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HEADER    PROTEIN BINDING                         14-OCT-10   3P8M              
TITLE     HUMAN DYNEIN LIGHT CHAIN (DYNLL2) IN COMPLEX WITH AN IN VITRO EVOLVED 
TITLE    2 PEPTIDE DIMERIZED BY LEUCINE ZIPPER                                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: DYNEIN LIGHT CHAIN 2;                                      
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: 8 KDA DYNEIN LIGHT CHAIN B, DLC8B, DYNEIN LIGHT CHAIN LC8-  
COMPND   5 TYPE 2;                                                              
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: GENERAL CONTROL PROTEIN GCN4;                              
COMPND   9 CHAIN: D, C;                                                         
COMPND  10 SYNONYM: AMINO ACID BIOSYNTHESIS REGULATORY PROTEIN;                 
COMPND  11 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: DYNLL2, DLC2;                                                  
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)STAR;                             
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET-15B;                                  
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;                       
SOURCE  13 ORGANISM_COMMON: BREWER'S YEAST,LAGER BEER YEAST,YEAST;              
SOURCE  14 ORGANISM_TAXID: 4932;                                                
SOURCE  15 GENE: GCN4, AAS3, ARG9, YEL009C;                                     
SOURCE  16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  18 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)STAR;                             
SOURCE  19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  20 EXPRESSION_SYSTEM_PLASMID: MODIFIED PET                              
KEYWDS    PHAGE DISPLAY, LEUCINE ZIPPER, HUB PROTEIN, PROTEIN BINDING           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    P.RAPALI,L.RADNAI,D.SUVEGES,C.HETENYI,V.HARMAT,F.TOLGYESI,            
AUTHOR   2 W.Y.WAHLGREN,G.KATONA,L.NYITRAY,G.PAL                                
REVDAT   1   31-AUG-11 3P8M    0                                                
JRNL        AUTH   P.RAPALI,L.RADNAI,D.SUVEGES,V.HARMAT,F.TOLGYESI,             
JRNL        AUTH 2 W.Y.WAHLGREN,G.KATONA,L.NYITRAY,G.PAL                        
JRNL        TITL   DIRECTED EVOLUTION REVEALS THE BINDING MOTIF PREFERENCE OF   
JRNL        TITL 2 THE LC8/DYNLL HUB PROTEIN AND PREDICTS LARGE NUMBERS OF      
JRNL        TITL 3 NOVEL BINDERS IN THE HUMAN PROTEOME.                         
JRNL        REF    PLOS ONE                      V.   6 18818 2011              
JRNL        REFN                   ESSN 1932-6203                               
JRNL        PMID   21533121                                                     
JRNL        DOI    10.1371/JOURNAL.PONE.0018818                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0102                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 42.31                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 7886                           
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.250                           
REMARK   3   R VALUE            (WORKING SET) : 0.248                           
REMARK   3   FREE R VALUE                     : 0.295                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.700                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 385                             
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.90                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.98                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 586                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 96.72                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3280                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 33                           
REMARK   3   BIN FREE R VALUE                    : 0.4040                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1975                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 41                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 52.80                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -3.09000                                             
REMARK   3    B22 (A**2) : 1.47000                                              
REMARK   3    B33 (A**2) : 1.62000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.451         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.391         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 46.408        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.915                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.894                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2037 ; 0.011 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  1315 ; 0.005 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2756 ; 1.119 ; 1.947       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  3227 ; 2.416 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   265 ; 5.772 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    92 ;35.696 ;25.326       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   344 ;19.644 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     5 ;23.120 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   307 ; 0.063 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2315 ; 0.003 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   408 ; 0.002 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1291 ; 0.175 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   534 ; 0.053 ; 1.500       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2050 ; 0.305 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   746 ; 0.523 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   701 ; 0.837 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : 3                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : A B                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A      5       A      88      3                      
REMARK   3           1     B      5       B      88      3                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   1    A    (A):    494 ;  0.03 ;  0.05           
REMARK   3   LOOSE POSITIONAL   1    B    (A):    553 ;  0.03 ;  5.00           
REMARK   3   TIGHT THERMAL      1    A (A**2):    494 ;  0.08 ;  0.50           
REMARK   3   LOOSE THERMAL      1    B (A**2):    553 ;  0.10 ; 10.00           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 2                                  
REMARK   3     CHAIN NAMES                    : D C                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     D    131       D     138      3                      
REMARK   3           1     C    131       C     138      3                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   2    D    (A):     46 ;  0.03 ;  0.05           
REMARK   3   LOOSE POSITIONAL   2    C    (A):     49 ;  0.03 ;  5.00           
REMARK   3   TIGHT THERMAL      2    D (A**2):     46 ;  0.08 ;  0.50           
REMARK   3   LOOSE THERMAL      2    C (A**2):     49 ;  0.09 ; 10.00           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 3                                  
REMARK   3     CHAIN NAMES                    : D C                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     D    144       D     167      3                      
REMARK   3           1     C    144       C     167      3                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   3    D    (A):    142 ;  0.04 ;  0.05           
REMARK   3   LOOSE POSITIONAL   3    C    (A):    146 ;  0.06 ;  5.00           
REMARK   3   TIGHT THERMAL      3    D (A**2):    142 ;  0.05 ;  0.50           
REMARK   3   LOOSE THERMAL      3    C (A**2):    146 ;  0.07 ; 10.00           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 6                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     3        A    89                          
REMARK   3    ORIGIN FOR THE GROUP (A):   3.3994  23.1894  10.4440              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1926 T22:   0.2670                                     
REMARK   3      T33:   0.1938 T12:  -0.0737                                     
REMARK   3      T13:   0.0238 T23:  -0.0875                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.2897 L22:   4.0868                                     
REMARK   3      L33:   4.3355 L12:  -0.3556                                     
REMARK   3      L13:   0.7182 L23:   0.7604                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0449 S12:  -0.2660 S13:   0.1238                       
REMARK   3      S21:   0.5119 S22:  -0.0707 S23:  -0.0328                       
REMARK   3      S31:  -0.3797 S32:  -0.0673 S33:   0.0258                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B     3        B    89                          
REMARK   3    ORIGIN FOR THE GROUP (A):   4.9480   5.2167   0.7907              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2118 T22:   0.3339                                     
REMARK   3      T33:   0.5872 T12:  -0.0279                                     
REMARK   3      T13:  -0.0704 T23:  -0.1880                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.1608 L22:   4.1802                                     
REMARK   3      L33:   4.3899 L12:  -0.1169                                     
REMARK   3      L13:  -1.9109 L23:   1.8421                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1217 S12:   0.3255 S13:  -1.3168                       
REMARK   3      S21:   0.1146 S22:   0.2544 S23:  -0.3178                       
REMARK   3      S31:   0.8667 S32:   0.0943 S33:  -0.1327                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D   130        D   139                          
REMARK   3    ORIGIN FOR THE GROUP (A):  14.2964  16.1350   7.7514              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0784 T22:   0.5328                                     
REMARK   3      T33:   0.5018 T12:  -0.0576                                     
REMARK   3      T13:   0.0456 T23:  -0.1369                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.4973 L22:   7.6947                                     
REMARK   3      L33:   0.7988 L12:   2.8792                                     
REMARK   3      L13:  -0.6593 L23:   2.0110                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2404 S12:   0.3878 S13:  -0.1191                       
REMARK   3      S21:   0.5806 S22:  -0.2408 S23:   0.2467                       
REMARK   3      S31:   0.1310 S32:  -0.1219 S33:   0.0004                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D   140        D   172                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -1.2632   6.1215  46.0130              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4307 T22:   0.2847                                     
REMARK   3      T33:   0.5319 T12:   0.0131                                     
REMARK   3      T13:   0.0251 T23:  -0.0416                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  14.8993 L22:   5.5659                                     
REMARK   3      L33:  13.2811 L12:   0.9239                                     
REMARK   3      L13:  -7.9179 L23:  -1.9598                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.8170 S12:  -0.3303 S13:   0.9704                       
REMARK   3      S21:   0.2462 S22:   0.0858 S23:   0.4338                       
REMARK   3      S31:  -0.7679 S32:   0.3303 S33:  -0.9028                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C   131        C   139                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -5.5963  11.8134   4.8656              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0830 T22:   0.3819                                     
REMARK   3      T33:   0.6278 T12:  -0.0095                                     
REMARK   3      T13:   0.0180 T23:  -0.2058                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  16.8751 L22:   8.4541                                     
REMARK   3      L33:   1.2078 L12:  -1.3916                                     
REMARK   3      L13:   1.3468 L23:   2.9155                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.5451 S12:   0.6379 S13:  -2.2845                       
REMARK   3      S21:  -0.1365 S22:  -0.4279 S23:   0.8404                       
REMARK   3      S31:   0.0209 S32:  -0.0052 S33:  -0.1172                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C   140        C   172                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -5.5012  12.2128  43.1662              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8320 T22:   0.5867                                     
REMARK   3      T33:   0.7852 T12:   0.0035                                     
REMARK   3      T13:   0.0977 T23:   0.0786                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.7804 L22:   3.7290                                     
REMARK   3      L33:  34.7805 L12:   1.2551                                     
REMARK   3      L13:  -6.3558 L23:   2.2053                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4593 S12:   0.2747 S13:   0.3172                       
REMARK   3      S21:   0.0521 S22:  -0.5625 S23:   1.1145                       
REMARK   3      S31:  -1.2478 S32:  -1.0099 S33:   1.0218                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 3P8M COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-NOV-10.                  
REMARK 100 THE RCSB ID CODE IS RCSB062093.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-MAR-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU RUH2R                       
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : CONFOCAL MIRRORS                   
REMARK 200  OPTICS                         : OSMIC BLUE                         
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV++                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : CRYSTALCLEAR                       
REMARK 200  DATA SCALING SOFTWARE          : CRYSTALCLEAR                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 8273                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 56.760                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.4                               
REMARK 200  DATA REDUNDANCY                : 3.230                              
REMARK 200  R MERGE                    (I) : 0.13100                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 6.4000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.00                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.12                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.57600                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.500                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ENTRY 2XQQ                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 58.60                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.97                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG8000, 0.2 M MGCL2, 0.1 M TRIS,    
REMARK 280  PH 7.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K             
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       26.91950            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       50.83850            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       34.20750            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       50.83850            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       26.91950            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       34.20750            
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: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 6400 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 12830 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -42.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, D, C                            
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     GLY A    -2                                                      
REMARK 465     SER A    -1                                                      
REMARK 465     HIS A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     SER A     2                                                      
REMARK 465     GLY B    -2                                                      
REMARK 465     SER B    -1                                                      
REMARK 465     HIS B     0                                                      
REMARK 465     MET B     1                                                      
REMARK 465     SER B     2                                                      
REMARK 465     GLY D   173                                                      
REMARK 465     GLU D   174                                                      
REMARK 465     ARG D   175                                                      
REMARK 465     GLY C   130                                                      
REMARK 465     GLY C   173                                                      
REMARK 465     GLU C   174                                                      
REMARK 465     ARG C   175                                                      
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   3    CG   OD1  OD2                                       
REMARK 470     ARG A   4    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A   5    CG   CD   CE   NZ                                   
REMARK 470     LYS A   9    CE   NZ                                             
REMARK 470     LYS A  36    CE   NZ                                             
REMARK 470     ARG A  60    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN A  80    CG   CD   OE1  NE2                                  
REMARK 470     ASP B   3    CG   OD1  OD2                                       
REMARK 470     ARG B   4    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B   5    CG   CD   CE   NZ                                   
REMARK 470     LYS B   9    CD   CE   NZ                                        
REMARK 470     GLN B  19    CG   CD   OE1  NE2                                  
REMARK 470     LYS B  31    CD   CE   NZ                                        
REMARK 470     ASN B  33    CG   OD1  ND2                                       
REMARK 470     LYS B  49    CG   CD   CE   NZ                                   
REMARK 470     GLN B  80    CG   CD   OE1  NE2                                  
REMARK 470     LYS D 145    CD   CE   NZ                                        
REMARK 470     GLN D 146    CD   OE1  NE2                                       
REMARK 470     LYS D 150    CE   NZ                                             
REMARK 470     LYS D 157    CD   CE   NZ                                        
REMARK 470     LYS D 169    CE   NZ                                             
REMARK 470     LYS D 170    CB   CG   CD   CE   NZ                              
REMARK 470     LEU D 171    CG   CD1  CD2                                       
REMARK 470     GLU C 139    CG   CD   OE1  OE2                                  
REMARK 470     LYS C 145    CG   CD   CE   NZ                                   
REMARK 470     GLN C 146    CD   OE1  NE2                                       
REMARK 470     LYS C 150    NZ                                                  
REMARK 470     GLU C 152    CG   CD   OE1  OE2                                  
REMARK 470     HIS C 160    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LYS C 169    NZ                                                  
REMARK 470     LYS C 170    CB   CG   CD   CE   NZ                              
REMARK 470     VAL C 172    CG1  CG2                                            
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  51      145.50     71.62                                   
REMARK 500    HIS A  72       56.59   -141.45                                   
REMARK 500    ARG B   4       54.50   -152.04                                   
REMARK 500    ASN B  51      144.90     72.78                                   
REMARK 500    HIS B  72       57.55   -144.83                                   
REMARK 500    GLU C 139      104.18    -59.04                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A  93        DISTANCE =  5.05 ANGSTROMS                       
REMARK 525    HOH A  96        DISTANCE =  5.50 ANGSTROMS                       
REMARK 525    HOH B  91        DISTANCE =  5.16 ANGSTROMS                       
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2XQQ   RELATED DB: PDB                                   
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 THE IN VITRO EVOLVED BINDING SEQUENCE.                               
DBREF  3P8M A    1    89  UNP    Q96FJ2   DYL2_HUMAN       1     89             
DBREF  3P8M B    1    89  UNP    Q96FJ2   DYL2_HUMAN       1     89             
DBREF  3P8M D  144   175  UNP    P03069   GCN4_YEAST     250    281             
DBREF  3P8M C  144   175  UNP    P03069   GCN4_YEAST     250    281             
SEQADV 3P8M GLY A   -2  UNP  Q96FJ2              EXPRESSION TAG                 
SEQADV 3P8M SER A   -1  UNP  Q96FJ2              EXPRESSION TAG                 
SEQADV 3P8M HIS A    0  UNP  Q96FJ2              EXPRESSION TAG                 
SEQADV 3P8M GLY B   -2  UNP  Q96FJ2              EXPRESSION TAG                 
SEQADV 3P8M SER B   -1  UNP  Q96FJ2              EXPRESSION TAG                 
SEQADV 3P8M HIS B    0  UNP  Q96FJ2              EXPRESSION TAG                 
SEQADV 3P8M GLY D  130  UNP  P03069              EXPRESSION TAG                 
SEQADV 3P8M SER D  131  UNP  P03069              EXPRESSION TAG                 
SEQADV 3P8M VAL D  132  UNP  P03069              SEE REMARK 999                 
SEQADV 3P8M SER D  133  UNP  P03069              SEE REMARK 999                 
SEQADV 3P8M ARG D  134  UNP  P03069              SEE REMARK 999                 
SEQADV 3P8M GLY D  135  UNP  P03069              SEE REMARK 999                 
SEQADV 3P8M THR D  136  UNP  P03069              SEE REMARK 999                 
SEQADV 3P8M GLN D  137  UNP  P03069              SEE REMARK 999                 
SEQADV 3P8M THR D  138  UNP  P03069              SEE REMARK 999                 
SEQADV 3P8M GLU D  139  UNP  P03069              SEE REMARK 999                 
SEQADV 3P8M GLY D  140  UNP  P03069              LINKER                         
SEQADV 3P8M GLY D  141  UNP  P03069              LINKER                         
SEQADV 3P8M SER D  142  UNP  P03069              LINKER                         
SEQADV 3P8M GLY D  143  UNP  P03069              LINKER                         
SEQADV 3P8M GLY C  130  UNP  P03069              EXPRESSION TAG                 
SEQADV 3P8M SER C  131  UNP  P03069              EXPRESSION TAG                 
SEQADV 3P8M VAL C  132  UNP  P03069              SEE REMARK 999                 
SEQADV 3P8M SER C  133  UNP  P03069              SEE REMARK 999                 
SEQADV 3P8M ARG C  134  UNP  P03069              SEE REMARK 999                 
SEQADV 3P8M GLY C  135  UNP  P03069              SEE REMARK 999                 
SEQADV 3P8M THR C  136  UNP  P03069              SEE REMARK 999                 
SEQADV 3P8M GLN C  137  UNP  P03069              SEE REMARK 999                 
SEQADV 3P8M THR C  138  UNP  P03069              SEE REMARK 999                 
SEQADV 3P8M GLU C  139  UNP  P03069              SEE REMARK 999                 
SEQADV 3P8M GLY C  140  UNP  P03069              LINKER                         
SEQADV 3P8M GLY C  141  UNP  P03069              LINKER                         
SEQADV 3P8M SER C  142  UNP  P03069              LINKER                         
SEQADV 3P8M GLY C  143  UNP  P03069              LINKER                         
SEQRES   1 A   92  GLY SER HIS MET SER ASP ARG LYS ALA VAL ILE LYS ASN          
SEQRES   2 A   92  ALA ASP MET SER GLU ASP MET GLN GLN ASP ALA VAL ASP          
SEQRES   3 A   92  CYS ALA THR GLN ALA MET GLU LYS TYR ASN ILE GLU LYS          
SEQRES   4 A   92  ASP ILE ALA ALA TYR ILE LYS LYS GLU PHE ASP LYS LYS          
SEQRES   5 A   92  TYR ASN PRO THR TRP HIS CYS ILE VAL GLY ARG ASN PHE          
SEQRES   6 A   92  GLY SER TYR VAL THR HIS GLU THR LYS HIS PHE ILE TYR          
SEQRES   7 A   92  PHE TYR LEU GLY GLN VAL ALA ILE LEU LEU PHE LYS SER          
SEQRES   8 A   92  GLY                                                          
SEQRES   1 B   92  GLY SER HIS MET SER ASP ARG LYS ALA VAL ILE LYS ASN          
SEQRES   2 B   92  ALA ASP MET SER GLU ASP MET GLN GLN ASP ALA VAL ASP          
SEQRES   3 B   92  CYS ALA THR GLN ALA MET GLU LYS TYR ASN ILE GLU LYS          
SEQRES   4 B   92  ASP ILE ALA ALA TYR ILE LYS LYS GLU PHE ASP LYS LYS          
SEQRES   5 B   92  TYR ASN PRO THR TRP HIS CYS ILE VAL GLY ARG ASN PHE          
SEQRES   6 B   92  GLY SER TYR VAL THR HIS GLU THR LYS HIS PHE ILE TYR          
SEQRES   7 B   92  PHE TYR LEU GLY GLN VAL ALA ILE LEU LEU PHE LYS SER          
SEQRES   8 B   92  GLY                                                          
SEQRES   1 D   46  GLY SER VAL SER ARG GLY THR GLN THR GLU GLY GLY SER          
SEQRES   2 D   46  GLY MET LYS GLN LEU GLU ASP LYS VAL GLU GLU LEU LEU          
SEQRES   3 D   46  SER LYS ASN TYR HIS LEU GLU ASN GLU VAL ALA ARG LEU          
SEQRES   4 D   46  LYS LYS LEU VAL GLY GLU ARG                                  
SEQRES   1 C   46  GLY SER VAL SER ARG GLY THR GLN THR GLU GLY GLY SER          
SEQRES   2 C   46  GLY MET LYS GLN LEU GLU ASP LYS VAL GLU GLU LEU LEU          
SEQRES   3 C   46  SER LYS ASN TYR HIS LEU GLU ASN GLU VAL ALA ARG LEU          
SEQRES   4 C   46  LYS LYS LEU VAL GLY GLU ARG                                  
FORMUL   5  HOH   *41(H2 O)                                                     
HELIX    1   1 SER A   14  TYR A   32  1                                  19    
HELIX    2   2 ILE A   34  ASN A   51  1                                  18    
HELIX    3   3 SER B   14  TYR B   32  1                                  19    
HELIX    4   4 ILE B   34  ASN B   51  1                                  18    
HELIX    5   5 GLY D  143  VAL D  172  1                                  30    
HELIX    6   6 SER C  142  VAL C  172  1                                  31    
SHEET    1   A 6 ALA A   6  MET A  13  0                                        
SHEET    2   A 6 HIS A  72  LEU A  78 -1  O  TYR A  77   N  VAL A   7           
SHEET    3   A 6 VAL A  81  LYS A  87 -1  O  LEU A  85   N  ILE A  74           
SHEET    4   A 6 TRP A  54  HIS A  68 -1  N  ILE A  57   O  LEU A  84           
SHEET    5   A 6 TRP B  54  HIS B  68 -1  O  GLY B  63   N  VAL A  58           
SHEET    6   A 6 VAL D 132  GLN D 137  0                                        
SHEET    1   B 6 ALA B   6  MET B  13  0                                        
SHEET    2   B 6 HIS B  72  LEU B  78 -1  O  TYR B  77   N  VAL B   7           
SHEET    3   B 6 VAL B  81  LYS B  87 -1  O  LEU B  85   N  ILE B  74           
SHEET    4   B 6 TRP B  54  HIS B  68 -1  N  ILE B  57   O  LEU B  84           
SHEET    5   B 6 TRP A  54  HIS A  68 -1  N  VAL A  58   O  GLY B  63           
SHEET    6   B 6 VAL C 132  GLN C 137  0                                        
CISPEP   1 PRO A   52    THR A   53          0        11.70                     
CISPEP   2 PRO B   52    THR B   53          0        11.42                     
CISPEP   3 GLY C  140    GLY C  141          0         2.12                     
CRYST1   53.839   68.415  101.677  90.00  90.00  90.00 P 21 21 21    8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.018574  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.014617  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009835        0.00000                         
ATOM      1  N   ASP A   3       1.721  25.525  29.037  1.00 89.78           N  
ANISOU    1  N   ASP A   3    13041  15595   5476   -524    609  -2359       N  
ATOM      2  CA  ASP A   3       2.590  24.516  29.728  1.00 91.89           C  
ANISOU    2  CA  ASP A   3    13410  16143   5360   -619    364  -1922       C  
ATOM      3  C   ASP A   3       3.516  23.803  28.737  1.00 87.07           C  
ANISOU    3  C   ASP A   3    12702  15095   5282   -715     85  -1548       C  
ATOM      4  O   ASP A   3       4.640  23.431  29.101  1.00 88.08           O  
ANISOU    4  O   ASP A   3    12890  15306   5269   -756   -271  -1396       O  
ATOM      5  CB  ASP A   3       1.728  23.483  30.481  1.00 95.38           C  
ANISOU    5  CB  ASP A   3    13879  17030   5329   -650    682  -1451       C  
ATOM      6  N   ARG A   4       3.023  23.628  27.498  1.00 81.96           N  
ANISOU    6  N   ARG A   4    11890  14021   5228   -732    246  -1430       N  
ATOM      7  CA  ARG A   4       3.727  22.929  26.399  1.00 76.90           C  
ANISOU    7  CA  ARG A   4    11124  12967   5125   -803     55  -1116       C  
ATOM      8  C   ARG A   4       4.548  23.907  25.502  1.00 73.42           C  
ANISOU    8  C   ARG A   4    10616  12142   5137   -809   -174  -1474       C  
ATOM      9  O   ARG A   4       4.052  24.370  24.461  1.00 70.29           O  
ANISOU    9  O   ARG A   4    10111  11421   5171   -788    -29  -1598       O  
ATOM     10  CB  ARG A   4       2.696  22.151  25.556  1.00 73.65           C  
ANISOU   10  CB  ARG A   4    10563  12359   5061   -828    359   -804       C  
ATOM     11  N   LYS A   5       5.799  24.182  25.906  1.00 73.97           N  
ANISOU   11  N   LYS A   5    10733  12266   5102   -849   -536  -1604       N  
ATOM     12  CA  LYS A   5       6.660  25.233  25.307  1.00 72.22           C  
ANISOU   12  CA  LYS A   5    10455  11745   5241   -898   -761  -1973       C  
ATOM     13  C   LYS A   5       7.246  24.815  23.948  1.00 67.46           C  
ANISOU   13  C   LYS A   5     9662  10755   5214   -961   -839  -1741       C  
ATOM     14  O   LYS A   5       7.466  23.617  23.695  1.00 66.06           O  
ANISOU   14  O   LYS A   5     9407  10581   5111   -964   -873  -1331       O  
ATOM     15  CB  LYS A   5       7.792  25.613  26.282  1.00 75.95           C  
ANISOU   15  CB  LYS A   5    11004  12462   5391   -942  -1132  -2205       C  
ATOM     16  N   ALA A   6       7.500  25.811  23.086  1.00 65.59           N  
ANISOU   16  N   ALA A   6     9355  10187   5379  -1009   -863  -2008       N  
ATOM     17  CA  ALA A   6       7.890  25.570  21.667  1.00 61.57           C  
ANISOU   17  CA  ALA A   6     8660   9343   5387  -1062   -863  -1823       C  
ATOM     18  C   ALA A   6       9.401  25.416  21.444  1.00 61.64           C  
ANISOU   18  C   ALA A   6     8532   9311   5577  -1169  -1182  -1784       C  
ATOM     19  O   ALA A   6      10.188  26.312  21.783  1.00 63.66           O  
ANISOU   19  O   ALA A   6     8791   9550   5847  -1263  -1391  -2080       O  
ATOM     20  CB  ALA A   6       7.358  26.685  20.759  1.00 59.95           C  
ANISOU   20  CB  ALA A   6     8441   8815   5520  -1060   -705  -2044       C  
ATOM     21  N   VAL A   7       9.789  24.285  20.856  1.00 59.50           N  
ANISOU   21  N   VAL A   7     8115   9012   5479  -1153  -1215  -1447       N  
ATOM     22  CA  VAL A   7      11.190  24.024  20.519  1.00 59.64           C  
ANISOU   22  CA  VAL A   7     7939   9002   5716  -1222  -1485  -1398       C  
ATOM     23  C   VAL A   7      11.310  23.705  19.025  1.00 56.07           C  
ANISOU   23  C   VAL A   7     7289   8307   5706  -1235  -1357  -1259       C  
ATOM     24  O   VAL A   7      10.811  22.686  18.556  1.00 54.28           O  
ANISOU   24  O   VAL A   7     7023   8045   5555  -1146  -1225  -1012       O  
ATOM     25  CB  VAL A   7      11.765  22.854  21.363  1.00 61.75           C  
ANISOU   25  CB  VAL A   7     8194   9518   5746  -1145  -1712  -1140       C  
ATOM     26  CG1 VAL A   7      13.108  22.393  20.820  1.00 61.55           C  
ANISOU   26  CG1 VAL A   7     7908   9446   6032  -1164  -1955  -1059       C  
ATOM     27  CG2 VAL A   7      11.893  23.268  22.813  1.00 65.84           C  
ANISOU   27  CG2 VAL A   7     8887  10349   5778  -1146  -1898  -1304       C  
ATOM     28  N   ILE A   8      11.968  24.588  18.282  1.00 55.64           N  
ANISOU   28  N   ILE A   8     7109   8094   5937  -1358  -1392  -1425       N  
ATOM     29  CA  ILE A   8      12.220  24.347  16.862  1.00 53.04           C  
ANISOU   29  CA  ILE A   8     6577   7608   5965  -1380  -1275  -1303       C  
ATOM     30  C   ILE A   8      13.445  23.477  16.651  1.00 53.50           C  
ANISOU   30  C   ILE A   8     6387   7767   6172  -1372  -1465  -1187       C  
ATOM     31  O   ILE A   8      14.554  23.878  16.972  1.00 55.63           O  
ANISOU   31  O   ILE A   8     6526   8112   6499  -1476  -1688  -1310       O  
ATOM     32  CB  ILE A   8      12.464  25.644  16.104  1.00 53.07           C  
ANISOU   32  CB  ILE A   8     6536   7414   6213  -1532  -1211  -1464       C  
ATOM     33  CG1 ILE A   8      11.203  26.523  16.137  1.00 52.73           C  
ANISOU   33  CG1 ILE A   8     6717   7215   6103  -1493  -1018  -1575       C  
ATOM     34  CG2 ILE A   8      12.907  25.321  14.667  1.00 50.92           C  
ANISOU   34  CG2 ILE A   8     6031   7080   6237  -1562  -1100  -1313       C  
ATOM     35  CD1 ILE A   8      11.464  28.010  15.911  1.00 54.76           C  
ANISOU   35  CD1 ILE A   8     7012   7231   6562  -1646  -1035  -1779       C  
ATOM     36  N   LYS A   9      13.247  22.297  16.086  1.00 51.83           N  
ANISOU   36  N   LYS A   9     6086   7547   6058  -1245  -1385   -981       N  
ATOM     37  CA  LYS A   9      14.361  21.411  15.818  1.00 52.84           C  
ANISOU   37  CA  LYS A   9     5958   7744   6373  -1188  -1553   -896       C  
ATOM     38  C   LYS A   9      15.074  21.820  14.541  1.00 52.02           C  
ANISOU   38  C   LYS A   9     5594   7597   6574  -1281  -1463   -981       C  
ATOM     39  O   LYS A   9      16.299  21.863  14.496  1.00 53.89           O  
ANISOU   39  O   LYS A   9     5583   7933   6959  -1336  -1630  -1043       O  
ATOM     40  CB  LYS A   9      13.906  19.963  15.744  1.00 52.39           C  
ANISOU   40  CB  LYS A   9     5908   7649   6347  -1008  -1517   -673       C  
ATOM     41  CG  LYS A   9      13.793  19.307  17.115  1.00 55.69           C  
ANISOU   41  CG  LYS A   9     6491   8171   6496   -920  -1703   -502       C  
ATOM     42  CD  LYS A   9      14.047  17.771  16.989  1.00 61.33           C  
ANISOU   42  CD  LYS A   9     7097   8806   7399   -746  -1795   -262       C  
ATOM     43  N   ASN A  10      14.307  22.123  13.502  1.00 49.80           N  
ANISOU   43  N   ASN A  10     5349   7202   6370  -1300  -1198   -972       N  
ATOM     44  CA  ASN A  10      14.880  22.546  12.220  1.00 49.43           C  
ANISOU   44  CA  ASN A  10     5078   7156   6546  -1395  -1070  -1008       C  
ATOM     45  C   ASN A  10      13.925  23.465  11.478  1.00 47.88           C  
ANISOU   45  C   ASN A  10     5031   6829   6329  -1463   -836  -1001       C  
ATOM     46  O   ASN A  10      12.700  23.292  11.553  1.00 45.97           O  
ANISOU   46  O   ASN A  10     4988   6514   5963  -1361   -725   -959       O  
ATOM     47  CB  ASN A  10      15.191  21.333  11.331  1.00 48.85           C  
ANISOU   47  CB  ASN A  10     4776   7158   6627  -1247  -1013   -954       C  
ATOM     48  CG  ASN A  10      16.335  20.486  11.866  1.00 51.22           C  
ANISOU   48  CG  ASN A  10     4857   7568   7035  -1156  -1256   -961       C  
ATOM     49  OD1 ASN A  10      17.477  20.953  11.982  1.00 53.08           O  
ANISOU   49  OD1 ASN A  10     4876   7918   7373  -1266  -1385  -1042       O  
ATOM     50  ND2 ASN A  10      16.032  19.219  12.180  1.00 51.42           N  
ANISOU   50  ND2 ASN A  10     4920   7545   7071   -954  -1330   -865       N  
ATOM     51  N   ALA A  11      14.501  24.422  10.746  1.00 48.90           N  
ANISOU   51  N   ALA A  11     5045   6934   6598  -1636   -765  -1019       N  
ATOM     52  CA  ALA A  11      13.728  25.357   9.921  1.00 47.90           C  
ANISOU   52  CA  ALA A  11     5044   6671   6484  -1695   -564   -957       C  
ATOM     53  C   ALA A  11      14.522  25.869   8.714  1.00 49.36           C  
ANISOU   53  C   ALA A  11     5009   6916   6829  -1852   -438   -872       C  
ATOM     54  O   ALA A  11      15.745  26.111   8.809  1.00 52.19           O  
ANISOU   54  O   ALA A  11     5150   7349   7331  -2018   -524   -913       O  
ATOM     55  CB  ALA A  11      13.280  26.523  10.752  1.00 48.90           C  
ANISOU   55  CB  ALA A  11     5413   6591   6575  -1784   -622  -1050       C  
ATOM     56  N   ASP A  12      13.818  26.005   7.585  1.00 48.14           N  
ANISOU   56  N   ASP A  12     4893   6766   6631  -1801   -236   -744       N  
ATOM     57  CA  ASP A  12      14.268  26.766   6.418  1.00 49.49           C  
ANISOU   57  CA  ASP A  12     4943   6977   6881  -1962    -75   -592       C  
ATOM     58  C   ASP A  12      13.042  27.571   6.028  1.00 49.01           C  
ANISOU   58  C   ASP A  12     5144   6721   6754  -1913     23   -467       C  
ATOM     59  O   ASP A  12      12.207  27.133   5.248  1.00 47.82           O  
ANISOU   59  O   ASP A  12     5026   6675   6466  -1749    132   -396       O  
ATOM     60  CB  ASP A  12      14.725  25.847   5.298  1.00 49.24           C  
ANISOU   60  CB  ASP A  12     4644   7262   6801  -1886     59   -560       C  
ATOM     61  CG  ASP A  12      15.074  26.596   4.019  1.00 51.34           C  
ANISOU   61  CG  ASP A  12     4799   7645   7061  -2043    267   -359       C  
ATOM     62  OD1 ASP A  12      16.207  27.072   3.845  1.00 54.83           O  
ANISOU   62  OD1 ASP A  12     5026   8163   7641  -2268    306   -307       O  
ATOM     63  OD2 ASP A  12      14.224  26.679   3.134  1.00 51.17           O  
ANISOU   63  OD2 ASP A  12     4885   7675   6882  -1945    398   -233       O  
ATOM     64  N   MET A  13      12.919  28.741   6.633  1.00 50.58           N  
ANISOU   64  N   MET A  13     5522   6626   7070  -2038    -42   -475       N  
ATOM     65  CA  MET A  13      11.669  29.497   6.641  1.00 50.19           C  
ANISOU   65  CA  MET A  13     5743   6329   6997  -1932     -6   -423       C  
ATOM     66  C   MET A  13      11.956  30.878   7.201  1.00 53.15           C  
ANISOU   66  C   MET A  13     6251   6348   7593  -2124    -86   -459       C  
ATOM     67  O   MET A  13      12.979  31.069   7.866  1.00 54.89           O  
ANISOU   67  O   MET A  13     6374   6540   7941  -2318   -208   -593       O  
ATOM     68  CB  MET A  13      10.672  28.799   7.553  1.00 47.85           C  
ANISOU   68  CB  MET A  13     5587   6046   6548  -1708    -71   -600       C  
ATOM     69  CG  MET A  13       9.246  29.354   7.492  1.00 47.67           C  
ANISOU   69  CG  MET A  13     5777   5846   6486  -1538    -11   -576       C  
ATOM     70  SD  MET A  13       8.036  28.375   8.437  1.00 45.60           S  
ANISOU   70  SD  MET A  13     5607   5687   6031  -1300    -23   -750       S  
ATOM     71  CE  MET A  13       6.706  28.206   7.260  1.00 43.91           C  
ANISOU   71  CE  MET A  13     5386   5543   5755  -1100    109   -606       C  
ATOM     72  N   SER A  14      11.078  31.843   6.942  1.00 54.11           N  
ANISOU   72  N   SER A  14     6581   6184   7792  -2066    -41   -360       N  
ATOM     73  CA  SER A  14      11.250  33.173   7.527  1.00 57.30           C  
ANISOU   73  CA  SER A  14     7137   6169   8462  -2223   -133   -443       C  
ATOM     74  C   SER A  14      10.890  33.115   8.992  1.00 56.79           C  
ANISOU   74  C   SER A  14     7212   6030   8336  -2123   -282   -813       C  
ATOM     75  O   SER A  14      10.155  32.255   9.418  1.00 53.98           O  
ANISOU   75  O   SER A  14     6892   5879   7739  -1901   -271   -917       O  
ATOM     76  CB  SER A  14      10.398  34.227   6.827  1.00 59.17           C  
ANISOU   76  CB  SER A  14     7561   6079   8839  -2150    -58   -221       C  
ATOM     77  OG  SER A  14       9.052  34.154   7.255  1.00 57.97           O  
ANISOU   77  OG  SER A  14     7583   5865   8576  -1844    -69   -362       O  
ATOM     78  N   GLU A  15      11.423  34.053   9.760  1.00 60.37           N  
ANISOU   78  N   GLU A  15     7736   6196   9004  -2306   -418  -1016       N  
ATOM     79  CA  GLU A  15      11.179  34.112  11.208  1.00 60.92           C  
ANISOU   79  CA  GLU A  15     7941   6231   8973  -2229   -572  -1413       C  
ATOM     80  C   GLU A  15       9.698  34.379  11.527  1.00 60.30           C  
ANISOU   80  C   GLU A  15     8092   6020   8798  -1931   -502  -1525       C  
ATOM     81  O   GLU A  15       9.104  33.712  12.384  1.00 58.76           O  
ANISOU   81  O   GLU A  15     7952   6051   8323  -1748   -510  -1718       O  
ATOM     82  CB  GLU A  15      12.069  35.190  11.834  1.00 65.17           C  
ANISOU   82  CB  GLU A  15     8498   6462   9799  -2506   -746  -1646       C  
ATOM     83  CG  GLU A  15      12.542  34.869  13.234  1.00 66.35           C  
ANISOU   83  CG  GLU A  15     8640   6799   9769  -2533   -959  -2034       C  
ATOM     84  CD  GLU A  15      13.713  35.777  13.631  1.00 71.33           C  
ANISOU   84  CD  GLU A  15     9187   7200  10715  -2876  -1158  -2243       C  
ATOM     85  OE1 GLU A  15      13.461  36.932  14.072  1.00 74.66           O  
ANISOU   85  OE1 GLU A  15     9790   7207  11368  -2933  -1237  -2500       O  
ATOM     86  OE2 GLU A  15      14.882  35.338  13.480  1.00 71.68           O  
ANISOU   86  OE2 GLU A  15     8962   7466  10806  -3087  -1238  -2168       O  
ATOM     87  N   ASP A  16       9.120  35.355  10.826  1.00 61.94           N  
ANISOU   87  N   ASP A  16     8415   5870   9248  -1884   -429  -1380       N  
ATOM     88  CA  ASP A  16       7.696  35.662  10.939  1.00 61.77           C  
ANISOU   88  CA  ASP A  16     8559   5717   9190  -1574   -356  -1457       C  
ATOM     89  C   ASP A  16       6.911  34.364  10.755  1.00 57.68           C  
ANISOU   89  C   ASP A  16     7954   5633   8330  -1352   -239  -1362       C  
ATOM     90  O   ASP A  16       6.220  33.929  11.679  1.00 57.13           O  
ANISOU   90  O   ASP A  16     7935   5726   8045  -1183   -225  -1603       O  
ATOM     91  CB  ASP A  16       7.259  36.726   9.909  1.00 64.09           C  
ANISOU   91  CB  ASP A  16     8945   5605   9799  -1533   -304  -1184       C  
ATOM     92  CG  ASP A  16       7.730  38.153  10.268  1.00 69.15           C  
ANISOU   92  CG  ASP A  16     9728   5683  10861  -1707   -425  -1335       C  
ATOM     93  OD1 ASP A  16       8.591  38.290  11.161  1.00 70.93           O  
ANISOU   93  OD1 ASP A  16     9937   5879  11133  -1920   -554  -1639       O  
ATOM     94  OD2 ASP A  16       7.243  39.139   9.652  1.00 71.73           O  
ANISOU   94  OD2 ASP A  16    10179   5583  11492  -1631   -410  -1149       O  
ATOM     95  N   MET A  17       7.046  33.737   9.587  1.00 55.40           N  
ANISOU   95  N   MET A  17     7522   5541   7986  -1371   -153  -1027       N  
ATOM     96  CA  MET A  17       6.366  32.466   9.295  1.00 51.98           C  
ANISOU   96  CA  MET A  17     6983   5484   7283  -1194    -60   -950       C  
ATOM     97  C   MET A  17       6.586  31.395  10.355  1.00 50.27           C  
ANISOU   97  C   MET A  17     6716   5548   6833  -1197   -101  -1150       C  
ATOM     98  O   MET A  17       5.665  30.654  10.677  1.00 48.69           O  
ANISOU   98  O   MET A  17     6513   5533   6452  -1022    -32  -1202       O  
ATOM     99  CB  MET A  17       6.842  31.897   7.963  1.00 50.96           C  
ANISOU   99  CB  MET A  17     6684   5558   7119  -1268      6   -640       C  
ATOM    100  CG  MET A  17       6.298  32.601   6.706  1.00 52.41           C  
ANISOU  100  CG  MET A  17     6902   5613   7398  -1190     74   -349       C  
ATOM    101  SD  MET A  17       6.146  31.426   5.334  1.00 51.27           S  
ANISOU  101  SD  MET A  17     6558   5909   7012  -1114    173   -118       S  
ATOM    102  CE  MET A  17       5.806  32.541   3.991  1.00 53.02           C  
ANISOU  102  CE  MET A  17     6853   5970   7320  -1076    210    263       C  
ATOM    103  N   GLN A  18       7.804  31.315  10.892  1.00 51.23           N  
ANISOU  103  N   GLN A  18     6786   5706   6971  -1402   -221  -1237       N  
ATOM    104  CA  GLN A  18       8.143  30.336  11.950  1.00 50.38           C  
ANISOU  104  CA  GLN A  18     6643   5862   6637  -1402   -304  -1384       C  
ATOM    105  C   GLN A  18       7.332  30.527  13.215  1.00 51.47           C  
ANISOU  105  C   GLN A  18     6951   6007   6596  -1270   -313  -1645       C  
ATOM    106  O   GLN A  18       6.778  29.571  13.740  1.00 50.06           O  
ANISOU  106  O   GLN A  18     6768   6072   6178  -1153   -262  -1644       O  
ATOM    107  CB  GLN A  18       9.628  30.377  12.308  1.00 51.83           C  
ANISOU  107  CB  GLN A  18     6720   6080   6892  -1634   -473  -1446       C  
ATOM    108  CG  GLN A  18      10.510  29.672  11.273  1.00 50.85           C  
ANISOU  108  CG  GLN A  18     6355   6120   6845  -1731   -444  -1216       C  
ATOM    109  CD  GLN A  18      11.991  29.738  11.597  1.00 52.53           C  
ANISOU  109  CD  GLN A  18     6401   6389   7166  -1954   -609  -1285       C  
ATOM    110  OE1 GLN A  18      12.445  29.241  12.630  1.00 53.32           O  
ANISOU  110  OE1 GLN A  18     6482   6642   7135  -1952   -776  -1435       O  
ATOM    111  NE2 GLN A  18      12.752  30.341  10.703  1.00 53.83           N  
ANISOU  111  NE2 GLN A  18     6428   6460   7564  -2151   -564  -1155       N  
ATOM    112  N   GLN A  19       7.277  31.759  13.711  1.00 54.50           N  
ANISOU  112  N   GLN A  19     7479   6123   7104  -1295   -370  -1875       N  
ATOM    113  CA  GLN A  19       6.409  32.078  14.843  1.00 56.28           C  
ANISOU  113  CA  GLN A  19     7863   6368   7151  -1136   -344  -2177       C  
ATOM    114  C   GLN A  19       4.950  31.788  14.484  1.00 54.76           C  
ANISOU  114  C   GLN A  19     7671   6240   6893   -888   -141  -2090       C  
ATOM    115  O   GLN A  19       4.189  31.251  15.297  1.00 54.69           O  
ANISOU  115  O   GLN A  19     7688   6473   6617   -756    -51  -2201       O  
ATOM    116  CB  GLN A  19       6.562  33.537  15.244  1.00 60.17           C  
ANISOU  116  CB  GLN A  19     8500   6492   7869  -1185   -438  -2476       C  
ATOM    117  CG  GLN A  19       5.646  33.978  16.393  1.00 64.22           C  
ANISOU  117  CG  GLN A  19     9168   7032   8199   -989   -395  -2865       C  
ATOM    118  CD  GLN A  19       5.954  33.289  17.734  1.00 66.41           C  
ANISOU  118  CD  GLN A  19     9474   7711   8045  -1013   -473  -3072       C  
ATOM    119  OE1 GLN A  19       7.089  33.335  18.233  1.00 67.61           O  
ANISOU  119  OE1 GLN A  19     9615   7911   8159  -1208   -684  -3187       O  
ATOM    120  NE2 GLN A  19       4.929  32.673  18.333  1.00 66.01           N  
ANISOU  120  NE2 GLN A  19     9449   7967   7664   -818   -306  -3108       N  
ATOM    121  N   ASP A  20       4.570  32.124  13.254  1.00 53.92           N  
ANISOU  121  N   ASP A  20     7517   5951   7019   -833    -71  -1872       N  
ATOM    122  CA  ASP A  20       3.176  31.969  12.804  1.00 52.94           C  
ANISOU  122  CA  ASP A  20     7359   5877   6879   -590     84  -1801       C  
ATOM    123  C   ASP A  20       2.747  30.526  12.742  1.00 49.85           C  
ANISOU  123  C   ASP A  20     6830   5850   6260   -551    179  -1660       C  
ATOM    124  O   ASP A  20       1.599  30.214  13.015  1.00 49.85           O  
ANISOU  124  O   ASP A  20     6794   5988   6157   -383    308  -1718       O  
ATOM    125  CB  ASP A  20       2.951  32.599  11.433  1.00 53.13           C  
ANISOU  125  CB  ASP A  20     7355   5665   7166   -540     95  -1556       C  
ATOM    126  CG  ASP A  20       1.513  33.033  11.232  1.00 54.25           C  
ANISOU  126  CG  ASP A  20     7501   5733   7376   -252    189  -1600       C  
ATOM    127  OD1 ASP A  20       1.017  33.880  12.020  1.00 57.35           O  
ANISOU  127  OD1 ASP A  20     8005   5937   7845   -117    196  -1884       O  
ATOM    128  OD2 ASP A  20       0.888  32.539  10.283  1.00 52.45           O  
ANISOU  128  OD2 ASP A  20     7148   5646   7132   -149    245  -1380       O  
ATOM    129  N   ALA A  21       3.668  29.656  12.351  1.00 47.89           N  
ANISOU  129  N   ALA A  21     6483   5738   5972   -708    117  -1482       N  
ATOM    130  CA  ALA A  21       3.465  28.214  12.495  1.00 45.92           C  
ANISOU  130  CA  ALA A  21     6123   5778   5544   -700    169  -1379       C  
ATOM    131  C   ALA A  21       3.240  27.844  13.967  1.00 47.14           C  
ANISOU  131  C   ALA A  21     6362   6104   5442   -684    187  -1535       C  
ATOM    132  O   ALA A  21       2.252  27.213  14.318  1.00 46.94           O  
ANISOU  132  O   ALA A  21     6300   6247   5285   -590    324  -1519       O  
ATOM    133  CB  ALA A  21       4.644  27.459  11.941  1.00 44.30           C  
ANISOU  133  CB  ALA A  21     5804   5647   5378   -848     74  -1220       C  
ATOM    134  N   VAL A  22       4.153  28.274  14.827  1.00 48.99           N  
ANISOU  134  N   VAL A  22     6700   6318   5596   -788     49  -1684       N  
ATOM    135  CA  VAL A  22       4.073  27.982  16.259  1.00 50.88           C  
ANISOU  135  CA  VAL A  22     7037   6775   5517   -778     38  -1829       C  
ATOM    136  C   VAL A  22       2.762  28.474  16.867  1.00 52.80           C  
ANISOU  136  C   VAL A  22     7354   7075   5632   -608    221  -2027       C  
ATOM    137  O   VAL A  22       2.229  27.826  17.766  1.00 53.91           O  
ANISOU  137  O   VAL A  22     7513   7493   5477   -568    326  -2027       O  
ATOM    138  CB  VAL A  22       5.274  28.577  17.048  1.00 53.18           C  
ANISOU  138  CB  VAL A  22     7422   7040   5743   -910   -182  -2025       C  
ATOM    139  CG1 VAL A  22       5.117  28.328  18.536  1.00 55.55           C  
ANISOU  139  CG1 VAL A  22     7839   7628   5637   -876   -200  -2185       C  
ATOM    140  CG2 VAL A  22       6.590  27.990  16.553  1.00 51.73           C  
ANISOU  140  CG2 VAL A  22     7111   6864   5678  -1067   -355  -1838       C  
ATOM    141  N   ASP A  23       2.239  29.600  16.375  1.00 53.74           N  
ANISOU  141  N   ASP A  23     7502   6939   5977   -500    266  -2176       N  
ATOM    142  CA  ASP A  23       0.922  30.096  16.826  1.00 55.77           C  
ANISOU  142  CA  ASP A  23     7778   7239   6170   -290    450  -2388       C  
ATOM    143  C   ASP A  23      -0.181  29.154  16.352  1.00 53.92           C  
ANISOU  143  C   ASP A  23     7371   7198   5916   -200    641  -2176       C  
ATOM    144  O   ASP A  23      -0.968  28.658  17.143  1.00 55.38           O  
ANISOU  144  O   ASP A  23     7519   7659   5862   -141    811  -2225       O  
ATOM    145  CB  ASP A  23       0.635  31.513  16.317  1.00 57.44           C  
ANISOU  145  CB  ASP A  23     8049   7071   6703   -163    423  -2571       C  
ATOM    146  CG  ASP A  23       1.702  32.521  16.735  1.00 60.17           C  
ANISOU  146  CG  ASP A  23     8554   7154   7154   -285    226  -2806       C  
ATOM    147  OD1 ASP A  23       2.222  32.423  17.875  1.00 61.84           O  
ANISOU  147  OD1 ASP A  23     8854   7551   7092   -366    154  -3025       O  
ATOM    148  OD2 ASP A  23       2.023  33.417  15.911  1.00 60.85           O  
ANISOU  148  OD2 ASP A  23     8671   6849   7598   -312    135  -2760       O  
ATOM    149  N   CYS A  24      -0.240  28.912  15.056  1.00 51.45           N  
ANISOU  149  N   CYS A  24     6940   6760   5847   -204    616  -1945       N  
ATOM    150  CA  CYS A  24      -1.234  28.001  14.516  1.00 50.31           C  
ANISOU  150  CA  CYS A  24     6607   6785   5720   -143    756  -1777       C  
ATOM    151  C   CYS A  24      -1.261  26.732  15.326  1.00 50.01           C  
ANISOU  151  C   CYS A  24     6534   7032   5435   -255    837  -1669       C  
ATOM    152  O   CYS A  24      -2.302  26.329  15.835  1.00 51.40           O  
ANISOU  152  O   CYS A  24     6619   7414   5493   -197   1028  -1690       O  
ATOM    153  CB  CYS A  24      -0.928  27.639  13.064  1.00 47.83           C  
ANISOU  153  CB  CYS A  24     6183   6370   5618   -189    665  -1543       C  
ATOM    154  SG  CYS A  24      -1.846  28.618  11.903  1.00 50.84           S  
ANISOU  154  SG  CYS A  24     6488   6576   6251     23    672  -1540       S  
ATOM    155  N   ALA A  25      -0.099  26.096  15.432  1.00 48.91           N  
ANISOU  155  N   ALA A  25     6449   6898   5234   -418    691  -1530       N  
ATOM    156  CA  ALA A  25       0.004  24.816  16.116  1.00 48.72           C  
ANISOU  156  CA  ALA A  25     6406   7086   5018   -523    725  -1353       C  
ATOM    157  C   ALA A  25      -0.700  24.954  17.453  1.00 51.59           C  
ANISOU  157  C   ALA A  25     6843   7691   5066   -476    890  -1475       C  
ATOM    158  O   ALA A  25      -1.495  24.102  17.838  1.00 52.21           O  
ANISOU  158  O   ALA A  25     6835   7967   5035   -501   1066  -1335       O  
ATOM    159  CB  ALA A  25       1.438  24.435  16.300  1.00 48.16           C  
ANISOU  159  CB  ALA A  25     6410   6981   4906   -651    509  -1256       C  
ATOM    160  N   THR A  26      -0.434  26.063  18.129  1.00 53.70           N  
ANISOU  160  N   THR A  26     7259   7945   5197   -414    845  -1755       N  
ATOM    161  CA  THR A  26      -1.009  26.311  19.452  1.00 57.43           C  
ANISOU  161  CA  THR A  26     7814   8698   5307   -350   1001  -1945       C  
ATOM    162  C   THR A  26      -2.528  26.451  19.420  1.00 58.74           C  
ANISOU  162  C   THR A  26     7829   8987   5501   -203   1289  -2036       C  
ATOM    163  O   THR A  26      -3.223  25.850  20.241  1.00 60.95           O  
ANISOU  163  O   THR A  26     8060   9593   5505   -220   1505  -1970       O  
ATOM    164  CB  THR A  26      -0.412  27.551  20.084  1.00 59.66           C  
ANISOU  164  CB  THR A  26     8275   8906   5485   -300    869  -2314       C  
ATOM    165  OG1 THR A  26       1.000  27.357  20.221  1.00 59.10           O  
ANISOU  165  OG1 THR A  26     8301   8780   5371   -455    597  -2234       O  
ATOM    166  CG2 THR A  26      -1.038  27.799  21.438  1.00 64.16           C  
ANISOU  166  CG2 THR A  26     8923   9824   5631   -211   1045  -2564       C  
ATOM    167  N   GLN A  27      -3.033  27.231  18.468  1.00 57.86           N  
ANISOU  167  N   GLN A  27     7627   8632   5725    -60   1291  -2161       N  
ATOM    168  CA  GLN A  27      -4.479  27.381  18.278  1.00 59.11           C  
ANISOU  168  CA  GLN A  27     7584   8893   5979    108   1528  -2250       C  
ATOM    169  C   GLN A  27      -5.098  26.024  18.004  1.00 57.86           C  
ANISOU  169  C   GLN A  27     7221   8925   5838    -14   1666  -1939       C  
ATOM    170  O   GLN A  27      -5.975  25.592  18.740  1.00 60.23           O  
ANISOU  170  O   GLN A  27     7406   9528   5947    -19   1917  -1935       O  
ATOM    171  CB  GLN A  27      -4.797  28.322  17.113  1.00 58.27           C  
ANISOU  171  CB  GLN A  27     7409   8464   6265    284   1437  -2343       C  
ATOM    172  CG  GLN A  27      -4.480  29.803  17.371  1.00 60.85           C  
ANISOU  172  CG  GLN A  27     7913   8532   6675    437   1337  -2680       C  
ATOM    173  CD  GLN A  27      -4.839  30.717  16.175  1.00 61.13           C  
ANISOU  173  CD  GLN A  27     7889   8212   7122    621   1239  -2686       C  
ATOM    174  OE1 GLN A  27      -4.623  30.352  14.998  1.00 58.58           O  
ANISOU  174  OE1 GLN A  27     7493   7771   6991    555   1126  -2400       O  
ATOM    175  NE2 GLN A  27      -5.377  31.915  16.476  1.00 63.97           N  
ANISOU  175  NE2 GLN A  27     8288   8406   7611    868   1274  -3015       N  
ATOM    176  N   ALA A  28      -4.625  25.362  16.946  1.00 54.52           N  
ANISOU  176  N   ALA A  28     6741   8322   5651   -124   1508  -1696       N  
ATOM    177  CA  ALA A  28      -5.064  24.014  16.594  1.00 53.54           C  
ANISOU  177  CA  ALA A  28     6433   8296   5611   -266   1586  -1426       C  
ATOM    178  C   ALA A  28      -5.152  23.085  17.805  1.00 55.80           C  
ANISOU  178  C   ALA A  28     6755   8848   5597   -420   1746  -1255       C  
ATOM    179  O   ALA A  28      -6.138  22.377  17.962  1.00 57.45           O  
ANISOU  179  O   ALA A  28     6770   9230   5825   -486   1960  -1141       O  
ATOM    180  CB  ALA A  28      -4.132  23.412  15.542  1.00 50.23           C  
ANISOU  180  CB  ALA A  28     6024   7654   5404   -374   1355  -1241       C  
ATOM    181  N   MET A  29      -4.133  23.096  18.661  1.00 56.60           N  
ANISOU  181  N   MET A  29     7090   8993   5420   -485   1636  -1220       N  
ATOM    182  CA  MET A  29      -4.100  22.213  19.848  1.00 59.20           C  
ANISOU  182  CA  MET A  29     7491   9593   5406   -625   1753   -993       C  
ATOM    183  C   MET A  29      -5.077  22.596  20.974  1.00 63.18           C  
ANISOU  183  C   MET A  29     7971  10476   5557   -561   2061  -1137       C  
ATOM    184  O   MET A  29      -5.396  21.770  21.821  1.00 65.79           O  
ANISOU  184  O   MET A  29     8295  11078   5623   -691   2241   -888       O  
ATOM    185  CB  MET A  29      -2.667  22.086  20.390  1.00 59.02           C  
ANISOU  185  CB  MET A  29     7710   9538   5176   -693   1495   -902       C  
ATOM    186  CG  MET A  29      -1.772  21.221  19.490  1.00 56.11           C  
ANISOU  186  CG  MET A  29     7315   8887   5116   -792   1258   -660       C  
ATOM    187  SD  MET A  29      -0.278  20.558  20.259  1.00 56.30           S  
ANISOU  187  SD  MET A  29     7535   8937   4919   -885    986   -424       S  
ATOM    188  CE  MET A  29      -0.955  19.136  21.122  1.00 60.19           C  
ANISOU  188  CE  MET A  29     8012   9628   5230  -1023   1183     14       C  
ATOM    189  N   GLU A  30      -5.541  23.840  20.971  1.00 64.28           N  
ANISOU  189  N   GLU A  30     8092  10630   5700   -355   2128  -1531       N  
ATOM    190  CA  GLU A  30      -6.623  24.285  21.868  1.00 68.64           C  
ANISOU  190  CA  GLU A  30     8550  11547   5979   -241   2455  -1752       C  
ATOM    191  C   GLU A  30      -7.980  23.755  21.404  1.00 69.30           C  
ANISOU  191  C   GLU A  30     8291  11739   6298   -257   2724  -1646       C  
ATOM    192  O   GLU A  30      -8.858  23.483  22.220  1.00 73.04           O  
ANISOU  192  O   GLU A  30     8630  12596   6525   -287   3051  -1626       O  
ATOM    193  CB  GLU A  30      -6.686  25.817  21.942  1.00 69.89           C  
ANISOU  193  CB  GLU A  30     8781  11617   6154     21   2416  -2254       C  
ATOM    194  CG  GLU A  30      -5.526  26.463  22.704  1.00 71.19           C  
ANISOU  194  CG  GLU A  30     9257  11767   6024     28   2203  -2463       C  
ATOM    195  CD  GLU A  30      -5.451  27.981  22.522  1.00 72.30           C  
ANISOU  195  CD  GLU A  30     9478  11648   6344    259   2095  -2951       C  
ATOM    196  OE1 GLU A  30      -6.486  28.608  22.204  1.00 73.86           O  
ANISOU  196  OE1 GLU A  30     9502  11807   6754    472   2261  -3180       O  
ATOM    197  OE2 GLU A  30      -4.350  28.550  22.702  1.00 72.28           O  
ANISOU  197  OE2 GLU A  30     9699  11462   6303    227   1830  -3105       O  
ATOM    198  N   LYS A  31      -8.137  23.636  20.084  1.00 66.10           N  
ANISOU  198  N   LYS A  31     7730  11026   6358   -241   2582  -1593       N  
ATOM    199  CA  LYS A  31      -9.378  23.174  19.454  1.00 66.52           C  
ANISOU  199  CA  LYS A  31     7423  11147   6702   -253   2761  -1534       C  
ATOM    200  C   LYS A  31      -9.475  21.648  19.449  1.00 66.39           C  
ANISOU  200  C   LYS A  31     7302  11172   6749   -556   2830  -1121       C  
ATOM    201  O   LYS A  31     -10.428  21.088  19.989  1.00 69.69           O  
ANISOU  201  O   LYS A  31     7506  11874   7097   -672   3134  -1007       O  
ATOM    202  CB  LYS A  31      -9.479  23.690  18.006  1.00 63.41           C  
ANISOU  202  CB  LYS A  31     6915  10435   6742   -100   2539  -1655       C  
ATOM    203  CG  LYS A  31     -10.908  23.956  17.604  1.00 66.19           C  
ANISOU  203  CG  LYS A  31     6899  10933   7317     51   2720  -1815       C  
ATOM    204  CD  LYS A  31     -11.129  24.522  16.203  1.00 65.70           C  
ANISOU  204  CD  LYS A  31     6711  10615   7634    240   2492  -1917       C  
ATOM    205  CE  LYS A  31     -12.601  24.258  15.821  1.00 70.00           C  
ANISOU  205  CE  LYS A  31     6810  11378   8409    298   2662  -1975       C  
ATOM    206  NZ  LYS A  31     -13.059  25.005  14.614  1.00 70.78           N  
ANISOU  206  NZ  LYS A  31     6750  11321   8821    562   2460  -2113       N  
ATOM    207  N   TYR A  32      -8.473  20.997  18.852  1.00 62.99           N  
ANISOU  207  N   TYR A  32     7015  10446   6473   -684   2555   -907       N  
ATOM    208  CA  TYR A  32      -8.495  19.556  18.590  1.00 62.81           C  
ANISOU  208  CA  TYR A  32     6891  10325   6646   -943   2551   -553       C  
ATOM    209  C   TYR A  32      -7.489  18.778  19.442  1.00 63.62           C  
ANISOU  209  C   TYR A  32     7260  10416   6497  -1108   2476   -230       C  
ATOM    210  O   TYR A  32      -6.336  19.203  19.600  1.00 62.20           O  
ANISOU  210  O   TYR A  32     7340  10136   6155  -1031   2246   -279       O  
ATOM    211  CB  TYR A  32      -8.217  19.277  17.099  1.00 59.07           C  
ANISOU  211  CB  TYR A  32     6321   9515   6605   -935   2287   -584       C  
ATOM    212  CG  TYR A  32      -9.085  20.068  16.160  1.00 58.28           C  
ANISOU  212  CG  TYR A  32     5985   9424   6735   -745   2287   -866       C  
ATOM    213  CD1 TYR A  32     -10.325  19.599  15.759  1.00 59.84           C  
ANISOU  213  CD1 TYR A  32     5824   9734   7177   -807   2436   -880       C  
ATOM    214  CD2 TYR A  32      -8.669  21.288  15.685  1.00 56.67           C  
ANISOU  214  CD2 TYR A  32     5904   9108   6518   -506   2123  -1100       C  
ATOM    215  CE1 TYR A  32     -11.121  20.334  14.909  1.00 59.77           C  
ANISOU  215  CE1 TYR A  32     5583   9760   7367   -602   2399  -1128       C  
ATOM    216  CE2 TYR A  32      -9.450  22.020  14.845  1.00 56.86           C  
ANISOU  216  CE2 TYR A  32     5729   9127   6747   -307   2098  -1306       C  
ATOM    217  CZ  TYR A  32     -10.676  21.547  14.463  1.00 58.20           C  
ANISOU  217  CZ  TYR A  32     5540   9443   7128   -337   2226  -1323       C  
ATOM    218  OH  TYR A  32     -11.438  22.306  13.619  1.00 58.67           O  
ANISOU  218  OH  TYR A  32     5391   9517   7383   -105   2160  -1520       O  
ATOM    219  N   ASN A  33      -7.933  17.628  19.963  1.00 66.45           N  
ANISOU  219  N   ASN A  33     7533  10862   6852  -1343   2656    119       N  
ATOM    220  CA  ASN A  33      -7.047  16.650  20.618  1.00 67.49           C  
ANISOU  220  CA  ASN A  33     7887  10913   6840  -1508   2551    521       C  
ATOM    221  C   ASN A  33      -6.362  15.709  19.611  1.00 64.56           C  
ANISOU  221  C   ASN A  33     7507  10099   6922  -1593   2267    668       C  
ATOM    222  O   ASN A  33      -5.229  15.291  19.827  1.00 63.92           O  
ANISOU  222  O   ASN A  33     7643   9860   6781  -1601   2038    853       O  
ATOM    223  CB  ASN A  33      -7.815  15.815  21.655  1.00 72.56           C  
ANISOU  223  CB  ASN A  33     8461  11820   7287  -1734   2878    897       C  
ATOM    224  CG  ASN A  33      -8.331  16.653  22.835  1.00 76.73           C  
ANISOU  224  CG  ASN A  33     9031  12866   7256  -1646   3174    768       C  
ATOM    225  OD1 ASN A  33      -7.891  16.488  23.976  1.00 80.17           O  
ANISOU  225  OD1 ASN A  33     9693  13554   7212  -1693   3224   1002       O  
ATOM    226  ND2 ASN A  33      -9.275  17.547  22.560  1.00 77.54           N  
ANISOU  226  ND2 ASN A  33     8907  13145   7410  -1498   3364    380       N  
ATOM    227  N   ILE A  34      -7.049  15.408  18.508  1.00 63.23           N  
ANISOU  227  N   ILE A  34     7071   9754   7197  -1634   2272    545       N  
ATOM    228  CA AILE A  34      -6.587  14.422  17.525  0.50 61.39           C  
ANISOU  228  CA AILE A  34     6783   9129   7410  -1722   2042    626       C  
ATOM    229  CA BILE A  34      -6.578  14.420  17.533  0.50 61.42           C  
ANISOU  229  CA BILE A  34     6790   9134   7412  -1722   2041    628       C  
ATOM    230  C   ILE A  34      -5.604  15.039  16.528  1.00 57.18           C  
ANISOU  230  C   ILE A  34     6340   8418   6965  -1523   1740    353       C  
ATOM    231  O   ILE A  34      -5.894  16.067  15.924  1.00 55.33           O  
ANISOU  231  O   ILE A  34     6033   8274   6716  -1360   1731     47       O  
ATOM    232  CB AILE A  34      -7.785  13.825  16.757  0.50 62.38           C  
ANISOU  232  CB AILE A  34     6561   9185   7956  -1865   2163    563       C  
ATOM    233  CB BILE A  34      -7.768  13.788  16.788  0.50 62.54           C  
ANISOU  233  CB BILE A  34     6586   9200   7975  -1872   2164    578       C  
ATOM    234  CG1AILE A  34      -8.770  13.174  17.736  0.50 67.23           C  
ANISOU  234  CG1AILE A  34     7045   9977   8520  -2112   2497    868       C  
ATOM    235  CG1BILE A  34      -8.622  12.971  17.766  0.50 67.58           C  
ANISOU  235  CG1BILE A  34     7121   9965   8591  -2139   2469    929       C  
ATOM    236  CG2AILE A  34      -7.316  12.819  15.734  0.50 61.01           C  
ANISOU  236  CG2AILE A  34     6331   8611   8237  -1943   1917    568       C  
ATOM    237  CG2BILE A  34      -7.290  12.912  15.655  0.50 60.68           C  
ANISOU  237  CG2BILE A  34     6289   8574   8191  -1921   1903    534       C  
ATOM    238  CD1AILE A  34      -9.796  12.275  17.075  0.50 68.89           C  
ANISOU  238  CD1AILE A  34     6907  10041   9227  -2339   2583    879       C  
ATOM    239  CD1BILE A  34      -7.816  11.990  18.620  0.50 69.98           C  
ANISOU  239  CD1BILE A  34     7677  10101   8811  -2289   2413   1395       C  
ATOM    240  N   GLU A  35      -4.448  14.397  16.341  1.00 56.02           N  
ANISOU  240  N   GLU A  35     6336   8018   6929  -1533   1499    483       N  
ATOM    241  CA  GLU A  35      -3.394  14.941  15.480  1.00 52.46           C  
ANISOU  241  CA  GLU A  35     5960   7440   6531  -1367   1240    259       C  
ATOM    242  C   GLU A  35      -3.857  15.232  14.062  1.00 50.33           C  
ANISOU  242  C   GLU A  35     5482   7110   6530  -1294   1192    -34       C  
ATOM    243  O   GLU A  35      -3.627  16.313  13.532  1.00 48.16           O  
ANISOU  243  O   GLU A  35     5235   6907   6156  -1138   1126   -254       O  
ATOM    244  CB  GLU A  35      -2.214  13.984  15.394  1.00 52.50           C  
ANISOU  244  CB  GLU A  35     6064   7182   6700  -1392   1010    432       C  
ATOM    245  CG  GLU A  35      -1.524  13.684  16.719  1.00 55.14           C  
ANISOU  245  CG  GLU A  35     6621   7572   6754  -1426    970    751       C  
ATOM    246  CD  GLU A  35      -1.843  12.304  17.243  1.00 58.75           C  
ANISOU  246  CD  GLU A  35     7070   7859   7393  -1602   1028   1138       C  
ATOM    247  OE1 GLU A  35      -2.982  12.095  17.735  1.00 61.19           O  
ANISOU  247  OE1 GLU A  35     7297   8295   7655  -1753   1291   1282       O  
ATOM    248  OE2 GLU A  35      -0.944  11.435  17.153  1.00 59.43           O  
ANISOU  248  OE2 GLU A  35     7216   7670   7693  -1588    812   1303       O  
ATOM    249  N   LYS A  36      -4.477  14.233  13.438  1.00 51.53           N  
ANISOU  249  N   LYS A  36     5431   7117   7029  -1415   1205    -25       N  
ATOM    250  CA  LYS A  36      -5.036  14.358  12.092  1.00 50.17           C  
ANISOU  250  CA  LYS A  36     5035   6936   7092  -1359   1143   -306       C  
ATOM    251  C   LYS A  36      -5.709  15.718  11.935  1.00 49.42           C  
ANISOU  251  C   LYS A  36     4885   7093   6797  -1203   1235   -494       C  
ATOM    252  O   LYS A  36      -5.502  16.400  10.931  1.00 47.44           O  
ANISOU  252  O   LYS A  36     4608   6863   6552  -1051   1104   -693       O  
ATOM    253  CB  LYS A  36      -6.056  13.246  11.849  1.00 52.84           C  
ANISOU  253  CB  LYS A  36     5122   7173   7780  -1556   1223   -279       C  
ATOM    254  CG  LYS A  36      -6.946  13.385  10.573  1.00 52.98           C  
ANISOU  254  CG  LYS A  36     4850   7270   8008  -1514   1171   -593       C  
ATOM    255  CD  LYS A  36      -8.215  12.455  10.629  1.00 55.97           C  
ANISOU  255  CD  LYS A  36     4933   7618   8715  -1752   1304   -569       C  
ATOM    256  N   ASP A  37      -6.505  16.096  12.940  1.00 51.30           N  
ANISOU  256  N   ASP A  37     5106   7526   6858  -1231   1464   -420       N  
ATOM    257  CA  ASP A  37      -7.244  17.367  12.942  1.00 51.35           C  
ANISOU  257  CA  ASP A  37     5044   7753   6712  -1055   1571   -613       C  
ATOM    258  C   ASP A  37      -6.389  18.603  13.231  1.00 49.76           C  
ANISOU  258  C   ASP A  37     5101   7567   6236   -873   1492   -697       C  
ATOM    259  O   ASP A  37      -6.623  19.661  12.659  1.00 49.27           O  
ANISOU  259  O   ASP A  37     5011   7539   6169   -688   1448   -885       O  
ATOM    260  CB  ASP A  37      -8.375  17.315  13.946  1.00 54.63           C  
ANISOU  260  CB  ASP A  37     5321   8399   7035  -1136   1870   -544       C  
ATOM    261  CG  ASP A  37      -9.389  16.260  13.607  1.00 57.03           C  
ANISOU  261  CG  ASP A  37     5308   8698   7661  -1335   1966   -491       C  
ATOM    262  OD1 ASP A  37      -9.566  16.003  12.396  1.00 56.26           O  
ANISOU  262  OD1 ASP A  37     5038   8493   7842  -1317   1794   -648       O  
ATOM    263  OD2 ASP A  37     -10.013  15.696  14.539  1.00 60.19           O  
ANISOU  263  OD2 ASP A  37     5621   9218   8029  -1522   2215   -297       O  
ATOM    264  N   ILE A  38      -5.407  18.480  14.110  1.00 49.57           N  
ANISOU  264  N   ILE A  38     5321   7506   6006   -928   1456   -554       N  
ATOM    265  CA  ILE A  38      -4.449  19.564  14.303  1.00 48.33           C  
ANISOU  265  CA  ILE A  38     5393   7323   5646   -797   1334   -659       C  
ATOM    266  C   ILE A  38      -3.725  19.785  12.947  1.00 45.60           C  
ANISOU  266  C   ILE A  38     5033   6798   5492   -728   1110   -747       C  
ATOM    267  O   ILE A  38      -3.638  20.904  12.442  1.00 44.55           O  
ANISOU  267  O   ILE A  38     4938   6643   5344   -588   1053   -893       O  
ATOM    268  CB  ILE A  38      -3.423  19.239  15.430  1.00 49.14           C  
ANISOU  268  CB  ILE A  38     5729   7438   5502   -882   1279   -489       C  
ATOM    269  CG1 ILE A  38      -4.128  18.981  16.770  1.00 52.53           C  
ANISOU  269  CG1 ILE A  38     6183   8109   5666   -958   1516   -362       C  
ATOM    270  CG2 ILE A  38      -2.439  20.377  15.610  1.00 48.22           C  
ANISOU  270  CG2 ILE A  38     5811   7292   5215   -776   1132   -642       C  
ATOM    271  CD1 ILE A  38      -3.352  18.079  17.715  1.00 54.12           C  
ANISOU  271  CD1 ILE A  38     6551   8322   5690  -1089   1456    -60       C  
ATOM    272  N   ALA A  39      -3.234  18.681  12.383  1.00 44.77           N  
ANISOU  272  N   ALA A  39     4871   6567   5571   -829    999   -647       N  
ATOM    273  CA  ALA A  39      -2.598  18.629  11.064  1.00 42.77           C  
ANISOU  273  CA  ALA A  39     4563   6207   5479   -781    822   -734       C  
ATOM    274  C   ALA A  39      -3.379  19.344   9.955  1.00 42.25           C  
ANISOU  274  C   ALA A  39     4352   6216   5485   -655    818   -894       C  
ATOM    275  O   ALA A  39      -2.818  20.089   9.177  1.00 41.06           O  
ANISOU  275  O   ALA A  39     4252   6045   5304   -561    711   -951       O  
ATOM    276  CB  ALA A  39      -2.384  17.170  10.675  1.00 42.88           C  
ANISOU  276  CB  ALA A  39     4473   6094   5726   -894    752   -667       C  
ATOM    277  N   ALA A  40      -4.677  19.102   9.879  1.00 43.67           N  
ANISOU  277  N   ALA A  40     4335   6494   5762   -658    929   -944       N  
ATOM    278  CA  ALA A  40      -5.501  19.744   8.869  1.00 43.78           C  
ANISOU  278  CA  ALA A  40     4185   6608   5838   -513    895  -1083       C  
ATOM    279  C   ALA A  40      -5.642  21.242   9.167  1.00 44.36           C  
ANISOU  279  C   ALA A  40     4377   6708   5769   -333    932  -1127       C  
ATOM    280  O   ALA A  40      -5.452  22.081   8.265  1.00 43.79           O  
ANISOU  280  O   ALA A  40     4333   6611   5692   -193    815  -1160       O  
ATOM    281  CB  ALA A  40      -6.842  19.082   8.798  1.00 45.44           C  
ANISOU  281  CB  ALA A  40     4115   6932   6217   -571    992  -1140       C  
ATOM    282  N   TYR A  41      -5.942  21.584  10.426  1.00 45.47           N  
ANISOU  282  N   TYR A  41     4595   6891   5789   -333   1094  -1127       N  
ATOM    283  CA  TYR A  41      -6.090  22.983  10.820  1.00 46.33           C  
ANISOU  283  CA  TYR A  41     4818   6986   5797   -152   1131  -1232       C  
ATOM    284  C   TYR A  41      -4.938  23.844  10.286  1.00 45.00           C  
ANISOU  284  C   TYR A  41     4860   6633   5603    -98    956  -1214       C  
ATOM    285  O   TYR A  41      -5.159  24.941   9.744  1.00 45.84           O  
ANISOU  285  O   TYR A  41     4989   6662   5767     74    897  -1267       O  
ATOM    286  CB  TYR A  41      -6.154  23.112  12.343  1.00 48.13           C  
ANISOU  286  CB  TYR A  41     5163   7298   5826   -191   1308  -1260       C  
ATOM    287  CG  TYR A  41      -6.402  24.528  12.838  1.00 49.81           C  
ANISOU  287  CG  TYR A  41     5478   7488   5957     12   1358  -1450       C  
ATOM    288  CD1 TYR A  41      -7.674  24.958  13.171  1.00 51.73           C  
ANISOU  288  CD1 TYR A  41     5543   7884   6226    170   1536  -1603       C  
ATOM    289  CD2 TYR A  41      -5.343  25.431  12.976  1.00 49.45           C  
ANISOU  289  CD2 TYR A  41     5687   7251   5848     44   1225  -1503       C  
ATOM    290  CE1 TYR A  41      -7.890  26.244  13.620  1.00 54.31           C  
ANISOU  290  CE1 TYR A  41     5962   8154   6519    387   1574  -1823       C  
ATOM    291  CE2 TYR A  41      -5.550  26.722  13.431  1.00 51.42           C  
ANISOU  291  CE2 TYR A  41     6040   7415   6079    225   1253  -1714       C  
ATOM    292  CZ  TYR A  41      -6.821  27.127  13.751  1.00 54.04           C  
ANISOU  292  CZ  TYR A  41     6211   7879   6440    413   1424  -1884       C  
ATOM    293  OH  TYR A  41      -7.023  28.423  14.206  1.00 56.89           O  
ANISOU  293  OH  TYR A  41     6674   8120   6822    627   1445  -2140       O  
ATOM    294  N   ILE A  42      -3.714  23.341  10.432  1.00 43.34           N  
ANISOU  294  N   ILE A  42     4787   6347   5334   -248    870  -1121       N  
ATOM    295  CA  ILE A  42      -2.526  24.109  10.083  1.00 42.44           C  
ANISOU  295  CA  ILE A  42     4844   6079   5200   -249    731  -1097       C  
ATOM    296  C   ILE A  42      -2.321  24.189   8.564  1.00 41.52           C  
ANISOU  296  C   ILE A  42     4642   5947   5187   -207    615  -1035       C  
ATOM    297  O   ILE A  42      -2.206  25.280   8.002  1.00 42.27           O  
ANISOU  297  O   ILE A  42     4805   5945   5310   -109    558  -1013       O  
ATOM    298  CB  ILE A  42      -1.289  23.510  10.733  1.00 41.48           C  
ANISOU  298  CB  ILE A  42     4843   5926   4991   -411    669  -1029       C  
ATOM    299  CG1 ILE A  42      -1.420  23.532  12.261  1.00 43.69           C  
ANISOU  299  CG1 ILE A  42     5238   6273   5088   -443    763  -1073       C  
ATOM    300  CG2 ILE A  42      -0.082  24.295  10.343  1.00 41.29           C  
ANISOU  300  CG2 ILE A  42     4938   5768   4982   -439    537  -1017       C  
ATOM    301  CD1 ILE A  42      -0.666  22.403  12.973  1.00 43.62           C  
ANISOU  301  CD1 ILE A  42     5275   6310   4988   -591    720   -937       C  
ATOM    302  N   LYS A  43      -2.273  23.035   7.910  1.00 40.35           N  
ANISOU  302  N   LYS A  43     4350   5891   5088   -282    581  -1005       N  
ATOM    303  CA  LYS A  43      -2.135  22.972   6.468  1.00 39.83           C  
ANISOU  303  CA  LYS A  43     4185   5895   5055   -238    482   -983       C  
ATOM    304  C   LYS A  43      -3.087  23.952   5.824  1.00 41.34           C  
ANISOU  304  C   LYS A  43     4325   6126   5256    -54    464   -982       C  
ATOM    305  O   LYS A  43      -2.717  24.676   4.894  1.00 41.93           O  
ANISOU  305  O   LYS A  43     4446   6192   5291     12    381   -887       O  
ATOM    306  CB  LYS A  43      -2.443  21.563   5.960  1.00 39.70           C  
ANISOU  306  CB  LYS A  43     3975   5988   5119   -305    462  -1049       C  
ATOM    307  CG  LYS A  43      -2.402  21.384   4.441  1.00 39.71           C  
ANISOU  307  CG  LYS A  43     3850   6136   5102   -247    356  -1092       C  
ATOM    308  CD  LYS A  43      -3.721  21.641   3.766  1.00 40.89           C  
ANISOU  308  CD  LYS A  43     3833   6436   5265   -112    324  -1153       C  
ATOM    309  CE  LYS A  43      -3.801  20.967   2.394  1.00 42.12           C  
ANISOU  309  CE  LYS A  43     3818   6798   5385    -91    205  -1264       C  
ATOM    310  NZ  LYS A  43      -2.803  21.458   1.385  1.00 41.95           N  
ANISOU  310  NZ  LYS A  43     3884   6876   5178    -51    140  -1178       N  
ATOM    311  N   LYS A  44      -4.323  23.971   6.315  1.00 42.39           N  
ANISOU  311  N   LYS A  44     4345   6313   5445     32    545  -1066       N  
ATOM    312  CA  LYS A  44      -5.363  24.811   5.718  1.00 44.23           C  
ANISOU  312  CA  LYS A  44     4479   6600   5726    249    507  -1079       C  
ATOM    313  C   LYS A  44      -5.059  26.292   5.879  1.00 45.19           C  
ANISOU  313  C   LYS A  44     4804   6514   5853    379    483  -1013       C  
ATOM    314  O   LYS A  44      -5.157  27.054   4.915  1.00 46.13           O  
ANISOU  314  O   LYS A  44     4935   6605   5987    519    371   -897       O  
ATOM    315  CB  LYS A  44      -6.748  24.464   6.293  1.00 45.68           C  
ANISOU  315  CB  LYS A  44     4445   6913   5998    309    620  -1210       C  
ATOM    316  CG  LYS A  44      -7.292  23.118   5.788  1.00 45.65           C  
ANISOU  316  CG  LYS A  44     4183   7093   6068    194    601  -1275       C  
ATOM    317  CD  LYS A  44      -8.446  22.595   6.607  1.00 47.26           C  
ANISOU  317  CD  LYS A  44     4171   7406   6379    151    763  -1373       C  
ATOM    318  CE  LYS A  44      -9.022  21.342   6.002  1.00 47.80           C  
ANISOU  318  CE  LYS A  44     3965   7609   6587     18    717  -1451       C  
ATOM    319  NZ  LYS A  44     -10.189  20.883   6.790  1.00 49.89           N  
ANISOU  319  NZ  LYS A  44     3983   7986   6985    -55    899  -1518       N  
ATOM    320  N   GLU A  45      -4.668  26.665   7.104  1.00 45.32           N  
ANISOU  320  N   GLU A  45     4983   6380   5855    325    575  -1083       N  
ATOM    321  CA AGLU A  45      -4.378  28.053   7.449  0.50 46.58           C  
ANISOU  321  CA AGLU A  45     5342   6285   6070    427    552  -1091       C  
ATOM    322  CA BGLU A  45      -4.353  28.054   7.452  0.50 46.52           C  
ANISOU  322  CA BGLU A  45     5337   6275   6061    424    551  -1090       C  
ATOM    323  C   GLU A  45      -3.208  28.565   6.603  1.00 46.11           C  
ANISOU  323  C   GLU A  45     5426   6075   6016    340    429   -900       C  
ATOM    324  O   GLU A  45      -3.247  29.673   6.085  1.00 48.04           O  
ANISOU  324  O   GLU A  45     5759   6130   6363    462    356   -794       O  
ATOM    325  CB AGLU A  45      -4.084  28.177   8.953  0.50 46.91           C  
ANISOU  325  CB AGLU A  45     5521   6257   6046    352    660  -1258       C  
ATOM    326  CB BGLU A  45      -3.989  28.185   8.937  0.50 46.78           C  
ANISOU  326  CB BGLU A  45     5515   6230   6027    341    652  -1250       C  
ATOM    327  CG AGLU A  45      -4.865  29.302   9.679  0.50 49.86           C  
ANISOU  327  CG AGLU A  45     5942   6501   6498    570    728  -1453       C  
ATOM    328  CG BGLU A  45      -3.689  29.632   9.371  0.50 48.73           C  
ANISOU  328  CG BGLU A  45     5968   6178   6368    437    615  -1341       C  
ATOM    329  CD AGLU A  45      -6.407  29.139   9.647  0.50 50.70           C  
ANISOU  329  CD AGLU A  45     5795   6802   6665    778    833  -1552       C  
ATOM    330  CD BGLU A  45      -4.166  29.965  10.787  0.50 50.39           C  
ANISOU  330  CD BGLU A  45     6232   6399   6515    513    745  -1617       C  
ATOM    331  OE1AGLU A  45      -6.959  28.122  10.149  0.50 48.36           O  
ANISOU  331  OE1AGLU A  45     5332   6768   6274    692    973  -1603       O  
ATOM    332  OE1BGLU A  45      -4.897  29.147  11.388  0.50 50.33           O  
ANISOU  332  OE1BGLU A  45     6082   6659   6382    511    892  -1695       O  
ATOM    333  OE2AGLU A  45      -7.064  30.065   9.127  0.50 52.00           O  
ANISOU  333  OE2AGLU A  45     5915   6843   6997   1028    771  -1566       O  
ATOM    334  OE2BGLU A  45      -3.806  31.052  11.300  0.50 52.03           O  
ANISOU  334  OE2BGLU A  45     6620   6352   6796    565    706  -1766       O  
ATOM    335  N   PHE A  46      -2.185  27.745   6.450  1.00 44.17           N  
ANISOU  335  N   PHE A  46     5188   5914   5680    132    412   -842       N  
ATOM    336  CA  PHE A  46      -1.037  28.138   5.644  1.00 44.40           C  
ANISOU  336  CA  PHE A  46     5303   5866   5701     24    334   -664       C  
ATOM    337  C   PHE A  46      -1.332  28.170   4.141  1.00 45.16           C  
ANISOU  337  C   PHE A  46     5297   6112   5747    117    267   -488       C  
ATOM    338  O   PHE A  46      -0.765  28.980   3.415  1.00 46.67           O  
ANISOU  338  O   PHE A  46     5580   6209   5944     99    220   -282       O  
ATOM    339  CB  PHE A  46       0.179  27.253   5.946  1.00 42.76           C  
ANISOU  339  CB  PHE A  46     5093   5729   5422   -196    338   -683       C  
ATOM    340  CG  PHE A  46       1.029  27.762   7.096  1.00 43.36           C  
ANISOU  340  CG  PHE A  46     5331   5614   5530   -318    331   -760       C  
ATOM    341  CD1 PHE A  46       2.353  28.127   6.889  1.00 43.50           C  
ANISOU  341  CD1 PHE A  46     5404   5542   5582   -485    275   -673       C  
ATOM    342  CD2 PHE A  46       0.494  27.893   8.382  1.00 43.57           C  
ANISOU  342  CD2 PHE A  46     5432   5587   5535   -269    380   -938       C  
ATOM    343  CE1 PHE A  46       3.128  28.617   7.939  1.00 44.26           C  
ANISOU  343  CE1 PHE A  46     5623   5476   5716   -606    233   -779       C  
ATOM    344  CE2 PHE A  46       1.263  28.369   9.423  1.00 44.30           C  
ANISOU  344  CE2 PHE A  46     5669   5547   5614   -373    346  -1049       C  
ATOM    345  CZ  PHE A  46       2.581  28.737   9.201  1.00 44.78           C  
ANISOU  345  CZ  PHE A  46     5781   5497   5735   -543    253   -979       C  
ATOM    346  N   ASP A  47      -2.212  27.293   3.671  1.00 44.74           N  
ANISOU  346  N   ASP A  47     5051   6311   5636    200    258   -560       N  
ATOM    347  CA  ASP A  47      -2.641  27.354   2.273  1.00 45.78           C  
ANISOU  347  CA  ASP A  47     5077   6643   5675    321    164   -430       C  
ATOM    348  C   ASP A  47      -3.283  28.707   2.005  1.00 48.41           C  
ANISOU  348  C   ASP A  47     5494   6808   6092    533     98   -272       C  
ATOM    349  O   ASP A  47      -3.110  29.281   0.936  1.00 50.20           O  
ANISOU  349  O   ASP A  47     5760   7078   6234    596     13    -27       O  
ATOM    350  CB  ASP A  47      -3.630  26.229   1.941  1.00 45.53           C  
ANISOU  350  CB  ASP A  47     4798   6889   5610    378    139   -602       C  
ATOM    351  CG  ASP A  47      -2.954  24.972   1.449  1.00 43.72           C  
ANISOU  351  CG  ASP A  47     4471   6856   5283    221    135   -694       C  
ATOM    352  OD1 ASP A  47      -1.804  25.025   1.022  1.00 44.34           O  
ANISOU  352  OD1 ASP A  47     4631   6948   5265    117    141   -596       O  
ATOM    353  OD2 ASP A  47      -3.575  23.912   1.465  1.00 43.72           O  
ANISOU  353  OD2 ASP A  47     4291   6992   5329    199    129   -879       O  
ATOM    354  N   LYS A  48      -4.020  29.211   2.987  1.00 49.22           N  
ANISOU  354  N   LYS A  48     5621   6722   6357    656    140   -406       N  
ATOM    355  CA  LYS A  48      -4.734  30.475   2.834  1.00 52.31           C  
ANISOU  355  CA  LYS A  48     6073   6905   6896    908     68   -304       C  
ATOM    356  C   LYS A  48      -3.798  31.684   2.845  1.00 53.77           C  
ANISOU  356  C   LYS A  48     6520   6716   7193    848     42   -106       C  
ATOM    357  O   LYS A  48      -3.855  32.545   1.959  1.00 56.15           O  
ANISOU  357  O   LYS A  48     6895   6902   7536    968    -63    177       O  
ATOM    358  CB  LYS A  48      -5.789  30.646   3.932  1.00 53.03           C  
ANISOU  358  CB  LYS A  48     6085   6924   7140   1074    148   -567       C  
ATOM    359  CG  LYS A  48      -6.741  31.807   3.622  1.00 56.87           C  
ANISOU  359  CG  LYS A  48     6557   7239   7809   1410     49   -497       C  
ATOM    360  CD  LYS A  48      -7.708  32.124   4.740  1.00 58.11           C  
ANISOU  360  CD  LYS A  48     6628   7318   8133   1600    154   -793       C  
ATOM    361  CE  LYS A  48      -8.319  33.479   4.492  1.00 62.31           C  
ANISOU  361  CE  LYS A  48     7212   7550   8911   1939     40   -719       C  
ATOM    362  NZ  LYS A  48      -9.727  33.553   4.969  1.00 65.43           N  
ANISOU  362  NZ  LYS A  48     7348   8069   9443   2236     93   -973       N  
ATOM    363  N   LYS A  49      -2.965  31.751   3.873  1.00 52.61           N  
ANISOU  363  N   LYS A  49     6509   6376   7105    658    126   -246       N  
ATOM    364  CA  LYS A  49      -2.113  32.922   4.085  1.00 54.59           C  
ANISOU  364  CA  LYS A  49     6989   6223   7529    569     98   -133       C  
ATOM    365  C   LYS A  49      -1.006  32.966   3.050  1.00 54.71           C  
ANISOU  365  C   LYS A  49     7049   6286   7452    364     70    187       C  
ATOM    366  O   LYS A  49      -0.748  34.007   2.440  1.00 57.88           O  
ANISOU  366  O   LYS A  49     7578   6433   7978    375     11    474       O  
ATOM    367  CB  LYS A  49      -1.457  32.903   5.474  1.00 53.61           C  
ANISOU  367  CB  LYS A  49     6969   5943   7455    399    168   -412       C  
ATOM    368  CG  LYS A  49      -2.342  33.241   6.682  1.00 54.56           C  
ANISOU  368  CG  LYS A  49     7109   5948   7673    582    223   -743       C  
ATOM    369  CD  LYS A  49      -1.507  33.096   7.973  1.00 53.25           C  
ANISOU  369  CD  LYS A  49     7052   5725   7453    377    271   -995       C  
ATOM    370  CE  LYS A  49      -2.346  33.009   9.232  1.00 54.15           C  
ANISOU  370  CE  LYS A  49     7144   5916   7512    520    375  -1344       C  
ATOM    371  NZ  LYS A  49      -1.652  32.307  10.373  1.00 51.81           N  
ANISOU  371  NZ  LYS A  49     6891   5786   7006    314    427  -1527       N  
ATOM    372  N   TYR A  50      -0.358  31.829   2.854  1.00 51.88           N  
ANISOU  372  N   TYR A  50     6576   6249   6886    180    123    146       N  
ATOM    373  CA  TYR A  50       0.887  31.779   2.102  1.00 52.07           C  
ANISOU  373  CA  TYR A  50     6611   6355   6815    -48    144    370       C  
ATOM    374  C   TYR A  50       0.800  30.991   0.784  1.00 51.88           C  
ANISOU  374  C   TYR A  50     6428   6765   6517    -15    140    514       C  
ATOM    375  O   TYR A  50       1.826  30.578   0.239  1.00 52.07           O  
ANISOU  375  O   TYR A  50     6396   6982   6405   -201    197    601       O  
ATOM    376  CB  TYR A  50       1.973  31.161   2.981  1.00 49.76           C  
ANISOU  376  CB  TYR A  50     6305   6076   6526   -293    201    172       C  
ATOM    377  CG  TYR A  50       2.066  31.770   4.343  1.00 50.30           C  
ANISOU  377  CG  TYR A  50     6513   5811   6788   -328    188    -39       C  
ATOM    378  CD1 TYR A  50       2.573  33.037   4.515  1.00 52.94           C  
ANISOU  378  CD1 TYR A  50     7010   5757   7348   -417    149     53       C  
ATOM    379  CD2 TYR A  50       1.649  31.071   5.474  1.00 48.74           C  
ANISOU  379  CD2 TYR A  50     6285   5693   6539   -284    215   -339       C  
ATOM    380  CE1 TYR A  50       2.670  33.601   5.775  1.00 53.76           C  
ANISOU  380  CE1 TYR A  50     7240   5569   7617   -446    120   -211       C  
ATOM    381  CE2 TYR A  50       1.742  31.634   6.743  1.00 49.34           C  
ANISOU  381  CE2 TYR A  50     6492   5530   6723   -307    204   -564       C  
ATOM    382  CZ  TYR A  50       2.252  32.892   6.878  1.00 51.60           C  
ANISOU  382  CZ  TYR A  50     6934   5445   7225   -380    148   -531       C  
ATOM    383  OH  TYR A  50       2.341  33.437   8.122  1.00 52.86           O  
ANISOU  383  OH  TYR A  50     7218   5388   7476   -396    120   -819       O  
ATOM    384  N   ASN A  51      -0.398  30.760   0.272  1.00 52.28           N  
ANISOU  384  N   ASN A  51     6381   7001   6479    221     71    501       N  
ATOM    385  CA  ASN A  51      -0.564  30.011  -0.987  1.00 52.48           C  
ANISOU  385  CA  ASN A  51     6250   7472   6218    269     36    575       C  
ATOM    386  C   ASN A  51      -0.276  28.504  -0.894  1.00 49.62           C  
ANISOU  386  C   ASN A  51     5711   7408   5733    159     88    280       C  
ATOM    387  O   ASN A  51       0.621  28.067  -0.164  1.00 47.58           O  
ANISOU  387  O   ASN A  51     5469   7059   5549    -25    169    150       O  
ATOM    388  CB  ASN A  51       0.298  30.607  -2.113  1.00 54.94           C  
ANISOU  388  CB  ASN A  51     6633   7881   6361    170     54    953       C  
ATOM    389  CG  ASN A  51      -0.202  31.944  -2.576  1.00 58.80           C  
ANISOU  389  CG  ASN A  51     7271   8137   6931    326    -37   1320       C  
ATOM    390  OD1 ASN A  51      -1.411  32.186  -2.623  1.00 60.15           O  
ANISOU  390  OD1 ASN A  51     7415   8284   7155    596   -159   1302       O  
ATOM    391  ND2 ASN A  51       0.722  32.822  -2.944  1.00 61.26           N  
ANISOU  391  ND2 ASN A  51     7727   8270   7279    159     16   1673       N  
ATOM    392  N   PRO A  52      -1.030  27.707  -1.668  1.00 49.80           N  
ANISOU  392  N   PRO A  52     5557   7778   5584    281     18    170       N  
ATOM    393  CA  PRO A  52      -0.767  26.270  -1.778  1.00 47.98           C  
ANISOU  393  CA  PRO A  52     5156   7803   5269    188     46   -111       C  
ATOM    394  C   PRO A  52       0.564  25.963  -2.446  1.00 48.21           C  
ANISOU  394  C   PRO A  52     5172   8021   5125     34    123    -54       C  
ATOM    395  O   PRO A  52       1.057  26.775  -3.221  1.00 50.34           O  
ANISOU  395  O   PRO A  52     5517   8371   5238     16    144    236       O  
ATOM    396  CB  PRO A  52      -1.917  25.747  -2.641  1.00 49.31           C  
ANISOU  396  CB  PRO A  52     5143   8294   5298    362    -79   -227       C  
ATOM    397  CG  PRO A  52      -2.567  26.942  -3.239  1.00 52.42           C  
ANISOU  397  CG  PRO A  52     5611   8688   5617    554   -181     66       C  
ATOM    398  CD  PRO A  52      -2.185  28.147  -2.469  1.00 52.33           C  
ANISOU  398  CD  PRO A  52     5821   8250   5811    525   -118    290       C  
ATOM    399  N   THR A  53       1.119  24.773  -2.218  1.00 46.70           N  
ANISOU  399  N   THR A  53     4864   7919   4961    -67    168   -319       N  
ATOM    400  CA  THR A  53       0.432  23.645  -1.571  1.00 44.87           C  
ANISOU  400  CA  THR A  53     4518   7643   4888    -47    132   -626       C  
ATOM    401  C   THR A  53       1.224  23.159  -0.385  1.00 42.72           C  
ANISOU  401  C   THR A  53     4290   7124   4816   -193    200   -719       C  
ATOM    402  O   THR A  53       2.315  22.611  -0.570  1.00 42.62           O  
ANISOU  402  O   THR A  53     4224   7188   4782   -284    241   -784       O  
ATOM    403  CB  THR A  53       0.276  22.448  -2.532  1.00 45.74           C  
ANISOU  403  CB  THR A  53     4425   8087   4866     -9     78   -887       C  
ATOM    404  OG1 THR A  53      -0.229  22.895  -3.791  1.00 48.28           O  
ANISOU  404  OG1 THR A  53     4702   8735   4906    121     -2   -792       O  
ATOM    405  CG2 THR A  53      -0.693  21.422  -1.950  1.00 45.14           C  
ANISOU  405  CG2 THR A  53     4225   7922   5004      0     23  -1158       C  
ATOM    406  N   TRP A  54       0.688  23.375   0.820  1.00 41.49           N  
ANISOU  406  N   TRP A  54     4221   6708   4834   -197    211   -727       N  
ATOM    407  CA  TRP A  54       1.349  22.937   2.063  1.00 39.99           C  
ANISOU  407  CA  TRP A  54     4092   6311   4790   -321    253   -790       C  
ATOM    408  C   TRP A  54       0.930  21.520   2.475  1.00 39.36           C  
ANISOU  408  C   TRP A  54     3890   6237   4828   -343    242   -988       C  
ATOM    409  O   TRP A  54      -0.149  21.037   2.113  1.00 40.05           O  
ANISOU  409  O   TRP A  54     3855   6419   4942   -276    215  -1097       O  
ATOM    410  CB  TRP A  54       1.020  23.883   3.215  1.00 39.54           C  
ANISOU  410  CB  TRP A  54     4201   6009   4813   -317    280   -715       C  
ATOM    411  CG  TRP A  54       1.549  25.243   3.039  1.00 41.02           C  
ANISOU  411  CG  TRP A  54     4530   6075   4980   -332    280   -534       C  
ATOM    412  CD1 TRP A  54       0.949  26.275   2.381  1.00 43.20           C  
ANISOU  412  CD1 TRP A  54     4858   6329   5227   -213    256   -384       C  
ATOM    413  CD2 TRP A  54       2.793  25.758   3.539  1.00 41.20           C  
ANISOU  413  CD2 TRP A  54     4656   5949   5050   -484    289   -470       C  
ATOM    414  NE1 TRP A  54       1.744  27.406   2.438  1.00 44.37           N  
ANISOU  414  NE1 TRP A  54     5153   6277   5425   -297    262   -211       N  
ATOM    415  CE2 TRP A  54       2.880  27.111   3.140  1.00 42.59           C  
ANISOU  415  CE2 TRP A  54     4948   5983   5249   -478    284   -281       C  
ATOM    416  CE3 TRP A  54       3.845  25.200   4.281  1.00 40.76           C  
ANISOU  416  CE3 TRP A  54     4589   5859   5038   -622    281   -548       C  
ATOM    417  CZ2 TRP A  54       3.970  27.913   3.453  1.00 43.75           C  
ANISOU  417  CZ2 TRP A  54     5191   5946   5486   -642    285   -190       C  
ATOM    418  CZ3 TRP A  54       4.936  25.988   4.587  1.00 41.35           C  
ANISOU  418  CZ3 TRP A  54     4737   5803   5170   -763    266   -474       C  
ATOM    419  CH2 TRP A  54       4.988  27.342   4.181  1.00 43.25           C  
ANISOU  419  CH2 TRP A  54     5085   5890   5456   -791    275   -308       C  
ATOM    420  N   HIS A  55       1.774  20.883   3.275  1.00 38.39           N  
ANISOU  420  N   HIS A  55     3795   5990   4801   -442    250  -1018       N  
ATOM    421  CA  HIS A  55       1.480  19.580   3.865  1.00 38.20           C  
ANISOU  421  CA  HIS A  55     3697   5883   4934   -482    239  -1131       C  
ATOM    422  C   HIS A  55       1.860  19.640   5.334  1.00 37.63           C  
ANISOU  422  C   HIS A  55     3767   5625   4905   -559    260  -1030       C  
ATOM    423  O   HIS A  55       2.653  20.479   5.712  1.00 37.62           O  
ANISOU  423  O   HIS A  55     3881   5581   4830   -590    253   -944       O  
ATOM    424  CB  HIS A  55       2.251  18.489   3.133  1.00 38.71           C  
ANISOU  424  CB  HIS A  55     3623   6014   5069   -487    189  -1281       C  
ATOM    425  CG  HIS A  55       2.156  18.596   1.645  1.00 39.21           C  
ANISOU  425  CG  HIS A  55     3565   6339   4991   -408    171  -1393       C  
ATOM    426  ND1 HIS A  55       1.017  18.280   0.954  1.00 40.36           N  
ANISOU  426  ND1 HIS A  55     3597   6615   5123   -347    131  -1528       N  
ATOM    427  CD2 HIS A  55       3.046  19.017   0.721  1.00 40.31           C  
ANISOU  427  CD2 HIS A  55     3672   6679   4962   -386    190  -1378       C  
ATOM    428  CE1 HIS A  55       1.211  18.494  -0.336  1.00 41.61           C  
ANISOU  428  CE1 HIS A  55     3676   7056   5076   -273    106  -1598       C  
ATOM    429  NE2 HIS A  55       2.436  18.940  -0.503  1.00 41.09           N  
ANISOU  429  NE2 HIS A  55     3662   7044   4905   -300    160  -1495       N  
ATOM    430  N   CYS A  56       1.272  18.789   6.167  1.00 37.96           N  
ANISOU  430  N   CYS A  56     3797   5571   5052   -602    283  -1031       N  
ATOM    431  CA  CYS A  56       1.534  18.855   7.602  1.00 38.28           C  
ANISOU  431  CA  CYS A  56     3985   5502   5057   -665    304   -913       C  
ATOM    432  C   CYS A  56       1.303  17.561   8.316  1.00 38.82           C  
ANISOU  432  C   CYS A  56     4024   5466   5259   -735    308   -858       C  
ATOM    433  O   CYS A  56       0.213  17.035   8.297  1.00 39.74           O  
ANISOU  433  O   CYS A  56     4049   5578   5472   -763    377   -878       O  
ATOM    434  CB  CYS A  56       0.662  19.928   8.293  1.00 38.95           C  
ANISOU  434  CB  CYS A  56     4174   5610   5014   -634    400   -883       C  
ATOM    435  SG  CYS A  56       0.909  20.055  10.128  1.00 39.72           S  
ANISOU  435  SG  CYS A  56     4461   5661   4967   -701    437   -784       S  
ATOM    436  N   ILE A  57       2.335  17.103   9.003  1.00 39.24           N  
ANISOU  436  N   ILE A  57     4150   5430   5328   -769    226   -764       N  
ATOM    437  CA  ILE A  57       2.291  15.879   9.769  1.00 40.90           C  
ANISOU  437  CA  ILE A  57     4367   5499   5671   -829    203   -635       C  
ATOM    438  C   ILE A  57       2.492  16.222  11.241  1.00 41.71           C  
ANISOU  438  C   ILE A  57     4655   5628   5563   -871    214   -448       C  
ATOM    439  O   ILE A  57       3.423  16.947  11.587  1.00 41.56           O  
ANISOU  439  O   ILE A  57     4728   5666   5395   -847    130   -451       O  
ATOM    440  CB  ILE A  57       3.391  14.881   9.322  1.00 41.54           C  
ANISOU  440  CB  ILE A  57     4364   5449   5967   -790     56   -672       C  
ATOM    441  CG1 ILE A  57       3.499  14.827   7.797  1.00 40.83           C  
ANISOU  441  CG1 ILE A  57     4103   5429   5979   -721     40   -921       C  
ATOM    442  CG2 ILE A  57       3.127  13.503   9.891  1.00 43.37           C  
ANISOU  442  CG2 ILE A  57     4587   5457   6431   -843     26   -531       C  
ATOM    443  CD1 ILE A  57       2.187  14.707   7.092  1.00 40.26           C  
ANISOU  443  CD1 ILE A  57     3928   5405   5963   -740    122  -1045       C  
ATOM    444  N   VAL A  58       1.627  15.672  12.087  1.00 43.21           N  
ANISOU  444  N   VAL A  58     4882   5800   5737   -947    318   -292       N  
ATOM    445  CA  VAL A  58       1.645  15.923  13.520  1.00 45.00           C  
ANISOU  445  CA  VAL A  58     5282   6122   5694   -987    358   -110       C  
ATOM    446  C   VAL A  58       1.651  14.587  14.273  1.00 47.56           C  
ANISOU  446  C   VAL A  58     5637   6317   6115  -1069    335    176       C  
ATOM    447  O   VAL A  58       0.823  13.726  14.031  1.00 48.40           O  
ANISOU  447  O   VAL A  58     5637   6302   6448  -1153    428    245       O  
ATOM    448  CB  VAL A  58       0.404  16.748  13.957  1.00 45.48           C  
ANISOU  448  CB  VAL A  58     5363   6361   5556  -1000    573   -167       C  
ATOM    449  CG1 VAL A  58       0.479  17.115  15.435  1.00 47.19           C  
ANISOU  449  CG1 VAL A  58     5764   6745   5420  -1022    624    -42       C  
ATOM    450  CG2 VAL A  58       0.269  17.992  13.104  1.00 43.78           C  
ANISOU  450  CG2 VAL A  58     5109   6202   5323   -900    582   -415       C  
ATOM    451  N   GLY A  59       2.591  14.423  15.194  1.00 49.09           N  
ANISOU  451  N   GLY A  59     5973   6528   6151  -1051    195    358       N  
ATOM    452  CA  GLY A  59       2.692  13.179  15.948  1.00 51.96           C  
ANISOU  452  CA  GLY A  59     6394   6749   6599  -1108    141    700       C  
ATOM    453  C   GLY A  59       3.861  13.119  16.896  1.00 53.48           C  
ANISOU  453  C   GLY A  59     6732   7002   6582  -1044    -72    889       C  
ATOM    454  O   GLY A  59       4.546  14.107  17.096  1.00 52.59           O  
ANISOU  454  O   GLY A  59     6677   7074   6231   -982   -166    729       O  
ATOM    455  N   ARG A  60       4.090  11.938  17.454  1.00 56.59           N  
ANISOU  455  N   ARG A  60     7177   7222   7100  -1061   -170   1235       N  
ATOM    456  CA  ARG A  60       5.105  11.737  18.495  1.00 59.29           C  
ANISOU  456  CA  ARG A  60     7662   7644   7218   -988   -401   1494       C  
ATOM    457  C   ARG A  60       6.118  10.656  18.138  1.00 60.64           C  
ANISOU  457  C   ARG A  60     7754   7497   7789   -867   -669   1613       C  
ATOM    458  O   ARG A  60       7.271  10.751  18.570  1.00 61.96           O  
ANISOU  458  O   ARG A  60     7947   7744   7847   -744   -928   1662       O  
ATOM    459  CB  ARG A  60       4.443  11.423  19.841  1.00 63.11           C  
ANISOU  459  CB  ARG A  60     8331   8296   7349  -1095   -281   1900       C  
ATOM    460  N   ASN A  61       5.699   9.643  17.369  1.00 60.92           N  
ANISOU  460  N   ASN A  61     7672   7173   8302   -893   -622   1628       N  
ATOM    461  CA  ASN A  61       6.579   8.539  16.967  1.00 62.75           C  
ANISOU  461  CA  ASN A  61     7811   7043   8987   -751   -864   1691       C  
ATOM    462  C   ASN A  61       6.515   8.321  15.466  1.00 60.26           C  
ANISOU  462  C   ASN A  61     7272   6523   9100   -707   -823   1276       C  
ATOM    463  O   ASN A  61       5.919   7.361  14.986  1.00 61.84           O  
ANISOU  463  O   ASN A  61     7403   6389   9703   -763   -770   1286       O  
ATOM    464  CB  ASN A  61       6.242   7.244  17.716  1.00 67.40           C  
ANISOU  464  CB  ASN A  61     8513   7317   9777   -809   -903   2190       C  
ATOM    465  CG  ASN A  61       6.602   7.301  19.190  1.00 70.88           C  
ANISOU  465  CG  ASN A  61     9176   7981   9774   -796  -1019   2647       C  
ATOM    466  OD1 ASN A  61       7.373   6.479  19.681  1.00 74.72           O  
ANISOU  466  OD1 ASN A  61     9717   8267  10405   -666  -1279   2973       O  
ATOM    467  ND2 ASN A  61       6.040   8.260  19.903  1.00 70.27           N  
ANISOU  467  ND2 ASN A  61     9223   8329   9147   -911   -838   2664       N  
ATOM    468  N   PHE A  62       7.143   9.226  14.730  1.00 57.11           N  
ANISOU  468  N   PHE A  62     6757   6337   8603   -618   -850    908       N  
ATOM    469  CA  PHE A  62       7.289   9.066  13.289  1.00 55.50           C  
ANISOU  469  CA  PHE A  62     6336   6026   8723   -546   -830    509       C  
ATOM    470  C   PHE A  62       8.604   9.626  12.756  1.00 54.32           C  
ANISOU  470  C   PHE A  62     6046   6049   8544   -390   -967    258       C  
ATOM    471  O   PHE A  62       9.298  10.379  13.444  1.00 54.05           O  
ANISOU  471  O   PHE A  62     6074   6244   8218   -374  -1061    342       O  
ATOM    472  CB  PHE A  62       6.127   9.723  12.559  1.00 52.79           C  
ANISOU  472  CB  PHE A  62     5953   5826   8278   -677   -585    278       C  
ATOM    473  CG  PHE A  62       6.179  11.212  12.565  1.00 49.67           C  
ANISOU  473  CG  PHE A  62     5601   5793   7477   -701   -499    148       C  
ATOM    474  CD1 PHE A  62       6.642  11.905  11.467  1.00 47.83           C  
ANISOU  474  CD1 PHE A  62     5230   5705   7235   -638   -487   -170       C  
ATOM    475  CD2 PHE A  62       5.766  11.921  13.669  1.00 50.00           C  
ANISOU  475  CD2 PHE A  62     5822   6024   7148   -789   -424    345       C  
ATOM    476  CE1 PHE A  62       6.686  13.286  11.467  1.00 45.87           C  
ANISOU  476  CE1 PHE A  62     5033   5721   6672   -675   -415   -256       C  
ATOM    477  CE2 PHE A  62       5.809  13.304  13.683  1.00 48.15           C  
ANISOU  477  CE2 PHE A  62     5634   6059   6599   -804   -360    191       C  
ATOM    478  CZ  PHE A  62       6.274  13.988  12.578  1.00 46.06           C  
ANISOU  478  CZ  PHE A  62     5241   5871   6386   -753   -363    -93       C  
ATOM    479  N   GLY A  63       8.922   9.223  11.523  1.00 54.05           N  
ANISOU  479  N   GLY A  63     5802   5917   8816   -287   -971    -68       N  
ATOM    480  CA  GLY A  63      10.079   9.710  10.766  1.00 53.03           C  
ANISOU  480  CA  GLY A  63     5477   5984   8686   -159  -1033   -349       C  
ATOM    481  C   GLY A  63       9.622  10.032   9.360  1.00 50.88           C  
ANISOU  481  C   GLY A  63     5066   5832   8432   -183   -855   -714       C  
ATOM    482  O   GLY A  63       8.578   9.569   8.938  1.00 50.68           O  
ANISOU  482  O   GLY A  63     5056   5669   8531   -248   -755   -786       O  
ATOM    483  N   SER A  64      10.385  10.848   8.644  1.00 49.82           N  
ANISOU  483  N   SER A  64     4788   5981   8159   -146   -817   -926       N  
ATOM    484  CA  SER A  64       9.988  11.271   7.282  1.00 48.38           C  
ANISOU  484  CA  SER A  64     4488   5989   7904   -167   -646  -1228       C  
ATOM    485  C   SER A  64      11.162  11.558   6.370  1.00 48.76           C  
ANISOU  485  C   SER A  64     4297   6279   7950    -64   -633  -1471       C  
ATOM    486  O   SER A  64      12.289  11.812   6.832  1.00 49.43           O  
ANISOU  486  O   SER A  64     4300   6445   8033    -21   -735  -1401       O  
ATOM    487  CB  SER A  64       9.157  12.552   7.321  1.00 45.69           C  
ANISOU  487  CB  SER A  64     4294   5852   7211   -329   -495  -1145       C  
ATOM    488  OG  SER A  64       9.964  13.635   7.729  1.00 45.06           O  
ANISOU  488  OG  SER A  64     4240   5963   6916   -377   -515  -1056       O  
ATOM    489  N   TYR A  65      10.874  11.512   5.070  1.00 48.50           N  
ANISOU  489  N   TYR A  65     4133   6396   7898    -32   -506  -1761       N  
ATOM    490  CA  TYR A  65      11.763  12.087   4.059  1.00 48.89           C  
ANISOU  490  CA  TYR A  65     3971   6794   7811      9   -406  -1962       C  
ATOM    491  C   TYR A  65      10.941  12.793   2.999  1.00 47.23           C  
ANISOU  491  C   TYR A  65     3784   6837   7321    -73   -230  -2065       C  
ATOM    492  O   TYR A  65      10.059  12.211   2.406  1.00 47.74           O  
ANISOU  492  O   TYR A  65     3850   6851   7438    -40   -209  -2243       O  
ATOM    493  CB  TYR A  65      12.687  11.051   3.421  1.00 51.84           C  
ANISOU  493  CB  TYR A  65     4070   7162   8464    224   -455  -2272       C  
ATOM    494  CG  TYR A  65      13.891  11.708   2.775  1.00 52.99           C  
ANISOU  494  CG  TYR A  65     3970   7694   8470    248   -354  -2386       C  
ATOM    495  CD1 TYR A  65      14.961  12.140   3.532  1.00 52.87           C  
ANISOU  495  CD1 TYR A  65     3874   7727   8485    227   -442  -2216       C  
ATOM    496  CD2 TYR A  65      13.936  11.935   1.399  1.00 54.10           C  
ANISOU  496  CD2 TYR A  65     3946   8191   8418    271   -164  -2653       C  
ATOM    497  CE1 TYR A  65      16.036  12.766   2.933  1.00 54.47           C  
ANISOU  497  CE1 TYR A  65     3817   8293   8587    206   -328  -2309       C  
ATOM    498  CE2 TYR A  65      15.031  12.556   0.799  1.00 54.57           C  
ANISOU  498  CE2 TYR A  65     3762   8638   8332    260    -29  -2716       C  
ATOM    499  CZ  TYR A  65      16.056  12.968   1.569  1.00 54.87           C  
ANISOU  499  CZ  TYR A  65     3706   8685   8456    215   -104  -2542       C  
ATOM    500  OH  TYR A  65      17.120  13.582   0.974  1.00 57.71           O  
ANISOU  500  OH  TYR A  65     3791   9431   8704    168     46  -2597       O  
ATOM    501  N   VAL A  66      11.234  14.057   2.784  1.00 46.01           N  
ANISOU  501  N   VAL A  66     3648   6945   6888   -186   -125  -1940       N  
ATOM    502  CA  VAL A  66      10.381  14.907   1.995  1.00 45.00           C  
ANISOU  502  CA  VAL A  66     3600   7020   6476   -268      9  -1919       C  
ATOM    503  C   VAL A  66      11.198  15.889   1.209  1.00 45.80           C  
ANISOU  503  C   VAL A  66     3584   7464   6352   -328    144  -1889       C  
ATOM    504  O   VAL A  66      12.381  16.039   1.417  1.00 47.33           O  
ANISOU  504  O   VAL A  66     3636   7731   6613   -344    142  -1869       O  
ATOM    505  CB  VAL A  66       9.425  15.720   2.892  1.00 43.10           C  
ANISOU  505  CB  VAL A  66     3623   6623   6129   -397     -2  -1649       C  
ATOM    506  CG1 VAL A  66       8.402  14.809   3.575  1.00 42.70           C  
ANISOU  506  CG1 VAL A  66     3680   6287   6257   -377    -82  -1643       C  
ATOM    507  CG2 VAL A  66      10.210  16.539   3.935  1.00 42.50           C  
ANISOU  507  CG2 VAL A  66     3630   6490   6027   -498    -51  -1430       C  
ATOM    508  N   THR A  67      10.543  16.567   0.292  1.00 45.83           N  
ANISOU  508  N   THR A  67     3635   7689   6090   -367    260  -1863       N  
ATOM    509  CA  THR A  67      11.171  17.566  -0.541  1.00 46.89           C  
ANISOU  509  CA  THR A  67     3685   8152   5977   -451    413  -1760       C  
ATOM    510  C   THR A  67      10.376  18.815  -0.392  1.00 45.31           C  
ANISOU  510  C   THR A  67     3716   7892   5605   -573    439  -1470       C  
ATOM    511  O   THR A  67       9.175  18.771  -0.542  1.00 44.34           O  
ANISOU  511  O   THR A  67     3717   7717   5411   -522    405  -1477       O  
ATOM    512  CB  THR A  67      11.132  17.151  -1.992  1.00 49.06           C  
ANISOU  512  CB  THR A  67     3789   8805   6045   -343    526  -1999       C  
ATOM    513  OG1 THR A  67      12.040  16.062  -2.180  1.00 51.22           O  
ANISOU  513  OG1 THR A  67     3812   9146   6502   -208    521  -2313       O  
ATOM    514  CG2 THR A  67      11.530  18.319  -2.887  1.00 50.86           C  
ANISOU  514  CG2 THR A  67     3983   9394   5944   -457    707  -1787       C  
ATOM    515  N   HIS A  68      11.031  19.930  -0.090  1.00 45.68           N  
ANISOU  515  N   HIS A  68     3805   7928   5622   -730    488  -1232       N  
ATOM    516  CA  HIS A  68      10.310  21.189   0.057  1.00 45.00           C  
ANISOU  516  CA  HIS A  68     3946   7725   5425   -830    503   -965       C  
ATOM    517  C   HIS A  68      10.847  22.306  -0.790  1.00 46.86           C  
ANISOU  517  C   HIS A  68     4149   8165   5491   -962    647   -738       C  
ATOM    518  O   HIS A  68      11.908  22.186  -1.368  1.00 49.28           O  
ANISOU  518  O   HIS A  68     4238   8728   5758  -1017    758   -770       O  
ATOM    519  CB  HIS A  68      10.237  21.611   1.527  1.00 43.59           C  
ANISOU  519  CB  HIS A  68     3943   7194   5425   -910    386   -872       C  
ATOM    520  CG  HIS A  68      11.539  22.015   2.134  1.00 43.96           C  
ANISOU  520  CG  HIS A  68     3904   7197   5601  -1056    360   -821       C  
ATOM    521  ND1 HIS A  68      12.044  23.292   2.028  1.00 45.64           N  
ANISOU  521  ND1 HIS A  68     4148   7391   5801  -1244    423   -625       N  
ATOM    522  CD2 HIS A  68      12.391  21.340   2.940  1.00 44.76           C  
ANISOU  522  CD2 HIS A  68     3889   7243   5875  -1048    250   -934       C  
ATOM    523  CE1 HIS A  68      13.185  23.371   2.698  1.00 47.02           C  
ANISOU  523  CE1 HIS A  68     4200   7529   6135  -1364    357   -655       C  
ATOM    524  NE2 HIS A  68      13.422  22.199   3.259  1.00 46.20           N  
ANISOU  524  NE2 HIS A  68     4001   7423   6129  -1232    244   -839       N  
ATOM    525  N   GLU A  69      10.063  23.371  -0.889  1.00 46.81           N  
ANISOU  525  N   GLU A  69     4348   8044   5392  -1004    653   -498       N  
ATOM    526  CA AGLU A  69      10.503  24.577  -1.548  0.50 49.42           C  
ANISOU  526  CA AGLU A  69     4700   8462   5612  -1157    773   -194       C  
ATOM    527  CA BGLU A  69      10.501  24.602  -1.540  0.50 49.01           C  
ANISOU  527  CA BGLU A  69     4652   8406   5562  -1160    773   -188       C  
ATOM    528  C   GLU A  69      11.398  25.362  -0.587  1.00 49.72           C  
ANISOU  528  C   GLU A  69     4766   8225   5897  -1373    748    -85       C  
ATOM    529  O   GLU A  69      11.227  25.317   0.640  1.00 47.59           O  
ANISOU  529  O   GLU A  69     4608   7654   5818  -1372    608   -189       O  
ATOM    530  CB AGLU A  69       9.310  25.413  -2.052  0.50 49.98           C  
ANISOU  530  CB AGLU A  69     4981   8478   5530  -1086    758     36       C  
ATOM    531  CB BGLU A  69       9.337  25.517  -1.982  0.50 49.28           C  
ANISOU  531  CB BGLU A  69     4906   8357   5459  -1101    756     56       C  
ATOM    532  CG AGLU A  69       8.642  24.844  -3.346  0.50 52.27           C  
ANISOU  532  CG AGLU A  69     5193   9171   5494   -912    792    -25       C  
ATOM    533  CG BGLU A  69       9.774  26.673  -2.948  0.50 52.16           C  
ANISOU  533  CG BGLU A  69     5290   8855   5671  -1247    895    443       C  
ATOM    534  CD AGLU A  69       7.348  25.585  -3.754  0.50 54.47           C  
ANISOU  534  CD AGLU A  69     5660   9396   5639   -794    718    187       C  
ATOM    535  CD BGLU A  69       8.735  27.796  -3.131  0.50 52.27           C  
ANISOU  535  CD BGLU A  69     5554   8648   5656  -1191    834    749       C  
ATOM    536  OE1AGLU A  69       6.957  26.553  -3.052  0.50 56.06           O  
ANISOU  536  OE1AGLU A  69     6054   9221   6025   -832    658    377       O  
ATOM    537  OE1BGLU A  69       7.570  27.646  -2.710  0.50 51.14           O  
ANISOU  537  OE1BGLU A  69     5533   8342   5555  -1008    701    634       O  
ATOM    538  OE2AGLU A  69       6.720  25.197  -4.775  0.50 54.31           O  
ANISOU  538  OE2AGLU A  69     5581   9719   5334   -647    704    139       O  
ATOM    539  OE2BGLU A  69       9.088  28.846  -3.706  0.50 53.67           O  
ANISOU  539  OE2BGLU A  69     5793   8808   5791  -1331    922   1123       O  
ATOM    540  N   THR A  70      12.372  26.045  -1.177  1.00 52.78           N  
ANISOU  540  N   THR A  70     5030   8758   6263  -1569    888    114       N  
ATOM    541  CA  THR A  70      13.236  26.944  -0.474  1.00 54.13           C  
ANISOU  541  CA  THR A  70     5200   8687   6678  -1821    870    235       C  
ATOM    542  C   THR A  70      12.385  27.898   0.388  1.00 53.17           C  
ANISOU  542  C   THR A  70     5394   8102   6704  -1836    734    329       C  
ATOM    543  O   THR A  70      11.349  28.412  -0.066  1.00 53.09           O  
ANISOU  543  O   THR A  70     5578   8008   6585  -1732    741    497       O  
ATOM    544  CB  THR A  70      14.084  27.716  -1.489  1.00 58.14           C  
ANISOU  544  CB  THR A  70     5563   9414   7113  -2049   1079    531       C  
ATOM    545  OG1 THR A  70      15.124  26.863  -1.978  1.00 59.78           O  
ANISOU  545  OG1 THR A  70     5422  10038   7253  -2058   1206    367       O  
ATOM    546  CG2 THR A  70      14.705  28.969  -0.861  1.00 61.11           C  
ANISOU  546  CG2 THR A  70     6001   9433   7786  -2353   1052    727       C  
ATOM    547  N   LYS A  71      12.829  28.072   1.636  1.00 52.56           N  
ANISOU  547  N   LYS A  71     5347   7759   6862  -1937    597    187       N  
ATOM    548  CA  LYS A  71      12.224  28.957   2.654  1.00 52.05           C  
ANISOU  548  CA  LYS A  71     5552   7266   6957  -1960    463    177       C  
ATOM    549  C   LYS A  71      10.805  28.589   3.058  1.00 49.45           C  
ANISOU  549  C   LYS A  71     5424   6838   6526  -1698    389     64       C  
ATOM    550  O   LYS A  71      10.030  29.451   3.478  1.00 49.84           O  
ANISOU  550  O   LYS A  71     5695   6588   6653  -1660    339    104       O  
ATOM    551  CB  LYS A  71      12.310  30.431   2.216  1.00 55.12           C  
ANISOU  551  CB  LYS A  71     6061   7403   7479  -2155    525    476       C  
ATOM    552  CG  LYS A  71      13.743  30.949   2.178  1.00 58.57           C  
ANISOU  552  CG  LYS A  71     6298   7841   8113  -2488    575    562       C  
ATOM    553  CD  LYS A  71      14.458  30.737   3.528  1.00 58.19           C  
ANISOU  553  CD  LYS A  71     6177   7676   8256  -2583    392    251       C  
ATOM    554  CE  LYS A  71      15.830  31.366   3.577  1.00 61.90           C  
ANISOU  554  CE  LYS A  71     6426   8115   8976  -2938    406    306       C  
ATOM    555  NZ  LYS A  71      16.555  31.334   2.241  1.00 64.71           N  
ANISOU  555  NZ  LYS A  71     6520   8808   9258  -3085    655    579       N  
ATOM    556  N   HIS A  72      10.470  27.311   2.946  1.00 47.12           N  
ANISOU  556  N   HIS A  72     5031   6779   6091  -1520    386    -93       N  
ATOM    557  CA  HIS A  72       9.116  26.863   3.266  1.00 45.17           C  
ANISOU  557  CA  HIS A  72     4922   6474   5764  -1302    339   -193       C  
ATOM    558  C   HIS A  72       9.159  25.508   3.974  1.00 43.37           C  
ANISOU  558  C   HIS A  72     4608   6333   5534  -1211    267   -419       C  
ATOM    559  O   HIS A  72       8.540  24.540   3.525  1.00 42.28           O  
ANISOU  559  O   HIS A  72     4404   6347   5312  -1064    287   -501       O  
ATOM    560  CB  HIS A  72       8.238  26.747   2.004  1.00 45.21           C  
ANISOU  560  CB  HIS A  72     4914   6674   5588  -1155    419    -81       C  
ATOM    561  CG  HIS A  72       7.997  28.042   1.292  1.00 47.65           C  
ANISOU  561  CG  HIS A  72     5340   6882   5881  -1198    467    206       C  
ATOM    562  ND1 HIS A  72       8.914  28.595   0.420  1.00 50.36           N  
ANISOU  562  ND1 HIS A  72     5600   7345   6188  -1368    572    441       N  
ATOM    563  CD2 HIS A  72       6.921  28.869   1.280  1.00 48.19           C  
ANISOU  563  CD2 HIS A  72     5591   6743   5975  -1080    428    324       C  
ATOM    564  CE1 HIS A  72       8.427  29.726  -0.069  1.00 52.56           C  
ANISOU  564  CE1 HIS A  72     6036   7458   6476  -1368    585    730       C  
ATOM    565  NE2 HIS A  72       7.221  29.917   0.440  1.00 51.18           N  
ANISOU  565  NE2 HIS A  72     6022   7070   6352  -1176    485    651       N  
ATOM    566  N   PHE A  73       9.881  25.435   5.084  1.00 43.44           N  
ANISOU  566  N   PHE A  73     4619   6237   5649  -1299    165   -514       N  
ATOM    567  CA  PHE A  73       9.956  24.186   5.840  1.00 42.27           C  
ANISOU  567  CA  PHE A  73     4413   6139   5507  -1210     75   -662       C  
ATOM    568  C   PHE A  73      10.190  24.420   7.306  1.00 42.51           C  
ANISOU  568  C   PHE A  73     4564   6015   5570  -1266    -61   -729       C  
ATOM    569  O   PHE A  73      11.099  25.165   7.664  1.00 44.15           O  
ANISOU  569  O   PHE A  73     4751   6165   5856  -1421   -128   -735       O  
ATOM    570  CB  PHE A  73      11.114  23.344   5.332  1.00 43.07           C  
ANISOU  570  CB  PHE A  73     4252   6443   5667  -1223     73   -716       C  
ATOM    571  CG  PHE A  73      11.355  22.102   6.143  1.00 42.58           C  
ANISOU  571  CG  PHE A  73     4131   6373   5671  -1124    -53   -829       C  
ATOM    572  CD1 PHE A  73      10.775  20.892   5.780  1.00 41.34           C  
ANISOU  572  CD1 PHE A  73     3922   6259   5525   -967    -35   -907       C  
ATOM    573  CD2 PHE A  73      12.165  22.140   7.267  1.00 43.46           C  
ANISOU  573  CD2 PHE A  73     4239   6424   5849  -1190   -210   -851       C  
ATOM    574  CE1 PHE A  73      10.993  19.746   6.526  1.00 41.36           C  
ANISOU  574  CE1 PHE A  73     3888   6193   5633   -878   -160   -960       C  
ATOM    575  CE2 PHE A  73      12.386  20.990   8.013  1.00 43.71           C  
ANISOU  575  CE2 PHE A  73     4230   6444   5933  -1080   -348   -894       C  
ATOM    576  CZ  PHE A  73      11.795  19.789   7.636  1.00 42.50           C  
ANISOU  576  CZ  PHE A  73     4041   6282   5821   -924   -315   -927       C  
ATOM    577  N   ILE A  74       9.412  23.749   8.148  1.00 41.34           N  
ANISOU  577  N   ILE A  74     4524   5829   5354  -1155   -103   -783       N  
ATOM    578  CA  ILE A  74       9.663  23.794   9.588  1.00 42.09           C  
ANISOU  578  CA  ILE A  74     4729   5861   5400  -1190   -239   -844       C  
ATOM    579  C   ILE A  74       9.363  22.471  10.278  1.00 41.36           C  
ANISOU  579  C   ILE A  74     4640   5821   5252  -1082   -295   -830       C  
ATOM    580  O   ILE A  74       8.452  21.738   9.900  1.00 40.08           O  
ANISOU  580  O   ILE A  74     4473   5665   5090   -985   -203   -800       O  
ATOM    581  CB  ILE A  74       8.903  24.949  10.275  1.00 42.64           C  
ANISOU  581  CB  ILE A  74     5023   5781   5395  -1208   -219   -901       C  
ATOM    582  CG1 ILE A  74       9.442  25.181  11.685  1.00 44.03           C  
ANISOU  582  CG1 ILE A  74     5294   5949   5484  -1273   -379  -1013       C  
ATOM    583  CG2 ILE A  74       7.399  24.683  10.328  1.00 41.45           C  
ANISOU  583  CG2 ILE A  74     4976   5621   5152  -1062    -98   -894       C  
ATOM    584  CD1 ILE A  74       8.888  26.443  12.325  1.00 45.37           C  
ANISOU  584  CD1 ILE A  74     5666   5964   5607  -1295   -369  -1152       C  
ATOM    585  N   TYR A  75      10.169  22.180  11.286  1.00 42.58           N  
ANISOU  585  N   TYR A  75     4793   6010   5375  -1112   -463   -840       N  
ATOM    586  CA  TYR A  75      10.002  20.987  12.083  1.00 42.99           C  
ANISOU  586  CA  TYR A  75     4874   6088   5370  -1021   -543   -761       C  
ATOM    587  C   TYR A  75      10.262  21.364  13.520  1.00 44.72           C  
ANISOU  587  C   TYR A  75     5243   6356   5393  -1062   -691   -775       C  
ATOM    588  O   TYR A  75      11.376  21.736  13.871  1.00 46.28           O  
ANISOU  588  O   TYR A  75     5368   6607   5606  -1133   -865   -839       O  
ATOM    589  CB  TYR A  75      10.968  19.910  11.638  1.00 43.41           C  
ANISOU  589  CB  TYR A  75     4708   6177   5607   -959   -645   -730       C  
ATOM    590  CG  TYR A  75      10.927  18.683  12.497  1.00 44.18           C  
ANISOU  590  CG  TYR A  75     4845   6244   5698   -861   -766   -600       C  
ATOM    591  CD1 TYR A  75       9.834  17.848  12.481  1.00 43.76           C  
ANISOU  591  CD1 TYR A  75     4868   6096   5662   -802   -659   -506       C  
ATOM    592  CD2 TYR A  75      11.995  18.350  13.321  1.00 47.04           C  
ANISOU  592  CD2 TYR A  75     5153   6664   6055   -836  -1002   -547       C  
ATOM    593  CE1 TYR A  75       9.785  16.704  13.250  1.00 45.22           C  
ANISOU  593  CE1 TYR A  75     5097   6207   5875   -735   -761   -327       C  
ATOM    594  CE2 TYR A  75      11.961  17.201  14.103  1.00 49.01           C  
ANISOU  594  CE2 TYR A  75     5454   6863   6301   -732  -1131   -361       C  
ATOM    595  CZ  TYR A  75      10.838  16.382  14.053  1.00 47.83           C  
ANISOU  595  CZ  TYR A  75     5405   6581   6186   -691   -996   -234       C  
ATOM    596  OH  TYR A  75      10.774  15.239  14.816  1.00 50.64           O  
ANISOU  596  OH  TYR A  75     5826   6843   6571   -613  -1110      6       O  
ATOM    597  N   PHE A  76       9.229  21.264  14.344  1.00 45.02           N  
ANISOU  597  N   PHE A  76     5466   6408   5228  -1023   -620   -732       N  
ATOM    598  CA  PHE A  76       9.305  21.750  15.709  1.00 47.33           C  
ANISOU  598  CA  PHE A  76     5927   6804   5249  -1053   -727   -787       C  
ATOM    599  C   PHE A  76       8.394  20.968  16.637  1.00 48.35           C  
ANISOU  599  C   PHE A  76     6196   7025   5147   -989   -657   -631       C  
ATOM    600  O   PHE A  76       7.439  20.332  16.187  1.00 47.02           O  
ANISOU  600  O   PHE A  76     6008   6795   5061   -948   -480   -522       O  
ATOM    601  CB  PHE A  76       8.942  23.233  15.751  1.00 47.58           C  
ANISOU  601  CB  PHE A  76     6071   6776   5228  -1114   -653  -1006       C  
ATOM    602  CG  PHE A  76       7.508  23.521  15.407  1.00 46.21           C  
ANISOU  602  CG  PHE A  76     5980   6538   5038  -1045   -408  -1023       C  
ATOM    603  CD1 PHE A  76       6.581  23.823  16.403  1.00 47.94           C  
ANISOU  603  CD1 PHE A  76     6364   6848   5001   -996   -314  -1103       C  
ATOM    604  CD2 PHE A  76       7.084  23.500  14.087  1.00 44.22           C  
ANISOU  604  CD2 PHE A  76     5618   6175   5006  -1018   -276   -974       C  
ATOM    605  CE1 PHE A  76       5.243  24.101  16.089  1.00 47.28           C  
ANISOU  605  CE1 PHE A  76     6307   6725   4930   -914    -89  -1138       C  
ATOM    606  CE2 PHE A  76       5.759  23.770  13.753  1.00 44.02           C  
ANISOU  606  CE2 PHE A  76     5634   6112   4977   -937    -86   -994       C  
ATOM    607  CZ  PHE A  76       4.828  24.070  14.759  1.00 45.26           C  
ANISOU  607  CZ  PHE A  76     5927   6340   4927   -882      9  -1078       C  
ATOM    608  N   TYR A  77       8.705  21.024  17.931  1.00 50.97           N  
ANISOU  608  N   TYR A  77     6656   7528   5180   -996   -799   -620       N  
ATOM    609  CA  TYR A  77       7.884  20.388  18.954  1.00 52.90           C  
ANISOU  609  CA  TYR A  77     7051   7921   5126   -958   -716   -439       C  
ATOM    610  C   TYR A  77       7.081  21.409  19.740  1.00 54.32           C  
ANISOU  610  C   TYR A  77     7402   8251   4985   -966   -580   -646       C  
ATOM    611  O   TYR A  77       7.623  22.413  20.226  1.00 55.77           O  
ANISOU  611  O   TYR A  77     7654   8507   5029   -997   -712   -904       O  
ATOM    612  CB  TYR A  77       8.730  19.616  19.952  1.00 55.96           C  
ANISOU  612  CB  TYR A  77     7479   8465   5317   -931   -970   -232       C  
ATOM    613  CG  TYR A  77       9.315  18.336  19.431  1.00 55.70           C  
ANISOU  613  CG  TYR A  77     7299   8280   5584   -872  -1090     22       C  
ATOM    614  CD1 TYR A  77      10.362  18.360  18.520  1.00 54.39           C  
ANISOU  614  CD1 TYR A  77     6923   7992   5751   -858  -1232    -88       C  
ATOM    615  CD2 TYR A  77       8.859  17.095  19.891  1.00 57.39           C  
ANISOU  615  CD2 TYR A  77     7575   8469   5761   -831  -1062    376       C  
ATOM    616  CE1 TYR A  77      10.929  17.187  18.058  1.00 54.91           C  
ANISOU  616  CE1 TYR A  77     6835   7920   6108   -767  -1345     88       C  
ATOM    617  CE2 TYR A  77       9.421  15.905  19.435  1.00 57.59           C  
ANISOU  617  CE2 TYR A  77     7470   8293   6119   -753  -1196    585       C  
ATOM    618  CZ  TYR A  77      10.455  15.962  18.516  1.00 56.73           C  
ANISOU  618  CZ  TYR A  77     7144   8072   6338   -703  -1340    411       C  
ATOM    619  OH  TYR A  77      11.043  14.806  18.051  1.00 58.11           O  
ANISOU  619  OH  TYR A  77     7167   8048   6862   -591  -1473    555       O  
ATOM    620  N   LEU A  78       5.788  21.119  19.873  1.00 54.29           N  
ANISOU  620  N   LEU A  78     7445   8295   4886   -938   -316   -557       N  
ATOM    621  CA  LEU A  78       4.909  21.842  20.776  1.00 56.61           C  
ANISOU  621  CA  LEU A  78     7880   8795   4831   -913   -148   -727       C  
ATOM    622  C   LEU A  78       4.600  20.831  21.870  1.00 59.61           C  
ANISOU  622  C   LEU A  78     8353   9435   4859   -923   -102   -418       C  
ATOM    623  O   LEU A  78       3.815  19.908  21.648  1.00 59.37           O  
ANISOU  623  O   LEU A  78     8262   9363   4933   -944     80   -149       O  
ATOM    624  CB  LEU A  78       3.631  22.305  20.060  1.00 54.95           C  
ANISOU  624  CB  LEU A  78     7604   8478   4796   -867    138   -852       C  
ATOM    625  CG  LEU A  78       3.203  23.744  20.391  1.00 56.42           C  
ANISOU  625  CG  LEU A  78     7879   8696   4859   -801    217  -1239       C  
ATOM    626  CD1 LEU A  78       3.693  24.671  19.299  1.00 54.55           C  
ANISOU  626  CD1 LEU A  78     7583   8150   4990   -803    115  -1423       C  
ATOM    627  CD2 LEU A  78       1.700  23.886  20.534  1.00 57.48           C  
ANISOU  627  CD2 LEU A  78     7983   8941   4913   -718    536  -1300       C  
ATOM    628  N   GLY A  79       5.261  20.984  23.021  1.00 62.92           N  
ANISOU  628  N   GLY A  79     8912  10119   4875   -920   -289   -439       N  
ATOM    629  CA  GLY A  79       5.279  19.959  24.060  1.00 66.23           C  
ANISOU  629  CA  GLY A  79     9434  10795   4936   -930   -326    -60       C  
ATOM    630  C   GLY A  79       6.082  18.733  23.637  1.00 65.49           C  
ANISOU  630  C   GLY A  79     9251  10494   5138   -933   -539    316       C  
ATOM    631  O   GLY A  79       7.134  18.837  22.997  1.00 63.50           O  
ANISOU  631  O   GLY A  79     8888  10057   5183   -914   -785    213       O  
ATOM    632  N   GLN A  80       5.560  17.560  23.983  1.00 67.43           N  
ANISOU  632  N   GLN A  80     9530  10758   5332   -959   -430    753       N  
ATOM    633  CA  GLN A  80       6.157  16.288  23.583  1.00 67.31           C  
ANISOU  633  CA  GLN A  80     9435  10478   5660   -941   -607   1122       C  
ATOM    634  C   GLN A  80       5.643  15.817  22.198  1.00 63.61           C  
ANISOU  634  C   GLN A  80     8780   9619   5770   -969   -445   1098       C  
ATOM    635  O   GLN A  80       5.853  14.655  21.813  1.00 64.02           O  
ANISOU  635  O   GLN A  80     8759   9408   6157   -960   -524   1381       O  
ATOM    636  CB  GLN A  80       5.880  15.232  24.663  1.00 71.88           C  
ANISOU  636  CB  GLN A  80    10159  11218   5932   -967   -592   1645       C  
ATOM    637  N   VAL A  81       4.983  16.721  21.459  1.00 60.48           N  
ANISOU  637  N   VAL A  81     8306   9183   5491   -988   -243    748       N  
ATOM    638  CA  VAL A  81       4.406  16.419  20.141  1.00 57.18           C  
ANISOU  638  CA  VAL A  81     7709   8473   5541  -1007    -96    676       C  
ATOM    639  C   VAL A  81       5.171  17.142  19.013  1.00 53.87           C  
ANISOU  639  C   VAL A  81     7166   7903   5398   -955   -227    353       C  
ATOM    640  O   VAL A  81       5.346  18.362  19.027  1.00 53.14           O  
ANISOU  640  O   VAL A  81     7111   7908   5170   -943   -237     68       O  
ATOM    641  CB  VAL A  81       2.881  16.786  20.072  1.00 56.94           C  
ANISOU  641  CB  VAL A  81     7652   8533   5449  -1061    254    586       C  
ATOM    642  CG1 VAL A  81       2.435  17.057  18.621  1.00 53.10           C  
ANISOU  642  CG1 VAL A  81     6980   7828   5366  -1043    340    349       C  
ATOM    643  CG2 VAL A  81       2.024  15.686  20.689  1.00 59.58           C  
ANISOU  643  CG2 VAL A  81     8002   8905   5728  -1163    436    969       C  
ATOM    644  N   ALA A  82       5.604  16.360  18.034  1.00 52.30           N  
ANISOU  644  N   ALA A  82     6815   7458   5596   -929   -314    403       N  
ATOM    645  CA  ALA A  82       6.340  16.853  16.892  1.00 49.46           C  
ANISOU  645  CA  ALA A  82     6311   6989   5492   -890   -405    155       C  
ATOM    646  C   ALA A  82       5.402  17.311  15.786  1.00 46.88           C  
ANISOU  646  C   ALA A  82     5891   6591   5331   -903   -193    -33       C  
ATOM    647  O   ALA A  82       4.355  16.732  15.565  1.00 46.73           O  
ANISOU  647  O   ALA A  82     5832   6512   5410   -930    -28     43       O  
ATOM    648  CB  ALA A  82       7.226  15.758  16.378  1.00 49.84           C  
ANISOU  648  CB  ALA A  82     6223   6856   5857   -827   -584    264       C  
ATOM    649  N   ILE A  83       5.811  18.352  15.072  1.00 45.51           N  
ANISOU  649  N   ILE A  83     5668   6424   5200   -892   -212   -263       N  
ATOM    650  CA  ILE A  83       5.001  18.981  14.011  1.00 43.33           C  
ANISOU  650  CA  ILE A  83     5318   6106   5036   -881    -48   -423       C  
ATOM    651  C   ILE A  83       5.852  19.313  12.789  1.00 41.90           C  
ANISOU  651  C   ILE A  83     5002   5869   5049   -867   -123   -543       C  
ATOM    652  O   ILE A  83       6.771  20.141  12.871  1.00 42.05           O  
ANISOU  652  O   ILE A  83     5039   5915   5024   -900   -225   -622       O  
ATOM    653  CB  ILE A  83       4.426  20.305  14.496  1.00 43.78           C  
ANISOU  653  CB  ILE A  83     5502   6248   4882   -879     49   -565       C  
ATOM    654  CG1 ILE A  83       3.452  20.069  15.655  1.00 45.72           C  
ANISOU  654  CG1 ILE A  83     5855   6624   4889   -885    185   -481       C  
ATOM    655  CG2 ILE A  83       3.758  21.040  13.345  1.00 42.10           C  
ANISOU  655  CG2 ILE A  83     5212   5973   4810   -836    164   -696       C  
ATOM    656  CD1 ILE A  83       3.362  21.244  16.601  1.00 47.29           C  
ANISOU  656  CD1 ILE A  83     6212   6952   4804   -868    207   -652       C  
ATOM    657  N   LEU A  84       5.557  18.644  11.674  1.00 40.93           N  
ANISOU  657  N   LEU A  84     4731   5687   5132   -832    -71   -565       N  
ATOM    658  CA  LEU A  84       6.235  18.890  10.402  1.00 39.81           C  
ANISOU  658  CA  LEU A  84     4445   5559   5121   -813    -96   -676       C  
ATOM    659  C   LEU A  84       5.313  19.640   9.483  1.00 38.64           C  
ANISOU  659  C   LEU A  84     4281   5448   4952   -792     36   -754       C  
ATOM    660  O   LEU A  84       4.185  19.238   9.271  1.00 38.40           O  
ANISOU  660  O   LEU A  84     4223   5414   4952   -761    126   -763       O  
ATOM    661  CB  LEU A  84       6.624  17.580   9.743  1.00 40.23           C  
ANISOU  661  CB  LEU A  84     4332   5559   5393   -759   -151   -693       C  
ATOM    662  CG  LEU A  84       7.172  17.616   8.301  1.00 39.96           C  
ANISOU  662  CG  LEU A  84     4115   5606   5460   -719   -134   -841       C  
ATOM    663  CD1 LEU A  84       8.369  18.544   8.152  1.00 39.35           C  
ANISOU  663  CD1 LEU A  84     3996   5628   5325   -767   -178   -857       C  
ATOM    664  CD2 LEU A  84       7.531  16.167   7.862  1.00 40.77           C  
ANISOU  664  CD2 LEU A  84     4059   5629   5802   -635   -201   -917       C  
ATOM    665  N   LEU A  85       5.806  20.723   8.914  1.00 38.32           N  
ANISOU  665  N   LEU A  85     4242   5440   4877   -813     38   -793       N  
ATOM    666  CA  LEU A  85       4.981  21.560   8.060  1.00 38.15           C  
ANISOU  666  CA  LEU A  85     4227   5442   4825   -772    135   -814       C  
ATOM    667  C   LEU A  85       5.845  22.072   6.955  1.00 38.15           C  
ANISOU  667  C   LEU A  85     4138   5509   4848   -803    128   -803       C  
ATOM    668  O   LEU A  85       6.933  22.572   7.242  1.00 39.24           O  
ANISOU  668  O   LEU A  85     4285   5621   5001   -895     71   -782       O  
ATOM    669  CB  LEU A  85       4.428  22.743   8.877  1.00 38.87           C  
ANISOU  669  CB  LEU A  85     4492   5451   4822   -772    171   -820       C  
ATOM    670  CG  LEU A  85       3.689  23.886   8.177  1.00 38.78           C  
ANISOU  670  CG  LEU A  85     4521   5401   4813   -704    236   -817       C  
ATOM    671  CD1 LEU A  85       2.461  23.408   7.404  1.00 38.15           C  
ANISOU  671  CD1 LEU A  85     4331   5415   4749   -592    304   -826       C  
ATOM    672  CD2 LEU A  85       3.287  24.866   9.233  1.00 39.79           C  
ANISOU  672  CD2 LEU A  85     4816   5412   4891   -685    254   -884       C  
ATOM    673  N   PHE A  86       5.393  21.969   5.707  1.00 37.82           N  
ANISOU  673  N   PHE A  86     3996   5581   4791   -740    185   -815       N  
ATOM    674  CA  PHE A  86       6.226  22.413   4.583  1.00 38.81           C  
ANISOU  674  CA  PHE A  86     4027   5837   4882   -777    211   -771       C  
ATOM    675  C   PHE A  86       5.488  22.507   3.277  1.00 38.94           C  
ANISOU  675  C   PHE A  86     3979   6020   4795   -688    266   -758       C  
ATOM    676  O   PHE A  86       4.430  21.959   3.129  1.00 38.80           O  
ANISOU  676  O   PHE A  86     3933   6035   4774   -595    261   -839       O  
ATOM    677  CB  PHE A  86       7.385  21.446   4.381  1.00 39.14           C  
ANISOU  677  CB  PHE A  86     3896   5981   4994   -800    177   -856       C  
ATOM    678  CG  PHE A  86       6.959  20.155   3.773  1.00 39.17           C  
ANISOU  678  CG  PHE A  86     3766   6078   5039   -693    176  -1006       C  
ATOM    679  CD1 PHE A  86       6.929  20.001   2.394  1.00 39.82           C  
ANISOU  679  CD1 PHE A  86     3713   6394   5023   -636    235  -1086       C  
ATOM    680  CD2 PHE A  86       6.544  19.107   4.578  1.00 39.31           C  
ANISOU  680  CD2 PHE A  86     3797   5950   5186   -658    114  -1068       C  
ATOM    681  CE1 PHE A  86       6.519  18.828   1.829  1.00 40.12           C  
ANISOU  681  CE1 PHE A  86     3624   6506   5114   -540    214  -1291       C  
ATOM    682  CE2 PHE A  86       6.127  17.911   4.016  1.00 39.65           C  
ANISOU  682  CE2 PHE A  86     3716   6015   5334   -581    100  -1228       C  
ATOM    683  CZ  PHE A  86       6.112  17.778   2.634  1.00 40.13           C  
ANISOU  683  CZ  PHE A  86     3634   6296   5316   -519    142  -1374       C  
ATOM    684  N   LYS A  87       6.093  23.164   2.308  1.00 40.35           N  
ANISOU  684  N   LYS A  87     4115   6336   4881   -729    316   -650       N  
ATOM    685  CA  LYS A  87       5.452  23.391   1.034  1.00 41.61           C  
ANISOU  685  CA  LYS A  87     4231   6703   4873   -639    352   -592       C  
ATOM    686  C   LYS A  87       6.081  22.588  -0.089  1.00 42.84           C  
ANISOU  686  C   LYS A  87     4190   7180   4906   -619    397   -704       C  
ATOM    687  O   LYS A  87       7.281  22.578  -0.270  1.00 43.50           O  
ANISOU  687  O   LYS A  87     4178   7358   4990   -711    454   -690       O  
ATOM    688  CB  LYS A  87       5.518  24.869   0.690  1.00 43.29           C  
ANISOU  688  CB  LYS A  87     4571   6845   5029   -688    387   -322       C  
ATOM    689  CG  LYS A  87       4.733  25.258  -0.539  1.00 44.94           C  
ANISOU  689  CG  LYS A  87     4775   7259   5040   -568    392   -188       C  
ATOM    690  CD  LYS A  87       4.565  26.766  -0.586  1.00 46.78           C  
ANISOU  690  CD  LYS A  87     5184   7284   5305   -588    393    112       C  
ATOM    691  CE  LYS A  87       3.904  27.215  -1.867  1.00 49.08           C  
ANISOU  691  CE  LYS A  87     5477   7798   5373   -460    377    323       C  
ATOM    692  NZ  LYS A  87       3.141  28.476  -1.633  1.00 51.16           N  
ANISOU  692  NZ  LYS A  87     5924   7755   5757   -370    313    547       N  
ATOM    693  N   SER A  88       5.237  21.916  -0.855  1.00 43.61           N  
ANISOU  693  N   SER A  88     4202   7468   4897   -493    368   -850       N  
ATOM    694  CA  SER A  88       5.661  21.299  -2.105  1.00 45.84           C  
ANISOU  694  CA  SER A  88     4306   8116   4992   -442    411   -995       C  
ATOM    695  C   SER A  88       4.421  21.103  -2.974  1.00 47.86           C  
ANISOU  695  C   SER A  88     4530   8581   5073   -305    342  -1084       C  
ATOM    696  O   SER A  88       3.456  20.461  -2.540  1.00 46.80           O  
ANISOU  696  O   SER A  88     4380   8313   5088   -250    252  -1252       O  
ATOM    697  CB  SER A  88       6.329  19.981  -1.823  1.00 45.27           C  
ANISOU  697  CB  SER A  88     4083   8022   5096   -431    396  -1287       C  
ATOM    698  OG  SER A  88       6.596  19.294  -3.025  1.00 47.45           O  
ANISOU  698  OG  SER A  88     4175   8653   5200   -346    433  -1518       O  
ATOM    699  N   GLY A  89       4.466  21.664  -4.196  1.00 52.34           N  
ANISOU  699  N   GLY A  89     5072   9497   5316   -263    382   -955       N  
ATOM    700  CA  GLY A  89       3.244  22.122  -4.925  1.00 54.80           C  
ANISOU  700  CA  GLY A  89     5419   9983   5417   -133    286   -862       C  
ATOM    701  C   GLY A  89       2.864  23.610  -4.660  1.00 55.84           C  
ANISOU  701  C   GLY A  89     5751   9911   5554   -136    279   -446       C  
ATOM    702  O   GLY A  89       1.929  24.171  -5.289  1.00 57.34           O  
ANISOU  702  O   GLY A  89     5976  10233   5574     -3    186   -295       O  
ATOM    703  OXT GLY A  89       3.469  24.316  -3.800  1.00 55.09           O  
ANISOU  703  OXT GLY A  89     5784   9493   5653   -259    344   -260       O  
TER     704      GLY A  89                                                      
ATOM    705  N   ASP B   3       5.277 -11.696  11.328  1.00130.79           N  
ANISOU  705  N   ASP B   3    17913   7973  23808   1912    325   4019       N  
ATOM    706  CA  ASP B   3       4.910 -10.584  12.263  1.00126.65           C  
ANISOU  706  CA  ASP B   3    17432   8327  22363   1820    156   4364       C  
ATOM    707  C   ASP B   3       4.863  -9.189  11.592  1.00117.46           C  
ANISOU  707  C   ASP B   3    15939   8022  20667   1580    -47   3651       C  
ATOM    708  O   ASP B   3       4.893  -8.167  12.286  1.00114.00           O  
ANISOU  708  O   ASP B   3    15465   8343  19505   1617   -256   3825       O  
ATOM    709  CB  ASP B   3       5.887 -10.566  13.452  1.00130.46           C  
ANISOU  709  CB  ASP B   3    18035   9088  22445   2439   -168   5114       C  
ATOM    710  N   ARG B   4       4.777  -9.146  10.259  1.00114.06           N  
ANISOU  710  N   ARG B   4    15273   7472  20590   1334     30   2858       N  
ATOM    711  CA  ARG B   4       4.722  -7.873   9.523  1.00105.97           C  
ANISOU  711  CA  ARG B   4    13956   7197  19109   1117   -129   2222       C  
ATOM    712  C   ARG B   4       3.967  -7.986   8.178  1.00103.70           C  
ANISOU  712  C   ARG B   4    13506   6731  19165    648     94   1480       C  
ATOM    713  O   ARG B   4       4.497  -7.624   7.121  1.00100.79           O  
ANISOU  713  O   ARG B   4    12887   6574  18833    674    -13    862       O  
ATOM    714  CB  ARG B   4       6.139  -7.321   9.301  1.00103.66           C  
ANISOU  714  CB  ARG B   4    13434   7309  18643   1570   -483   2010       C  
ATOM    715  N   LYS B   5       2.726  -8.480   8.231  1.00105.53           N  
ANISOU  715  N   LYS B   5    13863   6617  19616    212    410   1535       N  
ATOM    716  CA  LYS B   5       1.852  -8.571   7.041  1.00103.81           C  
ANISOU  716  CA  LYS B   5    13463   6318  19661   -273    607    829       C  
ATOM    717  C   LYS B   5       1.308  -7.186   6.621  1.00 96.42           C  
ANISOU  717  C   LYS B   5    12305   6232  18094   -532    466    468       C  
ATOM    718  O   LYS B   5       1.116  -6.292   7.461  1.00 93.24           O  
ANISOU  718  O   LYS B   5    11950   6345  17132   -501    351    836       O  
ATOM    719  CB  LYS B   5       0.697  -9.557   7.292  1.00108.89           C  
ANISOU  719  CB  LYS B   5    14271   6319  20780   -672   1000    992       C  
ATOM    720  N   ALA B   6       1.055  -7.025   5.320  1.00 94.16           N  
ANISOU  720  N   ALA B   6    11778   6091  17907   -774    483   -249       N  
ATOM    721  CA  ALA B   6       0.674  -5.722   4.736  1.00 87.80           C  
ANISOU  721  CA  ALA B   6    10748   6065  16546   -949    330   -602       C  
ATOM    722  C   ALA B   6      -0.836  -5.456   4.774  1.00 87.02           C  
ANISOU  722  C   ALA B   6    10591   6152  16320  -1418    488   -662       C  
ATOM    723  O   ALA B   6      -1.615  -6.241   4.230  1.00 90.45           O  
ANISOU  723  O   ALA B   6    10964   6234  17169  -1755    701   -989       O  
ATOM    724  CB  ALA B   6       1.171  -5.633   3.297  1.00 86.33           C  
ANISOU  724  CB  ALA B   6    10325   6033  16442   -947    256  -1304       C  
ATOM    725  N   VAL B   7      -1.241  -4.352   5.406  1.00 82.96           N  
ANISOU  725  N   VAL B   7    10062   6194  15263  -1441    389   -396       N  
ATOM    726  CA  VAL B   7      -2.654  -3.944   5.463  1.00 81.88           C  
ANISOU  726  CA  VAL B   7     9817   6320  14971  -1844    517   -466       C  
ATOM    727  C   VAL B   7      -2.766  -2.535   4.914  1.00 76.17           C  
ANISOU  727  C   VAL B   7     8871   6329  13738  -1833    308   -727       C  
ATOM    728  O   VAL B   7      -2.223  -1.603   5.501  1.00 73.03           O  
ANISOU  728  O   VAL B   7     8515   6294  12937  -1590    151   -463       O  
ATOM    729  CB  VAL B   7      -3.226  -3.989   6.921  1.00 83.64           C  
ANISOU  729  CB  VAL B   7    10246   6470  15060  -1906    675    165       C  
ATOM    730  CG1 VAL B   7      -4.576  -3.270   7.021  1.00 81.53           C  
ANISOU  730  CG1 VAL B   7     9807   6627  14541  -2262    771     69       C  
ATOM    731  CG2 VAL B   7      -3.358  -5.427   7.396  1.00 90.30           C  
ANISOU  731  CG2 VAL B   7    11316   6538  16455  -1991    954    459       C  
ATOM    732  N   ILE B   8      -3.460  -2.384   3.787  1.00 75.54           N  
ANISOU  732  N   ILE B   8     8549   6467  13684  -2088    306  -1248       N  
ATOM    733  CA  ILE B   8      -3.738  -1.056   3.214  1.00 70.86           C  
ANISOU  733  CA  ILE B   8     7744   6548  12629  -2086    131  -1447       C  
ATOM    734  C   ILE B   8      -4.938  -0.426   3.898  1.00 69.77           C  
ANISOU  734  C   ILE B   8     7535   6690  12285  -2289    206  -1245       C  
ATOM    735  O   ILE B   8      -6.028  -0.972   3.867  1.00 72.62           O  
ANISOU  735  O   ILE B   8     7799   6920  12872  -2618    373  -1369       O  
ATOM    736  CB  ILE B   8      -4.047  -1.133   1.709  1.00 71.28           C  
ANISOU  736  CB  ILE B   8     7551   6806  12726  -2250     74  -2060       C  
ATOM    737  CG1 ILE B   8      -2.820  -1.624   0.938  1.00 72.26           C  
ANISOU  737  CG1 ILE B   8     7710   6740  13003  -2042     15  -2332       C  
ATOM    738  CG2 ILE B   8      -4.516   0.235   1.191  1.00 67.19           C  
ANISOU  738  CG2 ILE B   8     6826   6969  11732  -2241    -88  -2158       C  
ATOM    739  CD1 ILE B   8      -3.174  -2.199  -0.426  1.00 74.89           C  
ANISOU  739  CD1 ILE B   8     7837   7115  13501  -2266     40  -2981       C  
ATOM    740  N   LYS B   9      -4.736   0.724   4.514  1.00 66.17           N  
ANISOU  740  N   LYS B   9     7099   6615  11428  -2106    100   -976       N  
ATOM    741  CA  LYS B   9      -5.839   1.439   5.131  1.00 65.49           C  
ANISOU  741  CA  LYS B   9     6911   6832  11138  -2268    177   -834       C  
ATOM    742  C   LYS B   9      -6.619   2.284   4.104  1.00 63.51           C  
ANISOU  742  C   LYS B   9     6352   7049  10729  -2370     69  -1196       C  
ATOM    743  O   LYS B   9      -7.856   2.279   4.098  1.00 64.70           O  
ANISOU  743  O   LYS B   9     6314   7325  10942  -2629    166  -1304       O  
ATOM    744  CB  LYS B   9      -5.330   2.277   6.303  1.00 63.22           C  
ANISOU  744  CB  LYS B   9     6765   6736  10517  -2039    136   -431       C  
ATOM    745  CG  LYS B   9      -5.101   1.442   7.558  1.00 66.79           C  
ANISOU  745  CG  LYS B   9     7487   6832  11055  -2016    284     11       C  
ATOM    746  N   ASN B  10      -5.884   2.995   3.249  1.00 60.82           N  
ANISOU  746  N   ASN B  10     5951   6971  10184  -2156   -123  -1362       N  
ATOM    747  CA  ASN B  10      -6.464   3.856   2.200  1.00 59.45           C  
ANISOU  747  CA  ASN B  10     5516   7265   9805  -2175   -253  -1630       C  
ATOM    748  C   ASN B  10      -5.538   4.026   1.012  1.00 58.52           C  
ANISOU  748  C   ASN B  10     5380   7283   9570  -2008   -401  -1870       C  
ATOM    749  O   ASN B  10      -4.312   4.150   1.180  1.00 57.23           O  
ANISOU  749  O   ASN B  10     5380   7000   9363  -1786   -434  -1752       O  
ATOM    750  CB  ASN B  10      -6.740   5.261   2.730  1.00 56.50           C  
ANISOU  750  CB  ASN B  10     5080   7241   9145  -2039   -292  -1400       C  
ATOM    751  CG  ASN B  10      -7.849   5.295   3.735  1.00 57.97           C  
ANISOU  751  CG  ASN B  10     5205   7435   9386  -2218   -137  -1239       C  
ATOM    752  OD1 ASN B  10      -8.995   4.917   3.440  1.00 60.53           O  
ANISOU  752  OD1 ASN B  10     5320   7829   9849  -2464    -78  -1428       O  
ATOM    753  ND2 ASN B  10      -7.527   5.762   4.945  1.00 57.10           N  
ANISOU  753  ND2 ASN B  10     5249   7294   9152  -2108    -61   -923       N  
ATOM    754  N   ALA B  11      -6.125   4.084  -0.179  1.00 59.65           N  
ANISOU  754  N   ALA B  11     5300   7734   9627  -2112   -490  -2211       N  
ATOM    755  CA  ALA B  11      -5.353   4.210  -1.410  1.00 59.53           C  
ANISOU  755  CA  ALA B  11     5253   7921   9443  -1987   -603  -2466       C  
ATOM    756  C   ALA B  11      -6.142   4.918  -2.513  1.00 60.13           C  
ANISOU  756  C   ALA B  11     5072   8558   9216  -2008   -747  -2654       C  
ATOM    757  O   ALA B  11      -7.339   4.699  -2.665  1.00 62.51           O  
ANISOU  757  O   ALA B  11     5158   9023   9566  -2208   -771  -2817       O  
ATOM    758  CB  ALA B  11      -4.910   2.836  -1.886  1.00 62.48           C  
ANISOU  758  CB  ALA B  11     5674   7950  10115  -2106   -536  -2814       C  
ATOM    759  N   ASP B  12      -5.446   5.783  -3.251  1.00 58.54           N  
ANISOU  759  N   ASP B  12     4884   8657   8699  -1791   -836  -2604       N  
ATOM    760  CA  ASP B  12      -5.901   6.332  -4.532  1.00 59.80           C  
ANISOU  760  CA  ASP B  12     4844   9369   8508  -1756   -983  -2770       C  
ATOM    761  C   ASP B  12      -4.685   6.205  -5.443  1.00 60.17           C  
ANISOU  761  C   ASP B  12     4990   9480   8391  -1647   -974  -2939       C  
ATOM    762  O   ASP B  12      -3.830   7.083  -5.518  1.00 58.12           O  
ANISOU  762  O   ASP B  12     4843   9287   7953  -1438   -947  -2694       O  
ATOM    763  CB  ASP B  12      -6.347   7.784  -4.383  1.00 57.92           C  
ANISOU  763  CB  ASP B  12     4540   9434   8034  -1566  -1050  -2398       C  
ATOM    764  CG  ASP B  12      -6.753   8.421  -5.700  1.00 59.71           C  
ANISOU  764  CG  ASP B  12     4584  10241   7860  -1463  -1214  -2459       C  
ATOM    765  OD1 ASP B  12      -7.908   8.277  -6.113  1.00 63.22           O  
ANISOU  765  OD1 ASP B  12     4772  11014   8234  -1562  -1347  -2629       O  
ATOM    766  OD2 ASP B  12      -5.934   9.108  -6.316  1.00 59.18           O  
ANISOU  766  OD2 ASP B  12     4618  10333   7535  -1275  -1209  -2315       O  
ATOM    767  N   MET B  13      -4.589   5.054  -6.090  1.00 63.34           N  
ANISOU  767  N   MET B  13     5340   9821   8905  -1812   -959  -3396       N  
ATOM    768  CA  MET B  13      -3.357   4.626  -6.734  1.00 64.04           C  
ANISOU  768  CA  MET B  13     5528   9834   8968  -1739   -889  -3630       C  
ATOM    769  C   MET B  13      -3.676   3.416  -7.607  1.00 68.61           C  
ANISOU  769  C   MET B  13     5961  10462   9643  -1968   -891  -4239       C  
ATOM    770  O   MET B  13      -4.709   2.765  -7.423  1.00 70.77           O  
ANISOU  770  O   MET B  13     6098  10655  10134  -2202   -909  -4444       O  
ATOM    771  CB  MET B  13      -2.341   4.248  -5.647  1.00 61.99           C  
ANISOU  771  CB  MET B  13     5489   8983   9078  -1640   -757  -3433       C  
ATOM    772  CG  MET B  13      -0.901   4.027  -6.105  1.00 62.16           C  
ANISOU  772  CG  MET B  13     5601   8905   9111  -1493   -676  -3588       C  
ATOM    773  SD  MET B  13       0.197   3.913  -4.652  1.00 59.55           S  
ANISOU  773  SD  MET B  13     5479   8004   9142  -1301   -597  -3232       S  
ATOM    774  CE  MET B  13       1.595   4.882  -5.235  1.00 58.39           C  
ANISOU  774  CE  MET B  13     5341   8123   8722  -1076   -554  -3184       C  
ATOM    775  N   SER B  14      -2.811   3.113  -8.566  1.00 70.49           N  
ANISOU  775  N   SER B  14     6203  10844   9736  -1925   -848  -4573       N  
ATOM    776  CA  SER B  14      -2.996   1.886  -9.345  1.00 75.26           C  
ANISOU  776  CA  SER B  14     6668  11434  10490  -2152   -813  -5238       C  
ATOM    777  C   SER B  14      -2.631   0.692  -8.472  1.00 75.97           C  
ANISOU  777  C   SER B  14     6884  10732  11248  -2236   -644  -5342       C  
ATOM    778  O   SER B  14      -1.851   0.817  -7.523  1.00 73.17           O  
ANISOU  778  O   SER B  14     6734   9944  11120  -2051   -567  -4944       O  
ATOM    779  CB  SER B  14      -2.120   1.878 -10.604  1.00 77.55           C  
ANISOU  779  CB  SER B  14     6924  12110  10428  -2079   -779  -5603       C  
ATOM    780  OG  SER B  14      -0.776   1.516 -10.297  1.00 76.80           O  
ANISOU  780  OG  SER B  14     6997  11558  10625  -1933   -606  -5601       O  
ATOM    781  N   GLU B  15      -3.150  -0.473  -8.830  1.00 80.59           N  
ANISOU  781  N   GLU B  15     7337  11135  12146  -2505   -584  -5892       N  
ATOM    782  CA  GLU B  15      -2.850  -1.714  -8.097  1.00 82.46           C  
ANISOU  782  CA  GLU B  15     7696  10555  13079  -2591   -390  -6001       C  
ATOM    783  C   GLU B  15      -1.380  -2.147  -8.190  1.00 82.58           C  
ANISOU  783  C   GLU B  15     7857  10213  13305  -2364   -263  -6094       C  
ATOM    784  O   GLU B  15      -0.786  -2.592  -7.203  1.00 81.64           O  
ANISOU  784  O   GLU B  15     7928   9460  13630  -2224   -160  -5786       O  
ATOM    785  CB  GLU B  15      -3.728  -2.844  -8.614  1.00 87.97           C  
ANISOU  785  CB  GLU B  15     8186  11138  14099  -2962   -320  -6656       C  
ATOM    786  CG  GLU B  15      -4.115  -3.818  -7.542  1.00 89.73           C  
ANISOU  786  CG  GLU B  15     8515  10558  15019  -3132   -132  -6532       C  
ATOM    787  CD  GLU B  15      -5.282  -4.635  -7.961  1.00 95.84           C  
ANISOU  787  CD  GLU B  15     9032  11321  16060  -3558    -73  -7109       C  
ATOM    788  OE1 GLU B  15      -5.085  -5.639  -8.718  1.00100.97           O  
ANISOU  788  OE1 GLU B  15     9571  11773  17017  -3731     48  -7803       O  
ATOM    789  OE2 GLU B  15      -6.406  -4.242  -7.551  1.00 95.36           O  
ANISOU  789  OE2 GLU B  15     8848  11474  15907  -3726   -143  -6911       O  
ATOM    790  N   ASP B  16      -0.815  -2.033  -9.386  1.00 84.17           N  
ANISOU  790  N   ASP B  16     7948  10857  13174  -2321   -271  -6525       N  
ATOM    791  CA  ASP B  16       0.609  -2.277  -9.584  1.00 84.54           C  
ANISOU  791  CA  ASP B  16     8080  10687  13354  -2088   -147  -6640       C  
ATOM    792  C   ASP B  16       1.430  -1.429  -8.621  1.00 79.42           C  
ANISOU  792  C   ASP B  16     7619   9896  12659  -1778   -180  -5955       C  
ATOM    793  O   ASP B  16       2.151  -1.967  -7.774  1.00 79.34           O  
ANISOU  793  O   ASP B  16     7741   9285  13118  -1611   -100  -5766       O  
ATOM    794  CB  ASP B  16       1.015  -2.006 -11.044  1.00 86.85           C  
ANISOU  794  CB  ASP B  16     8216  11648  13134  -2097   -143  -7138       C  
ATOM    795  CG  ASP B  16       0.484  -3.083 -12.016  1.00 93.37           C  
ANISOU  795  CG  ASP B  16     8833  12556  14084  -2392    -77  -7983       C  
ATOM    796  OD1 ASP B  16      -0.409  -3.873 -11.622  1.00 95.56           O  
ANISOU  796  OD1 ASP B  16     9061  12449  14798  -2633    -58  -8160       O  
ATOM    797  OD2 ASP B  16       0.959  -3.147 -13.176  1.00 96.58           O  
ANISOU  797  OD2 ASP B  16     9115  13422  14156  -2404    -22  -8502       O  
ATOM    798  N   MET B  17       1.289  -0.112  -8.739  1.00 75.73           N  
ANISOU  798  N   MET B  17     7151   9980  11642  -1698   -300  -5589       N  
ATOM    799  CA  MET B  17       1.961   0.821  -7.846  1.00 71.22           C  
ANISOU  799  CA  MET B  17     6723   9334  11002  -1450   -329  -4992       C  
ATOM    800  C   MET B  17       1.779   0.463  -6.370  1.00 69.72           C  
ANISOU  800  C   MET B  17     6683   8561  11245  -1403   -337  -4580       C  
ATOM    801  O   MET B  17       2.737   0.513  -5.600  1.00 68.55           O  
ANISOU  801  O   MET B  17     6642   8115  11286  -1175   -318  -4306       O  
ATOM    802  CB  MET B  17       1.446   2.242  -8.059  1.00 68.36           C  
ANISOU  802  CB  MET B  17     6335   9551  10084  -1431   -443  -4641       C  
ATOM    803  CG  MET B  17       1.971   2.951  -9.287  1.00 69.41           C  
ANISOU  803  CG  MET B  17     6393  10265   9715  -1371   -412  -4791       C  
ATOM    804  SD  MET B  17       2.018   4.764  -9.003  1.00 65.80           S  
ANISOU  804  SD  MET B  17     6005  10156   8837  -1205   -461  -4134       S  
ATOM    805  CE  MET B  17       2.401   5.314 -10.679  1.00 68.20           C  
ANISOU  805  CE  MET B  17     6222  11159   8531  -1197   -389  -4356       C  
ATOM    806  N   GLN B  18       0.559   0.111  -5.975  1.00 70.49           N  
ANISOU  806  N   GLN B  18     6769   8537  11474  -1620   -363  -4536       N  
ATOM    807  CA  GLN B  18       0.265  -0.220  -4.566  1.00 69.79           C  
ANISOU  807  CA  GLN B  18     6834   7944  11735  -1608   -338  -4108       C  
ATOM    808  C   GLN B  18       1.107  -1.383  -4.038  1.00 72.49           C  
ANISOU  808  C   GLN B  18     7302   7613  12626  -1479   -224  -4134       C  
ATOM    809  O   GLN B  18       1.704  -1.278  -2.958  1.00 71.06           O  
ANISOU  809  O   GLN B  18     7273   7160  12565  -1258   -243  -3682       O  
ATOM    810  CB  GLN B  18      -1.226  -0.531  -4.362  1.00 71.42           C  
ANISOU  810  CB  GLN B  18     6970   8133  12032  -1914   -330  -4141       C  
ATOM    811  CG  GLN B  18      -2.101   0.710  -4.325  1.00 68.33           C  
ANISOU  811  CG  GLN B  18     6487   8288  11186  -1953   -459  -3885       C  
ATOM    812  CD  GLN B  18      -3.565   0.390  -4.175  1.00 70.25           C  
ANISOU  812  CD  GLN B  18     6596   8557  11537  -2255   -448  -3977       C  
ATOM    813  OE1 GLN B  18      -3.990  -0.237  -3.203  1.00 71.58           O  
ANISOU  813  OE1 GLN B  18     6856   8270  12070  -2375   -330  -3789       O  
ATOM    814  NE2 GLN B  18      -4.355   0.837  -5.135  1.00 71.61           N  
ANISOU  814  NE2 GLN B  18     6535   9295  11377  -2376   -568  -4249       N  
ATOM    815  N   GLN B  19       1.142  -2.485  -4.790  1.00 77.01           N  
ANISOU  815  N   GLN B  19     7797   7928  13534  -1605   -109  -4671       N  
ATOM    816  CA  GLN B  19       2.007  -3.619  -4.457  1.00 80.41           C  
ANISOU  816  CA  GLN B  19     8322   7685  14543  -1443     15  -4747       C  
ATOM    817  C   GLN B  19       3.464  -3.139  -4.426  1.00 78.50           C  
ANISOU  817  C   GLN B  19     8094   7545  14186  -1074    -39  -4624       C  
ATOM    818  O   GLN B  19       4.241  -3.514  -3.544  1.00 79.07           O  
ANISOU  818  O   GLN B  19     8284   7182  14576   -805    -40  -4305       O  
ATOM    819  CB  GLN B  19       1.833  -4.777  -5.453  1.00 85.68           C  
ANISOU  819  CB  GLN B  19     8860   8107  15584  -1651    171  -5465       C  
ATOM    820  N   ASP B  20       3.816  -2.279  -5.375  1.00 76.58           N  
ANISOU  820  N   ASP B  20     7716   7907  13471  -1060    -84  -4854       N  
ATOM    821  CA  ASP B  20       5.202  -1.837  -5.536  1.00 75.48           C  
ANISOU  821  CA  ASP B  20     7535   7905  13240   -769    -87  -4850       C  
ATOM    822  C   ASP B  20       5.658  -1.008  -4.352  1.00 71.47           C  
ANISOU  822  C   ASP B  20     7130   7407  12617   -544   -209  -4234       C  
ATOM    823  O   ASP B  20       6.810  -1.095  -3.917  1.00 71.80           O  
ANISOU  823  O   ASP B  20     7161   7271  12846   -259   -225  -4132       O  
ATOM    824  CB  ASP B  20       5.366  -1.048  -6.835  1.00 74.89           C  
ANISOU  824  CB  ASP B  20     7309   8501  12645   -852    -64  -5188       C  
ATOM    825  CG  ASP B  20       6.750  -1.188  -7.432  1.00 76.85           C  
ANISOU  825  CG  ASP B  20     7445   8784  12968   -651     47  -5510       C  
ATOM    826  OD1 ASP B  20       7.160  -2.336  -7.775  1.00 80.80           O  
ANISOU  826  OD1 ASP B  20     7883   8906  13909   -615    168  -5959       O  
ATOM    827  OD2 ASP B  20       7.418  -0.135  -7.558  1.00 74.70           O  
ANISOU  827  OD2 ASP B  20     7133   8903  12346   -539     38  -5330       O  
ATOM    828  N   ALA B  21       4.746  -0.205  -3.831  1.00 68.23           N  
ANISOU  828  N   ALA B  21     6788   7230  11904   -670   -297  -3866       N  
ATOM    829  CA  ALA B  21       4.971   0.458  -2.561  1.00 65.35           C  
ANISOU  829  CA  ALA B  21     6528   6837  11462   -504   -401  -3318       C  
ATOM    830  C   ALA B  21       5.209  -0.603  -1.481  1.00 67.90           C  
ANISOU  830  C   ALA B  21     6989   6559  12248   -350   -403  -3070       C  
ATOM    831  O   ALA B  21       6.236  -0.606  -0.816  1.00 68.15           O  
ANISOU  831  O   ALA B  21     7037   6467  12390    -58   -473  -2864       O  
ATOM    832  CB  ALA B  21       3.779   1.322  -2.211  1.00 62.53           C  
ANISOU  832  CB  ALA B  21     6210   6772  10777   -694   -456  -3038       C  
ATOM    833  N   VAL B  22       4.268  -1.524  -1.336  1.00 70.49           N  
ANISOU  833  N   VAL B  22     7402   6520  12859   -545   -318  -3092       N  
ATOM    834  CA  VAL B  22       4.366  -2.549  -0.295  1.00 73.79           C  
ANISOU  834  CA  VAL B  22     7989   6323  13721   -415   -281  -2769       C  
ATOM    835  C   VAL B  22       5.677  -3.341  -0.369  1.00 77.17           C  
ANISOU  835  C   VAL B  22     8392   6372  14555    -82   -272  -2895       C  
ATOM    836  O   VAL B  22       6.185  -3.776   0.662  1.00 79.12           O  
ANISOU  836  O   VAL B  22     8763   6274  15025    189   -329  -2476       O  
ATOM    837  CB  VAL B  22       3.155  -3.509  -0.326  1.00 77.06           C  
ANISOU  837  CB  VAL B  22     8473   6340  14464   -733   -121  -2863       C  
ATOM    838  CG1 VAL B  22       3.317  -4.642   0.683  1.00 81.35           C  
ANISOU  838  CG1 VAL B  22     9219   6171  15519   -590    -31  -2489       C  
ATOM    839  CG2 VAL B  22       1.880  -2.738  -0.042  1.00 74.30           C  
ANISOU  839  CG2 VAL B  22     8123   6357  13749  -1016   -141  -2676       C  
ATOM    840  N   ASP B  23       6.216  -3.521  -1.576  1.00 78.41           N  
ANISOU  840  N   ASP B  23     8377   6626  14789    -85   -201  -3463       N  
ATOM    841  CA  ASP B  23       7.523  -4.172  -1.759  1.00 81.69           C  
ANISOU  841  CA  ASP B  23     8706   6745  15588    247   -179  -3662       C  
ATOM    842  C   ASP B  23       8.662  -3.262  -1.257  1.00 79.10           C  
ANISOU  842  C   ASP B  23     8294   6767  14994    567   -348  -3406       C  
ATOM    843  O   ASP B  23       9.521  -3.684  -0.456  1.00 81.12           O  
ANISOU  843  O   ASP B  23     8564   6731  15525    926   -442  -3135       O  
ATOM    844  CB  ASP B  23       7.785  -4.501  -3.237  1.00 83.89           C  
ANISOU  844  CB  ASP B  23     8792   7133  15948    128    -29  -4403       C  
ATOM    845  CG  ASP B  23       6.721  -5.399  -3.859  1.00 87.49           C  
ANISOU  845  CG  ASP B  23     9266   7303  16670   -215    135  -4804       C  
ATOM    846  OD1 ASP B  23       6.266  -6.357  -3.195  1.00 90.93           O  
ANISOU  846  OD1 ASP B  23     9849   7106  17592   -238    212  -4608       O  
ATOM    847  OD2 ASP B  23       6.352  -5.151  -5.035  1.00 87.47           O  
ANISOU  847  OD2 ASP B  23     9119   7728  16386   -468    197  -5327       O  
ATOM    848  N   CYS B  24       8.667  -2.019  -1.748  1.00 74.80           N  
ANISOU  848  N   CYS B  24     7643   6847  13930    438   -384  -3500       N  
ATOM    849  CA  CYS B  24       9.652  -1.031  -1.313  1.00 72.47           C  
ANISOU  849  CA  CYS B  24     7241   6910  13382    660   -509  -3312       C  
ATOM    850  C   CYS B  24       9.711  -0.970   0.189  1.00 72.03           C  
ANISOU  850  C   CYS B  24     7314   6717  13336    860   -685  -2738       C  
ATOM    851  O   CYS B  24      10.782  -1.118   0.778  1.00 74.06           O  
ANISOU  851  O   CYS B  24     7485   6902  13750   1200   -805  -2614       O  
ATOM    852  CB  CYS B  24       9.334   0.364  -1.840  1.00 68.06           C  
ANISOU  852  CB  CYS B  24     6620   6957  12283    439   -495  -3354       C  
ATOM    853  SG  CYS B  24      10.141   0.715  -3.401  1.00 70.27           S  
ANISOU  853  SG  CYS B  24     6670   7605  12422    392   -326  -3926       S  
ATOM    854  N   ALA B  25       8.552  -0.759   0.800  1.00 70.16           N  
ANISOU  854  N   ALA B  25     7259   6486  12911    654   -701  -2407       N  
ATOM    855  CA  ALA B  25       8.448  -0.673   2.248  1.00 70.05           C  
ANISOU  855  CA  ALA B  25     7390   6409  12815    798   -842  -1853       C  
ATOM    856  C   ALA B  25       9.145  -1.857   2.891  1.00 74.96           C  
ANISOU  856  C   ALA B  25     8076   6528  13877   1145   -900  -1642       C  
ATOM    857  O   ALA B  25       9.897  -1.703   3.853  1.00 75.62           O  
ANISOU  857  O   ALA B  25     8141   6701  13888   1454  -1085  -1320       O  
ATOM    858  CB  ALA B  25       7.003  -0.639   2.663  1.00 69.00           C  
ANISOU  858  CB  ALA B  25     7442   6234  12540    499   -773  -1603       C  
ATOM    859  N   THR B  26       8.903  -3.035   2.323  1.00 78.63           N  
ANISOU  859  N   THR B  26     8594   6470  14808   1100   -743  -1849       N  
ATOM    860  CA  THR B  26       9.465  -4.264   2.831  1.00 84.23           C  
ANISOU  860  CA  THR B  26     9383   6583  16037   1433   -753  -1642       C  
ATOM    861  C   THR B  26      10.978  -4.248   2.678  1.00 85.95           C  
ANISOU  861  C   THR B  26     9362   6892  16401   1845   -885  -1823       C  
ATOM    862  O   THR B  26      11.695  -4.580   3.630  1.00 89.19           O  
ANISOU  862  O   THR B  26     9787   7165  16935   2245  -1061  -1426       O  
ATOM    863  CB  THR B  26       8.854  -5.507   2.117  1.00 88.48           C  
ANISOU  863  CB  THR B  26    10002   6492  17124   1248   -502  -1938       C  
ATOM    864  OG1 THR B  26       7.431  -5.522   2.291  1.00 87.45           O  
ANISOU  864  OG1 THR B  26    10047   6301  16878    844   -377  -1793       O  
ATOM    865  CG2 THR B  26       9.431  -6.826   2.672  1.00 95.25           C  
ANISOU  865  CG2 THR B  26    10961   6614  18613   1623   -479  -1672       C  
ATOM    866  N   GLN B  27      11.470  -3.873   1.494  1.00 84.44           N  
ANISOU  866  N   GLN B  27     8935   6965  16183   1759   -798  -2411       N  
ATOM    867  CA  GLN B  27      12.928  -3.814   1.258  1.00 86.15           C  
ANISOU  867  CA  GLN B  27     8869   7309  16554   2117   -882  -2659       C  
ATOM    868  C   GLN B  27      13.577  -2.861   2.246  1.00 83.87           C  
ANISOU  868  C   GLN B  27     8485   7486  15895   2326  -1140  -2311       C  
ATOM    869  O   GLN B  27      14.473  -3.234   3.001  1.00 87.09           O  
ANISOU  869  O   GLN B  27     8801   7793  16497   2751  -1330  -2079       O  
ATOM    870  CB  GLN B  27      13.251  -3.358  -0.169  1.00 84.62           C  
ANISOU  870  CB  GLN B  27     8446   7444  16259   1915   -706  -3323       C  
ATOM    871  CG  GLN B  27      12.967  -4.398  -1.259  1.00 88.50           C  
ANISOU  871  CG  GLN B  27     8933   7528  17162   1783   -461  -3835       C  
ATOM    872  CD  GLN B  27      13.368  -3.898  -2.646  1.00 87.72           C  
ANISOU  872  CD  GLN B  27     8601   7865  16862   1605   -289  -4476       C  
ATOM    873  OE1 GLN B  27      13.253  -2.696  -2.949  1.00 83.36           O  
ANISOU  873  OE1 GLN B  27     7999   7900  15772   1399   -297  -4479       O  
ATOM    874  NE2 GLN B  27      13.839  -4.818  -3.496  1.00 91.76           N  
ANISOU  874  NE2 GLN B  27     8973   8082  17809   1685   -108  -5016       N  
ATOM    875  N   ALA B  28      13.089  -1.628   2.237  1.00 78.73           N  
ANISOU  875  N   ALA B  28     7842   7349  14721   2029  -1146  -2292       N  
ATOM    876  CA  ALA B  28      13.546  -0.597   3.165  1.00 76.76           C  
ANISOU  876  CA  ALA B  28     7500   7569  14093   2138  -1357  -2033       C  
ATOM    877  C   ALA B  28      13.649  -1.098   4.615  1.00 79.94           C  
ANISOU  877  C   ALA B  28     8035   7818  14519   2459  -1593  -1464       C  
ATOM    878  O   ALA B  28      14.628  -0.806   5.310  1.00 81.70           O  
ANISOU  878  O   ALA B  28     8067   8310  14663   2772  -1823  -1362       O  
ATOM    879  CB  ALA B  28      12.643   0.624   3.094  1.00 71.41           C  
ANISOU  879  CB  ALA B  28     6906   7299  12928   1747  -1292  -2001       C  
ATOM    880  N   MET B  29      12.656  -1.854   5.070  1.00 81.36           N  
ANISOU  880  N   MET B  29     8524   7595  14792   2380  -1533  -1094       N  
ATOM    881  CA  MET B  29      12.648  -2.337   6.456  1.00 84.77           C  
ANISOU  881  CA  MET B  29     9131   7896  15179   2665  -1721   -473       C  
ATOM    882  C   MET B  29      13.618  -3.509   6.699  1.00 91.15           C  
ANISOU  882  C   MET B  29     9880   8267  16485   3175  -1837   -322       C  
ATOM    883  O   MET B  29      13.958  -3.808   7.844  1.00 94.83           O  
ANISOU  883  O   MET B  29    10416   8745  16868   3528  -2061    197       O  
ATOM    884  CB  MET B  29      11.224  -2.692   6.898  1.00 84.70           C  
ANISOU  884  CB  MET B  29     9473   7617  15089   2375  -1568    -95       C  
ATOM    885  CG  MET B  29      10.318  -1.465   7.113  1.00 79.14           C  
ANISOU  885  CG  MET B  29     8817   7417  13835   1988  -1533    -84       C  
ATOM    886  SD  MET B  29       8.793  -1.773   8.047  1.00 79.30           S  
ANISOU  886  SD  MET B  29     9198   7255  13677   1724  -1400    454       S  
ATOM    887  CE  MET B  29       9.433  -1.730   9.732  1.00 83.25           C  
ANISOU  887  CE  MET B  29     9772   8028  13830   2132  -1685   1075       C  
ATOM    888  N   GLU B  30      14.068  -4.160   5.631  1.00 92.95           N  
ANISOU  888  N   GLU B  30     9968   8134  17213   3236  -1687   -772       N  
ATOM    889  CA  GLU B  30      15.151  -5.145   5.744  1.00 99.32           C  
ANISOU  889  CA  GLU B  30    10632   8560  18543   3765  -1796   -730       C  
ATOM    890  C   GLU B  30      16.498  -4.459   5.929  1.00 99.48           C  
ANISOU  890  C   GLU B  30    10259   9129  18409   4091  -2058   -912       C  
ATOM    891  O   GLU B  30      17.386  -4.996   6.586  1.00104.56           O  
ANISOU  891  O   GLU B  30    10776   9683  19268   4610  -2296   -651       O  
ATOM    892  CB  GLU B  30      15.218  -6.044   4.505  1.00101.70           C  
ANISOU  892  CB  GLU B  30    10872   8311  19458   3712  -1518  -1252       C  
ATOM    893  CG  GLU B  30      14.066  -7.037   4.396  1.00104.16           C  
ANISOU  893  CG  GLU B  30    11526   7934  20115   3479  -1265  -1093       C  
ATOM    894  CD  GLU B  30      13.992  -7.716   3.035  1.00105.93           C  
ANISOU  894  CD  GLU B  30    11657   7747  20845   3298   -965  -1773       C  
ATOM    895  OE1 GLU B  30      15.032  -7.797   2.347  1.00107.61           O  
ANISOU  895  OE1 GLU B  30    11562   8019  21305   3524   -960  -2251       O  
ATOM    896  OE2 GLU B  30      12.892  -8.173   2.653  1.00106.24           O  
ANISOU  896  OE2 GLU B  30    11904   7431  21031   2917   -724  -1869       O  
ATOM    897  N   LYS B  31      16.636  -3.278   5.325  1.00 94.36           N  
ANISOU  897  N   LYS B  31     9403   9039  17410   3783  -2004  -1360       N  
ATOM    898  CA  LYS B  31      17.882  -2.510   5.357  1.00 94.22           C  
ANISOU  898  CA  LYS B  31     8967   9559  17270   3985  -2183  -1644       C  
ATOM    899  C   LYS B  31      17.981  -1.674   6.628  1.00 93.16           C  
ANISOU  899  C   LYS B  31     8812   9965  16620   4063  -2483  -1268       C  
ATOM    900  O   LYS B  31      18.926  -1.822   7.396  1.00 97.38           O  
ANISOU  900  O   LYS B  31     9124  10694  17180   4505  -2786  -1106       O  
ATOM    901  CB  LYS B  31      17.982  -1.595   4.129  1.00 89.64           C  
ANISOU  901  CB  LYS B  31     8190   9305  16563   3591  -1937  -2267       C  
ATOM    902  CG  LYS B  31      19.401  -1.411   3.596  1.00 92.01           C  
ANISOU  902  CG  LYS B  31     8019   9845  17093   3820  -1953  -2755       C  
ATOM    903  N   TYR B  32      16.987  -0.820   6.842  1.00 88.20           N  
ANISOU  903  N   TYR B  32     8394   9589  15526   3645  -2402  -1153       N  
ATOM    904  CA  TYR B  32      17.017   0.202   7.904  1.00 86.81           C  
ANISOU  904  CA  TYR B  32     8165   9998  14817   3613  -2623   -954       C  
ATOM    905  C   TYR B  32      16.011  -0.042   9.040  1.00 87.45           C  
ANISOU  905  C   TYR B  32     8625  10019  14583   3589  -2705   -332       C  
ATOM    906  O   TYR B  32      14.827  -0.308   8.792  1.00 85.21           O  
ANISOU  906  O   TYR B  32     8664   9407  14304   3285  -2475   -181       O  
ATOM    907  CB  TYR B  32      16.737   1.603   7.314  1.00 81.06           C  
ANISOU  907  CB  TYR B  32     7334   9678  13785   3145  -2442  -1356       C  
ATOM    908  CG  TYR B  32      17.597   1.943   6.116  1.00 80.34           C  
ANISOU  908  CG  TYR B  32     6912   9670  13944   3081  -2280  -1944       C  
ATOM    909  CD1 TYR B  32      18.857   2.525   6.274  1.00 81.65           C  
ANISOU  909  CD1 TYR B  32     6650  10249  14122   3254  -2425  -2240       C  
ATOM    910  CD2 TYR B  32      17.158   1.661   4.827  1.00 78.49           C  
ANISOU  910  CD2 TYR B  32     6770   9132  13919   2838  -1971  -2224       C  
ATOM    911  CE1 TYR B  32      19.644   2.822   5.176  1.00 81.34           C  
ANISOU  911  CE1 TYR B  32     6302  10286  14315   3171  -2226  -2770       C  
ATOM    912  CE2 TYR B  32      17.942   1.940   3.729  1.00 78.42           C  
ANISOU  912  CE2 TYR B  32     6472   9233  14089   2776  -1792  -2742       C  
ATOM    913  CZ  TYR B  32      19.179   2.520   3.903  1.00 79.80           C  
ANISOU  913  CZ  TYR B  32     6241   9787  14290   2936  -1900  -2999       C  
ATOM    914  OH  TYR B  32      19.942   2.785   2.793  1.00 80.27           O  
ANISOU  914  OH  TYR B  32     6013   9955  14531   2846  -1670  -3510       O  
ATOM    915  N   ASN B  33      16.494   0.090  10.280  1.00 90.59           N  
ANISOU  915  N   ASN B  33     8949  10795  14674   3896  -3028     -4       N  
ATOM    916  CA  ASN B  33      15.639   0.084  11.467  1.00 91.34           C  
ANISOU  916  CA  ASN B  33     9359  11012  14331   3857  -3108    559       C  
ATOM    917  C   ASN B  33      14.964   1.451  11.678  1.00 85.92           C  
ANISOU  917  C   ASN B  33     8681  10818  13146   3410  -3018    368       C  
ATOM    918  O   ASN B  33      13.838   1.513  12.153  1.00 84.60           O  
ANISOU  918  O   ASN B  33     8819  10610  12711   3170  -2895    678       O  
ATOM    919  CB  ASN B  33      16.431  -0.315  12.721  1.00 97.40           C  
ANISOU  919  CB  ASN B  33    10042  12070  14894   4385  -3505    993       C  
ATOM    920  N   ILE B  34      15.640   2.539  11.316  1.00 83.34           N  
ANISOU  920  N   ILE B  34     8006  10922  12736   3291  -3048   -150       N  
ATOM    921  CA  ILE B  34      15.144   3.894  11.626  1.00 79.42           C  
ANISOU  921  CA  ILE B  34     7476  10884  11814   2922  -2978   -341       C  
ATOM    922  C   ILE B  34      14.135   4.397  10.571  1.00 73.85           C  
ANISOU  922  C   ILE B  34     6923   9932  11202   2451  -2611   -562       C  
ATOM    923  O   ILE B  34      14.372   4.320   9.365  1.00 72.23           O  
ANISOU  923  O   ILE B  34     6623   9488  11331   2361  -2438   -884       O  
ATOM    924  CB  ILE B  34      16.296   4.940  11.807  1.00 79.78           C  
ANISOU  924  CB  ILE B  34     7068  11501  11742   2969  -3150   -803       C  
ATOM    925  CG1 ILE B  34      17.465   4.389  12.646  1.00 85.60           C  
ANISOU  925  CG1 ILE B  34     7553  12523  12447   3484  -3553   -676       C  
ATOM    926  CG2 ILE B  34      15.758   6.197  12.478  1.00 77.46           C  
ANISOU  926  CG2 ILE B  34     6773  11657  11000   2656  -3114   -916       C  
ATOM    927  CD1 ILE B  34      17.085   3.877  14.041  1.00 89.38           C  
ANISOU  927  CD1 ILE B  34     8266  13194  12497   3734  -3806    -79       C  
ATOM    928  N   GLU B  35      13.003   4.912  11.032  1.00 71.33           N  
ANISOU  928  N   GLU B  35     6826   9710  10566   2168  -2496   -389       N  
ATOM    929  CA  GLU B  35      11.932   5.301  10.119  1.00 66.93           C  
ANISOU  929  CA  GLU B  35     6416   8934  10080   1772  -2187   -523       C  
ATOM    930  C   GLU B  35      12.399   6.313   9.090  1.00 63.72           C  
ANISOU  930  C   GLU B  35     5758   8665   9786   1584  -2049  -1021       C  
ATOM    931  O   GLU B  35      12.172   6.139   7.889  1.00 61.73           O  
ANISOU  931  O   GLU B  35     5534   8150   9771   1443  -1853  -1197       O  
ATOM    932  CB  GLU B  35      10.732   5.898  10.872  1.00 65.33           C  
ANISOU  932  CB  GLU B  35     6407   8905   9509   1517  -2097   -317       C  
ATOM    933  CG  GLU B  35      10.036   4.952  11.846  1.00 68.50           C  
ANISOU  933  CG  GLU B  35     7102   9162   9760   1615  -2141    217       C  
ATOM    934  CD  GLU B  35      10.367   5.269  13.292  1.00 72.08           C  
ANISOU  934  CD  GLU B  35     7523  10102   9761   1788  -2367    422       C  
ATOM    935  OE1 GLU B  35      11.513   4.949  13.726  1.00 75.75           O  
ANISOU  935  OE1 GLU B  35     7823  10747  10209   2147  -2643    457       O  
ATOM    936  OE2 GLU B  35       9.479   5.847  13.978  1.00 70.94           O  
ANISOU  936  OE2 GLU B  35     7492  10194   9268   1572  -2270    520       O  
ATOM    937  N   LYS B  36      13.025   7.382   9.584  1.00 63.59           N  
ANISOU  937  N   LYS B  36     5499   9079   9583   1566  -2135  -1248       N  
ATOM    938  CA  LYS B  36      13.567   8.441   8.740  1.00 61.34           C  
ANISOU  938  CA  LYS B  36     4962   8927   9415   1379  -1976  -1692       C  
ATOM    939  C   LYS B  36      14.166   7.814   7.514  1.00 61.78           C  
ANISOU  939  C   LYS B  36     4929   8718   9824   1456  -1878  -1882       C  
ATOM    940  O   LYS B  36      13.840   8.213   6.403  1.00 59.18           O  
ANISOU  940  O   LYS B  36     4625   8272   9587   1222  -1627  -2055       O  
ATOM    941  CB  LYS B  36      14.629   9.236   9.512  1.00 63.60           C  
ANISOU  941  CB  LYS B  36     4911   9663   9590   1468  -2148  -1955       C  
ATOM    942  CG  LYS B  36      15.486  10.240   8.700  1.00 62.90           C  
ANISOU  942  CG  LYS B  36     4498   9693   9706   1302  -1975  -2437       C  
ATOM    943  CD  LYS B  36      16.723  10.689   9.527  1.00 66.38           C  
ANISOU  943  CD  LYS B  36     4538  10574  10109   1450  -2204  -2735       C  
ATOM    944  CE  LYS B  36      17.773  11.434   8.696  1.00 67.22           C  
ANISOU  944  CE  LYS B  36     4274  10757  10509   1316  -2023  -3221       C  
ATOM    945  NZ  LYS B  36      18.288  10.664   7.517  1.00 66.57           N  
ANISOU  945  NZ  LYS B  36     4143  10405  10745   1425  -1908  -3290       N  
ATOM    946  N   ASP B  37      15.015   6.806   7.738  1.00 65.52           N  
ANISOU  946  N   ASP B  37     5300   9111  10483   1805  -2077  -1834       N  
ATOM    947  CA  ASP B  37      15.739   6.116   6.669  1.00 66.73           C  
ANISOU  947  CA  ASP B  37     5318   9026  11010   1932  -1994  -2071       C  
ATOM    948  C   ASP B  37      14.877   5.225   5.813  1.00 65.79           C  
ANISOU  948  C   ASP B  37     5475   8459  11062   1840  -1815  -1968       C  
ATOM    949  O   ASP B  37      15.134   5.112   4.620  1.00 65.68           O  
ANISOU  949  O   ASP B  37     5375   8327  11251   1755  -1622  -2274       O  
ATOM    950  CB  ASP B  37      16.873   5.286   7.249  1.00 71.60           C  
ANISOU  950  CB  ASP B  37     5720   9672  11812   2381  -2276  -2038       C  
ATOM    951  CG  ASP B  37      17.878   6.126   7.919  1.00 73.08           C  
ANISOU  951  CG  ASP B  37     5540  10353  11872   2470  -2461  -2264       C  
ATOM    952  OD1 ASP B  37      18.067   7.251   7.420  1.00 70.71           O  
ANISOU  952  OD1 ASP B  37     5066  10259  11540   2175  -2268  -2614       O  
ATOM    953  OD2 ASP B  37      18.465   5.680   8.930  1.00 77.46           O  
ANISOU  953  OD2 ASP B  37     5973  11096  12360   2827  -2790  -2091       O  
ATOM    954  N   ILE B  38      13.895   4.560   6.412  1.00 65.93           N  
ANISOU  954  N   ILE B  38     5801   8247  11002   1848  -1865  -1571       N  
ATOM    955  CA  ILE B  38      12.957   3.766   5.626  1.00 65.38           C  
ANISOU  955  CA  ILE B  38     5972   7761  11105   1695  -1678  -1524       C  
ATOM    956  C   ILE B  38      12.230   4.736   4.701  1.00 61.21           C  
ANISOU  956  C   ILE B  38     5466   7383  10406   1310  -1447  -1741       C  
ATOM    957  O   ILE B  38      12.131   4.512   3.495  1.00 60.62           O  
ANISOU  957  O   ILE B  38     5376   7182  10474   1187  -1271  -2003       O  
ATOM    958  CB  ILE B  38      11.933   3.033   6.503  1.00 66.54           C  
ANISOU  958  CB  ILE B  38     6436   7658  11189   1700  -1726  -1052       C  
ATOM    959  CG1 ILE B  38      12.610   2.093   7.489  1.00 71.66           C  
ANISOU  959  CG1 ILE B  38     7101   8162  11964   2117  -1958   -724       C  
ATOM    960  CG2 ILE B  38      11.000   2.228   5.649  1.00 66.38           C  
ANISOU  960  CG2 ILE B  38     6607   7213  11400   1504  -1519  -1092       C  
ATOM    961  CD1 ILE B  38      11.803   1.878   8.752  1.00 72.76           C  
ANISOU  961  CD1 ILE B  38     7507   8306  11832   2125  -2038   -192       C  
ATOM    962  N   ALA B  39      11.745   5.822   5.304  1.00 58.88           N  
ANISOU  962  N   ALA B  39     5196   7379   9795   1144  -1455  -1629       N  
ATOM    963  CA  ALA B  39      11.086   6.930   4.607  1.00 55.35           C  
ANISOU  963  CA  ALA B  39     4754   7097   9176    830  -1259  -1763       C  
ATOM    964  C   ALA B  39      11.864   7.433   3.385  1.00 54.83           C  
ANISOU  964  C   ALA B  39     4485   7135   9209    766  -1098  -2132       C  
ATOM    965  O   ALA B  39      11.285   7.626   2.310  1.00 53.69           O  
ANISOU  965  O   ALA B  39     4405   6970   9022    569   -914  -2230       O  
ATOM    966  CB  ALA B  39      10.861   8.081   5.579  1.00 53.89           C  
ANISOU  966  CB  ALA B  39     4543   7209   8724    743  -1305  -1662       C  
ATOM    967  N   ALA B  40      13.160   7.648   3.547  1.00 56.18           N  
ANISOU  967  N   ALA B  40     4398   7455   9490    928  -1160  -2332       N  
ATOM    968  CA  ALA B  40      13.980   8.138   2.447  1.00 56.49           C  
ANISOU  968  CA  ALA B  40     4224   7610   9629    852   -965  -2680       C  
ATOM    969  C   ALA B  40      14.114   7.099   1.333  1.00 58.24           C  
ANISOU  969  C   ALA B  40     4462   7620  10045    903   -860  -2866       C  
ATOM    970  O   ALA B  40      14.003   7.414   0.146  1.00 57.64           O  
ANISOU  970  O   ALA B  40     4378   7614   9909    722   -630  -3053       O  
ATOM    971  CB  ALA B  40      15.340   8.535   2.953  1.00 58.52           C  
ANISOU  971  CB  ALA B  40     4152   8083   9998   1005  -1056  -2889       C  
ATOM    972  N   TYR B  41      14.353   5.857   1.726  1.00 60.79           N  
ANISOU  972  N   TYR B  41     4809   7687  10599   1160  -1018  -2813       N  
ATOM    973  CA  TYR B  41      14.516   4.778   0.772  1.00 63.05           C  
ANISOU  973  CA  TYR B  41     5093   7719  11142   1229   -915  -3045       C  
ATOM    974  C   TYR B  41      13.381   4.746  -0.229  1.00 61.31           C  
ANISOU  974  C   TYR B  41     5072   7451  10773    940   -728  -3095       C  
ATOM    975  O   TYR B  41      13.589   4.572  -1.433  1.00 62.35           O  
ANISOU  975  O   TYR B  41     5128   7626  10935    853   -539  -3427       O  
ATOM    976  CB  TYR B  41      14.590   3.441   1.503  1.00 66.42           C  
ANISOU  976  CB  TYR B  41     5603   7768  11864   1530  -1104  -2861       C  
ATOM    977  CG  TYR B  41      14.833   2.264   0.579  1.00 69.71           C  
ANISOU  977  CG  TYR B  41     5991   7850  12643   1626   -982  -3157       C  
ATOM    978  CD1 TYR B  41      16.113   1.739   0.398  1.00 73.06           C  
ANISOU  978  CD1 TYR B  41     6141   8209  13407   1928  -1004  -3428       C  
ATOM    979  CD2 TYR B  41      13.774   1.667  -0.108  1.00 69.58           C  
ANISOU  979  CD2 TYR B  41     6189   7592  12655   1411   -840  -3215       C  
ATOM    980  CE1 TYR B  41      16.328   0.639  -0.452  1.00 76.57           C  
ANISOU  980  CE1 TYR B  41     6547   8318  14228   2021   -863  -3754       C  
ATOM    981  CE2 TYR B  41      13.979   0.584  -0.953  1.00 72.97           C  
ANISOU  981  CE2 TYR B  41     6577   7709  13437   1474   -709  -3563       C  
ATOM    982  CZ  TYR B  41      15.253   0.081  -1.127  1.00 76.32           C  
ANISOU  982  CZ  TYR B  41     6747   8040  14208   1779   -709  -3834       C  
ATOM    983  OH  TYR B  41      15.415  -0.985  -1.969  1.00 80.12           O  
ANISOU  983  OH  TYR B  41     7182   8194  15067   1834   -551  -4225       O  
ATOM    984  N   ILE B  42      12.176   4.908   0.289  1.00 59.28           N  
ANISOU  984  N   ILE B  42     5045   7147  10332    795   -787  -2784       N  
ATOM    985  CA  ILE B  42      10.971   4.772  -0.517  1.00 58.27           C  
ANISOU  985  CA  ILE B  42     5081   6985  10072    542   -666  -2812       C  
ATOM    986  C   ILE B  42      10.764   6.001  -1.393  1.00 56.02           C  
ANISOU  986  C   ILE B  42     4747   7067   9471    324   -506  -2899       C  
ATOM    987  O   ILE B  42      10.662   5.902  -2.620  1.00 56.97           O  
ANISOU  987  O   ILE B  42     4840   7299   9506    206   -354  -3152       O  
ATOM    988  CB  ILE B  42       9.732   4.558   0.360  1.00 57.11           C  
ANISOU  988  CB  ILE B  42     5157   6684   9857    456   -766  -2456       C  
ATOM    989  CG1 ILE B  42       9.875   3.275   1.191  1.00 60.39           C  
ANISOU  989  CG1 ILE B  42     5665   6689  10589    668   -885  -2293       C  
ATOM    990  CG2 ILE B  42       8.513   4.452  -0.516  1.00 56.53           C  
ANISOU  990  CG2 ILE B  42     5184   6631   9661    192   -657  -2543       C  
ATOM    991  CD1 ILE B  42       9.130   3.304   2.516  1.00 59.87           C  
ANISOU  991  CD1 ILE B  42     5777   6560  10410    666  -1001  -1847       C  
ATOM    992  N   LYS B  43      10.715   7.164  -0.760  1.00 53.60           N  
ANISOU  992  N   LYS B  43     4427   6950   8987    277   -529  -2689       N  
ATOM    993  CA  LYS B  43      10.571   8.406  -1.509  1.00 52.06           C  
ANISOU  993  CA  LYS B  43     4195   7038   8546    100   -355  -2702       C  
ATOM    994  C   LYS B  43      11.485   8.402  -2.724  1.00 53.79           C  
ANISOU  994  C   LYS B  43     4264   7396   8775     89   -161  -3023       C  
ATOM    995  O   LYS B  43      11.081   8.737  -3.831  1.00 53.94           O  
ANISOU  995  O   LYS B  43     4321   7603   8569    -57     -3  -3079       O  
ATOM    996  CB  LYS B  43      10.892   9.610  -0.616  1.00 50.63           C  
ANISOU  996  CB  LYS B  43     3943   6977   8317     96   -369  -2549       C  
ATOM    997  CG  LYS B  43      10.824  10.990  -1.316  1.00 49.59           C  
ANISOU  997  CG  LYS B  43     3777   7051   8013    -73   -147  -2517       C  
ATOM    998  CD  LYS B  43      12.146  11.417  -1.931  1.00 50.65           C  
ANISOU  998  CD  LYS B  43     3701   7304   8237    -76     44  -2763       C  
ATOM    999  CE  LYS B  43      12.212  12.920  -2.112  1.00 50.49           C  
ANISOU  999  CE  LYS B  43     3643   7397   8143   -230    262  -2658       C  
ATOM   1000  NZ  LYS B  43      11.206  13.483  -3.053  1.00 49.74           N  
ANISOU 1000  NZ  LYS B  43     3716   7386   7794   -357    405  -2439       N  
ATOM   1001  N   LYS B  44      12.729   8.019  -2.491  1.00 55.84           N  
ANISOU 1001  N   LYS B  44     4336   7600   9280    259   -175  -3229       N  
ATOM   1002  CA  LYS B  44      13.750   8.077  -3.520  1.00 57.95           C  
ANISOU 1002  CA  LYS B  44     4409   8020   9586    251     40  -3564       C  
ATOM   1003  C   LYS B  44      13.403   7.119  -4.632  1.00 59.76           C  
ANISOU 1003  C   LYS B  44     4700   8222   9783    211    129  -3811       C  
ATOM   1004  O   LYS B  44      13.449   7.481  -5.809  1.00 60.64           O  
ANISOU 1004  O   LYS B  44     4786   8591   9662     67    353  -3968       O  
ATOM   1005  CB  LYS B  44      15.120   7.778  -2.919  1.00 59.87           C  
ANISOU 1005  CB  LYS B  44     4391   8208  10148    474    -28  -3757       C  
ATOM   1006  CG  LYS B  44      15.639   8.918  -2.055  1.00 58.67           C  
ANISOU 1006  CG  LYS B  44     4099   8201   9991    455    -60  -3645       C  
ATOM   1007  CD  LYS B  44      16.805   8.505  -1.164  1.00 61.16           C  
ANISOU 1007  CD  LYS B  44     4147   8493  10598    719   -247  -3791       C  
ATOM   1008  CE  LYS B  44      17.414   9.706  -0.458  1.00 60.73           C  
ANISOU 1008  CE  LYS B  44     3887   8652  10536    648   -243  -3807       C  
ATOM   1009  NZ  LYS B  44      18.592   9.337   0.371  1.00 63.50           N  
ANISOU 1009  NZ  LYS B  44     3916   9075  11136    915   -457  -3991       N  
ATOM   1010  N   GLU B  45      13.022   5.907  -4.253  1.00 60.78           N  
ANISOU 1010  N   GLU B  45     4915   8046  10134    326    -30  -3842       N  
ATOM   1011  CA  GLU B  45      12.768   4.889  -5.248  1.00 63.67           C  
ANISOU 1011  CA  GLU B  45     5300   8338  10550    283     60  -4175       C  
ATOM   1012  C   GLU B  45      11.607   5.292  -6.137  1.00 62.52           C  
ANISOU 1012  C   GLU B  45     5297   8456  10002     27    137  -4140       C  
ATOM   1013  O   GLU B  45      11.670   5.160  -7.358  1.00 64.77           O  
ANISOU 1013  O   GLU B  45     5529   8983  10097    -77    308  -4453       O  
ATOM   1014  CB  GLU B  45      12.527   3.517  -4.615  1.00 65.58           C  
ANISOU 1014  CB  GLU B  45     5618   8115  11182    440    -96  -4192       C  
ATOM   1015  CG  GLU B  45      13.149   2.377  -5.440  1.00 70.92           C  
ANISOU 1015  CG  GLU B  45     6165   8620  12160    535     32  -4691       C  
ATOM   1016  CD  GLU B  45      14.670   2.566  -5.655  1.00 74.47           C  
ANISOU 1016  CD  GLU B  45     6331   9196  12766    720    141  -4951       C  
ATOM   1017  OE1 GLU B  45      15.355   3.096  -4.735  1.00 72.74           O  
ANISOU 1017  OE1 GLU B  45     6009   9000  12628    882     20  -4723       O  
ATOM   1018  OE2 GLU B  45      15.177   2.192  -6.747  1.00 78.94           O  
ANISOU 1018  OE2 GLU B  45     6751   9876  13364    692    356  -5421       O  
ATOM   1019  N   PHE B  46      10.556   5.809  -5.530  1.00 59.67           N  
ANISOU 1019  N   PHE B  46     5092   8094   9484    -62      8  -3768       N  
ATOM   1020  CA  PHE B  46       9.411   6.244  -6.301  1.00 59.07           C  
ANISOU 1020  CA  PHE B  46     5115   8295   9032   -264     39  -3699       C  
ATOM   1021  C   PHE B  46       9.708   7.486  -7.139  1.00 58.89           C  
ANISOU 1021  C   PHE B  46     5047   8684   8641   -345    222  -3624       C  
ATOM   1022  O   PHE B  46       9.149   7.641  -8.221  1.00 60.59           O  
ANISOU 1022  O   PHE B  46     5290   9223   8509   -467    297  -3699       O  
ATOM   1023  CB  PHE B  46       8.209   6.463  -5.392  1.00 56.86           C  
ANISOU 1023  CB  PHE B  46     4978   7897   8728   -320   -132  -3335       C  
ATOM   1024  CG  PHE B  46       7.362   5.217  -5.188  1.00 58.30           C  
ANISOU 1024  CG  PHE B  46     5235   7798   9115   -374   -237  -3444       C  
ATOM   1025  CD1 PHE B  46       6.035   5.185  -5.607  1.00 58.28           C  
ANISOU 1025  CD1 PHE B  46     5282   7946   8913   -558   -282  -3434       C  
ATOM   1026  CD2 PHE B  46       7.896   4.091  -4.573  1.00 59.76           C  
ANISOU 1026  CD2 PHE B  46     5425   7558   9721   -235   -279  -3549       C  
ATOM   1027  CE1 PHE B  46       5.262   4.044  -5.429  1.00 60.17           C  
ANISOU 1027  CE1 PHE B  46     5563   7906   9391   -654   -339  -3576       C  
ATOM   1028  CE2 PHE B  46       7.118   2.954  -4.376  1.00 61.60           C  
ANISOU 1028  CE2 PHE B  46     5741   7461  10203   -308   -324  -3627       C  
ATOM   1029  CZ  PHE B  46       5.804   2.928  -4.813  1.00 61.65           C  
ANISOU 1029  CZ  PHE B  46     5784   7610  10029   -543   -338  -3665       C  
ATOM   1030  N   ASP B  47      10.579   8.367  -6.659  1.00 57.71           N  
ANISOU 1030  N   ASP B  47     4822   8538   8563   -283    302  -3476       N  
ATOM   1031  CA  ASP B  47      11.001   9.503  -7.465  1.00 58.17           C  
ANISOU 1031  CA  ASP B  47     4837   8914   8350   -372    542  -3402       C  
ATOM   1032  C   ASP B  47      11.607   8.998  -8.757  1.00 61.79           C  
ANISOU 1032  C   ASP B  47     5201   9613   8661   -411    746  -3784       C  
ATOM   1033  O   ASP B  47      11.355   9.549  -9.828  1.00 63.41           O  
ANISOU 1033  O   ASP B  47     5449  10180   8463   -522    912  -3731       O  
ATOM   1034  CB  ASP B  47      12.019  10.372  -6.724  1.00 57.29           C  
ANISOU 1034  CB  ASP B  47     4603   8716   8446   -327    630  -3302       C  
ATOM   1035  CG  ASP B  47      11.374  11.503  -5.945  1.00 54.63           C  
ANISOU 1035  CG  ASP B  47     4363   8326   8066   -372    575  -2904       C  
ATOM   1036  OD1 ASP B  47      10.214  11.852  -6.230  1.00 54.74           O  
ANISOU 1036  OD1 ASP B  47     4527   8434   7837   -438    532  -2660       O  
ATOM   1037  OD2 ASP B  47      12.025  12.074  -5.056  1.00 53.72           O  
ANISOU 1037  OD2 ASP B  47     4146   8097   8169   -340    578  -2864       O  
ATOM   1038  N   LYS B  48      12.389   7.928  -8.651  1.00 63.65           N  
ANISOU 1038  N   LYS B  48     5305   9659   9217   -300    735  -4165       N  
ATOM   1039  CA  LYS B  48      13.081   7.356  -9.806  1.00 67.41           C  
ANISOU 1039  CA  LYS B  48     5652  10343   9618   -323    954  -4621       C  
ATOM   1040  C   LYS B  48      12.134   6.695 -10.807  1.00 69.58           C  
ANISOU 1040  C   LYS B  48     6017  10833   9584   -439    937  -4842       C  
ATOM   1041  O   LYS B  48      12.166   7.028 -12.004  1.00 72.14           O  
ANISOU 1041  O   LYS B  48     6329  11604   9475   -556   1141  -4964       O  
ATOM   1042  CB  LYS B  48      14.126   6.326  -9.372  1.00 69.03           C  
ANISOU 1042  CB  LYS B  48     5666  10236  10323   -132    934  -4991       C  
ATOM   1043  CG  LYS B  48      15.043   5.950 -10.520  1.00 73.37           C  
ANISOU 1043  CG  LYS B  48     6028  11025  10825   -151   1224  -5488       C  
ATOM   1044  CD  LYS B  48      16.028   4.840 -10.195  1.00 75.93           C  
ANISOU 1044  CD  LYS B  48     6135  11027  11687     74   1208  -5898       C  
ATOM   1045  CE  LYS B  48      16.625   4.301 -11.485  1.00 80.39           C  
ANISOU 1045  CE  LYS B  48     6534  11845  12164     23   1507  -6473       C  
ATOM   1046  NZ  LYS B  48      18.020   3.895 -11.315  1.00 83.91           N  
ANISOU 1046  NZ  LYS B  48     6666  12154  13059    227   1625  -6820       N  
ATOM   1047  N   LYS B  49      11.319   5.752 -10.312  1.00 69.03           N  
ANISOU 1047  N   LYS B  49     6026  10468   9732   -416    708  -4906       N  
ATOM   1048  CA  LYS B  49      10.446   4.919 -11.155  1.00 71.34           C  
ANISOU 1048  CA  LYS B  49     6351  10906   9846   -542    674  -5239       C  
ATOM   1049  C   LYS B  49       9.286   5.733 -11.717  1.00 70.60           C  
ANISOU 1049  C   LYS B  49     6369  11251   9202   -693    611  -4957       C  
ATOM   1050  O   LYS B  49       8.988   5.656 -12.903  1.00 73.64           O  
ANISOU 1050  O   LYS B  49     6725  12093   9161   -805    693  -5208       O  
ATOM   1051  CB  LYS B  49       9.909   3.724 -10.360  1.00 71.20           C  
ANISOU 1051  CB  LYS B  49     6377  10373  10299   -499    482  -5351       C  
ATOM   1052  N   TYR B  50       8.665   6.545 -10.863  1.00 66.99           N  
ANISOU 1052  N   TYR B  50     6022  10687   8742   -673    465  -4440       N  
ATOM   1053  CA  TYR B  50       7.420   7.225 -11.202  1.00 66.39           C  
ANISOU 1053  CA  TYR B  50     6033  10942   8251   -766    352  -4143       C  
ATOM   1054  C   TYR B  50       7.483   8.751 -11.294  1.00 64.89           C  
ANISOU 1054  C   TYR B  50     5905  10989   7760   -737    450  -3643       C  
ATOM   1055  O   TYR B  50       6.455   9.405 -11.291  1.00 64.26           O  
ANISOU 1055  O   TYR B  50     5893  11073   7448   -752    331  -3305       O  
ATOM   1056  CB  TYR B  50       6.352   6.835 -10.182  1.00 64.20           C  
ANISOU 1056  CB  TYR B  50     5820  10335   8238   -783    109  -3982       C  
ATOM   1057  CG  TYR B  50       6.233   5.344  -9.954  1.00 66.05           C  
ANISOU 1057  CG  TYR B  50     6018  10216   8860   -822     43  -4400       C  
ATOM   1058  CD1 TYR B  50       5.679   4.510 -10.931  1.00 69.53           C  
ANISOU 1058  CD1 TYR B  50     6385  10876   9155   -966     36  -4866       C  
ATOM   1059  CD2 TYR B  50       6.664   4.767  -8.761  1.00 64.52           C  
ANISOU 1059  CD2 TYR B  50     5861   9470   9183   -712     -5  -4329       C  
ATOM   1060  CE1 TYR B  50       5.568   3.140 -10.730  1.00 71.51           C  
ANISOU 1060  CE1 TYR B  50     6600  10726   9841  -1021     18  -5274       C  
ATOM   1061  CE2 TYR B  50       6.548   3.398  -8.544  1.00 66.60           C  
ANISOU 1061  CE2 TYR B  50     6115   9335   9854   -732    -34  -4651       C  
ATOM   1062  CZ  TYR B  50       5.999   2.587  -9.542  1.00 69.98           C  
ANISOU 1062  CZ  TYR B  50     6471   9913  10204   -898     -3  -5136       C  
ATOM   1063  OH  TYR B  50       5.888   1.225  -9.373  1.00 72.54           O  
ANISOU 1063  OH  TYR B  50     6779   9780  11002   -940     11  -5494       O  
ATOM   1064  N   ASN B  51       8.673   9.316 -11.387  1.00 65.33           N  
ANISOU 1064  N   ASN B  51     5918  11043   7860   -697    683  -3607       N  
ATOM   1065  CA  ASN B  51       8.852  10.767 -11.496  1.00 64.79           C  
ANISOU 1065  CA  ASN B  51     5907  11122   7588   -694    845  -3151       C  
ATOM   1066  C   ASN B  51       8.580  11.533 -10.203  1.00 60.94           C  
ANISOU 1066  C   ASN B  51     5473  10278   7401   -638    739  -2760       C  
ATOM   1067  O   ASN B  51       7.691  11.179  -9.438  1.00 58.92           O  
ANISOU 1067  O   ASN B  51     5263   9832   7292   -617    497  -2688       O  
ATOM   1068  CB  ASN B  51       7.986  11.359 -12.617  1.00 67.20           C  
ANISOU 1068  CB  ASN B  51     6293  11932   7306   -734    862  -2916       C  
ATOM   1069  CG  ASN B  51       8.461  10.958 -13.983  1.00 71.33           C  
ANISOU 1069  CG  ASN B  51     6764  12921   7415   -800   1052  -3246       C  
ATOM   1070  OD1 ASN B  51       9.648  10.822 -14.214  1.00 73.22           O  
ANISOU 1070  OD1 ASN B  51     6919  13136   7764   -823   1303  -3488       O  
ATOM   1071  ND2 ASN B  51       7.540  10.787 -14.898  1.00 74.22           N  
ANISOU 1071  ND2 ASN B  51     7154  13761   7285   -832    935  -3279       N  
ATOM   1072  N   PRO B  52       9.341  12.604  -9.970  1.00 60.41           N  
ANISOU 1072  N   PRO B  52     5390  10133   7429   -637    948  -2534       N  
ATOM   1073  CA  PRO B  52       9.116  13.462  -8.809  1.00 57.56           C  
ANISOU 1073  CA  PRO B  52     5062   9476   7331   -604    887  -2215       C  
ATOM   1074  C   PRO B  52       7.814  14.227  -8.916  1.00 57.01           C  
ANISOU 1074  C   PRO B  52     5116   9509   7034   -589    796  -1804       C  
ATOM   1075  O   PRO B  52       7.338  14.427 -10.036  1.00 59.48           O  
ANISOU 1075  O   PRO B  52     5484  10176   6939   -596    848  -1678       O  
ATOM   1076  CB  PRO B  52      10.274  14.448  -8.861  1.00 58.68           C  
ANISOU 1076  CB  PRO B  52     5128   9570   7596   -652   1200  -2145       C  
ATOM   1077  CG  PRO B  52      10.861  14.319 -10.217  1.00 62.33           C  
ANISOU 1077  CG  PRO B  52     5562  10369   7750   -715   1454  -2287       C  
ATOM   1078  CD  PRO B  52      10.474  13.036 -10.797  1.00 63.07           C  
ANISOU 1078  CD  PRO B  52     5654  10659   7650   -693   1289  -2619       C  
ATOM   1079  N   THR B  53       7.264  14.701  -7.794  1.00 54.39           N  
ANISOU 1079  N   THR B  53     4811   8913   6940   -553    672  -1597       N  
ATOM   1080  CA  THR B  53       7.943  14.746  -6.486  1.00 52.13           C  
ANISOU 1080  CA  THR B  53     4455   8292   7060   -541    648  -1698       C  
ATOM   1081  C   THR B  53       7.176  14.016  -5.401  1.00 49.81           C  
ANISOU 1081  C   THR B  53     4187   7818   6919   -501    367  -1736       C  
ATOM   1082  O   THR B  53       6.088  14.470  -5.003  1.00 48.80           O  
ANISOU 1082  O   THR B  53     4119   7668   6755   -492    272  -1496       O  
ATOM   1083  CB  THR B  53       8.077  16.194  -6.003  1.00 51.84           C  
ANISOU 1083  CB  THR B  53     4418   8101   7174   -560    822  -1422       C  
ATOM   1084  OG1 THR B  53       8.500  17.027  -7.095  1.00 55.17           O  
ANISOU 1084  OG1 THR B  53     4863   8672   7426   -607   1122  -1251       O  
ATOM   1085  CG2 THR B  53       9.064  16.276  -4.859  1.00 50.62           C  
ANISOU 1085  CG2 THR B  53     4138   7714   7382   -573    833  -1626       C  
ATOM   1086  N   TRP B  54       7.731  12.903  -4.919  1.00 49.32           N  
ANISOU 1086  N   TRP B  54     4075   7622   7043   -467    253  -2015       N  
ATOM   1087  CA  TRP B  54       7.096  12.117  -3.855  1.00 47.79           C  
ANISOU 1087  CA  TRP B  54     3926   7230   7001   -432     22  -2012       C  
ATOM   1088  C   TRP B  54       7.511  12.570  -2.458  1.00 46.21           C  
ANISOU 1088  C   TRP B  54     3691   6847   7019   -381    -26  -1931       C  
ATOM   1089  O   TRP B  54       8.534  13.190  -2.272  1.00 46.55           O  
ANISOU 1089  O   TRP B  54     3629   6885   7171   -367     88  -2001       O  
ATOM   1090  CB  TRP B  54       7.393  10.626  -4.010  1.00 48.98           C  
ANISOU 1090  CB  TRP B  54     4063   7278   7266   -396    -73  -2302       C  
ATOM   1091  CG  TRP B  54       6.827  10.014  -5.249  1.00 51.23           C  
ANISOU 1091  CG  TRP B  54     4367   7753   7342   -472    -58  -2470       C  
ATOM   1092  CD1 TRP B  54       7.400   9.998  -6.488  1.00 53.72           C  
ANISOU 1092  CD1 TRP B  54     4625   8311   7473   -499     98  -2677       C  
ATOM   1093  CD2 TRP B  54       5.586   9.296  -5.376  1.00 51.93           C  
ANISOU 1093  CD2 TRP B  54     4510   7849   7371   -550   -196  -2499       C  
ATOM   1094  NE1 TRP B  54       6.591   9.333  -7.380  1.00 55.63           N  
ANISOU 1094  NE1 TRP B  54     4885   8746   7507   -580     43  -2848       N  
ATOM   1095  CE2 TRP B  54       5.474   8.889  -6.722  1.00 54.11           C  
ANISOU 1095  CE2 TRP B  54     4746   8401   7413   -619   -141  -2759       C  
ATOM   1096  CE3 TRP B  54       4.552   8.972  -4.486  1.00 51.02           C  
ANISOU 1096  CE3 TRP B  54     4453   7561   7370   -589   -342  -2353       C  
ATOM   1097  CZ2 TRP B  54       4.380   8.185  -7.196  1.00 55.43           C  
ANISOU 1097  CZ2 TRP B  54     4905   8679   7474   -728   -251  -2912       C  
ATOM   1098  CZ3 TRP B  54       3.462   8.258  -4.967  1.00 52.12           C  
ANISOU 1098  CZ3 TRP B  54     4587   7774   7440   -709   -423  -2484       C  
ATOM   1099  CH2 TRP B  54       3.388   7.874  -6.305  1.00 54.44           C  
ANISOU 1099  CH2 TRP B  54     4817   8346   7520   -778   -390  -2779       C  
ATOM   1100  N   HIS B  55       6.682  12.246  -1.477  1.00 45.17           N  
ANISOU 1100  N   HIS B  55     3630   6600   6932   -371   -187  -1809       N  
ATOM   1101  CA  HIS B  55       6.981  12.476  -0.068  1.00 44.30           C  
ANISOU 1101  CA  HIS B  55     3494   6380   6956   -317   -269  -1755       C  
ATOM   1102  C   HIS B  55       6.592  11.209   0.698  1.00 44.69           C  
ANISOU 1102  C   HIS B  55     3627   6278   7073   -264   -453  -1730       C  
ATOM   1103  O   HIS B  55       5.743  10.460   0.229  1.00 45.25           O  
ANISOU 1103  O   HIS B  55     3778   6304   7108   -322   -488  -1719       O  
ATOM   1104  CB  HIS B  55       6.185  13.668   0.445  1.00 43.04           C  
ANISOU 1104  CB  HIS B  55     3354   6254   6744   -378   -212  -1559       C  
ATOM   1105  CG  HIS B  55       6.266  14.868  -0.438  1.00 42.78           C  
ANISOU 1105  CG  HIS B  55     3285   6302   6667   -428     -5  -1491       C  
ATOM   1106  ND1 HIS B  55       7.386  15.650  -0.527  1.00 43.38           N  
ANISOU 1106  ND1 HIS B  55     3254   6367   6859   -445    162  -1593       N  
ATOM   1107  CD2 HIS B  55       5.359  15.423  -1.267  1.00 43.63           C  
ANISOU 1107  CD2 HIS B  55     3445   6498   6635   -456     69  -1304       C  
ATOM   1108  CE1 HIS B  55       7.178  16.630  -1.381  1.00 44.25           C  
ANISOU 1108  CE1 HIS B  55     3384   6512   6918   -493    365  -1439       C  
ATOM   1109  NE2 HIS B  55       5.953  16.516  -1.847  1.00 44.21           N  
ANISOU 1109  NE2 HIS B  55     3478   6581   6737   -476    294  -1242       N  
ATOM   1110  N   CYS B  56       7.210  10.948   1.848  1.00 44.96           N  
ANISOU 1110  N   CYS B  56     3637   6242   7204   -156   -565  -1720       N  
ATOM   1111  CA  CYS B  56       6.920   9.717   2.584  1.00 46.05           C  
ANISOU 1111  CA  CYS B  56     3879   6203   7411    -81   -714  -1620       C  
ATOM   1112  C   CYS B  56       7.160   9.833   4.056  1.00 46.36           C  
ANISOU 1112  C   CYS B  56     3923   6275   7414     14   -836  -1481       C  
ATOM   1113  O   CYS B  56       8.249  10.176   4.475  1.00 47.46           O  
ANISOU 1113  O   CYS B  56     3927   6519   7585    128   -891  -1589       O  
ATOM   1114  CB  CYS B  56       7.764   8.544   2.087  1.00 48.40           C  
ANISOU 1114  CB  CYS B  56     4148   6339   7901     48   -756  -1791       C  
ATOM   1115  SG  CYS B  56       7.498   6.977   3.060  1.00 51.19           S  
ANISOU 1115  SG  CYS B  56     4656   6365   8426    178   -909  -1594       S  
ATOM   1116  N   ILE B  57       6.149   9.482   4.835  1.00 46.44           N  
ANISOU 1116  N   ILE B  57     4072   6227   7344    -37   -877  -1258       N  
ATOM   1117  CA  ILE B  57       6.212   9.533   6.278  1.00 47.47           C  
ANISOU 1117  CA  ILE B  57     4237   6446   7354     40   -983  -1091       C  
ATOM   1118  C   ILE B  57       6.010   8.135   6.797  1.00 49.69           C  
ANISOU 1118  C   ILE B  57     4676   6502   7700    133  -1073   -868       C  
ATOM   1119  O   ILE B  57       5.067   7.467   6.404  1.00 50.14           O  
ANISOU 1119  O   ILE B  57     4852   6360   7840      8   -995   -786       O  
ATOM   1120  CB  ILE B  57       5.098  10.436   6.882  1.00 46.44           C  
ANISOU 1120  CB  ILE B  57     4138   6461   7043   -119   -895   -989       C  
ATOM   1121  CG1 ILE B  57       4.953  11.747   6.090  1.00 44.44           C  
ANISOU 1121  CG1 ILE B  57     3769   6310   6805   -229   -749  -1152       C  
ATOM   1122  CG2 ILE B  57       5.392  10.715   8.350  1.00 47.67           C  
ANISOU 1122  CG2 ILE B  57     4283   6818   7010    -41   -989   -910       C  
ATOM   1123  CD1 ILE B  57       6.272  12.427   5.788  1.00 44.12           C  
ANISOU 1123  CD1 ILE B  57     3564   6354   6844   -160   -734  -1375       C  
ATOM   1124  N   VAL B  58       6.886   7.718   7.696  1.00 51.97           N  
ANISOU 1124  N   VAL B  58     4953   6828   7962    353  -1234   -765       N  
ATOM   1125  CA  VAL B  58       6.879   6.375   8.256  1.00 55.35           C  
ANISOU 1125  CA  VAL B  58     5543   7003   8482    504  -1320   -483       C  
ATOM   1126  C   VAL B  58       6.905   6.444   9.788  1.00 57.70           C  
ANISOU 1126  C   VAL B  58     5909   7525   8487    619  -1445   -191       C  
ATOM   1127  O   VAL B  58       7.797   7.075  10.382  1.00 58.56           O  
ANISOU 1127  O   VAL B  58     5860   7959   8429    762  -1593   -292       O  
ATOM   1128  CB  VAL B  58       8.106   5.570   7.765  1.00 57.65           C  
ANISOU 1128  CB  VAL B  58     5743   7109   9050    762  -1427   -602       C  
ATOM   1129  CG1 VAL B  58       8.043   4.132   8.262  1.00 61.36           C  
ANISOU 1129  CG1 VAL B  58     6399   7214   9699    939  -1486   -274       C  
ATOM   1130  CG2 VAL B  58       8.207   5.619   6.224  1.00 55.82           C  
ANISOU 1130  CG2 VAL B  58     5414   6758   9035    643  -1287   -956       C  
ATOM   1131  N   GLY B  59       5.942   5.789  10.436  1.00 59.19           N  
ANISOU 1131  N   GLY B  59     6317   7573   8599    542  -1376    152       N  
ATOM   1132  CA  GLY B  59       5.857   5.853  11.896  1.00 61.71           C  
ANISOU 1132  CA  GLY B  59     6724   8160   8559    629  -1462    459       C  
ATOM   1133  C   GLY B  59       4.702   5.096  12.518  1.00 63.77           C  
ANISOU 1133  C   GLY B  59     7241   8235   8751    496  -1312    860       C  
ATOM   1134  O   GLY B  59       4.011   4.330  11.853  1.00 63.85           O  
ANISOU 1134  O   GLY B  59     7361   7837   9060    351  -1156    912       O  
ATOM   1135  N   ARG B  60       4.495   5.338  13.807  1.00 65.97           N  
ANISOU 1135  N   ARG B  60     7596   8846   8623    523  -1342   1110       N  
ATOM   1136  CA  ARG B  60       3.534   4.572  14.606  1.00 69.42           C  
ANISOU 1136  CA  ARG B  60     8288   9153   8934    422  -1183   1565       C  
ATOM   1137  C   ARG B  60       2.527   5.433  15.365  1.00 68.56           C  
ANISOU 1137  C   ARG B  60     8176   9422   8450    174  -1018   1549       C  
ATOM   1138  O   ARG B  60       1.419   4.977  15.641  1.00 70.15           O  
ANISOU 1138  O   ARG B  60     8531   9472   8649    -39   -784   1789       O  
ATOM   1139  CB  ARG B  60       4.266   3.640  15.591  1.00 75.03           C  
ANISOU 1139  CB  ARG B  60     9164   9862   9482    758  -1357   2052       C  
ATOM   1140  CG  ARG B  60       5.784   3.781  15.574  1.00 77.18           C  
ANISOU 1140  CG  ARG B  60     9250  10331   9742   1128  -1688   1905       C  
ATOM   1141  CD  ARG B  60       6.423   3.632  16.947  1.00 83.96           C  
ANISOU 1141  CD  ARG B  60    10158  11618  10122   1437  -1925   2272       C  
ATOM   1142  NE  ARG B  60       7.651   4.439  17.032  1.00 84.20           N  
ANISOU 1142  NE  ARG B  60     9876  12114  10001   1651  -2223   1895       N  
ATOM   1143  CZ  ARG B  60       8.846   4.000  17.417  1.00 88.94           C  
ANISOU 1143  CZ  ARG B  60    10376  12867  10548   2065  -2542   2030       C  
ATOM   1144  NH1 ARG B  60       9.041   2.730  17.774  1.00 95.50           N  
ANISOU 1144  NH1 ARG B  60    11422  13391  11472   2370  -2623   2595       N  
ATOM   1145  NH2 ARG B  60       9.867   4.852  17.444  1.00 88.23           N  
ANISOU 1145  NH2 ARG B  60     9946  13231  10346   2182  -2777   1590       N  
ATOM   1146  N   ASN B  61       2.911   6.653  15.729  1.00 66.86           N  
ANISOU 1146  N   ASN B  61     7770   9684   7948    192  -1113   1243       N  
ATOM   1147  CA  ASN B  61       2.011   7.566  16.437  1.00 66.37           C  
ANISOU 1147  CA  ASN B  61     7667   9986   7563    -26   -943   1141       C  
ATOM   1148  C   ASN B  61       2.053   8.949  15.820  1.00 62.23           C  
ANISOU 1148  C   ASN B  61     6884   9618   7141   -137   -918    618       C  
ATOM   1149  O   ASN B  61       2.634   9.873  16.390  1.00 62.61           O  
ANISOU 1149  O   ASN B  61     6778  10062   6945    -75  -1014    365       O  
ATOM   1150  CB  ASN B  61       2.355   7.635  17.924  1.00 70.69           C  
ANISOU 1150  CB  ASN B  61     8276  11030   7552    111  -1048   1354       C  
ATOM   1151  CG  ASN B  61       2.033   6.350  18.653  1.00 75.55           C  
ANISOU 1151  CG  ASN B  61     9190  11500   8013    182   -989   1972       C  
ATOM   1152  OD1 ASN B  61       1.237   6.337  19.583  1.00 78.35           O  
ANISOU 1152  OD1 ASN B  61     9668  12093   8009     42   -805   2201       O  
ATOM   1153  ND2 ASN B  61       2.645   5.261  18.226  1.00 77.28           N  
ANISOU 1153  ND2 ASN B  61     9528  11307   8527    396  -1114   2250       N  
ATOM   1154  N   PHE B  62       1.436   9.076  14.643  1.00 58.99           N  
ANISOU 1154  N   PHE B  62     6421   8892   7100   -298   -783    457       N  
ATOM   1155  CA  PHE B  62       1.300  10.362  13.968  1.00 55.25           C  
ANISOU 1155  CA  PHE B  62     5734   8498   6758   -401   -715     52       C  
ATOM   1156  C   PHE B  62      -0.015  10.480  13.232  1.00 53.50           C  
ANISOU 1156  C   PHE B  62     5494   8085   6749   -622   -507     21       C  
ATOM   1157  O   PHE B  62      -0.718   9.490  13.005  1.00 54.71           O  
ANISOU 1157  O   PHE B  62     5769   7994   7021   -719   -426    240       O  
ATOM   1158  CB  PHE B  62       2.455  10.587  12.996  1.00 53.34           C  
ANISOU 1158  CB  PHE B  62     5369   8143   6754   -263   -864   -177       C  
ATOM   1159  CG  PHE B  62       2.380   9.745  11.762  1.00 51.94           C  
ANISOU 1159  CG  PHE B  62     5252   7576   6906   -270   -857   -122       C  
ATOM   1160  CD1 PHE B  62       1.906  10.273  10.583  1.00 49.58           C  
ANISOU 1160  CD1 PHE B  62     4857   7157   6822   -394   -752   -319       C  
ATOM   1161  CD2 PHE B  62       2.763   8.428  11.781  1.00 54.21           C  
ANISOU 1161  CD2 PHE B  62     5686   7625   7285   -143   -950    120       C  
ATOM   1162  CE1 PHE B  62       1.817   9.496   9.441  1.00 49.00           C  
ANISOU 1162  CE1 PHE B  62     4821   6798   6997   -416   -750   -325       C  
ATOM   1163  CE2 PHE B  62       2.678   7.651  10.638  1.00 53.73           C  
ANISOU 1163  CE2 PHE B  62     5660   7204   7549   -172   -920     89       C  
ATOM   1164  CZ  PHE B  62       2.204   8.191   9.470  1.00 51.13           C  
ANISOU 1164  CZ  PHE B  62     5221   6827   7378   -320   -825   -159       C  
ATOM   1165  N   GLY B  63      -0.327  11.724  12.874  1.00 51.58           N  
ANISOU 1165  N   GLY B  63     5072   7948   6574   -694   -418   -265       N  
ATOM   1166  CA  GLY B  63      -1.493  12.098  12.054  1.00 49.64           C  
ANISOU 1166  CA  GLY B  63     4737   7583   6540   -847   -263   -341       C  
ATOM   1167  C   GLY B  63      -1.049  13.127  11.011  1.00 47.07           C  
ANISOU 1167  C   GLY B  63     4259   7210   6416   -788   -286   -590       C  
ATOM   1168  O   GLY B  63       0.000  13.753  11.157  1.00 46.63           O  
ANISOU 1168  O   GLY B  63     4141   7242   6334   -687   -354   -751       O  
ATOM   1169  N   SER B  64      -1.835  13.292   9.954  1.00 45.82           N  
ANISOU 1169  N   SER B  64     4028   6930   6451   -853   -223   -614       N  
ATOM   1170  CA  SER B  64      -1.456  14.172   8.856  1.00 43.94           C  
ANISOU 1170  CA  SER B  64     3680   6634   6378   -785   -229   -758       C  
ATOM   1171  C   SER B  64      -2.644  14.799   8.171  1.00 43.54           C  
ANISOU 1171  C   SER B  64     3504   6585   6452   -834   -128   -764       C  
ATOM   1172  O   SER B  64      -3.784  14.315   8.287  1.00 44.21           O  
ANISOU 1172  O   SER B  64     3564   6696   6535   -939    -82   -688       O  
ATOM   1173  CB  SER B  64      -0.682  13.386   7.797  1.00 43.59           C  
ANISOU 1173  CB  SER B  64     3700   6441   6420   -726   -352   -744       C  
ATOM   1174  OG  SER B  64      -1.489  12.378   7.179  1.00 43.89           O  
ANISOU 1174  OG  SER B  64     3782   6375   6519   -816   -368   -657       O  
ATOM   1175  N   TYR B  65      -2.364  15.897   7.474  1.00 42.53           N  
ANISOU 1175  N   TYR B  65     3282   6430   6447   -751    -85   -846       N  
ATOM   1176  CA  TYR B  65      -3.266  16.406   6.454  1.00 42.50           C  
ANISOU 1176  CA  TYR B  65     3168   6420   6560   -723    -49   -790       C  
ATOM   1177  C   TYR B  65      -2.442  16.862   5.269  1.00 41.65           C  
ANISOU 1177  C   TYR B  65     3069   6241   6515   -625    -73   -780       C  
ATOM   1178  O   TYR B  65      -1.544  17.663   5.423  1.00 41.40           O  
ANISOU 1178  O   TYR B  65     3032   6142   6557   -577      3   -858       O  
ATOM   1179  CB  TYR B  65      -4.193  17.510   6.963  1.00 43.29           C  
ANISOU 1179  CB  TYR B  65     3119   6563   6767   -700    100   -826       C  
ATOM   1180  CG  TYR B  65      -5.403  17.670   6.057  1.00 44.31           C  
ANISOU 1180  CG  TYR B  65     3108   6743   6982   -657     84   -724       C  
ATOM   1181  CD1 TYR B  65      -6.469  16.770   6.115  1.00 44.44           C  
ANISOU 1181  CD1 TYR B  65     3063   6870   6950   -771     39   -700       C  
ATOM   1182  CD2 TYR B  65      -5.449  18.678   5.098  1.00 44.56           C  
ANISOU 1182  CD2 TYR B  65     3059   6725   7145   -500    109   -640       C  
ATOM   1183  CE1 TYR B  65      -7.531  16.885   5.266  1.00 45.72           C  
ANISOU 1183  CE1 TYR B  65     3049   7142   7180   -727    -12   -650       C  
ATOM   1184  CE2 TYR B  65      -6.522  18.803   4.246  1.00 45.37           C  
ANISOU 1184  CE2 TYR B  65     3015   6938   7282   -417     47   -523       C  
ATOM   1185  CZ  TYR B  65      -7.556  17.904   4.329  1.00 46.40           C  
ANISOU 1185  CZ  TYR B  65     3047   7230   7350   -530    -31   -555       C  
ATOM   1186  OH  TYR B  65      -8.644  18.036   3.492  1.00 48.97           O  
ANISOU 1186  OH  TYR B  65     3171   7730   7706   -443   -123   -483       O  
ATOM   1187  N   VAL B  66      -2.752  16.330   4.092  1.00 41.73           N  
ANISOU 1187  N   VAL B  66     3079   6291   6486   -617   -162   -707       N  
ATOM   1188  CA  VAL B  66      -1.927  16.533   2.914  1.00 41.84           C  
ANISOU 1188  CA  VAL B  66     3124   6290   6482   -545   -176   -689       C  
ATOM   1189  C   VAL B  66      -2.748  16.708   1.646  1.00 42.90           C  
ANISOU 1189  C   VAL B  66     3182   6563   6551   -487   -222   -570       C  
ATOM   1190  O   VAL B  66      -3.936  16.480   1.641  1.00 44.01           O  
ANISOU 1190  O   VAL B  66     3225   6817   6678   -511   -282   -540       O  
ATOM   1191  CB  VAL B  66      -0.982  15.353   2.717  1.00 41.31           C  
ANISOU 1191  CB  VAL B  66     3163   6187   6346   -588   -273   -789       C  
ATOM   1192  CG1 VAL B  66      -0.040  15.277   3.869  1.00 41.31           C  
ANISOU 1192  CG1 VAL B  66     3213   6103   6380   -588   -263   -876       C  
ATOM   1193  CG2 VAL B  66      -1.758  14.083   2.618  1.00 41.87           C  
ANISOU 1193  CG2 VAL B  66     3253   6285   6369   -685   -380   -808       C  
ATOM   1194  N   THR B  67      -2.091  17.125   0.573  1.00 43.40           N  
ANISOU 1194  N   THR B  67     3275   6656   6556   -409   -192   -504       N  
ATOM   1195  CA  THR B  67      -2.724  17.242  -0.730  1.00 45.10           C  
ANISOU 1195  CA  THR B  67     3433   7085   6617   -330   -261   -371       C  
ATOM   1196  C   THR B  67      -1.959  16.413  -1.741  1.00 45.29           C  
ANISOU 1196  C   THR B  67     3530   7224   6452   -374   -320   -478       C  
ATOM   1197  O   THR B  67      -0.757  16.540  -1.846  1.00 44.74           O  
ANISOU 1197  O   THR B  67     3542   7050   6406   -376   -219   -527       O  
ATOM   1198  CB  THR B  67      -2.721  18.685  -1.183  1.00 46.46           C  
ANISOU 1198  CB  THR B  67     3581   7213   6858   -167   -122   -123       C  
ATOM   1199  OG1 THR B  67      -3.636  19.429  -0.373  1.00 47.18           O  
ANISOU 1199  OG1 THR B  67     3565   7213   7148   -103    -70    -56       O  
ATOM   1200  CG2 THR B  67      -3.145  18.772  -2.633  1.00 48.95           C  
ANISOU 1200  CG2 THR B  67     3865   7809   6924    -53   -208     64       C  
ATOM   1201  N   HIS B  68      -2.631  15.547  -2.477  1.00 46.44           N  
ANISOU 1201  N   HIS B  68     3620   7598   6427   -423   -473   -568       N  
ATOM   1202  CA  HIS B  68      -1.909  14.724  -3.436  1.00 47.38           C  
ANISOU 1202  CA  HIS B  68     3792   7836   6372   -475   -508   -743       C  
ATOM   1203  C   HIS B  68      -2.475  14.781  -4.834  1.00 50.24           C  
ANISOU 1203  C   HIS B  68     4075   8589   6423   -420   -603   -701       C  
ATOM   1204  O   HIS B  68      -3.574  15.261  -5.059  1.00 51.59           O  
ANISOU 1204  O   HIS B  68     4125   8961   6517   -338   -696   -544       O  
ATOM   1205  CB  HIS B  68      -1.810  13.276  -2.964  1.00 47.00           C  
ANISOU 1205  CB  HIS B  68     3772   7654   6429   -628   -585  -1024       C  
ATOM   1206  CG  HIS B  68      -3.106  12.540  -2.942  1.00 47.65           C  
ANISOU 1206  CG  HIS B  68     3741   7848   6515   -740   -713  -1129       C  
ATOM   1207  ND1 HIS B  68      -3.646  11.960  -4.066  1.00 50.60           N  
ANISOU 1207  ND1 HIS B  68     4009   8517   6698   -800   -830  -1310       N  
ATOM   1208  CD2 HIS B  68      -3.943  12.237  -1.921  1.00 47.65           C  
ANISOU 1208  CD2 HIS B  68     3695   7718   6689   -833   -726  -1119       C  
ATOM   1209  CE1 HIS B  68      -4.792  11.371  -3.747  1.00 52.20           C  
ANISOU 1209  CE1 HIS B  68     4083   8755   6995   -931   -914  -1420       C  
ATOM   1210  NE2 HIS B  68      -4.995  11.525  -2.451  1.00 50.15           N  
ANISOU 1210  NE2 HIS B  68     3864   8227   6962   -956   -836  -1287       N  
ATOM   1211  N   GLU B  69      -1.671  14.301  -5.772  1.00 51.61           N  
ANISOU 1211  N   GLU B  69     4303   8903   6403   -449   -579   -854       N  
ATOM   1212  CA  GLU B  69      -2.080  14.134  -7.158  1.00 55.18           C  
ANISOU 1212  CA  GLU B  69     4683   9809   6471   -423   -680   -895       C  
ATOM   1213  C   GLU B  69      -3.039  12.978  -7.246  1.00 56.02           C  
ANISOU 1213  C   GLU B  69     4653  10071   6560   -566   -876  -1216       C  
ATOM   1214  O   GLU B  69      -2.924  11.994  -6.489  1.00 54.45           O  
ANISOU 1214  O   GLU B  69     4477   9577   6634   -717   -874  -1467       O  
ATOM   1215  CB  GLU B  69      -0.901  13.771  -8.058  1.00 56.80           C  
ANISOU 1215  CB  GLU B  69     4972  10129   6480   -456   -566  -1070       C  
ATOM   1216  CG  GLU B  69      -0.107  14.935  -8.658  1.00 59.96           C  
ANISOU 1216  CG  GLU B  69     5466  10598   6717   -332   -361   -749       C  
ATOM   1217  CD  GLU B  69       0.612  14.522  -9.955  1.00 66.81           C  
ANISOU 1217  CD  GLU B  69     6357  11815   7210   -368   -283   -929       C  
ATOM   1218  OE1 GLU B  69       0.282  13.435 -10.529  1.00 70.49           O  
ANISOU 1218  OE1 GLU B  69     6743  12549   7491   -466   -428  -1304       O  
ATOM   1219  OE2 GLU B  69       1.496  15.293 -10.415  1.00 69.68           O  
ANISOU 1219  OE2 GLU B  69     6809  12193   7472   -317    -50   -720       O  
ATOM   1220  N   THR B  70      -3.972  13.095  -8.187  1.00 59.09           N  
ANISOU 1220  N   THR B  70     4889  10929   6631   -517  -1040  -1200       N  
ATOM   1221  CA  THR B  70      -4.861  12.002  -8.523  1.00 61.33           C  
ANISOU 1221  CA  THR B  70     4993  11451   6857   -683  -1224  -1586       C  
ATOM   1222  C   THR B  70      -4.064  10.734  -8.879  1.00 61.80           C  
ANISOU 1222  C   THR B  70     5114  11421   6946   -869  -1169  -2051       C  
ATOM   1223  O   THR B  70      -3.087  10.782  -9.639  1.00 62.49           O  
ANISOU 1223  O   THR B  70     5297  11632   6812   -825  -1071  -2106       O  
ATOM   1224  CB  THR B  70      -5.814  12.405  -9.657  1.00 65.67           C  
ANISOU 1224  CB  THR B  70     5343  12636   6971   -569  -1434  -1518       C  
ATOM   1225  OG1 THR B  70      -6.904  13.149  -9.098  1.00 65.90           O  
ANISOU 1225  OG1 THR B  70     5224  12681   7131   -444  -1529  -1234       O  
ATOM   1226  CG2 THR B  70      -6.403  11.177 -10.364  1.00 69.54           C  
ANISOU 1226  CG2 THR B  70     5633  13481   7307   -779  -1608  -2059       C  
ATOM   1227  N   LYS B  71      -4.500   9.622  -8.285  1.00 61.62           N  
ANISOU 1227  N   LYS B  71     5027  11146   7236  -1076  -1201  -2372       N  
ATOM   1228  CA  LYS B  71      -3.913   8.294  -8.462  1.00 62.67           C  
ANISOU 1228  CA  LYS B  71     5199  11077   7536  -1255  -1139  -2836       C  
ATOM   1229  C   LYS B  71      -2.465   8.178  -7.994  1.00 60.35           C  
ANISOU 1229  C   LYS B  71     5120  10362   7448  -1187   -955  -2787       C  
ATOM   1230  O   LYS B  71      -1.696   7.393  -8.563  1.00 61.90           O  
ANISOU 1230  O   LYS B  71     5342  10522   7654  -1241   -886  -3136       O  
ATOM   1231  CB  LYS B  71      -4.049   7.838  -9.914  1.00 67.03           C  
ANISOU 1231  CB  LYS B  71     5610  12158   7700  -1325  -1234  -3237       C  
ATOM   1232  CG  LYS B  71      -5.474   7.599 -10.330  1.00 70.14           C  
ANISOU 1232  CG  LYS B  71     5729  12964   7956  -1443  -1447  -3444       C  
ATOM   1233  CD  LYS B  71      -6.158   6.596  -9.403  1.00 70.26           C  
ANISOU 1233  CD  LYS B  71     5666  12548   8479  -1691  -1425  -3687       C  
ATOM   1234  CE  LYS B  71      -7.537   6.178  -9.876  1.00 74.60           C  
ANISOU 1234  CE  LYS B  71     5883  13509   8950  -1875  -1615  -4030       C  
ATOM   1235  NZ  LYS B  71      -8.321   7.288 -10.531  1.00 76.79           N  
ANISOU 1235  NZ  LYS B  71     5968  14455   8753  -1670  -1840  -3766       N  
ATOM   1236  N   HIS B  72      -2.114   8.930  -6.946  1.00 56.86           N  
ANISOU 1236  N   HIS B  72     4798   9620   7184  -1069   -879  -2402       N  
ATOM   1237  CA  HIS B  72      -0.762   8.914  -6.392  1.00 54.83           C  
ANISOU 1237  CA  HIS B  72     4696   9009   7125   -989   -736  -2349       C  
ATOM   1238  C   HIS B  72      -0.785   9.083  -4.878  1.00 52.12           C  
ANISOU 1238  C   HIS B  72     4437   8272   7093   -963   -711  -2098       C  
ATOM   1239  O   HIS B  72      -0.174   9.996  -4.336  1.00 50.14           O  
ANISOU 1239  O   HIS B  72     4254   7934   6862   -841   -638  -1845       O  
ATOM   1240  CB  HIS B  72       0.087  10.027  -7.009  1.00 54.53           C  
ANISOU 1240  CB  HIS B  72     4704   9183   6829   -839   -631  -2148       C  
ATOM   1241  CG  HIS B  72       0.291   9.899  -8.489  1.00 57.79           C  
ANISOU 1241  CG  HIS B  72     5063  10029   6864   -851   -616  -2362       C  
ATOM   1242  ND1 HIS B  72      -0.638  10.331  -9.415  1.00 60.32           N  
ANISOU 1242  ND1 HIS B  72     5284  10844   6788   -834   -732  -2289       N  
ATOM   1243  CD2 HIS B  72       1.334   9.410  -9.202  1.00 59.37           C  
ANISOU 1243  CD2 HIS B  72     5280  10286   6989   -865   -497  -2650       C  
ATOM   1244  CE1 HIS B  72      -0.173  10.114 -10.632  1.00 63.56           C  
ANISOU 1244  CE1 HIS B  72     5673  11626   6848   -847   -684  -2512       C  
ATOM   1245  NE2 HIS B  72       1.023   9.556 -10.532  1.00 62.70           N  
ANISOU 1245  NE2 HIS B  72     5632  11250   6938   -878   -523  -2752       N  
ATOM   1246  N   PHE B  73      -1.482   8.197  -4.186  1.00 52.57           N  
ANISOU 1246  N   PHE B  73     4484   8100   7388  -1095   -751  -2183       N  
ATOM   1247  CA  PHE B  73      -1.530   8.261  -2.731  1.00 50.53           C  
ANISOU 1247  CA  PHE B  73     4316   7519   7362  -1081   -716  -1941       C  
ATOM   1248  C   PHE B  73      -1.788   6.920  -2.102  1.00 52.01           C  
ANISOU 1248  C   PHE B  73     4555   7355   7851  -1221   -699  -2065       C  
ATOM   1249  O   PHE B  73      -2.728   6.220  -2.500  1.00 54.51           O  
ANISOU 1249  O   PHE B  73     4770   7710   8228  -1404   -724  -2273       O  
ATOM   1250  CB  PHE B  73      -2.669   9.166  -2.306  1.00 50.02           C  
ANISOU 1250  CB  PHE B  73     4165   7626   7214  -1089   -746  -1707       C  
ATOM   1251  CG  PHE B  73      -2.913   9.175  -0.821  1.00 48.58           C  
ANISOU 1251  CG  PHE B  73     4053   7185   7217  -1113   -692  -1506       C  
ATOM   1252  CD1 PHE B  73      -2.326  10.143  -0.024  1.00 46.33           C  
ANISOU 1252  CD1 PHE B  73     3837   6850   6916   -977   -637  -1286       C  
ATOM   1253  CD2 PHE B  73      -3.717   8.209  -0.229  1.00 49.90           C  
ANISOU 1253  CD2 PHE B  73     4213   7176   7569  -1290   -673  -1556       C  
ATOM   1254  CE1 PHE B  73      -2.529  10.151   1.334  1.00 46.00           C  
ANISOU 1254  CE1 PHE B  73     3854   6647   6973  -1000   -589  -1134       C  
ATOM   1255  CE2 PHE B  73      -3.946   8.217   1.127  1.00 49.35           C  
ANISOU 1255  CE2 PHE B  73     4222   6922   7606  -1316   -598  -1344       C  
ATOM   1256  CZ  PHE B  73      -3.357   9.179   1.913  1.00 47.71           C  
ANISOU 1256  CZ  PHE B  73     4083   6725   7316  -1164   -568  -1138       C  
ATOM   1257  N   ILE B  74      -1.006   6.577  -1.085  1.00 51.20           N  
ANISOU 1257  N   ILE B  74     4595   6913   7943  -1137   -654  -1923       N  
ATOM   1258  CA  ILE B  74      -1.241   5.325  -0.344  1.00 52.96           C  
ANISOU 1258  CA  ILE B  74     4908   6741   8473  -1241   -610  -1927       C  
ATOM   1259  C   ILE B  74      -0.921   5.447   1.132  1.00 51.70           C  
ANISOU 1259  C   ILE B  74     4889   6373   8379  -1141   -587  -1578       C  
ATOM   1260  O   ILE B  74       0.014   6.132   1.536  1.00 49.97           O  
ANISOU 1260  O   ILE B  74     4710   6217   8059   -955   -619  -1449       O  
ATOM   1261  CB  ILE B  74      -0.478   4.115  -0.961  1.00 55.32           C  
ANISOU 1261  CB  ILE B  74     5241   6766   9011  -1232   -581  -2230       C  
ATOM   1262  CG1 ILE B  74      -0.971   2.814  -0.355  1.00 58.15           C  
ANISOU 1262  CG1 ILE B  74     5681   6673   9738  -1377   -500  -2230       C  
ATOM   1263  CG2 ILE B  74       0.993   4.229  -0.767  1.00 54.63           C  
ANISOU 1263  CG2 ILE B  74     5226   6571   8957   -988   -592  -2178       C  
ATOM   1264  CD1 ILE B  74      -0.443   1.612  -1.068  1.00 61.65           C  
ANISOU 1264  CD1 ILE B  74     6126   6813  10486  -1398   -445  -2594       C  
ATOM   1265  N   TYR B  75      -1.732   4.784   1.934  1.00 53.14           N  
ANISOU 1265  N   TYR B  75     5132   6342   8717  -1284   -520  -1442       N  
ATOM   1266  CA  TYR B  75      -1.557   4.804   3.367  1.00 53.10           C  
ANISOU 1266  CA  TYR B  75     5270   6194   8710  -1208   -488  -1092       C  
ATOM   1267  C   TYR B  75      -1.795   3.393   3.851  1.00 56.64           C  
ANISOU 1267  C   TYR B  75     5852   6203   9465  -1312   -389  -1005       C  
ATOM   1268  O   TYR B  75      -2.915   2.899   3.761  1.00 58.47           O  
ANISOU 1268  O   TYR B  75     6033   6351   9832  -1566   -282  -1071       O  
ATOM   1269  CB  TYR B  75      -2.535   5.784   4.029  1.00 51.61           C  
ANISOU 1269  CB  TYR B  75     5014   6273   8320  -1293   -447   -924       C  
ATOM   1270  CG  TYR B  75      -2.481   5.749   5.531  1.00 51.78           C  
ANISOU 1270  CG  TYR B  75     5179   6213   8281  -1251   -390   -595       C  
ATOM   1271  CD1 TYR B  75      -1.376   6.216   6.207  1.00 51.18           C  
ANISOU 1271  CD1 TYR B  75     5180   6202   8062  -1024   -471   -461       C  
ATOM   1272  CD2 TYR B  75      -3.515   5.225   6.271  1.00 54.35           C  
ANISOU 1272  CD2 TYR B  75     5547   6432   8671  -1448   -248   -434       C  
ATOM   1273  CE1 TYR B  75      -1.295   6.178   7.587  1.00 52.25           C  
ANISOU 1273  CE1 TYR B  75     5438   6349   8064   -972   -444   -172       C  
ATOM   1274  CE2 TYR B  75      -3.445   5.181   7.655  1.00 55.89           C  
ANISOU 1274  CE2 TYR B  75     5889   6608   8737  -1406   -181   -107       C  
ATOM   1275  CZ  TYR B  75      -2.323   5.663   8.307  1.00 54.52           C  
ANISOU 1275  CZ  TYR B  75     5797   6550   8365  -1155   -297     22       C  
ATOM   1276  OH  TYR B  75      -2.235   5.633   9.678  1.00 56.61           O  
ANISOU 1276  OH  TYR B  75     6197   6886   8425  -1100   -256    329       O  
ATOM   1277  N   PHE B  76      -0.740   2.756   4.363  1.00 58.09           N  
ANISOU 1277  N   PHE B  76     6187   6099   9783  -1109   -417   -852       N  
ATOM   1278  CA  PHE B  76      -0.785   1.347   4.710  1.00 62.17           C  
ANISOU 1278  CA  PHE B  76     6852   6105  10661  -1153   -311   -740       C  
ATOM   1279  C   PHE B  76       0.163   0.982   5.833  1.00 63.84           C  
ANISOU 1279  C   PHE B  76     7253   6115  10888   -874   -363   -345       C  
ATOM   1280  O   PHE B  76       1.149   1.661   6.053  1.00 62.07           O  
ANISOU 1280  O   PHE B  76     6999   6127  10455   -623   -516   -303       O  
ATOM   1281  CB  PHE B  76      -0.445   0.515   3.489  1.00 64.05           C  
ANISOU 1281  CB  PHE B  76     7022   6098  11215  -1184   -294  -1153       C  
ATOM   1282  CG  PHE B  76       0.975   0.663   3.029  1.00 63.22           C  
ANISOU 1282  CG  PHE B  76     6887   6033  11100   -888   -418  -1293       C  
ATOM   1283  CD1 PHE B  76       1.918  -0.334   3.309  1.00 66.71           C  
ANISOU 1283  CD1 PHE B  76     7438   6035  11872   -664   -418  -1211       C  
ATOM   1284  CD2 PHE B  76       1.371   1.766   2.285  1.00 59.60           C  
ANISOU 1284  CD2 PHE B  76     6278   6027  10340   -828   -513  -1504       C  
ATOM   1285  CE1 PHE B  76       3.251  -0.232   2.855  1.00 66.06           C  
ANISOU 1285  CE1 PHE B  76     7277   6003  11820   -386   -521  -1389       C  
ATOM   1286  CE2 PHE B  76       2.695   1.882   1.832  1.00 59.97           C  
ANISOU 1286  CE2 PHE B  76     6269   6113  10400   -589   -585  -1663       C  
ATOM   1287  CZ  PHE B  76       3.642   0.868   2.121  1.00 62.66           C  
ANISOU 1287  CZ  PHE B  76     6682   6047  11076   -368   -594  -1631       C  
ATOM   1288  N   TYR B  77      -0.154  -0.107   6.531  1.00 68.01           N  
ANISOU 1288  N   TYR B  77     7961   6207  11670   -923   -229    -52       N  
ATOM   1289  CA  TYR B  77       0.658  -0.610   7.631  1.00 70.73           C  
ANISOU 1289  CA  TYR B  77     8506   6343  12025   -632   -283    402       C  
ATOM   1290  C   TYR B  77       1.463  -1.805   7.163  1.00 74.50           C  
ANISOU 1290  C   TYR B  77     9044   6282  12979   -448   -278    330       C  
ATOM   1291  O   TYR B  77       0.925  -2.724   6.522  1.00 77.18           O  
ANISOU 1291  O   TYR B  77     9392   6190  13742   -660   -100    120       O  
ATOM   1292  CB  TYR B  77      -0.212  -1.060   8.818  1.00 74.04           C  
ANISOU 1292  CB  TYR B  77     9124   6606  12399   -778   -101    886       C  
ATOM   1293  CG  TYR B  77      -0.818   0.057   9.633  1.00 71.62           C  
ANISOU 1293  CG  TYR B  77     8785   6828  11599   -875   -101   1041       C  
ATOM   1294  CD1 TYR B  77      -1.882   0.797   9.131  1.00 68.87           C  
ANISOU 1294  CD1 TYR B  77     8253   6761  11151  -1175    -17    745       C  
ATOM   1295  CD2 TYR B  77      -0.335   0.367  10.916  1.00 72.67           C  
ANISOU 1295  CD2 TYR B  77     9048   7201  11360   -653   -190   1462       C  
ATOM   1296  CE1 TYR B  77      -2.449   1.842   9.869  1.00 67.21           C  
ANISOU 1296  CE1 TYR B  77     7990   7005  10542  -1249      6    847       C  
ATOM   1297  CE2 TYR B  77      -0.892   1.409  11.672  1.00 70.82           C  
ANISOU 1297  CE2 TYR B  77     8764   7463  10677   -755   -165   1530       C  
ATOM   1298  CZ  TYR B  77      -1.953   2.146  11.139  1.00 68.42           C  
ANISOU 1298  CZ  TYR B  77     8278   7375  10344  -1053    -51   1214       C  
ATOM   1299  OH  TYR B  77      -2.534   3.190  11.843  1.00 67.31           O  
ANISOU 1299  OH  TYR B  77     8061   7686   9825  -1144     -1   1234       O  
ATOM   1300  N   LEU B  78       2.754  -1.786   7.495  1.00 75.09           N  
ANISOU 1300  N   LEU B  78     9131   6387  13010    -53   -469    466       N  
ATOM   1301  CA  LEU B  78       3.616  -2.951   7.370  1.00 79.41           C  
ANISOU 1301  CA  LEU B  78     9752   6399  14020    219   -478    523       C  
ATOM   1302  C   LEU B  78       3.980  -3.324   8.799  1.00 83.14           C  
ANISOU 1302  C   LEU B  78    10439   6771  14378    508   -551   1190       C  
ATOM   1303  O   LEU B  78       4.790  -2.661   9.435  1.00 82.21           O  
ANISOU 1303  O   LEU B  78    10269   7070  13895    793   -785   1355       O  
ATOM   1304  CB  LEU B  78       4.850  -2.612   6.552  1.00 77.65           C  
ANISOU 1304  CB  LEU B  78     9317   6351  13835    474   -652    122       C  
ATOM   1305  CG  LEU B  78       5.235  -3.659   5.508  1.00 80.96           C  
ANISOU 1305  CG  LEU B  78     9678   6262  14820    513   -546   -264       C  
ATOM   1306  CD1 LEU B  78       4.731  -3.252   4.135  1.00 77.71           C  
ANISOU 1306  CD1 LEU B  78     9082   6071  14374    187   -454   -884       C  
ATOM   1307  CD2 LEU B  78       6.750  -3.837   5.478  1.00 83.21           C  
ANISOU 1307  CD2 LEU B  78     9851   6508  15255    971   -724   -310       C  
ATOM   1308  N   GLY B  79       3.338  -4.363   9.318  1.00 87.98           N  
ANISOU 1308  N   GLY B  79    11286   6859  15281    413   -338   1575       N  
ATOM   1309  CA  GLY B  79       3.385  -4.654  10.752  1.00 91.93           C  
ANISOU 1309  CA  GLY B  79    12033   7335  15560    615   -357   2299       C  
ATOM   1310  C   GLY B  79       2.637  -3.598  11.555  1.00 88.92           C  
ANISOU 1310  C   GLY B  79    11663   7570  14549    405   -354   2468       C  
ATOM   1311  O   GLY B  79       1.598  -3.091  11.118  1.00 85.72           O  
ANISOU 1311  O   GLY B  79    11165   7331  14074      0   -196   2167       O  
ATOM   1312  N   GLN B  80       3.169  -3.256  12.727  1.00 90.41           N  
ANISOU 1312  N   GLN B  80    11940   8133  14276    694   -538   2918       N  
ATOM   1313  CA  GLN B  80       2.570  -2.225  13.586  1.00 88.17           C  
ANISOU 1313  CA  GLN B  80    11654   8477  13369    529   -537   3041       C  
ATOM   1314  C   GLN B  80       3.062  -0.811  13.229  1.00 82.33           C  
ANISOU 1314  C   GLN B  80    10626   8374  12280    559   -767   2549       C  
ATOM   1315  O   GLN B  80       2.905   0.125  14.020  1.00 81.08           O  
ANISOU 1315  O   GLN B  80    10430   8772  11602    528   -829   2609       O  
ATOM   1316  CB  GLN B  80       2.864  -2.528  15.060  1.00 93.25           C  
ANISOU 1316  CB  GLN B  80    12528   9284  13619    803   -611   3739       C  
ATOM   1317  N   VAL B  81       3.647  -0.662  12.036  1.00 79.42           N  
ANISOU 1317  N   VAL B  81    10055   7909  12210    604   -859   2052       N  
ATOM   1318  CA  VAL B  81       4.217   0.615  11.565  1.00 74.22           C  
ANISOU 1318  CA  VAL B  81     9128   7761  11310    634  -1035   1596       C  
ATOM   1319  C   VAL B  81       3.451   1.134  10.354  1.00 69.83           C  
ANISOU 1319  C   VAL B  81     8428   7206  10896    287   -885   1114       C  
ATOM   1320  O   VAL B  81       3.313   0.436   9.346  1.00 70.32           O  
ANISOU 1320  O   VAL B  81     8475   6877  11367    195   -785    886       O  
ATOM   1321  CB  VAL B  81       5.716   0.469  11.189  1.00 74.98           C  
ANISOU 1321  CB  VAL B  81     9072   7841  11574   1017  -1278   1430       C  
ATOM   1322  CG1 VAL B  81       6.127   1.505  10.158  1.00 69.90           C  
ANISOU 1322  CG1 VAL B  81     8155   7490  10913    929  -1326    860       C  
ATOM   1323  CG2 VAL B  81       6.599   0.564  12.437  1.00 77.98           C  
ANISOU 1323  CG2 VAL B  81     9466   8552  11610   1386  -1534   1790       C  
ATOM   1324  N   ALA B  82       2.968   2.367  10.474  1.00 66.07           N  
ANISOU 1324  N   ALA B  82     7837   7191  10075    115   -874    955       N  
ATOM   1325  CA  ALA B  82       2.190   3.026   9.440  1.00 62.21           C  
ANISOU 1325  CA  ALA B  82     7202   6795   9639   -169   -760    571       C  
ATOM   1326  C   ALA B  82       3.102   3.726   8.428  1.00 59.27           C  
ANISOU 1326  C   ALA B  82     6624   6591   9302    -60   -881    167       C  
ATOM   1327  O   ALA B  82       4.166   4.223   8.791  1.00 59.09           O  
ANISOU 1327  O   ALA B  82     6519   6794   9138    168  -1041    146       O  
ATOM   1328  CB  ALA B  82       1.250   4.018  10.076  1.00 60.44           C  
ANISOU 1328  CB  ALA B  82     6945   6940   9077   -365   -673    621       C  
ATOM   1329  N   ILE B  83       2.668   3.754   7.165  1.00 57.66           N  
ANISOU 1329  N   ILE B  83     6325   6309   9272   -238   -795   -155       N  
ATOM   1330  CA  ILE B  83       3.452   4.288   6.043  1.00 55.48           C  
ANISOU 1330  CA  ILE B  83     5877   6168   9034   -169   -852   -521       C  
ATOM   1331  C   ILE B  83       2.587   5.136   5.112  1.00 52.82           C  
ANISOU 1331  C   ILE B  83     5425   6058   8585   -401   -765   -752       C  
ATOM   1332  O   ILE B  83       1.685   4.627   4.437  1.00 53.27           O  
ANISOU 1332  O   ILE B  83     5481   5992   8766   -598   -677   -868       O  
ATOM   1333  CB  ILE B  83       4.064   3.152   5.194  1.00 57.82           C  
ANISOU 1333  CB  ILE B  83     6173   6106   9689    -75   -846   -713       C  
ATOM   1334  CG1 ILE B  83       5.046   2.319   6.025  1.00 61.17           C  
ANISOU 1334  CG1 ILE B  83     6684   6284  10272    232   -955   -469       C  
ATOM   1335  CG2 ILE B  83       4.741   3.717   3.942  1.00 55.62           C  
ANISOU 1335  CG2 ILE B  83     5713   6020   9400    -55   -852  -1111       C  
ATOM   1336  CD1 ILE B  83       5.159   0.896   5.567  1.00 64.73           C  
ANISOU 1336  CD1 ILE B  83     7214   6209  11171    284   -883   -524       C  
ATOM   1337  N   LEU B  84       2.886   6.432   5.065  1.00 50.30           N  
ANISOU 1337  N   LEU B  84     4991   6070   8049   -369   -792   -824       N  
ATOM   1338  CA  LEU B  84       2.214   7.356   4.149  1.00 47.96           C  
ANISOU 1338  CA  LEU B  84     4583   5995   7644   -518   -723   -985       C  
ATOM   1339  C   LEU B  84       3.161   7.692   3.004  1.00 47.04           C  
ANISOU 1339  C   LEU B  84     4360   5966   7545   -437   -727  -1237       C  
ATOM   1340  O   LEU B  84       4.323   7.986   3.224  1.00 46.93           O  
ANISOU 1340  O   LEU B  84     4297   5993   7540   -281   -769  -1280       O  
ATOM   1341  CB  LEU B  84       1.815   8.627   4.901  1.00 46.26           C  
ANISOU 1341  CB  LEU B  84     4323   6029   7222   -543   -696   -866       C  
ATOM   1342  CG  LEU B  84       1.296   9.808   4.087  1.00 44.45           C  
ANISOU 1342  CG  LEU B  84     3973   6014   6900   -617   -628   -964       C  
ATOM   1343  CD1 LEU B  84       0.051   9.386   3.301  1.00 44.73           C  
ANISOU 1343  CD1 LEU B  84     3979   6053   6961   -777   -598  -1007       C  
ATOM   1344  CD2 LEU B  84       1.004  11.008   4.999  1.00 43.37           C  
ANISOU 1344  CD2 LEU B  84     3791   6042   6644   -617   -577   -871       C  
ATOM   1345  N   LEU B  85       2.657   7.627   1.787  1.00 46.99           N  
ANISOU 1345  N   LEU B  85     4300   6027   7525   -552   -677  -1415       N  
ATOM   1346  CA  LEU B  85       3.456   7.877   0.607  1.00 47.17           C  
ANISOU 1346  CA  LEU B  85     4235   6173   7513   -502   -643  -1647       C  
ATOM   1347  C   LEU B  85       2.558   8.486  -0.425  1.00 46.51           C  
ANISOU 1347  C   LEU B  85     4088   6346   7237   -629   -599  -1701       C  
ATOM   1348  O   LEU B  85       1.470   7.996  -0.651  1.00 47.33           O  
ANISOU 1348  O   LEU B  85     4187   6453   7340   -763   -621  -1732       O  
ATOM   1349  CB  LEU B  85       4.015   6.551   0.074  1.00 50.00           C  
ANISOU 1349  CB  LEU B  85     4606   6301   8088   -462   -648  -1880       C  
ATOM   1350  CG  LEU B  85       4.742   6.503  -1.275  1.00 50.91           C  
ANISOU 1350  CG  LEU B  85     4624   6550   8170   -443   -579  -2200       C  
ATOM   1351  CD1 LEU B  85       5.960   7.423  -1.248  1.00 49.54           C  
ANISOU 1351  CD1 LEU B  85     4365   6525   7933   -309   -538  -2197       C  
ATOM   1352  CD2 LEU B  85       5.138   5.073  -1.624  1.00 53.31           C  
ANISOU 1352  CD2 LEU B  85     4935   6559   8759   -408   -568  -2464       C  
ATOM   1353  N   PHE B  86       3.008   9.553  -1.059  1.00 45.82           N  
ANISOU 1353  N   PHE B  86     3936   6481   6991   -584   -535  -1701       N  
ATOM   1354  CA  PHE B  86       2.175  10.257  -2.022  1.00 46.19           C  
ANISOU 1354  CA  PHE B  86     3928   6805   6814   -649   -507  -1664       C  
ATOM   1355  C   PHE B  86       2.917  11.293  -2.823  1.00 46.05           C  
ANISOU 1355  C   PHE B  86     3871   6978   6645   -584   -391  -1636       C  
ATOM   1356  O   PHE B  86       3.975  11.718  -2.440  1.00 45.63           O  
ANISOU 1356  O   PHE B  86     3811   6838   6689   -516   -315  -1635       O  
ATOM   1357  CB  PHE B  86       1.052  10.978  -1.304  1.00 45.02           C  
ANISOU 1357  CB  PHE B  86     3769   6699   6637   -682   -531  -1428       C  
ATOM   1358  CG  PHE B  86       1.499  12.181  -0.578  1.00 43.32           C  
ANISOU 1358  CG  PHE B  86     3553   6459   6445   -600   -455  -1257       C  
ATOM   1359  CD1 PHE B  86       1.480  13.414  -1.188  1.00 43.53           C  
ANISOU 1359  CD1 PHE B  86     3536   6634   6369   -553   -359  -1136       C  
ATOM   1360  CD2 PHE B  86       1.944  12.088   0.724  1.00 43.29           C  
ANISOU 1360  CD2 PHE B  86     3590   6288   6571   -570   -470  -1221       C  
ATOM   1361  CE1 PHE B  86       1.896  14.556  -0.502  1.00 42.92           C  
ANISOU 1361  CE1 PHE B  86     3443   6476   6386   -504   -251  -1028       C  
ATOM   1362  CE2 PHE B  86       2.361  13.235   1.428  1.00 42.39           C  
ANISOU 1362  CE2 PHE B  86     3442   6178   6484   -521   -395  -1146       C  
ATOM   1363  CZ  PHE B  86       2.339  14.465   0.806  1.00 41.85           C  
ANISOU 1363  CZ  PHE B  86     3319   6197   6382   -502   -272  -1076       C  
ATOM   1364  N   LYS B  87       2.308  11.741  -3.905  1.00 47.24           N  
ANISOU 1364  N   LYS B  87     3987   7408   6551   -607   -374  -1592       N  
ATOM   1365  CA  LYS B  87       2.942  12.676  -4.807  1.00 48.26           C  
ANISOU 1365  CA  LYS B  87     4106   7729   6501   -554   -227  -1508       C  
ATOM   1366  C   LYS B  87       2.305  14.067  -4.746  1.00 48.14           C  
ANISOU 1366  C   LYS B  87     4089   7790   6412   -496   -171  -1161       C  
ATOM   1367  O   LYS B  87       1.077  14.205  -4.804  1.00 48.75           O  
ANISOU 1367  O   LYS B  87     4132   7991   6398   -488   -282  -1033       O  
ATOM   1368  CB  LYS B  87       2.836  12.138  -6.219  1.00 50.73           C  
ANISOU 1368  CB  LYS B  87     4390   8355   6529   -593   -234  -1694       C  
ATOM   1369  CG  LYS B  87       3.567  12.967  -7.227  1.00 52.58           C  
ANISOU 1369  CG  LYS B  87     4633   8818   6527   -551    -46  -1596       C  
ATOM   1370  CD  LYS B  87       3.710  12.197  -8.516  1.00 55.42           C  
ANISOU 1370  CD  LYS B  87     4959   9505   6592   -602    -38  -1886       C  
ATOM   1371  CE  LYS B  87       4.360  13.023  -9.580  1.00 57.74           C  
ANISOU 1371  CE  LYS B  87     5275  10087   6574   -571    177  -1745       C  
ATOM   1372  NZ  LYS B  87       5.160  12.146 -10.468  1.00 60.88           N  
ANISOU 1372  NZ  LYS B  87     5627  10673   6829   -633    275  -2156       N  
ATOM   1373  N   SER B  88       3.143  15.088  -4.627  1.00 47.91           N  
ANISOU 1373  N   SER B  88     4073   7663   6466   -454     13  -1031       N  
ATOM   1374  CA  SER B  88       2.714  16.477  -4.781  1.00 49.01           C  
ANISOU 1374  CA  SER B  88     4220   7818   6582   -385    131   -696       C  
ATOM   1375  C   SER B  88       3.951  17.362  -5.040  1.00 50.94           C  
ANISOU 1375  C   SER B  88     4477   7961   6916   -393    404   -639       C  
ATOM   1376  O   SER B  88       4.879  17.398  -4.200  1.00 49.63           O  
ANISOU 1376  O   SER B  88     4270   7580   7006   -441    473   -814       O  
ATOM   1377  CB  SER B  88       2.021  16.948  -3.508  1.00 47.21           C  
ANISOU 1377  CB  SER B  88     3967   7380   6589   -366     81   -603       C  
ATOM   1378  OG  SER B  88       1.717  18.339  -3.570  1.00 48.56           O  
ANISOU 1378  OG  SER B  88     4134   7477   6838   -283    232   -312       O  
ATOM   1379  N   GLY B  89       3.970  18.077  -6.178  1.00 54.82           N  
ANISOU 1379  N   GLY B  89     5011   8624   7193   -350    563   -391       N  
ATOM   1380  CA  GLY B  89       5.182  18.800  -6.664  1.00 56.91           C  
ANISOU 1380  CA  GLY B  89     5288   8822   7510   -399    880   -338       C  
ATOM   1381  C   GLY B  89       4.939  20.221  -7.193  1.00 60.11           C  
ANISOU 1381  C   GLY B  89     5763   9168   7907   -328   1119    116       C  
ATOM   1382  O   GLY B  89       3.803  20.609  -7.542  1.00 61.29           O  
ANISOU 1382  O   GLY B  89     5954   9436   7897   -191   1014    436       O  
ATOM   1383  OXT GLY B  89       5.884  21.033  -7.296  1.00 61.88           O  
ANISOU 1383  OXT GLY B  89     5991   9206   8314   -400   1437    187       O  
TER    1384      GLY B  89                                                      
ATOM   1385  N   GLY D 130      13.072  26.433  -6.188  1.00 86.63           N  
ANISOU 1385  N   GLY D 130     6989  15298  10627   -494  -1112   2867       N  
ATOM   1386  CA  GLY D 130      13.863  25.906  -5.027  1.00 80.93           C  
ANISOU 1386  CA  GLY D 130     6299  14287  10161   -442   -700   2296       C  
ATOM   1387  C   GLY D 130      13.424  24.503  -4.633  1.00 77.67           C  
ANISOU 1387  C   GLY D 130     5867  13997   9644   -431   -704   1690       C  
ATOM   1388  O   GLY D 130      12.232  24.225  -4.562  1.00 78.68           O  
ANISOU 1388  O   GLY D 130     5844  14111   9938   -350   -966   1644       O  
ATOM   1389  N   SER D 131      14.381  23.615  -4.391  1.00 74.38           N  
ANISOU 1389  N   SER D 131     5571  13665   9022   -513   -418   1228       N  
ATOM   1390  CA  SER D 131      14.074  22.212  -4.140  1.00 72.05           C  
ANISOU 1390  CA  SER D 131     5255  13487   8634   -528   -409    681       C  
ATOM   1391  C   SER D 131      15.087  21.589  -3.185  1.00 67.98           C  
ANISOU 1391  C   SER D 131     4803  12715   8310   -516   -101    261       C  
ATOM   1392  O   SER D 131      16.270  21.412  -3.530  1.00 68.33           O  
ANISOU 1392  O   SER D 131     4930  12879   8151   -629    110    137       O  
ATOM   1393  CB  SER D 131      14.041  21.438  -5.458  1.00 75.50           C  
ANISOU 1393  CB  SER D 131     5739  14515   8431   -725   -510    549       C  
ATOM   1394  OG  SER D 131      12.708  21.229  -5.869  1.00 78.18           O  
ANISOU 1394  OG  SER D 131     5953  15035   8716   -695   -869    612       O  
ATOM   1395  N   VAL D 132      14.605  21.235  -1.998  1.00 64.47           N  
ANISOU 1395  N   VAL D 132     4312  11920   8264   -397    -85     43       N  
ATOM   1396  CA  VAL D 132      15.456  20.805  -0.905  1.00 61.01           C  
ANISOU 1396  CA  VAL D 132     3948  11180   8052   -373    118   -244       C  
ATOM   1397  C   VAL D 132      14.935  19.488  -0.360  1.00 59.38           C  
ANISOU 1397  C   VAL D 132     3723  10916   7920   -368    100   -632       C  
ATOM   1398  O   VAL D 132      13.816  19.445   0.125  1.00 59.26           O  
ANISOU 1398  O   VAL D 132     3649  10764   8101   -309     19   -636       O  
ATOM   1399  CB  VAL D 132      15.414  21.852   0.214  1.00 59.32           C  
ANISOU 1399  CB  VAL D 132     3739  10546   8252   -274    181    -70       C  
ATOM   1400  CG1 VAL D 132      16.136  21.351   1.438  1.00 56.37           C  
ANISOU 1400  CG1 VAL D 132     3467   9895   8055   -270    312   -359       C  
ATOM   1401  CG2 VAL D 132      15.984  23.156  -0.278  1.00 60.95           C  
ANISOU 1401  CG2 VAL D 132     3931  10737   8489   -277    227    309       C  
ATOM   1402  N   SER D 133      15.721  18.420  -0.444  1.00 58.71           N  
ANISOU 1402  N   SER D 133     3658  10897   7749   -437    193   -961       N  
ATOM   1403  CA  SER D 133      15.284  17.112   0.068  1.00 57.83           C  
ANISOU 1403  CA  SER D 133     3514  10679   7776   -439    185  -1301       C  
ATOM   1404  C   SER D 133      15.851  16.886   1.459  1.00 55.14           C  
ANISOU 1404  C   SER D 133     3288   9931   7729   -396    254  -1364       C  
ATOM   1405  O   SER D 133      17.037  17.087   1.643  1.00 55.08           O  
ANISOU 1405  O   SER D 133     3325   9830   7771   -404    314  -1363       O  
ATOM   1406  CB  SER D 133      15.757  15.980  -0.862  1.00 59.66           C  
ANISOU 1406  CB  SER D 133     3647  11186   7832   -552    235  -1654       C  
ATOM   1407  OG  SER D 133      15.464  16.246  -2.236  1.00 62.91           O  
ANISOU 1407  OG  SER D 133     4001  12063   7837   -652    176  -1602       O  
ATOM   1408  N   ARG D 134      15.037  16.460   2.422  1.00 53.79           N  
ANISOU 1408  N   ARG D 134     3166   9528   7742   -375    243  -1420       N  
ATOM   1409  CA  ARG D 134      15.521  16.240   3.794  1.00 52.37           C  
ANISOU 1409  CA  ARG D 134     3152   9003   7743   -380    276  -1433       C  
ATOM   1410  C   ARG D 134      14.596  15.383   4.636  1.00 52.30           C  
ANISOU 1410  C   ARG D 134     3205   8802   7862   -418    301  -1541       C  
ATOM   1411  O   ARG D 134      13.422  15.272   4.338  1.00 53.14           O  
ANISOU 1411  O   ARG D 134     3212   8984   7994   -419    323  -1591       O  
ATOM   1412  CB  ARG D 134      15.702  17.582   4.509  1.00 51.76           C  
ANISOU 1412  CB  ARG D 134     3179   8774   7710   -356    316  -1214       C  
ATOM   1413  CG  ARG D 134      14.425  18.189   5.083  1.00 51.64           C  
ANISOU 1413  CG  ARG D 134     3171   8644   7804   -359    383  -1141       C  
ATOM   1414  CD  ARG D 134      14.566  19.685   5.284  1.00 52.20           C  
ANISOU 1414  CD  ARG D 134     3225   8628   7981   -329    440   -950       C  
ATOM   1415  NE  ARG D 134      15.500  20.031   6.365  1.00 51.85           N  
ANISOU 1415  NE  ARG D 134     3345   8383   7969   -376    488   -976       N  
ATOM   1416  CZ  ARG D 134      16.009  21.249   6.573  1.00 52.13           C  
ANISOU 1416  CZ  ARG D 134     3357   8325   8125   -363    546   -872       C  
ATOM   1417  NH1 ARG D 134      15.694  22.266   5.772  1.00 53.44           N  
ANISOU 1417  NH1 ARG D 134     3344   8541   8420   -295    572   -675       N  
ATOM   1418  NH2 ARG D 134      16.839  21.457   7.586  1.00 51.83           N  
ANISOU 1418  NH2 ARG D 134     3462   8131   8099   -424    555   -953       N  
ATOM   1419  N   GLY D 135      15.112  14.829   5.729  1.00 51.96           N  
ANISOU 1419  N   GLY D 135     3332   8498   7910   -464    290  -1550       N  
ATOM   1420  CA  GLY D 135      14.305  13.998   6.637  1.00 52.28           C  
ANISOU 1420  CA  GLY D 135     3487   8331   8045   -543    347  -1598       C  
ATOM   1421  C   GLY D 135      14.221  14.466   8.085  1.00 52.39           C  
ANISOU 1421  C   GLY D 135     3780   8124   7999   -641    409  -1464       C  
ATOM   1422  O   GLY D 135      14.976  15.339   8.518  1.00 51.82           O  
ANISOU 1422  O   GLY D 135     3814   8029   7845   -641    366  -1359       O  
ATOM   1423  N   THR D 136      13.276  13.888   8.827  1.00 53.39           N  
ANISOU 1423  N   THR D 136     4022   8102   8162   -755    540  -1499       N  
ATOM   1424  CA  THR D 136      13.100  14.148  10.256  1.00 54.18           C  
ANISOU 1424  CA  THR D 136     4432   8025   8129   -925    650  -1413       C  
ATOM   1425  C   THR D 136      12.976  12.836  11.025  1.00 56.00           C  
ANISOU 1425  C   THR D 136     4858   8054   8364  -1060    647  -1357       C  
ATOM   1426  O   THR D 136      12.573  11.807  10.475  1.00 56.31           O  
ANISOU 1426  O   THR D 136     4735   8050   8607  -1024    656  -1447       O  
ATOM   1427  CB  THR D 136      11.804  14.904  10.535  1.00 54.74           C  
ANISOU 1427  CB  THR D 136     4467   8080   8250  -1004    931  -1516       C  
ATOM   1428  OG1 THR D 136      10.677  14.037  10.293  1.00 56.43           O  
ANISOU 1428  OG1 THR D 136     4560   8237   8642  -1037   1068  -1648       O  
ATOM   1429  CG2 THR D 136      11.685  16.118   9.658  1.00 53.51           C  
ANISOU 1429  CG2 THR D 136     4056   8071   8202   -858    918  -1525       C  
ATOM   1430  N   GLN D 137      13.267  12.892  12.315  1.00 57.55           N  
ANISOU 1430  N   GLN D 137     5405   8129   8332  -1241    642  -1208       N  
ATOM   1431  CA  GLN D 137      13.010  11.758  13.190  1.00 60.07           C  
ANISOU 1431  CA  GLN D 137     5974   8244   8603  -1423    665  -1073       C  
ATOM   1432  C   GLN D 137      12.698  12.235  14.603  1.00 62.43           C  
ANISOU 1432  C   GLN D 137     6682   8511   8528  -1711    840   -990       C  
ATOM   1433  O   GLN D 137      13.387  13.108  15.139  1.00 62.61           O  
ANISOU 1433  O   GLN D 137     6865   8624   8300  -1763    735   -949       O  
ATOM   1434  CB  GLN D 137      14.204  10.813  13.218  1.00 60.88           C  
ANISOU 1434  CB  GLN D 137     6105   8207   8816  -1358    294   -872       C  
ATOM   1435  CG  GLN D 137      13.993   9.570  14.064  1.00 63.91           C  
ANISOU 1435  CG  GLN D 137     6731   8331   9220  -1535    263   -643       C  
ATOM   1436  CD  GLN D 137      13.039   8.587  13.446  1.00 63.85           C  
ANISOU 1436  CD  GLN D 137     6489   8205   9566  -1508    475   -793       C  
ATOM   1437  OE1 GLN D 137      13.254   8.106  12.336  1.00 62.79           O  
ANISOU 1437  OE1 GLN D 137     5983   8082   9791  -1315    392   -973       O  
ATOM   1438  NE2 GLN D 137      11.988   8.257  14.174  1.00 66.31           N  
ANISOU 1438  NE2 GLN D 137     7009   8403   9782  -1731    776   -755       N  
ATOM   1439  N   THR D 138      11.667  11.639  15.199  1.00 64.64           N  
ANISOU 1439  N   THR D 138     7121   8668   8771  -1925   1132  -1000       N  
ATOM   1440  CA  THR D 138      11.287  11.936  16.579  1.00 67.93           C  
ANISOU 1440  CA  THR D 138     7965   9069   8774  -2278   1375   -950       C  
ATOM   1441  C   THR D 138      12.221  11.227  17.574  1.00 71.36           C  
ANISOU 1441  C   THR D 138     8825   9427   8861  -2452   1049   -562       C  
ATOM   1442  O   THR D 138      12.875  10.239  17.228  1.00 71.36           O  
ANISOU 1442  O   THR D 138     8747   9280   9085  -2308    707   -332       O  
ATOM   1443  CB  THR D 138       9.815  11.539  16.863  1.00 69.77           C  
ANISOU 1443  CB  THR D 138     8214   9181   9113  -2485   1868  -1118       C  
ATOM   1444  OG1 THR D 138       9.651  10.121  16.746  1.00 70.77           O  
ANISOU 1444  OG1 THR D 138     8346   9104   9437  -2490   1810   -939       O  
ATOM   1445  CG2 THR D 138       8.894  12.239  15.890  1.00 67.12           C  
ANISOU 1445  CG2 THR D 138     7421   8896   9184  -2303   2102  -1477       C  
ATOM   1446  N   GLU D 139      12.288  11.726  18.805  1.00 74.94           N  
ANISOU 1446  N   GLU D 139     9708   9974   8790  -2775   1136   -498       N  
ATOM   1447  CA  GLU D 139      13.163  11.120  19.799  1.00 79.36           C  
ANISOU 1447  CA  GLU D 139    10705  10496   8951  -2969    754    -80       C  
ATOM   1448  C   GLU D 139      12.449  10.846  21.114  1.00 84.96           C  
ANISOU 1448  C   GLU D 139    11943  11218   9119  -3452   1071     45       C  
ATOM   1449  O   GLU D 139      13.089  10.784  22.172  1.00 89.66           O  
ANISOU 1449  O   GLU D 139    12999  11902   9165  -3719    803    340       O  
ATOM   1450  CB  GLU D 139      14.368  12.021  20.043  1.00 79.16           C  
ANISOU 1450  CB  GLU D 139    10736  10645   8696  -2911    373    -71       C  
ATOM   1451  CG  GLU D 139      15.142  12.394  18.784  1.00 75.52           C  
ANISOU 1451  CG  GLU D 139     9779  10184   8731  -2482    116   -205       C  
ATOM   1452  CD  GLU D 139      16.360  13.255  19.084  1.00 77.24           C  
ANISOU 1452  CD  GLU D 139    10040  10532   8776  -2445   -240   -205       C  
ATOM   1453  OE1 GLU D 139      16.435  13.837  20.189  1.00 81.22           O  
ANISOU 1453  OE1 GLU D 139    10908  11184   8768  -2745   -215   -221       O  
ATOM   1454  OE2 GLU D 139      17.254  13.351  18.215  1.00 76.78           O  
ANISOU 1454  OE2 GLU D 139     9641  10432   9096  -2138   -525   -227       O  
ATOM   1455  N   GLY D 140      11.130  10.672  21.056  1.00136.55           N  
ANISOU 1455  N   GLY D 140    16519  24056  11305   1942   4281   5250       N  
ATOM   1456  CA  GLY D 140      10.329  10.451  22.259  1.00128.61           C  
ANISOU 1456  CA  GLY D 140    15609  22294  10963   1864   3785   4842       C  
ATOM   1457  C   GLY D 140      10.661   9.137  22.935  1.00121.94           C  
ANISOU 1457  C   GLY D 140    14786  21299  10243   1671   3371   3627       C  
ATOM   1458  O   GLY D 140      11.244   8.243  22.320  1.00123.97           O  
ANISOU 1458  O   GLY D 140    15020  22151   9932   1683   3389   3058       O  
ATOM   1459  N   GLY D 141      10.289   9.025  24.206  1.00114.83           N  
ANISOU 1459  N   GLY D 141    13947  19584  10098   1533   3071   3269       N  
ATOM   1460  CA  GLY D 141      10.544   7.814  24.986  1.00109.04           C  
ANISOU 1460  CA  GLY D 141    13236  18611   9581   1421   2718   2277       C  
ATOM   1461  C   GLY D 141      11.291   8.087  26.275  1.00104.35           C  
ANISOU 1461  C   GLY D 141    12534  17222   9890   1173   2845   2056       C  
ATOM   1462  O   GLY D 141      11.193   7.306  27.224  1.00 99.09           O  
ANISOU 1462  O   GLY D 141    11883  16225   9542   1133   2500   1471       O  
ATOM   1463  N   SER D 142      12.033   9.194  26.311  1.00107.29           N  
ANISOU 1463  N   SER D 142    12778  17343  10643    964   3365   2530       N  
ATOM   1464  CA  SER D 142      12.786   9.602  27.507  1.00104.67           C  
ANISOU 1464  CA  SER D 142    12270  16414  11085    571   3518   2284       C  
ATOM   1465  C   SER D 142      11.888  10.181  28.634  1.00100.49           C  
ANISOU 1465  C   SER D 142    11917  15111  11153    407   3343   2328       C  
ATOM   1466  O   SER D 142      11.086  11.092  28.397  1.00102.73           O  
ANISOU 1466  O   SER D 142    12406  15066  11560    490   3550   2942       O  
ATOM   1467  CB  SER D 142      13.860  10.616  27.104  1.00110.79           C  
ANISOU 1467  CB  SER D 142    12845  17191  12057    258   4209   2696       C  
ATOM   1468  OG  SER D 142      14.572  10.157  25.965  1.00115.21           O  
ANISOU 1468  OG  SER D 142    13256  18517  12001    464   4430   2749       O  
ATOM   1469  N   GLY D 143      12.037   9.645  29.850  1.00 95.15           N  
ANISOU 1469  N   GLY D 143    11140  14187  10823    233   3017   1729       N  
ATOM   1470  CA  GLY D 143      11.251  10.077  31.018  1.00 91.20           C  
ANISOU 1470  CA  GLY D 143    10794  13028  10829     54   2861   1641       C  
ATOM   1471  C   GLY D 143      10.058   9.188  31.334  1.00 85.90           C  
ANISOU 1471  C   GLY D 143    10303  12348   9987    376   2284   1443       C  
ATOM   1472  O   GLY D 143       9.168   9.576  32.090  1.00 83.72           O  
ANISOU 1472  O   GLY D 143    10179  11587  10041    333   2185   1498       O  
ATOM   1473  N   MET D 144      10.053   7.989  30.760  1.00 84.64           N  
ANISOU 1473  N   MET D 144    10130  12695   9336    660   1974   1169       N  
ATOM   1474  CA  MET D 144       8.949   7.043  30.886  1.00 81.22           C  
ANISOU 1474  CA  MET D 144     9863  12295   8700    872   1487    924       C  
ATOM   1475  C   MET D 144       9.014   6.294  32.220  1.00 76.48           C  
ANISOU 1475  C   MET D 144     9225  11371   8462    799   1203    434       C  
ATOM   1476  O   MET D 144       7.992   6.118  32.892  1.00 73.11           O  
ANISOU 1476  O   MET D 144     8927  10652   8198    805    918    378       O  
ATOM   1477  CB  MET D 144       8.988   6.072  29.696  1.00 84.06           C  
ANISOU 1477  CB  MET D 144    10273  13272   8392   1091   1401    714       C  
ATOM   1478  CG  MET D 144       7.810   5.134  29.587  1.00 83.04           C  
ANISOU 1478  CG  MET D 144    10314  13262   7976   1169    970    409       C  
ATOM   1479  SD  MET D 144       7.258   4.924  27.874  1.00 90.20           S  
ANISOU 1479  SD  MET D 144    11262  15092   7916   1257    929    514       S  
ATOM   1480  CE  MET D 144       5.681   4.079  28.141  1.00 88.62           C  
ANISOU 1480  CE  MET D 144    11149  14954   7568   1133    378    154       C  
ATOM   1481  N   LYS D 145      10.216   5.853  32.601  1.00 76.87           N  
ANISOU 1481  N   LYS D 145     9041  11556   8607    769   1302    155       N  
ATOM   1482  CA  LYS D 145      10.412   5.200  33.899  1.00 73.72           C  
ANISOU 1482  CA  LYS D 145     8520  10995   8494    762   1069   -156       C  
ATOM   1483  C   LYS D 145      10.035   6.162  35.002  1.00 71.88           C  
ANISOU 1483  C   LYS D 145     8275  10399   8636    412   1049    -81       C  
ATOM   1484  O   LYS D 145       9.380   5.777  35.966  1.00 68.84           O  
ANISOU 1484  O   LYS D 145     7971   9784   8399    425    777   -223       O  
ATOM   1485  CB  LYS D 145      11.849   4.748  34.117  1.00 76.19           C  
ANISOU 1485  CB  LYS D 145     8437  11691   8820    837   1218   -303       C  
ATOM   1486  CG  LYS D 145      12.070   4.060  35.482  1.00 73.76           C  
ANISOU 1486  CG  LYS D 145     7920  11381   8722    920    970   -470       C  
ATOM   1487  N   GLN D 146      10.449   7.417  34.852  1.00 74.69           N  
ANISOU 1487  N   GLN D 146     8558  10664   9156     74   1417    120       N  
ATOM   1488  CA  GLN D 146      10.033   8.495  35.769  1.00 74.60           C  
ANISOU 1488  CA  GLN D 146     8636  10168   9537   -315   1572    126       C  
ATOM   1489  C   GLN D 146       8.513   8.469  36.022  1.00 71.49           C  
ANISOU 1489  C   GLN D 146     8569   9364   9231   -100   1365    261       C  
ATOM   1490  O   GLN D 146       8.057   8.487  37.171  1.00 69.14           O  
ANISOU 1490  O   GLN D 146     8311   8818   9139   -242   1232     41       O  
ATOM   1491  CB  GLN D 146      10.440   9.863  35.209  1.00 79.57           C  
ANISOU 1491  CB  GLN D 146     9302  10548  10383   -645   2159    419       C  
ATOM   1492  CG  GLN D 146      11.955  10.121  35.200  1.00 83.50           C  
ANISOU 1492  CG  GLN D 146     9395  11437  10894  -1063   2436    233       C  
ATOM   1493  N   LEU D 147       7.745   8.405  34.935  1.00 72.08           N  
ANISOU 1493  N   LEU D 147     8808   9499   9076    233   1334    630       N  
ATOM   1494  CA  LEU D 147       6.292   8.366  35.018  1.00 70.34           C  
ANISOU 1494  CA  LEU D 147     8764   9082   8878    456   1127    831       C  
ATOM   1495  C   LEU D 147       5.823   7.051  35.607  1.00 66.46           C  
ANISOU 1495  C   LEU D 147     8273   8709   8269    557    642    442       C  
ATOM   1496  O   LEU D 147       5.050   7.042  36.572  1.00 64.56           O  
ANISOU 1496  O   LEU D 147     8090   8175   8262    515    513    365       O  
ATOM   1497  CB  LEU D 147       5.660   8.567  33.639  1.00 73.62           C  
ANISOU 1497  CB  LEU D 147     9220   9819   8932    766   1161   1354       C  
ATOM   1498  CG  LEU D 147       5.844   9.954  33.000  1.00 78.89           C  
ANISOU 1498  CG  LEU D 147     9933  10281   9758    793   1730   1988       C  
ATOM   1499  CD1 LEU D 147       5.604   9.887  31.501  1.00 82.96           C  
ANISOU 1499  CD1 LEU D 147    10388  11452   9679   1119   1710   2497       C  
ATOM   1500  CD2 LEU D 147       4.940  11.011  33.646  1.00 80.13           C  
ANISOU 1500  CD2 LEU D 147    10231   9772  10440    854   2042   2353       C  
ATOM   1501  N   GLU D 148       6.277   5.943  35.027  1.00 66.35           N  
ANISOU 1501  N   GLU D 148     8220   9066   7923    694    460    204       N  
ATOM   1502  CA  GLU D 148       5.914   4.620  35.534  1.00 64.04           C  
ANISOU 1502  CA  GLU D 148     7984   8746   7599    788    136   -150       C  
ATOM   1503  C   GLU D 148       6.121   4.519  37.046  1.00 61.47           C  
ANISOU 1503  C   GLU D 148     7585   8165   7604    678     69   -306       C  
ATOM   1504  O   GLU D 148       5.251   4.043  37.769  1.00 59.51           O  
ANISOU 1504  O   GLU D 148     7425   7711   7472    693   -133   -372       O  
ATOM   1505  CB  GLU D 148       6.720   3.529  34.832  1.00 66.03           C  
ANISOU 1505  CB  GLU D 148     8235   9272   7580    955    164   -436       C  
ATOM   1506  CG  GLU D 148       6.065   2.991  33.584  1.00 68.61           C  
ANISOU 1506  CG  GLU D 148     8715   9885   7468   1013     82   -542       C  
ATOM   1507  CD  GLU D 148       6.978   2.117  32.778  1.00 72.00           C  
ANISOU 1507  CD  GLU D 148     9187  10548   7619   1160    275   -876       C  
ATOM   1508  OE1 GLU D 148       8.157   1.986  33.159  1.00 72.57           O  
ANISOU 1508  OE1 GLU D 148     9108  10586   7878   1298    479   -909       O  
ATOM   1509  OE2 GLU D 148       6.521   1.568  31.756  1.00 75.58           O  
ANISOU 1509  OE2 GLU D 148     9789  11292   7633   1127    246  -1123       O  
ATOM   1510  N   ASP D 149       7.280   4.974  37.507  1.00 62.49           N  
ANISOU 1510  N   ASP D 149     7500   8418   7824    528    245   -358       N  
ATOM   1511  CA  ASP D 149       7.604   4.991  38.935  1.00 61.71           C  
ANISOU 1511  CA  ASP D 149     7236   8325   7885    356    172   -510       C  
ATOM   1512  C   ASP D 149       6.737   5.959  39.729  1.00 60.66           C  
ANISOU 1512  C   ASP D 149     7237   7832   7976     86    246   -496       C  
ATOM   1513  O   ASP D 149       6.449   5.710  40.888  1.00 59.68           O  
ANISOU 1513  O   ASP D 149     7087   7691   7899     14    107   -629       O  
ATOM   1514  CB  ASP D 149       9.077   5.348  39.154  1.00 64.78           C  
ANISOU 1514  CB  ASP D 149     7246   9140   8227    150    334   -602       C  
ATOM   1515  CG  ASP D 149      10.035   4.259  38.675  1.00 66.85           C  
ANISOU 1515  CG  ASP D 149     7285   9805   8309    525    304   -598       C  
ATOM   1516  OD1 ASP D 149       9.568   3.172  38.241  1.00 66.14           O  
ANISOU 1516  OD1 ASP D 149     7418   9548   8163    912    204   -604       O  
ATOM   1517  OD2 ASP D 149      11.269   4.496  38.734  1.00 70.30           O  
ANISOU 1517  OD2 ASP D 149     7305  10724   8681    407    439   -616       O  
ATOM   1518  N   LYS D 150       6.343   7.067  39.117  1.00 62.14           N  
ANISOU 1518  N   LYS D 150     7569   7735   8305    -17    535   -294       N  
ATOM   1519  CA  LYS D 150       5.483   8.046  39.782  1.00 62.61           C  
ANISOU 1519  CA  LYS D 150     7798   7329   8662   -183    757   -250       C  
ATOM   1520  C   LYS D 150       4.056   7.537  39.919  1.00 60.11           C  
ANISOU 1520  C   LYS D 150     7611   6866   8362    106    514    -95       C  
ATOM   1521  O   LYS D 150       3.403   7.775  40.931  1.00 59.65           O  
ANISOU 1521  O   LYS D 150     7618   6565   8479     17    560   -196       O  
ATOM   1522  CB  LYS D 150       5.485   9.391  39.040  1.00 66.61           C  
ANISOU 1522  CB  LYS D 150     8436   7467   9404   -271   1274     54       C  
ATOM   1523  CG  LYS D 150       4.822  10.569  39.819  1.00 68.93           C  
ANISOU 1523  CG  LYS D 150     8945   7112  10133   -464   1732     39       C  
ATOM   1524  CD  LYS D 150       5.231  10.643  41.305  1.00 69.09           C  
ANISOU 1524  CD  LYS D 150     8914   7141  10195   -954   1749   -575       C  
ATOM   1525  N   VAL D 151       3.572   6.834  38.906  1.00 59.45           N  
ANISOU 1525  N   VAL D 151     7533   6996   8057    394    279    102       N  
ATOM   1526  CA  VAL D 151       2.254   6.195  38.986  1.00 58.28           C  
ANISOU 1526  CA  VAL D 151     7412   6850   7878    562      6    185       C  
ATOM   1527  C   VAL D 151       2.186   5.164  40.130  1.00 55.72           C  
ANISOU 1527  C   VAL D 151     7089   6494   7588    495   -227   -121       C  
ATOM   1528  O   VAL D 151       1.333   5.227  41.019  1.00 54.66           O  
ANISOU 1528  O   VAL D 151     6974   6178   7614    464   -241   -109       O  
ATOM   1529  CB  VAL D 151       1.896   5.493  37.653  1.00 59.59           C  
ANISOU 1529  CB  VAL D 151     7544   7410   7687    724   -222    286       C  
ATOM   1530  CG1 VAL D 151       0.633   4.684  37.803  1.00 59.17           C  
ANISOU 1530  CG1 VAL D 151     7453   7444   7585    735   -520    238       C  
ATOM   1531  CG2 VAL D 151       1.732   6.522  36.524  1.00 63.29           C  
ANISOU 1531  CG2 VAL D 151     7963   8054   8030    876     -7    768       C  
ATOM   1532  N   GLU D 152       3.109   4.220  40.094  1.00 55.49           N  
ANISOU 1532  N   GLU D 152     7025   6647   7410    530   -348   -326       N  
ATOM   1533  CA  GLU D 152       3.301   3.293  41.196  1.00 54.81           C  
ANISOU 1533  CA  GLU D 152     6913   6552   7357    556   -477   -468       C  
ATOM   1534  C   GLU D 152       3.249   4.007  42.550  1.00 54.35           C  
ANISOU 1534  C   GLU D 152     6791   6460   7398    358   -389   -510       C  
ATOM   1535  O   GLU D 152       2.577   3.569  43.471  1.00 53.77           O  
ANISOU 1535  O   GLU D 152     6750   6311   7368    367   -472   -498       O  
ATOM   1536  CB  GLU D 152       4.652   2.589  41.063  1.00 56.22           C  
ANISOU 1536  CB  GLU D 152     6969   6980   7409    702   -466   -557       C  
ATOM   1537  CG  GLU D 152       4.666   1.466  40.031  1.00 59.41           C  
ANISOU 1537  CG  GLU D 152     7513   7329   7731    923   -486   -645       C  
ATOM   1538  CD  GLU D 152       5.950   0.630  40.094  1.00 64.21           C  
ANISOU 1538  CD  GLU D 152     7993   8097   8305   1210   -375   -670       C  
ATOM   1539  OE1 GLU D 152       6.329   0.177  41.206  1.00 66.53           O  
ANISOU 1539  OE1 GLU D 152     8141   8467   8668   1358   -402   -535       O  
ATOM   1540  OE2 GLU D 152       6.587   0.427  39.031  1.00 67.08           O  
ANISOU 1540  OE2 GLU D 152     8365   8581   8541   1337   -233   -772       O  
ATOM   1541  N   GLU D 153       3.982   5.102  42.672  1.00 55.84           N  
ANISOU 1541  N   GLU D 153     6896   6719   7601    119   -169   -606       N  
ATOM   1542  CA  GLU D 153       4.051   5.817  43.936  1.00 56.96           C  
ANISOU 1542  CA  GLU D 153     6991   6886   7763   -195    -24   -815       C  
ATOM   1543  C   GLU D 153       2.656   6.294  44.297  1.00 56.26           C  
ANISOU 1543  C   GLU D 153     7102   6381   7891   -174    114   -741       C  
ATOM   1544  O   GLU D 153       2.181   6.063  45.402  1.00 56.11           O  
ANISOU 1544  O   GLU D 153     7086   6410   7820   -230     76   -834       O  
ATOM   1545  CB  GLU D 153       5.015   6.996  43.837  1.00 59.96           C  
ANISOU 1545  CB  GLU D 153     7286   7314   8179   -591    291  -1029       C  
ATOM   1546  CG  GLU D 153       5.256   7.696  45.157  1.00 63.10           C  
ANISOU 1546  CG  GLU D 153     7618   7849   8506  -1076    468  -1434       C  
ATOM   1547  CD  GLU D 153       5.855   9.088  44.975  1.00 68.18           C  
ANISOU 1547  CD  GLU D 153     8310   8250   9345  -1601    959  -1726       C  
ATOM   1548  OE1 GLU D 153       6.844   9.249  44.195  1.00 69.90           O  
ANISOU 1548  OE1 GLU D 153     8355   8653   9548  -1714   1022  -1689       O  
ATOM   1549  OE2 GLU D 153       5.328  10.023  45.616  1.00 70.75           O  
ANISOU 1549  OE2 GLU D 153     8864   8146   9871  -1915   1362  -2008       O  
ATOM   1550  N   LEU D 154       2.002   6.953  43.349  1.00 56.66           N  
ANISOU 1550  N   LEU D 154     7273   6101   8154    -39    300   -501       N  
ATOM   1551  CA  LEU D 154       0.700   7.574  43.607  1.00 57.47           C  
ANISOU 1551  CA  LEU D 154     7484   5840   8511     71    524   -331       C  
ATOM   1552  C   LEU D 154      -0.346   6.516  43.894  1.00 55.36           C  
ANISOU 1552  C   LEU D 154     7151   5701   8181    259    201   -208       C  
ATOM   1553  O   LEU D 154      -1.015   6.588  44.904  1.00 55.86           O  
ANISOU 1553  O   LEU D 154     7233   5666   8323    217    304   -277       O  
ATOM   1554  CB  LEU D 154       0.261   8.463  42.438  1.00 59.75           C  
ANISOU 1554  CB  LEU D 154     7820   5876   9003    301    797     84       C  
ATOM   1555  CG  LEU D 154       1.011   9.787  42.294  1.00 63.56           C  
ANISOU 1555  CG  LEU D 154     8448   5973   9729     92   1351     35       C  
ATOM   1556  CD1 LEU D 154       0.659  10.516  40.992  1.00 66.28           C  
ANISOU 1556  CD1 LEU D 154     8817   6137  10226    437   1624    642       C  
ATOM   1557  CD2 LEU D 154       0.703  10.651  43.501  1.00 66.21           C  
ANISOU 1557  CD2 LEU D 154     8959   5841  10354   -147   1829   -279       C  
ATOM   1558  N   LEU D 155      -0.468   5.522  43.021  1.00 54.12           N  
ANISOU 1558  N   LEU D 155     6926   5760   7874    405   -132    -84       N  
ATOM   1559  CA  LEU D 155      -1.340   4.372  43.282  1.00 53.13           C  
ANISOU 1559  CA  LEU D 155     6752   5714   7718    447   -394    -58       C  
ATOM   1560  C   LEU D 155      -1.262   3.904  44.736  1.00 52.61           C  
ANISOU 1560  C   LEU D 155     6716   5627   7643    348   -384   -200       C  
ATOM   1561  O   LEU D 155      -2.282   3.678  45.393  1.00 53.18           O  
ANISOU 1561  O   LEU D 155     6756   5639   7811    345   -362   -114       O  
ATOM   1562  CB  LEU D 155      -0.953   3.190  42.394  1.00 52.95           C  
ANISOU 1562  CB  LEU D 155     6748   5852   7517    470   -654   -149       C  
ATOM   1563  CG  LEU D 155      -1.708   3.031  41.082  1.00 54.76           C  
ANISOU 1563  CG  LEU D 155     6887   6297   7620    492   -802    -43       C  
ATOM   1564  CD1 LEU D 155      -0.806   2.421  40.029  1.00 55.46           C  
ANISOU 1564  CD1 LEU D 155     7060   6546   7464    496   -883   -238       C  
ATOM   1565  CD2 LEU D 155      -2.935   2.200  41.272  1.00 55.53           C  
ANISOU 1565  CD2 LEU D 155     6890   6440   7769    361   -963    -61       C  
ATOM   1566  N   SER D 156      -0.043   3.754  45.231  1.00 52.50           N  
ANISOU 1566  N   SER D 156     6702   5778   7466    279   -397   -365       N  
ATOM   1567  CA  SER D 156       0.168   3.219  46.549  1.00 53.07           C  
ANISOU 1567  CA  SER D 156     6733   6038   7390    237   -430   -400       C  
ATOM   1568  C   SER D 156      -0.247   4.224  47.620  1.00 54.56           C  
ANISOU 1568  C   SER D 156     6935   6233   7560     33   -178   -558       C  
ATOM   1569  O   SER D 156      -1.034   3.901  48.518  1.00 55.20           O  
ANISOU 1569  O   SER D 156     7023   6334   7616     41   -138   -484       O  
ATOM   1570  CB  SER D 156       1.618   2.812  46.729  1.00 54.24           C  
ANISOU 1570  CB  SER D 156     6748   6564   7296    272   -532   -450       C  
ATOM   1571  OG  SER D 156       1.723   1.891  47.797  1.00 55.92           O  
ANISOU 1571  OG  SER D 156     6883   7028   7337    398   -616   -273       O  
ATOM   1572  N   LYS D 157       0.277   5.444  47.528  1.00 56.00           N  
ANISOU 1572  N   LYS D 157     7147   6359   7770   -183     71   -806       N  
ATOM   1573  CA  LYS D 157      -0.113   6.519  48.447  1.00 58.68           C  
ANISOU 1573  CA  LYS D 157     7584   6561   8150   -432    461  -1088       C  
ATOM   1574  C   LYS D 157      -1.636   6.608  48.514  1.00 58.44           C  
ANISOU 1574  C   LYS D 157     7625   6180   8397   -200    628   -855       C  
ATOM   1575  O   LYS D 157      -2.203   6.794  49.572  1.00 60.50           O  
ANISOU 1575  O   LYS D 157     7923   6467   8597   -284    840   -992       O  
ATOM   1576  CB  LYS D 157       0.473   7.864  47.995  1.00 61.25           C  
ANISOU 1576  CB  LYS D 157     8020   6587   8663   -692    856  -1353       C  
ATOM   1577  CG  LYS D 157       1.969   8.066  48.296  1.00 63.57           C  
ANISOU 1577  CG  LYS D 157     8164   7343   8646  -1126    810  -1742       C  
ATOM   1578  N   ASN D 158      -2.271   6.441  47.361  1.00 56.96           N  
ANISOU 1578  N   ASN D 158     7397   5793   8452     80    521   -497       N  
ATOM   1579  CA  ASN D 158      -3.711   6.556  47.181  1.00 57.65           C  
ANISOU 1579  CA  ASN D 158     7402   5707   8794    328    636   -185       C  
ATOM   1580  C   ASN D 158      -4.493   5.512  47.967  1.00 57.08           C  
ANISOU 1580  C   ASN D 158     7222   5836   8629    325    455   -103       C  
ATOM   1581  O   ASN D 158      -5.329   5.858  48.802  1.00 59.11           O  
ANISOU 1581  O   ASN D 158     7454   6027   8975    354    743    -97       O  
ATOM   1582  CB  ASN D 158      -4.026   6.365  45.694  1.00 57.11           C  
ANISOU 1582  CB  ASN D 158     7196   5697   8804    551    409    168       C  
ATOM   1583  CG  ASN D 158      -4.841   7.459  45.116  1.00 60.34           C  
ANISOU 1583  CG  ASN D 158     7522   5903   9501    848    752    531       C  
ATOM   1584  OD1 ASN D 158      -4.774   8.603  45.547  1.00 63.33           O  
ANISOU 1584  OD1 ASN D 158     8066   5871  10123    887   1281    466       O  
ATOM   1585  ND2 ASN D 158      -5.623   7.114  44.095  1.00 61.84           N  
ANISOU 1585  ND2 ASN D 158     7433   6409   9652   1063    493    932       N  
ATOM   1586  N   TYR D 159      -4.231   4.238  47.668  1.00 55.13           N  
ANISOU 1586  N   TYR D 159     6931   5773   8243    296     65    -29       N  
ATOM   1587  CA  TYR D 159      -4.867   3.133  48.367  1.00 55.42           C  
ANISOU 1587  CA  TYR D 159     6909   5901   8247    254    -37     92       C  
ATOM   1588  C   TYR D 159      -4.766   3.375  49.868  1.00 57.09           C  
ANISOU 1588  C   TYR D 159     7177   6252   8259    171    192    -22       C  
ATOM   1589  O   TYR D 159      -5.767   3.324  50.583  1.00 58.74           O  
ANISOU 1589  O   TYR D 159     7314   6477   8527    175    377     88       O  
ATOM   1590  CB  TYR D 159      -4.203   1.813  47.967  1.00 54.56           C  
ANISOU 1590  CB  TYR D 159     6866   5811   8053    237   -321    121       C  
ATOM   1591  CG  TYR D 159      -4.491   0.595  48.858  1.00 55.99           C  
ANISOU 1591  CG  TYR D 159     7078   5973   8221    208   -311    297       C  
ATOM   1592  CD1 TYR D 159      -5.769   0.086  49.002  1.00 57.86           C  
ANISOU 1592  CD1 TYR D 159     7214   6108   8660     91   -246    449       C  
ATOM   1593  CD2 TYR D 159      -3.471  -0.064  49.508  1.00 56.63           C  
ANISOU 1593  CD2 TYR D 159     7244   6173   8098    317   -334    389       C  
ATOM   1594  CE1 TYR D 159      -6.018  -1.027  49.793  1.00 59.92           C  
ANISOU 1594  CE1 TYR D 159     7537   6265   8963     41   -145    667       C  
ATOM   1595  CE2 TYR D 159      -3.707  -1.165  50.283  1.00 59.24           C  
ANISOU 1595  CE2 TYR D 159     7622   6439   8447    374   -243    691       C  
ATOM   1596  CZ  TYR D 159      -4.974  -1.651  50.433  1.00 60.83           C  
ANISOU 1596  CZ  TYR D 159     7802   6415   8895    216   -121    823       C  
ATOM   1597  OH  TYR D 159      -5.170  -2.765  51.235  1.00 64.21           O  
ANISOU 1597  OH  TYR D 159     8310   6703   9381    259     59   1188       O  
ATOM   1598  N   HIS D 160      -3.558   3.683  50.333  1.00 57.61           N  
ANISOU 1598  N   HIS D 160     7323   6530   8036     61    193   -264       N  
ATOM   1599  CA  HIS D 160      -3.308   3.903  51.770  1.00 60.45           C  
ANISOU 1599  CA  HIS D 160     7691   7256   8021   -100    364   -447       C  
ATOM   1600  C   HIS D 160      -4.056   5.095  52.333  1.00 62.67           C  
ANISOU 1600  C   HIS D 160     8052   7365   8392   -209    830   -722       C  
ATOM   1601  O   HIS D 160      -4.504   5.066  53.465  1.00 65.45           O  
ANISOU 1601  O   HIS D 160     8401   7958   8506   -285   1031   -788       O  
ATOM   1602  CB  HIS D 160      -1.819   4.061  52.037  1.00 61.71           C  
ANISOU 1602  CB  HIS D 160     7798   7863   7783   -274    230   -693       C  
ATOM   1603  CG  HIS D 160      -1.068   2.766  52.012  1.00 62.19           C  
ANISOU 1603  CG  HIS D 160     7735   8239   7655    -63   -111   -339       C  
ATOM   1604  ND1 HIS D 160      -0.095   2.484  51.071  1.00 61.38           N  
ANISOU 1604  ND1 HIS D 160     7576   8127   7618     46   -315   -301       N  
ATOM   1605  CD2 HIS D 160      -1.154   1.675  52.810  1.00 63.14           C  
ANISOU 1605  CD2 HIS D 160     7786   8641   7560    119   -191     56       C  
ATOM   1606  CE1 HIS D 160       0.393   1.277  51.299  1.00 62.47           C  
ANISOU 1606  CE1 HIS D 160     7621   8490   7624    324   -480     79       C  
ATOM   1607  NE2 HIS D 160      -0.229   0.768  52.349  1.00 64.23           N  
ANISOU 1607  NE2 HIS D 160     7842   8869   7690    381   -402    339       N  
ATOM   1608  N   LEU D 161      -4.183   6.142  51.536  1.00 62.52           N  
ANISOU 1608  N   LEU D 161     8118   6911   8725   -173   1075   -846       N  
ATOM   1609  CA  LEU D 161      -4.953   7.298  51.936  1.00 65.79           C  
ANISOU 1609  CA  LEU D 161     8646   6974   9375   -159   1660  -1041       C  
ATOM   1610  C   LEU D 161      -6.413   6.917  52.062  1.00 66.37           C  
ANISOU 1610  C   LEU D 161     8551   6989   9677    135   1750   -646       C  
ATOM   1611  O   LEU D 161      -7.062   7.273  53.036  1.00 70.04           O  
ANISOU 1611  O   LEU D 161     9047   7465  10097    124   2162   -790       O  
ATOM   1612  CB  LEU D 161      -4.787   8.457  50.940  1.00 66.60           C  
ANISOU 1612  CB  LEU D 161     8878   6527   9900    -69   1984  -1075       C  
ATOM   1613  CG  LEU D 161      -3.488   9.255  51.023  1.00 68.04           C  
ANISOU 1613  CG  LEU D 161     9256   6638   9954   -491   2178  -1607       C  
ATOM   1614  CD1 LEU D 161      -3.617  10.573  50.299  1.00 70.08           C  
ANISOU 1614  CD1 LEU D 161     9723   6154  10749   -385   2778  -1600       C  
ATOM   1615  CD2 LEU D 161      -3.091   9.471  52.476  1.00 72.08           C  
ANISOU 1615  CD2 LEU D 161     9858   7520  10008   -963   2392  -2236       C  
ATOM   1616  N   GLU D 162      -6.933   6.199  51.078  1.00 63.89           N  
ANISOU 1616  N   GLU D 162     8024   6678   9572    347   1392   -195       N  
ATOM   1617  CA  GLU D 162      -8.335   5.768  51.112  1.00 65.23           C  
ANISOU 1617  CA  GLU D 162     7913   6922   9948    532   1429    179       C  
ATOM   1618  C   GLU D 162      -8.683   5.026  52.397  1.00 66.57           C  
ANISOU 1618  C   GLU D 162     8064   7367   9860    381   1488    163       C  
ATOM   1619  O   GLU D 162      -9.699   5.318  53.035  1.00 69.80           O  
ANISOU 1619  O   GLU D 162     8345   7799  10377    488   1867    247       O  
ATOM   1620  CB  GLU D 162      -8.686   4.907  49.897  1.00 63.17           C  
ANISOU 1620  CB  GLU D 162     7402   6790   9809    578    957    521       C  
ATOM   1621  CG  GLU D 162      -9.508   5.665  48.860  1.00 65.59           C  
ANISOU 1621  CG  GLU D 162     7424   7076  10418    895   1061    859       C  
ATOM   1622  CD  GLU D 162      -9.414   5.074  47.462  1.00 64.50           C  
ANISOU 1622  CD  GLU D 162     7105   7181  10219    854    568   1031       C  
ATOM   1623  OE1 GLU D 162      -8.934   3.920  47.332  1.00 62.21           O  
ANISOU 1623  OE1 GLU D 162     6911   6976   9747    559    199    858       O  
ATOM   1624  OE2 GLU D 162      -9.835   5.769  46.500  1.00 66.86           O  
ANISOU 1624  OE2 GLU D 162     7165   7601  10636   1143    605   1362       O  
ATOM   1625  N   ASN D 163      -7.831   4.085  52.780  1.00 65.00           N  
ANISOU 1625  N   ASN D 163     7974   7402   9319    192   1169    124       N  
ATOM   1626  CA  ASN D 163      -8.052   3.288  53.995  1.00 67.17           C  
ANISOU 1626  CA  ASN D 163     8235   7994   9292     96   1230    252       C  
ATOM   1627  C   ASN D 163      -8.117   4.171  55.250  1.00 70.96           C  
ANISOU 1627  C   ASN D 163     8819   8697   9446     14   1694    -87       C  
ATOM   1628  O   ASN D 163      -8.926   3.939  56.152  1.00 73.94           O  
ANISOU 1628  O   ASN D 163     9113   9275   9706     21   1963     47       O  
ATOM   1629  CB  ASN D 163      -6.956   2.219  54.166  1.00 66.31           C  
ANISOU 1629  CB  ASN D 163     8217   8112   8867     36    873    381       C  
ATOM   1630  CG  ASN D 163      -6.975   1.150  53.057  1.00 64.10           C  
ANISOU 1630  CG  ASN D 163     7904   7533   8916     80    547    649       C  
ATOM   1631  OD1 ASN D 163      -7.607   1.328  52.011  1.00 62.97           O  
ANISOU 1631  OD1 ASN D 163     7649   7148   9125     80    475    643       O  
ATOM   1632  ND2 ASN D 163      -6.264   0.043  53.286  1.00 64.48           N  
ANISOU 1632  ND2 ASN D 163     8039   7640   8819    127    394    885       N  
ATOM   1633  N   GLU D 164      -7.255   5.176  55.290  1.00 71.49           N  
ANISOU 1633  N   GLU D 164     9072   8734   9354   -123   1833   -579       N  
ATOM   1634  CA  GLU D 164      -7.254   6.146  56.371  1.00 76.64           C  
ANISOU 1634  CA  GLU D 164     9882   9536   9700   -321   2353  -1105       C  
ATOM   1635  C   GLU D 164      -8.635   6.870  56.471  1.00 79.75           C  
ANISOU 1635  C   GLU D 164    10247   9516  10537    -72   2960  -1072       C  
ATOM   1636  O   GLU D 164      -9.203   7.060  57.564  1.00 84.16           O  
ANISOU 1636  O   GLU D 164    10832  10299  10843   -121   3399  -1250       O  
ATOM   1637  CB  GLU D 164      -6.136   7.183  56.126  1.00 77.73           C  
ANISOU 1637  CB  GLU D 164    10231   9539   9761   -611   2468  -1708       C  
ATOM   1638  CG  GLU D 164      -5.213   7.623  57.292  1.00 82.87           C  
ANISOU 1638  CG  GLU D 164    10990  10809   9686  -1126   2618  -2388       C  
ATOM   1639  CD  GLU D 164      -5.496   6.994  58.631  1.00 86.56           C  
ANISOU 1639  CD  GLU D 164    11353  12055   9481  -1207   2627  -2326       C  
ATOM   1640  OE1 GLU D 164      -6.648   6.552  58.871  1.00 87.11           O  
ANISOU 1640  OE1 GLU D 164    11355  11997   9744   -905   2793  -1906       O  
ATOM   1641  OE2 GLU D 164      -4.585   6.968  59.494  1.00 90.42           O  
ANISOU 1641  OE2 GLU D 164    11779  13392   9184  -1598   2494  -2685       O  
ATOM   1642  N   VAL D 165      -9.156   7.276  55.314  1.00 78.08           N  
ANISOU 1642  N   VAL D 165     9935   8786  10944    239   3002   -797       N  
ATOM   1643  CA  VAL D 165     -10.480   7.903  55.215  1.00 81.52           C  
ANISOU 1643  CA  VAL D 165    10205   8904  11864    625   3537   -566       C  
ATOM   1644  C   VAL D 165     -11.566   6.968  55.775  1.00 82.52           C  
ANISOU 1644  C   VAL D 165     9994   9431  11925    702   3485   -154       C  
ATOM   1645  O   VAL D 165     -12.265   7.320  56.734  1.00 87.07           O  
ANISOU 1645  O   VAL D 165    10560  10089  12433    772   4044   -276       O  
ATOM   1646  CB  VAL D 165     -10.830   8.261  53.739  1.00 80.03           C  
ANISOU 1646  CB  VAL D 165     9812   8354  12240   1006   3422   -114       C  
ATOM   1647  CG1 VAL D 165     -12.259   8.806  53.626  1.00 84.63           C  
ANISOU 1647  CG1 VAL D 165    10058   8800  13295   1516   3933    307       C  
ATOM   1648  CG2 VAL D 165      -9.822   9.239  53.166  1.00 80.02           C  
ANISOU 1648  CG2 VAL D 165    10150   7883  12370    948   3590   -433       C  
ATOM   1649  N   ALA D 166     -11.687   5.780  55.166  1.00 78.80           N  
ANISOU 1649  N   ALA D 166     9271   9178  11491    644   2880    288       N  
ATOM   1650  CA  ALA D 166     -12.646   4.752  55.606  1.00 80.21           C  
ANISOU 1650  CA  ALA D 166     9133   9681  11662    590   2822    689       C  
ATOM   1651  C   ALA D 166     -12.549   4.533  57.126  1.00 83.38           C  
ANISOU 1651  C   ALA D 166     9708  10423  11550    418   3131    517       C  
ATOM   1652  O   ALA D 166     -13.572   4.444  57.830  1.00 87.22           O  
ANISOU 1652  O   ALA D 166     9979  11103  12056    487   3526    700       O  
ATOM   1653  CB  ALA D 166     -12.415   3.417  54.837  1.00 76.33           C  
ANISOU 1653  CB  ALA D 166     8528   9254  11219    378   2184    991       C  
ATOM   1654  N   ARG D 167     -11.307   4.469  57.611  1.00 82.39           N  
ANISOU 1654  N   ARG D 167     9912  10482  10910    199   2952    192       N  
ATOM   1655  CA  ARG D 167     -11.015   4.260  59.033  1.00 86.29           C  
ANISOU 1655  CA  ARG D 167    10539  11527  10720     14   3157     41       C  
ATOM   1656  C   ARG D 167     -11.537   5.414  59.907  1.00 92.01           C  
ANISOU 1656  C   ARG D 167    11372  12295  11291     27   3893   -456       C  
ATOM   1657  O   ARG D 167     -12.074   5.182  60.995  1.00 96.55           O  
ANISOU 1657  O   ARG D 167    11895  13310  11481    -14   4235   -397       O  
ATOM   1658  CB  ARG D 167      -9.503   4.086  59.237  1.00 85.04           C  
ANISOU 1658  CB  ARG D 167    10586  11726   9999   -206   2767   -200       C  
ATOM   1659  CG  ARG D 167      -9.122   3.507  60.589  1.00 89.51           C  
ANISOU 1659  CG  ARG D 167    11157  13111   9740   -351   2784    -97       C  
ATOM   1660  CD  ARG D 167      -7.627   3.627  60.866  1.00 90.20           C  
ANISOU 1660  CD  ARG D 167    11322  13775   9174   -573   2454   -415       C  
ATOM   1661  NE  ARG D 167      -7.136   5.005  60.738  1.00 91.47           N  
ANISOU 1661  NE  ARG D 167    11665  13794   9296   -859   2694  -1281       N  
ATOM   1662  CZ  ARG D 167      -7.413   6.015  61.574  1.00 97.30           C  
ANISOU 1662  CZ  ARG D 167    12561  14695   9711  -1121   3276  -1968       C  
ATOM   1663  NH1 ARG D 167      -8.191   5.838  62.635  1.00102.25           N  
ANISOU 1663  NH1 ARG D 167    13154  15754   9941  -1101   3651  -1889       N  
ATOM   1664  NH2 ARG D 167      -6.911   7.228  61.347  1.00 98.98           N  
ANISOU 1664  NH2 ARG D 167    12999  14587  10020  -1434   3569  -2774       N  
ATOM   1665  N   LEU D 168     -11.372   6.646  59.424  1.00 92.64           N  
ANISOU 1665  N   LEU D 168    11633  11874  11691     91   4214   -935       N  
ATOM   1666  CA  LEU D 168     -11.801   7.848  60.160  1.00 99.30           C  
ANISOU 1666  CA  LEU D 168    12681  12538  12510    111   5070  -1519       C  
ATOM   1667  C   LEU D 168     -13.310   8.125  60.052  1.00102.15           C  
ANISOU 1667  C   LEU D 168    12752  12597  13462    591   5620  -1134       C  
ATOM   1668  O   LEU D 168     -13.924   8.552  61.028  1.00108.35           O  
ANISOU 1668  O   LEU D 168    13592  13511  14064    636   6313  -1406       O  
ATOM   1669  CB  LEU D 168     -10.995   9.074  59.700  1.00100.40           C  
ANISOU 1669  CB  LEU D 168    13184  12110  12854    -26   5345  -2175       C  
ATOM   1670  CG  LEU D 168      -9.527   9.118  60.155  1.00100.97           C  
ANISOU 1670  CG  LEU D 168    13506  12648  12211   -624   5041  -2804       C  
ATOM   1671  CD1 LEU D 168      -8.707  10.166  59.396  1.00100.63           C  
ANISOU 1671  CD1 LEU D 168    13747  11958  12529   -809   5214  -3310       C  
ATOM   1672  CD2 LEU D 168      -9.460   9.371  61.655  1.00108.72           C  
ANISOU 1672  CD2 LEU D 168    14649  14288  12373  -1025   5493  -3462       C  
ATOM   1673  N   LYS D 169     -13.890   7.885  58.871  1.00 98.48           N  
ANISOU 1673  N   LYS D 169    11931  11842  13645    938   5321   -513       N  
ATOM   1674  CA  LYS D 169     -15.345   7.973  58.668  1.00101.66           C  
ANISOU 1674  CA  LYS D 169    11851  12204  14570   1399   5696     11       C  
ATOM   1675  C   LYS D 169     -16.100   7.099  59.677  1.00104.58           C  
ANISOU 1675  C   LYS D 169    11960  13165  14608   1268   5801    261       C  
ATOM   1676  O   LYS D 169     -17.131   7.525  60.223  1.00110.87           O  
ANISOU 1676  O   LYS D 169    12534  14019  15569   1561   6490    335       O  
ATOM   1677  CB  LYS D 169     -15.737   7.565  57.237  1.00 97.56           C  
ANISOU 1677  CB  LYS D 169    10873  11630  14564   1624   5131    659       C  
ATOM   1678  CG  LYS D 169     -15.725   8.706  56.215  1.00 98.49           C  
ANISOU 1678  CG  LYS D 169    11002  11200  15219   2082   5380    741       C  
ATOM   1679  CD  LYS D 169     -16.340   8.276  54.881  1.00 95.71           C  
ANISOU 1679  CD  LYS D 169    10043  11094  15226   2325   4843   1456       C  
ATOM   1680  N   LYS D 170     -15.586   5.886  59.913  1.00100.98           N  
ANISOU 1680  N   LYS D 170    11529  13115  13722    877   5196    446       N  
ATOM   1681  CA  LYS D 170     -16.136   4.971  60.918  1.00103.96           C  
ANISOU 1681  CA  LYS D 170    11734  14029  13734    707   5313    754       C  
ATOM   1682  C   LYS D 170     -16.162   5.618  62.305  1.00110.59           C  
ANISOU 1682  C   LYS D 170    12842  15183  13994    673   6027    257       C  
ATOM   1683  O   LYS D 170     -17.128   5.447  63.061  1.00115.95           O  
ANISOU 1683  O   LYS D 170    13274  16184  14595    761   6522    478       O  
ATOM   1684  N   LEU D 171     -15.106   6.371  62.623  1.00111.08           N  
ANISOU 1684  N   LEU D 171    13381  15199  13621    488   6110   -462       N  
ATOM   1685  CA  LEU D 171     -15.001   7.057  63.909  1.00118.38           C  
ANISOU 1685  CA  LEU D 171    14611  16487  13878    316   6790  -1145       C  
ATOM   1686  C   LEU D 171     -16.037   8.180  64.041  1.00124.69           C  
ANISOU 1686  C   LEU D 171    15390  16812  15175    702   7772  -1436       C  
ATOM   1687  O   LEU D 171     -16.809   8.217  65.013  1.00131.30           O  
ANISOU 1687  O   LEU D 171    16138  18021  15726    774   8407  -1482       O  
ATOM   1688  CB  LEU D 171     -13.587   7.612  64.105  1.00118.35           C  
ANISOU 1688  CB  LEU D 171    15061  16595  13308   -109   6617  -1941       C  
ATOM   1689  N   VAL D 172     -16.056   9.092  63.063  1.00123.62           N  
ANISOU 1689  N   VAL D 172    15326  15854  15790   1010   7963  -1564       N  
ATOM   1690  CA  VAL D 172     -16.986  10.240  63.083  1.00130.57           C  
ANISOU 1690  CA  VAL D 172    16199  16136  17275   1528   8999  -1740       C  
ATOM   1691  C   VAL D 172     -18.378   9.810  62.633  1.00131.01           C  
ANISOU 1691  C   VAL D 172    15533  16299  17943   2087   9052   -801       C  
ATOM   1692  O   VAL D 172     -19.266   9.600  63.456  1.00136.15           O  
ANISOU 1692  O   VAL D 172    15926  17370  18434   2205   9550   -656       O  
ATOM   1693  CB  VAL D 172     -16.516  11.416  62.172  1.00130.78           C  
ANISOU 1693  CB  VAL D 172    16555  15183  17951   1748   9297  -2065       C  
ATOM   1694  CG1 VAL D 172     -17.415  12.634  62.379  1.00139.94           C  
ANISOU 1694  CG1 VAL D 172    17801  15644  19723   2340  10571  -2262       C  
ATOM   1695  CG2 VAL D 172     -15.052  11.783  62.444  1.00129.82           C  
ANISOU 1695  CG2 VAL D 172    17053  14999  17274   1063   9129  -2987       C  
TER    1696      VAL D 172                                                      
ATOM   1697  N   SER C 131      -6.027  17.038  -7.937  1.00 89.94           N  
ANISOU 1697  N   SER C 131     9773  17912   6488   2559  -1094  -3200       N  
ATOM   1698  CA  SER C 131      -5.649  17.601  -6.620  1.00 82.02           C  
ANISOU 1698  CA  SER C 131     8896  16012   6256   2153   -710  -2582       C  
ATOM   1699  C   SER C 131      -6.661  17.202  -5.553  1.00 76.75           C  
ANISOU 1699  C   SER C 131     8044  14492   6623   2024   -968  -2864       C  
ATOM   1700  O   SER C 131      -7.819  17.588  -5.626  1.00 78.22           O  
ANISOU 1700  O   SER C 131     8219  14542   6955   2156  -1338  -2799       O  
ATOM   1701  CB  SER C 131      -5.532  19.115  -6.717  1.00 82.96           C  
ANISOU 1701  CB  SER C 131     9334  16153   6033   2092   -510  -1507       C  
ATOM   1702  OG  SER C 131      -4.166  19.475  -6.762  1.00 83.26           O  
ANISOU 1702  OG  SER C 131     9480  16371   5782   1911     56  -1086       O  
ATOM   1703  N   VAL C 132      -6.204  16.433  -4.570  1.00 71.53           N  
ANISOU 1703  N   VAL C 132     7217  13278   6681   1769   -759  -3137       N  
ATOM   1704  CA  VAL C 132      -7.062  15.800  -3.577  1.00 67.77           C  
ANISOU 1704  CA  VAL C 132     6505  12082   7161   1632   -925  -3425       C  
ATOM   1705  C   VAL C 132      -6.490  16.008  -2.199  1.00 61.69           C  
ANISOU 1705  C   VAL C 132     5821  10719   6897   1265   -535  -2982       C  
ATOM   1706  O   VAL C 132      -5.437  15.490  -1.891  1.00 60.51           O  
ANISOU 1706  O   VAL C 132     5632  10519   6839   1136   -299  -3050       O  
ATOM   1707  CB  VAL C 132      -7.122  14.283  -3.823  1.00 70.28           C  
ANISOU 1707  CB  VAL C 132     6406  12369   7929   1740  -1154  -4319       C  
ATOM   1708  CG1 VAL C 132      -7.855  13.576  -2.698  1.00 66.84           C  
ANISOU 1708  CG1 VAL C 132     5691  11119   8584   1536  -1211  -4449       C  
ATOM   1709  CG2 VAL C 132      -7.758  13.990  -5.181  1.00 77.10           C  
ANISOU 1709  CG2 VAL C 132     7100  13890   8302   2153  -1621  -4967       C  
ATOM   1710  N   SER C 133      -7.175  16.759  -1.357  1.00 58.82           N  
ANISOU 1710  N   SER C 133     5540   9942   6867   1114   -491  -2588       N  
ATOM   1711  CA  SER C 133      -6.682  17.026  -0.007  1.00 54.11           C  
ANISOU 1711  CA  SER C 133     5008   8909   6640    797   -148  -2230       C  
ATOM   1712  C   SER C 133      -7.277  16.000   0.954  1.00 52.37           C  
ANISOU 1712  C   SER C 133     4529   8230   7140    648   -184  -2482       C  
ATOM   1713  O   SER C 133      -8.479  15.775   0.926  1.00 54.16           O  
ANISOU 1713  O   SER C 133     4567   8280   7731    711   -400  -2710       O  
ATOM   1714  CB  SER C 133      -7.079  18.443   0.428  1.00 53.12           C  
ANISOU 1714  CB  SER C 133     5039   8631   6513    716    -52  -1745       C  
ATOM   1715  OG  SER C 133      -6.774  19.409  -0.559  1.00 55.85           O  
ANISOU 1715  OG  SER C 133     5567   9327   6323    874    -71  -1397       O  
ATOM   1716  N   ARG C 134      -6.462  15.398   1.809  1.00 50.06           N  
ANISOU 1716  N   ARG C 134     4198   7729   7093    453     23  -2392       N  
ATOM   1717  CA  ARG C 134      -6.945  14.419   2.783  1.00 49.94           C  
ANISOU 1717  CA  ARG C 134     3935   7284   7753    290     35  -2435       C  
ATOM   1718  C   ARG C 134      -6.004  14.182   3.953  1.00 47.83           C  
ANISOU 1718  C   ARG C 134     3730   6857   7586     62    277  -2076       C  
ATOM   1719  O   ARG C 134      -4.838  14.493   3.884  1.00 46.67           O  
ANISOU 1719  O   ARG C 134     3743   6882   7107     56    382  -1968       O  
ATOM   1720  CB  ARG C 134      -7.207  13.080   2.114  1.00 53.27           C  
ANISOU 1720  CB  ARG C 134     4000   7583   8657    432   -239  -2972       C  
ATOM   1721  CG  ARG C 134      -5.985  12.220   1.941  1.00 54.10           C  
ANISOU 1721  CG  ARG C 134     3997   7691   8867    442   -237  -3146       C  
ATOM   1722  CD  ARG C 134      -6.188  11.216   0.813  1.00 59.16           C  
ANISOU 1722  CD  ARG C 134     4263   8403   9812    690   -568  -3909       C  
ATOM   1723  NE  ARG C 134      -7.159  10.173   1.139  1.00 61.59           N  
ANISOU 1723  NE  ARG C 134     4121   8170  11110    656   -757  -4161       N  
ATOM   1724  CZ  ARG C 134      -7.724   9.358   0.247  1.00 66.34           C  
ANISOU 1724  CZ  ARG C 134     4289   8734  12181    884  -1111  -4931       C  
ATOM   1725  NH1 ARG C 134      -7.435   9.452  -1.048  1.00 69.33           N  
ANISOU 1725  NH1 ARG C 134     4659   9717  11967   1186  -1327  -5554       N  
ATOM   1726  NH2 ARG C 134      -8.593   8.437   0.651  1.00 69.16           N  
ANISOU 1726  NH2 ARG C 134     4175   8478  13625    815  -1242  -5100       N  
ATOM   1727  N   GLY C 135      -6.525  13.591   5.021  1.00 48.43           N  
ANISOU 1727  N   GLY C 135     3647   6621   8133   -117    360  -1876       N  
ATOM   1728  CA  GLY C 135      -5.722  13.262   6.203  1.00 47.87           C  
ANISOU 1728  CA  GLY C 135     3618   6458   8109   -306    526  -1470       C  
ATOM   1729  C   GLY C 135      -5.697  11.800   6.636  1.00 50.61           C  
ANISOU 1729  C   GLY C 135     3659   6420   9150   -384    440  -1357       C  
ATOM   1730  O   GLY C 135      -6.485  10.991   6.175  1.00 53.24           O  
ANISOU 1730  O   GLY C 135     3674   6464  10089   -331    293  -1619       O  
ATOM   1731  N   THR C 136      -4.767  11.487   7.533  1.00 50.96           N  
ANISOU 1731  N   THR C 136     3760   6429   9171   -498    496   -958       N  
ATOM   1732  CA  THR C 136      -4.632  10.161   8.145  1.00 54.43           C  
ANISOU 1732  CA  THR C 136     3912   6460  10306   -592    408   -632       C  
ATOM   1733  C   THR C 136      -4.497  10.297   9.656  1.00 55.49           C  
ANISOU 1733  C   THR C 136     4191   6741  10149   -785    604     75       C  
ATOM   1734  O   THR C 136      -4.086  11.335  10.165  1.00 53.11           O  
ANISOU 1734  O   THR C 136     4192   6864   9122   -807    735    156       O  
ATOM   1735  CB  THR C 136      -3.350   9.443   7.696  1.00 55.24           C  
ANISOU 1735  CB  THR C 136     3887   6391  10710   -487    168   -820       C  
ATOM   1736  OG1 THR C 136      -2.213  10.086   8.299  1.00 53.31           O  
ANISOU 1736  OG1 THR C 136     3930   6432   9892   -517    225   -568       O  
ATOM   1737  CG2 THR C 136      -3.229   9.441   6.183  1.00 54.84           C  
ANISOU 1737  CG2 THR C 136     3726   6426  10681   -269     15  -1594       C  
ATOM   1738  N   GLN C 137      -4.815   9.217  10.361  1.00 60.09           N  
ANISOU 1738  N   GLN C 137     4513   6983  11334   -912    608    587       N  
ATOM   1739  CA  GLN C 137      -4.526   9.112  11.792  1.00 62.74           C  
ANISOU 1739  CA  GLN C 137     4962   7531  11345  -1066    741   1368       C  
ATOM   1740  C   GLN C 137      -4.260   7.674  12.192  1.00 68.32           C  
ANISOU 1740  C   GLN C 137     5337   7713  12908  -1127    564   1953       C  
ATOM   1741  O   GLN C 137      -4.995   6.767  11.805  1.00 71.25           O  
ANISOU 1741  O   GLN C 137     5307   7530  14233  -1167    537   1945       O  
ATOM   1742  CB  GLN C 137      -5.678   9.654  12.614  1.00 63.85           C  
ANISOU 1742  CB  GLN C 137     5162   8010  11089  -1233   1134   1649       C  
ATOM   1743  CG  GLN C 137      -5.428   9.639  14.103  1.00 67.75           C  
ANISOU 1743  CG  GLN C 137     5786   8944  11011  -1370   1309   2416       C  
ATOM   1744  CD  GLN C 137      -4.425  10.658  14.530  1.00 64.78           C  
ANISOU 1744  CD  GLN C 137     5754   9145   9715  -1277   1229   2238       C  
ATOM   1745  OE1 GLN C 137      -4.627  11.840  14.320  1.00 61.28           O  
ANISOU 1745  OE1 GLN C 137     5468   9026   8787  -1235   1355   1706       O  
ATOM   1746  NE2 GLN C 137      -3.339  10.215  15.146  1.00 67.68           N  
ANISOU 1746  NE2 GLN C 137     6185   9597   9932  -1234    985   2671       N  
ATOM   1747  N   THR C 138      -3.203   7.483  12.974  1.00 70.38           N  
ANISOU 1747  N   THR C 138     5720   8109  12911  -1122    405   2451       N  
ATOM   1748  CA  THR C 138      -2.846   6.157  13.490  1.00 76.93           C  
ANISOU 1748  CA  THR C 138     6236   8426  14565  -1171    182   3175       C  
ATOM   1749  C   THR C 138      -3.777   5.720  14.644  1.00 83.25           C  
ANISOU 1749  C   THR C 138     6946   9300  15383  -1394    496   4173       C  
ATOM   1750  O   THR C 138      -4.357   6.562  15.345  1.00 82.58           O  
ANISOU 1750  O   THR C 138     7132   9884  14360  -1496    867   4335       O  
ATOM   1751  CB  THR C 138      -1.350   6.098  13.941  1.00 77.62           C  
ANISOU 1751  CB  THR C 138     6464   8636  14389  -1058   -170   3397       C  
ATOM   1752  OG1 THR C 138      -1.125   6.994  15.039  1.00 77.36           O  
ANISOU 1752  OG1 THR C 138     6831   9395  13165  -1090    -29   3765       O  
ATOM   1753  CG2 THR C 138      -0.433   6.473  12.793  1.00 72.17           C  
ANISOU 1753  CG2 THR C 138     5792   7862  13765   -869   -388   2440       C  
ATOM   1754  N   GLU C 139      -3.912   4.402  14.817  1.00 89.94           N  
ANISOU 1754  N   GLU C 139     7357   9448  17369  -1473    367   4819       N  
ATOM   1755  CA  GLU C 139      -4.763   3.819  15.858  1.00 97.74           C  
ANISOU 1755  CA  GLU C 139     8173  10409  18555  -1708    702   5924       C  
ATOM   1756  C   GLU C 139      -4.295   4.300  17.234  1.00101.08           C  
ANISOU 1756  C   GLU C 139     9014  11720  17670  -1751    817   6761       C  
ATOM   1757  O   GLU C 139      -3.271   3.841  17.740  1.00104.86           O  
ANISOU 1757  O   GLU C 139     9532  12174  18135  -1664    440   7338       O  
ATOM   1758  CB  GLU C 139      -4.737   2.288  15.774  1.00105.10           C  
ANISOU 1758  CB  GLU C 139     8504  10311  21115  -1761    453   6538       C  
ATOM   1759  N   GLY C 140      -5.036   5.239  17.825  1.00116.27           N  
ANISOU 1759  N   GLY C 140    17829  16073  10274  -6451   -424    503       N  
ATOM   1760  CA  GLY C 140      -4.607   5.907  19.058  1.00110.51           C  
ANISOU 1760  CA  GLY C 140    16856  14985  10145  -5549   -532    800       C  
ATOM   1761  C   GLY C 140      -4.438   4.942  20.222  1.00109.04           C  
ANISOU 1761  C   GLY C 140    17034  14285  10112  -5652    270    638       C  
ATOM   1762  O   GLY C 140      -5.325   4.131  20.465  1.00113.92           O  
ANISOU 1762  O   GLY C 140    17675  15175  10434  -6417    650    162       O  
ATOM   1763  N   GLY C 141      -3.329   5.012  20.963  1.00103.93           N  
ANISOU 1763  N   GLY C 141    16692  13005   9790  -4954    558   1003       N  
ATOM   1764  CA  GLY C 141      -2.255   5.998  20.765  1.00 99.83           C  
ANISOU 1764  CA  GLY C 141    16087  12381   9462  -4328    167   1489       C  
ATOM   1765  C   GLY C 141      -0.966   5.566  21.447  1.00 97.05           C  
ANISOU 1765  C   GLY C 141    16077  11658   9138  -3799    753   1770       C  
ATOM   1766  O   GLY C 141      -0.676   4.371  21.536  1.00 99.52           O  
ANISOU 1766  O   GLY C 141    17042  11608   9162  -3773   1523   1682       O  
ATOM   1767  N   SER C 142      -0.192   6.537  21.921  1.00 93.89           N  
ANISOU 1767  N   SER C 142    15326  11419   8927  -3364    427   2100       N  
ATOM   1768  CA  SER C 142       1.108   6.264  22.538  1.00 93.05           C  
ANISOU 1768  CA  SER C 142    15247  11427   8679  -2834    881   2378       C  
ATOM   1769  C   SER C 142       0.935   5.674  23.918  1.00 92.23           C  
ANISOU 1769  C   SER C 142    15143  11147   8753  -2399   1298   2315       C  
ATOM   1770  O   SER C 142      -0.085   5.893  24.579  1.00 91.42           O  
ANISOU 1770  O   SER C 142    14831  10900   9003  -2568   1082   2096       O  
ATOM   1771  CB  SER C 142       1.934   7.548  22.667  1.00 91.65           C  
ANISOU 1771  CB  SER C 142    14665  11681   8476  -2844    413   2661       C  
ATOM   1772  OG  SER C 142       1.391   8.595  21.879  1.00 92.15           O  
ANISOU 1772  OG  SER C 142    14815  11627   8570  -3287   -244   2647       O  
ATOM   1773  N   GLY C 143       1.944   4.931  24.355  1.00 93.80           N  
ANISOU 1773  N   GLY C 143    15569  11459   8610  -1733   1909   2519       N  
ATOM   1774  CA  GLY C 143       1.987   4.440  25.730  1.00 93.69           C  
ANISOU 1774  CA  GLY C 143    15621  11330   8643  -1148   2306   2552       C  
ATOM   1775  C   GLY C 143       2.319   5.588  26.663  1.00 90.15           C  
ANISOU 1775  C   GLY C 143    14349  11422   8479  -1074   1794   2717       C  
ATOM   1776  O   GLY C 143       1.990   5.580  27.849  1.00 88.97           O  
ANISOU 1776  O   GLY C 143    14084  11156   8565   -860   1853   2673       O  
ATOM   1777  N   MET C 144       2.967   6.594  26.110  1.00 89.37           N  
ANISOU 1777  N   MET C 144    13811  11873   8269  -1389   1333   2878       N  
ATOM   1778  CA  MET C 144       3.428   7.693  26.913  1.00 88.00           C  
ANISOU 1778  CA  MET C 144    13098  12207   8130  -1545    956   3007       C  
ATOM   1779  C   MET C 144       2.282   8.639  27.257  1.00 85.26           C  
ANISOU 1779  C   MET C 144    12805  11283   8305  -1956    419   2824       C  
ATOM   1780  O   MET C 144       2.259   9.195  28.353  1.00 84.07           O  
ANISOU 1780  O   MET C 144    12449  11195   8296  -1915    301   2838       O  
ATOM   1781  CB  MET C 144       4.519   8.438  26.171  1.00 90.65           C  
ANISOU 1781  CB  MET C 144    13163  13322   7955  -1989    757   3180       C  
ATOM   1782  CG  MET C 144       5.196   9.496  27.019  1.00 91.77           C  
ANISOU 1782  CG  MET C 144    12867  14157   7845  -2410    518   3270       C  
ATOM   1783  SD  MET C 144       6.997   9.350  27.045  1.00 98.56           S  
ANISOU 1783  SD  MET C 144    12886  16862   7697  -2351    851   3479       S  
ATOM   1784  CE  MET C 144       7.456  10.758  28.042  1.00100.44           C  
ANISOU 1784  CE  MET C 144    12811  17758   7593  -3390    518   3438       C  
ATOM   1785  N   LYS C 145       1.351   8.840  26.320  1.00 85.18           N  
ANISOU 1785  N   LYS C 145    13063  10828   8473  -2260    103   2661       N  
ATOM   1786  CA  LYS C 145       0.142   9.597  26.608  1.00 84.49           C  
ANISOU 1786  CA  LYS C 145    12977  10383   8740  -2307   -358   2485       C  
ATOM   1787  C   LYS C 145      -0.639   8.849  27.687  1.00 83.38           C  
ANISOU 1787  C   LYS C 145    12644  10107   8928  -2034    -45   2255       C  
ATOM   1788  O   LYS C 145      -1.097   9.449  28.664  1.00 82.55           O  
ANISOU 1788  O   LYS C 145    12370   9926   9069  -1869   -224   2196       O  
ATOM   1789  CB  LYS C 145      -0.704   9.788  25.349  1.00 86.62           C  
ANISOU 1789  CB  LYS C 145    13423  10536   8953  -2508   -733   2361       C  
ATOM   1790  N   GLN C 146      -0.763   7.536  27.518  1.00 84.28           N  
ANISOU 1790  N   GLN C 146    12957  10122   8944  -2042    495   2113       N  
ATOM   1791  CA  GLN C 146      -1.410   6.690  28.513  1.00 84.62           C  
ANISOU 1791  CA  GLN C 146    13080   9949   9120  -1962    946   1874       C  
ATOM   1792  C   GLN C 146      -0.917   7.047  29.922  1.00 82.40           C  
ANISOU 1792  C   GLN C 146    12580   9733   8994  -1529   1003   2045       C  
ATOM   1793  O   GLN C 146      -1.724   7.319  30.830  1.00 81.71           O  
ANISOU 1793  O   GLN C 146    12273   9569   9202  -1533    907   1851       O  
ATOM   1794  CB  GLN C 146      -1.146   5.208  28.196  1.00 87.73           C  
ANISOU 1794  CB  GLN C 146    14199  10018   9114  -1971   1723   1809       C  
ATOM   1795  CG  GLN C 146      -1.847   4.684  26.928  1.00 90.84           C  
ANISOU 1795  CG  GLN C 146    14931  10315   9268  -2654   1785   1515       C  
ATOM   1796  N   LEU C 147       0.407   7.066  30.085  1.00 82.23           N  
ANISOU 1796  N   LEU C 147    12528  10035   8679  -1178   1153   2386       N  
ATOM   1797  CA  LEU C 147       1.039   7.359  31.378  1.00 81.40           C  
ANISOU 1797  CA  LEU C 147    12135  10253   8537   -826   1216   2562       C  
ATOM   1798  C   LEU C 147       0.767   8.792  31.796  1.00 79.74           C  
ANISOU 1798  C   LEU C 147    11641  10077   8577  -1182    633   2534       C  
ATOM   1799  O   LEU C 147       0.253   9.042  32.879  1.00 78.91           O  
ANISOU 1799  O   LEU C 147    11447   9803   8730  -1092    612   2423       O  
ATOM   1800  CB  LEU C 147       2.554   7.103  31.336  1.00 83.87           C  
ANISOU 1800  CB  LEU C 147    12251  11360   8254   -391   1466   2908       C  
ATOM   1801  CG  LEU C 147       3.017   5.644  31.212  1.00 87.69           C  
ANISOU 1801  CG  LEU C 147    13229  11812   8276    414   2189   3030       C  
ATOM   1802  CD1 LEU C 147       4.452   5.595  30.732  1.00 91.57           C  
ANISOU 1802  CD1 LEU C 147    13328  13389   8074    887   2304   3349       C  
ATOM   1803  CD2 LEU C 147       2.869   4.858  32.526  1.00 88.79           C  
ANISOU 1803  CD2 LEU C 147    13712  11693   8330   1083   2677   3055       C  
ATOM   1804  N   GLU C 148       1.099   9.729  30.923  1.00 80.59           N  
ANISOU 1804  N   GLU C 148    11798  10305   8517  -1587    221   2628       N  
ATOM   1805  CA  GLU C 148       0.857  11.140  31.192  1.00 81.14           C  
ANISOU 1805  CA  GLU C 148    12050  10160   8619  -1908   -242   2616       C  
ATOM   1806  C   GLU C 148      -0.554  11.343  31.718  1.00 80.45           C  
ANISOU 1806  C   GLU C 148    12007   9570   8988  -1607   -402   2364       C  
ATOM   1807  O   GLU C 148      -0.747  11.961  32.756  1.00 80.56           O  
ANISOU 1807  O   GLU C 148    12077   9438   9094  -1528   -460   2325       O  
ATOM   1808  CB  GLU C 148       1.081  11.980  29.934  1.00 83.55           C  
ANISOU 1808  CB  GLU C 148    12773  10358   8612  -2353   -604   2707       C  
ATOM   1809  CG  GLU C 148       2.512  12.451  29.782  1.00 86.19           C  
ANISOU 1809  CG  GLU C 148    13102  11331   8315  -2973   -540   2903       C  
ATOM   1810  CD  GLU C 148       2.799  13.069  28.426  1.00 89.25           C  
ANISOU 1810  CD  GLU C 148    13994  11610   8307  -3517   -783   2977       C  
ATOM   1811  OE1 GLU C 148       1.889  13.099  27.570  1.00 89.08           O  
ANISOU 1811  OE1 GLU C 148    14321  11007   8519  -3268  -1037   2918       O  
ATOM   1812  OE2 GLU C 148       3.946  13.522  28.215  1.00 92.99           O  
ANISOU 1812  OE2 GLU C 148    14477  12724   8130  -4257   -709   3076       O  
ATOM   1813  N   ASP C 149      -1.530  10.791  31.006  1.00 80.96           N  
ANISOU 1813  N   ASP C 149    11988   9534   9237  -1487   -440   2161       N  
ATOM   1814  CA  ASP C 149      -2.937  10.896  31.396  1.00 82.26           C  
ANISOU 1814  CA  ASP C 149    11933   9645   9676  -1218   -582   1858       C  
ATOM   1815  C   ASP C 149      -3.225  10.188  32.727  1.00 80.72           C  
ANISOU 1815  C   ASP C 149    11485   9466   9720  -1126   -151   1681       C  
ATOM   1816  O   ASP C 149      -4.060  10.654  33.516  1.00 81.76           O  
ANISOU 1816  O   ASP C 149    11429   9605  10031   -882   -262   1493       O  
ATOM   1817  CB  ASP C 149      -3.843  10.322  30.296  1.00 84.89           C  
ANISOU 1817  CB  ASP C 149    12059  10247   9947  -1343   -668   1621       C  
ATOM   1818  CG  ASP C 149      -3.816  11.144  29.008  1.00 87.43           C  
ANISOU 1818  CG  ASP C 149    12654  10567   9996  -1294  -1177   1781       C  
ATOM   1819  OD1 ASP C 149      -3.142  12.191  28.955  1.00 87.68           O  
ANISOU 1819  OD1 ASP C 149    13200  10258   9854  -1224  -1421   2057       O  
ATOM   1820  OD2 ASP C 149      -4.472  10.727  28.032  1.00 90.42           O  
ANISOU 1820  OD2 ASP C 149    12827  11300  10226  -1431  -1296   1610       O  
ATOM   1821  N   LYS C 150      -2.547   9.068  32.970  1.00 79.24           N  
ANISOU 1821  N   LYS C 150    11394   9273   9440  -1215    373   1751       N  
ATOM   1822  CA  LYS C 150      -2.748   8.333  34.209  1.00 78.81           C  
ANISOU 1822  CA  LYS C 150    11342   9118   9483  -1100    845   1624       C  
ATOM   1823  C   LYS C 150      -2.188   9.095  35.407  1.00 77.26           C  
ANISOU 1823  C   LYS C 150    11049   8960   9344   -873    747   1805       C  
ATOM   1824  O   LYS C 150      -2.786   9.085  36.480  1.00 77.33           O  
ANISOU 1824  O   LYS C 150    10964   8872   9546   -785    879   1625       O  
ATOM   1825  CB  LYS C 150      -2.143   6.932  34.132  1.00 79.81           C  
ANISOU 1825  CB  LYS C 150    11931   9096   9297  -1025   1502   1709       C  
ATOM   1826  CG  LYS C 150      -2.550   5.997  35.295  1.00 81.26           C  
ANISOU 1826  CG  LYS C 150    12460   8981   9434   -958   2101   1533       C  
ATOM   1827  CD  LYS C 150      -4.056   6.030  35.610  1.00 82.82           C  
ANISOU 1827  CD  LYS C 150    12400   9204   9861  -1483   2075   1029       C  
ATOM   1828  CE  LYS C 150      -4.534   4.800  36.395  1.00 85.80           C  
ANISOU 1828  CE  LYS C 150    13425   9198   9975  -1792   2849    755       C  
ATOM   1829  N   VAL C 151      -1.049   9.755  35.229  1.00 76.98           N  
ANISOU 1829  N   VAL C 151    11038   9163   9047   -921    547   2117       N  
ATOM   1830  CA  VAL C 151      -0.458  10.563  36.301  1.00 77.03           C  
ANISOU 1830  CA  VAL C 151    10993   9345   8928   -981    455   2243       C  
ATOM   1831  C   VAL C 151      -1.421  11.697  36.668  1.00 77.80           C  
ANISOU 1831  C   VAL C 151    11293   8999   9268  -1009    114   2048       C  
ATOM   1832  O   VAL C 151      -1.768  11.885  37.842  1.00 77.21           O  
ANISOU 1832  O   VAL C 151    11191   8810   9334   -886    218   1937       O  
ATOM   1833  CB  VAL C 151       0.909  11.135  35.886  1.00 78.77           C  
ANISOU 1833  CB  VAL C 151    11178  10141   8609  -1356    317   2523       C  
ATOM   1834  CG1 VAL C 151       1.398  12.132  36.904  1.00 80.63           C  
ANISOU 1834  CG1 VAL C 151    11472  10598   8566  -1759    206   2558       C  
ATOM   1835  CG2 VAL C 151       1.914  10.022  35.738  1.00 79.76           C  
ANISOU 1835  CG2 VAL C 151    10986  10964   8353  -1007    702   2739       C  
ATOM   1836  N   GLU C 152      -1.838  12.445  35.642  1.00 79.76           N  
ANISOU 1836  N   GLU C 152    11829   9003   9472  -1044   -266   2029       N  
ATOM   1837  CA  GLU C 152      -2.861  13.497  35.780  1.00 82.79           C  
ANISOU 1837  CA  GLU C 152    12554   8977   9922   -695   -575   1880       C  
ATOM   1838  C   GLU C 152      -4.040  13.001  36.599  1.00 82.52           C  
ANISOU 1838  C   GLU C 152    12032   9065  10255   -277   -408   1562       C  
ATOM   1839  O   GLU C 152      -4.492  13.659  37.531  1.00 84.25           O  
ANISOU 1839  O   GLU C 152    12414   9083  10513     15   -418   1459       O  
ATOM   1840  CB  GLU C 152      -3.361  13.975  34.406  1.00 85.90           C  
ANISOU 1840  CB  GLU C 152    13227   9253  10155   -482   -962   1902       C  
ATOM   1841  N   GLU C 153      -4.522  11.823  36.253  1.00 81.51           N  
ANISOU 1841  N   GLU C 153    11397   9279  10293   -362   -188   1373       N  
ATOM   1842  CA  GLU C 153      -5.663  11.259  36.943  1.00 82.99           C  
ANISOU 1842  CA  GLU C 153    11106   9749  10675   -258     44    990       C  
ATOM   1843  C   GLU C 153      -5.365  11.020  38.416  1.00 80.91           C  
ANISOU 1843  C   GLU C 153    10902   9300  10538   -302    415    982       C  
ATOM   1844  O   GLU C 153      -6.149  11.392  39.288  1.00 82.74           O  
ANISOU 1844  O   GLU C 153    10954   9599  10883    -57    441    752       O  
ATOM   1845  CB  GLU C 153      -6.067   9.940  36.304  1.00 83.79           C  
ANISOU 1845  CB  GLU C 153    10941  10171  10722   -710    359    756       C  
ATOM   1846  CG  GLU C 153      -7.377   9.390  36.843  1.00 87.66           C  
ANISOU 1846  CG  GLU C 153    10910  11182  11213   -919    617    250       C  
ATOM   1847  CD  GLU C 153      -7.585   7.929  36.495  1.00 89.77           C  
ANISOU 1847  CD  GLU C 153    11321  11538  11247  -1721   1172    -16       C  
ATOM   1848  OE1 GLU C 153      -7.364   7.562  35.313  1.00 90.36           O  
ANISOU 1848  OE1 GLU C 153    11562  11643  11128  -1999   1119     38       O  
ATOM   1849  OE2 GLU C 153      -7.972   7.156  37.411  1.00 91.48           O  
ANISOU 1849  OE2 GLU C 153    11653  11714  11390  -2132   1716   -295       O  
ATOM   1850  N   LEU C 154      -4.230  10.390  38.680  1.00 78.14           N  
ANISOU 1850  N   LEU C 154    10776   8830  10081   -510    709   1241       N  
ATOM   1851  CA  LEU C 154      -3.842  10.053  40.041  1.00 76.90           C  
ANISOU 1851  CA  LEU C 154    10690   8608   9919   -473   1063   1288       C  
ATOM   1852  C   LEU C 154      -3.541  11.319  40.845  1.00 77.07           C  
ANISOU 1852  C   LEU C 154    10855   8523   9903   -413    802   1387       C  
ATOM   1853  O   LEU C 154      -4.056  11.467  41.937  1.00 77.64           O  
ANISOU 1853  O   LEU C 154    10895   8499  10103   -310    944   1210       O  
ATOM   1854  CB  LEU C 154      -2.635   9.097  40.036  1.00 76.19           C  
ANISOU 1854  CB  LEU C 154    10792   8640   9514   -422   1414   1603       C  
ATOM   1855  CG  LEU C 154      -2.888   7.652  39.561  1.00 77.30           C  
ANISOU 1855  CG  LEU C 154    11243   8605   9520   -441   1923   1499       C  
ATOM   1856  CD1 LEU C 154      -1.591   6.862  39.455  1.00 78.07           C  
ANISOU 1856  CD1 LEU C 154    11672   8846   9143    -10   2257   1895       C  
ATOM   1857  CD2 LEU C 154      -3.842   6.933  40.491  1.00 79.02           C  
ANISOU 1857  CD2 LEU C 154    11660   8563   9800   -611   2391   1154       C  
ATOM   1858  N   LEU C 155      -2.719  12.224  40.305  1.00 77.66           N  
ANISOU 1858  N   LEU C 155    11213   8588   9706   -604    483   1631       N  
ATOM   1859  CA  LEU C 155      -2.433  13.501  40.970  1.00 79.74           C  
ANISOU 1859  CA  LEU C 155    11950   8614   9733   -794    313   1676       C  
ATOM   1860  C   LEU C 155      -3.717  14.117  41.486  1.00 82.01           C  
ANISOU 1860  C   LEU C 155    12420   8486  10252   -316    256   1392       C  
ATOM   1861  O   LEU C 155      -3.778  14.603  42.617  1.00 83.38           O  
ANISOU 1861  O   LEU C 155    12848   8463  10368   -327    380   1315       O  
ATOM   1862  CB  LEU C 155      -1.762  14.488  40.012  1.00 82.37           C  
ANISOU 1862  CB  LEU C 155    12858   8806   9633  -1201      5   1861       C  
ATOM   1863  CG  LEU C 155      -0.233  14.612  40.040  1.00 83.41           C  
ANISOU 1863  CG  LEU C 155    12973   9539   9179  -1975     55   2100       C  
ATOM   1864  CD1 LEU C 155       0.326  14.888  38.640  1.00 85.22           C  
ANISOU 1864  CD1 LEU C 155    13429   9869   9081  -2353   -151   2248       C  
ATOM   1865  CD2 LEU C 155       0.208  15.711  41.002  1.00 87.30           C  
ANISOU 1865  CD2 LEU C 155    14088   9908   9172  -2623     82   2063       C  
ATOM   1866  N   SER C 156      -4.741  14.092  40.642  1.00 83.65           N  
ANISOU 1866  N   SER C 156    12438   8717  10626    149     75   1227       N  
ATOM   1867  CA  SER C 156      -5.998  14.766  40.940  1.00 88.19           C  
ANISOU 1867  CA  SER C 156    13059   9210  11240    866    -27    970       C  
ATOM   1868  C   SER C 156      -6.782  14.027  42.014  1.00 87.57           C  
ANISOU 1868  C   SER C 156    12315   9505  11450    946    318    640       C  
ATOM   1869  O   SER C 156      -7.186  14.626  43.016  1.00 89.91           O  
ANISOU 1869  O   SER C 156    12822   9618  11720   1269    420    508       O  
ATOM   1870  CB  SER C 156      -6.827  14.931  39.664  1.00 91.91           C  
ANISOU 1870  CB  SER C 156    13327   9976  11616   1416   -364    900       C  
ATOM   1871  OG  SER C 156      -7.721  16.024  39.777  1.00 99.00           O  
ANISOU 1871  OG  SER C 156    14624  10748  12244   2404   -557    811       O  
ATOM   1872  N   LYS C 157      -6.976  12.727  41.808  1.00 85.37           N  
ANISOU 1872  N   LYS C 157    11412   9675  11350    571    568    492       N  
ATOM   1873  CA  LYS C 157      -7.573  11.854  42.835  1.00 85.43           C  
ANISOU 1873  CA  LYS C 157    11009   9949  11501    351   1024    173       C  
ATOM   1874  C   LYS C 157      -6.876  11.995  44.196  1.00 83.07           C  
ANISOU 1874  C   LYS C 157    11099   9242  11218    236   1264    316       C  
ATOM   1875  O   LYS C 157      -7.519  11.957  45.241  1.00 84.71           O  
ANISOU 1875  O   LYS C 157    11155   9531  11497    303   1515     52       O  
ATOM   1876  CB  LYS C 157      -7.509  10.387  42.419  1.00 84.11           C  
ANISOU 1876  CB  LYS C 157    10682   9966  11307   -243   1399     81       C  
ATOM   1877  CG  LYS C 157      -8.541   9.942  41.390  1.00 88.25           C  
ANISOU 1877  CG  LYS C 157    10660  11157  11713   -456   1346   -273       C  
ATOM   1878  CD  LYS C 157      -8.670   8.405  41.359  1.00 88.84           C  
ANISOU 1878  CD  LYS C 157    10898  11259  11597  -1299   1962   -509       C  
ATOM   1879  CE  LYS C 157      -8.956   7.820  42.759  1.00 89.65           C  
ANISOU 1879  CE  LYS C 157    11189  11213  11661  -1613   2531   -740       C  
ATOM   1880  NZ  LYS C 157      -9.668   6.499  42.747  1.00 94.96           N  
ANISOU 1880  NZ  LYS C 157    12055  12088  11935  -2614   3191  -1207       N  
ATOM   1881  N   ASN C 158      -5.559  12.167  44.157  1.00 80.28           N  
ANISOU 1881  N   ASN C 158    11164   8633  10704     18   1182    713       N  
ATOM   1882  CA  ASN C 158      -4.729  12.301  45.355  1.00 79.16           C  
ANISOU 1882  CA  ASN C 158    11285   8388  10402   -174   1355    882       C  
ATOM   1883  C   ASN C 158      -5.021  13.551  46.157  1.00 81.89           C  
ANISOU 1883  C   ASN C 158    12036   8408  10668    -57   1246    775       C  
ATOM   1884  O   ASN C 158      -5.347  13.485  47.341  1.00 82.36           O  
ANISOU 1884  O   ASN C 158    12085   8424  10782    -35   1504    612       O  
ATOM   1885  CB  ASN C 158      -3.256  12.358  44.965  1.00 77.99           C  
ANISOU 1885  CB  ASN C 158    11288   8458   9887   -485   1226   1287       C  
ATOM   1886  CG  ASN C 158      -2.395  11.481  45.827  1.00 77.34           C  
ANISOU 1886  CG  ASN C 158    11066   8772   9548   -511   1549   1490       C  
ATOM   1887  OD1 ASN C 158      -2.829  10.428  46.300  1.00 77.05           O  
ANISOU 1887  OD1 ASN C 158    10991   8656   9628   -285   1937   1389       O  
ATOM   1888  ND2 ASN C 158      -1.147  11.891  46.011  1.00 78.90           N  
ANISOU 1888  ND2 ASN C 158    11234   9504   9237   -802   1422   1772       N  
ATOM   1889  N   TYR C 159      -4.859  14.696  45.504  1.00 84.51           N  
ANISOU 1889  N   TYR C 159    12928   8411  10769     -1    919    876       N  
ATOM   1890  CA  TYR C 159      -5.139  15.979  46.124  1.00 89.07           C  
ANISOU 1890  CA  TYR C 159    14317   8434  11089    180    889    785       C  
ATOM   1891  C   TYR C 159      -6.509  15.899  46.788  1.00 91.38           C  
ANISOU 1891  C   TYR C 159    14254   8805  11660    899   1068    422       C  
ATOM   1892  O   TYR C 159      -6.648  16.200  47.972  1.00 92.85           O  
ANISOU 1892  O   TYR C 159    14696   8794  11787    889   1304    290       O  
ATOM   1893  CB  TYR C 159      -5.072  17.106  45.075  1.00 93.51           C  
ANISOU 1893  CB  TYR C 159    15792   8467  11269    358    583    916       C  
ATOM   1894  CG  TYR C 159      -5.670  18.454  45.487  1.00100.82           C  
ANISOU 1894  CG  TYR C 159    17923   8587  11797    938    623    806       C  
ATOM   1895  CD1 TYR C 159      -5.171  19.172  46.580  1.00103.75           C  
ANISOU 1895  CD1 TYR C 159    19223   8442  11754    388    870    780       C  
ATOM   1896  CD2 TYR C 159      -6.713  19.019  44.760  1.00106.24           C  
ANISOU 1896  CD2 TYR C 159    18927   9065  12372   2111    443    739       C  
ATOM   1897  CE1 TYR C 159      -5.717  20.406  46.941  1.00111.75           C  
ANISOU 1897  CE1 TYR C 159    21662   8522  12273    987   1010    679       C  
ATOM   1898  CE2 TYR C 159      -7.260  20.243  45.115  1.00114.94           C  
ANISOU 1898  CE2 TYR C 159    21355   9363  12951   2954    548    684       C  
ATOM   1899  CZ  TYR C 159      -6.761  20.930  46.200  1.00117.53           C  
ANISOU 1899  CZ  TYR C 159    22810   8955  12891   2382    867    651       C  
ATOM   1900  OH  TYR C 159      -7.318  22.137  46.535  1.00127.26           O  
ANISOU 1900  OH  TYR C 159    25643   9218  13492   3298   1066    593       O  
ATOM   1901  N   HIS C 160      -7.505  15.451  46.029  1.00 92.57           N  
ANISOU 1901  N   HIS C 160    13717   9426  12029   1428    975    227       N  
ATOM   1902  CA  HIS C 160      -8.884  15.383  46.525  1.00 96.91           C  
ANISOU 1902  CA  HIS C 160    13674  10467  12678   2080   1134   -185       C  
ATOM   1903  C   HIS C 160      -9.029  14.420  47.712  1.00 94.16           C  
ANISOU 1903  C   HIS C 160    12826  10393  12557   1554   1585   -414       C  
ATOM   1904  O   HIS C 160      -9.791  14.694  48.651  1.00 97.56           O  
ANISOU 1904  O   HIS C 160    13135  10970  12962   1899   1808   -707       O  
ATOM   1905  CB  HIS C 160      -9.843  14.995  45.393  1.00100.14           C  
ANISOU 1905  CB  HIS C 160    13237  11720  13093   2507    932   -386       C  
ATOM   1906  N   LEU C 161      -8.296  13.303  47.656  1.00 88.95           N  
ANISOU 1906  N   LEU C 161    12003   9771  12020    821   1757   -265       N  
ATOM   1907  CA ALEU C 161      -8.303  12.326  48.743  0.50 87.24           C  
ANISOU 1907  CA ALEU C 161    11641   9635  11871    362   2236   -403       C  
ATOM   1908  CA BLEU C 161      -8.276  12.316  48.743  0.50 87.18           C  
ANISOU 1908  CA BLEU C 161    11642   9619  11862    353   2236   -394       C  
ATOM   1909  C   LEU C 161      -7.662  12.912  50.006  1.00 86.53           C  
ANISOU 1909  C   LEU C 161    12094   9117  11665    295   2331   -255       C  
ATOM   1910  O   LEU C 161      -8.180  12.734  51.104  1.00 88.03           O  
ANISOU 1910  O   LEU C 161    12213   9354  11879    251   2664   -506       O  
ATOM   1911  CB ALEU C 161      -7.609  11.028  48.308  0.50 83.84           C  
ANISOU 1911  CB ALEU C 161    11244   9208  11400   -127   2446   -205       C  
ATOM   1912  CB BLEU C 161      -7.506  11.045  48.341  0.50 83.65           C  
ANISOU 1912  CB BLEU C 161    11261   9154  11368   -130   2440   -171       C  
ATOM   1913  CG ALEU C 161      -7.736   9.796  49.214  0.50 83.81           C  
ANISOU 1913  CG ALEU C 161    11383   9166  11294   -533   3045   -348       C  
ATOM   1914  CG BLEU C 161      -8.308   9.885  47.734  0.50 85.40           C  
ANISOU 1914  CG BLEU C 161    11142   9732  11571   -498   2746   -492       C  
ATOM   1915  CD1ALEU C 161      -9.152   9.622  49.749  0.50 87.86           C  
ANISOU 1915  CD1ALEU C 161    11458  10086  11837   -743   3361   -931       C  
ATOM   1916  CD1BLEU C 161      -7.423   8.659  47.517  0.50 82.49           C  
ANISOU 1916  CD1BLEU C 161    11302   9045  10994   -803   3086   -214       C  
ATOM   1917  CD2ALEU C 161      -7.276   8.544  48.465  0.50 82.24           C  
ANISOU 1917  CD2ALEU C 161    11489   8857  10901   -804   3309   -192       C  
ATOM   1918  CD2BLEU C 161      -9.471   9.533  48.647  0.50 89.74           C  
ANISOU 1918  CD2BLEU C 161    11372  10643  12079   -775   3173  -1013       C  
ATOM   1919  N   GLU C 162      -6.548  13.620  49.845  1.00 85.32           N  
ANISOU 1919  N   GLU C 162    12477   8652  11289    147   2065    109       N  
ATOM   1920  CA  GLU C 162      -5.899  14.290  50.979  1.00 86.24           C  
ANISOU 1920  CA  GLU C 162    13137   8508  11119   -133   2138    209       C  
ATOM   1921  C   GLU C 162      -6.826  15.267  51.707  1.00 90.83           C  
ANISOU 1921  C   GLU C 162    14112   8721  11676    276   2242   -103       C  
ATOM   1922  O   GLU C 162      -6.857  15.288  52.932  1.00 91.51           O  
ANISOU 1922  O   GLU C 162    14351   8730  11685    103   2514   -218       O  
ATOM   1923  CB  GLU C 162      -4.630  15.015  50.532  1.00 86.49           C  
ANISOU 1923  CB  GLU C 162    13676   8473  10711   -615   1852    551       C  
ATOM   1924  CG  GLU C 162      -3.368  14.292  50.931  1.00 84.45           C  
ANISOU 1924  CG  GLU C 162    13120   8831  10134  -1104   1917    856       C  
ATOM   1925  CD  GLU C 162      -2.181  14.680  50.099  1.00 85.69           C  
ANISOU 1925  CD  GLU C 162    13358   9374   9824  -1606   1634   1149       C  
ATOM   1926  OE1 GLU C 162      -2.246  15.714  49.386  1.00 88.31           O  
ANISOU 1926  OE1 GLU C 162    14298   9251  10004  -1810   1419   1111       O  
ATOM   1927  OE2 GLU C 162      -1.170  13.945  50.169  1.00 85.32           O  
ANISOU 1927  OE2 GLU C 162    12819  10151   9446  -1742   1662   1421       O  
ATOM   1928  N   ASN C 163      -7.571  16.071  50.948  1.00 94.94           N  
ANISOU 1928  N   ASN C 163    14855   9045  12172    950   2044   -221       N  
ATOM   1929  CA  ASN C 163      -8.492  17.066  51.526  1.00101.50           C  
ANISOU 1929  CA  ASN C 163    16189   9550  12824   1708   2173   -489       C  
ATOM   1930  C   ASN C 163      -9.569  16.399  52.376  1.00102.58           C  
ANISOU 1930  C   ASN C 163    15465  10291  13218   1974   2521   -898       C  
ATOM   1931  O   ASN C 163      -9.965  16.912  53.423  1.00106.13           O  
ANISOU 1931  O   ASN C 163    16278  10524  13521   2230   2789  -1101       O  
ATOM   1932  CB  ASN C 163      -9.160  17.905  50.424  1.00107.38           C  
ANISOU 1932  CB  ASN C 163    17274  10164  13359   2731   1897   -492       C  
ATOM   1933  CG  ASN C 163      -8.176  18.795  49.663  1.00108.58           C  
ANISOU 1933  CG  ASN C 163    18674   9503  13078   2420   1645   -133       C  
ATOM   1934  OD1 ASN C 163      -6.960  18.627  49.748  1.00104.46           O  
ANISOU 1934  OD1 ASN C 163    18393   8845  12449   1308   1616     98       O  
ATOM   1935  ND2 ASN C 163      -8.712  19.746  48.907  1.00115.74           N  
ANISOU 1935  ND2 ASN C 163    20391   9986  13598   3434   1486    -95       N  
ATOM   1936  N   GLU C 164     -10.040  15.255  51.892  1.00100.37           N  
ANISOU 1936  N   GLU C 164    14141  10773  13221   1794   2567  -1053       N  
ATOM   1937  CA  GLU C 164     -11.021  14.438  52.596  1.00102.36           C  
ANISOU 1937  CA  GLU C 164    13572  11733  13587   1665   2971  -1498       C  
ATOM   1938  C   GLU C 164     -10.467  13.993  53.958  1.00 99.32           C  
ANISOU 1938  C   GLU C 164    13553  10967  13217    995   3345  -1460       C  
ATOM   1939  O   GLU C 164     -11.158  14.063  54.981  1.00102.73           O  
ANISOU 1939  O   GLU C 164    13860  11577  13595   1083   3687  -1796       O  
ATOM   1940  CB  GLU C 164     -11.381  13.217  51.722  1.00101.23           C  
ANISOU 1940  CB  GLU C 164    12594  12312  13555   1179   3019  -1648       C  
ATOM   1941  CG  GLU C 164     -12.857  12.760  51.610  1.00108.18           C  
ANISOU 1941  CG  GLU C 164    12360  14452  14292   1228   3247  -2251       C  
ATOM   1942  CD  GLU C 164     -13.873  13.608  52.342  1.00115.71           C  
ANISOU 1942  CD  GLU C 164    12955  15973  15035   2091   3358  -2616       C  
ATOM   1943  OE1 GLU C 164     -13.486  14.448  53.225  1.00115.45           O  
ANISOU 1943  OE1 GLU C 164    13748  15113  15004   2516   3403  -2451       O  
ATOM   1944  OE2 GLU C 164     -15.099  13.435  52.051  1.00123.49           O  
ANISOU 1944  OE2 GLU C 164    12790  18391  15737   2339   3436  -3110       O  
ATOM   1945  N   VAL C 165      -9.216  13.538  53.948  1.00 93.90           N  
ANISOU 1945  N   VAL C 165    13267   9898  12513    415   3276  -1045       N  
ATOM   1946  CA  VAL C 165      -8.501  13.140  55.161  1.00 91.86           C  
ANISOU 1946  CA  VAL C 165    13376   9412  12111    -76   3547   -901       C  
ATOM   1947  C   VAL C 165      -8.438  14.315  56.143  1.00 94.77           C  
ANISOU 1947  C   VAL C 165    14349   9386  12274     37   3566   -958       C  
ATOM   1948  O   VAL C 165      -8.972  14.234  57.249  1.00 96.94           O  
ANISOU 1948  O   VAL C 165    14632   9675  12523      0   3921  -1229       O  
ATOM   1949  CB  VAL C 165      -7.052  12.658  54.834  1.00 87.85           C  
ANISOU 1949  CB  VAL C 165    13094   8873  11410   -428   3370   -383       C  
ATOM   1950  CG1 VAL C 165      -6.246  12.410  56.115  1.00 87.70           C  
ANISOU 1950  CG1 VAL C 165    13396   8873  11052   -740   3570   -186       C  
ATOM   1951  CG2 VAL C 165      -7.074  11.407  53.947  1.00 85.76           C  
ANISOU 1951  CG2 VAL C 165    12516   8823  11245   -482   3477   -316       C  
ATOM   1952  N   ALA C 166      -7.804  15.407  55.727  1.00 95.79           N  
ANISOU 1952  N   ALA C 166    15128   9106  12159     78   3245   -736       N  
ATOM   1953  CA  ALA C 166      -7.711  16.609  56.558  1.00100.29           C  
ANISOU 1953  CA  ALA C 166    16635   9115  12355     55   3336   -811       C  
ATOM   1954  C   ALA C 166      -9.079  17.008  57.111  1.00105.62           C  
ANISOU 1954  C   ALA C 166    17279   9732  13117    853   3634  -1256       C  
ATOM   1955  O   ALA C 166      -9.197  17.369  58.280  1.00108.28           O  
ANISOU 1955  O   ALA C 166    18074   9809  13256    738   3937  -1421       O  
ATOM   1956  CB  ALA C 166      -7.112  17.764  55.767  1.00103.16           C  
ANISOU 1956  CB  ALA C 166    17958   8922  12314    -12   3042   -604       C  
ATOM   1957  N   ARG C 167     -10.102  16.929  56.261  1.00108.13           N  
ANISOU 1957  N   ARG C 167    16967  10476  13640   1675   3552  -1460       N  
ATOM   1958  CA  ARG C 167     -11.481  17.271  56.638  1.00115.17           C  
ANISOU 1958  CA  ARG C 167    17510  11773  14477   2636   3812  -1910       C  
ATOM   1959  C   ARG C 167     -11.996  16.389  57.784  1.00114.83           C  
ANISOU 1959  C   ARG C 167    16771  12269  14587   2159   4267  -2257       C  
ATOM   1960  O   ARG C 167     -12.711  16.867  58.679  1.00120.33           O  
ANISOU 1960  O   ARG C 167    17585  13032  15100   2632   4597  -2581       O  
ATOM   1961  CB  ARG C 167     -12.405  17.169  55.419  1.00118.66           C  
ANISOU 1961  CB  ARG C 167    17067  13046  14972   3499   3580  -2058       C  
ATOM   1962  CG  ARG C 167     -13.758  17.824  55.609  1.00128.87           C  
ANISOU 1962  CG  ARG C 167    18013  15006  15946   4873   3754  -2461       C  
ATOM   1963  CD  ARG C 167     -14.714  17.490  54.472  1.00133.33           C  
ANISOU 1963  CD  ARG C 167    17282  16928  16448   5576   3519  -2666       C  
ATOM   1964  NE  ARG C 167     -14.864  16.051  54.281  1.00128.52           N  
ANISOU 1964  NE  ARG C 167    15426  17247  16156   4360   3621  -2886       N  
ATOM   1965  CZ  ARG C 167     -15.484  15.219  55.124  1.00129.99           C  
ANISOU 1965  CZ  ARG C 167    14795  18237  16356   3659   4083  -3341       C  
ATOM   1966  NH1 ARG C 167     -16.037  15.650  56.253  1.00135.27           N  
ANISOU 1966  NH1 ARG C 167    15507  19059  16829   4085   4453  -3639       N  
ATOM   1967  NH2 ARG C 167     -15.549  13.927  54.838  1.00127.21           N  
ANISOU 1967  NH2 ARG C 167    13739  18469  16124   2444   4245  -3518       N  
ATOM   1968  N   LEU C 168     -11.632  15.108  57.757  1.00109.49           N  
ANISOU 1968  N   LEU C 168    15543  11908  14149   1266   4343  -2186       N  
ATOM   1969  CA  LEU C 168     -11.930  14.222  58.870  1.00109.68           C  
ANISOU 1969  CA  LEU C 168    15293  12194  14186    643   4829  -2445       C  
ATOM   1970  C   LEU C 168     -10.922  14.436  59.995  1.00107.51           C  
ANISOU 1970  C   LEU C 168    15897  11209  13740    161   4919  -2167       C  
ATOM   1971  O   LEU C 168     -11.271  14.370  61.176  1.00110.01           O  
ANISOU 1971  O   LEU C 168    16336  11518  13942    -24   5310  -2411       O  
ATOM   1972  CB  LEU C 168     -11.958  12.767  58.407  1.00106.77           C  
ANISOU 1972  CB  LEU C 168    14392  12251  13925    -68   4989  -2474       C  
ATOM   1973  CG  LEU C 168     -13.261  12.404  57.680  1.00112.35           C  
ANISOU 1973  CG  LEU C 168    14046  14033  14608     38   5102  -2983       C  
ATOM   1974  CD1 LEU C 168     -13.082  11.154  56.804  1.00109.48           C  
ANISOU 1974  CD1 LEU C 168    13495  13855  14248   -722   5167  -2930       C  
ATOM   1975  CD2 LEU C 168     -14.437  12.237  58.680  1.00118.68           C  
ANISOU 1975  CD2 LEU C 168    14292  15611  15191   -129   5644  -3607       C  
ATOM   1976  N   LYS C 169      -9.680  14.724  59.625  1.00104.29           N  
ANISOU 1976  N   LYS C 169    16034  10373  13218    -94   4558  -1687       N  
ATOM   1977  CA  LYS C 169      -8.625  15.009  60.601  1.00103.89           C  
ANISOU 1977  CA  LYS C 169    16673   9988  12813   -652   4571  -1426       C  
ATOM   1978  C   LYS C 169      -8.900  16.345  61.334  1.00109.68           C  
ANISOU 1978  C   LYS C 169    18235  10186  13250   -465   4698  -1638       C  
ATOM   1979  O   LYS C 169      -8.422  16.548  62.456  1.00111.23           O  
ANISOU 1979  O   LYS C 169    18942  10209  13110   -990   4873  -1617       O  
ATOM   1980  CB  LYS C 169      -7.242  15.023  59.907  1.00100.71           C  
ANISOU 1980  CB  LYS C 169    16439   9644  12182  -1051   4153   -922       C  
ATOM   1981  CG  LYS C 169      -6.044  14.640  60.802  1.00 99.91           C  
ANISOU 1981  CG  LYS C 169    16488   9870  11603  -1679   4162   -599       C  
ATOM   1982  CD  LYS C 169      -5.546  13.202  60.576  1.00 96.53           C  
ANISOU 1982  CD  LYS C 169    15567   9935  11172  -1587   4201   -290       C  
ATOM   1983  CE  LYS C 169      -4.630  13.086  59.358  1.00 94.01           C  
ANISOU 1983  CE  LYS C 169    14990   9981  10746  -1554   3806     86       C  
ATOM   1984  N   LYS C 170      -9.664  17.242  60.698  1.00114.29           N  
ANISOU 1984  N   LYS C 170    19063  10514  13847    358   4640  -1831       N  
ATOM   1985  CA  LYS C 170     -10.109  18.500  61.314  1.00121.57           C  
ANISOU 1985  CA  LYS C 170    21024  10790  14376    859   4880  -2058       C  
ATOM   1986  C   LYS C 170     -11.217  18.264  62.343  1.00125.32           C  
ANISOU 1986  C   LYS C 170    21051  11623  14940   1277   5360  -2517       C  
ATOM   1987  O   LYS C 170     -11.272  18.945  63.361  1.00129.64           O  
ANISOU 1987  O   LYS C 170    22457  11665  15132   1256   5677  -2673       O  
ATOM   1988  N   LEU C 171     -12.092  17.295  62.070  1.00124.54           N  
ANISOU 1988  N   LEU C 171    19650  12451  15216   1511   5458  -2772       N  
ATOM   1989  CA  LEU C 171     -13.146  16.884  63.020  1.00128.57           C  
ANISOU 1989  CA  LEU C 171    19530  13583  15737   1627   5962  -3269       C  
ATOM   1990  C   LEU C 171     -12.595  16.148  64.264  1.00124.77           C  
ANISOU 1990  C   LEU C 171    19263  12915  15228    537   6257  -3227       C  
ATOM   1991  O   LEU C 171     -13.146  16.280  65.365  1.00128.71           O  
ANISOU 1991  O   LEU C 171    19874  13468  15559    539   6697  -3565       O  
ATOM   1992  CB  LEU C 171     -14.181  15.990  62.310  1.00130.19           C  
ANISOU 1992  CB  LEU C 171    18293  15020  16151   1802   6023  -3611       C  
ATOM   1993  CG  LEU C 171     -15.054  16.633  61.219  1.00136.55           C  
ANISOU 1993  CG  LEU C 171    18530  16511  16839   3093   5791  -3773       C  
ATOM   1994  CD1 LEU C 171     -15.330  15.658  60.080  1.00134.26           C  
ANISOU 1994  CD1 LEU C 171    17090  17168  16752   2727   5579  -3825       C  
ATOM   1995  CD2 LEU C 171     -16.359  17.156  61.802  1.00147.03           C  
ANISOU 1995  CD2 LEU C 171    19331  18728  17803   4151   6186  -4317       C  
ATOM   1996  N   VAL C 172     -11.522  15.373  64.079  1.00117.87           N  
ANISOU 1996  N   VAL C 172    18457  11896  14429   -254   6031  -2801       N  
ATOM   1997  CA  VAL C 172     -10.912  14.607  65.170  1.00115.29           C  
ANISOU 1997  CA  VAL C 172    18389  11484  13930  -1058   6265  -2660       C  
ATOM   1998  C   VAL C 172     -10.189  15.516  66.163  1.00116.83           C  
ANISOU 1998  C   VAL C 172    19525  11153  13708  -1352   6261  -2528       C  
ATOM   1999  O   VAL C 172     -10.190  15.258  67.366  1.00117.81           O  
ANISOU 1999  O   VAL C 172    19892  11256  13612  -1758   6594  -2633       O  
ATOM   2000  CB  VAL C 172      -9.912  13.563  64.634  1.00109.60           C  
ANISOU 2000  CB  VAL C 172    17552  10876  13214  -1481   6025  -2180       C  
TER    2001      VAL C 172                                                      
HETATM 2002  O   HOH A  90      10.298  13.367  12.947  1.00 43.64           O  
ANISOU 2002  O   HOH A  90     4680   5575   6323   -472   -981    -88       O  
HETATM 2003  O   HOH A  91       8.946  20.924  -4.214  1.00 41.94           O  
ANISOU 2003  O   HOH A  91     3347   8464   4125   -552    754  -1107       O  
HETATM 2004  O   HOH A  92       7.772  36.169   5.564  1.00 48.14           O  
ANISOU 2004  O   HOH A  92     6609   4009   7671  -1687     15    211       O  
HETATM 2005  O   HOH A  93      12.034  17.949  22.185  1.00 60.54           O  
ANISOU 2005  O   HOH A  93     7992   9459   5550   -760  -1978    244       O  
HETATM 2006  O   HOH A  94       1.948  30.442  20.421  1.00 46.69           O  
ANISOU 2006  O   HOH A  94     6979   6642   4116   -385    297  -3071       O  
HETATM 2007  O   HOH A  95      10.263  31.394  16.628  1.00 39.35           O  
ANISOU 2007  O   HOH A  95     5501   4621   4827  -1713   -983  -2432       O  
HETATM 2008  O   HOH A  96      12.702  30.359  18.004  1.00 54.62           O  
ANISOU 2008  O   HOH A  96     7170   7061   6522  -1959  -1504  -2548       O  
HETATM 2009  O   HOH A  97      16.821  25.345  14.644  1.00 56.84           O  
ANISOU 2009  O   HOH A  97     6046   8113   7438  -1898  -1632  -1455       O  
HETATM 2010  O   HOH A  98     -13.029  23.476  19.917  1.00 54.77           O  
ANISOU 2010  O   HOH A  98     5015  10426   5366    -31   3576  -1896       O  
HETATM 2011  O   HOH A  99      -7.651  19.844  23.074  1.00 73.47           O  
ANISOU 2011  O   HOH A  99     8889  12688   6336  -1029   2986   -291       O  
HETATM 2012  O   HOH A 100      10.849  16.542  25.119  1.00 53.52           O  
ANISOU 2012  O   HOH A 100     7636   9146   3553   -677  -2000   1052       O  
HETATM 2013  O   HOH A 101       8.706  14.204  25.236  1.00 58.65           O  
ANISOU 2013  O   HOH A 101     8464   9486   4331   -734  -1471   2008       O  
HETATM 2014  O   HOH A 102     -11.769  20.853   4.323  1.00 48.89           O  
ANISOU 2014  O   HOH A 102     3306   8233   7036    183    519  -1763       O  
HETATM 2015  O   HOH A 103       3.423  12.698  23.822  1.00 62.78           O  
ANISOU 2015  O   HOH A 103     8851   9478   5522  -1240     31   2439       O  
HETATM 2016  O   HOH B  90       1.653  -8.783   3.455  1.00 80.23           O  
ANISOU 2016  O   HOH B  90     9843   3400  17238   -818    711  -1239       O  
HETATM 2017  O   HOH B  91      -4.397  -6.958  -3.657  1.00 76.32           O  
ANISOU 2017  O   HOH B  91     7502   5933  15562  -3379    658  -5475       O  
HETATM 2018  O   HOH B  92      17.381  -3.765  11.402  1.00 89.01           O  
ANISOU 2018  O   HOH B  92     9095   9198  15527   5274  -3361   1313       O  
HETATM 2019  O   HOH B  93      -9.164  10.311 -10.474  1.00 53.72           O  
ANISOU 2019  O   HOH B  93     2986  12075   5347  -1003  -2043  -2555       O  
HETATM 2020  O   HOH B  94      -0.317  18.245  -5.294  1.00 39.48           O  
ANISOU 2020  O   HOH B  94     2928   6885   5187   -117    -13     20       O  
HETATM 2021  O   HOH B  95       9.347  13.935 -14.651  1.00 53.52           O  
ANISOU 2021  O   HOH B  95     4679  10886   4768   -795   1651  -2191       O  
HETATM 2022  O   HOH B  96      -3.652  -7.600  -7.773  1.00 84.02           O  
ANISOU 2022  O   HOH B  96     7804   7951  16165  -3603    515  -7806       O  
HETATM 2023  O   HOH B  97      -2.272  -4.898  -2.052  1.00 74.47           O  
ANISOU 2023  O   HOH B  97     7727   6075  14493  -2416    312  -4060       O  
HETATM 2024  O   HOH B  98      -8.326   2.583  -4.303  1.00 51.68           O  
ANISOU 2024  O   HOH B  98     3428   7713   8495  -2734   -790  -3853       O  
HETATM 2025  O   HOH B  99      10.819  -0.324  -5.606  1.00 64.88           O  
ANISOU 2025  O   HOH B  99     5748   6976  11924    313    -15  -4933       O  
HETATM 2026  O   HOH B 100      -6.962  10.151 -12.782  1.00 62.01           O  
ANISOU 2026  O   HOH B 100     4357  13699   5504   -903  -1926  -2761       O  
HETATM 2027  O   HOH D  13      17.154  12.814  15.806  1.00 50.76           O  
ANISOU 2027  O   HOH D  13     5571   7035   6680  -1609   -436   -442       O  
HETATM 2028  O   HOH D  14      14.672  16.006  12.998  1.00 36.51           O  
ANISOU 2028  O   HOH D  14     3260   5321   5291   -516  -1446   -502       O  
HETATM 2029  O   HOH D  15      15.253   8.922  19.092  1.00 58.34           O  
ANISOU 2029  O   HOH D  15     7809   7380   6977  -2540   -364    639       O  
HETATM 2030  O   HOH D  16      13.947  12.527  23.956  1.00 78.14           O  
ANISOU 2030  O   HOH D  16    12173  10961   6553  -4245    691    168       O  
HETATM 2031  O   HOH D  18      15.304   9.713  23.052  1.00 75.45           O  
ANISOU 2031  O   HOH D  18    11623   9990   7055  -3720   -436   1242       O  
HETATM 2032  O   HOH D  19      -0.509   7.200  51.746  1.00 56.68           O  
ANISOU 2032  O   HOH D  19     7374   6925   7235  -1064    944  -1863       O  
HETATM 2033  O   HOH D  39      16.245  17.703  -4.047  1.00 46.91           O  
ANISOU 2033  O   HOH D  39     2070  10615   5137   -839    216  -1178       O  
HETATM 2034  O   HOH D  43      16.452  23.242  -6.137  1.00 63.62           O  
ANISOU 2034  O   HOH D  43     4494  12997   6681   -923    -31   1146       O  
HETATM 2035  O   HOH D  47      16.940  12.820  22.548  1.00 66.64           O  
ANISOU 2035  O   HOH D  47    10041   9400   5876  -3389   -692    412       O  
HETATM 2036  O   HOH D  48      20.497  12.224  19.889  1.00 70.26           O  
ANISOU 2036  O   HOH D  48     9228   9363   8102  -2213  -2111    581       O  
HETATM 2037  O   HOH C  10      -7.771  19.720  -2.918  1.00 45.10           O  
ANISOU 2037  O   HOH C  10     4279   8802   4053   1443   -683  -1419       O  
HETATM 2038  O   HOH C  41      -3.531  16.722  37.953  1.00 72.05           O  
ANISOU 2038  O   HOH C  41    13220   6169   7986   -164   -740   1797       O  
HETATM 2039  O   HOH C  49     -14.366  14.764  68.182  1.00110.34           O  
ANISOU 2039  O   HOH C  49    17079  11885  12957   -756   8001  -4405       O  
HETATM 2040  O   HOH C  50     -11.303  13.002  68.699  1.00 96.13           O  
ANISOU 2040  O   HOH C  50    16581   9069  10872  -2414   7533  -3068       O  
HETATM 2041  O   HOH C  51     -11.537  18.306  69.251  1.00112.23           O  
ANISOU 2041  O   HOH C  51    21229   9273  12137   -885   7398  -3515       O  
HETATM 2042  O   HOH C  52     -13.175  18.693  67.274  1.00117.15           O  
ANISOU 2042  O   HOH C  52    20787  10512  13213   1194   7239  -3823       O  
MASTER      483    0    0    6   12    0    0    6 2016    4    0   24          
END

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Related entries of code: 3p8m

Entries with 90% protein sequence similarity cutoff in PDBbind
PDB Code	Check Database	Protein Sequence Similarity
1p4b	RCSB PDB PDBbind	12aa, >1P4B_3\|Chain... at 91%
1swi	RCSB PDB PDBbind	33aa, >1SWI_1\|Chains... at 93%
Complexes with the same small molecule ligand
PDB Code	Check Database	Ligand Name
No complexes with the same small molecule ligand are found!

Entry Information

PDB ID	3p8m
Complex Type	Protein-Protein
PDBbind Subset	general set
Protein Name	DYNEIN LIGHT CHAIN 2, CYTOPLASMIC
Ligand Name	General control protein GCN4
EC.Number	E.C.6.3.2.9
Resolution	2.9(Å)
Affinity (Kd/Ki/IC50)	Kd<0.007uM
Release Year	2011
Protein/NA Sequence	Check fasta file
Primary Reference	(2011) Plos One Vol. 6: pp. e18818-e18818

Links to External Databases

RCSB PDB	The mother database
PDBsum	Enhanced annotations on PDB entries
Pubchem	Comprehensive collection of chemical and biological data
UniProtKB AC	UniProt accession number (AC): Q96FJ2 P03069
Entrez Gene ID	NCBI Entrez Gene ID: 140735 856709
ASD	Information of known allosteric effects of PDB entries

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