B  28      -1.643 -29.861  -9.273  1.00 84.59           N  
ANISOU 3747  N   ILE B  28     9454  14191   8495   -927   -432   -848       N  
ATOM   3748  CA  ILE B  28      -1.373 -28.518  -9.771  1.00 79.39           C  
ANISOU 3748  CA  ILE B  28     8478  13832   7857   -833   -499   -763       C  
ATOM   3749  C   ILE B  28      -0.299 -28.570 -10.857  1.00 80.88           C  
ANISOU 3749  C   ILE B  28     8616  14126   7990   -649   -520   -817       C  
ATOM   3750  O   ILE B  28       0.637 -29.366 -10.771  1.00 83.85           O  
ANISOU 3750  O   ILE B  28     9148  14366   8346   -476   -514   -868       O  
ATOM   3751  CB  ILE B  28      -0.913 -27.583  -8.631  1.00 72.19           C  
ANISOU 3751  CB  ILE B  28     7492  12925   7013   -735   -519   -597       C  
ATOM   3752  CG1 ILE B  28      -1.919 -27.613  -7.478  1.00 77.44           C  
ANISOU 3752  CG1 ILE B  28     8233  13473   7719   -906   -481   -550       C  
ATOM   3753  CG2 ILE B  28      -0.726 -26.158  -9.131  1.00 63.85           C  
ANISOU 3753  CG2 ILE B  28     6188  12117   5954   -692   -546   -515       C  
ATOM   3754  CD1 ILE B  28      -1.591 -26.647  -6.362  1.00 78.21           C  
ANISOU 3754  CD1 ILE B  28     8260  13587   7871   -826   -502   -400       C  
ATOM   3755  N   PHE B  29      -0.448 -27.732 -11.881  1.00 77.47           N  
ANISOU 3755  N   PHE B  29     7988  13941   7507   -663   -539   -814       N  
ATOM   3756  CA  PHE B  29       0.523 -27.653 -12.970  1.00 74.44           C  
ANISOU 3756  CA  PHE B  29     7548  13687   7047   -529   -525   -866       C  
ATOM   3757  C   PHE B  29       1.901 -27.273 -12.438  1.00 76.55           C  
ANISOU 3757  C   PHE B  29     7755  13977   7354   -361   -504   -813       C  
ATOM   3758  O   PHE B  29       2.014 -26.537 -11.458  1.00 85.15           O  
ANISOU 3758  O   PHE B  29     8783  15060   8511   -368   -509   -700       O  
ATOM   3759  CB  PHE B  29       0.061 -26.647 -14.029  1.00 76.46           C  
ANISOU 3759  CB  PHE B  29     7666  14181   7205   -570   -534   -835       C  
ATOM   3760  CG  PHE B  29       0.948 -26.587 -15.244  1.00 80.91           C  
ANISOU 3760  CG  PHE B  29     8206  14878   7656   -477   -488   -896       C  
ATOM   3761  CD1 PHE B  29       1.095 -27.691 -16.068  1.00 79.76           C  
ANISOU 3761  CD1 PHE B  29     8144  14713   7446   -449   -486  -1064       C  
ATOM   3762  CD2 PHE B  29       1.620 -25.420 -15.571  1.00 79.65           C  
ANISOU 3762  CD2 PHE B  29     7972  14853   7440   -445   -421   -799       C  
ATOM   3763  CE1 PHE B  29       1.907 -27.637 -17.187  1.00 73.87           C  
ANISOU 3763  CE1 PHE B  29     7373  14110   6586   -364   -429  -1133       C  
ATOM   3764  CE2 PHE B  29       2.432 -25.359 -16.692  1.00 72.79           C  
ANISOU 3764  CE2 PHE B  29     7094  14117   6448   -399   -340   -867       C  
ATOM   3765  CZ  PHE B  29       2.575 -26.469 -17.500  1.00 68.07           C  
ANISOU 3765  CZ  PHE B  29     6544  13529   5790   -346   -351  -1033       C  
ATOM   3766  N   ALA B  30       2.941 -27.780 -13.091  1.00 70.75           N  
ANISOU 3766  N   ALA B  30     7014  13304   6563   -212   -478   -927       N  
ATOM   3767  CA  ALA B  30       4.313 -27.618 -12.617  1.00 71.90           C  
ANISOU 3767  CA  ALA B  30     7049  13544   6725    -33   -465   -956       C  
ATOM   3768  C   ALA B  30       4.768 -26.161 -12.537  1.00 75.64           C  
ANISOU 3768  C   ALA B  30     7310  14222   7207   -132   -403   -873       C  
ATOM   3769  O   ALA B  30       5.659 -25.825 -11.757  1.00 83.11           O  
ANISOU 3769  O   ALA B  30     8132  15257   8190    -60   -400   -891       O  
ATOM   3770  CB  ALA B  30       5.264 -28.425 -13.482  1.00 72.70           C  
ANISOU 3770  CB  ALA B  30     7146  13734   6743    152   -440  -1134       C  
ATOM   3771  N   LEU B  31       4.159 -25.302 -13.347  1.00 71.36           N  
ANISOU 3771  N   LEU B  31     6755  13754   6606   -290   -349   -797       N  
ATOM   3772  CA  LEU B  31       4.482 -23.879 -13.334  1.00 67.56           C  
ANISOU 3772  CA  LEU B  31     6184  13389   6098   -410   -254   -705       C  
ATOM   3773  C   LEU B  31       3.380 -23.093 -12.633  1.00 66.65           C  
ANISOU 3773  C   LEU B  31     6140  13157   6028   -501   -297   -538       C  
ATOM   3774  O   LEU B  31       2.277 -22.954 -13.160  1.00 71.86           O  
ANISOU 3774  O   LEU B  31     6881  13794   6629   -528   -336   -482       O  
ATOM   3775  CB  LEU B  31       4.681 -23.364 -14.761  1.00 68.41           C  
ANISOU 3775  CB  LEU B  31     6310  13635   6048   -477   -139   -725       C  
ATOM   3776  CG  LEU B  31       5.884 -23.944 -15.508  1.00 73.16           C  
ANISOU 3776  CG  LEU B  31     6804  14408   6586   -409    -55   -910       C  
ATOM   3777  CD1 LEU B  31       5.703 -23.822 -17.012  1.00 74.77           C  
ANISOU 3777  CD1 LEU B  31     7101  14697   6613   -451     26   -929       C  
ATOM   3778  CD2 LEU B  31       7.161 -23.250 -15.068  1.00 76.24           C  
ANISOU 3778  CD2 LEU B  31     7004  14976   6988   -484     72   -983       C  
ATOM   3779  N   ASN B  32       3.684 -22.584 -11.444  1.00 65.85           N  
ANISOU 3779  N   ASN B  32     5990  13017   6015   -526   -297   -483       N  
ATOM   3780  CA  ASN B  32       2.682 -21.913 -10.624  1.00 69.69           C  
ANISOU 3780  CA  ASN B  32     6539  13389   6550   -586   -336   -343       C  
ATOM   3781  C   ASN B  32       3.262 -20.879  -9.662  1.00 74.10           C  
ANISOU 3781  C   ASN B  32     7052  13952   7151   -659   -278   -289       C  
ATOM   3782  O   ASN B  32       4.467 -20.852  -9.414  1.00 81.82           O  
ANISOU 3782  O   ASN B  32     7906  15041   8140   -667   -229   -389       O  
ATOM   3783  CB  ASN B  32       1.868 -22.944  -9.838  1.00 66.49           C  
ANISOU 3783  CB  ASN B  32     6191  12843   6229   -542   -444   -349       C  
ATOM   3784  CG  ASN B  32       2.732 -23.803  -8.938  1.00 71.38           C  
ANISOU 3784  CG  ASN B  32     6811  13401   6910   -431   -483   -420       C  
ATOM   3785  OD1 ASN B  32       3.072 -23.409  -7.823  1.00 73.25           O  
ANISOU 3785  OD1 ASN B  32     7018  13617   7197   -417   -498   -377       O  
ATOM   3786  ND2 ASN B  32       3.095 -24.986  -9.420  1.00 75.12           N  
ANISOU 3786  ND2 ASN B  32     7344  13845   7354   -318   -507   -536       N  
ATOM   3787  N   ILE B  33       2.392 -20.029  -9.122  1.00 68.83           N  
ANISOU 3787  N   ILE B  33     6466  13191   6495   -708   -283   -160       N  
ATOM   3788  CA  ILE B  33       2.797 -19.038  -8.128  1.00 67.37           C  
ANISOU 3788  CA  ILE B  33     6275  12975   6346   -792   -228   -114       C  
ATOM   3789  C   ILE B  33       2.011 -19.225  -6.836  1.00 73.74           C  
ANISOU 3789  C   ILE B  33     7102  13670   7248   -752   -324    -51       C  
ATOM   3790  O   ILE B  33       0.838 -18.865  -6.756  1.00 78.29           O  
ANISOU 3790  O   ILE B  33     7757  14179   7812   -738   -351     40       O  
ATOM   3791  CB  ILE B  33       2.554 -17.602  -8.620  1.00 68.15           C  
ANISOU 3791  CB  ILE B  33     6533  13026   6334   -886   -103    -11       C  
ATOM   3792  CG1 ILE B  33       3.256 -17.356  -9.954  1.00 69.25           C  
ANISOU 3792  CG1 ILE B  33     6721  13253   6340   -957     32    -59       C  
ATOM   3793  CG2 ILE B  33       3.022 -16.595  -7.580  1.00 67.99           C  
ANISOU 3793  CG2 ILE B  33     6537  12951   6346  -1013    -23      6       C  
ATOM   3794  CD1 ILE B  33       3.010 -15.972 -10.502  1.00 72.73           C  
ANISOU 3794  CD1 ILE B  33     7434  13582   6618  -1032    180     61       C  
ATOM   3795  N   MET B  34       2.660 -19.780  -5.821  1.00 77.92           N  
ANISOU 3795  N   MET B  34     7559  14202   7846   -711   -377   -112       N  
ATOM   3796  CA  MET B  34       1.992 -20.022  -4.551  1.00 76.01           C  
ANISOU 3796  CA  MET B  34     7374  13841   7666   -679   -448    -52       C  
ATOM   3797  C   MET B  34       2.369 -18.941  -3.545  1.00 73.88           C  
ANISOU 3797  C   MET B  34     7086  13576   7410   -751   -412    -24       C  
ATOM   3798  O   MET B  34       3.542 -18.765  -3.229  1.00 76.18           O  
ANISOU 3798  O   MET B  34     7266  13985   7693   -766   -399   -124       O  
ATOM   3799  CB  MET B  34       2.360 -21.407  -4.018  1.00 70.20           C  
ANISOU 3799  CB  MET B  34     6666  13058   6949   -545   -536   -121       C  
ATOM   3800  CG  MET B  34       1.383 -21.958  -2.999  1.00 70.08           C  
ANISOU 3800  CG  MET B  34     6797  12870   6961   -544   -574    -52       C  
ATOM   3801  SD  MET B  34       1.624 -23.720  -2.716  1.00 96.37           S  
ANISOU 3801  SD  MET B  34    10319  16043  10252   -390   -633   -116       S  
ATOM   3802  CE  MET B  34       0.319 -24.045  -1.532  1.00160.68           C  
ANISOU 3802  CE  MET B  34    18672  23976  18405   -507   -599    -25       C  
ATOM   3803  N   GLY B  35       1.375 -18.211  -3.047  1.00 69.46           N  
ANISOU 3803  N   GLY B  35     6615  12917   6859   -793   -395     81       N  
ATOM   3804  CA  GLY B  35       1.647 -17.106  -2.145  1.00 65.05           C  
ANISOU 3804  CA  GLY B  35     6081  12334   6301   -873   -345    103       C  
ATOM   3805  C   GLY B  35       0.566 -16.802  -1.128  1.00 65.82           C  
ANISOU 3805  C   GLY B  35     6263  12321   6423   -852   -369    191       C  
ATOM   3806  O   GLY B  35      -0.389 -17.559  -0.970  1.00 67.50           O  
ANISOU 3806  O   GLY B  35     6491  12496   6658   -797   -420    221       O  
ATOM   3807  N   TRP B  36       0.729 -15.680  -0.434  1.00 69.82           N  
ANISOU 3807  N   TRP B  36     6828  12786   6915   -923   -309    209       N  
ATOM   3808  CA  TRP B  36      -0.200 -15.245   0.600  1.00 71.83           C  
ANISOU 3808  CA  TRP B  36     7161  12950   7180   -897   -315    276       C  
ATOM   3809  C   TRP B  36      -0.658 -13.812   0.351  1.00 76.21           C  
ANISOU 3809  C   TRP B  36     7871  13416   7671   -912   -217    339       C  
ATOM   3810  O   TRP B  36       0.156 -12.935   0.023  1.00 85.09           O  
ANISOU 3810  O   TRP B  36     9082  14504   8745  -1028   -114    312       O  
ATOM   3811  CB  TRP B  36       0.456 -15.319   1.982  1.00 72.06           C  
ANISOU 3811  CB  TRP B  36     7164  12990   7227   -927   -353    224       C  
ATOM   3812  CG  TRP B  36       0.780 -16.705   2.457  1.00 71.30           C  
ANISOU 3812  CG  TRP B  36     7016  12931   7145   -834   -458    186       C  
ATOM   3813  CD1 TRP B  36       1.940 -17.394   2.249  1.00 72.30           C  
ANISOU 3813  CD1 TRP B  36     7045  13170   7257   -775   -520     85       C  
ATOM   3814  CD2 TRP B  36      -0.060 -17.560   3.239  1.00 66.11           C  
ANISOU 3814  CD2 TRP B  36     6448  12183   6488   -774   -497    240       C  
ATOM   3815  NE1 TRP B  36       1.871 -18.629   2.846  1.00 65.61           N  
ANISOU 3815  NE1 TRP B  36     6270  12271   6387   -633   -611     92       N  
ATOM   3816  CE2 TRP B  36       0.653 -18.756   3.461  1.00 65.49           C  
ANISOU 3816  CE2 TRP B  36     6394  12110   6378   -664   -580    192       C  
ATOM   3817  CE3 TRP B  36      -1.347 -17.433   3.770  1.00 69.14           C  
ANISOU 3817  CE3 TRP B  36     6904  12491   6876   -805   -452    307       C  
ATOM   3818  CZ2 TRP B  36       0.122 -19.818   4.191  1.00 70.07           C  
ANISOU 3818  CZ2 TRP B  36     7147  12558   6919   -607   -599    235       C  
ATOM   3819  CZ3 TRP B  36      -1.873 -18.489   4.494  1.00 77.77           C  
ANISOU 3819  CZ3 TRP B  36     8102  13501   7945   -798   -457    324       C  
ATOM   3820  CH2 TRP B  36      -1.140 -19.665   4.697  1.00 77.29           C  
ANISOU 3820  CH2 TRP B  36     8141  13385   7841   -712   -520    301       C  
ATOM   3821  N   TYR B  37      -1.961 -13.591   0.512  1.00 70.58           N  
ANISOU 3821  N   TYR B  37     7207  12670   6938   -795   -234    404       N  
ATOM   3822  CA  TYR B  37      -2.563 -12.262   0.451  1.00 74.66           C  
ANISOU 3822  CA  TYR B  37     7915  13085   7366   -713   -162    466       C  
ATOM   3823  C   TYR B  37      -3.173 -11.945   1.814  1.00 77.48           C  
ANISOU 3823  C   TYR B  37     8287  13405   7747   -682   -165    469       C  
ATOM   3824  O   TYR B  37      -3.217 -12.811   2.686  1.00 80.87           O  
ANISOU 3824  O   TYR B  37     8588  13891   8249   -730   -219    436       O  
ATOM   3825  CB  TYR B  37      -3.659 -12.218  -0.617  1.00 80.14           C  
ANISOU 3825  CB  TYR B  37     8626  13847   7977   -514   -201    507       C  
ATOM   3826  CG  TYR B  37      -3.172 -12.400  -2.039  1.00 78.91           C  
ANISOU 3826  CG  TYR B  37     8503  13721   7757   -516   -190    514       C  
ATOM   3827  CD1 TYR B  37      -2.824 -13.655  -2.523  1.00 73.51           C  
ANISOU 3827  CD1 TYR B  37     7629  13158   7144   -587   -253    452       C  
ATOM   3828  CD2 TYR B  37      -3.084 -11.319  -2.906  1.00 77.92           C  
ANISOU 3828  CD2 TYR B  37     8652  13481   7474   -437   -102    583       C  
ATOM   3829  CE1 TYR B  37      -2.386 -13.825  -3.822  1.00 70.84           C  
ANISOU 3829  CE1 TYR B  37     7321  12860   6737   -586   -235    447       C  
ATOM   3830  CE2 TYR B  37      -2.647 -11.478  -4.207  1.00 79.86           C  
ANISOU 3830  CE2 TYR B  37     8956  13753   7634   -446    -74    592       C  
ATOM   3831  CZ  TYR B  37      -2.300 -12.734  -4.660  1.00 79.84           C  
ANISOU 3831  CZ  TYR B  37     8710  13908   7719   -524   -145    517       C  
ATOM   3832  OH  TYR B  37      -1.865 -12.899  -5.955  1.00 87.40           O  
ANISOU 3832  OH  TYR B  37     9722  14904   8581   -530   -111    514       O  
ATOM   3833  N   ARG B  38      -3.648 -10.717   2.005  1.00 74.30           N  
ANISOU 3833  N   ARG B  38     8084  12886   7259   -586    -97    510       N  
ATOM   3834  CA  ARG B  38      -4.275 -10.352   3.276  1.00 73.27           C  
ANISOU 3834  CA  ARG B  38     7974  12730   7137   -538    -89    500       C  
ATOM   3835  C   ARG B  38      -5.326  -9.253   3.153  1.00 76.45           C  
ANISOU 3835  C   ARG B  38     8557  13070   7420   -291    -53    539       C  
ATOM   3836  O   ARG B  38      -5.249  -8.400   2.269  1.00 77.92           O  
ANISOU 3836  O   ARG B  38     8986  13130   7488   -183      0    593       O  
ATOM   3837  CB  ARG B  38      -3.223  -9.942   4.311  1.00 73.40           C  
ANISOU 3837  CB  ARG B  38     8067  12645   7178   -733    -35    454       C  
ATOM   3838  CG  ARG B  38      -2.633  -8.556   4.095  1.00 78.64           C  
ANISOU 3838  CG  ARG B  38     9024  13108   7748   -812    100    453       C  
ATOM   3839  CD  ARG B  38      -1.598  -8.232   5.160  1.00 84.38           C  
ANISOU 3839  CD  ARG B  38     9762  13803   8496  -1049    147    350       C  
ATOM   3840  NE  ARG B  38      -0.947  -6.947   4.923  1.00 92.25           N  
ANISOU 3840  NE  ARG B  38    11056  14598   9397  -1219    318    310       N  
ATOM   3841  CZ  ARG B  38       0.043  -6.465   5.667  1.00 98.20           C  
ANISOU 3841  CZ  ARG B  38    11834  15336  10141  -1486    392    172       C  
ATOM   3842  NH1 ARG B  38       0.498  -7.164   6.698  1.00 95.79           N  
ANISOU 3842  NH1 ARG B  38    11266  15227   9904  -1545    275     74       N  
ATOM   3843  NH2 ARG B  38       0.579  -5.286   5.382  1.00104.07           N  
ANISOU 3843  NH2 ARG B  38    12890  15870  10783  -1697    591    117       N  
ATOM   3844  N   GLN B  39      -6.308  -9.283   4.050  1.00 77.74           N  
ANISOU 3844  N   GLN B  39     8624  13321   7590   -181    -74    507       N  
ATOM   3845  CA  GLN B  39      -7.306  -8.219   4.129  1.00 80.72           C  
ANISOU 3845  CA  GLN B  39     9157  13671   7843    109    -48    514       C  
ATOM   3846  C   GLN B  39      -7.295  -7.538   5.494  1.00 92.04           C  
ANISOU 3846  C   GLN B  39    10718  14981   9272     73     27    489       C  
ATOM   3847  O   GLN B  39      -7.697  -8.128   6.498  1.00 92.69           O  
ANISOU 3847  O   GLN B  39    10606  15193   9420      3     14    433       O  
ATOM   3848  CB  GLN B  39      -8.709  -8.750   3.827  1.00 72.36           C  
ANISOU 3848  CB  GLN B  39     7822  12916   6755    333   -135    445       C  
ATOM   3849  CG  GLN B  39      -8.968  -9.039   2.362  1.00 70.28           C  
ANISOU 3849  CG  GLN B  39     7495  12784   6424    479   -218    452       C  
ATOM   3850  CD  GLN B  39     -10.447  -9.159   2.046  1.00 72.56           C  
ANISOU 3850  CD  GLN B  39     7535  13413   6622    775   -308    339       C  
ATOM   3851  OE1 GLN B  39     -10.829  -9.647   0.982  1.00 82.63           O  
ANISOU 3851  OE1 GLN B  39     8654  14895   7846    871   -400    292       O  
ATOM   3852  NE2 GLN B  39     -11.287  -8.707   2.969  1.00 65.96           N  
ANISOU 3852  NE2 GLN B  39     6635  12677   5750    925   -282    265       N  
ATOM   3853  N   ALA B  40      -6.831  -6.293   5.523  1.00 95.91           N  
ANISOU 3853  N   ALA B  40    11575  15200   9665    101    125    523       N  
ATOM   3854  CA  ALA B  40      -6.822  -5.502   6.746  1.00 90.86           C  
ANISOU 3854  CA  ALA B  40    11111  14417   8996     77    207    483       C  
ATOM   3855  C   ALA B  40      -8.224  -4.974   7.036  1.00 92.39           C  
ANISOU 3855  C   ALA B  40    11324  14695   9087    456    195    457       C  
ATOM   3856  O   ALA B  40      -9.018  -4.787   6.113  1.00 95.06           O  
ANISOU 3856  O   ALA B  40    11672  15124   9323    777    141    478       O  
ATOM   3857  CB  ALA B  40      -5.830  -4.353   6.620  1.00 92.63           C  
ANISOU 3857  CB  ALA B  40    11756  14303   9134    -71    347    497       C  
ATOM   3858  N   PRO B  41      -8.539  -4.747   8.321  1.00 93.97           N  
ANISOU 3858  N   PRO B  41    11508  14902   9293    445    237    392       N  
ATOM   3859  CA  PRO B  41      -9.839  -4.193   8.716  1.00 97.63           C  
ANISOU 3859  CA  PRO B  41    11969  15476   9650    812    242    333       C  
ATOM   3860  C   PRO B  41     -10.139  -2.860   8.034  1.00103.32           C  
ANISOU 3860  C   PRO B  41    13121  15962  10174   1189    283    377       C  
ATOM   3861  O   PRO B  41      -9.597  -1.828   8.429  1.00106.54           O  
ANISOU 3861  O   PRO B  41    13958  16021  10503   1147    401    396       O  
ATOM   3862  CB  PRO B  41      -9.681  -3.987  10.224  1.00 96.67           C  
ANISOU 3862  CB  PRO B  41    11887  15291   9554    653    320    268       C  
ATOM   3863  CG  PRO B  41      -8.692  -5.016  10.633  1.00 93.32           C  
ANISOU 3863  CG  PRO B  41    11281  14904   9271    244    292    279       C  
ATOM   3864  CD  PRO B  41      -7.721  -5.113   9.491  1.00 94.51           C  
ANISOU 3864  CD  PRO B  41    11519  14934   9455    109    267    351       C  
ATOM   3865  N   GLY B  42     -10.992  -2.893   7.016  1.00107.05           N  
ANISOU 3865  N   GLY B  42    13510  16621  10544   1559    187    383       N  
ATOM   3866  CA  GLY B  42     -11.398  -1.686   6.320  1.00115.43           C  
ANISOU 3866  CA  GLY B  42    15020  17473  11364   2023    202    434       C  
ATOM   3867  C   GLY B  42     -10.545  -1.362   5.109  1.00119.23           C  
ANISOU 3867  C   GLY B  42    15882  17659  11761   1955    240    572       C  
ATOM   3868  O   GLY B  42     -10.622  -0.261   4.563  1.00120.45           O  
ANISOU 3868  O   GLY B  42    16577  17504  11683   2273    303    648       O  
ATOM   3869  N   LYS B  43      -9.727  -2.320   4.685  1.00119.45           N  
ANISOU 3869  N   LYS B  43    15665  17766  11953   1553    218    602       N  
ATOM   3870  CA  LYS B  43      -8.859  -2.126   3.528  1.00115.68           C  
ANISOU 3870  CA  LYS B  43    15494  17054  11404   1430    275    713       C  
ATOM   3871  C   LYS B  43      -8.951  -3.291   2.546  1.00109.88           C  
ANISOU 3871  C   LYS B  43    14359  16642  10747   1395    134    716       C  
ATOM   3872  O   LYS B  43      -9.343  -4.399   2.915  1.00103.34           O  
ANISOU 3872  O   LYS B  43    13018  16163  10085   1289     28    628       O  
ATOM   3873  CB  LYS B  43      -7.409  -1.904   3.970  1.00112.44           C  
ANISOU 3873  CB  LYS B  43    15289  16345  11090    899    445    719       C  
ATOM   3874  CG  LYS B  43      -7.203  -0.625   4.767  1.00117.04           C  
ANISOU 3874  CG  LYS B  43    16365  16547  11558    885    617    702       C  
ATOM   3875  CD  LYS B  43      -5.750  -0.440   5.170  1.00121.62           C  
ANISOU 3875  CD  LYS B  43    17078  16910  12222    312    784    649       C  
ATOM   3876  CE  LYS B  43      -5.563   0.841   5.968  1.00128.69           C  
ANISOU 3876  CE  LYS B  43    18483  17421  12992    252    971    598       C  
ATOM   3877  NZ  LYS B  43      -4.145   1.042   6.378  1.00129.43           N  
ANISOU 3877  NZ  LYS B  43    18656  17368  13153   -346   1137    487       N  
ATOM   3878  N   GLN B  44      -8.587  -3.030   1.294  1.00111.64           N  
ANISOU 3878  N   GLN B  44    14866  16723  10830   1469    156    812       N  
ATOM   3879  CA  GLN B  44      -8.703  -4.023   0.229  1.00107.01           C  
ANISOU 3879  CA  GLN B  44    13964  16422  10273   1481     25    810       C  
ATOM   3880  C   GLN B  44      -7.722  -5.179   0.391  1.00 98.12           C  
ANISOU 3880  C   GLN B  44    12488  15395   9399    971     35    773       C  
ATOM   3881  O   GLN B  44      -6.803  -5.121   1.208  1.00102.06           O  
ANISOU 3881  O   GLN B  44    13024  15732  10021    614    143    757       O  
ATOM   3882  CB  GLN B  44      -8.516  -3.370  -1.143  1.00111.62           C  
ANISOU 3882  CB  GLN B  44    15010  16799  10601   1702     64    931       C  
ATOM   3883  CG  GLN B  44      -9.607  -2.382  -1.517  1.00119.27           C  
ANISOU 3883  CG  GLN B  44    16328  17725  11263   2343     -1    968       C  
ATOM   3884  CD  GLN B  44      -9.475  -1.880  -2.940  1.00125.78           C  
ANISOU 3884  CD  GLN B  44    17628  18368  11794   2603     16   1098       C  
ATOM   3885  OE1 GLN B  44      -8.499  -2.182  -3.628  1.00123.17           O  
ANISOU 3885  OE1 GLN B  44    17394  17910  11497   2248    117   1162       O  
ATOM   3886  NE2 GLN B  44     -10.460  -1.113  -3.392  1.00134.32           N  
ANISOU 3886  NE2 GLN B  44    19020  19454  12561   3256    -82   1130       N  
ATOM   3887  N   ARG B  45      -7.927  -6.228  -0.400  1.00 86.79           N  
ANISOU 3887  N   ARG B  45    10720  14240   8016    967    -88    742       N  
ATOM   3888  CA  ARG B  45      -7.081  -7.414  -0.349  1.00 79.26           C  
ANISOU 3888  CA  ARG B  45     9457  13387   7270    567    -97    701       C  
ATOM   3889  C   ARG B  45      -5.713  -7.147  -0.971  1.00 78.32           C  
ANISOU 3889  C   ARG B  45     9596  13031   7131    300     34    763       C  
ATOM   3890  O   ARG B  45      -5.596  -6.934  -2.178  1.00 76.04           O  
ANISOU 3890  O   ARG B  45     9502  12694   6697    403     52    824       O  
ATOM   3891  CB  ARG B  45      -7.777  -8.595  -1.033  1.00 79.72           C  
ANISOU 3891  CB  ARG B  45     9127  13794   7369    643   -249    627       C  
ATOM   3892  CG  ARG B  45      -6.965  -9.879  -1.063  1.00 80.79           C  
ANISOU 3892  CG  ARG B  45     9005  14002   7689    291   -261    586       C  
ATOM   3893  CD  ARG B  45      -7.866 -11.105  -1.179  1.00 88.65           C  
ANISOU 3893  CD  ARG B  45     9610  15319   8754    299   -378    469       C  
ATOM   3894  NE  ARG B  45      -9.001 -10.883  -2.072  1.00101.89           N  
ANISOU 3894  NE  ARG B  45    11216  17231  10267    631   -482    416       N  
ATOM   3895  CZ  ARG B  45      -8.971 -11.069  -3.389  1.00109.68           C  
ANISOU 3895  CZ  ARG B  45    12226  18304  11144    738   -547    420       C  
ATOM   3896  NH1 ARG B  45     -10.055 -10.842  -4.118  1.00116.80           N  
ANISOU 3896  NH1 ARG B  45    13043  19470  11865   1088   -669    347       N  
ATOM   3897  NH2 ARG B  45      -7.856 -11.479  -3.978  1.00104.14           N  
ANISOU 3897  NH2 ARG B  45    11617  17459  10493    519   -497    477       N  
ATOM   3898  N   GLU B  46      -4.683  -7.164  -0.131  1.00 83.40           N  
ANISOU 3898  N   GLU B  46    10224  13562   7902    -45    129    725       N  
ATOM   3899  CA  GLU B  46      -3.326  -6.832  -0.548  1.00 88.82           C  
ANISOU 3899  CA  GLU B  46    11102  14078   8569   -356    284    722       C  
ATOM   3900  C   GLU B  46      -2.447  -8.078  -0.611  1.00 89.82           C  
ANISOU 3900  C   GLU B  46    10852  14412   8863   -613    226    638       C  
ATOM   3901  O   GLU B  46      -2.601  -8.996   0.196  1.00 89.58           O  
ANISOU 3901  O   GLU B  46    10506  14549   8980   -639    110    582       O  
ATOM   3902  CB  GLU B  46      -2.725  -5.815   0.428  1.00 96.34           C  
ANISOU 3902  CB  GLU B  46    12311  14790   9504   -562    442    684       C  
ATOM   3903  CG  GLU B  46      -1.286  -5.416   0.140  1.00100.92           C  
ANISOU 3903  CG  GLU B  46    13043  15241  10060   -966    636    616       C  
ATOM   3904  CD  GLU B  46      -0.658  -4.647   1.287  1.00104.29           C  
ANISOU 3904  CD  GLU B  46    13599  15523  10502  -1237    766    511       C  
ATOM   3905  OE1 GLU B  46      -1.338  -4.453   2.318  1.00101.45           O  
ANISOU 3905  OE1 GLU B  46    13228  15143  10175  -1087    696    512       O  
ATOM   3906  OE2 GLU B  46       0.515  -4.239   1.159  1.00109.36           O  
ANISOU 3906  OE2 GLU B  46    14339  16099  11115  -1620    947    401       O  
ATOM   3907  N   LEU B  47      -1.529  -8.107  -1.573  1.00 90.43           N  
ANISOU 3907  N   LEU B  47    10998  14468   8893   -784    319    626       N  
ATOM   3908  CA  LEU B  47      -0.572  -9.203  -1.692  1.00 86.14           C  
ANISOU 3908  CA  LEU B  47    10123  14125   8481   -990    277    525       C  
ATOM   3909  C   LEU B  47       0.502  -9.125  -0.612  1.00 80.46           C  
ANISOU 3909  C   LEU B  47     9285  13434   7853  -1268    331    395       C  
ATOM   3910  O   LEU B  47       1.180  -8.106  -0.474  1.00 79.10           O  
ANISOU 3910  O   LEU B  47     9333  13118   7604  -1491    509    344       O  
ATOM   3911  CB  LEU B  47       0.086  -9.196  -3.074  1.00 83.35           C  
ANISOU 3911  CB  LEU B  47     9869  13773   8027  -1084    380    527       C  
ATOM   3912  CG  LEU B  47       1.270 -10.150  -3.261  1.00 77.72           C  
ANISOU 3912  CG  LEU B  47     8841  13271   7418  -1297    373    389       C  
ATOM   3913  CD1 LEU B  47       0.831 -11.599  -3.107  1.00 76.33           C  
ANISOU 3913  CD1 LEU B  47     8333  13293   7376  -1132    159    369       C  
ATOM   3914  CD2 LEU B  47       1.938  -9.929  -4.608  1.00 80.29           C  
ANISOU 3914  CD2 LEU B  47     9306  13586   7614  -1422    528    378       C  
ATOM   3915  N   VAL B  48       0.653 -10.204   0.151  1.00 72.91           N  
ANISOU 3915  N   VAL B  48     8004  12664   7033  -1255    182    327       N  
ATOM   3916  CA  VAL B  48       1.688 -10.269   1.176  1.00 72.30           C  
ANISOU 3916  CA  VAL B  48     7773  12685   7014  -1449    183    183       C  
ATOM   3917  C   VAL B  48       2.992 -10.797   0.600  1.00 81.20           C  
ANISOU 3917  C   VAL B  48     8688  14011   8153  -1612    208     37       C  
ATOM   3918  O   VAL B  48       3.975 -10.061   0.491  1.00 82.33           O  
ANISOU 3918  O   VAL B  48     8863  14179   8240  -1881    365    -94       O  
ATOM   3919  CB  VAL B  48       1.284 -11.172   2.353  1.00 66.61           C  
ANISOU 3919  CB  VAL B  48     6868  12059   6383  -1312     11    180       C  
ATOM   3920  CG1 VAL B  48       2.395 -11.219   3.390  1.00 55.60           C  
ANISOU 3920  CG1 VAL B  48     5324  10799   5002  -1454    -16     19       C  
ATOM   3921  CG2 VAL B  48      -0.002 -10.684   2.973  1.00 69.93           C  
ANISOU 3921  CG2 VAL B  48     7444  12338   6788  -1167      4    288       C  
ATOM   3922  N   ALA B  49       3.002 -12.074   0.226  1.00 82.79           N  
ANISOU 3922  N   ALA B  49     8678  14364   8416  -1463     70     35       N  
ATOM   3923  CA  ALA B  49       4.249 -12.694  -0.214  1.00 84.82           C  
ANISOU 3923  CA  ALA B  49     8695  14852   8679  -1550     68   -130       C  
ATOM   3924  C   ALA B  49       4.027 -13.909  -1.101  1.00 85.08           C  
ANISOU 3924  C   ALA B  49     8628  14956   8741  -1368    -32    -92       C  
ATOM   3925  O   ALA B  49       3.484 -14.915  -0.656  1.00 89.66           O  
ANISOU 3925  O   ALA B  49     9156  15533   9378  -1177   -184    -43       O  
ATOM   3926  CB  ALA B  49       5.098 -13.075   0.990  1.00 87.16           C  
ANISOU 3926  CB  ALA B  49     8764  15347   9005  -1556    -37   -294       C  
ATOM   3927  N   ALA B  50       4.470 -13.820  -2.351  1.00 77.33           N  
ANISOU 3927  N   ALA B  50     7652  14027   7704  -1452     75   -126       N  
ATOM   3928  CA  ALA B  50       4.291 -14.914  -3.297  1.00 69.57           C  
ANISOU 3928  CA  ALA B  50     6593  13110   6731  -1295     -4   -109       C  
ATOM   3929  C   ALA B  50       5.622 -15.546  -3.692  1.00 65.23           C  
ANISOU 3929  C   ALA B  50     5795  12816   6174  -1332      6   -307       C  
ATOM   3930  O   ALA B  50       6.633 -14.857  -3.800  1.00 66.73           O  
ANISOU 3930  O   ALA B  50     5898  13143   6314  -1555    151   -454       O  
ATOM   3931  CB  ALA B  50       3.553 -14.424  -4.532  1.00 71.80           C  
ANISOU 3931  CB  ALA B  50     7093  13263   6923  -1288     86     18       C  
ATOM   3932  N   ILE B  51       5.621 -16.860  -3.897  1.00 63.63           N  
ANISOU 3932  N   ILE B  51     5484  12685   6007  -1119   -133   -335       N  
ATOM   3933  CA  ILE B  51       6.805 -17.548  -4.406  1.00 66.65           C  
ANISOU 3933  CA  ILE B  51     5639  13322   6364  -1075   -136   -530       C  
ATOM   3934  C   ILE B  51       6.495 -18.313  -5.694  1.00 72.75           C  
ANISOU 3934  C   ILE B  51     6462  14070   7109   -975   -136   -498       C  
ATOM   3935  O   ILE B  51       5.453 -18.963  -5.816  1.00 76.65           O  
ANISOU 3935  O   ILE B  51     7097  14393   7633   -841   -231   -372       O  
ATOM   3936  CB  ILE B  51       7.456 -18.483  -3.347  1.00 62.97           C  
ANISOU 3936  CB  ILE B  51     4996  13009   5921   -848   -314   -658       C  
ATOM   3937  CG1 ILE B  51       8.811 -18.994  -3.844  1.00 67.06           C  
ANISOU 3937  CG1 ILE B  51     5229  13866   6384   -774   -310   -911       C  
ATOM   3938  CG2 ILE B  51       6.545 -19.651  -3.000  1.00 57.85           C  
ANISOU 3938  CG2 ILE B  51     4521  12151   5309   -595   -470   -526       C  
ATOM   3939  CD1 ILE B  51       9.551 -19.852  -2.842  1.00 62.84           C  
ANISOU 3939  CD1 ILE B  51     4530  13526   5822   -469   -505  -1062       C  
ATOM   3940  N   HIS B  52       7.400 -18.207  -6.660  1.00 72.07           N  
ANISOU 3940  N   HIS B  52     6254  14175   6954  -1073    -10   -637       N  
ATOM   3941  CA  HIS B  52       7.252 -18.894  -7.936  1.00 67.91           C  
ANISOU 3941  CA  HIS B  52     5767  13658   6379   -988      4   -637       C  
ATOM   3942  C   HIS B  52       7.698 -20.346  -7.802  1.00 70.31           C  
ANISOU 3942  C   HIS B  52     5933  14068   6712   -709   -152   -763       C  
ATOM   3943  O   HIS B  52       8.442 -20.690  -6.884  1.00 79.21           O  
ANISOU 3943  O   HIS B  52     6895  15341   7861   -581   -243   -890       O  
ATOM   3944  CB  HIS B  52       8.070 -18.178  -9.015  1.00 69.99           C  
ANISOU 3944  CB  HIS B  52     5983  14080   6529  -1218    232   -742       C  
ATOM   3945  CG  HIS B  52       7.932 -18.777 -10.379  1.00 74.32           C  
ANISOU 3945  CG  HIS B  52     6591  14648   6999  -1143    263   -744       C  
ATOM   3946  ND1 HIS B  52       6.708 -19.082 -10.940  1.00 78.65           N  
ANISOU 3946  ND1 HIS B  52     7361  14993   7529  -1027    179   -573       N  
ATOM   3947  CD2 HIS B  52       8.861 -19.127 -11.299  1.00 71.49           C  
ANISOU 3947  CD2 HIS B  52     6081  14520   6562  -1168    369   -922       C  
ATOM   3948  CE1 HIS B  52       6.892 -19.594 -12.141  1.00 77.76           C  
ANISOU 3948  CE1 HIS B  52     7252  14965   7327   -984    224   -636       C  
ATOM   3949  NE2 HIS B  52       8.191 -19.634 -12.385  1.00 71.82           N  
ANISOU 3949  NE2 HIS B  52     6288  14462   6538  -1064    346   -838       N  
ATOM   3950  N   SER B  53       7.240 -21.197  -8.715  1.00 86.80           N  
ANISOU 3950  N   SER B  53    10317  15378   7285   -632  -1119  -3447       N  
ATOM   3951  CA  SER B  53       7.642 -22.598  -8.720  1.00 92.74           C  
ANISOU 3951  CA  SER B  53    11173  15910   8153   -456  -1037  -3734       C  
ATOM   3952  C   SER B  53       9.109 -22.730  -9.109  1.00101.02           C  
ANISOU 3952  C   SER B  53    12076  17227   9079   -229  -1015  -3775       C  
ATOM   3953  O   SER B  53       9.715 -23.790  -8.940  1.00 85.39           O  
ANISOU 3953  O   SER B  53    10178  15057   7208     -5   -949  -3955       O  
ATOM   3954  CB  SER B  53       6.769 -23.404  -9.684  1.00 95.90           C  
ANISOU 3954  CB  SER B  53    11576  16329   8532   -553   -988  -4094       C  
ATOM   3955  OG  SER B  53       6.917 -22.941 -11.014  1.00 99.76           O  
ANISOU 3955  OG  SER B  53    11816  17343   8744   -603  -1007  -4193       O  
ATOM   3956  N   GLY B  54       9.671 -21.645  -9.633  1.00105.40           N  
ANISOU 3956  N   GLY B  54    12412  18227   9409   -287  -1066  -3597       N  
ATOM   3957  CA  GLY B  54      11.065 -21.610 -10.030  1.00107.73           C  
ANISOU 3957  CA  GLY B  54    12516  18872   9543   -112  -1048  -3606       C  
ATOM   3958  C   GLY B  54      11.967 -21.014  -8.966  1.00103.73           C  
ANISOU 3958  C   GLY B  54    12006  18336   9072    -53  -1090  -3303       C  
ATOM   3959  O   GLY B  54      13.090 -20.605  -9.257  1.00102.37           O  
ANISOU 3959  O   GLY B  54    11629  18545   8724     12  -1096  -3225       O  
ATOM   3960  N   GLY B  55      11.471 -20.954  -7.733  1.00 80.94           N  
ANISOU 3960  N   GLY B  55     9325  15037   6390    -95  -1116  -3139       N  
ATOM   3961  CA  GLY B  55      12.278 -20.528  -6.605  1.00 79.98           C  
ANISOU 3961  CA  GLY B  55     9212  14872   6305    -38  -1153  -2889       C  
ATOM   3962  C   GLY B  55      12.190 -19.055  -6.252  1.00 94.81           C  
ANISOU 3962  C   GLY B  55    11042  16874   8109   -280  -1228  -2594       C  
ATOM   3963  O   GLY B  55      12.212 -18.696  -5.074  1.00 76.45           O  
ANISOU 3963  O   GLY B  55     8820  14345   5881   -318  -1261  -2413       O  
ATOM   3964  N   THR B  56      12.099 -18.200  -7.266  1.00 77.83           N  
ANISOU 3964  N   THR B  56     8739  15053   5781   -443  -1250  -2546       N  
ATOM   3965  CA  THR B  56      12.062 -16.754  -7.056  1.00 76.78           C  
ANISOU 3965  CA  THR B  56     8573  15012   5586   -672  -1312  -2263       C  
ATOM   3966  C   THR B  56      10.867 -16.317  -6.206  1.00 77.97           C  
ANISOU 3966  C   THR B  56     8935  14773   5920   -796  -1343  -2156       C  
ATOM   3967  O   THR B  56       9.812 -16.951  -6.232  1.00 79.12           O  
ANISOU 3967  O   THR B  56     9199  14687   6177   -776  -1321  -2294       O  
ATOM   3968  CB  THR B  56      12.053 -15.988  -8.396  1.00 79.14           C  
ANISOU 3968  CB  THR B  56     8691  15712   5668   -815  -1326  -2206       C  
ATOM   3969  OG1 THR B  56      10.991 -16.477  -9.225  1.00 83.23           O  
ANISOU 3969  OG1 THR B  56     9230  16215   6180   -815  -1307  -2385       O  
ATOM   3970  CG2 THR B  56      13.374 -16.174  -9.121  1.00 79.48           C  
ANISOU 3970  CG2 THR B  56     8489  16217   5494   -730  -1296  -2265       C  
ATOM   3971  N   THR B  57      11.042 -15.237  -5.449  1.00 73.14           N  
ANISOU 3971  N   THR B  57     8359  14102   5330   -934  -1388  -1928       N  
ATOM   3972  CA  THR B  57       9.996 -14.747  -4.557  1.00 71.41           C  
ANISOU 3972  CA  THR B  57     8323  13538   5271  -1032  -1410  -1837       C  
ATOM   3973  C   THR B  57       9.612 -13.303  -4.860  1.00 81.68           C  
ANISOU 3973  C   THR B  57     9615  14887   6533  -1226  -1452  -1637       C  
ATOM   3974  O   THR B  57      10.192 -12.663  -5.737  1.00 84.60           O  
ANISOU 3974  O   THR B  57     9845  15550   6750  -1309  -1466  -1535       O  
ATOM   3975  CB  THR B  57      10.426 -14.829  -3.079  1.00 73.37           C  
ANISOU 3975  CB  THR B  57     8674  13583   5619   -999  -1417  -1774       C  
ATOM   3976  OG1 THR B  57      11.523 -13.935  -2.848  1.00 74.28           O  
ANISOU 3976  OG1 THR B  57     8687  13908   5629  -1099  -1450  -1626       O  
ATOM   3977  CG2 THR B  57      10.840 -16.245  -2.711  1.00 71.55           C  
ANISOU 3977  CG2 THR B  57     8471  13272   5441   -777  -1377  -1919       C  
ATOM   3978  N   ASN B  58       8.631 -12.800  -4.115  1.00 80.76           N  
ANISOU 3978  N   ASN B  58     9650  14477   6557  -1288  -1466  -1573       N  
ATOM   3979  CA  ASN B  58       8.155 -11.429  -4.257  1.00 80.69           C  
ANISOU 3979  CA  ASN B  58     9675  14422   6560  -1431  -1501  -1385       C  
ATOM   3980  C   ASN B  58       7.369 -11.003  -3.020  1.00 81.93           C  
ANISOU 3980  C   ASN B  58    10007  14236   6888  -1457  -1503  -1359       C  
ATOM   3981  O   ASN B  58       6.490 -11.731  -2.554  1.00 85.88           O  
ANISOU 3981  O   ASN B  58    10583  14565   7482  -1380  -1480  -1480       O  
ATOM   3982  CB  ASN B  58       7.287 -11.286  -5.508  1.00 81.67           C  
ANISOU 3982  CB  ASN B  58     9726  14692   6613  -1430  -1511  -1369       C  
ATOM   3983  CG  ASN B  58       6.879  -9.850  -5.773  1.00 84.06           C  
ANISOU 3983  CG  ASN B  58    10060  14954   6925  -1538  -1548  -1129       C  
ATOM   3984  OD1 ASN B  58       7.562  -8.912  -5.362  1.00 91.38           O  
ANISOU 3984  OD1 ASN B  58    11033  15817   7871  -1653  -1560   -975       O  
ATOM   3985  ND2 ASN B  58       5.757  -9.671  -6.462  1.00 79.54           N  
ANISOU 3985  ND2 ASN B  58     9464  14417   6340  -1503  -1565  -1095       N  
ATOM   3986  N   TYR B  59       7.687  -9.824  -2.494  1.00 81.43           N  
ANISOU 3986  N   TYR B  59    10004  14079   6857  -1581  -1524  -1216       N  
ATOM   3987  CA  TYR B  59       7.056  -9.334  -1.273  1.00 80.34           C  
ANISOU 3987  CA  TYR B  59    10022  13643   6862  -1608  -1519  -1220       C  
ATOM   3988  C   TYR B  59       6.497  -7.930  -1.460  1.00 77.46           C  
ANISOU 3988  C   TYR B  59     9733  13135   6564  -1692  -1536  -1074       C  
ATOM   3989  O   TYR B  59       6.905  -7.205  -2.366  1.00 76.18           O  
ANISOU 3989  O   TYR B  59     9517  13094   6334  -1774  -1557   -921       O  
ATOM   3990  CB  TYR B  59       8.061  -9.325  -0.118  1.00 80.27           C  
ANISOU 3990  CB  TYR B  59    10040  13615   6845  -1669  -1520  -1241       C  
ATOM   3991  CG  TYR B  59       8.750 -10.649   0.114  1.00 75.72           C  
ANISOU 3991  CG  TYR B  59     9389  13176   6206  -1550  -1507  -1343       C  
ATOM   3992  CD1 TYR B  59       9.932 -10.964  -0.545  1.00 75.05           C  
ANISOU 3992  CD1 TYR B  59     9152  13380   5986  -1535  -1515  -1329       C  
ATOM   3993  CD2 TYR B  59       8.224 -11.582   0.994  1.00 71.18           C  
ANISOU 3993  CD2 TYR B  59     8895  12443   5706  -1441  -1481  -1440       C  
ATOM   3994  CE1 TYR B  59      10.565 -12.172  -0.337  1.00 77.88           C  
ANISOU 3994  CE1 TYR B  59     9446  13844   6302  -1376  -1499  -1421       C  
ATOM   3995  CE2 TYR B  59       8.849 -12.793   1.209  1.00 73.40           C  
ANISOU 3995  CE2 TYR B  59     9134  12800   5953  -1306  -1467  -1504       C  
ATOM   3996  CZ  TYR B  59      10.020 -13.083   0.542  1.00 79.14           C  
ANISOU 3996  CZ  TYR B  59     9716  13793   6562  -1255  -1476  -1500       C  
ATOM   3997  OH  TYR B  59      10.649 -14.289   0.753  1.00 83.95           O  
ANISOU 3997  OH  TYR B  59    10286  14460   7150  -1073  -1458  -1564       O  
ATOM   3998  N   ALA B  60       5.564  -7.549  -0.593  1.00 76.09           N  
ANISOU 3998  N   ALA B  60     9685  12702   6522  -1663  -1523  -1113       N  
ATOM   3999  CA  ALA B  60       5.039  -6.190  -0.590  1.00 78.09           C  
ANISOU 3999  CA  ALA B  60    10041  12757   6874  -1704  -1530   -992       C  
ATOM   4000  C   ALA B  60       6.069  -5.249   0.026  1.00 84.23           C  
ANISOU 4000  C   ALA B  60    10899  13435   7671  -1885  -1533   -941       C  
ATOM   4001  O   ALA B  60       6.977  -5.690   0.729  1.00 83.71           O  
ANISOU 4001  O   ALA B  60    10804  13457   7545  -1958  -1531  -1027       O  
ATOM   4002  CB  ALA B  60       3.730  -6.126   0.175  1.00 72.57           C  
ANISOU 4002  CB  ALA B  60     9430  11847   6298  -1593  -1505  -1086       C  
ATOM   4003  N   ASN B  61       5.924  -3.955  -0.237  1.00 90.85           N  
ANISOU 4003  N   ASN B  61    11837  14090   8593  -1959  -1539   -799       N  
ATOM   4004  CA  ASN B  61       6.878  -2.967   0.258  1.00 99.91           C  
ANISOU 4004  CA  ASN B  61    13075  15116   9770  -2181  -1536   -759       C  
ATOM   4005  C   ASN B  61       6.745  -2.691   1.754  1.00 99.57           C  
ANISOU 4005  C   ASN B  61    13161  14850   9822  -2220  -1509   -945       C  
ATOM   4006  O   ASN B  61       7.593  -2.024   2.347  1.00 97.78           O  
ANISOU 4006  O   ASN B  61    12995  14559   9599  -2430  -1506   -976       O  
ATOM   4007  CB  ASN B  61       6.762  -1.660  -0.530  1.00107.51           C  
ANISOU 4007  CB  ASN B  61    14136  15901  10814  -2261  -1543   -531       C  
ATOM   4008  CG  ASN B  61       7.212  -1.806  -1.970  1.00113.79           C  
ANISOU 4008  CG  ASN B  61    14784  16990  11462  -2294  -1570   -322       C  
ATOM   4009  OD1 ASN B  61       8.395  -1.660  -2.280  1.00112.43           O  
ANISOU 4009  OD1 ASN B  61    14537  17005  11176  -2499  -1576   -244       O  
ATOM   4010  ND2 ASN B  61       6.268  -2.093  -2.860  1.00119.61           N  
ANISOU 4010  ND2 ASN B  61    15455  17817  12175  -2103  -1585   -237       N  
ATOM   4011  N   SER B  62       5.681  -3.206   2.361  1.00101.58           N  
ANISOU 4011  N   SER B  62    13441  15021  10135  -2039  -1487  -1077       N  
ATOM   4012  CA  SER B  62       5.433  -2.985   3.782  1.00106.07           C  
ANISOU 4012  CA  SER B  62    14112  15424  10766  -2059  -1455  -1263       C  
ATOM   4013  C   SER B  62       5.825  -4.197   4.623  1.00100.95           C  
ANISOU 4013  C   SER B  62    13370  14988   9997  -2046  -1453  -1392       C  
ATOM   4014  O   SER B  62       5.792  -4.146   5.853  1.00102.15           O  
ANISOU 4014  O   SER B  62    13574  15091  10146  -2083  -1431  -1537       O  
ATOM   4015  CB  SER B  62       3.962  -2.633   4.020  1.00113.09           C  
ANISOU 4015  CB  SER B  62    15086  16093  11790  -1872  -1420  -1318       C  
ATOM   4016  OG  SER B  62       3.108  -3.668   3.567  1.00116.51           O  
ANISOU 4016  OG  SER B  62    15405  16682  12181  -1694  -1422  -1315       O  
ATOM   4017  N   VAL B  63       6.197  -5.283   3.955  1.00 94.23           N  
ANISOU 4017  N   VAL B  63    12384  14376   9042  -1983  -1474  -1338       N  
ATOM   4018  CA  VAL B  63       6.568  -6.514   4.644  1.00 86.34           C  
ANISOU 4018  CA  VAL B  63    11310  13548   7947  -1931  -1472  -1421       C  
ATOM   4019  C   VAL B  63       7.985  -6.952   4.288  1.00 87.93           C  
ANISOU 4019  C   VAL B  63    11384  14012   8013  -2000  -1505  -1365       C  
ATOM   4020  O   VAL B  63       8.516  -7.899   4.870  1.00 84.29           O  
ANISOU 4020  O   VAL B  63    10856  13703   7467  -1944  -1510  -1406       O  
ATOM   4021  CB  VAL B  63       5.593  -7.659   4.312  1.00 82.04           C  
ANISOU 4021  CB  VAL B  63    10730  13021   7422  -1750  -1452  -1450       C  
ATOM   4022  CG1 VAL B  63       4.170  -7.272   4.689  1.00 74.96           C  
ANISOU 4022  CG1 VAL B  63     9915  11932   6634  -1677  -1417  -1510       C  
ATOM   4023  CG2 VAL B  63       5.678  -8.017   2.837  1.00 91.44           C  
ANISOU 4023  CG2 VAL B  63    11825  14343   8576  -1696  -1472  -1366       C  
ATOM   4024  N   LYS B  64       8.593  -6.258   3.330  1.00 90.97           N  
ANISOU 4024  N   LYS B  64    11727  14466   8371  -2111  -1526  -1253       N  
ATOM   4025  CA  LYS B  64       9.943  -6.582   2.883  1.00 83.64           C  
ANISOU 4025  CA  LYS B  64    10644  13841   7295  -2183  -1552  -1198       C  
ATOM   4026  C   LYS B  64      10.965  -6.326   3.984  1.00 88.46           C  
ANISOU 4026  C   LYS B  64    11224  14566   7822  -2337  -1568  -1254       C  
ATOM   4027  O   LYS B  64      11.084  -5.208   4.486  1.00 89.99           O  
ANISOU 4027  O   LYS B  64    11509  14623   8058  -2538  -1567  -1274       O  
ATOM   4028  CB  LYS B  64      10.303  -5.774   1.635  1.00 78.05           C  
ANISOU 4028  CB  LYS B  64     9894  13200   6560  -2307  -1564  -1046       C  
ATOM   4029  N   GLY B  65      11.701  -7.368   4.355  1.00 94.67           N  
ANISOU 4029  N   GLY B  65    11878  15605   8487  -2239  -1582  -1284       N  
ATOM   4030  CA  GLY B  65      12.698  -7.263   5.404  1.00101.31           C  
ANISOU 4030  CA  GLY B  65    12643  16641   9207  -2358  -1608  -1328       C  
ATOM   4031  C   GLY B  65      12.210  -7.858   6.709  1.00101.13           C  
ANISOU 4031  C   GLY B  65    12685  16548   9192  -2247  -1600  -1414       C  
ATOM   4032  O   GLY B  65      13.003  -8.148   7.606  1.00 99.63           O  
ANISOU 4032  O   GLY B  65    12398  16587   8867  -2269  -1627  -1433       O  
ATOM   4033  N   ARG B  66      10.897  -8.037   6.813  1.00 97.20           N  
ANISOU 4033  N   ARG B  66    12330  15770   8830  -2132  -1564  -1452       N  
ATOM   4034  CA  ARG B  66      10.292  -8.626   8.001  1.00 86.76           C  
ANISOU 4034  CA  ARG B  66    11070  14385   7510  -2038  -1545  -1515       C  
ATOM   4035  C   ARG B  66       9.720 -10.005   7.689  1.00 81.20           C  
ANISOU 4035  C   ARG B  66    10367  13639   6848  -1801  -1522  -1478       C  
ATOM   4036  O   ARG B  66       9.868 -10.938   8.478  1.00 81.96           O  
ANISOU 4036  O   ARG B  66    10443  13812   6885  -1692  -1520  -1456       O  
ATOM   4037  CB  ARG B  66       9.201  -7.710   8.566  1.00 82.83           C  
ANISOU 4037  CB  ARG B  66    10727  13622   7123  -2118  -1509  -1614       C  
ATOM   4038  CG  ARG B  66       9.702  -6.330   8.978  1.00 86.69           C  
ANISOU 4038  CG  ARG B  66    11258  14082   7600  -2364  -1519  -1691       C  
ATOM   4039  CD  ARG B  66       8.620  -5.507   9.670  1.00 87.37           C  
ANISOU 4039  CD  ARG B  66    11501  13899   7798  -2397  -1472  -1827       C  
ATOM   4040  NE  ARG B  66       7.481  -5.232   8.799  1.00 88.50           N  
ANISOU 4040  NE  ARG B  66    11737  13778   8111  -2278  -1441  -1789       N  
ATOM   4041  CZ  ARG B  66       6.307  -5.850   8.886  1.00 88.69           C  
ANISOU 4041  CZ  ARG B  66    11786  13720   8193  -2099  -1406  -1807       C  
ATOM   4042  NH1 ARG B  66       6.111  -6.781   9.810  1.00 86.77           N  
ANISOU 4042  NH1 ARG B  66    11506  13599   7864  -2030  -1390  -1847       N  
ATOM   4043  NH2 ARG B  66       5.326  -5.536   8.050  1.00 88.24           N  
ANISOU 4043  NH2 ARG B  66    11780  13480   8267  -1997  -1387  -1769       N  
ATOM   4044  N   PHE B  67       9.075 -10.127   6.533  1.00 80.27           N  
ANISOU 4044  N   PHE B  67    10274  13399   6827  -1733  -1504  -1464       N  
ATOM   4045  CA  PHE B  67       8.478 -11.394   6.116  1.00 79.74           C  
ANISOU 4045  CA  PHE B  67    10218  13268   6811  -1550  -1475  -1466       C  
ATOM   4046  C   PHE B  67       9.382 -12.129   5.129  1.00 80.19           C  
ANISOU 4046  C   PHE B  67    10156  13505   6808  -1444  -1491  -1434       C  
ATOM   4047  O   PHE B  67      10.132 -11.504   4.379  1.00 87.41           O  
ANISOU 4047  O   PHE B  67    10975  14580   7657  -1523  -1516  -1401       O  
ATOM   4048  CB  PHE B  67       7.097 -11.172   5.488  1.00 80.87           C  
ANISOU 4048  CB  PHE B  67    10438  13212   7075  -1539  -1444  -1506       C  
ATOM   4049  CG  PHE B  67       6.032 -10.752   6.468  1.00 84.95           C  
ANISOU 4049  CG  PHE B  67    11057  13566   7656  -1578  -1412  -1560       C  
ATOM   4050  CD1 PHE B  67       6.337 -10.519   7.800  1.00 83.04           C  
ANISOU 4050  CD1 PHE B  67    10842  13356   7354  -1641  -1411  -1583       C  
ATOM   4051  CD2 PHE B  67       4.718 -10.605   6.055  1.00 87.56           C  
ANISOU 4051  CD2 PHE B  67    11430  13758   8081  -1546  -1382  -1597       C  
ATOM   4052  CE1 PHE B  67       5.356 -10.134   8.696  1.00 79.49           C  
ANISOU 4052  CE1 PHE B  67    10468  12794   6940  -1670  -1372  -1656       C  
ATOM   4053  CE2 PHE B  67       3.734 -10.223   6.948  1.00 88.32           C  
ANISOU 4053  CE2 PHE B  67    11592  13744   8221  -1562  -1345  -1660       C  
ATOM   4054  CZ  PHE B  67       4.054  -9.987   8.270  1.00 80.68           C  
ANISOU 4054  CZ  PHE B  67    10658  12801   7195  -1623  -1336  -1696       C  
ATOM   4055  N   THR B  68       9.304 -13.456   5.132  1.00 76.26           N  
ANISOU 4055  N   THR B  68     9667  12976   6332  -1268  -1467  -1448       N  
ATOM   4056  CA  THR B  68      10.111 -14.275   4.233  1.00 81.92           C  
ANISOU 4056  CA  THR B  68    10279  13844   7003  -1122  -1468  -1458       C  
ATOM   4057  C   THR B  68       9.395 -15.574   3.876  1.00 84.39           C  
ANISOU 4057  C   THR B  68    10673  13972   7418   -967  -1419  -1530       C  
ATOM   4058  O   THR B  68       9.081 -16.380   4.750  1.00 68.28           O  
ANISOU 4058  O   THR B  68     8730  11779   5435   -890  -1395  -1507       O  
ATOM   4059  CB  THR B  68      11.488 -14.600   4.845  1.00 85.77           C  
ANISOU 4059  CB  THR B  68    10650  14572   7367  -1036  -1500  -1393       C  
ATOM   4060  OG1 THR B  68      12.239 -13.390   5.008  1.00 87.57           O  
ANISOU 4060  OG1 THR B  68    10780  15009   7485  -1227  -1543  -1353       O  
ATOM   4061  CG2 THR B  68      12.263 -15.550   3.945  1.00 88.07           C  
ANISOU 4061  CG2 THR B  68    10831  15011   7620   -831  -1488  -1425       C  
ATOM   4062  N   ILE B  69       9.144 -15.776   2.587  1.00 84.56           N  
ANISOU 4062  N   ILE B  69    10654  14018   7456   -941  -1403  -1616       N  
ATOM   4063  CA  ILE B  69       8.391 -16.940   2.129  1.00 85.71           C  
ANISOU 4063  CA  ILE B  69    10879  13985   7701   -843  -1353  -1730       C  
ATOM   4064  C   ILE B  69       9.298 -18.046   1.588  1.00 86.56           C  
ANISOU 4064  C   ILE B  69    10931  14167   7789   -637  -1331  -1803       C  
ATOM   4065  O   ILE B  69      10.315 -17.778   0.951  1.00 89.94           O  
ANISOU 4065  O   ILE B  69    11207  14866   8101   -586  -1353  -1805       O  
ATOM   4066  CB  ILE B  69       7.331 -16.544   1.068  1.00 67.74           C  
ANISOU 4066  CB  ILE B  69     8593  11697   5448   -950  -1344  -1817       C  
ATOM   4067  CG1 ILE B  69       6.448 -17.739   0.706  1.00 68.35           C  
ANISOU 4067  CG1 ILE B  69     8753  11592   5623   -905  -1290  -1964       C  
ATOM   4068  CG2 ILE B  69       7.991 -15.964  -0.173  1.00 89.15           C  
ANISOU 4068  CG2 ILE B  69    11149  14687   8038   -966  -1371  -1824       C  
ATOM   4069  CD1 ILE B  69       5.403 -17.427  -0.337  1.00 68.51           C  
ANISOU 4069  CD1 ILE B  69     8728  11669   5634  -1008  -1288  -2059       C  
ATOM   4070  N   SER B  70       8.928 -19.291   1.867  1.00 70.96           N  
ANISOU 4070  N   SER B  70     9084  11946   5931   -517  -1281  -1863       N  
ATOM   4071  CA  SER B  70       9.646 -20.442   1.337  1.00 76.39           C  
ANISOU 4071  CA  SER B  70     9758  12624   6642   -288  -1246  -1965       C  
ATOM   4072  C   SER B  70       8.660 -21.557   1.014  1.00 83.26           C  
ANISOU 4072  C   SER B  70    10792  13175   7670   -279  -1177  -2122       C  
ATOM   4073  O   SER B  70       7.466 -21.432   1.286  1.00 89.55           O  
ANISOU 4073  O   SER B  70    11688  13800   8539   -457  -1162  -2126       O  
ATOM   4074  CB  SER B  70      10.685 -20.937   2.341  1.00 79.70           C  
ANISOU 4074  CB  SER B  70    10176  13059   7046    -86  -1259  -1822       C  
ATOM   4075  OG  SER B  70      10.065 -21.380   3.535  1.00 84.16           O  
ANISOU 4075  OG  SER B  70    10915  13348   7714   -106  -1242  -1703       O  
ATOM   4076  N   ARG B  71       9.152 -22.648   0.435  1.00 85.07           N  
ANISOU 4076  N   ARG B  71    11042  13328   7952    -77  -1129  -2267       N  
ATOM   4077  CA  ARG B  71       8.277 -23.766   0.097  1.00 92.25           C  
ANISOU 4077  CA  ARG B  71    12124  13903   9025    -93  -1055  -2450       C  
ATOM   4078  C   ARG B  71       8.957 -25.122   0.274  1.00100.42           C  
ANISOU 4078  C   ARG B  71    13283  14686  10188    190   -997  -2498       C  
ATOM   4079  O   ARG B  71      10.180 -25.210   0.382  1.00 91.30           O  
ANISOU 4079  O   ARG B  71    12028  13694   8967    440  -1016  -2429       O  
ATOM   4080  CB  ARG B  71       7.717 -23.617  -1.320  1.00 93.02           C  
ANISOU 4080  CB  ARG B  71    12130  14152   9062   -217  -1041  -2701       C  
ATOM   4081  CG  ARG B  71       8.758 -23.695  -2.427  1.00 92.02           C  
ANISOU 4081  CG  ARG B  71    11831  14323   8811    -44  -1037  -2854       C  
ATOM   4082  CD  ARG B  71       8.120 -23.456  -3.786  1.00 85.58           C  
ANISOU 4082  CD  ARG B  71    10905  13717   7895   -197  -1030  -3078       C  
ATOM   4083  NE  ARG B  71       7.017 -24.377  -4.041  1.00 88.47           N  
ANISOU 4083  NE  ARG B  71    11427  13788   8399   -307   -969  -3298       N  
ATOM   4084  CZ  ARG B  71       6.170 -24.268  -5.060  1.00 95.74           C  
ANISOU 4084  CZ  ARG B  71    12271  14863   9243   -485   -964  -3497       C  
ATOM   4085  NH1 ARG B  71       6.296 -23.270  -5.924  1.00102.19           N  
ANISOU 4085  NH1 ARG B  71    12868  16112   9848   -551  -1018  -3471       N  
ATOM   4086  NH2 ARG B  71       5.194 -25.153  -5.212  1.00 93.47           N  
ANISOU 4086  NH2 ARG B  71    12122  14313   9081   -613   -906  -3710       N  
ATOM   4087  N   ASP B  72       8.151 -26.177   0.294  1.00120.00           N  
ANISOU 4087  N   ASP B  72    15976  16765  12854    148   -923  -2616       N  
ATOM   4088  CA  ASP B  72       8.645 -27.523   0.538  1.00136.95           C  
ANISOU 4088  CA  ASP B  72    18302  18560  15173    411   -856  -2646       C  
ATOM   4089  C   ASP B  72       9.161 -28.154  -0.751  1.00143.54           C  
ANISOU 4089  C   ASP B  72    19085  19438  16016    590   -805  -2973       C  
ATOM   4090  O   ASP B  72       9.049 -27.562  -1.823  1.00140.55           O  
ANISOU 4090  O   ASP B  72    18528  19384  15492    474   -823  -3166       O  
ATOM   4091  CB  ASP B  72       7.527 -28.371   1.140  1.00144.59           C  
ANISOU 4091  CB  ASP B  72    19544  19045  16349    244   -789  -2624       C  
ATOM   4092  CG  ASP B  72       8.043 -29.621   1.828  1.00150.49           C  
ANISOU 4092  CG  ASP B  72    20518  19372  17290    513   -731  -2507       C  
ATOM   4093  OD1 ASP B  72       8.576 -29.507   2.954  1.00150.84           O  
ANISOU 4093  OD1 ASP B  72    20571  19437  17305    652   -771  -2184       O  
ATOM   4094  OD2 ASP B  72       7.908 -30.720   1.244  1.00153.46           O  
ANISOU 4094  OD2 ASP B  72    21066  19396  17845    587   -645  -2737       O  
ATOM   4095  N   ASN B  73       9.714 -29.359  -0.630  1.00152.39           N  
ANISOU 4095  N   ASN B  73    20366  20231  17305    883   -739  -3029       N  
ATOM   4096  CA  ASN B  73      10.261 -30.105  -1.757  1.00160.87           C  
ANISOU 4096  CA  ASN B  73    21416  21297  18409   1106   -673  -3370       C  
ATOM   4097  C   ASN B  73       9.342 -30.450  -2.925  1.00168.73           C  
ANISOU 4097  C   ASN B  73    22455  22214  19438    875   -610  -3768       C  
ATOM   4098  O   ASN B  73       9.526 -29.952  -4.036  1.00171.50           O  
ANISOU 4098  O   ASN B  73    22584  22978  19601    836   -625  -3989       O  
ATOM   4099  CB  ASN B  73      10.839 -31.437  -1.274  1.00163.17           C  
ANISOU 4099  CB  ASN B  73    21939  21124  18935   1468   -599  -3347       C  
ATOM   4100  CG  ASN B  73      12.089 -31.261  -0.439  1.00160.93           C  
ANISOU 4100  CG  ASN B  73    21538  21034  18574   1819   -656  -3029       C  
ATOM   4101  OD1 ASN B  73      12.085 -31.499   0.769  1.00159.14           O  
ANISOU 4101  OD1 ASN B  73    21454  20573  18438   1881   -674  -2702       O  
ATOM   4102  ND2 ASN B  73      13.171 -30.841  -1.082  1.00161.30           N  
ANISOU 4102  ND2 ASN B  73    21302  21556  18427   2039   -686  -3120       N  
ATOM   4103  N   ALA B  74       8.357 -31.305  -2.668  1.00172.53           N  
ANISOU 4103  N   ALA B  74    23215  22197  20144    703   -540  -3853       N  
ATOM   4104  CA  ALA B  74       7.436 -31.745  -3.709  1.00176.80           C  
ANISOU 4104  CA  ALA B  74    23806  22647  20721    453   -478  -4254       C  
ATOM   4105  C   ALA B  74       6.027 -31.826  -3.129  1.00179.21           C  
ANISOU 4105  C   ALA B  74    24281  22673  21139     60   -464  -4172       C  
ATOM   4106  O   ALA B  74       5.071 -32.131  -3.842  1.00184.88           O  
ANISOU 4106  O   ALA B  74    25033  23337  21878   -223   -421  -4471       O  
ATOM   4107  CB  ALA B  74       7.819 -33.063  -4.363  1.00180.55           C  
ANISOU 4107  CB  ALA B  74    24454  22770  21377    676   -365  -4619       C  
ATOM   4108  N   ALA B  75       5.904 -31.541  -1.837  1.00173.03           N  
ANISOU 4108  N   ALA B  75    23578  21763  20403     33   -501  -3776       N  
ATOM   4109  CA  ALA B  75       4.612 -31.592  -1.161  1.00167.63           C  
ANISOU 4109  CA  ALA B  75    23032  20856  19805   -328   -484  -3662       C  
ATOM   4110  C   ALA B  75       3.755 -30.370  -1.486  1.00160.17           C  
ANISOU 4110  C   ALA B  75    21847  20367  18644   -631   -558  -3664       C  
ATOM   4111  O   ALA B  75       2.604 -30.280  -1.058  1.00161.05           O  
ANISOU 4111  O   ALA B  75    22008  20399  18784   -941   -547  -3606       O  
ATOM   4112  CB  ALA B  75       4.805 -31.722   0.344  1.00166.82           C  
ANISOU 4112  CB  ALA B  75    23082  20505  19798   -237   -492  -3238       C  
ATOM   4113  N   ASN B  76       4.329 -29.441  -2.248  1.00151.30           N  
ANISOU 4113  N   ASN B  76    20460  19725  17304   -532   -628  -3719       N  
ATOM   4114  CA  ASN B  76       3.663 -28.192  -2.616  1.00139.15           C  
ANISOU 4114  CA  ASN B  76    18688  18624  15558   -756   -705  -3684       C  
ATOM   4115  C   ASN B  76       3.153 -27.403  -1.415  1.00129.98           C  
ANISOU 4115  C   ASN B  76    17529  17478  14379   -883   -753  -3345       C  
ATOM   4116  O   ASN B  76       2.097 -26.772  -1.475  1.00126.98           O  
ANISOU 4116  O   ASN B  76    17060  17260  13925  -1133   -778  -3341       O  
ATOM   4117  CB  ASN B  76       2.530 -28.443  -3.614  1.00138.24           C  
ANISOU 4117  CB  ASN B  76    18531  18580  15413  -1042   -674  -4008       C  
ATOM   4118  CG  ASN B  76       3.041 -28.783  -5.000  1.00139.94           C  
ANISOU 4118  CG  ASN B  76    18639  18993  15537   -939   -651  -4362       C  
ATOM   4119  OD1 ASN B  76       4.072 -28.269  -5.437  1.00139.66           O  
ANISOU 4119  OD1 ASN B  76    18443  19261  15361   -714   -692  -4329       O  
ATOM   4120  ND2 ASN B  76       2.322 -29.652  -5.700  1.00141.74           N  
ANISOU 4120  ND2 ASN B  76    18944  19078  15831  -1124   -582  -4718       N  
ATOM   4121  N   THR B  77       3.913 -27.444  -0.326  1.00 95.83           N  
ANISOU 4121  N   THR B  77    11879  13661  10872  -1115    326    732       N  
ATOM   4122  CA  THR B  77       3.557 -26.726   0.890  1.00 87.55           C  
ANISOU 4122  CA  THR B  77    10822  12860   9586   -847    274    748       C  
ATOM   4123  C   THR B  77       4.395 -25.457   1.016  1.00 82.49           C  
ANISOU 4123  C   THR B  77    10160  12224   8959   -565    -23    587       C  
ATOM   4124  O   THR B  77       5.609 -25.489   0.836  1.00 86.55           O  
ANISOU 4124  O   THR B  77    10768  12505   9613   -483   -163    555       O  
ATOM   4125  CB  THR B  77       3.770 -27.603   2.140  1.00 88.59           C  
ANISOU 4125  CB  THR B  77    11165  12951   9546   -717    426    962       C  
ATOM   4126  OG1 THR B  77       3.071 -28.843   1.977  1.00 83.03           O  
ANISOU 4126  OG1 THR B  77    10490  12164   8893  -1004    753   1116       O  
ATOM   4127  CG2 THR B  77       3.258 -26.895   3.385  1.00 96.01           C  
ANISOU 4127  CG2 THR B  77    12099  14186  10196   -437    399    973       C  
ATOM   4128  N   VAL B  78       3.741 -24.341   1.321  1.00 77.76           N  
ANISOU 4128  N   VAL B  78     9425  11877   8242   -422   -103    475       N  
ATOM   4129  CA  VAL B  78       4.434 -23.064   1.457  1.00 77.72           C  
ANISOU 4129  CA  VAL B  78     9384  11861   8284   -171   -350    292       C  
ATOM   4130  C   VAL B  78       4.452 -22.563   2.900  1.00 82.67           C  
ANISOU 4130  C   VAL B  78    10074  12673   8665    132   -433    258       C  
ATOM   4131  O   VAL B  78       3.412 -22.497   3.560  1.00 89.54           O  
ANISOU 4131  O   VAL B  78    10910  13802   9310    177   -309    316       O  
ATOM   4132  CB  VAL B  78       3.839 -21.995   0.513  1.00 74.30           C  
ANISOU 4132  CB  VAL B  78     8756  11521   7952   -207   -392    155       C  
ATOM   4133  CG1 VAL B  78       4.172 -20.590   0.996  1.00 73.52           C  
ANISOU 4133  CG1 VAL B  78     8613  11469   7854     76   -570    -26       C  
ATOM   4134  CG2 VAL B  78       4.336 -22.210  -0.907  1.00 74.09           C  
ANISOU 4134  CG2 VAL B  78     8706  11264   8180   -390   -399    134       C  
ATOM   4135  N   TYR B  79       5.643 -22.216   3.381  1.00 77.93           N  
ANISOU 4135  N   TYR B  79     9552  11950   8108    347   -644    146       N  
ATOM   4136  CA  TYR B  79       5.807 -21.708   4.737  1.00 74.96           C  
ANISOU 4136  CA  TYR B  79     9236  11759   7487    666   -771     60       C  
ATOM   4137  C   TYR B  79       6.157 -20.221   4.731  1.00 70.85           C  
ANISOU 4137  C   TYR B  79     8592  11244   7085    834   -987   -237       C  
ATOM   4138  O   TYR B  79       7.157 -19.808   4.135  1.00 69.61           O  
ANISOU 4138  O   TYR B  79     8385  10847   7216    823  -1135   -386       O  
ATOM   4139  CB  TYR B  79       6.893 -22.495   5.470  1.00 71.70           C  
ANISOU 4139  CB  TYR B  79     8999  11251   6994    825   -862    130       C  
ATOM   4140  CG  TYR B  79       6.704 -23.995   5.423  1.00 76.01           C  
ANISOU 4140  CG  TYR B  79     9693  11710   7475    668   -617    435       C  
ATOM   4141  CD1 TYR B  79       5.918 -24.646   6.365  1.00 79.62           C  
ANISOU 4141  CD1 TYR B  79    10271  12359   7622    746   -405    645       C  
ATOM   4142  CD2 TYR B  79       7.316 -24.761   4.439  1.00 80.60           C  
ANISOU 4142  CD2 TYR B  79    10304  11997   8323    447   -568    513       C  
ATOM   4143  CE1 TYR B  79       5.745 -26.018   6.327  1.00 86.35           C  
ANISOU 4143  CE1 TYR B  79    11266  13086   8458    596   -134    927       C  
ATOM   4144  CE2 TYR B  79       7.149 -26.132   4.392  1.00 87.15           C  
ANISOU 4144  CE2 TYR B  79    11277  12711   9125    296   -319    774       C  
ATOM   4145  CZ  TYR B  79       6.363 -26.756   5.338  1.00 92.76           C  
ANISOU 4145  CZ  TYR B  79    12102  13589   9552    365    -95    981       C  
ATOM   4146  OH  TYR B  79       6.195 -28.121   5.295  1.00 98.36           O  
ANISOU 4146  OH  TYR B  79    12961  14139  10273    208    198   1245       O  
ATOM   4147  N   LEU B  80       5.326 -19.425   5.398  1.00 70.02           N  
ANISOU 4147  N   LEU B  80     8434  11393   6778    989   -976   -323       N  
ATOM   4148  CA  LEU B  80       5.538 -17.986   5.482  1.00 74.05           C  
ANISOU 4148  CA  LEU B  80     8836  11903   7398   1156  -1140   -613       C  
ATOM   4149  C   LEU B  80       6.054 -17.579   6.859  1.00 83.35           C  
ANISOU 4149  C   LEU B  80    10087  13220   8361   1475  -1332   -803       C  
ATOM   4150  O   LEU B  80       5.350 -17.700   7.863  1.00 86.86           O  
ANISOU 4150  O   LEU B  80    10606  13943   8452   1636  -1266   -740       O  
ATOM   4151  CB  LEU B  80       4.247 -17.230   5.159  1.00 74.97           C  
ANISOU 4151  CB  LEU B  80     8825  12195   7464   1127   -998   -612       C  
ATOM   4152  CG  LEU B  80       4.335 -15.702   5.184  1.00 69.57           C  
ANISOU 4152  CG  LEU B  80     8038  11482   6913   1302  -1108   -891       C  
ATOM   4153  CD1 LEU B  80       5.381 -15.211   4.197  1.00 70.52           C  
ANISOU 4153  CD1 LEU B  80     8098  11251   7445   1225  -1205  -1026       C  
ATOM   4154  CD2 LEU B  80       2.981 -15.078   4.886  1.00 62.51           C  
ANISOU 4154  CD2 LEU B  80     7027  10789   5933   1301   -943   -841       C  
ATOM   4155  N   GLN B  81       7.292 -17.097   6.890  1.00 85.09           N  
ANISOU 4155  N   GLN B  81    10275  13255   8802   1571  -1566  -1052       N  
ATOM   4156  CA  GLN B  81       7.940 -16.663   8.120  1.00 79.35           C  
ANISOU 4156  CA  GLN B  81     9582  12661   7906   1876  -1805  -1310       C  
ATOM   4157  C   GLN B  81       7.650 -15.190   8.378  1.00 74.62           C  
ANISOU 4157  C   GLN B  81     8868  12114   7371   2010  -1878  -1632       C  
ATOM   4158  O   GLN B  81       8.054 -14.324   7.602  1.00 72.54           O  
ANISOU 4158  O   GLN B  81     8470  11597   7495   1920  -1912  -1822       O  
ATOM   4159  CB  GLN B  81       9.450 -16.880   8.016  1.00 81.85           C  
ANISOU 4159  CB  GLN B  81     9875  12757   8467   1902  -2031  -1461       C  
ATOM   4160  CG  GLN B  81      10.231 -16.535   9.272  1.00 86.69           C  
ANISOU 4160  CG  GLN B  81    10498  13538   8901   2228  -2323  -1762       C  
ATOM   4161  CD  GLN B  81      10.235 -17.662  10.285  1.00 88.97           C  
ANISOU 4161  CD  GLN B  81    10984  14084   8737   2437  -2336  -1540       C  
ATOM   4162  OE1 GLN B  81       9.531 -18.660  10.125  1.00 94.32           O  
ANISOU 4162  OE1 GLN B  81    11797  14802   9238   2325  -2084  -1157       O  
ATOM   4163  NE2 GLN B  81      11.036 -17.511  11.334  1.00 85.00           N  
ANISOU 4163  NE2 GLN B  81    10496  13754   8047   2753  -2620  -1789       N  
ATOM   4164  N   MET B  82       6.949 -14.909   9.469  1.00 79.86           N  
ANISOU 4164  N   MET B  82     9596  13088   7659   2237  -1874  -1685       N  
ATOM   4165  CA  MET B  82       6.598 -13.537   9.814  1.00 86.29           C  
ANISOU 4165  CA  MET B  82    10321  13963   8502   2387  -1922  -1994       C  
ATOM   4166  C   MET B  82       7.280 -13.096  11.103  1.00 91.05           C  
ANISOU 4166  C   MET B  82    10961  14727   8908   2703  -2195  -2348       C  
ATOM   4167  O   MET B  82       6.882 -13.497  12.196  1.00100.95           O  
ANISOU 4167  O   MET B  82    12353  16304   9701   2931  -2204  -2282       O  
ATOM   4168  CB  MET B  82       5.080 -13.385   9.937  1.00 85.78           C  
ANISOU 4168  CB  MET B  82    10272  14140   8180   2399  -1673  -1805       C  
ATOM   4169  CG  MET B  82       4.327 -13.660   8.646  1.00 84.29           C  
ANISOU 4169  CG  MET B  82    10001  13841   8185   2109  -1434  -1525       C  
ATOM   4170  SD  MET B  82       2.573 -13.262   8.767  1.00 96.03           S  
ANISOU 4170  SD  MET B  82    11433  15628   9427   2147  -1172  -1378       S  
ATOM   4171  CE  MET B  82       2.079 -14.318  10.124  1.00111.30           C  
ANISOU 4171  CE  MET B  82    13541  17908  10842   2298  -1088  -1174       C  
ATOM   4172  N   ASN B  83       8.309 -12.267  10.968  1.00 82.79           N  
ANISOU 4172  N   ASN B  83     9784  13458   8215   2722  -2409  -2737       N  
ATOM   4173  CA  ASN B  83       9.045 -11.770  12.122  1.00 84.08           C  
ANISOU 4173  CA  ASN B  83     9935  13769   8242   3007  -2709  -3159       C  
ATOM   4174  C   ASN B  83       8.815 -10.280  12.342  1.00 88.02           C  
ANISOU 4174  C   ASN B  83    10324  14215   8903   3098  -2737  -3571       C  
ATOM   4175  O   ASN B  83       8.521  -9.547  11.397  1.00 76.51           O  
ANISOU 4175  O   ASN B  83     8764  12484   7824   2917  -2563  -3574       O  
ATOM   4176  CB  ASN B  83      10.538 -12.057  11.966  1.00 84.65           C  
ANISOU 4176  CB  ASN B  83     9912  13650   8601   2977  -2967  -3353       C  
ATOM   4177  CG  ASN B  83      10.825 -13.525  11.725  1.00 83.23           C  
ANISOU 4177  CG  ASN B  83     9850  13487   8287   2901  -2925  -2948       C  
ATOM   4178  OD1 ASN B  83      11.550 -13.884  10.798  1.00 83.02           O  
ANISOU 4178  OD1 ASN B  83     9746  13165   8632   2689  -2919  -2869       O  
ATOM   4179  ND2 ASN B  83      10.251 -14.384  12.558  1.00 85.87           N  
ANISOU 4179  ND2 ASN B  83    10383  14150   8095   3084  -2866  -2681       N  
ATOM   4180  N   SER B  84       8.954  -9.848  13.594  1.00 90.96           N  
ANISOU 4180  N   SER B  84    10731  14853   8977   3400  -2946  -3915       N  
ATOM   4181  CA  SER B  84       8.748  -8.453  13.979  1.00 97.91           C  
ANISOU 4181  CA  SER B  84    11527  15702   9973   3520  -2982  -4355       C  
ATOM   4182  C   SER B  84       7.383  -7.928  13.531  1.00 99.95           C  
ANISOU 4182  C   SER B  84    11815  15951  10211   3456  -2647  -4131       C  
ATOM   4183  O   SER B  84       7.296  -6.949  12.789  1.00102.51           O  
ANISOU 4183  O   SER B  84    12018  15969  10960   3332  -2522  -4267       O  
ATOM   4184  CB  SER B  84       9.871  -7.567  13.432  1.00 97.69           C  
ANISOU 4184  CB  SER B  84    11280  15270  10569   3383  -3123  -4790       C  
ATOM   4185  OG  SER B  84       9.708  -6.221  13.844  1.00104.71           O  
ANISOU 4185  OG  SER B  84    12091  16094  11599   3495  -3139  -5245       O  
ATOM   4186  N   LEU B  85       6.323  -8.587  13.988  1.00 94.82           N  
ANISOU 4186  N   LEU B  85    11319  15637   9074   3556  -2485  -3780       N  
ATOM   4187  CA  LEU B  85       4.964  -8.226  13.597  1.00 92.52           C  
ANISOU 4187  CA  LEU B  85    11033  15398   8725   3508  -2170  -3538       C  
ATOM   4188  C   LEU B  85       4.546  -6.859  14.132  1.00 96.22           C  
ANISOU 4188  C   LEU B  85    11465  15892   9201   3707  -2156  -3913       C  
ATOM   4189  O   LEU B  85       5.056  -6.391  15.150  1.00101.50           O  
ANISOU 4189  O   LEU B  85    12161  16680   9724   3942  -2382  -4330       O  
ATOM   4190  CB  LEU B  85       3.973  -9.303  14.047  1.00 94.46           C  
ANISOU 4190  CB  LEU B  85    11426  15997   8467   3564  -1990  -3099       C  
ATOM   4191  CG  LEU B  85       4.067 -10.635  13.300  1.00 92.36           C  
ANISOU 4191  CG  LEU B  85    11189  15659   8245   3312  -1892  -2664       C  
ATOM   4192  CD1 LEU B  85       3.171 -11.681  13.937  1.00 96.45           C  
ANISOU 4192  CD1 LEU B  85    11858  16510   8279   3390  -1700  -2283       C  
ATOM   4193  CD2 LEU B  85       3.708 -10.446  11.836  1.00 87.12           C  
ANISOU 4193  CD2 LEU B  85    10386  14718   7996   3004  -1704  -2482       C  
ATOM   4194  N   LYS B  86       3.610  -6.226  13.432  1.00 96.25           N  
ANISOU 4194  N   LYS B  86    11407  15794   9370   3628  -1889  -3774       N  
ATOM   4195  CA  LYS B  86       3.144  -4.890  13.781  1.00 99.27           C  
ANISOU 4195  CA  LYS B  86    11757  16146   9817   3805  -1817  -4090       C  
ATOM   4196  C   LYS B  86       1.616  -4.867  13.841  1.00 96.00           C  
ANISOU 4196  C   LYS B  86    11380  15998   9097   3891  -1527  -3775       C  
ATOM   4197  O   LYS B  86       0.964  -5.771  13.317  1.00 82.61           O  
ANISOU 4197  O   LYS B  86     9685  14426   7278   3743  -1365  -3327       O  
ATOM   4198  CB  LYS B  86       3.665  -3.876  12.756  1.00106.77           C  
ANISOU 4198  CB  LYS B  86    12562  16614  11390   3653  -1759  -4288       C  
ATOM   4199  CG  LYS B  86       5.181  -3.743  12.733  1.00115.09           C  
ANISOU 4199  CG  LYS B  86    13535  17380  12813   3567  -2024  -4662       C  
ATOM   4200  CD  LYS B  86       5.632  -2.663  11.761  1.00115.46           C  
ANISOU 4200  CD  LYS B  86    13446  16922  13502   3430  -1897  -4851       C  
ATOM   4201  CE  LYS B  86       7.138  -2.465  11.811  1.00116.73           C  
ANISOU 4201  CE  LYS B  86    13490  16792  14070   3340  -2145  -5274       C  
ATOM   4202  NZ  LYS B  86       7.579  -1.350  10.928  1.00115.87           N  
ANISOU 4202  NZ  LYS B  86    13252  16154  14621   3216  -1969  -5472       N  
ATOM   4203  N   PRO B  87       1.035  -3.845  14.494  1.00101.08           N  
ANISOU 4203  N   PRO B  87    12042  16736   9629   4129  -1455  -4027       N  
ATOM   4204  CA  PRO B  87      -0.429  -3.753  14.565  1.00105.26           C  
ANISOU 4204  CA  PRO B  87    12581  17526   9888   4231  -1170  -3744       C  
ATOM   4205  C   PRO B  87      -1.099  -3.562  13.203  1.00105.53           C  
ANISOU 4205  C   PRO B  87    12477  17385  10236   4040   -923  -3429       C  
ATOM   4206  O   PRO B  87      -2.285  -3.859  13.065  1.00109.62           O  
ANISOU 4206  O   PRO B  87    12960  18155  10535   4053   -703  -3102       O  
ATOM   4207  CB  PRO B  87      -0.665  -2.524  15.454  1.00108.30           C  
ANISOU 4207  CB  PRO B  87    13006  17954  10190   4528  -1168  -4165       C  
ATOM   4208  CG  PRO B  87       0.619  -1.762  15.416  1.00111.22           C  
ANISOU 4208  CG  PRO B  87    13331  17958  10968   4500  -1396  -4660       C  
ATOM   4209  CD  PRO B  87       1.685  -2.801  15.304  1.00107.62           C  
ANISOU 4209  CD  PRO B  87    12881  17471  10538   4331  -1641  -4605       C  
ATOM   4210  N   GLU B  88      -0.353  -3.078  12.214  1.00103.17           N  
ANISOU 4210  N   GLU B  88    12092  16674  10434   3881   -953  -3527       N  
ATOM   4211  CA  GLU B  88      -0.899  -2.911  10.870  1.00100.69           C  
ANISOU 4211  CA  GLU B  88    11663  16203  10391   3738   -734  -3224       C  
ATOM   4212  C   GLU B  88      -0.783  -4.193  10.050  1.00 94.62           C  
ANISOU 4212  C   GLU B  88    10864  15468   9620   3461   -748  -2847       C  
ATOM   4213  O   GLU B  88      -1.226  -4.248   8.903  1.00 92.85           O  
ANISOU 4213  O   GLU B  88    10544  15169   9565   3334   -596  -2580       O  
ATOM   4214  CB  GLU B  88      -0.228  -1.744  10.138  1.00106.50           C  
ANISOU 4214  CB  GLU B  88    12340  16464  11662   3728   -694  -3467       C  
ATOM   4215  CG  GLU B  88       1.284  -1.844  10.031  1.00111.32           C  
ANISOU 4215  CG  GLU B  88    12950  16739  12607   3578   -916  -3732       C  
ATOM   4216  CD  GLU B  88       1.995  -1.218  11.214  1.00123.66           C  
ANISOU 4216  CD  GLU B  88    14555  18261  14167   3739  -1118  -4264       C  
ATOM   4217  OE1 GLU B  88       1.322  -0.914  12.222  1.00130.05           O  
ANISOU 4217  OE1 GLU B  88    15432  19357  14624   3970  -1108  -4396       O  
ATOM   4218  OE2 GLU B  88       3.225  -1.024  11.133  1.00126.68           O  
ANISOU 4218  OE2 GLU B  88    14890  18337  14904   3639  -1286  -4569       O  
ATOM   4219  N   ASP B  89      -0.182  -5.220  10.641  1.00 92.75           N  
ANISOU 4219  N   ASP B  89    10713  15348   9179   3391   -929  -2835       N  
ATOM   4220  CA  ASP B  89      -0.096  -6.527   9.999  1.00 88.66           C  
ANISOU 4220  CA  ASP B  89    10189  14869   8629   3137   -926  -2487       C  
ATOM   4221  C   ASP B  89      -1.283  -7.391  10.406  1.00 88.35           C  
ANISOU 4221  C   ASP B  89    10164  15232   8172   3141   -765  -2165       C  
ATOM   4222  O   ASP B  89      -1.439  -8.515   9.927  1.00 85.14           O  
ANISOU 4222  O   ASP B  89     9746  14888   7716   2926   -711  -1864       O  
ATOM   4223  CB  ASP B  89       1.215  -7.227  10.360  1.00 91.75           C  
ANISOU 4223  CB  ASP B  89    10665  15144   9054   3065  -1177  -2614       C  
ATOM   4224  CG  ASP B  89       2.429  -6.519   9.794  1.00 97.91           C  
ANISOU 4224  CG  ASP B  89    11385  15500  10317   2998  -1311  -2903       C  
ATOM   4225  OD1 ASP B  89       2.300  -5.873   8.732  1.00 99.95           O  
ANISOU 4225  OD1 ASP B  89    11552  15506  10920   2913  -1166  -2853       O  
ATOM   4226  OD2 ASP B  89       3.512  -6.610  10.409  1.00101.12           O  
ANISOU 4226  OD2 ASP B  89    11828  15832  10761   3043  -1551  -3178       O  
ATOM   4227  N   THR B  90      -2.113  -6.858  11.298  1.00 89.75           N  
ANISOU 4227  N   THR B  90    10366  15666   8070   3383   -670  -2243       N  
ATOM   4228  CA  THR B  90      -3.331  -7.539  11.717  1.00 89.85           C  
ANISOU 4228  CA  THR B  90    10368  16056   7717   3406   -467  -1950       C  
ATOM   4229  C   THR B  90      -4.321  -7.567  10.562  1.00 83.66           C  
ANISOU 4229  C   THR B  90     9391  15314   7082   3243   -261  -1680       C  
ATOM   4230  O   THR B  90      -4.873  -6.535  10.184  1.00 87.51           O  
ANISOU 4230  O   THR B  90     9776  15779   7695   3366   -163  -1748       O  
ATOM   4231  CB  THR B  90      -3.984  -6.840  12.923  1.00101.06           C  
ANISOU 4231  CB  THR B  90    11852  17731   8814   3733   -395  -2116       C  
ATOM   4232  OG1 THR B  90      -3.088  -6.872  14.041  1.00106.75           O  
ANISOU 4232  OG1 THR B  90    12751  18472   9336   3913   -610  -2386       O  
ATOM   4233  CG2 THR B  90      -5.283  -7.534  13.304  1.00103.38           C  
ANISOU 4233  CG2 THR B  90    12109  18401   8769   3746   -139  -1794       C  
ATOM   4234  N   ALA B  91      -4.539  -8.752  10.002  1.00 80.17           N  
ANISOU 4234  N   ALA B  91     8897  14938   6626   2981   -196  -1384       N  
ATOM   4235  CA  ALA B  91      -5.402  -8.893   8.837  1.00 81.23           C  
ANISOU 4235  CA  ALA B  91     8827  15138   6899   2808    -44  -1160       C  
ATOM   4236  C   ALA B  91      -5.900 -10.324   8.672  1.00 77.05           C  
ANISOU 4236  C   ALA B  91     8246  14784   6246   2548     71   -869       C  
ATOM   4237  O   ALA B  91      -5.698 -11.169   9.544  1.00 74.70           O  
ANISOU 4237  O   ALA B  91     8087  14566   5731   2534     83   -799       O  
ATOM   4238  CB  ALA B  91      -4.668  -8.443   7.583  1.00 81.64           C  
ANISOU 4238  CB  ALA B  91     8832  14853   7335   2700   -145  -1220       C  
ATOM   4239  N   VAL B  92      -6.555 -10.584   7.546  1.00 76.81           N  
ANISOU 4239  N   VAL B  92     8016  14813   6356   2355    164   -707       N  
ATOM   4240  CA  VAL B  92      -7.023 -11.924   7.220  1.00 83.18           C  
ANISOU 4240  CA  VAL B  92     8737  15746   7120   2061    279   -473       C  
ATOM   4241  C   VAL B  92      -6.173 -12.494   6.097  1.00 83.48           C  
ANISOU 4241  C   VAL B  92     8791  15510   7418   1803    154   -440       C  
ATOM   4242  O   VAL B  92      -6.283 -12.063   4.951  1.00 90.08           O  
ANISOU 4242  O   VAL B  92     9493  16288   8446   1756    123   -449       O  
ATOM   4243  CB  VAL B  92      -8.487 -11.914   6.763  1.00 91.12           C  
ANISOU 4243  CB  VAL B  92     9459  17077   8084   2010    473   -347       C  
ATOM   4244  CG1 VAL B  92      -8.992 -13.338   6.596  1.00 89.40           C  
ANISOU 4244  CG1 VAL B  92     9144  16983   7840   1687    620   -150       C  
ATOM   4245  CG2 VAL B  92      -9.344 -11.145   7.756  1.00101.47           C  
ANISOU 4245  CG2 VAL B  92    10736  18648   9171   2303    607   -392       C  
ATOM   4246  N   TYR B  93      -5.330 -13.466   6.431  1.00 79.09           N  
ANISOU 4246  N   TYR B  93     8409  14795   6849   1666     95   -391       N  
ATOM   4247  CA  TYR B  93      -4.381 -14.023   5.473  1.00 73.86           C  
ANISOU 4247  CA  TYR B  93     7793  13842   6427   1444    -25   -373       C  
ATOM   4248  C   TYR B  93      -4.961 -15.181   4.664  1.00 71.75           C  
ANISOU 4248  C   TYR B  93     7397  13651   6215   1116    104   -186       C  
ATOM   4249  O   TYR B  93      -5.405 -16.183   5.225  1.00 71.85           O  
ANISOU 4249  O   TYR B  93     7426  13785   6089    988    260    -44       O  
ATOM   4250  CB  TYR B  93      -3.099 -14.462   6.187  1.00 76.78           C  
ANISOU 4250  CB  TYR B  93     8405  13989   6778   1483   -167   -430       C  
ATOM   4251  CG  TYR B  93      -2.231 -13.311   6.650  1.00 76.90           C  
ANISOU 4251  CG  TYR B  93     8515  13848   6856   1746   -357   -692       C  
ATOM   4252  CD1 TYR B  93      -2.556 -12.581   7.787  1.00 85.03           C  
ANISOU 4252  CD1 TYR B  93     9593  15054   7661   2028   -355   -826       C  
ATOM   4253  CD2 TYR B  93      -1.085 -12.956   5.951  1.00 70.34           C  
ANISOU 4253  CD2 TYR B  93     7717  12685   6325   1705   -524   -826       C  
ATOM   4254  CE1 TYR B  93      -1.766 -11.529   8.212  1.00 85.96           C  
ANISOU 4254  CE1 TYR B  93     9780  15019   7862   2249   -529  -1118       C  
ATOM   4255  CE2 TYR B  93      -0.289 -11.907   6.368  1.00 69.86           C  
ANISOU 4255  CE2 TYR B  93     7710  12456   6375   1915   -679  -1101       C  
ATOM   4256  CZ  TYR B  93      -0.633 -11.197   7.498  1.00 79.50           C  
ANISOU 4256  CZ  TYR B  93     8971  13857   7381   2179   -689  -1262       C  
ATOM   4257  OH  TYR B  93       0.158 -10.152   7.915  1.00 80.13           O  
ANISOU 4257  OH  TYR B  93     9088  13761   7595   2370   -845  -1586       O  
ATOM   4258  N   TYR B  94      -4.949 -15.031   3.342  1.00 77.98           N  
ANISOU 4258  N   TYR B  94     8059  14361   7208    990     54   -198       N  
ATOM   4259  CA  TYR B  94      -5.436 -16.065   2.435  1.00 79.78           C  
ANISOU 4259  CA  TYR B  94     8147  14656   7509    675    140    -84       C  
ATOM   4260  C   TYR B  94      -4.287 -16.719   1.675  1.00 79.71           C  
ANISOU 4260  C   TYR B  94     8274  14315   7698    487     32    -79       C  
ATOM   4261  O   TYR B  94      -3.400 -16.034   1.163  1.00 83.19           O  
ANISOU 4261  O   TYR B  94     8793  14522   8294    595   -112   -170       O  
ATOM   4262  CB  TYR B  94      -6.422 -15.476   1.423  1.00 64.60           C  
ANISOU 4262  CB  TYR B  94     5956  12970   5622    693    164   -106       C  
ATOM   4263  CG  TYR B  94      -7.676 -14.884   2.025  1.00 69.32           C  
ANISOU 4263  CG  TYR B  94     6371  13926   6043    865    290   -101       C  
ATOM   4264  CD1 TYR B  94      -8.760 -15.689   2.348  1.00 69.03           C  
ANISOU 4264  CD1 TYR B  94     6153  14171   5905    691    474    -15       C  
ATOM   4265  CD2 TYR B  94      -7.783 -13.519   2.251  1.00 79.26           C  
ANISOU 4265  CD2 TYR B  94     7627  15223   7264   1199    249   -188       C  
ATOM   4266  CE1 TYR B  94      -9.911 -15.151   2.891  1.00 81.78           C  
ANISOU 4266  CE1 TYR B  94     7582  16119   7373    854    605     -7       C  
ATOM   4267  CE2 TYR B  94      -8.930 -12.972   2.793  1.00 78.96           C  
ANISOU 4267  CE2 TYR B  94     7423  15511   7066   1374    376   -180       C  
ATOM   4268  CZ  TYR B  94      -9.990 -13.792   3.111  1.00 81.50           C  
ANISOU 4268  CZ  TYR B  94     7558  16132   7277   1205    548    -86       C  
ATOM   4269  OH  TYR B  94     -11.133 -13.250   3.651  1.00 84.10           O  
ANISOU 4269  OH  TYR B  94     7705  16791   7459   1385    690    -76       O  
ATOM   4270  N   CYS B  95      -4.312 -18.046   1.600  1.00 70.26           N  
ANISOU 4270  N   CYS B  95     7101  13080   6515    207    129     29       N  
ATOM   4271  CA  CYS B  95      -3.350 -18.783   0.789  1.00 66.45           C  
ANISOU 4271  CA  CYS B  95     6728  12300   6220      7     57     44       C  
ATOM   4272  C   CYS B  95      -3.852 -18.837  -0.652  1.00 65.84           C  
ANISOU 4272  C   CYS B  95     6453  12306   6256   -159     51     11       C  
ATOM   4273  O   CYS B  95      -5.054 -18.944  -0.892  1.00 61.70           O  
ANISOU 4273  O   CYS B  95     5696  12088   5659   -245    150     13       O  
ATOM   4274  CB  CYS B  95      -3.146 -20.194   1.341  1.00 61.57           C  
ANISOU 4274  CB  CYS B  95     6241  11578   5575   -204    190    175       C  
ATOM   4275  SG  CYS B  95      -1.828 -21.133   0.536  1.00 96.45           S  
ANISOU 4275  SG  CYS B  95    10836  15595  10216   -409    115    200       S  
ATOM   4276  N   ASN B  96      -2.932 -18.762  -1.608  1.00 63.12           N  
ANISOU 4276  N   ASN B  96     6193  11708   6083   -187    -67    -29       N  
ATOM   4277  CA  ASN B  96      -3.306 -18.651  -3.012  1.00 68.66           C  
ANISOU 4277  CA  ASN B  96     6737  12498   6852   -265    -96    -70       C  
ATOM   4278  C   ASN B  96      -2.370 -19.389  -3.965  1.00 76.78           C  
ANISOU 4278  C   ASN B  96     7886  13238   8048   -452   -142    -68       C  
ATOM   4279  O   ASN B  96      -1.158 -19.438  -3.751  1.00 73.93           O  
ANISOU 4279  O   ASN B  96     7734  12547   7808   -412   -202    -55       O  
ATOM   4280  CB  ASN B  96      -3.411 -17.177  -3.412  1.00 68.15           C  
ANISOU 4280  CB  ASN B  96     6607  12502   6784     48   -172   -123       C  
ATOM   4281  CG  ASN B  96      -3.578 -16.986  -4.905  1.00 69.38           C  
ANISOU 4281  CG  ASN B  96     6656  12719   6987     46   -212   -142       C  
ATOM   4282  OD1 ASN B  96      -2.620 -16.683  -5.612  1.00 68.56           O  
ANISOU 4282  OD1 ASN B  96     6686  12337   7026    113   -270   -143       O  
ATOM   4283  ND2 ASN B  96      -4.799 -17.171  -5.393  1.00 77.75           N  
ANISOU 4283  ND2 ASN B  96     7464  14158   7920    -19   -178   -161       N  
ATOM   4284  N   VAL B  97      -2.948 -19.962  -5.016  1.00 82.82           N  
ANISOU 4284  N   VAL B  97     8504  14147   8818   -648   -116   -102       N  
ATOM   4285  CA  VAL B  97      -2.184 -20.667  -6.037  1.00 80.82           C  
ANISOU 4285  CA  VAL B  97     8353  13655   8702   -822   -147   -119       C  
ATOM   4286  C   VAL B  97      -2.565 -20.188  -7.434  1.00 81.36           C  
ANISOU 4286  C   VAL B  97     8280  13896   8738   -749   -214   -187       C  
ATOM   4287  O   VAL B  97      -3.708 -20.349  -7.868  1.00 89.71           O  
ANISOU 4287  O   VAL B  97     9094  15312   9678   -827   -201   -256       O  
ATOM   4288  CB  VAL B  97      -2.402 -22.190  -5.958  1.00 77.04           C  
ANISOU 4288  CB  VAL B  97     7873  13138   8261  -1186    -28   -113       C  
ATOM   4289  CG1 VAL B  97      -1.763 -22.882  -7.151  1.00 71.81           C  
ANISOU 4289  CG1 VAL B  97     7289  12271   7723  -1361    -55   -163       C  
ATOM   4290  CG2 VAL B  97      -1.849 -22.741  -4.654  1.00 78.46           C  
ANISOU 4290  CG2 VAL B  97     8247  13105   8460  -1214     56     -3       C  
ATOM   4291  N   LYS B  98      -1.601 -19.588  -8.126  1.00 70.37           N  
ANISOU 4291  N   LYS B  98     7033  12257   7448   -581   -279   -169       N  
ATOM   4292  CA  LYS B  98      -1.777 -19.182  -9.513  1.00 66.96           C  
ANISOU 4292  CA  LYS B  98     6529  11944   6971   -470   -323   -201       C  
ATOM   4293  C   LYS B  98      -1.298 -20.298 -10.429  1.00 66.76           C  
ANISOU 4293  C   LYS B  98     6581  11771   7013   -723   -321   -246       C  
ATOM   4294  O   LYS B  98      -0.097 -20.513 -10.569  1.00 68.91           O  
ANISOU 4294  O   LYS B  98     7071  11662   7452   -744   -311   -201       O  
ATOM   4295  CB  LYS B  98      -0.982 -17.909  -9.808  1.00 53.43           C  
ANISOU 4295  CB  LYS B  98     4944  10007   5351   -137   -338   -138       C  
ATOM   4296  CG  LYS B  98      -1.827 -16.661 -10.000  1.00 61.21           C  
ANISOU 4296  CG  LYS B  98     5781  11276   6200    184   -337   -118       C  
ATOM   4297  CD  LYS B  98      -2.171 -16.009  -8.675  1.00 66.26           C  
ANISOU 4297  CD  LYS B  98     6383  11971   6822    304   -317   -116       C  
ATOM   4298  CE  LYS B  98      -2.870 -14.676  -8.885  1.00 71.83           C  
ANISOU 4298  CE  LYS B  98     6974  12890   7428    660   -291    -85       C  
ATOM   4299  NZ  LYS B  98      -3.109 -13.960  -7.602  1.00 75.52           N  
ANISOU 4299  NZ  LYS B  98     7432  13370   7891    800   -262   -102       N  
ATOM   4300  N   ASP B  99      -2.238 -21.003 -11.050  1.00 66.31           N  
ANISOU 4300  N   ASP B  99     6333  12023   6840   -914   -328   -356       N  
ATOM   4301  CA  ASP B  99      -1.910 -22.125 -11.921  1.00 69.96           C  
ANISOU 4301  CA  ASP B  99     6851  12373   7357  -1176   -320   -444       C  
ATOM   4302  C   ASP B  99      -1.952 -21.716 -13.392  1.00 84.87           C  
ANISOU 4302  C   ASP B  99     8706  14415   9127  -1002   -398   -502       C  
ATOM   4303  O   ASP B  99      -2.973 -21.230 -13.881  1.00 93.37           O  
ANISOU 4303  O   ASP B  99     9554  15915  10007   -861   -466   -572       O  
ATOM   4304  CB  ASP B  99      -2.876 -23.286 -11.668  1.00 69.81           C  
ANISOU 4304  CB  ASP B  99     6639  12566   7318  -1537   -261   -575       C  
ATOM   4305  CG  ASP B  99      -2.488 -24.548 -12.417  1.00 72.78           C  
ANISOU 4305  CG  ASP B  99     7095  12764   7792  -1846   -223   -689       C  
ATOM   4306  OD1 ASP B  99      -1.925 -24.440 -13.526  1.00 76.36           O  
ANISOU 4306  OD1 ASP B  99     7649  13141   8224  -1751   -288   -724       O  
ATOM   4307  OD2 ASP B  99      -2.751 -25.651 -11.894  1.00 73.66           O  
ANISOU 4307  OD2 ASP B  99     7180  12801   8007  -2176   -104   -738       O  
ATOM   4308  N   PHE B 100      -0.841 -21.921 -14.094  1.00 86.98           N  
ANISOU 4308  N   PHE B 100     9200  14349   9499   -987   -382   -465       N  
ATOM   4309  CA  PHE B 100      -0.759 -21.598 -15.515  1.00 86.85           C  
ANISOU 4309  CA  PHE B 100     9200  14444   9354   -798   -428   -497       C  
ATOM   4310  C   PHE B 100      -1.036 -22.826 -16.376  1.00 84.54           C  
ANISOU 4310  C   PHE B 100     8853  14271   8999  -1085   -456   -693       C  
ATOM   4311  O   PHE B 100      -0.270 -23.140 -17.286  1.00 79.70           O  
ANISOU 4311  O   PHE B 100     8413  13461   8408  -1074   -438   -704       O  
ATOM   4312  CB  PHE B 100       0.618 -21.027 -15.862  1.00 81.54           C  
ANISOU 4312  CB  PHE B 100     8804  13337   8840   -587   -361   -342       C  
ATOM   4313  CG  PHE B 100       1.036 -19.877 -14.992  1.00 83.80           C  
ANISOU 4313  CG  PHE B 100     9152  13436   9254   -345   -322   -196       C  
ATOM   4314  CD1 PHE B 100       0.317 -18.694 -14.991  1.00 90.50           C  
ANISOU 4314  CD1 PHE B 100     9874  14549   9965    -35   -336   -145       C  
ATOM   4315  CD2 PHE B 100       2.158 -19.974 -14.186  1.00 80.64           C  
ANISOU 4315  CD2 PHE B 100     8926  12600   9113   -416   -274   -128       C  
ATOM   4316  CE1 PHE B 100       0.702 -17.632 -14.193  1.00 87.21           C  
ANISOU 4316  CE1 PHE B 100     9515  13935   9687    176   -286    -45       C  
ATOM   4317  CE2 PHE B 100       2.550 -18.916 -13.387  1.00 78.06           C  
ANISOU 4317  CE2 PHE B 100     8636  12110   8914   -205   -253    -49       C  
ATOM   4318  CZ  PHE B 100       1.821 -17.744 -13.391  1.00 80.03           C  
ANISOU 4318  CZ  PHE B 100     8769  12595   9043     79   -252    -15       C  
ATOM   4319  N   GLY B 101      -2.134 -23.516 -16.086  1.00 88.76           N  
ANISOU 4319  N   GLY B 101     9137  15118   9468  -1346   -485   -864       N  
ATOM   4320  CA  GLY B 101      -2.478 -24.734 -16.797  1.00 93.68           C  
ANISOU 4320  CA  GLY B 101     9673  15847  10073  -1669   -502  -1106       C  
ATOM   4321  C   GLY B 101      -2.924 -24.492 -18.226  1.00 94.64           C  
ANISOU 4321  C   GLY B 101     9681  16343   9935  -1485   -637  -1263       C  
ATOM   4322  O   GLY B 101      -2.638 -25.290 -19.118  1.00 91.23           O  
ANISOU 4322  O   GLY B 101     9319  15858   9486  -1634   -651  -1425       O  
ATOM   4323  N   ALA B 102      -3.629 -23.387 -18.444  1.00 94.10           N  
ANISOU 4323  N   ALA B 102     9445  16664   9646  -1134   -732  -1216       N  
ATOM   4324  CA  ALA B 102      -4.145 -23.058 -19.766  1.00 87.72           C  
ANISOU 4324  CA  ALA B 102     8513  16284   8531   -879   -873  -1345       C  
ATOM   4325  C   ALA B 102      -3.205 -22.123 -20.523  1.00 85.74           C  
ANISOU 4325  C   ALA B 102     8547  15836   8194   -445   -832  -1116       C  
ATOM   4326  O   ALA B 102      -3.527 -21.665 -21.620  1.00 89.32           O  
ANISOU 4326  O   ALA B 102     8955  16626   8358   -126   -921  -1151       O  
ATOM   4327  CB  ALA B 102      -5.525 -22.445 -19.654  1.00 87.82           C  
ANISOU 4327  CB  ALA B 102     8158  16878   8332   -714   -993  -1425       C  
ATOM   4328  N   ILE B 103      -2.054 -21.836 -19.918  1.00 81.81           N  
ANISOU 4328  N   ILE B 103     8331  14801   7952   -420   -686   -885       N  
ATOM   4329  CA  ILE B 103      -1.000 -21.030 -20.542  1.00 80.55           C  
ANISOU 4329  CA  ILE B 103     8453  14342   7811    -69   -588   -664       C  
ATOM   4330  C   ILE B 103      -1.399 -19.585 -20.858  1.00 83.74           C  
ANISOU 4330  C   ILE B 103     8812  14981   8023    437   -582   -490       C  
ATOM   4331  O   ILE B 103      -0.695 -18.646 -20.481  1.00 84.63           O  
ANISOU 4331  O   ILE B 103     9093  14759   8305    663   -448   -261       O  
ATOM   4332  CB  ILE B 103      -0.443 -21.703 -21.814  1.00 75.72           C  
ANISOU 4332  CB  ILE B 103     8001  13667   7101    -85   -584   -759       C  
ATOM   4333  CG1 ILE B 103      -0.052 -23.151 -21.518  1.00 71.21           C  
ANISOU 4333  CG1 ILE B 103     7485  12834   6736   -579   -563   -931       C  
ATOM   4334  CG2 ILE B 103       0.740 -20.919 -22.358  1.00 74.59           C  
ANISOU 4334  CG2 ILE B 103     8160  13144   7036    251   -425   -503       C  
ATOM   4335  CD1 ILE B 103       0.435 -23.907 -22.725  1.00 63.75           C  
ANISOU 4335  CD1 ILE B 103     6690  11834   5700   -626   -557  -1065       C  
ATOM   4336  N   ILE B 104      -2.518 -19.412 -21.555  1.00 79.97           N  
ANISOU 4336  N   ILE B 104     8102  15075   7206    620   -719   -610       N  
ATOM   4337  CA  ILE B 104      -2.997 -18.084 -21.925  1.00 74.66           C  
ANISOU 4337  CA  ILE B 104     7381  14672   6313   1141   -707   -436       C  
ATOM   4338  C   ILE B 104      -3.411 -17.271 -20.700  1.00 78.49           C  
ANISOU 4338  C   ILE B 104     7754  15136   6934   1203   -664   -319       C  
ATOM   4339  O   ILE B 104      -3.114 -16.080 -20.605  1.00 75.90           O  
ANISOU 4339  O   ILE B 104     7547  14642   6649   1573   -534    -85       O  
ATOM   4340  CB  ILE B 104      -4.183 -18.169 -22.904  1.00 75.07           C  
ANISOU 4340  CB  ILE B 104     7168  15414   5942   1331   -900   -621       C  
ATOM   4341  CG1 ILE B 104      -3.825 -19.069 -24.089  1.00 79.43           C  
ANISOU 4341  CG1 ILE B 104     7822  16022   6337   1245   -966   -797       C  
ATOM   4342  CG2 ILE B 104      -4.582 -16.782 -23.384  1.00 77.24           C  
ANISOU 4342  CG2 ILE B 104     7436  15945   5965   1941   -861   -395       C  
ATOM   4343  CD1 ILE B 104      -2.617 -18.600 -24.865  1.00 72.16           C  
ANISOU 4343  CD1 ILE B 104     7281  14704   5431   1550   -781   -551       C  
ATOM   4344  N   TYR B 105      -4.097 -17.919 -19.764  1.00 85.60           N  
ANISOU 4344  N   TYR B 105     8428  16185   7911    843   -747   -486       N  
ATOM   4345  CA  TYR B 105      -4.507 -17.259 -18.529  1.00 85.63           C  
ANISOU 4345  CA  TYR B 105     8329  16178   8029    877   -702   -397       C  
ATOM   4346  C   TYR B 105      -4.049 -18.034 -17.298  1.00 91.50           C  
ANISOU 4346  C   TYR B 105     9134  16564   9069    442   -650   -440       C  
ATOM   4347  O   TYR B 105      -3.242 -18.959 -17.398  1.00 89.04           O  
ANISOU 4347  O   TYR B 105     8987  15935   8911    155   -623   -491       O  
ATOM   4348  CB  TYR B 105      -6.023 -17.050 -18.501  1.00 81.80           C  
ANISOU 4348  CB  TYR B 105     7465  16322   7292    978   -829   -516       C  
ATOM   4349  CG  TYR B 105      -6.832 -18.319 -18.640  1.00 81.44           C  
ANISOU 4349  CG  TYR B 105     7139  16628   7176    574   -969   -821       C  
ATOM   4350  CD1 TYR B 105      -7.213 -19.050 -17.522  1.00 82.47           C  
ANISOU 4350  CD1 TYR B 105     7125  16715   7494    161   -940   -929       C  
ATOM   4351  CD2 TYR B 105      -7.224 -18.782 -19.889  1.00 87.47           C  
ANISOU 4351  CD2 TYR B 105     7780  17765   7692    614  -1114  -1013       C  
ATOM   4352  CE1 TYR B 105      -7.955 -20.208 -17.643  1.00 86.61           C  
ANISOU 4352  CE1 TYR B 105     7383  17515   8011   -229  -1021  -1215       C  
ATOM   4353  CE2 TYR B 105      -7.969 -19.940 -20.020  1.00 93.01           C  
ANISOU 4353  CE2 TYR B 105     8199  18771   8371    219  -1235  -1342       C  
ATOM   4354  CZ  TYR B 105      -8.332 -20.648 -18.893  1.00 92.69           C  
ANISOU 4354  CZ  TYR B 105     8011  18638   8569   -216  -1173  -1439       C  
ATOM   4355  OH  TYR B 105      -9.070 -21.803 -19.017  1.00 96.20           O  
ANISOU 4355  OH  TYR B 105     8166  19339   9046   -632  -1247  -1771       O  
ATOM   4356  N   ASP B 106      -4.567 -17.652 -16.135  1.00 99.43           N  
ANISOU 4356  N   ASP B 106    10015  17628  10134    424   -626   -408       N  
ATOM   4357  CA  ASP B 106      -4.176 -18.289 -14.883  1.00103.85           C  
ANISOU 4357  CA  ASP B 106    10646  17885  10929     85   -567   -418       C  
ATOM   4358  C   ASP B 106      -5.374 -18.591 -13.985  1.00 98.83           C  
ANISOU 4358  C   ASP B 106     9722  17595  10233    -90   -585   -517       C  
ATOM   4359  O   ASP B 106      -6.214 -17.726 -13.735  1.00 99.06           O  
ANISOU 4359  O   ASP B 106     9572  17933  10132    161   -599   -483       O  
ATOM   4360  CB  ASP B 106      -3.153 -17.424 -14.140  1.00111.71           C  
ANISOU 4360  CB  ASP B 106    11888  18428  12128    265   -468   -242       C  
ATOM   4361  CG  ASP B 106      -3.599 -15.981 -14.003  1.00121.93           C  
ANISOU 4361  CG  ASP B 106    13123  19865  13339    683   -434   -131       C  
ATOM   4362  OD1 ASP B 106      -4.374 -15.511 -14.864  1.00125.26           O  
ANISOU 4362  OD1 ASP B 106    13396  20663  13533    937   -476   -127       O  
ATOM   4363  OD2 ASP B 106      -3.170 -15.315 -13.036  1.00123.76           O  
ANISOU 4363  OD2 ASP B 106    13458  19839  13728    773   -366    -57       O  
ATOM   4364  N   TYR B 107      -5.441 -19.829 -13.506  1.00 93.58           N  
ANISOU 4364  N   TYR B 107     9020  16858   9678   -512   -557   -629       N  
ATOM   4365  CA  TYR B 107      -6.516 -20.268 -12.626  1.00 94.79           C  
ANISOU 4365  CA  TYR B 107     8912  17284   9820   -725   -521   -715       C  
ATOM   4366  C   TYR B 107      -6.109 -20.034 -11.174  1.00 98.31           C  
ANISOU 4366  C   TYR B 107     9512  17447  10396   -727   -410   -568       C  
ATOM   4367  O   TYR B 107      -5.065 -20.512 -10.732  1.00103.71           O  
ANISOU 4367  O   TYR B 107    10458  17704  11243   -863   -352   -499       O  
ATOM   4368  CB  TYR B 107      -6.804 -21.753 -12.862  1.00 95.23           C  
ANISOU 4368  CB  TYR B 107     8857  17373   9954  -1183   -498   -908       C  
ATOM   4369  CG  TYR B 107      -8.166 -22.229 -12.399  1.00103.05           C  
ANISOU 4369  CG  TYR B 107     9476  18758  10919  -1406   -461  -1057       C  
ATOM   4370  CD1 TYR B 107      -9.017 -21.398 -11.682  1.00103.67           C  
ANISOU 4370  CD1 TYR B 107     9360  19126  10904  -1201   -442   -991       C  
ATOM   4371  CD2 TYR B 107      -8.598 -23.519 -12.681  1.00111.84           C  
ANISOU 4371  CD2 TYR B 107    10426  19936  12130  -1830   -421  -1277       C  
ATOM   4372  CE1 TYR B 107     -10.258 -21.838 -11.260  1.00108.61           C  
ANISOU 4372  CE1 TYR B 107     9627  20109  11533  -1407   -383  -1125       C  
ATOM   4373  CE2 TYR B 107      -9.837 -23.968 -12.264  1.00116.84           C  
ANISOU 4373  CE2 TYR B 107    10694  20908  12793  -2059   -355  -1428       C  
ATOM   4374  CZ  TYR B 107     -10.663 -23.123 -11.554  1.00114.35           C  
ANISOU 4374  CZ  TYR B 107    10178  20889  12382  -1843   -336  -1345       C  
ATOM   4375  OH  TYR B 107     -11.896 -23.570 -11.140  1.00118.77           O  
ANISOU 4375  OH  TYR B 107    10352  21783  12993  -2072   -247  -1493       O  
ATOM   4376  N   ASP B 108      -6.933 -19.297 -10.436  1.00 94.22           N  
ANISOU 4376  N   ASP B 108     8827  17185   9787   -553   -385   -529       N  
ATOM   4377  CA  ASP B 108      -6.647 -19.006  -9.033  1.00 87.86           C  
ANISOU 4377  CA  ASP B 108     8156  16173   9055   -513   -290   -415       C  
ATOM   4378  C   ASP B 108      -7.327 -19.984  -8.081  1.00 85.29           C  
ANISOU 4378  C   ASP B 108     7700  15948   8759   -830   -167   -452       C  
ATOM   4379  O   ASP B 108      -8.538 -20.192  -8.147  1.00 88.45           O  
ANISOU 4379  O   ASP B 108     7782  16744   9082   -924   -141   -548       O  
ATOM   4380  CB  ASP B 108      -7.063 -17.577  -8.680  1.00 92.90           C  
ANISOU 4380  CB  ASP B 108     8733  16979   9586   -111   -299   -342       C  
ATOM   4381  CG  ASP B 108      -6.124 -16.538  -9.253  1.00 99.74           C  
ANISOU 4381  CG  ASP B 108     9816  17583  10499    211   -342   -257       C  
ATOM   4382  OD1 ASP B 108      -4.941 -16.866  -9.477  1.00105.34           O  
ANISOU 4382  OD1 ASP B 108    10772  17894  11360    123   -348   -229       O  
ATOM   4383  OD2 ASP B 108      -6.569 -15.392  -9.475  1.00101.49           O  
ANISOU 4383  OD2 ASP B 108     9958  17981  10624    559   -346   -212       O  
ATOM   4384  N   TYR B 109      -6.536 -20.582  -7.197  1.00 80.93           N  
ANISOU 4384  N   TYR B 109     7389  15037   8325   -978    -78   -369       N  
ATOM   4385  CA  TYR B 109      -7.075 -21.413  -6.128  1.00 82.82           C  
ANISOU 4385  CA  TYR B 109     7567  15315   8586  -1214     91   -343       C  
ATOM   4386  C   TYR B 109      -6.877 -20.707  -4.793  1.00 89.55           C  
ANISOU 4386  C   TYR B 109     8560  16092   9373   -974    142   -217       C  
ATOM   4387  O   TYR B 109      -5.758 -20.338  -4.442  1.00 93.33           O  
ANISOU 4387  O   TYR B 109     9313  16253   9895   -820     82   -148       O  
ATOM   4388  CB  TYR B 109      -6.393 -22.781  -6.103  1.00 77.72           C  
ANISOU 4388  CB  TYR B 109     7098  14334   8097  -1553    187   -331       C  
ATOM   4389  CG  TYR B 109      -6.644 -23.624  -7.331  1.00 75.66           C  
ANISOU 4389  CG  TYR B 109     6697  14139   7910  -1834    161   -496       C  
ATOM   4390  CD1 TYR B 109      -7.865 -24.253  -7.527  1.00 82.49           C  
ANISOU 4390  CD1 TYR B 109     7232  15324   8788  -2094    246   -646       C  
ATOM   4391  CD2 TYR B 109      -5.654 -23.800  -8.291  1.00 72.33           C  
ANISOU 4391  CD2 TYR B 109     6463  13463   7557  -1842     57   -525       C  
ATOM   4392  CE1 TYR B 109      -8.098 -25.029  -8.649  1.00 88.07           C  
ANISOU 4392  CE1 TYR B 109     7795  16106   9562  -2357    204   -851       C  
ATOM   4393  CE2 TYR B 109      -5.878 -24.574  -9.416  1.00 74.44           C  
ANISOU 4393  CE2 TYR B 109     6615  13803   7868  -2084     28   -703       C  
ATOM   4394  CZ  TYR B 109      -7.102 -25.187  -9.588  1.00 81.82           C  
ANISOU 4394  CZ  TYR B 109     7217  15067   8803  -2343     90   -880       C  
ATOM   4395  OH  TYR B 109      -7.329 -25.958 -10.705  1.00 81.31           O  
ANISOU 4395  OH  TYR B 109     7021  15089   8782  -2589     43  -1109       O  
ATOM   4396  N   TRP B 110      -7.962 -20.517  -4.050  1.00 86.34           N  
ANISOU 4396  N   TRP B 110     7951  15990   8863   -939    252   -207       N  
ATOM   4397  CA  TRP B 110      -7.891 -19.790  -2.787  1.00 76.34           C  
ANISOU 4397  CA  TRP B 110     6804  14706   7495   -682    300   -112       C  
ATOM   4398  C   TRP B 110      -8.049 -20.692  -1.567  1.00 84.14           C  
ANISOU 4398  C   TRP B 110     7874  15631   8466   -846    509    -12       C  
ATOM   4399  O   TRP B 110      -8.540 -21.816  -1.668  1.00 68.95           O  
ANISOU 4399  O   TRP B 110     5835  13739   6623  -1171    664    -16       O  
ATOM   4400  CB  TRP B 110      -8.929 -18.666  -2.755  1.00 74.16           C  
ANISOU 4400  CB  TRP B 110     6283  14810   7083   -415    284   -147       C  
ATOM   4401  CG  TRP B 110      -8.648 -17.579  -3.741  1.00 74.60           C  
ANISOU 4401  CG  TRP B 110     6333  14880   7133   -146    114   -191       C  
ATOM   4402  CD1 TRP B 110      -9.202 -17.431  -4.977  1.00 81.88           C  
ANISOU 4402  CD1 TRP B 110     7030  16050   8030   -134     29   -267       C  
ATOM   4403  CD2 TRP B 110      -7.732 -16.490  -3.577  1.00 74.24           C  
ANISOU 4403  CD2 TRP B 110     6519  14579   7108    164     28   -161       C  
ATOM   4404  NE1 TRP B 110      -8.692 -16.313  -5.593  1.00 85.24           N  
ANISOU 4404  NE1 TRP B 110     7560  16381   8445    190    -79   -244       N  
ATOM   4405  CE2 TRP B 110      -7.787 -15.718  -4.753  1.00 78.19           C  
ANISOU 4405  CE2 TRP B 110     6941  15159   7610    356    -68   -186       C  
ATOM   4406  CE3 TRP B 110      -6.873 -16.091  -2.549  1.00 71.11           C  
ANISOU 4406  CE3 TRP B 110     6381  13902   6736    304     26   -132       C  
ATOM   4407  CZ2 TRP B 110      -7.016 -14.571  -4.931  1.00 74.57           C  
ANISOU 4407  CZ2 TRP B 110     6658  14461   7215    662   -121   -164       C  
ATOM   4408  CZ3 TRP B 110      -6.108 -14.952  -2.726  1.00 66.97           C  
ANISOU 4408  CZ3 TRP B 110     6001  13161   6285    585    -61   -158       C  
ATOM   4409  CH2 TRP B 110      -6.184 -14.206  -3.908  1.00 66.47           C  
ANISOU 4409  CH2 TRP B 110     5860  13135   6261    751   -112   -164       C  
ATOM   4410  N   GLY B 111      -7.617 -20.188  -0.416  1.00 66.83           N  
ANISOU 4410  N   GLY B 111     5884  13340   6167   -606    525     71       N  
ATOM   4411  CA  GLY B 111      -7.747 -20.908   0.836  1.00 73.47           C  
ANISOU 4411  CA  GLY B 111     6839  14144   6931   -667    733    197       C  
ATOM   4412  C   GLY B 111      -8.950 -20.429   1.625  1.00 80.57           C  
ANISOU 4412  C   GLY B 111     7544  15393   7674   -533    885    221       C  
ATOM   4413  O   GLY B 111      -9.646 -19.501   1.210  1.00 84.55           O  
ANISOU 4413  O   GLY B 111     7825  16165   8136   -380    810    134       O  
ATOM   4414  N   GLN B 112      -9.197 -21.065   2.766  1.00 78.17           N  
ANISOU 4414  N   GLN B 112     7332  15088   7279   -565   1118    355       N  
ATOM   4415  CA  GLN B 112     -10.326 -20.703   3.614  1.00 80.89           C  
ANISOU 4415  CA  GLN B 112     7512  15751   7472   -437   1310    400       C  
ATOM   4416  C   GLN B 112     -10.072 -19.377   4.325  1.00 77.58           C  
ANISOU 4416  C   GLN B 112     7221  15401   6855     -8   1176    366       C  
ATOM   4417  O   GLN B 112     -11.009 -18.655   4.668  1.00 76.61           O  
ANISOU 4417  O   GLN B 112     6914  15575   6620    165   1251    343       O  
ATOM   4418  CB  GLN B 112     -10.597 -21.806   4.638  1.00 93.40           C  
ANISOU 4418  CB  GLN B 112     9196  17280   9013   -576   1642    583       C  
ATOM   4419  CG  GLN B 112     -10.837 -23.178   4.027  1.00100.48           C  
ANISOU 4419  CG  GLN B 112     9980  18050  10146  -1021   1828    608       C  
ATOM   4420  CD  GLN B 112     -12.167 -23.278   3.306  1.00107.55           C  
ANISOU 4420  CD  GLN B 112    10419  19261  11183  -1264   1927    480       C  
ATOM   4421  OE1 GLN B 112     -12.334 -24.099   2.404  1.00114.15           O  
ANISOU 4421  OE1 GLN B 112    11092  20038  12242  -1620   1956    383       O  
ATOM   4422  NE2 GLN B 112     -13.124 -22.449   3.708  1.00109.58           N  
ANISOU 4422  NE2 GLN B 112    10455  19867  11314  -1065   1977    458       N  
ATOM   4423  N   GLY B 113      -8.800 -19.061   4.544  1.00 74.36           N  
ANISOU 4423  N   GLY B 113     7116  14716   6422    160    983    342       N  
ATOM   4424  CA  GLY B 113      -8.425 -17.823   5.201  1.00 74.75           C  
ANISOU 4424  CA  GLY B 113     7297  14782   6324    544    841    257       C  
ATOM   4425  C   GLY B 113      -8.212 -18.002   6.690  1.00 80.39           C  
ANISOU 4425  C   GLY B 113     8247  15501   6797    740    951    343       C  
ATOM   4426  O   GLY B 113      -9.021 -18.636   7.367  1.00 86.67           O  
ANISOU 4426  O   GLY B 113     8993  16463   7473    680   1222    486       O  
ATOM   4427  N   THR B 114      -7.118 -17.447   7.201  1.00 82.78           N  
ANISOU 4427  N   THR B 114     8799  15627   7028    984    748    249       N  
ATOM   4428  CA  THR B 114      -6.825 -17.516   8.629  1.00 93.47           C  
ANISOU 4428  CA  THR B 114    10391  17020   8103   1236    800    294       C  
ATOM   4429  C   THR B 114      -6.670 -16.126   9.234  1.00 96.48           C  
ANISOU 4429  C   THR B 114    10825  17486   8348   1606    643     90       C  
ATOM   4430  O   THR B 114      -6.122 -15.218   8.605  1.00 90.27           O  
ANISOU 4430  O   THR B 114    10008  16557   7733   1673    424    -99       O  
ATOM   4431  CB  THR B 114      -5.556 -18.339   8.919  1.00 96.61           C  
ANISOU 4431  CB  THR B 114    11065  17146   8498   1212    700    352       C  
ATOM   4432  OG1 THR B 114      -4.467 -17.836   8.136  1.00 97.63           O  
ANISOU 4432  OG1 THR B 114    11228  17021   8848   1202    407    178       O  
ATOM   4433  CG2 THR B 114      -5.784 -19.804   8.586  1.00 96.46           C  
ANISOU 4433  CG2 THR B 114    11038  17035   8577    878    929    579       C  
ATOM   4434  N   GLN B 115      -7.158 -15.971  10.460  1.00 97.04           N  
ANISOU 4434  N   GLN B 115    10982  17774   8116   1851    782    126       N  
ATOM   4435  CA  GLN B 115      -7.107 -14.690  11.151  1.00 91.90           C  
ANISOU 4435  CA  GLN B 115    10388  17222   7309   2211    664    -89       C  
ATOM   4436  C   GLN B 115      -5.795 -14.526  11.909  1.00 88.41           C  
ANISOU 4436  C   GLN B 115    10222  16623   6747   2433    421   -249       C  
ATOM   4437  O   GLN B 115      -5.333 -15.452  12.575  1.00 86.21           O  
ANISOU 4437  O   GLN B 115    10137  16326   6291   2456    456   -115       O  
ATOM   4438  CB  GLN B 115      -8.290 -14.555  12.111  1.00 93.94           C  
ANISOU 4438  CB  GLN B 115    10601  17814   7278   2394    934      4       C  
ATOM   4439  CG  GLN B 115      -8.337 -13.232  12.854  1.00 99.96           C  
ANISOU 4439  CG  GLN B 115    11424  18693   7865   2776    840   -231       C  
ATOM   4440  CD  GLN B 115      -8.590 -12.054  11.935  1.00103.66           C  
ANISOU 4440  CD  GLN B 115    11689  19115   8582   2794    735   -409       C  
ATOM   4441  OE1 GLN B 115      -8.021 -10.978  12.116  1.00102.75           O  
ANISOU 4441  OE1 GLN B 115    11657  18888   8497   3019    550   -668       O  
ATOM   4442  NE2 GLN B 115      -9.455 -12.250  10.947  1.00108.29           N  
ANISOU 4442  NE2 GLN B 115    12004  19789   9350   2569    864   -277       N  
ATOM   4443  N   VAL B 116      -5.196 -13.346  11.793  1.00 90.21           N  
ANISOU 4443  N   VAL B 116    10456  16734   7085   2603    184   -541       N  
ATOM   4444  CA  VAL B 116      -3.972 -13.025  12.515  1.00 91.14           C  
ANISOU 4444  CA  VAL B 116    10780  16728   7119   2824    -77   -774       C  
ATOM   4445  C   VAL B 116      -4.138 -11.701  13.253  1.00 94.77           C  
ANISOU 4445  C   VAL B 116    11259  17304   7446   3157   -150  -1066       C  
ATOM   4446  O   VAL B 116      -4.318 -10.653  12.631  1.00 98.47           O  
ANISOU 4446  O   VAL B 116    11590  17677   8149   3168   -184  -1231       O  
ATOM   4447  CB  VAL B 116      -2.758 -12.934  11.569  1.00 84.38           C  
ANISOU 4447  CB  VAL B 116     9912  15518   6630   2659   -325   -910       C  
ATOM   4448  CG1 VAL B 116      -1.540 -12.414  12.315  1.00 76.88           C  
ANISOU 4448  CG1 VAL B 116     9112  14463   5637   2897   -611  -1223       C  
ATOM   4449  CG2 VAL B 116      -2.468 -14.290  10.947  1.00 74.28           C  
ANISOU 4449  CG2 VAL B 116     8654  14111   5457   2359   -265   -646       C  
ATOM   4450  N   THR B 117      -4.084 -11.754  14.579  1.00 90.83           N  
ANISOU 4450  N   THR B 117    10942  17010   6561   3448   -156  -1126       N  
ATOM   4451  CA  THR B 117      -4.270 -10.562  15.396  1.00 91.87           C  
ANISOU 4451  CA  THR B 117    11112  17274   6521   3782   -213  -1426       C  
ATOM   4452  C   THR B 117      -2.994 -10.199  16.151  1.00 92.44           C  
ANISOU 4452  C   THR B 117    11353  17267   6504   4009   -539  -1778       C  
ATOM   4453  O   THR B 117      -2.451 -11.013  16.896  1.00 89.31           O  
ANISOU 4453  O   THR B 117    11134  16972   5829   4122   -617  -1709       O  
ATOM   4454  CB  THR B 117      -5.421 -10.743  16.406  1.00 95.95           C  
ANISOU 4454  CB  THR B 117    11687  18158   6612   3994     66  -1256       C  
ATOM   4455  OG1 THR B 117      -6.603 -11.176  15.720  1.00 88.40           O  
ANISOU 4455  OG1 THR B 117    10533  17293   5761   3760    368   -942       O  
ATOM   4456  CG2 THR B 117      -5.709  -9.436  17.128  1.00 91.68           C  
ANISOU 4456  CG2 THR B 117    11170  17743   5922   4331     29  -1578       C  
ATOM   4457  N   VAL B 118      -2.521  -8.973  15.950  1.00 93.02           N  
ANISOU 4457  N   VAL B 118    11359  17160   6824   4087   -721  -2163       N  
ATOM   4458  CA  VAL B 118      -1.337  -8.483  16.646  1.00 97.96           C  
ANISOU 4458  CA  VAL B 118    12089  17713   7418   4291  -1045  -2583       C  
ATOM   4459  C   VAL B 118      -1.724  -7.533  17.778  1.00104.50           C  
ANISOU 4459  C   VAL B 118    12998  18767   7940   4658  -1055  -2894       C  
ATOM   4460  O   VAL B 118      -2.349  -6.497  17.546  1.00 92.96           O  
ANISOU 4460  O   VAL B 118    11438  17254   6629   4703   -939  -3031       O  
ATOM   4461  CB  VAL B 118      -0.367  -7.770  15.682  1.00 86.77           C  
ANISOU 4461  CB  VAL B 118    10539  15886   6545   4109  -1241  -2860       C  
ATOM   4462  CG1 VAL B 118       0.789  -7.151  16.451  1.00 89.21           C  
ANISOU 4462  CG1 VAL B 118    10905  16133   6860   4316  -1571  -3364       C  
ATOM   4463  CG2 VAL B 118       0.145  -8.741  14.631  1.00 83.39           C  
ANISOU 4463  CG2 VAL B 118    10057  15241   6386   3778  -1253  -2581       C  
ATOM   4464  N   SER B 119      -1.351  -7.897  19.001  1.00 95.92           N  
ANISOU 4464  N   SER B 119    12101  17937   6406   4946  -1189  -3002       N  
ATOM   4465  CA  SER B 119      -1.693  -7.109  20.183  1.00124.80           C  
ANISOU 4465  CA  SER B 119    15868  21856   9694   5331  -1208  -3304       C  
ATOM   4466  C   SER B 119      -1.004  -5.748  20.181  1.00127.73           C  
ANISOU 4466  C   SER B 119    16159  22007  10367   5408  -1453  -3891       C  
ATOM   4467  O   SER B 119       0.208  -5.657  20.374  1.00129.38           O  
ANISOU 4467  O   SER B 119    16371  22098  10688   5434  -1784  -4233       O  
ATOM   4468  CB  SER B 119      -1.327  -7.874  21.457  1.00125.29           C  
ANISOU 4468  CB  SER B 119    16116  22118   9370   5565  -1302  -3204       C  
ATOM   4469  OG  SER B 119      -1.989  -9.126  21.512  1.00124.44           O  
ANISOU 4469  OG  SER B 119    16095  22163   9022   5497  -1020  -2658       O  
ATOM   4470  N   SER B 120      -1.784  -4.694  19.966  1.00129.48           N  
ANISOU 4470  N   SER B 120    16293  22160  10744   5443  -1274  -4009       N  
ATOM   4471  CA  SER B 120      -1.248  -3.337  19.942  1.00132.59           C  
ANISOU 4471  CA  SER B 120    16613  22297  11468   5508  -1431  -4558       C  
ATOM   4472  C   SER B 120      -0.806  -2.890  21.333  1.00138.85           C  
ANISOU 4472  C   SER B 120    17513  23236  12008   5805  -1656  -4944       C  
ATOM   4473  O   SER B 120       0.387  -2.759  21.603  1.00108.72           O  
ANISOU 4473  O   SER B 120    13665  19281   8362   5796  -1982  -5290       O  
ATOM   4474  CB  SER B 120      -2.284  -2.360  19.381  1.00131.93           C  
ANISOU 4474  CB  SER B 120    16421  22089  11617   5492  -1134  -4510       C  
TER    4475      SER B 120                                                      
HETATM 4476  CAA XQC A1401      -4.584 -11.320 -51.709  1.00 64.07           C  
HETATM 4477  CAB XQC A1401      -4.657 -12.841 -51.623  1.00 67.24           C  
HETATM 4478  CAC XQC A1401      -3.575 -13.473 -52.490  1.00 67.04           C  
HETATM 4479  CAD XQC A1401      -6.046 -13.360 -52.005  1.00 67.67           C  
HETATM 4480  CAE XQC A1401      -6.246 -13.514 -53.501  1.00 65.89           C  
HETATM 4481  CAF XQC A1401      -6.404 -12.402 -54.324  1.00 65.48           C  
HETATM 4482  CAG XQC A1401      -6.595 -12.561 -55.691  1.00 69.94           C  
HETATM 4483  CAH XQC A1401      -6.643 -13.837 -56.242  1.00 74.86           C  
HETATM 4484  CAJ XQC A1401      -6.497 -14.950 -55.423  1.00 72.28           C  
HETATM 4485  CAK XQC A1401      -6.307 -14.789 -54.056  1.00 66.37           C  
HETATM 4486  CAM XQC A1401      -3.112 -12.826 -49.670  1.00 66.87           C  
HETATM 4487  CAN XQC A1401      -2.820 -13.641 -48.416  1.00 67.52           C  
HETATM 4488  CAP XQC A1401      -1.512 -13.205 -47.874  1.00 68.74           C  
HETATM 4489  CAQ XQC A1401      -1.339 -12.990 -46.512  1.00 71.58           C  
HETATM 4490  CAR XQC A1401      -0.100 -12.581 -46.029  1.00 75.68           C  
HETATM 4491  CAS XQC A1401       0.965 -12.395 -46.904  1.00 74.39           C  
HETATM 4492  CAU XQC A1401       0.792 -12.615 -48.259  1.00 75.98           C  
HETATM 4493  CAW XQC A1401      -0.445 -13.021 -48.744  1.00 71.66           C  
HETATM 4494  NAL XQC A1401      -4.385 -13.209 -50.249  1.00 64.63           N  
HETATM 4495  OAI XQC A1401      -6.832 -13.996 -57.582  1.00 77.74           O  
HETATM 4496  OAO XQC A1401      -3.872 -13.464 -47.460  1.00 65.32           O  
HETATM 4497  OAT XQC A1401       2.180 -11.996 -46.431  1.00 64.73           O  
HETATM 4498  OAV XQC A1401       1.833 -12.434 -49.118  1.00 78.60           O  
HETATM 4499 NA    NA A1402      -6.467  -4.741 -62.167  1.00 96.70          NA  
HETATM 4500  C10 1WV A1403     -13.605 -21.491 -50.627  1.00 97.37           C  
HETATM 4501  C13 1WV A1403     -12.435 -20.635 -54.201  1.00108.76           C  
HETATM 4502  C17 1WV A1403     -12.607 -21.502 -57.826  1.00115.90           C  
HETATM 4503  C20 1WV A1403     -14.085 -22.821 -59.361  1.00114.99           C  
HETATM 4504  C07 1WV A1403     -13.207 -22.476 -47.468  1.00 89.85           C  
HETATM 4505  C08 1WV A1403     -14.193 -21.561 -48.199  1.00 94.25           C  
HETATM 4506  C09 1WV A1403     -13.582 -20.706 -49.313  1.00 96.58           C  
HETATM 4507  C11 1WV A1403     -12.996 -20.652 -51.755  1.00 97.96           C  
HETATM 4508  C12 1WV A1403     -13.035 -21.457 -53.058  1.00104.28           C  
HETATM 4509  C14 1WV A1403     -12.484 -21.448 -55.499  1.00112.56           C  
HETATM 4510  O15 1WV A1403     -12.439 -22.677 -55.473  1.00115.09           O  
HETATM 4511  O16 1WV A1403     -12.551 -20.700 -56.638  1.00113.95           O  
HETATM 4512  C18 1WV A1403     -14.045 -21.968 -58.090  1.00115.52           C  
HETATM 4513  O19 1WV A1403     -14.897 -20.832 -58.257  1.00112.01           O  
HETATM 4514  O21 1WV A1403     -13.242 -23.965 -59.204  1.00114.01           O  
HETATM 4515  O   HOH A1501      -4.929  -4.771 -60.340  1.00 47.16           O  
HETATM 4516  O   HOH A1502       1.640 -15.057 -54.587  1.00123.27           O  
CONECT 1908 4499                                                                
CONECT 1940 2622                                                                
CONECT 2566 4499                                                                
CONECT 2568 2616                                                                
CONECT 2589 4499                                                                
CONECT 2614 4499                                                                
CONECT 2616 2568                                                                
CONECT 2622 1940                                                                
CONECT 3721 4275                                                                
CONECT 4275 3721                                                                
CONECT 4476 4477                                                                
CONECT 4477 4476 4478 4479 4494                                                 
CONECT 4478 4477                                                                
CONECT 4479 4477 4480                                                           
CONECT 4480 4479 4481 4485                                                      
CONECT 4481 4480 4482                                                           
CONECT 4482 4481 4483                                                           
CONECT 4483 4482 4484 4495                                                      
CONECT 4484 4483 4485                                                           
CONECT 4485 4480 4484                                                           
CONECT 4486 4487 4494                                                           
CONECT 4487 4486 4488 4496                                                      
CONECT 4488 4487 4489 4493                                                      
CONECT 4489 4488 4490                                                           
CONECT 4490 4489 4491                                                           
CONECT 4491 4490 4492 4497                                                      
CONECT 4492 4491 4493 4498                                                      
CONECT 4493 4488 4492                                                           
CONECT 4494 4477 4486                                                           
CONECT 4495 4483                                                                
CONECT 4496 4487                                                                
CONECT 4497 4491                                                                
CONECT 4498 4492                                                                
CONECT 4499 1908 2566 2589 2614                                                 
CONECT 4499 4515                                                                
CONECT 4500 4506 4507                                                           
CONECT 4501 4508 4509                                                           
CONECT 4502 4511 4512                                                           
CONECT 4503 4512 4514                                                           
CONECT 4504 4505                                                                
CONECT 4505 4504 4506                                                           
CONECT 4506 4500 4505                                                           
CONECT 4507 4500 4508                                                           
CONECT 4508 4501 4507                                                           
CONECT 4509 4501 4510 4511                                                      
CONECT 4510 4509                                                                
CONECT 4511 4502 4509                                                           
CONECT 4512 4502 4503 4513                                                      
CONECT 4513 4512                                                                
CONECT 4514 4503                                                                
CONECT 4515 4499                                                                
MASTER      461    0    3   27   17    0    6    6 4514    2   51   47          
END