CNRS Nantes University UFIP UFIP
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***  BSA_mono  ***

elNémo ID: 20021013032316939

Job options:

ID        	=	 20021013032316939
JOBID     	=	 BSA_mono
USERID    	=	 unknown
PRIVAT    	=	 0

NMODES    	=	 5
DQMIN     	=	 -100
DQMAX     	=	 100
DQSTEP    	=	 20
DOGRAPHS  	=	 on

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:

HEADER BSA_mono

HEADER    TRANSPORT PROTEIN                       07-DEC-11   XXXX              
TITLE     CRYSTAL STRUCTURE OF BOVINE SERUM ALBUMIN                             
KEYWDS    ALLERGEN, STRUCTURAL GENOMICS, PSI-BIOLOGY, NEW YORK STRUCTURAL       
KEYWDS   2 GENOMICS RESEARCH CONSORTIUM, NYSGRC, CARRIER PROTEIN, TRANSPORT     
KEYWDS   3 PROTEIN                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.A.MAJOREK, P.J.POREBSKI, M.CHRUSZCZ, S.C.ALMO, W.MINOR, NEW YORK    
AUTHOR   2 STRUCTURAL GENOMICS RESEARCH CONSORTIUM (NYSGRC)                     
JRNL        AUTH   K.A.MAJOREK, P.J.POREBSKI, A.DAYAL, M.D.ZIMMERMAN,           
JRNL        AUTH 2 K.JABLONSKA, A.J.STEWART, M.CHRUSZCZ, W.MINOR                
JRNL        TITL   STRUCTURAL AND IMMUNOLOGIC CHARACTERIZATION OF BOVINE,       
JRNL        TITL 2 HORSE, AND RABBIT SERUM ALBUMINS.                            
JRNL        REF    MOL.IMMUNOL.                  V.  52   174 2012              
JRNL        REFN   ASTM MOIMD5  UK ISSN 0161-5890                               
JRNL        PMID   22677715                                                     
JRNL        DOI    10.1016/J.MOLIMM.2012.05.011                                 
SEQRES   1 A  583  ASP THR HIS LYS SER GLU ILE ALA HIS ARG PHE LYS ASP          
SEQRES   2 A  583  LEU GLY GLU GLU HIS PHE LYS GLY LEU VAL LEU ILE ALA          
SEQRES   3 A  583  PHE SER GLN TYR LEU GLN GLN CYS PRO PHE ASP GLU HIS          
SEQRES   4 A  583  VAL LYS LEU VAL ASN GLU LEU THR GLU PHE ALA LYS THR          
SEQRES   5 A  583  CYS VAL ALA ASP GLU SER HIS ALA GLY CYS GLU LYS SER          
SEQRES   6 A  583  LEU HIS THR LEU PHE GLY ASP GLU LEU CYS LYS VAL ALA          
SEQRES   7 A  583  SER LEU ARG GLU THR TYR GLY ASP MET ALA ASP CYS CYS          
SEQRES   8 A  583  GLU LYS GLN GLU PRO GLU ARG ASN GLU CYS PHE LEU SER          
SEQRES   9 A  583  HIS LYS ASP ASP SER PRO ASP LEU PRO LYS LEU LYS PRO          
SEQRES  10 A  583  ASP PRO ASN THR LEU CYS ASP GLU PHE LYS ALA ASP GLU          
SEQRES  11 A  583  LYS LYS PHE TRP GLY LYS TYR LEU TYR GLU ILE ALA ARG          
SEQRES  12 A  583  ARG HIS PRO TYR PHE TYR ALA PRO GLU LEU LEU TYR TYR          
SEQRES  13 A  583  ALA ASN LYS TYR ASN GLY VAL PHE GLN GLU CYS CYS GLN          
SEQRES  14 A  583  ALA GLU ASP LYS GLY ALA CYS LEU LEU PRO LYS ILE GLU          
SEQRES  15 A  583  THR MET ARG GLU LYS VAL LEU THR SER SER ALA ARG GLN          
SEQRES  16 A  583  ARG LEU ARG CYS ALA SER ILE GLN LYS PHE GLY GLU ARG          
SEQRES  17 A  583  ALA LEU LYS ALA TRP SER VAL ALA ARG LEU SER GLN LYS          
SEQRES  18 A  583  PHE PRO LYS ALA GLU PHE VAL GLU VAL THR LYS LEU VAL          
SEQRES  19 A  583  THR ASP LEU THR LYS VAL HIS LYS GLU CYS CYS HIS GLY          
SEQRES  20 A  583  ASP LEU LEU GLU CYS ALA ASP ASP ARG ALA ASP LEU ALA          
SEQRES  21 A  583  LYS TYR ILE CYS ASP ASN GLN ASP THR ILE SER SER LYS          
SEQRES  22 A  583  LEU LYS GLU CYS CYS ASP LYS PRO LEU LEU GLU LYS SER          
SEQRES  23 A  583  HIS CYS ILE ALA GLU VAL GLU LYS ASP ALA ILE PRO GLU          
SEQRES  24 A  583  ASN LEU PRO PRO LEU THR ALA ASP PHE ALA GLU ASP LYS          
SEQRES  25 A  583  ASP VAL CYS LYS ASN TYR GLN GLU ALA LYS ASP ALA PHE          
SEQRES  26 A  583  LEU GLY SER PHE LEU TYR GLU TYR SER ARG ARG HIS PRO          
SEQRES  27 A  583  GLU TYR ALA VAL SER VAL LEU LEU ARG LEU ALA LYS GLU          
SEQRES  28 A  583  TYR GLU ALA THR LEU GLU GLU CYS CYS ALA LYS ASP ASP          
SEQRES  29 A  583  PRO HIS ALA CYS TYR SER THR VAL PHE ASP LYS LEU LYS          
SEQRES  30 A  583  HIS LEU VAL ASP GLU PRO GLN ASN LEU ILE LYS GLN ASN          
SEQRES  31 A  583  CYS ASP GLN PHE GLU LYS LEU GLY GLU TYR GLY PHE GLN          
SEQRES  32 A  583  ASN ALA LEU ILE VAL ARG TYR THR ARG LYS VAL PRO GLN          
SEQRES  33 A  583  VAL SER THR PRO THR LEU VAL GLU VAL SER ARG SER LEU          
SEQRES  34 A  583  GLY LYS VAL GLY THR ARG CYS CYS THR LYS PRO GLU SER          
SEQRES  35 A  583  GLU ARG MET PRO CYS THR GLU ASP TYR LEU SER LEU ILE          
SEQRES  36 A  583  LEU ASN ARG LEU CYS VAL LEU HIS GLU LYS THR PRO VAL          
SEQRES  37 A  583  SER GLU LYS VAL THR LYS CYS CYS THR GLU SER LEU VAL          
SEQRES  38 A  583  ASN ARG ARG PRO CYS PHE SER ALA LEU THR PRO ASP GLU          
SEQRES  39 A  583  THR TYR VAL PRO LYS ALA PHE ASP GLU LYS LEU PHE THR          
SEQRES  40 A  583  PHE HIS ALA ASP ILE CYS THR LEU PRO ASP THR GLU LYS          
SEQRES  41 A  583  GLN ILE LYS LYS GLN THR ALA LEU VAL GLU LEU LEU LYS          
SEQRES  42 A  583  HIS LYS PRO LYS ALA THR GLU GLU GLN LEU LYS THR VAL          
SEQRES  43 A  583  MET GLU ASN PHE VAL ALA PHE VAL ASP LYS CYS CYS ALA          
SEQRES  44 A  583  ALA ASP ASP LYS GLU ALA CYS PHE ALA VAL GLU GLY PRO          
SEQRES  45 A  583  LYS LEU VAL VAL SER THR GLN THR ALA LEU ALA                  
SEQRES   1 B  583  ASP THR HIS LYS SER GLU ILE ALA HIS ARG PHE LYS ASP          
SEQRES   2 B  583  LEU GLY GLU GLU HIS PHE LYS GLY LEU VAL LEU ILE ALA          
SEQRES   3 B  583  PHE SER GLN TYR LEU GLN GLN CYS PRO PHE ASP GLU HIS          
SEQRES   4 B  583  VAL LYS LEU VAL ASN GLU LEU THR GLU PHE ALA LYS THR          
SEQRES   5 B  583  CYS VAL ALA ASP GLU SER HIS ALA GLY CYS GLU LYS SER          
SEQRES   6 B  583  LEU HIS THR LEU PHE GLY ASP GLU LEU CYS LYS VAL ALA          
SEQRES   7 B  583  SER LEU ARG GLU THR TYR GLY ASP MET ALA ASP CYS CYS          
SEQRES   8 B  583  GLU LYS GLN GLU PRO GLU ARG ASN GLU CYS PHE LEU SER          
SEQRES   9 B  583  HIS LYS ASP ASP SER PRO ASP LEU PRO LYS LEU LYS PRO          
SEQRES  10 B  583  ASP PRO ASN THR LEU CYS ASP GLU PHE LYS ALA ASP GLU          
SEQRES  11 B  583  LYS LYS PHE TRP GLY LYS TYR LEU TYR GLU ILE ALA ARG          
SEQRES  12 B  583  ARG HIS PRO TYR PHE TYR ALA PRO GLU LEU LEU TYR TYR          
SEQRES  13 B  583  ALA ASN LYS TYR ASN GLY VAL PHE GLN GLU CYS CYS GLN          
SEQRES  14 B  583  ALA GLU ASP LYS GLY ALA CYS LEU LEU PRO LYS ILE GLU          
SEQRES  15 B  583  THR MET ARG GLU LYS VAL LEU THR SER SER ALA ARG GLN          
SEQRES  16 B  583  ARG LEU ARG CYS ALA SER ILE GLN LYS PHE GLY GLU ARG          
SEQRES  17 B  583  ALA LEU LYS ALA TRP SER VAL ALA ARG LEU SER GLN LYS          
SEQRES  18 B  583  PHE PRO LYS ALA GLU PHE VAL GLU VAL THR LYS LEU VAL          
SEQRES  19 B  583  THR ASP LEU THR LYS VAL HIS LYS GLU CYS CYS HIS GLY          
SEQRES  20 B  583  ASP LEU LEU GLU CYS ALA ASP ASP ARG ALA ASP LEU ALA          
SEQRES  21 B  583  LYS TYR ILE CYS ASP ASN GLN ASP THR ILE SER SER LYS          
SEQRES  22 B  583  LEU LYS GLU CYS CYS ASP LYS PRO LEU LEU GLU LYS SER          
SEQRES  23 B  583  HIS CYS ILE ALA GLU VAL GLU LYS ASP ALA ILE PRO GLU          
SEQRES  24 B  583  ASN LEU PRO PRO LEU THR ALA ASP PHE ALA GLU ASP LYS          
SEQRES  25 B  583  ASP VAL CYS LYS ASN TYR GLN GLU ALA LYS ASP ALA PHE          
SEQRES  26 B  583  LEU GLY SER PHE LEU TYR GLU TYR SER ARG ARG HIS PRO          
SEQRES  27 B  583  GLU TYR ALA VAL SER VAL LEU LEU ARG LEU ALA LYS GLU          
SEQRES  28 B  583  TYR GLU ALA THR LEU GLU GLU CYS CYS ALA LYS ASP ASP          
SEQRES  29 B  583  PRO HIS ALA CYS TYR SER THR VAL PHE ASP LYS LEU LYS          
SEQRES  30 B  583  HIS LEU VAL ASP GLU PRO GLN ASN LEU ILE LYS GLN ASN          
SEQRES  31 B  583  CYS ASP GLN PHE GLU LYS LEU GLY GLU TYR GLY PHE GLN          
SEQRES  32 B  583  ASN ALA LEU ILE VAL ARG TYR THR ARG LYS VAL PRO GLN          
SEQRES  33 B  583  VAL SER THR PRO THR LEU VAL GLU VAL SER ARG SER LEU          
SEQRES  34 B  583  GLY LYS VAL GLY THR ARG CYS CYS THR LYS PRO GLU SER          
SEQRES  35 B  583  GLU ARG MET PRO CYS THR GLU ASP TYR LEU SER LEU ILE          
SEQRES  36 B  583  LEU ASN ARG LEU CYS VAL LEU HIS GLU LYS THR PRO VAL          
SEQRES  37 B  583  SER GLU LYS VAL THR LYS CYS CYS THR GLU SER LEU VAL          
SEQRES  38 B  583  ASN ARG ARG PRO CYS PHE SER ALA LEU THR PRO ASP GLU          
SEQRES  39 B  583  THR TYR VAL PRO LYS ALA PHE ASP GLU LYS LEU PHE THR          
SEQRES  40 B  583  PHE HIS ALA ASP ILE CYS THR LEU PRO ASP THR GLU LYS          
SEQRES  41 B  583  GLN ILE LYS LYS GLN THR ALA LEU VAL GLU LEU LEU LYS          
SEQRES  42 B  583  HIS LYS PRO LYS ALA THR GLU GLU GLN LEU LYS THR VAL          
SEQRES  43 B  583  MET GLU ASN PHE VAL ALA PHE VAL ASP LYS CYS CYS ALA          
SEQRES  44 B  583  ALA ASP ASP LYS GLU ALA CYS PHE ALA VAL GLU GLY PRO          
SEQRES  45 B  583  LYS LEU VAL VAL SER THR GLN THR ALA LEU ALA                  
HETNAM      CA CALCIUM ION                                                      
HETNAM     ACT ACETATE ION                                                      
FORMUL   3   CA    6(CA 2+)                                                     
FORMUL   9  ACT    C2 H3 O2 1-                                                  
FORMUL  10  HOH   *44(H2 O)                                                     
HELIX    1   1 SER A    5  LEU A   31  1                                  27    
HELIX    2   2 PRO A   35  ASP A   56  1                                  22    
HELIX    3   3 SER A   65  LYS A   76  1                                  12    
HELIX    4   4 SER A   79  GLY A   85  1                                   7    
HELIX    5   5 ASP A   86  LYS A   93  5                                   8    
HELIX    6   6 PRO A   96  SER A  104  1                                   9    
HELIX    7   7 ASP A  118  ASP A  129  1                                  12    
HELIX    8   8 ASP A  129  HIS A  145  1                                  17    
HELIX    9   9 TYR A  149  CYS A  168  1                                  20    
HELIX   10  10 ASP A  172  PHE A  222  1                                  51    
HELIX   11  11 GLU A  226  HIS A  246  1                                  21    
HELIX   12  12 ASP A  248  ASN A  266  1                                  19    
HELIX   13  13 GLN A  267  ILE A  270  5                                   4    
HELIX   14  14 GLU A  276  LYS A  280  5                                   5    
HELIX   15  15 PRO A  281  GLU A  291  1                                  11    
HELIX   16  16 PRO A  303  ALA A  309  1                                   7    
HELIX   17  17 ASP A  313  ALA A  321  1                                   9    
HELIX   18  18 ALA A  321  HIS A  337  1                                  17    
HELIX   19  19 ALA A  341  CYS A  360  1                                  20    
HELIX   20  20 ASP A  364  SER A  370  1                                   7    
HELIX   21  21 THR A  371  VAL A  414  1                                  44    
HELIX   22  22 SER A  418  CYS A  437  1                                  20    
HELIX   23  23 PRO A  440  SER A  442  5                                   3    
HELIX   24  24 GLU A  443  THR A  466  1                                  24    
HELIX   25  25 SER A  469  SER A  479  1                                  11    
HELIX   26  26 ASN A  482  LEU A  490  1                                   9    
HELIX   27  27 ASP A  502  PHE A  506  5                                   5    
HELIX   28  28 HIS A  509  LEU A  515  5                                   7    
HELIX   29  29 PRO A  516  LYS A  535  1                                  20    
HELIX   30  30 THR A  539  ALA A  559  1                                  21    
HELIX   31  31 ASP A  562  LEU A  582  1                                  21    
HELIX   32  32 SER B    5  GLY B   15  1                                  11    
HELIX   33  33 GLY B   15  LEU B   31  1                                  17    
HELIX   34  34 PRO B   35  ASP B   56  1                                  22    
HELIX   35  35 SER B   65  LYS B   76  1                                  12    
HELIX   36  36 SER B   79  GLY B   85  1                                   7    
HELIX   37  37 ASP B   86  LYS B   93  5                                   8    
HELIX   38  38 PRO B   96  SER B  104  1                                   9    
HELIX   39  39 ASP B  118  ASP B  129  1                                  12    
HELIX   40  40 ASP B  129  HIS B  145  1                                  17    
HELIX   41  41 TYR B  149  CYS B  168  1                                  20    
HELIX   42  42 ASP B  172  PHE B  222  1                                  51    
HELIX   43  43 GLU B  226  HIS B  246  1                                  21    
HELIX   44  44 ASP B  248  ASN B  266  1                                  19    
HELIX   45  45 GLN B  267  ILE B  270  5                                   4    
HELIX   46  46 GLU B  276  LYS B  280  5                                   5    
HELIX   47  47 PRO B  281  GLU B  291  1                                  11    
HELIX   48  48 PRO B  303  ALA B  309  1                                   7    
HELIX   49  49 ASP B  313  ALA B  321  1                                   9    
HELIX   50  50 ALA B  321  HIS B  337  1                                  17    
HELIX   51  51 ALA B  341  CYS B  360  1                                  20    
HELIX   52  52 ASP B  364  SER B  370  1                                   7    
HELIX   53  53 THR B  371  VAL B  414  1                                  44    
HELIX   54  54 SER B  418  CYS B  437  1                                  20    
HELIX   55  55 PRO B  440  SER B  442  5                                   3    
HELIX   56  56 GLU B  443  THR B  466  1                                  24    
HELIX   57  57 SER B  469  SER B  479  1                                  11    
HELIX   58  58 ASN B  482  LEU B  490  1                                   9    
HELIX   59  59 ASP B  502  PHE B  506  5                                   5    
HELIX   60  60 HIS B  509  LEU B  515  5                                   7    
HELIX   61  61 PRO B  516  LYS B  535  1                                  20    
HELIX   62  62 THR B  539  CYS B  558  1                                  20    
HELIX   63  63 ASP B  562  LEU B  582  1                                  21    
SSBOND   1 CYS A   53    CYS A   62                          1555   1555  2.03  
SSBOND   2 CYS A   75    CYS A   91                          1555   1555  2.06  
SSBOND   3 CYS A   90    CYS A  101                          1555   1555  2.05  
SSBOND   4 CYS A  123    CYS A  168                          1555   1555  2.05  
SSBOND   5 CYS A  167    CYS A  176                          1555   1555  2.08  
SSBOND   6 CYS A  199    CYS A  245                          1555   1555  2.04  
SSBOND   7 CYS A  244    CYS A  252                          1555   1555  2.03  
SSBOND   8 CYS A  264    CYS A  278                          1555   1555  2.05  
SSBOND   9 CYS A  277    CYS A  288                          1555   1555  2.05  
SSBOND  10 CYS A  315    CYS A  360                          1555   1555  2.04  
SSBOND  11 CYS A  359    CYS A  368                          1555   1555  2.04  
SSBOND  12 CYS A  391    CYS A  437                          1555   1555  2.04  
SSBOND  13 CYS A  436    CYS A  447                          1555   1555  2.05  
SSBOND  14 CYS A  460    CYS A  476                          1555   1555  2.03  
SSBOND  15 CYS A  475    CYS A  486                          1555   1555  2.06  
SSBOND  16 CYS A  513    CYS A  558                          1555   1555  2.03  
SSBOND  17 CYS A  557    CYS A  566                          1555   1555  2.04  
SSBOND  18 CYS B   53    CYS B   62                          1555   1555  2.02  
SSBOND  19 CYS B   75    CYS B   91                          1555   1555  2.10  
SSBOND  20 CYS B   90    CYS B  101                          1555   1555  2.05  
SSBOND  21 CYS B  123    CYS B  168                          1555   1555  2.04  
SSBOND  22 CYS B  167    CYS B  176                          1555   1555  2.07  
SSBOND  23 CYS B  199    CYS B  245                          1555   1555  2.06  
SSBOND  24 CYS B  244    CYS B  252                          1555   1555  2.02  
SSBOND  25 CYS B  264    CYS B  278                          1555   1555  2.03  
SSBOND  26 CYS B  277    CYS B  288                          1555   1555  2.03  
SSBOND  27 CYS B  315    CYS B  360                          1555   1555  2.03  
SSBOND  28 CYS B  359    CYS B  368                          1555   1555  2.02  
SSBOND  29 CYS B  391    CYS B  437                          1555   1555  2.05  
SSBOND  30 CYS B  436    CYS B  447                          1555   1555  2.03  
SSBOND  31 CYS B  460    CYS B  476                          1555   1555  2.02  
SSBOND  32 CYS B  475    CYS B  486                          1555   1555  2.07  
SSBOND  33 CYS B  513    CYS B  558                          1555   1555  2.02  
SSBOND  34 CYS B  557    CYS B  566                          1555   1555  2.05  
LINK        CA    CA A 584                 O   HOH A 591     1555   1555  2.28  
LINK        CA    CA A 586                 O   HOH A 607     1555   1555  2.34  
LINK        CA    CA A 585                 O   HOH A 592     1555   1555  2.34  
LINK        CA    CA B 584                 O   HOH B 590     1555   1555  2.34  
LINK        CA    CA B 586                 O   HOH B 593     1555   1555  2.35  
LINK        CA    CA A 585                 O   HOH A 604     1555   1555  2.36  
LINK        CA    CA B 584                 O   HOH B 589     1555   1555  2.36  
LINK         O   SER A 109                CA    CA A 585     1555   1555  2.36  
LINK         OE2 GLU A 251                CA    CA A 584     1555   1555  2.38  
LINK        CA    CA B 585                 O   HOH B 607     1555   1555  2.38  
LINK         OD2 ASP B  13                CA    CA B 586     1555   1555  2.39  
LINK         OD1 ASP A 254                CA    CA A 586     1555   1555  2.40  
LINK         OD2 ASP A  13                CA    CA A 586     1555   1555  2.40  
LINK         O   SER B 109                CA    CA B 584     1555   1555  2.40  
LINK        CA    CA A 585                 O   HOH A 593     1555   1555  2.40  
LINK        CA    CA B 584                 O   HOH B 591     1555   1555  2.41  
LINK         OD2 ASP B 248                CA    CA B 585     1555   1555  2.41  
LINK        CA    CA B 586                 O   HOH B 594     1555   1555  2.42  
LINK        CA    CA B 584                 O   HOH B 592     1555   1555  2.43  
LINK         OD1 ASP B 254                CA    CA B 586     1555   1555  2.44  
LINK         OE2 GLU B 251                CA    CA B 585     1555   1555  2.44  
LINK        CA    CA A 584                 O   HOH A 589     1555   1555  2.45  
LINK         OD2 ASP A 248                CA    CA A 584     1555   1555  2.47  
LINK         OD2 ASP A 111                CA    CA A 585     1555   1555  2.50  
LINK         OD2 ASP B 111                CA    CA B 584     1555   1555  2.50  
LINK         OE1 GLU B 243                CA    CA B 585     1555   1555  2.50  
LINK         OE2 GLU A   6                CA    CA A 584     1555   1555  2.51  
LINK        CA    CA B 585                 O   HOH B 606     1555   1555  2.51  
LINK         OD1 ASP B 258                CA    CA B 586     1555   1555  2.55  
LINK        CA    CA A 586                 O   HOH A 605     1555   1555  2.58  
LINK         OG  SER A 109                CA    CA A 585     1555   1555  2.60  
LINK         OD1 ASP A 258                CA    CA A 586     1555   1555  2.61  
LINK         OG  SER B 109                CA    CA B 584     1555   1555  2.76  
LINK         OD2 ASP A 258                CA    CA A 586     1555   1555  2.93  
LINK         OD2 ASP B 258                CA    CA B 586     1555   1555  2.97  
CISPEP   1 GLU A   95    PRO A   96          1        -0.88                     
CISPEP   2 GLU B   95    PRO B   96          1        -0.60                     
SITE     1 AC1  5 GLU A   6  ASP A 248  GLU A 251  HOH A 589                    
SITE     2 AC1  5 HOH A 591                                                     
SITE     1 AC2  5 SER A 109  ASP A 111  HOH A 592  HOH A 593                    
SITE     2 AC2  5 HOH A 604                                                     
SITE     1 AC3  5 ASP A  13  ASP A 254  ASP A 258  HOH A 605                    
SITE     2 AC3  5 HOH A 607                                                     
SITE     1 AC4  6 SER B 109  ASP B 111  HOH B 589  HOH B 590                    
SITE     2 AC4  6 HOH B 591  HOH B 592                                          
SITE     1 AC5  5 GLU B 243  ASP B 248  GLU B 251  HOH B 606                    
SITE     2 AC5  5 HOH B 607                                                     
SITE     1 AC6  5 ASP B  13  ASP B 254  ASP B 258  HOH B 593                    
SITE     2 AC6  5 HOH B 594                                                     
SITE     1 AC7  1 GLU B  48                                                     
CRYST1  215.661   45.096  142.408  90.00 114.01  90.00 C 1 2 1       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      0.004637  0.000000  0.002066        0.00000                         
SCALE2      0.000000  0.022175  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007687        0.00000                         
MODEL        1                                                                  
ATOM      1  N   HIS A   3      22.804  29.493  13.350  1.00115.31           N  
ANISOU    1  N   HIS A   3    18486  12114  13212   1578  -2751  -1165       N  
ATOM      2  CA  HIS A   3      22.625  29.884  11.922  1.00114.42           C  
ANISOU    2  CA  HIS A   3    18748  11776  12951   1711  -2955  -1186       C  
ATOM      3  C   HIS A   3      22.410  28.626  11.068  1.00113.83           C  
ANISOU    3  C   HIS A   3    18663  11696  12890   1736  -2929  -1193       C  
ATOM      4  O   HIS A   3      21.737  27.667  11.497  1.00121.89           O  
ANISOU    4  O   HIS A   3    19380  12856  14078   1740  -2894  -1302       O  
ATOM      5  CB  HIS A   3      23.855  30.667  11.443  1.00114.63           C  
ANISOU    5  CB  HIS A   3    19121  11670  12763   1618  -2872   -980       C  
ATOM      6  N   LYS A   4      22.950  28.651   9.851  1.00105.77           N  
ANISOU    6  N   LYS A   4    17988  10511  11690   1747  -2948  -1087       N  
ATOM      7  CA  LYS A   4      23.158  27.452   9.050  1.00 97.77           C  
ANISOU    7  CA  LYS A   4    16996   9499  10654   1722  -2852  -1029       C  
ATOM      8  C   LYS A   4      24.543  26.853   9.357  1.00 88.40           C  
ANISOU    8  C   LYS A   4    15749   8415   9424   1517  -2524   -805       C  
ATOM      9  O   LYS A   4      24.781  25.677   9.085  1.00 86.68           O  
ANISOU    9  O   LYS A   4    15432   8261   9243   1468  -2393   -757       O  
ATOM     10  CB  LYS A   4      23.034  27.791   7.557  1.00100.51           C  
ANISOU   10  CB  LYS A   4    17760   9612  10817   1835  -3040  -1040       C  
ATOM     11  CG  LYS A   4      21.745  28.518   7.167  1.00102.35           C  
ANISOU   11  CG  LYS A   4    18108   9707  11074   2059  -3403  -1265       C  
ATOM     12  CD  LYS A   4      21.873  29.217   5.819  1.00103.29           C  
ANISOU   12  CD  LYS A   4    18729   9560  10956   2144  -3591  -1232       C  
ATOM     13  N   SER A   5      25.442  27.652   9.936  1.00 79.83           N  
ANISOU   13  N   SER A   5    14714   7346   8271   1402  -2404   -682       N  
ATOM     14  CA  SER A   5      26.837  27.243  10.155  1.00 73.62           C  
ANISOU   14  CA  SER A   5    13900   6639   7434   1216  -2113   -486       C  
ATOM     15  C   SER A   5      27.311  27.561  11.579  1.00 67.75           C  
ANISOU   15  C   SER A   5    12909   6048   6784   1104  -1973   -431       C  
ATOM     16  O   SER A   5      27.612  28.699  11.887  1.00 73.38           O  
ANISOU   16  O   SER A   5    13741   6713   7428   1080  -2002   -403       O  
ATOM     17  CB  SER A   5      27.741  27.942   9.140  1.00 71.62           C  
ANISOU   17  CB  SER A   5    14045   6218   6950   1161  -2081   -370       C  
ATOM     18  OG  SER A   5      29.107  27.686   9.385  1.00 70.06           O  
ANISOU   18  OG  SER A   5    13809   6100   6711    980  -1804   -208       O  
ATOM     19  N   GLU A   6      27.388  26.551  12.433  1.00 62.49           N  
ANISOU   19  N   GLU A   6    11920   5558   6266   1033  -1826   -414       N  
ATOM     20  CA  GLU A   6      27.788  26.744  13.818  1.00 60.97           C  
ANISOU   20  CA  GLU A   6    11491   5512   6163    927  -1700   -366       C  
ATOM     21  C   GLU A   6      29.117  27.517  13.915  1.00 58.13           C  
ANISOU   21  C   GLU A   6    11280   5125   5683    805  -1558   -212       C  
ATOM     22  O   GLU A   6      29.204  28.480  14.652  1.00 58.45           O  
ANISOU   22  O   GLU A   6    11304   5182   5723    781  -1579   -212       O  
ATOM     23  CB  GLU A   6      27.874  25.414  14.563  1.00 60.81           C  
ANISOU   23  CB  GLU A   6    11166   5656   6282    849  -1547   -340       C  
ATOM     24  CG  GLU A   6      27.906  25.532  16.081  1.00 63.95           C  
ANISOU   24  CG  GLU A   6    11302   6207   6790    764  -1466   -337       C  
ATOM     25  CD  GLU A   6      28.200  24.209  16.817  1.00 67.50           C  
ANISOU   25  CD  GLU A   6    11503   6797   7346    663  -1303   -279       C  
ATOM     26  OE1 GLU A   6      28.271  23.134  16.137  1.00 67.71           O  
ANISOU   26  OE1 GLU A   6    11540   6806   7379    672  -1264   -257       O  
ATOM     27  OE2 GLU A   6      28.365  24.253  18.075  1.00 71.77           O  
ANISOU   27  OE2 GLU A   6    11856   7457   7956    576  -1222   -255       O  
ATOM     28  N   ILE A   7      30.124  27.157  13.138  1.00 55.15           N  
ANISOU   28  N   ILE A   7    11053   4700   5201    729  -1419    -96       N  
ATOM     29  CA  ILE A   7      31.399  27.831  13.273  1.00 53.17           C  
ANISOU   29  CA  ILE A   7    10910   4439   4852    596  -1265     29       C  
ATOM     30  C   ILE A   7      31.250  29.313  12.876  1.00 55.99           C  
ANISOU   30  C   ILE A   7    11566   4641   5067    631  -1405      8       C  
ATOM     31  O   ILE A   7      31.836  30.193  13.524  1.00 54.09           O  
ANISOU   31  O   ILE A   7    11335   4418   4800    549  -1347     61       O  
ATOM     32  CB  ILE A   7      32.545  27.111  12.509  1.00 50.92           C  
ANISOU   32  CB  ILE A   7    10707   4148   4492    496  -1071    132       C  
ATOM     33  CG1 ILE A   7      33.919  27.557  13.020  1.00 50.49           C  
ANISOU   33  CG1 ILE A   7    10632   4150   4403    337   -871    241       C  
ATOM     34  CG2 ILE A   7      32.446  27.338  11.040  1.00 51.96           C  
ANISOU   34  CG2 ILE A   7    11183   4105   4455    540  -1145    119       C  
ATOM     35  CD1 ILE A   7      35.077  27.009  12.211  1.00 49.69           C  
ANISOU   35  CD1 ILE A   7    10621   4036   4221    233   -680    312       C  
ATOM     36  N   ALA A   8      30.445  29.592  11.851  1.00 57.82           N  
ANISOU   36  N   ALA A   8    12044   4714   5210    757  -1603    -73       N  
ATOM     37  CA  ALA A   8      30.183  30.976  11.459  1.00 60.39           C  
ANISOU   37  CA  ALA A   8    12679   4867   5398    810  -1778   -105       C  
ATOM     38  C   ALA A   8      29.567  31.793  12.597  1.00 61.57           C  
ANISOU   38  C   ALA A   8    12668   5072   5652    865  -1898   -187       C  
ATOM     39  O   ALA A   8      29.995  32.935  12.869  1.00 60.74           O  
ANISOU   39  O   ALA A   8    12709   4905   5464    814  -1909   -146       O  
ATOM     40  CB  ALA A   8      29.277  31.029  10.233  1.00 58.89           C  
ANISOU   40  CB  ALA A   8    12762   4498   5116    964  -2011   -201       C  
ATOM     41  N   HIS A   9      28.533  31.229  13.214  1.00 64.46           N  
ANISOU   41  N   HIS A   9    12749   5547   6195    964  -1992   -315       N  
ATOM     42  CA  HIS A   9      27.818  31.910  14.292  1.00 69.51           C  
ANISOU   42  CA  HIS A   9    13208   6254   6948   1022  -2107   -426       C  
ATOM     43  C   HIS A   9      28.806  32.240  15.391  1.00 66.04           C  
ANISOU   43  C   HIS A   9    12626   5934   6530    865  -1909   -308       C  
ATOM     44  O   HIS A   9      28.872  33.369  15.852  1.00 68.68           O  
ANISOU   44  O   HIS A   9    13034   6230   6832    863  -1973   -318       O  
ATOM     45  CB  HIS A   9      26.673  31.033  14.828  1.00 77.02           C  
ANISOU   45  CB  HIS A   9    13835   7337   8092   1108  -2174   -581       C  
ATOM     46  CG  HIS A   9      25.806  31.714  15.849  1.00 86.64           C  
ANISOU   46  CG  HIS A   9    14866   8624   9429   1174  -2302   -734       C  
ATOM     47  ND1 HIS A   9      24.493  32.063  15.603  1.00 97.05           N  
ANISOU   47  ND1 HIS A   9    16185   9879  10810   1353  -2564   -952       N  
ATOM     48  CD2 HIS A   9      26.070  32.130  17.112  1.00 95.55           C  
ANISOU   48  CD2 HIS A   9    15799   9878  10626   1088  -2208   -716       C  
ATOM     49  CE1 HIS A   9      23.985  32.659  16.668  1.00 97.27           C  
ANISOU   49  CE1 HIS A   9    16017   9998  10943   1370  -2617  -1067       C  
ATOM     50  NE2 HIS A   9      24.922  32.715  17.599  1.00 98.51           N  
ANISOU   50  NE2 HIS A   9    16060  10269  11100   1208  -2402   -921       N  
ATOM     51  N   ARG A  10      29.619  31.276  15.778  1.00 62.07           N  
ANISOU   51  N   ARG A  10    11938   5566   6079    739  -1677   -198       N  
ATOM     52  CA  ARG A  10      30.561  31.506  16.851  1.00 63.19           C  
ANISOU   52  CA  ARG A  10    11930   5827   6254    598  -1499    -96       C  
ATOM     53  C   ARG A  10      31.500  32.644  16.551  1.00 63.22           C  
ANISOU   53  C   ARG A  10    12196   5721   6105    518  -1457     -2       C  
ATOM     54  O   ARG A  10      31.755  33.491  17.413  1.00 66.85           O  
ANISOU   54  O   ARG A  10    12607   6216   6578    470  -1446     11       O  
ATOM     55  CB  ARG A  10      31.391  30.256  17.158  1.00 62.38           C  
ANISOU   55  CB  ARG A  10    11627   5858   6216    484  -1275      7       C  
ATOM     56  CG  ARG A  10      30.607  29.030  17.585  1.00 61.51           C  
ANISOU   56  CG  ARG A  10    11252   5866   6254    526  -1281    -64       C  
ATOM     57  CD  ARG A  10      29.588  29.272  18.690  1.00 62.56           C  
ANISOU   57  CD  ARG A  10    11166   6094   6510    571  -1378   -188       C  
ATOM     58  NE  ARG A  10      28.759  28.080  18.824  1.00 61.95           N  
ANISOU   58  NE  ARG A  10    10889   6099   6549    605  -1389   -272       N  
ATOM     59  CZ  ARG A  10      27.451  28.068  19.046  1.00 62.67           C  
ANISOU   59  CZ  ARG A  10    10864   6216   6731    698  -1533   -447       C  
ATOM     60  NH1 ARG A  10      26.765  29.183  19.227  1.00 63.74           N  
ANISOU   60  NH1 ARG A  10    11042   6309   6867    783  -1694   -569       N  
ATOM     61  NH2 ARG A  10      26.819  26.908  19.094  1.00 66.08           N  
ANISOU   61  NH2 ARG A  10    11130   6720   7259    703  -1516   -512       N  
ATOM     62  N   PHE A  11      32.025  32.661  15.343  1.00 64.12           N  
ANISOU   62  N   PHE A  11    12592   5701   6069    490  -1425     60       N  
ATOM     63  CA  PHE A  11      32.953  33.697  14.947  1.00 66.99           C  
ANISOU   63  CA  PHE A  11    13237   5950   6267    386  -1365    147       C  
ATOM     64  C   PHE A  11      32.268  35.061  14.965  1.00 69.23           C  
ANISOU   64  C   PHE A  11    13727   6094   6483    477  -1591     72       C  
ATOM     65  O   PHE A  11      32.828  36.023  15.466  1.00 66.57           O  
ANISOU   65  O   PHE A  11    13453   5741   6100    395  -1552    119       O  
ATOM     66  CB  PHE A  11      33.516  33.407  13.563  1.00 68.44           C  
ANISOU   66  CB  PHE A  11    13706   6010   6290    336  -1293    206       C  
ATOM     67  CG  PHE A  11      34.717  34.240  13.222  1.00 70.41           C  
ANISOU   67  CG  PHE A  11    14199   6177   6375    170  -1148    305       C  
ATOM     68  CD1 PHE A  11      35.991  33.763  13.471  1.00 69.70           C  
ANISOU   68  CD1 PHE A  11    13971   6205   6306      4   -880    393       C  
ATOM     69  CD2 PHE A  11      34.577  35.500  12.674  1.00 71.15           C  
ANISOU   69  CD2 PHE A  11    14661   6076   6297    177  -1282    300       C  
ATOM     70  CE1 PHE A  11      37.105  34.519  13.164  1.00 71.00           C  
ANISOU   70  CE1 PHE A  11    14342   6306   6329   -165   -730    464       C  
ATOM     71  CE2 PHE A  11      35.692  36.256  12.359  1.00 72.53           C  
ANISOU   71  CE2 PHE A  11    15071   6174   6313      0  -1132    388       C  
ATOM     72  CZ  PHE A  11      36.959  35.770  12.601  1.00 71.17           C  
ANISOU   72  CZ  PHE A  11    14740   6134   6169   -178   -846    465       C  
ATOM     73  N   LYS A  12      31.047  35.132  14.436  1.00 73.75           N  
ANISOU   73  N   LYS A  12    14398   6564   7059    653  -1838    -54       N  
ATOM     74  CA  LYS A  12      30.287  36.387  14.481  1.00 77.44           C  
ANISOU   74  CA  LYS A  12    15046   6896   7483    770  -2091   -154       C  
ATOM     75  C   LYS A  12      30.064  36.860  15.909  1.00 72.56           C  
ANISOU   75  C   LYS A  12    14147   6416   7009    770  -2098   -206       C  
ATOM     76  O   LYS A  12      30.440  37.959  16.222  1.00 75.16           O  
ANISOU   76  O   LYS A  12    14610   6680   7268    725  -2122   -175       O  
ATOM     77  CB  LYS A  12      28.950  36.290  13.735  1.00 80.98           C  
ANISOU   77  CB  LYS A  12    15601   7225   7942    981  -2375   -313       C  
ATOM     78  CG  LYS A  12      29.108  36.464  12.234  1.00 88.45           C  
ANISOU   78  CG  LYS A  12    16983   7946   8677   1000  -2457   -271       C  
ATOM     79  CD  LYS A  12      27.761  36.361  11.525  1.00 95.27           C  
ANISOU   79  CD  LYS A  12    17946   8691   9563   1225  -2762   -441       C  
ATOM     80  CE  LYS A  12      27.906  36.355  10.015  1.00 97.22           C  
ANISOU   80  CE  LYS A  12    18623   8721   9597   1242  -2836   -396       C  
ATOM     81  NZ  LYS A  12      27.310  35.126   9.419  1.00103.36           N  
ANISOU   81  NZ  LYS A  12    19284   9540  10447   1332  -2864   -463       N  
ATOM     82  N   ASP A  13      29.458  36.037  16.756  1.00 69.88           N  
ANISOU   82  N   ASP A  13    13434   6260   6858    810  -2074   -286       N  
ATOM     83  CA  ASP A  13      29.095  36.479  18.089  1.00 68.94           C  
ANISOU   83  CA  ASP A  13    13056   6269   6870    817  -2097   -361       C  
ATOM     84  C   ASP A  13      30.313  36.811  18.927  1.00 65.30           C  
ANISOU   84  C   ASP A  13    12523   5898   6392    641  -1882   -217       C  
ATOM     85  O   ASP A  13      30.265  37.760  19.675  1.00 67.11           O  
ANISOU   85  O   ASP A  13    12730   6133   6636    640  -1937   -249       O  
ATOM     86  CB  ASP A  13      28.250  35.438  18.828  1.00 74.18           C  
ANISOU   86  CB  ASP A  13    13345   7117   7725    861  -2081   -473       C  
ATOM     87  CG  ASP A  13      26.781  35.428  18.386  1.00 80.98           C  
ANISOU   87  CG  ASP A  13    14201   7915   8651   1057  -2341   -688       C  
ATOM     88  OD1 ASP A  13      26.423  36.110  17.408  1.00 86.40           O  
ANISOU   88  OD1 ASP A  13    15190   8406   9233   1175  -2547   -741       O  
ATOM     89  OD2 ASP A  13      25.971  34.713  19.014  1.00 89.57           O  
ANISOU   89  OD2 ASP A  13    14986   9149   9897   1089  -2342   -813       O  
ATOM     90  N   LEU A  14      31.397  36.050  18.818  1.00 61.38           N  
ANISOU   90  N   LEU A  14    11982   5469   5870    500  -1647    -72       N  
ATOM     91  CA  LEU A  14      32.538  36.215  19.741  1.00 58.31           C  
ANISOU   91  CA  LEU A  14    11462   5193   5499    339  -1442     44       C  
ATOM     92  C   LEU A  14      33.608  37.217  19.315  1.00 59.16           C  
ANISOU   92  C   LEU A  14    11849   5180   5448    227  -1371    147       C  
ATOM     93  O   LEU A  14      34.308  37.784  20.162  1.00 58.67           O  
ANISOU   93  O   LEU A  14    11708   5182   5401    126  -1275    200       O  
ATOM     94  CB  LEU A  14      33.219  34.865  19.984  1.00 55.79           C  
ANISOU   94  CB  LEU A  14    10919   5023   5257    244  -1228    129       C  
ATOM     95  CG  LEU A  14      32.370  33.836  20.740  1.00 53.89           C  
ANISOU   95  CG  LEU A  14    10362   4933   5180    300  -1245     49       C  
ATOM     96  CD1 LEU A  14      32.964  32.426  20.611  1.00 50.58           C  
ANISOU   96  CD1 LEU A  14     9808   4603   4807    231  -1075    130       C  
ATOM     97  CD2 LEU A  14      32.211  34.292  22.186  1.00 49.58           C  
ANISOU   97  CD2 LEU A  14     9597   4511   4728    269  -1241     14       C  
ATOM     98  N   GLY A  15      33.752  37.407  18.008  1.00 59.66           N  
ANISOU   98  N   GLY A  15    12242   5071   5357    233  -1410    174       N  
ATOM     99  CA  GLY A  15      34.857  38.152  17.464  1.00 60.82           C  
ANISOU   99  CA  GLY A  15    12665   5105   5337     89  -1297    277       C  
ATOM    100  C   GLY A  15      36.145  37.351  17.360  1.00 61.12           C  
ANISOU  100  C   GLY A  15    12603   5246   5375    -77  -1017    385       C  
ATOM    101  O   GLY A  15      36.415  36.457  18.141  1.00 57.67           O  
ANISOU  101  O   GLY A  15    11841   4988   5083   -106   -895    401       O  
ATOM    102  N   GLU A  16      36.970  37.714  16.386  1.00 64.96           N  
ANISOU  102  N   GLU A  16    13386   5608   5689   -196   -916    449       N  
ATOM    103  CA  GLU A  16      38.205  37.000  16.119  1.00 66.07           C  
ANISOU  103  CA  GLU A  16    13454   5831   5819   -354   -652    523       C  
ATOM    104  C   GLU A  16      39.110  36.838  17.346  1.00 63.89           C  
ANISOU  104  C   GLU A  16    12856   5742   5679   -460   -477    563       C  
ATOM    105  O   GLU A  16      39.743  35.816  17.492  1.00 65.13           O  
ANISOU  105  O   GLU A  16    12796   6027   5924   -512   -318    586       O  
ATOM    106  CB  GLU A  16      38.956  37.680  14.975  1.00 69.83           C  
ANISOU  106  CB  GLU A  16    14322   6137   6072   -492   -565    569       C  
ATOM    107  CG  GLU A  16      40.188  36.930  14.497  1.00 73.79           C  
ANISOU  107  CG  GLU A  16    14771   6713   6551   -655   -291    614       C  
ATOM    108  CD  GLU A  16      40.734  37.435  13.161  1.00 79.89           C  
ANISOU  108  CD  GLU A  16    15962   7309   7085   -789   -208    638       C  
ATOM    109  OE1 GLU A  16      41.846  36.986  12.776  1.00 85.07           O  
ANISOU  109  OE1 GLU A  16    16585   8025   7712   -951     39    657       O  
ATOM    110  OE2 GLU A  16      40.065  38.266  12.491  1.00 84.25           O  
ANISOU  110  OE2 GLU A  16    16880   7658   7474   -736   -389    630       O  
ATOM    111  N   GLU A  17      39.167  37.820  18.224  1.00 63.34           N  
ANISOU  111  N   GLU A  17    12757   5683   5627   -485   -520    563       N  
ATOM    112  CA  GLU A  17      40.150  37.810  19.304  1.00 64.93           C  
ANISOU  112  CA  GLU A  17    12703   6039   5931   -601   -355    602       C  
ATOM    113  C   GLU A  17      39.863  36.635  20.278  1.00 63.86           C  
ANISOU  113  C   GLU A  17    12180   6094   5992   -528   -343    588       C  
ATOM    114  O   GLU A  17      40.708  35.755  20.516  1.00 60.42           O  
ANISOU  114  O   GLU A  17    11546   5777   5636   -599   -179    620       O  
ATOM    115  CB  GLU A  17      40.085  39.154  20.033  1.00 70.11           C  
ANISOU  115  CB  GLU A  17    13427   6652   6560   -622   -437    597       C  
ATOM    116  CG  GLU A  17      41.343  39.576  20.763  1.00 77.10           C  
ANISOU  116  CG  GLU A  17    14198   7625   7473   -787   -256    642       C  
ATOM    117  CD  GLU A  17      41.120  40.816  21.632  1.00 82.42           C  
ANISOU  117  CD  GLU A  17    14898   8271   8145   -782   -362    629       C  
ATOM    118  OE1 GLU A  17      40.602  41.832  21.104  1.00 89.72           O  
ANISOU  118  OE1 GLU A  17    16128   9022   8941   -749   -506    610       O  
ATOM    119  OE2 GLU A  17      41.463  40.776  22.837  1.00 79.07           O  
ANISOU  119  OE2 GLU A  17    14203   7994   7847   -809   -311    634       O  
ATOM    120  N   HIS A  18      38.647  36.648  20.825  1.00 60.76           N  
ANISOU  120  N   HIS A  18    11693   5719   5673   -386   -525    527       N  
ATOM    121  CA  HIS A  18      38.190  35.655  21.765  1.00 55.66           C  
ANISOU  121  CA  HIS A  18    10724   5232   5191   -325   -533    504       C  
ATOM    122  C   HIS A  18      38.056  34.318  21.061  1.00 55.15           C  
ANISOU  122  C   HIS A  18    10608   5188   5157   -285   -492    505       C  
ATOM    123  O   HIS A  18      38.376  33.257  21.654  1.00 52.72           O  
ANISOU  123  O   HIS A  18    10053   5015   4964   -307   -399    528       O  
ATOM    124  CB  HIS A  18      36.843  36.078  22.368  1.00 53.80           C  
ANISOU  124  CB  HIS A  18    10432   4998   5010   -194   -734    411       C  
ATOM    125  CG  HIS A  18      36.930  37.241  23.303  1.00 54.43           C  
ANISOU  125  CG  HIS A  18    10495   5091   5095   -224   -774    400       C  
ATOM    126  ND1 HIS A  18      38.135  37.740  23.765  1.00 54.62           N  
ANISOU  126  ND1 HIS A  18    10505   5151   5099   -362   -632    475       N  
ATOM    127  CD2 HIS A  18      35.964  37.980  23.906  1.00 53.92           C  
ANISOU  127  CD2 HIS A  18    10405   5019   5063   -134   -940    310       C  
ATOM    128  CE1 HIS A  18      37.909  38.754  24.583  1.00 53.00           C  
ANISOU  128  CE1 HIS A  18    10286   4949   4904   -356   -711    444       C  
ATOM    129  NE2 HIS A  18      36.601  38.910  24.699  1.00 52.78           N  
ANISOU  129  NE2 HIS A  18    10246   4898   4909   -217   -896    343       N  
ATOM    130  N   PHE A  19      37.584  34.350  19.807  1.00 54.47           N  
ANISOU  130  N   PHE A  19    10768   4964   4965   -226   -569    479       N  
ATOM    131  CA  PHE A  19      37.500  33.104  18.999  1.00 53.62           C  
ANISOU  131  CA  PHE A  19    10640   4862   4872   -191   -527    479       C  
ATOM    132  C   PHE A  19      38.865  32.425  18.986  1.00 53.25           C  
ANISOU  132  C   PHE A  19    10487   4897   4847   -320   -304    548       C  
ATOM    133  O   PHE A  19      38.940  31.261  19.292  1.00 49.04           O  
ANISOU  133  O   PHE A  19     9740   4467   4424   -303   -251    554       O  
ATOM    134  CB  PHE A  19      37.023  33.357  17.564  1.00 53.71           C  
ANISOU  134  CB  PHE A  19    10976   4696   4737   -132   -624    451       C  
ATOM    135  CG  PHE A  19      36.781  32.103  16.776  1.00 52.79           C  
ANISOU  135  CG  PHE A  19    10832   4584   4641    -79   -605    438       C  
ATOM    136  CD1 PHE A  19      37.810  31.489  16.092  1.00 52.19           C  
ANISOU  136  CD1 PHE A  19    10796   4514   4518   -178   -425    491       C  
ATOM    137  CD2 PHE A  19      35.520  31.537  16.717  1.00 53.08           C  
ANISOU  137  CD2 PHE A  19    10797   4622   4750     67   -767    359       C  
ATOM    138  CE1 PHE A  19      37.601  30.340  15.372  1.00 50.51           C  
ANISOU  138  CE1 PHE A  19    10560   4305   4326   -128   -410    475       C  
ATOM    139  CE2 PHE A  19      35.306  30.353  16.020  1.00 52.10           C  
ANISOU  139  CE2 PHE A  19    10641   4504   4650    112   -748    346       C  
ATOM    140  CZ  PHE A  19      36.346  29.777  15.323  1.00 51.04           C  
ANISOU  140  CZ  PHE A  19    10565   4368   4462     18   -574    409       C  
ATOM    141  N   LYS A  20      39.944  33.166  18.681  1.00 54.78           N  
ANISOU  141  N   LYS A  20    10824   5046   4945   -452   -178    589       N  
ATOM    142  CA  LYS A  20      41.285  32.556  18.659  1.00 55.02           C  
ANISOU  142  CA  LYS A  20    10733   5162   5010   -575     36    624       C  
ATOM    143  C   LYS A  20      41.729  32.091  20.057  1.00 52.53           C  
ANISOU  143  C   LYS A  20    10086   5014   4861   -593     87    640       C  
ATOM    144  O   LYS A  20      42.265  31.005  20.210  1.00 52.09           O  
ANISOU  144  O   LYS A  20     9843   5050   4899   -603    176    646       O  
ATOM    145  CB  LYS A  20      42.335  33.475  18.039  1.00 57.71           C  
ANISOU  145  CB  LYS A  20    11290   5425   5213   -730    174    642       C  
ATOM    146  CG  LYS A  20      41.984  33.945  16.632  1.00 62.19           C  
ANISOU  146  CG  LYS A  20    12232   5811   5589   -734    131    634       C  
ATOM    147  CD  LYS A  20      43.078  33.713  15.597  1.00 63.51           C  
ANISOU  147  CD  LYS A  20    12531   5948   5654   -881    338    635       C  
ATOM    148  CE  LYS A  20      44.188  34.744  15.676  1.00 66.05           C  
ANISOU  148  CE  LYS A  20    12956   6250   5891  -1071    494    646       C  
ATOM    149  NZ  LYS A  20      45.159  34.614  14.556  1.00 67.95           N  
ANISOU  149  NZ  LYS A  20    13362   6447   6007  -1232    702    626       N  
ATOM    150  N   GLY A  21      41.506  32.901  21.074  1.00 51.35           N  
ANISOU  150  N   GLY A  21     9872   4895   4742   -592     20    643       N  
ATOM    151  CA  GLY A  21      41.800  32.471  22.442  1.00 51.14           C  
ANISOU  151  CA  GLY A  21     9555   5017   4859   -602     44    658       C  
ATOM    152  C   GLY A  21      41.144  31.126  22.789  1.00 50.31           C  
ANISOU  152  C   GLY A  21     9261   4989   4866   -509     -9    649       C  
ATOM    153  O   GLY A  21      41.818  30.150  23.110  1.00 49.98           O  
ANISOU  153  O   GLY A  21     9047   5032   4911   -534     74    668       O  
ATOM    154  N   LEU A  22      39.827  31.069  22.656  1.00 49.55           N  
ANISOU  154  N   LEU A  22     9210   4853   4764   -403   -154    608       N  
ATOM    155  CA  LEU A  22      39.073  29.887  23.027  1.00 47.56           C  
ANISOU  155  CA  LEU A  22     8791   4669   4610   -330   -208    588       C  
ATOM    156  C   LEU A  22      39.547  28.612  22.287  1.00 49.59           C  
ANISOU  156  C   LEU A  22     9019   4931   4892   -328   -125    607       C  
ATOM    157  O   LEU A  22      39.662  27.557  22.880  1.00 52.18           O  
ANISOU  157  O   LEU A  22     9165   5342   5317   -324   -102    622       O  
ATOM    158  CB  LEU A  22      37.600  30.149  22.774  1.00 46.74           C  
ANISOU  158  CB  LEU A  22     8765   4509   4487   -221   -372    513       C  
ATOM    159  CG  LEU A  22      37.046  31.143  23.777  1.00 47.34           C  
ANISOU  159  CG  LEU A  22     8792   4614   4580   -211   -459    474       C  
ATOM    160  CD1 LEU A  22      35.663  31.591  23.340  1.00 48.15           C  
ANISOU  160  CD1 LEU A  22     8998   4640   4657    -95   -633    372       C  
ATOM    161  CD2 LEU A  22      37.037  30.519  25.168  1.00 46.12           C  
ANISOU  161  CD2 LEU A  22     8380   4603   4539   -247   -426    486       C  
ATOM    162  N   VAL A  23      39.826  28.720  20.995  1.00 50.32           N  
ANISOU  162  N   VAL A  23     9304   4926   4888   -334    -84    602       N  
ATOM    163  CA  VAL A  23      40.385  27.630  20.235  1.00 49.12           C  
ANISOU  163  CA  VAL A  23     9136   4777   4751   -341      7    610       C  
ATOM    164  C   VAL A  23      41.802  27.277  20.690  1.00 49.90           C  
ANISOU  164  C   VAL A  23     9084   4961   4915   -434    156    638       C  
ATOM    165  O   VAL A  23      42.152  26.094  20.764  1.00 49.53           O  
ANISOU  165  O   VAL A  23     8895   4968   4954   -416    195    640       O  
ATOM    166  CB  VAL A  23      40.386  27.974  18.739  1.00 49.08           C  
ANISOU  166  CB  VAL A  23     9399   4644   4606   -343     24    592       C  
ATOM    167  CG1 VAL A  23      41.102  26.898  17.957  1.00 47.68           C  
ANISOU  167  CG1 VAL A  23     9197   4478   4442   -364    141    589       C  
ATOM    168  CG2 VAL A  23      38.954  28.111  18.272  1.00 48.12           C  
ANISOU  168  CG2 VAL A  23     9405   4436   4440   -225   -150    547       C  
ATOM    169  N   LEU A  24      42.635  28.279  20.963  1.00 50.64           N  
ANISOU  169  N   LEU A  24     9209   5061   4971   -529    232    650       N  
ATOM    170  CA  LEU A  24      43.984  27.999  21.484  1.00 50.70           C  
ANISOU  170  CA  LEU A  24     9049   5156   5057   -611    361    654       C  
ATOM    171  C   LEU A  24      43.842  27.171  22.757  1.00 51.08           C  
ANISOU  171  C   LEU A  24     8858   5307   5245   -563    297    675       C  
ATOM    172  O   LEU A  24      44.610  26.219  23.011  1.00 51.80           O  
ANISOU  172  O   LEU A  24     8793   5459   5429   -566    349    669       O  
ATOM    173  CB  LEU A  24      44.719  29.296  21.807  1.00 50.52           C  
ANISOU  173  CB  LEU A  24     9078   5132   4984   -719    430    658       C  
ATOM    174  CG  LEU A  24      46.111  29.225  22.443  1.00 50.52           C  
ANISOU  174  CG  LEU A  24     8897   5226   5072   -808    551    642       C  
ATOM    175  CD1 LEU A  24      46.921  28.092  21.812  1.00 50.00           C  
ANISOU  175  CD1 LEU A  24     8741   5193   5066   -814    654    599       C  
ATOM    176  CD2 LEU A  24      46.837  30.582  22.311  1.00 48.58           C  
ANISOU  176  CD2 LEU A  24     8770   4948   4740   -937    647    630       C  
ATOM    177  N   ILE A  25      42.841  27.530  23.556  1.00 48.96           N  
ANISOU  177  N   ILE A  25     8570   5050   4984   -519    180    689       N  
ATOM    178  CA  ILE A  25      42.616  26.833  24.793  1.00 49.91           C  
ANISOU  178  CA  ILE A  25     8500   5257   5208   -494    122    710       C  
ATOM    179  C   ILE A  25      42.220  25.390  24.509  1.00 50.68           C  
ANISOU  179  C   ILE A  25     8538   5356   5361   -429     92    707       C  
ATOM    180  O   ILE A  25      42.828  24.467  25.049  1.00 49.68           O  
ANISOU  180  O   ILE A  25     8273   5283   5321   -433    110    724       O  
ATOM    181  CB  ILE A  25      41.575  27.536  25.677  1.00 48.24           C  
ANISOU  181  CB  ILE A  25     8281   5062   4985   -474     17    707       C  
ATOM    182  CG1 ILE A  25      42.166  28.815  26.279  1.00 47.48           C  
ANISOU  182  CG1 ILE A  25     8196   4983   4862   -544     46    717       C  
ATOM    183  CG2 ILE A  25      41.170  26.610  26.806  1.00 48.24           C  
ANISOU  183  CG2 ILE A  25     8115   5140   5073   -458    -37    723       C  
ATOM    184  CD1 ILE A  25      41.110  29.783  26.736  1.00 47.40           C  
ANISOU  184  CD1 ILE A  25     8240   4958   4812   -518    -57    692       C  
ATOM    185  N   ALA A  26      41.214  25.211  23.652  1.00 52.36           N  
ANISOU  185  N   ALA A  26     8865   5504   5524   -367     36    682       N  
ATOM    186  CA  ALA A  26      40.713  23.883  23.299  1.00 50.98           C  
ANISOU  186  CA  ALA A  26     8651   5323   5397   -306      2    673       C  
ATOM    187  C   ALA A  26      41.880  22.991  22.942  1.00 51.45           C  
ANISOU  187  C   ALA A  26     8646   5397   5506   -321     92    681       C  
ATOM    188  O   ALA A  26      42.088  21.968  23.591  1.00 51.45           O  
ANISOU  188  O   ALA A  26     8514   5440   5593   -308     72    698       O  
ATOM    189  CB  ALA A  26      39.746  23.947  22.132  1.00 52.01           C  
ANISOU  189  CB  ALA A  26     8939   5367   5455   -240    -53    631       C  
ATOM    190  N   PHE A  27      42.678  23.391  21.962  1.00 50.04           N  
ANISOU  190  N   PHE A  27     8562   5179   5270   -356    190    659       N  
ATOM    191  CA  PHE A  27      43.820  22.570  21.584  1.00 52.14           C  
ANISOU  191  CA  PHE A  27     8749   5467   5593   -371    284    638       C  
ATOM    192  C   PHE A  27      44.775  22.367  22.729  1.00 53.13           C  
ANISOU  192  C   PHE A  27     8691   5674   5821   -404    300    648       C  
ATOM    193  O   PHE A  27      45.320  21.279  22.901  1.00 55.32           O  
ANISOU  193  O   PHE A  27     8850   5978   6191   -373    297    634       O  
ATOM    194  CB  PHE A  27      44.565  23.155  20.405  1.00 55.63           C  
ANISOU  194  CB  PHE A  27     9322   5865   5949   -432    410    597       C  
ATOM    195  CG  PHE A  27      43.894  22.908  19.082  1.00 56.69           C  
ANISOU  195  CG  PHE A  27     9633   5912   5993   -389    401    577       C  
ATOM    196  CD1 PHE A  27      43.734  21.626  18.608  1.00 58.22           C  
ANISOU  196  CD1 PHE A  27     9781   6100   6239   -322    384    558       C  
ATOM    197  CD2 PHE A  27      43.434  23.956  18.320  1.00 58.03           C  
ANISOU  197  CD2 PHE A  27    10027   5997   6023   -413    398    575       C  
ATOM    198  CE1 PHE A  27      43.113  21.394  17.387  1.00 61.98           C  
ANISOU  198  CE1 PHE A  27    10423   6495   6632   -280    370    536       C  
ATOM    199  CE2 PHE A  27      42.819  23.738  17.096  1.00 60.08           C  
ANISOU  199  CE2 PHE A  27    10468   6166   6192   -368    374    554       C  
ATOM    200  CZ  PHE A  27      42.660  22.458  16.624  1.00 61.36           C  
ANISOU  200  CZ  PHE A  27    10573   6332   6409   -302    364    533       C  
ATOM    201  N   SER A  28      44.964  23.385  23.553  1.00 53.33           N  
ANISOU  201  N   SER A  28     8695   5734   5835   -458    300    667       N  
ATOM    202  CA  SER A  28      45.830  23.194  24.712  1.00 52.24           C  
ANISOU  202  CA  SER A  28     8386   5669   5794   -481    295    674       C  
ATOM    203  C   SER A  28      45.279  22.188  25.740  1.00 49.73           C  
ANISOU  203  C   SER A  28     7970   5377   5549   -427    178    716       C  
ATOM    204  O   SER A  28      46.045  21.471  26.344  1.00 51.08           O  
ANISOU  204  O   SER A  28     8019   5580   5808   -415    158    711       O  
ATOM    205  CB  SER A  28      46.160  24.531  25.354  1.00 52.21           C  
ANISOU  205  CB  SER A  28     8386   5694   5758   -555    322    683       C  
ATOM    206  OG  SER A  28      46.772  25.396  24.416  1.00 53.64           O  
ANISOU  206  OG  SER A  28     8671   5843   5867   -625    441    644       O  
ATOM    207  N   GLN A  29      43.972  22.107  25.932  1.00 48.58           N  
ANISOU  207  N   GLN A  29     7881   5212   5365   -399     97    745       N  
ATOM    208  CA  GLN A  29      43.426  21.192  26.947  1.00 48.44           C  
ANISOU  208  CA  GLN A  29     7790   5217   5399   -378      3    781       C  
ATOM    209  C   GLN A  29      43.337  19.740  26.457  1.00 49.35           C  
ANISOU  209  C   GLN A  29     7893   5296   5561   -321    -26    776       C  
ATOM    210  O   GLN A  29      43.554  18.819  27.217  1.00 47.89           O  
ANISOU  210  O   GLN A  29     7640   5120   5437   -311    -84    800       O  
ATOM    211  CB  GLN A  29      42.067  21.666  27.452  1.00 48.01           C  
ANISOU  211  CB  GLN A  29     7778   5169   5293   -388    -60    792       C  
ATOM    212  CG  GLN A  29      42.142  22.999  28.179  1.00 48.39           C  
ANISOU  212  CG  GLN A  29     7822   5257   5308   -440    -54    797       C  
ATOM    213  CD  GLN A  29      40.810  23.514  28.679  1.00 48.16           C  
ANISOU  213  CD  GLN A  29     7819   5241   5238   -445   -116    781       C  
ATOM    214  OE1 GLN A  29      39.783  23.401  27.994  1.00 49.47           O  
ANISOU  214  OE1 GLN A  29     8050   5371   5376   -403   -149    743       O  
ATOM    215  NE2 GLN A  29      40.823  24.125  29.865  1.00 47.25           N  
ANISOU  215  NE2 GLN A  29     7648   5181   5123   -495   -136    796       N  
ATOM    216  N   TYR A  30      43.051  19.548  25.173  1.00 51.16           N  
ANISOU  216  N   TYR A  30     8205   5477   5757   -284     10    743       N  
ATOM    217  CA  TYR A  30      43.027  18.214  24.591  1.00 51.30           C  
ANISOU  217  CA  TYR A  30     8216   5456   5819   -228    -10    730       C  
ATOM    218  C   TYR A  30      44.419  17.651  24.399  1.00 51.47           C  
ANISOU  218  C   TYR A  30     8153   5487   5915   -212     35    698       C  
ATOM    219  O   TYR A  30      44.633  16.486  24.653  1.00 54.09           O  
ANISOU  219  O   TYR A  30     8429   5804   6318   -170    -22    700       O  
ATOM    220  CB  TYR A  30      42.315  18.206  23.244  1.00 52.71           C  
ANISOU  220  CB  TYR A  30     8514   5578   5935   -190     12    696       C  
ATOM    221  CG  TYR A  30      40.823  18.208  23.323  1.00 53.66           C  
ANISOU  221  CG  TYR A  30     8691   5680   6018   -172    -66    699       C  
ATOM    222  CD1 TYR A  30      40.109  17.065  23.083  1.00 56.76           C  
ANISOU  222  CD1 TYR A  30     9085   6041   6439   -130   -119    691       C  
ATOM    223  CD2 TYR A  30      40.123  19.365  23.603  1.00 54.89           C  
ANISOU  223  CD2 TYR A  30     8894   5847   6116   -196    -87    693       C  
ATOM    224  CE1 TYR A  30      38.723  17.062  23.133  1.00 58.16           C  
ANISOU  224  CE1 TYR A  30     9297   6209   6593   -120   -184    669       C  
ATOM    225  CE2 TYR A  30      38.750  19.385  23.638  1.00 54.64           C  
ANISOU  225  CE2 TYR A  30     8894   5803   6062   -173   -160    665       C  
ATOM    226  CZ  TYR A  30      38.053  18.239  23.413  1.00 55.82           C  
ANISOU  226  CZ  TYR A  30     9031   5931   6246   -139   -204    648       C  
ATOM    227  OH  TYR A  30      36.692  18.263  23.484  1.00 55.08           O  
ANISOU  227  OH  TYR A  30     8949   5837   6144   -125   -272    598       O  
ATOM    228  N   LEU A  31      45.348  18.462  23.928  1.00 52.71           N  
ANISOU  228  N   LEU A  31     8305   5664   6058   -249    137    655       N  
ATOM    229  CA  LEU A  31      46.696  17.998  23.612  1.00 56.39           C  
ANISOU  229  CA  LEU A  31     8674   6148   6602   -240    197    588       C  
ATOM    230  C   LEU A  31      47.736  18.732  24.457  1.00 56.60           C  
ANISOU  230  C   LEU A  31     8595   6235   6673   -292    227    569       C  
ATOM    231  O   LEU A  31      48.397  19.653  23.998  1.00 58.64           O  
ANISOU  231  O   LEU A  31     8864   6516   6900   -356    342    522       O  
ATOM    232  CB  LEU A  31      46.992  18.222  22.139  1.00 57.66           C  
ANISOU  232  CB  LEU A  31     8918   6284   6708   -255    320    523       C  
ATOM    233  CG  LEU A  31      46.023  17.599  21.136  1.00 59.35           C  
ANISOU  233  CG  LEU A  31     9250   6433   6868   -202    298    529       C  
ATOM    234  CD1 LEU A  31      46.513  17.968  19.727  1.00 56.91           C  
ANISOU  234  CD1 LEU A  31     9035   6099   6488   -237    434    460       C  
ATOM    235  CD2 LEU A  31      45.911  16.071  21.333  1.00 58.34           C  
ANISOU  235  CD2 LEU A  31     9047   6286   6834   -120    206    529       C  
ATOM    236  N   GLN A  32      47.912  18.266  25.681  1.00 56.83           N  
ANISOU  236  N   GLN A  32     8532   6286   6775   -269    122    602       N  
ATOM    237  CA  GLN A  32      48.604  19.033  26.702  1.00 56.55           C  
ANISOU  237  CA  GLN A  32     8413   6304   6768   -315    116    602       C  
ATOM    238  C   GLN A  32      50.125  18.916  26.635  1.00 57.03           C  
ANISOU  238  C   GLN A  32     8332   6403   6933   -311    165    499       C  
ATOM    239  O   GLN A  32      50.817  19.549  27.413  1.00 53.54           O  
ANISOU  239  O   GLN A  32     7807   6007   6527   -347    164    480       O  
ATOM    240  CB  GLN A  32      48.123  18.570  28.082  1.00 55.31           C  
ANISOU  240  CB  GLN A  32     8238   6147   6632   -296    -27    678       C  
ATOM    241  CG  GLN A  32      46.615  18.525  28.244  1.00 54.13           C  
ANISOU  241  CG  GLN A  32     8200   5970   6399   -307    -74    755       C  
ATOM    242  CD  GLN A  32      46.188  17.832  29.519  1.00 53.35           C  
ANISOU  242  CD  GLN A  32     8094   5863   6314   -305   -200    817       C  
ATOM    243  OE1 GLN A  32      45.674  16.743  29.474  1.00 51.59           O  
ANISOU  243  OE1 GLN A  32     7908   5593   6099   -271   -264    839       O  
ATOM    244  NE2 GLN A  32      46.421  18.463  30.662  1.00 56.18           N  
ANISOU  244  NE2 GLN A  32     8417   6261   6666   -350   -233    845       N  
ATOM    245  N   GLN A  33      50.636  18.080  25.739  1.00 60.78           N  
ANISOU  245  N   GLN A  33     8768   6861   7464   -263    202    418       N  
ATOM    246  CA  GLN A  33      52.069  17.874  25.603  1.00 63.60           C  
ANISOU  246  CA  GLN A  33     8968   7261   7936   -252    249    286       C  
ATOM    247  C   GLN A  33      52.627  18.511  24.343  1.00 67.09           C  
ANISOU  247  C   GLN A  33     9424   7728   8340   -329    444    187       C  
ATOM    248  O   GLN A  33      53.839  18.450  24.099  1.00 73.34           O  
ANISOU  248  O   GLN A  33    10075   8567   9224   -343    519     49       O  
ATOM    249  CB  GLN A  33      52.384  16.385  25.546  1.00 64.69           C  
ANISOU  249  CB  GLN A  33     9033   7365   8182   -139    144    236       C  
ATOM    250  CG  GLN A  33      51.992  15.559  26.760  1.00 63.89           C  
ANISOU  250  CG  GLN A  33     8935   7221   8120    -67    -57    320       C  
ATOM    251  CD  GLN A  33      52.522  14.126  26.636  1.00 66.20           C  
ANISOU  251  CD  GLN A  33     9158   7468   8528     48   -166    248       C  
ATOM    252  OE1 GLN A  33      53.734  13.902  26.755  1.00 70.07           O  
ANISOU  252  OE1 GLN A  33     9496   7987   9142     95   -188    120       O  
ATOM    253  NE2 GLN A  33      51.630  13.156  26.361  1.00 62.20           N  
ANISOU  253  NE2 GLN A  33     8755   6888   7988     97   -238    314       N  
ATOM    254  N   CYS A  34      51.765  19.092  23.513  1.00 69.63           N  
ANISOU  254  N   CYS A  34     9919   8013   8524   -382    524    244       N  
ATOM    255  CA  CYS A  34      52.224  19.696  22.256  1.00 70.71           C  
ANISOU  255  CA  CYS A  34    10120   8155   8593   -470    711    160       C  
ATOM    256  C   CYS A  34      52.753  21.085  22.554  1.00 70.87           C  
ANISOU  256  C   CYS A  34    10141   8215   8569   -591    810    144       C  
ATOM    257  O   CYS A  34      52.344  21.693  23.535  1.00 73.37           O  
ANISOU  257  O   CYS A  34    10470   8538   8868   -599    730    229       O  
ATOM    258  CB  CYS A  34      51.097  19.739  21.222  1.00 70.81           C  
ANISOU  258  CB  CYS A  34    10344   8095   8468   -470    734    224       C  
ATOM    259  SG  CYS A  34      50.907  18.192  20.307  1.00 72.21           S  
ANISOU  259  SG  CYS A  34    10516   8231   8691   -366    704    178       S  
ATOM    260  N   PRO A  35      53.672  21.590  21.724  1.00 72.96           N  
ANISOU  260  N   PRO A  35    10397   8509   8816   -696    992     27       N  
ATOM    261  CA  PRO A  35      54.248  22.918  21.964  1.00 70.84           C  
ANISOU  261  CA  PRO A  35    10137   8275   8505   -830   1101      1       C  
ATOM    262  C   PRO A  35      53.439  24.070  21.374  1.00 69.53           C  
ANISOU  262  C   PRO A  35    10230   8040   8148   -922   1164     88       C  
ATOM    263  O   PRO A  35      52.709  23.900  20.386  1.00 68.65           O  
ANISOU  263  O   PRO A  35    10298   7859   7929   -910   1182    123       O  
ATOM    264  CB  PRO A  35      55.633  22.829  21.303  1.00 71.98           C  
ANISOU  264  CB  PRO A  35    10147   8482   8721   -913   1278   -187       C  
ATOM    265  CG  PRO A  35      55.518  21.754  20.270  1.00 74.09           C  
ANISOU  265  CG  PRO A  35    10436   8723   8993   -852   1305   -241       C  
ATOM    266  CD  PRO A  35      54.269  20.938  20.540  1.00 75.03           C  
ANISOU  266  CD  PRO A  35    10634   8775   9097   -707   1115   -100       C  
ATOM    267  N   PHE A  36      53.605  25.241  21.985  1.00 67.49           N  
ANISOU  267  N   PHE A  36     9994   7796   7853  -1008   1186    115       N  
ATOM    268  CA  PHE A  36      52.801  26.414  21.696  1.00 66.33           C  
ANISOU  268  CA  PHE A  36    10090   7575   7538  -1077   1199    205       C  
ATOM    269  C   PHE A  36      52.801  26.781  20.230  1.00 69.31           C  
ANISOU  269  C   PHE A  36    10686   7883   7766  -1175   1348    169       C  
ATOM    270  O   PHE A  36      51.743  27.019  19.662  1.00 70.18           O  
ANISOU  270  O   PHE A  36    11020   7900   7745  -1147   1291    250       O  
ATOM    271  CB  PHE A  36      53.307  27.584  22.539  1.00 66.84           C  
ANISOU  271  CB  PHE A  36    10115   7676   7606  -1172   1226    205       C  
ATOM    272  CG  PHE A  36      52.553  28.863  22.338  1.00 64.70           C  
ANISOU  272  CG  PHE A  36    10092   7322   7170  -1240   1223    288       C  
ATOM    273  CD1 PHE A  36      51.263  29.001  22.795  1.00 62.41           C  
ANISOU  273  CD1 PHE A  36     9898   6983   6833  -1143   1058    402       C  
ATOM    274  CD2 PHE A  36      53.146  29.928  21.712  1.00 66.51           C  
ANISOU  274  CD2 PHE A  36    10458   7519   7293  -1404   1382    241       C  
ATOM    275  CE1 PHE A  36      50.578  30.182  22.626  1.00 63.47           C  
ANISOU  275  CE1 PHE A  36    10253   7036   6827  -1188   1033    460       C  
ATOM    276  CE2 PHE A  36      52.465  31.124  21.539  1.00 67.03           C  
ANISOU  276  CE2 PHE A  36    10774   7491   7203  -1460   1359    317       C  
ATOM    277  CZ  PHE A  36      51.180  31.249  21.994  1.00 65.29           C  
ANISOU  277  CZ  PHE A  36    10639   7220   6948  -1341   1174    423       C  
ATOM    278  N   ASP A  37      53.974  26.807  19.606  1.00 76.04           N  
ANISOU  278  N   ASP A  37    11478   8777   8636  -1292   1535     37       N  
ATOM    279  CA  ASP A  37      54.062  27.159  18.175  1.00 80.44           C  
ANISOU  279  CA  ASP A  37    12265   9267   9033  -1414   1701     -7       C  
ATOM    280  C   ASP A  37      53.180  26.292  17.281  1.00 78.93           C  
ANISOU  280  C   ASP A  37    12204   9005   8779  -1311   1639     34       C  
ATOM    281  O   ASP A  37      52.535  26.804  16.367  1.00 81.03           O  
ANISOU  281  O   ASP A  37    12755   9166   8866  -1356   1661     83       O  
ATOM    282  CB  ASP A  37      55.510  27.110  17.678  1.00 85.29           C  
ANISOU  282  CB  ASP A  37    12749   9959   9699  -1558   1926   -186       C  
ATOM    283  CG  ASP A  37      56.311  28.352  18.076  1.00 91.94           C  
ANISOU  283  CG  ASP A  37    13583  10831  10517  -1731   2049   -234       C  
ATOM    284  OD1 ASP A  37      55.788  29.186  18.845  1.00 93.99           O  
ANISOU  284  OD1 ASP A  37    13916  11057  10738  -1721   1943   -124       O  
ATOM    285  OD2 ASP A  37      57.467  28.505  17.622  1.00 97.87           O  
ANISOU  285  OD2 ASP A  37    14251  11643  11291  -1884   2257   -393       O  
ATOM    286  N   GLU A  38      53.128  24.991  17.550  1.00 76.21           N  
ANISOU  286  N   GLU A  38    11669   8709   8578  -1169   1547     14       N  
ATOM    287  CA  GLU A  38      52.313  24.100  16.736  1.00 76.00           C  
ANISOU  287  CA  GLU A  38    11750   8621   8508  -1069   1485     45       C  
ATOM    288  C   GLU A  38      50.836  24.378  16.973  1.00 72.28           C  
ANISOU  288  C   GLU A  38    11449   8064   7950   -976   1307    191       C  
ATOM    289  O   GLU A  38      50.053  24.353  16.044  1.00 73.58           O  
ANISOU  289  O   GLU A  38    11827   8139   7990   -955   1287    224       O  
ATOM    290  CB  GLU A  38      52.629  22.617  16.998  1.00 80.70           C  
ANISOU  290  CB  GLU A  38    12103   9279   9280   -941   1422    -16       C  
ATOM    291  CG  GLU A  38      54.083  22.192  16.755  1.00 85.85           C  
ANISOU  291  CG  GLU A  38    12551  10022  10048  -1004   1577   -194       C  
ATOM    292  CD  GLU A  38      54.599  22.531  15.359  1.00 94.45           C  
ANISOU  292  CD  GLU A  38    13787  11091  11009  -1153   1801   -298       C  
ATOM    293  OE1 GLU A  38      54.521  21.648  14.465  1.00104.80           O  
ANISOU  293  OE1 GLU A  38    15124  12383  12312  -1109   1832   -351       O  
ATOM    294  OE2 GLU A  38      55.083  23.680  15.150  1.00 93.73           O  
ANISOU  294  OE2 GLU A  38    13798  10998  10817  -1324   1950   -328       O  
ATOM    295  N   HIS A  39      50.449  24.659  18.213  1.00 70.08           N  
ANISOU  295  N   HIS A  39    11075   7813   7737   -922   1175    265       N  
ATOM    296  CA  HIS A  39      49.049  24.939  18.511  1.00 66.29           C  
ANISOU  296  CA  HIS A  39    10728   7268   7193   -838   1010    376       C  
ATOM    297  C   HIS A  39      48.592  26.266  17.874  1.00 65.18           C  
ANISOU  297  C   HIS A  39    10870   7029   6866   -921   1038    410       C  
ATOM    298  O   HIS A  39      47.458  26.390  17.401  1.00 63.46           O  
ANISOU  298  O   HIS A  39    10838   6723   6553   -855    934    460       O  
ATOM    299  CB  HIS A  39      48.810  24.927  20.021  1.00 66.82           C  
ANISOU  299  CB  HIS A  39    10621   7397   7370   -778    880    432       C  
ATOM    300  CG  HIS A  39      48.583  23.556  20.597  1.00 69.26           C  
ANISOU  300  CG  HIS A  39    10755   7748   7814   -658    771    443       C  
ATOM    301  ND1 HIS A  39      48.246  22.464  19.826  1.00 68.95           N  
ANISOU  301  ND1 HIS A  39    10736   7677   7786   -585    753    425       N  
ATOM    302  CD2 HIS A  39      48.566  23.121  21.882  1.00 70.09           C  
ANISOU  302  CD2 HIS A  39    10689   7909   8032   -603    664    476       C  
ATOM    303  CE1 HIS A  39      48.064  21.413  20.605  1.00 68.00           C  
ANISOU  303  CE1 HIS A  39    10464   7589   7783   -493    643    446       C  
ATOM    304  NE2 HIS A  39      48.257  21.783  21.858  1.00 67.50           N  
ANISOU  304  NE2 HIS A  39    10292   7578   7779   -506    587    478       N  
ATOM    305  N   VAL A  40      49.477  27.251  17.824  1.00 61.83           N  
ANISOU  305  N   VAL A  40    10491   6613   6389  -1066   1173    373       N  
ATOM    306  CA  VAL A  40      49.134  28.482  17.149  1.00 62.39           C  
ANISOU  306  CA  VAL A  40    10863   6572   6270  -1157   1201    403       C  
ATOM    307  C   VAL A  40      48.803  28.254  15.656  1.00 64.78           C  
ANISOU  307  C   VAL A  40    11418   6772   6426  -1171   1250    385       C  
ATOM    308  O   VAL A  40      47.900  28.916  15.112  1.00 64.39           O  
ANISOU  308  O   VAL A  40    11643   6596   6224  -1153   1161    436       O  
ATOM    309  CB  VAL A  40      50.238  29.544  17.283  1.00 62.34           C  
ANISOU  309  CB  VAL A  40    10874   6587   6224  -1337   1362    357       C  
ATOM    310  CG1 VAL A  40      49.911  30.725  16.388  1.00 62.36           C  
ANISOU  310  CG1 VAL A  40    11242   6447   6004  -1443   1397    386       C  
ATOM    311  CG2 VAL A  40      50.365  30.018  18.718  1.00 60.86           C  
ANISOU  311  CG2 VAL A  40    10504   6474   6147  -1320   1286    389       C  
ATOM    312  N   LYS A  41      49.541  27.348  15.005  1.00 64.94           N  
ANISOU  312  N   LYS A  41    11348   6838   6489  -1200   1381    303       N  
ATOM    313  CA  LYS A  41      49.330  27.068  13.588  1.00 66.83           C  
ANISOU  313  CA  LYS A  41    11817   6989   6588  -1223   1443    276       C  
ATOM    314  C   LYS A  41      47.936  26.518  13.435  1.00 68.09           C  
ANISOU  314  C   LYS A  41    12056   7080   6736  -1048   1239    345       C  
ATOM    315  O   LYS A  41      47.183  26.972  12.572  1.00 69.67           O  
ANISOU  315  O   LYS A  41    12550   7150   6770  -1041   1182    376       O  
ATOM    316  CB  LYS A  41      50.340  26.053  13.014  1.00 66.70           C  
ANISOU  316  CB  LYS A  41    11644   7052   6648  -1266   1609    159       C  
ATOM    317  CG  LYS A  41      51.724  26.582  12.658  1.00 67.22           C  
ANISOU  317  CG  LYS A  41    11695   7167   6680  -1474   1859     46       C  
ATOM    318  N   LEU A  42      47.598  25.553  14.295  1.00 68.65           N  
ANISOU  318  N   LEU A  42    11871   7231   6982   -911   1123    363       N  
ATOM    319  CA  LEU A  42      46.310  24.866  14.235  1.00 68.10           C  
ANISOU  319  CA  LEU A  42    11828   7117   6930   -751    941    411       C  
ATOM    320  C   LEU A  42      45.194  25.869  14.446  1.00 67.55           C  
ANISOU  320  C   LEU A  42    11941   6959   6766   -710    789    475       C  
ATOM    321  O   LEU A  42      44.186  25.837  13.746  1.00 69.79           O  
ANISOU  321  O   LEU A  42    12411   7145   6961   -631    679    488       O  
ATOM    322  CB  LEU A  42      46.222  23.721  15.272  1.00 68.37           C  
ANISOU  322  CB  LEU A  42    11561   7253   7164   -641    854    419       C  
ATOM    323  CG  LEU A  42      47.234  22.560  15.137  1.00 69.47           C  
ANISOU  323  CG  LEU A  42    11499   7472   7425   -642    957    344       C  
ATOM    324  CD1 LEU A  42      47.114  21.497  16.223  1.00 66.26           C  
ANISOU  324  CD1 LEU A  42    10839   7141   7198   -534    844    364       C  
ATOM    325  CD2 LEU A  42      47.104  21.885  13.779  1.00 69.60           C  
ANISOU  325  CD2 LEU A  42    11648   7429   7369   -623   1008    298       C  
ATOM    326  N   VAL A  43      45.391  26.788  15.384  1.00 68.18           N  
ANISOU  326  N   VAL A  43    11971   7070   6864   -759    778    504       N  
ATOM    327  CA  VAL A  43      44.383  27.812  15.654  1.00 66.80           C  
ANISOU  327  CA  VAL A  43    11957   6816   6609   -718    629    549       C  
ATOM    328  C   VAL A  43      44.118  28.646  14.420  1.00 66.46           C  
ANISOU  328  C   VAL A  43    12275   6618   6358   -766    632    546       C  
ATOM    329  O   VAL A  43      42.976  28.846  14.024  1.00 66.73           O  
ANISOU  329  O   VAL A  43    12481   6552   6321   -665    470    557       O  
ATOM    330  CB  VAL A  43      44.796  28.766  16.773  1.00 65.26           C  
ANISOU  330  CB  VAL A  43    11671   6673   6452   -784    639    572       C  
ATOM    331  CG1 VAL A  43      43.789  29.906  16.858  1.00 63.79           C  
ANISOU  331  CG1 VAL A  43    11687   6384   6164   -744    488    602       C  
ATOM    332  CG2 VAL A  43      44.892  28.017  18.080  1.00 61.06           C  
ANISOU  332  CG2 VAL A  43    10817   6275   6108   -725    598    584       C  
ATOM    333  N   ASN A  44      45.185  29.129  13.811  1.00 69.32           N  
ANISOU  333  N   ASN A  44    12759   6958   6620   -927    816    521       N  
ATOM    334  CA  ASN A  44      45.048  29.974  12.626  1.00 71.15           C  
ANISOU  334  CA  ASN A  44    13377   7028   6626  -1005    835    522       C  
ATOM    335  C   ASN A  44      44.327  29.255  11.481  1.00 73.61           C  
ANISOU  335  C   ASN A  44    13857   7252   6859   -914    767    508       C  
ATOM    336  O   ASN A  44      43.481  29.837  10.795  1.00 75.72           O  
ANISOU  336  O   ASN A  44    14428   7366   6974   -867    634    525       O  
ATOM    337  CB  ASN A  44      46.421  30.465  12.189  1.00 70.89           C  
ANISOU  337  CB  ASN A  44    13420   7006   6508  -1222   1082    483       C  
ATOM    338  CG  ASN A  44      47.022  31.464  13.167  1.00 70.61           C  
ANISOU  338  CG  ASN A  44    13304   7019   6507  -1323   1131    497       C  
ATOM    339  OD1 ASN A  44      46.345  31.960  14.064  1.00 69.48           O  
ANISOU  339  OD1 ASN A  44    13110   6873   6415  -1234    970    544       O  
ATOM    340  ND2 ASN A  44      48.302  31.775  12.990  1.00 71.08           N  
ANISOU  340  ND2 ASN A  44    13347   7123   6539  -1515   1358    443       N  
ATOM    341  N   GLU A  45      44.643  27.981  11.298  1.00 73.64           N  
ANISOU  341  N   GLU A  45    13664   7345   6971   -878    840    471       N  
ATOM    342  CA  GLU A  45      43.998  27.184  10.273  1.00 74.61           C  
ANISOU  342  CA  GLU A  45    13911   7398   7039   -787    779    452       C  
ATOM    343  C   GLU A  45      42.497  27.143  10.464  1.00 68.94           C  
ANISOU  343  C   GLU A  45    13237   6616   6341   -605    522    479       C  
ATOM    344  O   GLU A  45      41.715  27.451   9.562  1.00 67.50           O  
ANISOU  344  O   GLU A  45    13340   6290   6015   -552    407    476       O  
ATOM    345  CB  GLU A  45      44.552  25.761  10.299  1.00 79.11           C  
ANISOU  345  CB  GLU A  45    14206   8092   7762   -759    877    406       C  
ATOM    346  CG  GLU A  45      45.564  25.491   9.187  1.00 85.51           C  
ANISOU  346  CG  GLU A  45    15120   8894   8476   -893   1093    339       C  
ATOM    347  CD  GLU A  45      46.322  24.184   9.395  1.00 91.47           C  
ANISOU  347  CD  GLU A  45    15559   9786   9410   -872   1197    274       C  
ATOM    348  OE1 GLU A  45      47.243  24.167  10.244  1.00 93.32           O  
ANISOU  348  OE1 GLU A  45    15547  10138   9774   -931   1293    246       O  
ATOM    349  OE2 GLU A  45      45.995  23.167   8.722  1.00 97.52           O  
ANISOU  349  OE2 GLU A  45    16324  10538  10191   -788   1171    246       O  
ATOM    350  N   LEU A  46      42.090  26.779  11.661  1.00 65.35           N  
ANISOU  350  N   LEU A  46    12502   6265   6064   -514    429    495       N  
ATOM    351  CA  LEU A  46      40.671  26.682  11.955  1.00 63.34           C  
ANISOU  351  CA  LEU A  46    12239   5975   5854   -353    202    496       C  
ATOM    352  C   LEU A  46      40.023  28.045  11.842  1.00 63.56           C  
ANISOU  352  C   LEU A  46    12525   5874   5749   -340     67    504       C  
ATOM    353  O   LEU A  46      38.904  28.177  11.347  1.00 64.12           O  
ANISOU  353  O   LEU A  46    12758   5841   5765   -221   -116    477       O  
ATOM    354  CB  LEU A  46      40.469  26.114  13.349  1.00 60.91           C  
ANISOU  354  CB  LEU A  46    11589   5808   5747   -295    157    508       C  
ATOM    355  CG  LEU A  46      39.088  25.531  13.602  1.00 61.12           C  
ANISOU  355  CG  LEU A  46    11535   5833   5854   -142    -32    483       C  
ATOM    356  CD1 LEU A  46      38.716  24.552  12.498  1.00 59.41           C  
ANISOU  356  CD1 LEU A  46    11400   5563   5611    -74    -53    450       C  
ATOM    357  CD2 LEU A  46      39.056  24.867  14.982  1.00 56.67           C  
ANISOU  357  CD2 LEU A  46    10646   5412   5474   -123    -38    498       C  
ATOM    358  N   THR A  47      40.744  29.075  12.267  1.00 63.72           N  
ANISOU  358  N   THR A  47    12595   5895   5719   -459    150    532       N  
ATOM    359  CA  THR A  47      40.225  30.418  12.153  1.00 65.87           C  
ANISOU  359  CA  THR A  47    13135   6034   5858   -454     22    540       C  
ATOM    360  C   THR A  47      40.044  30.855  10.702  1.00 67.54           C  
ANISOU  360  C   THR A  47    13758   6056   5847   -475    -11    532       C  
ATOM    361  O   THR A  47      39.051  31.508  10.381  1.00 67.10           O  
ANISOU  361  O   THR A  47    13929   5863   5704   -374   -220    515       O  
ATOM    362  CB  THR A  47      41.075  31.438  12.925  1.00 65.86           C  
ANISOU  362  CB  THR A  47    13107   6069   5848   -589    123    573       C  
ATOM    363  OG1 THR A  47      41.194  31.007  14.284  1.00 62.03           O  
ANISOU  363  OG1 THR A  47    12254   5752   5562   -560    136    580       O  
ATOM    364  CG2 THR A  47      40.417  32.817  12.878  1.00 64.94           C  
ANISOU  364  CG2 THR A  47    13266   5804   5604   -563    -43    577       C  
ATOM    365  N   GLU A  48      40.970  30.500   9.823  1.00 68.75           N  
ANISOU  365  N   GLU A  48    14018   6199   5907   -603    183    532       N  
ATOM    366  CA  GLU A  48      40.754  30.811   8.410  1.00 73.45           C  
ANISOU  366  CA  GLU A  48    15022   6609   6276   -626    151    524       C  
ATOM    367  C   GLU A  48      39.518  30.105   7.885  1.00 69.50           C  
ANISOU  367  C   GLU A  48    14562   6048   5796   -431    -56    489       C  
ATOM    368  O   GLU A  48      38.725  30.674   7.139  1.00 69.85           O  
ANISOU  368  O   GLU A  48    14933   5916   5691   -358   -236    476       O  
ATOM    369  CB  GLU A  48      41.977  30.487   7.543  1.00 79.74           C  
ANISOU  369  CB  GLU A  48    15913   7417   6967   -812    419    514       C  
ATOM    370  CG  GLU A  48      43.030  31.597   7.539  1.00 86.24           C  
ANISOU  370  CG  GLU A  48    16905   8204   7657  -1034    596    533       C  
ATOM    371  CD  GLU A  48      42.542  32.931   6.963  1.00 93.57           C  
ANISOU  371  CD  GLU A  48    18295   8910   8349  -1065    460    564       C  
ATOM    372  OE1 GLU A  48      41.776  32.941   5.955  1.00101.19           O  
ANISOU  372  OE1 GLU A  48    19577   9710   9161   -985    314    559       O  
ATOM    373  OE2 GLU A  48      42.952  33.982   7.512  1.00 95.29           O  
ANISOU  373  OE2 GLU A  48    18572   9107   8527  -1170    494    591       O  
ATOM    374  N   PHE A  49      39.341  28.857   8.268  1.00 67.28           N  
ANISOU  374  N   PHE A  49    13958   5905   5700   -344    -42    467       N  
ATOM    375  CA  PHE A  49      38.185  28.142   7.781  1.00 64.67           C  
ANISOU  375  CA  PHE A  49    13647   5525   5400   -170   -228    423       C  
ATOM    376  C   PHE A  49      36.932  28.845   8.282  1.00 62.65           C  
ANISOU  376  C   PHE A  49    13427   5204   5174    -22   -493    394       C  
ATOM    377  O   PHE A  49      36.002  29.086   7.524  1.00 64.25           O  
ANISOU  377  O   PHE A  49    13871   5260   5280     92   -689    351       O  
ATOM    378  CB  PHE A  49      38.199  26.708   8.230  1.00 61.35           C  
ANISOU  378  CB  PHE A  49    12868   5263   5180   -112   -170    406       C  
ATOM    379  CG  PHE A  49      36.979  25.966   7.816  1.00 60.92           C  
ANISOU  379  CG  PHE A  49    12809   5166   5171     60   -358    354       C  
ATOM    380  CD1 PHE A  49      36.010  25.645   8.726  1.00 60.87           C  
ANISOU  380  CD1 PHE A  49    12561   5233   5332    185   -508    321       C  
ATOM    381  CD2 PHE A  49      36.779  25.639   6.505  1.00 61.86           C  
ANISOU  381  CD2 PHE A  49    13178   5170   5158     88   -385    327       C  
ATOM    382  CE1 PHE A  49      34.868  24.976   8.341  1.00 61.15           C  
ANISOU  382  CE1 PHE A  49    12583   5233   5417    334   -676    254       C  
ATOM    383  CE2 PHE A  49      35.642  24.975   6.110  1.00 61.49           C  
ANISOU  383  CE2 PHE A  49    13125   5081   5157    249   -566    268       C  
ATOM    384  CZ  PHE A  49      34.686  24.634   7.028  1.00 60.71           C  
ANISOU  384  CZ  PHE A  49    12766   5062   5239    372   -711    228       C  
ATOM    385  N   ALA A  50      36.930  29.205   9.553  1.00 59.67           N  
ANISOU  385  N   ALA A  50    12811   4932   4928    -24   -502    406       N  
ATOM    386  CA  ALA A  50      35.797  29.938  10.114  1.00 59.36           C  
ANISOU  386  CA  ALA A  50    12781   4846   4928    106   -740    359       C  
ATOM    387  C   ALA A  50      35.423  31.190   9.284  1.00 60.56           C  
ANISOU  387  C   ALA A  50    13364   4777   4869    128   -898    346       C  
ATOM    388  O   ALA A  50      34.239  31.457   9.057  1.00 60.69           O  
ANISOU  388  O   ALA A  50    13485   4694   4879    290  -1149    271       O  
ATOM    389  CB  ALA A  50      36.086  30.316  11.551  1.00 55.71           C  
ANISOU  389  CB  ALA A  50    12048   4520   4600     60   -690    382       C  
ATOM    390  N   LYS A  51      36.419  31.922   8.798  1.00 61.28           N  
ANISOU  390  N   LYS A  51    13712   4786   4786    -36   -757    409       N  
ATOM    391  CA  LYS A  51      36.149  33.126   8.006  1.00 65.35           C  
ANISOU  391  CA  LYS A  51    14681   5073   5078    -37   -901    408       C  
ATOM    392  C   LYS A  51      35.474  32.790   6.675  1.00 66.53           C  
ANISOU  392  C   LYS A  51    15128   5059   5091     62  -1045    367       C  
ATOM    393  O   LYS A  51      34.491  33.419   6.291  1.00 68.14           O  
ANISOU  393  O   LYS A  51    15576   5097   5217    202  -1314    313       O  
ATOM    394  CB  LYS A  51      37.427  33.932   7.765  1.00 66.88           C  
ANISOU  394  CB  LYS A  51    15095   5215   5103   -268   -688    483       C  
ATOM    395  CG  LYS A  51      37.809  34.826   8.931  1.00 67.94           C  
ANISOU  395  CG  LYS A  51    15093   5415   5305   -336   -655    511       C  
ATOM    396  CD  LYS A  51      38.957  35.778   8.574  1.00 72.39           C  
ANISOU  396  CD  LYS A  51    15937   5892   5676   -567   -472    571       C  
ATOM    397  CE  LYS A  51      39.948  36.000   9.722  1.00 74.28           C  
ANISOU  397  CE  LYS A  51    15882   6303   6040   -705   -273    603       C  
ATOM    398  NZ  LYS A  51      41.262  35.317   9.475  1.00 75.84           N  
ANISOU  398  NZ  LYS A  51    15952   6620   6245   -892     42    619       N  
ATOM    399  N   THR A  52      36.001  31.794   5.987  1.00 66.83           N  
ANISOU  399  N   THR A  52    15141   5143   5107     -2   -875    383       N  
ATOM    400  CA  THR A  52      35.368  31.292   4.797  1.00 68.97           C  
ANISOU  400  CA  THR A  52    15641   5287   5275     97   -999    341       C  
ATOM    401  C   THR A  52      33.872  31.083   5.011  1.00 69.47           C  
ANISOU  401  C   THR A  52    15603   5327   5465    344  -1305    245       C  
ATOM    402  O   THR A  52      33.061  31.507   4.196  1.00 71.09           O  
ANISOU  402  O   THR A  52    16127   5343   5543    463  -1541    193       O  
ATOM    403  CB  THR A  52      36.010  29.967   4.362  1.00 68.04           C  
ANISOU  403  CB  THR A  52    15356   5289   5207     30   -780    351       C  
ATOM    404  OG1 THR A  52      37.388  30.193   4.040  1.00 67.57           O  
ANISOU  404  OG1 THR A  52    15409   5244   5021   -202   -497    409       O  
ATOM    405  CG2 THR A  52      35.297  29.397   3.151  1.00 69.51           C  
ANISOU  405  CG2 THR A  52    15766   5349   5296    143   -917    302       C  
ATOM    406  N   CYS A  53      33.510  30.425   6.101  1.00 68.91           N  
ANISOU  406  N   CYS A  53    15095   5446   5643    417  -1302    211       N  
ATOM    407  CA  CYS A  53      32.112  30.050   6.340  1.00 69.70           C  
ANISOU  407  CA  CYS A  53    15039   5556   5888    631  -1554     98       C  
ATOM    408  C   CYS A  53      31.223  31.261   6.645  1.00 71.17           C  
ANISOU  408  C   CYS A  53    15365   5624   6053    752  -1824     25       C  
ATOM    409  O   CYS A  53      30.021  31.279   6.307  1.00 69.67           O  
ANISOU  409  O   CYS A  53    15237   5345   5891    941  -2092    -94       O  
ATOM    410  CB  CYS A  53      32.027  29.058   7.498  1.00 69.37           C  
ANISOU  410  CB  CYS A  53    14505   5749   6103    641  -1454     83       C  
ATOM    411  SG  CYS A  53      32.815  27.466   7.184  1.00 73.21           S  
ANISOU  411  SG  CYS A  53    14793   6368   6656    555  -1205    135       S  
ATOM    412  N   VAL A  54      31.819  32.268   7.287  1.00 70.44           N  
ANISOU  412  N   VAL A  54    15314   5531   5919    648  -1759     83       N  
ATOM    413  CA  VAL A  54      31.127  33.516   7.557  1.00 71.23           C  
ANISOU  413  CA  VAL A  54    15577   5506   5981    747  -2004     21       C  
ATOM    414  C   VAL A  54      30.803  34.254   6.248  1.00 74.17           C  
ANISOU  414  C   VAL A  54    16474   5599   6109    807  -2207      3       C  
ATOM    415  O   VAL A  54      29.664  34.712   6.027  1.00 76.46           O  
ANISOU  415  O   VAL A  54    16892   5759   6401   1002  -2522   -117       O  
ATOM    416  CB  VAL A  54      31.974  34.427   8.482  1.00 70.61           C  
ANISOU  416  CB  VAL A  54    15451   5483   5896    601  -1866    100       C  
ATOM    417  CG1 VAL A  54      31.357  35.824   8.561  1.00 70.48           C  
ANISOU  417  CG1 VAL A  54    15689   5292   5796    694  -2126     43       C  
ATOM    418  CG2 VAL A  54      32.084  33.804   9.862  1.00 66.58           C  
ANISOU  418  CG2 VAL A  54    14442   5227   5629    577  -1730     98       C  
ATOM    419  N   ALA A  55      31.818  34.388   5.402  1.00 74.82           N  
ANISOU  419  N   ALA A  55    16864   5588   5977    634  -2029    111       N  
ATOM    420  CA  ALA A  55      31.628  34.884   4.053  1.00 78.63           C  
ANISOU  420  CA  ALA A  55    17870   5805   6200    658  -2182    111       C  
ATOM    421  C   ALA A  55      30.605  34.026   3.285  1.00 80.41           C  
ANISOU  421  C   ALA A  55    18109   5982   6463    851  -2378      9       C  
ATOM    422  O   ALA A  55      29.774  34.572   2.567  1.00 84.93           O  
ANISOU  422  O   ALA A  55    19015   6339   6918   1001  -2676    -66       O  
ATOM    423  CB  ALA A  55      32.967  34.912   3.313  1.00 78.52           C  
ANISOU  423  CB  ALA A  55    18118   5746   5969    405  -1891    235       C  
ATOM    424  N   ASP A  56      30.670  32.697   3.439  1.00 77.77           N  
ANISOU  424  N   ASP A  56    17420   5837   6292    851  -2223      1       N  
ATOM    425  CA  ASP A  56      29.865  31.767   2.632  1.00 77.67           C  
ANISOU  425  CA  ASP A  56    17419   5786   6304   1001  -2361    -84       C  
ATOM    426  C   ASP A  56      29.344  30.535   3.408  1.00 75.43           C  
ANISOU  426  C   ASP A  56    16614   5734   6310   1087  -2320   -154       C  
ATOM    427  O   ASP A  56      29.925  29.444   3.341  1.00 69.69           O  
ANISOU  427  O   ASP A  56    15694   5142   5643    998  -2094   -103       O  
ATOM    428  CB  ASP A  56      30.686  31.305   1.416  1.00 79.14           C  
ANISOU  428  CB  ASP A  56    17895   5892   6282    864  -2182     -1       C  
ATOM    429  CG  ASP A  56      29.886  30.410   0.472  1.00 81.90           C  
ANISOU  429  CG  ASP A  56    18310   6178   6629   1016  -2334    -85       C  
ATOM    430  OD1 ASP A  56      30.509  29.570  -0.253  1.00 81.70           O  
ANISOU  430  OD1 ASP A  56    18330   6180   6530    916  -2140    -35       O  
ATOM    431  OD2 ASP A  56      28.628  30.528   0.492  1.00 82.99           O  
ANISOU  431  OD2 ASP A  56    18431   6249   6854   1237  -2647   -214       O  
ATOM    432  N   GLU A  57      28.227  30.708   4.115  1.00 76.72           N  
ANISOU  432  N   GLU A  57    16566   5937   6648   1258  -2544   -284       N  
ATOM    433  CA  GLU A  57      27.692  29.651   4.992  1.00 75.66           C  
ANISOU  433  CA  GLU A  57    15941   6023   6784   1317  -2501   -358       C  
ATOM    434  C   GLU A  57      27.461  28.315   4.291  1.00 72.87           C  
ANISOU  434  C   GLU A  57    15507   5706   6474   1358  -2463   -386       C  
ATOM    435  O   GLU A  57      27.341  27.290   4.960  1.00 70.49           O  
ANISOU  435  O   GLU A  57    14823   5591   6368   1347  -2351   -405       O  
ATOM    436  CB  GLU A  57      26.421  30.116   5.727  1.00 78.47           C  
ANISOU  436  CB  GLU A  57    16118   6396   7302   1495  -2765   -527       C  
ATOM    437  CG  GLU A  57      26.707  31.169   6.808  1.00 83.26           C  
ANISOU  437  CG  GLU A  57    16647   7049   7940   1435  -2741   -500       C  
ATOM    438  CD  GLU A  57      25.531  31.461   7.770  1.00 86.95           C  
ANISOU  438  CD  GLU A  57    16832   7594   8609   1584  -2942   -679       C  
ATOM    439  OE1 GLU A  57      25.819  31.853   8.922  1.00 86.14           O  
ANISOU  439  OE1 GLU A  57    16512   7619   8599   1507  -2840   -652       O  
ATOM    440  OE2 GLU A  57      24.330  31.324   7.398  1.00 92.91           O  
ANISOU  440  OE2 GLU A  57    17578   8288   9435   1775  -3200   -858       O  
ATOM    441  N   SER A  58      27.414  28.325   2.964  1.00 72.89           N  
ANISOU  441  N   SER A  58    15881   5525   6288   1398  -2557   -385       N  
ATOM    442  CA  SER A  58      27.204  27.106   2.178  1.00 72.89           C  
ANISOU  442  CA  SER A  58    15848   5539   6308   1441  -2533   -414       C  
ATOM    443  C   SER A  58      28.454  26.326   1.819  1.00 70.01           C  
ANISOU  443  C   SER A  58    15478   5250   5874   1257  -2215   -279       C  
ATOM    444  O   SER A  58      28.356  25.245   1.266  1.00 67.89           O  
ANISOU  444  O   SER A  58    15144   5012   5639   1283  -2172   -299       O  
ATOM    445  CB  SER A  58      26.508  27.432   0.862  1.00 77.28           C  
ANISOU  445  CB  SER A  58    16819   5855   6689   1584  -2803   -493       C  
ATOM    446  OG  SER A  58      25.124  27.476   1.070  1.00 84.00           O  
ANISOU  446  OG  SER A  58    17543   6685   7688   1800  -3103   -675       O  
ATOM    447  N   HIS A  59      29.626  26.864   2.119  1.00 69.37           N  
ANISOU  447  N   HIS A  59    15459   5198   5702   1073  -1994   -155       N  
ATOM    448  CA  HIS A  59      30.852  26.197   1.737  1.00 68.55           C  
ANISOU  448  CA  HIS A  59    15353   5162   5531    898  -1695    -52       C  
ATOM    449  C   HIS A  59      30.974  24.784   2.377  1.00 65.17           C  
ANISOU  449  C   HIS A  59    14476   4950   5336    891  -1542    -57       C  
ATOM    450  O   HIS A  59      30.432  24.510   3.450  1.00 60.79           O  
ANISOU  450  O   HIS A  59    13582   4527   4990    953  -1590    -99       O  
ATOM    451  CB  HIS A  59      32.035  27.106   2.051  1.00 70.17           C  
ANISOU  451  CB  HIS A  59    15673   5368   5619    703  -1497     55       C  
ATOM    452  CG  HIS A  59      33.315  26.658   1.432  1.00 72.70           C  
ANISOU  452  CG  HIS A  59    16080   5718   5824    515  -1206    134       C  
ATOM    453  ND1 HIS A  59      34.054  25.588   1.916  1.00 71.47           N  
ANISOU  453  ND1 HIS A  59    15572   5760   5825    435   -970    161       N  
ATOM    454  CD2 HIS A  59      33.990  27.140   0.359  1.00 73.76           C  
ANISOU  454  CD2 HIS A  59    16620   5707   5698    387  -1114    176       C  
ATOM    455  CE1 HIS A  59      35.126  25.427   1.153  1.00 72.95           C  
ANISOU  455  CE1 HIS A  59    15921   5930   5867    275   -746    203       C  
ATOM    456  NE2 HIS A  59      35.105  26.351   0.201  1.00 75.93           N  
ANISOU  456  NE2 HIS A  59    16757   6105   5987    233   -816    214       N  
ATOM    457  N   ALA A  60      31.597  23.870   1.635  1.00 65.61           N  
ANISOU  457  N   ALA A  60    14561   5025   5343    824  -1379    -25       N  
ATOM    458  CA  ALA A  60      31.875  22.492   2.084  1.00 63.11           C  
ANISOU  458  CA  ALA A  60    13875   4888   5216    805  -1225    -21       C  
ATOM    459  C   ALA A  60      32.417  22.472   3.521  1.00 62.24           C  
ANISOU  459  C   ALA A  60    13412   4958   5277    721  -1082     30       C  
ATOM    460  O   ALA A  60      33.430  23.096   3.807  1.00 62.73           O  
ANISOU  460  O   ALA A  60    13517   5045   5273    580   -919    104       O  
ATOM    461  CB  ALA A  60      32.897  21.853   1.151  1.00 60.98           C  
ANISOU  461  CB  ALA A  60    13726   4611   4832    691  -1012     23       C  
ATOM    462  N   GLY A  61      31.733  21.774   4.418  1.00 61.49           N  
ANISOU  462  N   GLY A  61    12983   4983   5395    800  -1145    -15       N  
ATOM    463  CA  GLY A  61      32.217  21.595   5.778  1.00 60.19           C  
ANISOU  463  CA  GLY A  61    12490   4989   5393    722  -1015     33       C  
ATOM    464  C   GLY A  61      31.604  22.527   6.788  1.00 60.96           C  
ANISOU  464  C   GLY A  61    12502   5108   5553    758  -1138      7       C  
ATOM    465  O   GLY A  61      31.590  22.220   7.983  1.00 60.33           O  
ANISOU  465  O   GLY A  61    12120   5169   5634    732  -1088     16       O  
ATOM    466  N   CYS A  62      31.086  23.662   6.328  1.00 62.07           N  
ANISOU  466  N   CYS A  62    12914   5105   5565    820  -1307    -32       N  
ATOM    467  CA  CYS A  62      30.625  24.706   7.248  1.00 63.13           C  
ANISOU  467  CA  CYS A  62    12995   5249   5743    848  -1419    -61       C  
ATOM    468  C   CYS A  62      29.417  24.309   8.107  1.00 61.95           C  
ANISOU  468  C   CYS A  62    12554   5194   5792    962  -1563   -174       C  
ATOM    469  O   CYS A  62      29.074  25.013   9.055  1.00 62.67           O  
ANISOU  469  O   CYS A  62    12528   5332   5951    972  -1625   -207       O  
ATOM    470  CB  CYS A  62      30.283  25.983   6.469  1.00 66.89           C  
ANISOU  470  CB  CYS A  62    13860   5525   6031    907  -1600    -91       C  
ATOM    471  SG  CYS A  62      31.687  26.764   5.649  1.00 67.50           S  
ANISOU  471  SG  CYS A  62    14309   5486   5852    732  -1421     36       S  
ATOM    472  N   GLU A  63      28.767  23.211   7.747  1.00 62.43           N  
ANISOU  472  N   GLU A  63    12506   5277   5938   1039  -1613   -243       N  
ATOM    473  CA  GLU A  63      27.547  22.737   8.404  1.00 64.88           C  
ANISOU  473  CA  GLU A  63    12554   5669   6428   1135  -1744   -374       C  
ATOM    474  C   GLU A  63      27.885  21.807   9.547  1.00 66.96           C  
ANISOU  474  C   GLU A  63    12472   6118   6853   1035  -1568   -326       C  
ATOM    475  O   GLU A  63      27.026  21.487  10.371  1.00 72.17           O  
ANISOU  475  O   GLU A  63    12888   6871   7661   1065  -1627   -420       O  
ATOM    476  CB  GLU A  63      26.662  21.961   7.423  1.00 66.59           C  
ANISOU  476  CB  GLU A  63    12830   5814   6658   1260  -1884   -482       C  
ATOM    477  CG  GLU A  63      27.149  20.545   7.059  1.00 68.44           C  
ANISOU  477  CG  GLU A  63    12968   6105   6929   1205  -1728   -423       C  
ATOM    478  CD  GLU A  63      28.375  20.515   6.145  1.00 69.20           C  
ANISOU  478  CD  GLU A  63    13305   6130   6858   1122  -1577   -297       C  
ATOM    479  OE1 GLU A  63      28.577  19.530   5.409  1.00 74.20           O  
ANISOU  479  OE1 GLU A  63    13962   6752   7480   1124  -1517   -287       O  
ATOM    480  OE2 GLU A  63      29.148  21.480   6.148  1.00 70.57           O  
ANISOU  480  OE2 GLU A  63    13644   6260   6910   1045  -1510   -218       O  
ATOM    481  N   LYS A  64      29.129  21.346   9.571  1.00 64.38           N  
ANISOU  481  N   LYS A  64    12130   5838   6493    913  -1356   -191       N  
ATOM    482  CA  LYS A  64      29.562  20.393  10.558  1.00 62.29           C  
ANISOU  482  CA  LYS A  64    11577   5725   6364    823  -1202   -136       C  
ATOM    483  C   LYS A  64      29.654  21.030  11.942  1.00 58.92           C  
ANISOU  483  C   LYS A  64    10978   5400   6009    758  -1168   -115       C  
ATOM    484  O   LYS A  64      29.949  22.194  12.086  1.00 63.11           O  
ANISOU  484  O   LYS A  64    11626   5892   6461    739  -1185    -91       O  
ATOM    485  CB  LYS A  64      30.917  19.794  10.130  1.00 64.03           C  
ANISOU  485  CB  LYS A  64    11842   5956   6529    728  -1006    -18       C  
ATOM    486  CG  LYS A  64      30.836  18.948   8.862  1.00 65.10           C  
ANISOU  486  CG  LYS A  64    12106   6014   6614    783  -1019    -43       C  
ATOM    487  CD  LYS A  64      32.202  18.606   8.296  1.00 66.25           C  
ANISOU  487  CD  LYS A  64    12335   6156   6681    690   -830     48       C  
ATOM    488  CE  LYS A  64      32.096  17.496   7.270  1.00 68.48           C  
ANISOU  488  CE  LYS A  64    12669   6395   6953    740   -828     17       C  
ATOM    489  NZ  LYS A  64      33.295  17.382   6.388  1.00 71.62           N  
ANISOU  489  NZ  LYS A  64    13221   6757   7234    664   -667     70       N  
ATOM    490  N   SER A  65      29.396  20.255  12.965  1.00 56.71           N  
ANISOU  490  N   SER A  65    10432   5245   5871    717  -1120   -126       N  
ATOM    491  CA  SER A  65      29.535  20.728  14.320  1.00 56.80           C  
ANISOU  491  CA  SER A  65    10274   5359   5946    642  -1072   -102       C  
ATOM    492  C   SER A  65      30.980  21.072  14.612  1.00 56.96           C  
ANISOU  492  C   SER A  65    10328   5404   5909    535   -912     38       C  
ATOM    493  O   SER A  65      31.899  20.575  13.955  1.00 59.33           O  
ANISOU  493  O   SER A  65    10705   5678   6160    500   -805    111       O  
ATOM    494  CB  SER A  65      29.080  19.639  15.299  1.00 56.72           C  
ANISOU  494  CB  SER A  65    10001   5470   6081    595  -1031   -127       C  
ATOM    495  OG  SER A  65      29.999  18.551  15.348  1.00 57.65           O  
ANISOU  495  OG  SER A  65    10058   5623   6222    524   -891    -22       O  
ATOM    496  N   LEU A  66      31.190  21.883  15.634  1.00 56.94           N  
ANISOU  496  N   LEU A  66    10250   5462   5924    480   -890     61       N  
ATOM    497  CA  LEU A  66      32.550  22.200  16.051  1.00 59.31           C  
ANISOU  497  CA  LEU A  66    10548   5799   6189    373   -739    179       C  
ATOM    498  C   LEU A  66      33.311  20.957  16.468  1.00 58.20           C  
ANISOU  498  C   LEU A  66    10244   5740   6128    306   -608    250       C  
ATOM    499  O   LEU A  66      34.510  20.834  16.219  1.00 57.29           O  
ANISOU  499  O   LEU A  66    10163   5626   5979    246   -485    325       O  
ATOM    500  CB  LEU A  66      32.524  23.184  17.212  1.00 59.21           C  
ANISOU  500  CB  LEU A  66    10451   5846   6198    330   -751    182       C  
ATOM    501  CG  LEU A  66      32.131  24.537  16.678  1.00 62.41           C  
ANISOU  501  CG  LEU A  66    11065   6146   6501    388   -868    132       C  
ATOM    502  CD1 LEU A  66      31.369  25.349  17.742  1.00 65.47           C  
ANISOU  502  CD1 LEU A  66    11343   6588   6946    405   -962     60       C  
ATOM    503  CD2 LEU A  66      33.425  25.183  16.187  1.00 63.74           C  
ANISOU  503  CD2 LEU A  66    11409   6258   6550    309   -753    230       C  
ATOM    504  N   HIS A  67      32.624  20.065  17.167  1.00 56.74           N  
ANISOU  504  N   HIS A  67     9880   5625   6052    309   -637    216       N  
ATOM    505  CA  HIS A  67      33.254  18.828  17.559  1.00 57.44           C  
ANISOU  505  CA  HIS A  67     9839   5771   6213    256   -542    278       C  
ATOM    506  C   HIS A  67      33.765  18.100  16.342  1.00 56.78           C  
ANISOU  506  C   HIS A  67     9858   5622   6093    290   -500    294       C  
ATOM    507  O   HIS A  67      34.885  17.614  16.365  1.00 58.20           O  
ANISOU  507  O   HIS A  67    10003   5823   6285    243   -392    360       O  
ATOM    508  CB  HIS A  67      32.302  17.932  18.328  1.00 58.34           C  
ANISOU  508  CB  HIS A  67     9792   5946   6429    248   -588    231       C  
ATOM    509  CG  HIS A  67      32.072  18.391  19.719  1.00 57.92           C  
ANISOU  509  CG  HIS A  67     9609   5979   6418    179   -585    231       C  
ATOM    510  ND1 HIS A  67      33.105  18.577  20.613  1.00 59.00           N  
ANISOU  510  ND1 HIS A  67     9685   6171   6561     99   -499    324       N  
ATOM    511  CD2 HIS A  67      30.935  18.746  20.363  1.00 60.09           C  
ANISOU  511  CD2 HIS A  67     9803   6298   6730    178   -658    136       C  
ATOM    512  CE1 HIS A  67      32.606  19.013  21.760  1.00 60.31           C  
ANISOU  512  CE1 HIS A  67     9750   6407   6757     49   -519    299       C  
ATOM    513  NE2 HIS A  67      31.293  19.122  21.635  1.00 61.37           N  
ANISOU  513  NE2 HIS A  67     9867   6540   6911     91   -607    182       N  
ATOM    514  N   THR A  68      32.971  18.031  15.272  1.00 54.94           N  
ANISOU  514  N   THR A  68     9750   5308   5817    375   -588    223       N  
ATOM    515  CA  THR A  68      33.444  17.313  14.114  1.00 53.65           C  
ANISOU  515  CA  THR A  68     9689   5084   5613    404   -544    233       C  
ATOM    516  C   THR A  68      34.666  18.006  13.563  1.00 53.59           C  
ANISOU  516  C   THR A  68     9818   5042   5501    353   -435    289       C  
ATOM    517  O   THR A  68      35.653  17.332  13.195  1.00 51.69           O  
ANISOU  517  O   THR A  68     9562   4812   5266    319   -322    324       O  
ATOM    518  CB  THR A  68      32.370  17.142  13.029  1.00 54.39           C  
ANISOU  518  CB  THR A  68     9909   5089   5669    507   -668    143       C  
ATOM    519  OG1 THR A  68      31.460  16.138  13.468  1.00 54.49           O  
ANISOU  519  OG1 THR A  68     9764   5144   5794    531   -727     89       O  
ATOM    520  CG2 THR A  68      33.004  16.684  11.710  1.00 51.50           C  
ANISOU  520  CG2 THR A  68     9700   4646   5221    528   -611    158       C  
ATOM    521  N   LEU A  69      34.599  19.338  13.495  1.00 51.37           N  
ANISOU  521  N   LEU A  69     9671   4719   5128    345   -468    285       N  
ATOM    522  CA  LEU A  69      35.641  20.084  12.810  1.00 53.41           C  
ANISOU  522  CA  LEU A  69    10106   4925   5263    284   -366    324       C  
ATOM    523  C   LEU A  69      36.916  20.056  13.621  1.00 54.97           C  
ANISOU  523  C   LEU A  69    10157   5215   5512    180   -215    389       C  
ATOM    524  O   LEU A  69      37.960  19.678  13.121  1.00 58.75           O  
ANISOU  524  O   LEU A  69    10650   5700   5971    128    -86    405       O  
ATOM    525  CB  LEU A  69      35.223  21.522  12.538  1.00 53.77           C  
ANISOU  525  CB  LEU A  69    10358   4885   5189    298   -453    305       C  
ATOM    526  CG  LEU A  69      34.171  21.735  11.436  1.00 54.01           C  
ANISOU  526  CG  LEU A  69    10607   4785   5128    407   -611    232       C  
ATOM    527  CD1 LEU A  69      33.553  23.124  11.463  1.00 52.46           C  
ANISOU  527  CD1 LEU A  69    10578   4506   4847    446   -749    198       C  
ATOM    528  CD2 LEU A  69      34.799  21.466  10.088  1.00 53.66           C  
ANISOU  528  CD2 LEU A  69    10774   4655   4959    385   -531    245       C  
ATOM    529  N   PHE A  70      36.819  20.471  14.869  1.00 55.15           N  
ANISOU  529  N   PHE A  70    10038   5312   5604    151   -236    412       N  
ATOM    530  CA  PHE A  70      37.942  20.472  15.788  1.00 54.97           C  
ANISOU  530  CA  PHE A  70     9865   5379   5643     63   -122    466       C  
ATOM    531  C   PHE A  70      38.536  19.072  15.879  1.00 54.77           C  
ANISOU  531  C   PHE A  70     9689   5404   5716     63    -58    477       C  
ATOM    532  O   PHE A  70      39.737  18.894  15.732  1.00 57.26           O  
ANISOU  532  O   PHE A  70     9970   5746   6041      9     62    489       O  
ATOM    533  CB  PHE A  70      37.447  20.943  17.163  1.00 55.27           C  
ANISOU  533  CB  PHE A  70     9769   5486   5746     50   -187    479       C  
ATOM    534  CG  PHE A  70      38.497  20.944  18.234  1.00 54.87           C  
ANISOU  534  CG  PHE A  70     9561   5525   5762    -30    -97    532       C  
ATOM    535  CD1 PHE A  70      39.438  21.961  18.299  1.00 54.68           C  
ANISOU  535  CD1 PHE A  70     9589   5504   5682   -105    -12    555       C  
ATOM    536  CD2 PHE A  70      38.515  19.945  19.199  1.00 54.75           C  
ANISOU  536  CD2 PHE A  70     9358   5583   5861    -33   -107    554       C  
ATOM    537  CE1 PHE A  70      40.397  21.984  19.299  1.00 55.73           C  
ANISOU  537  CE1 PHE A  70     9570   5720   5885   -171     59    590       C  
ATOM    538  CE2 PHE A  70      39.473  19.942  20.207  1.00 56.04           C  
ANISOU  538  CE2 PHE A  70     9390   5819   6085    -96    -48    598       C  
ATOM    539  CZ  PHE A  70      40.417  20.970  20.260  1.00 57.56           C  
ANISOU  539  CZ  PHE A  70     9615   6021   6232   -159     32    611       C  
ATOM    540  N   GLY A  71      37.683  18.085  16.121  1.00 53.55           N  
ANISOU  540  N   GLY A  71     9446   5261   5639    122   -142    461       N  
ATOM    541  CA  GLY A  71      38.080  16.692  16.093  1.00 53.82           C  
ANISOU  541  CA  GLY A  71     9372   5317   5759    137   -111    466       C  
ATOM    542  C   GLY A  71      38.769  16.197  14.832  1.00 55.37           C  
ANISOU  542  C   GLY A  71     9658   5467   5915    152    -32    440       C  
ATOM    543  O   GLY A  71      39.732  15.438  14.899  1.00 57.70           O  
ANISOU  543  O   GLY A  71     9854   5794   6273    136     41    443       O  
ATOM    544  N   ASP A  72      38.298  16.614  13.666  1.00 57.43           N  
ANISOU  544  N   ASP A  72    10110   5645   6065    185    -53    404       N  
ATOM    545  CA  ASP A  72      38.982  16.247  12.430  1.00 56.67           C  
ANISOU  545  CA  ASP A  72    10120   5503   5907    183     38    374       C  
ATOM    546  C   ASP A  72      40.385  16.866  12.428  1.00 57.85           C  
ANISOU  546  C   ASP A  72    10269   5689   6022     83    194    381       C  
ATOM    547  O   ASP A  72      41.296  16.371  11.772  1.00 59.17           O  
ANISOU  547  O   ASP A  72    10434   5863   6187     55    307    345       O  
ATOM    548  CB  ASP A  72      38.207  16.737  11.223  1.00 56.90           C  
ANISOU  548  CB  ASP A  72    10392   5427   5801    228    -22    337       C  
ATOM    549  CG  ASP A  72      36.942  15.949  10.964  1.00 57.22           C  
ANISOU  549  CG  ASP A  72    10429   5430   5884    331   -162    301       C  
ATOM    550  OD1 ASP A  72      36.731  14.841  11.556  1.00 53.67           O  
ANISOU  550  OD1 ASP A  72     9801   5031   5562    357   -190    303       O  
ATOM    551  OD2 ASP A  72      36.155  16.459  10.117  1.00 57.18           O  
ANISOU  551  OD2 ASP A  72    10618   5334   5776    384   -251    263       O  
ATOM    552  N   GLU A  73      40.574  17.937  13.181  1.00 57.05           N  
ANISOU  552  N   GLU A  73    10159   5617   5901     24    205    414       N  
ATOM    553  CA  GLU A  73      41.866  18.579  13.213  1.00 60.03           C  
ANISOU  553  CA  GLU A  73    10530   6030   6249    -81    354    411       C  
ATOM    554  C   GLU A  73      42.824  17.788  14.067  1.00 61.70           C  
ANISOU  554  C   GLU A  73    10496   6339   6610    -97    409    407       C  
ATOM    555  O   GLU A  73      43.945  17.521  13.634  1.00 62.66           O  
ANISOU  555  O   GLU A  73    10575   6488   6746   -145    538    356       O  
ATOM    556  CB  GLU A  73      41.749  20.010  13.699  1.00 61.32           C  
ANISOU  556  CB  GLU A  73    10778   6183   6339   -139    340    444       C  
ATOM    557  CG  GLU A  73      42.491  20.990  12.821  1.00 67.17           C  
ANISOU  557  CG  GLU A  73    11718   6871   6932   -243    468    424       C  
ATOM    558  CD  GLU A  73      42.031  20.975  11.364  1.00 70.17           C  
ANISOU  558  CD  GLU A  73    12357   7136   7166   -220    459    395       C  
ATOM    559  OE1 GLU A  73      40.807  21.017  11.106  1.00 74.20           O  
ANISOU  559  OE1 GLU A  73    12981   7575   7639   -124    303    400       O  
ATOM    560  OE2 GLU A  73      42.905  20.921  10.477  1.00 71.96           O  
ANISOU  560  OE2 GLU A  73    12675   7348   7318   -302    609    354       O  
ATOM    561  N   LEU A  74      42.396  17.387  15.268  1.00 61.56           N  
ANISOU  561  N   LEU A  74    10321   6368   6699    -57    309    448       N  
ATOM    562  CA  LEU A  74      43.268  16.592  16.137  1.00 61.27           C  
ANISOU  562  CA  LEU A  74    10073   6406   6800    -60    328    447       C  
ATOM    563  C   LEU A  74      43.783  15.396  15.378  1.00 62.53           C  
ANISOU  563  C   LEU A  74    10192   6555   7012    -17    368    390       C  
ATOM    564  O   LEU A  74      44.979  15.130  15.359  1.00 66.02           O  
ANISOU  564  O   LEU A  74    10530   7041   7515    -44    458    337       O  
ATOM    565  CB  LEU A  74      42.549  16.100  17.383  1.00 62.08           C  
ANISOU  565  CB  LEU A  74    10061   6537   6990    -21    200    501       C  
ATOM    566  CG  LEU A  74      42.004  17.134  18.373  1.00 62.59           C  
ANISOU  566  CG  LEU A  74    10125   6628   7029    -58    149    549       C  
ATOM    567  CD1 LEU A  74      41.672  16.418  19.671  1.00 62.14           C  
ANISOU  567  CD1 LEU A  74     9930   6613   7069    -45     58    590       C  
ATOM    568  CD2 LEU A  74      42.961  18.285  18.631  1.00 62.16           C  
ANISOU  568  CD2 LEU A  74    10067   6609   6941   -139    241    549       C  
ATOM    569  N   CYS A  75      42.884  14.682  14.726  1.00 62.67           N  
ANISOU  569  N   CYS A  75    10285   6515   7010     53    299    386       N  
ATOM    570  CA  CYS A  75      43.274  13.493  13.970  1.00 65.82           C  
ANISOU  570  CA  CYS A  75    10653   6897   7458    103    325    329       C  
ATOM    571  C   CYS A  75      44.279  13.738  12.841  1.00 64.81           C  
ANISOU  571  C   CYS A  75    10591   6768   7267     52    483    249       C  
ATOM    572  O   CYS A  75      45.026  12.839  12.470  1.00 63.18           O  
ANISOU  572  O   CYS A  75    10295   6578   7132     77    532    179       O  
ATOM    573  CB  CYS A  75      42.032  12.769  13.454  1.00 67.99           C  
ANISOU  573  CB  CYS A  75    11012   7107   7716    182    219    338       C  
ATOM    574  SG  CYS A  75      41.105  12.082  14.855  1.00 72.85           S  
ANISOU  574  SG  CYS A  75    11503   7740   8438    219     66    403       S  
ATOM    575  N   LYS A  76      44.335  14.961  12.324  1.00 66.47           N  
ANISOU  575  N   LYS A  76    10958   6956   7342    -26    564    249       N  
ATOM    576  CA  LYS A  76      45.301  15.285  11.280  1.00 65.22           C  
ANISOU  576  CA  LYS A  76    10883   6796   7102   -109    736    169       C  
ATOM    577  C   LYS A  76      46.683  15.596  11.857  1.00 65.55           C  
ANISOU  577  C   LYS A  76    10758   6927   7220   -193    859    116       C  
ATOM    578  O   LYS A  76      47.589  15.877  11.089  1.00 72.54           O  
ANISOU  578  O   LYS A  76    11682   7828   8050   -283   1024     29       O  
ATOM    579  CB  LYS A  76      44.781  16.422  10.370  1.00 63.92           C  
ANISOU  579  CB  LYS A  76    11001   6548   6739   -168    768    188       C  
ATOM    580  CG  LYS A  76      43.684  15.989   9.392  1.00 63.67           C  
ANISOU  580  CG  LYS A  76    11149   6420   6623    -85    675    192       C  
ATOM    581  CD  LYS A  76      43.000  17.156   8.665  1.00 61.32           C  
ANISOU  581  CD  LYS A  76    11148   6020   6131   -119    648    219       C  
ATOM    582  N   VAL A  77      46.856  15.530  13.179  1.00 64.32           N  
ANISOU  582  N   VAL A  77    10421   6830   7187   -171    784    155       N  
ATOM    583  CA  VAL A  77      48.155  15.820  13.817  1.00 66.67           C  
ANISOU  583  CA  VAL A  77    10546   7214   7573   -238    877     95       C  
ATOM    584  C   VAL A  77      49.117  14.648  13.626  1.00 71.10           C  
ANISOU  584  C   VAL A  77    10927   7819   8269   -191    915    -20       C  
ATOM    585  O   VAL A  77      48.859  13.523  14.087  1.00 70.86           O  
ANISOU  585  O   VAL A  77    10790   7781   8352    -80    785     -5       O  
ATOM    586  CB  VAL A  77      48.018  16.144  15.337  1.00 65.72           C  
ANISOU  586  CB  VAL A  77    10303   7135   7534   -223    767    173       C  
ATOM    587  CG1 VAL A  77      49.377  16.256  16.023  1.00 63.71           C  
ANISOU  587  CG1 VAL A  77     9848   6966   7393   -269    836     97       C  
ATOM    588  CG2 VAL A  77      47.247  17.438  15.538  1.00 61.80           C  
ANISOU  588  CG2 VAL A  77     9964   6605   6911   -279    747    259       C  
ATOM    589  N   ALA A  78      50.247  14.929  12.975  1.00 77.40           N  
ANISOU  589  N   ALA A  78    11689   8662   9056   -282   1095   -146       N  
ATOM    590  CA  ALA A  78      51.174  13.879  12.543  1.00 80.31           C  
ANISOU  590  CA  ALA A  78    11899   9072   9543   -242   1152   -292       C  
ATOM    591  C   ALA A  78      51.748  13.088  13.732  1.00 82.02           C  
ANISOU  591  C   ALA A  78    11861   9340   9963   -146   1027   -321       C  
ATOM    592  O   ALA A  78      51.845  11.859  13.664  1.00 85.42           O  
ANISOU  592  O   ALA A  78    12196   9757  10501    -35    942   -372       O  
ATOM    593  CB  ALA A  78      52.290  14.465  11.675  1.00 78.86           C  
ANISOU  593  CB  ALA A  78    11718   8940   9305   -384   1389   -441       C  
ATOM    594  N   SER A  79      52.080  13.784  14.823  1.00 81.83           N  
ANISOU  594  N   SER A  79    11748   9361   9983   -183    998   -286       N  
ATOM    595  CA  SER A  79      52.728  13.158  15.998  1.00 83.44           C  
ANISOU  595  CA  SER A  79    11728   9606  10369   -100    873   -320       C  
ATOM    596  C   SER A  79      51.768  12.462  16.982  1.00 80.40           C  
ANISOU  596  C   SER A  79    11359   9165  10025     11    649   -178       C  
ATOM    597  O   SER A  79      52.188  11.975  18.031  1.00 82.13           O  
ANISOU  597  O   SER A  79    11437   9398  10369     77    523   -184       O  
ATOM    598  CB  SER A  79      53.542  14.218  16.760  1.00 87.38           C  
ANISOU  598  CB  SER A  79    12126  10178  10895   -193    939   -352       C  
ATOM    599  OG  SER A  79      52.728  15.309  17.183  1.00 89.79           O  
ANISOU  599  OG  SER A  79    12581  10460  11076   -260    926   -206       O  
ATOM    600  N   LEU A  80      50.489  12.400  16.634  1.00 76.76           N  
ANISOU  600  N   LEU A  80    11074   8636   9455     27    599    -62       N  
ATOM    601  CA  LEU A  80      49.445  12.036  17.591  1.00 74.55           C  
ANISOU  601  CA  LEU A  80    10832   8311   9181     86    421     75       C  
ATOM    602  C   LEU A  80      49.725  10.770  18.383  1.00 72.46           C  
ANISOU  602  C   LEU A  80    10445   8027   9060    191    264     65       C  
ATOM    603  O   LEU A  80      49.714  10.796  19.607  1.00 72.76           O  
ANISOU  603  O   LEU A  80    10432   8071   9144    200    154    128       O  
ATOM    604  CB  LEU A  80      48.092  11.927  16.872  1.00 75.13           C  
ANISOU  604  CB  LEU A  80    11090   8316   9140    100    396    153       C  
ATOM    605  CG  LEU A  80      46.858  11.682  17.735  1.00 74.34           C  
ANISOU  605  CG  LEU A  80    11043   8177   9028    132    244    278       C  
ATOM    606  CD1 LEU A  80      46.693  12.768  18.794  1.00 73.62           C  
ANISOU  606  CD1 LEU A  80    10945   8125   8905     67    228    351       C  
ATOM    607  CD2 LEU A  80      45.620  11.555  16.860  1.00 72.76           C  
ANISOU  607  CD2 LEU A  80    11001   7914   8730    152    229    313       C  
ATOM    608  N   ARG A  81      49.978   9.659  17.698  1.00 74.37           N  
ANISOU  608  N   ARG A  81    10654   8237   9366    269    245    -16       N  
ATOM    609  CA  ARG A  81      50.210   8.387  18.388  1.00 72.24           C  
ANISOU  609  CA  ARG A  81    10297   7924   9225    378     74    -28       C  
ATOM    610  C   ARG A  81      51.567   8.355  19.089  1.00 71.65           C  
ANISOU  610  C   ARG A  81    10037   7900   9287    407     44   -135       C  
ATOM    611  O   ARG A  81      51.656   7.901  20.228  1.00 69.41           O  
ANISOU  611  O   ARG A  81     9712   7586   9074    460   -121    -89       O  
ATOM    612  CB  ARG A  81      50.058   7.192  17.449  1.00 74.52           C  
ANISOU  612  CB  ARG A  81    10610   8156   9546    462     48    -88       C  
ATOM    613  CG  ARG A  81      50.315   5.867  18.157  1.00 75.86           C  
ANISOU  613  CG  ARG A  81    10714   8264   9846    577   -145   -101       C  
ATOM    614  CD  ARG A  81      49.884   4.665  17.347  1.00 76.56           C  
ANISOU  614  CD  ARG A  81    10860   8277   9951    658   -196   -128       C  
ATOM    615  NE  ARG A  81      48.627   4.105  17.837  1.00 75.51           N  
ANISOU  615  NE  ARG A  81    10862   8060   9767    665   -326     18       N  
ATOM    616  CZ  ARG A  81      47.455   4.148  17.199  1.00 77.35           C  
ANISOU  616  CZ  ARG A  81    11229   8264   9896    632   -288     87       C  
ATOM    617  NH1 ARG A  81      46.393   3.603  17.773  1.00 78.13           N  
ANISOU  617  NH1 ARG A  81    11425   8295   9967    628   -407    197       N  
ATOM    618  NH2 ARG A  81      47.319   4.727  16.002  1.00 78.22           N  
ANISOU  618  NH2 ARG A  81    11387   8407   9927    597   -137     39       N  
ATOM    619  N   GLU A  82      52.612   8.848  18.422  1.00 73.33           N  
ANISOU  619  N   GLU A  82    10143   8186   9531    366    200   -286       N  
ATOM    620  CA  GLU A  82      53.951   8.945  19.042  1.00 75.22           C  
ANISOU  620  CA  GLU A  82    10182   8489   9911    386    185   -419       C  
ATOM    621  C   GLU A  82      53.884   9.561  20.438  1.00 74.60           C  
ANISOU  621  C   GLU A  82    10090   8420   9834    361     85   -315       C  
ATOM    622  O   GLU A  82      54.534   9.078  21.361  1.00 73.47           O  
ANISOU  622  O   GLU A  82     9833   8269   9814    440    -63   -359       O  
ATOM    623  CB  GLU A  82      54.925   9.767  18.174  1.00 75.04           C  
ANISOU  623  CB  GLU A  82    10067   8561   9885    288    417   -583       C  
ATOM    624  N   THR A  83      53.087  10.619  20.581  1.00 72.12           N  
ANISOU  624  N   THR A  83     9902   8119   9382    257    156   -184       N  
ATOM    625  CA  THR A  83      53.048  11.394  21.815  1.00 71.28           C  
ANISOU  625  CA  THR A  83     9784   8036   9262    213     96    -97       C  
ATOM    626  C   THR A  83      51.965  10.976  22.832  1.00 71.06           C  
ANISOU  626  C   THR A  83     9867   7939   9192    245    -80     73       C  
ATOM    627  O   THR A  83      52.196  11.068  24.050  1.00 72.08           O  
ANISOU  627  O   THR A  83     9954   8071   9361    254   -195    114       O  
ATOM    628  CB  THR A  83      52.890  12.893  21.496  1.00 70.40           C  
ANISOU  628  CB  THR A  83     9738   7980   9031     76    270    -67       C  
ATOM    629  OG1 THR A  83      54.002  13.329  20.700  1.00 71.49           O  
ANISOU  629  OG1 THR A  83     9773   8186   9205     18    444   -232       O  
ATOM    630  CG2 THR A  83      52.773  13.732  22.798  1.00 67.49           C  
ANISOU  630  CG2 THR A  83     9362   7637   8644     30    205     27       C  
ATOM    631  N   TYR A  84      50.799  10.536  22.345  1.00 68.06           N  
ANISOU  631  N   TYR A  84     9631   7500   8729    252    -97    161       N  
ATOM    632  CA  TYR A  84      49.644  10.293  23.217  1.00 65.06           C  
ANISOU  632  CA  TYR A  84     9364   7067   8288    245   -222    311       C  
ATOM    633  C   TYR A  84      49.073   8.856  23.184  1.00 68.17           C  
ANISOU  633  C   TYR A  84     9822   7368   8710    324   -355    343       C  
ATOM    634  O   TYR A  84      47.999   8.600  23.724  1.00 67.44           O  
ANISOU  634  O   TYR A  84     9838   7231   8555    298   -432    455       O  
ATOM    635  CB  TYR A  84      48.538  11.315  22.906  1.00 62.38           C  
ANISOU  635  CB  TYR A  84     9147   6746   7809    155   -127    396       C  
ATOM    636  CG  TYR A  84      48.956  12.787  22.944  1.00 58.85           C  
ANISOU  636  CG  TYR A  84     8675   6371   7313     68     -3    380       C  
ATOM    637  CD1 TYR A  84      48.912  13.526  24.124  1.00 56.07           C  
ANISOU  637  CD1 TYR A  84     8305   6053   6947     19    -46    444       C  
ATOM    638  CD2 TYR A  84      49.368  13.434  21.785  1.00 59.53           C  
ANISOU  638  CD2 TYR A  84     8774   6487   7358     25    159    301       C  
ATOM    639  CE1 TYR A  84      49.280  14.864  24.151  1.00 56.37           C  
ANISOU  639  CE1 TYR A  84     8327   6150   6940    -62     62    429       C  
ATOM    640  CE2 TYR A  84      49.746  14.769  21.798  1.00 60.36           C  
ANISOU  640  CE2 TYR A  84     8880   6646   7409    -68    272    288       C  
ATOM    641  CZ  TYR A  84      49.698  15.485  22.982  1.00 58.71           C  
ANISOU  641  CZ  TYR A  84     8644   6468   7197   -108    220    353       C  
ATOM    642  OH  TYR A  84      50.055  16.814  22.941  1.00 56.89           O  
ANISOU  642  OH  TYR A  84     8424   6282   6909   -202    333    338       O  
ATOM    643  N   GLY A  85      49.790   7.924  22.558  1.00 72.16           N  
ANISOU  643  N   GLY A  85    10261   7847   9311    413   -380    235       N  
ATOM    644  CA  GLY A  85      49.414   6.515  22.551  1.00 71.24           C  
ANISOU  644  CA  GLY A  85    10201   7632   9234    496   -521    253       C  
ATOM    645  C   GLY A  85      47.997   6.213  22.082  1.00 72.13           C  
ANISOU  645  C   GLY A  85    10464   7696   9247    464   -510    346       C  
ATOM    646  O   GLY A  85      47.605   6.589  20.983  1.00 68.55           O  
ANISOU  646  O   GLY A  85    10046   7266   8734    441   -384    321       O  
ATOM    647  N   ASP A  86      47.225   5.549  22.946  1.00 75.90           N  
ANISOU  647  N   ASP A  86    11035   8102   9702    455   -645    448       N  
ATOM    648  CA  ASP A  86      45.845   5.134  22.656  1.00 77.33           C  
ANISOU  648  CA  ASP A  86    11346   8234   9804    419   -652    524       C  
ATOM    649  C   ASP A  86      44.924   6.291  22.254  1.00 73.57           C  
ANISOU  649  C   ASP A  86    10914   7820   9219    334   -523    561       C  
ATOM    650  O   ASP A  86      43.842   6.055  21.741  1.00 73.33           O  
ANISOU  650  O   ASP A  86    10967   7760   9133    318   -511    586       O  
ATOM    651  CB  ASP A  86      45.216   4.446  23.877  1.00 83.25           C  
ANISOU  651  CB  ASP A  86    12190   8911  10532    382   -797    625       C  
ATOM    652  CG  ASP A  86      45.813   3.088  24.163  1.00 94.50           C  
ANISOU  652  CG  ASP A  86    13633  10232  12042    471   -958    602       C  
ATOM    653  OD1 ASP A  86      46.878   2.762  23.598  1.00105.22           O  
ANISOU  653  OD1 ASP A  86    14893  11589  13498    573   -970    494       O  
ATOM    654  OD2 ASP A  86      45.217   2.341  24.975  1.00103.56           O  
ANISOU  654  OD2 ASP A  86    14898  11294  13156    434  -1077    684       O  
ATOM    655  N   MET A  87      45.305   7.530  22.535  1.00 68.67           N  
ANISOU  655  N   MET A  87    10244   7278   8570    283   -443    560       N  
ATOM    656  CA  MET A  87      44.478   8.651  22.121  1.00 68.90           C  
ANISOU  656  CA  MET A  87    10328   7353   8499    216   -340    586       C  
ATOM    657  C   MET A  87      44.246   8.641  20.602  1.00 67.15           C  
ANISOU  657  C   MET A  87    10154   7117   8241    248   -250    524       C  
ATOM    658  O   MET A  87      43.180   9.016  20.132  1.00 65.10           O  
ANISOU  658  O   MET A  87     9983   6850   7903    223   -225    546       O  
ATOM    659  CB  MET A  87      45.113   9.976  22.546  1.00 69.06           C  
ANISOU  659  CB  MET A  87    10290   7450   8499    162   -265    581       C  
ATOM    660  CG  MET A  87      44.188  11.164  22.362  1.00 67.02           C  
ANISOU  660  CG  MET A  87    10106   7225   8135     95   -195    617       C  
ATOM    661  SD  MET A  87      44.979  12.652  22.947  1.00 66.42           S  
ANISOU  661  SD  MET A  87     9971   7227   8040     28   -120    615       S  
ATOM    662  CE  MET A  87      43.538  13.672  23.234  1.00 66.94           C  
ANISOU  662  CE  MET A  87    10134   7306   7996    -35   -121    677       C  
ATOM    663  N   ALA A  88      45.269   8.228  19.858  1.00 67.74           N  
ANISOU  663  N   ALA A  88    10169   7191   8377    304   -207    434       N  
ATOM    664  CA  ALA A  88      45.186   8.000  18.416  1.00 67.59           C  
ANISOU  664  CA  ALA A  88    10199   7151   8329    338   -127    366       C  
ATOM    665  C   ALA A  88      44.005   7.119  18.034  1.00 64.61           C  
ANISOU  665  C   ALA A  88     9917   6704   7929    372   -201    400       C  
ATOM    666  O   ALA A  88      43.388   7.343  16.995  1.00 64.79           O  
ANISOU  666  O   ALA A  88    10028   6711   7878    373   -145    380       O  
ATOM    667  CB  ALA A  88      46.478   7.357  17.906  1.00 65.97           C  
ANISOU  667  CB  ALA A  88     9891   6953   8221    399    -97    250       C  
ATOM    668  N   ASP A  89      43.705   6.126  18.858  1.00 62.33           N  
ANISOU  668  N   ASP A  89     9621   6367   7695    393   -329    446       N  
ATOM    669  CA  ASP A  89      42.572   5.240  18.600  1.00 62.75           C  
ANISOU  669  CA  ASP A  89     9759   6352   7731    409   -399    474       C  
ATOM    670  C   ASP A  89      41.244   5.977  18.585  1.00 61.60           C  
ANISOU  670  C   ASP A  89     9691   6222   7493    346   -378    518       C  
ATOM    671  O   ASP A  89      40.305   5.539  17.928  1.00 60.19           O  
ANISOU  671  O   ASP A  89     9579   6002   7287    363   -396    505       O  
ATOM    672  CB  ASP A  89      42.494   4.099  19.630  1.00 65.27           C  
ANISOU  672  CB  ASP A  89    10081   6607   8112    417   -539    524       C  
ATOM    673  CG  ASP A  89      43.623   3.078  19.483  1.00 66.39           C  
ANISOU  673  CG  ASP A  89    10166   6703   8358    511   -604    462       C  
ATOM    674  OD1 ASP A  89      43.998   2.428  20.478  1.00 67.14           O  
ANISOU  674  OD1 ASP A  89    10253   6749   8506    524   -725    494       O  
ATOM    675  OD2 ASP A  89      44.116   2.898  18.361  1.00 72.63           O  
ANISOU  675  OD2 ASP A  89    10926   7497   9175    573   -541    372       O  
ATOM    676  N   CYS A  90      41.145   7.111  19.273  1.00 63.02           N  
ANISOU  676  N   CYS A  90     9856   6461   7628    281   -345    556       N  
ATOM    677  CA  CYS A  90      39.899   7.882  19.221  1.00 60.71           C  
ANISOU  677  CA  CYS A  90     9626   6185   7256    234   -334    573       C  
ATOM    678  C   CYS A  90      39.529   8.270  17.809  1.00 59.61           C  
ANISOU  678  C   CYS A  90     9565   6028   7056    274   -277    516       C  
ATOM    679  O   CYS A  90      38.355   8.340  17.491  1.00 60.60           O  
ANISOU  679  O   CYS A  90     9750   6133   7140    275   -310    503       O  
ATOM    680  CB  CYS A  90      39.953   9.110  20.098  1.00 60.78           C  
ANISOU  680  CB  CYS A  90     9606   6259   7227    167   -306    609       C  
ATOM    681  SG  CYS A  90      40.366   8.719  21.815  1.00 65.12           S  
ANISOU  681  SG  CYS A  90    10089   6825   7830    114   -380    679       S  
ATOM    682  N   CYS A  91      40.521   8.472  16.957  1.00 57.68           N  
ANISOU  682  N   CYS A  91     9323   5788   6805    306   -197    470       N  
ATOM    683  CA  CYS A  91      40.267   8.801  15.569  1.00 60.39           C  
ANISOU  683  CA  CYS A  91     9770   6103   7072    336   -140    417       C  
ATOM    684  C   CYS A  91      39.509   7.744  14.756  1.00 61.73           C  
ANISOU  684  C   CYS A  91     9996   6207   7251    397   -196    384       C  
ATOM    685  O   CYS A  91      38.825   8.063  13.778  1.00 61.77           O  
ANISOU  685  O   CYS A  91    10111   6179   7181    421   -190    351       O  
ATOM    686  CB  CYS A  91      41.590   9.104  14.898  1.00 64.31           C  
ANISOU  686  CB  CYS A  91    10252   6621   7561    334    -26    364       C  
ATOM    687  SG  CYS A  91      42.336  10.601  15.591  1.00 69.47           S  
ANISOU  687  SG  CYS A  91    10872   7346   8178    249     56    388       S  
ATOM    688  N   GLU A  92      39.630   6.485  15.149  1.00 62.93           N  
ANISOU  688  N   GLU A  92    10086   6331   7492    426   -260    392       N  
ATOM    689  CA  GLU A  92      38.954   5.409  14.450  1.00 63.25           C  
ANISOU  689  CA  GLU A  92    10174   6307   7550    479   -315    360       C  
ATOM    690  C   GLU A  92      37.466   5.446  14.697  1.00 59.77           C  
ANISOU  690  C   GLU A  92     9777   5851   7082    454   -386    375       C  
ATOM    691  O   GLU A  92      36.733   4.694  14.064  1.00 56.72           O  
ANISOU  691  O   GLU A  92     9436   5413   6703    493   -432    340       O  
ATOM    692  CB  GLU A  92      39.494   4.062  14.908  1.00 70.05           C  
ANISOU  692  CB  GLU A  92    10970   7133   8514    511   -379    366       C  
ATOM    693  CG  GLU A  92      40.941   3.810  14.523  1.00 76.36           C  
ANISOU  693  CG  GLU A  92    11706   7942   9364    558   -325    312       C  
ATOM    694  CD  GLU A  92      41.395   2.425  14.912  1.00 82.94           C  
ANISOU  694  CD  GLU A  92    12489   8722  10303    612   -420    304       C  
ATOM    695  OE1 GLU A  92      42.025   2.300  15.987  1.00 92.17           O  
ANISOU  695  OE1 GLU A  92    13590   9900  11532    600   -472    336       O  
ATOM    696  OE2 GLU A  92      41.109   1.458  14.153  1.00 91.53           O  
ANISOU  696  OE2 GLU A  92    13616   9748  11413    670   -455    263       O  
ATOM    697  N   LYS A  93      37.023   6.306  15.619  1.00 58.14           N  
ANISOU  697  N   LYS A  93     9547   5692   6852    390   -393    413       N  
ATOM    698  CA  LYS A  93      35.619   6.371  16.027  1.00 56.22           C  
ANISOU  698  CA  LYS A  93     9313   5449   6597    353   -454    405       C  
ATOM    699  C   LYS A  93      34.856   7.519  15.375  1.00 54.12           C  
ANISOU  699  C   LYS A  93     9116   5193   6255    372   -451    356       C  
ATOM    700  O   LYS A  93      35.447   8.474  14.891  1.00 52.27           O  
ANISOU  700  O   LYS A  93     8932   4970   5959    387   -395    355       O  
ATOM    701  CB  LYS A  93      35.504   6.555  17.535  1.00 56.97           C  
ANISOU  701  CB  LYS A  93     9338   5591   6715    264   -472    461       C  
ATOM    702  CG  LYS A  93      36.209   5.513  18.360  1.00 58.79           C  
ANISOU  702  CG  LYS A  93     9528   5800   7011    240   -503    516       C  
ATOM    703  CD  LYS A  93      36.079   5.805  19.861  1.00 59.21           C  
ANISOU  703  CD  LYS A  93     9540   5895   7063    141   -520    575       C  
ATOM    704  CE  LYS A  93      36.568   4.639  20.718  1.00 59.63           C  
ANISOU  704  CE  LYS A  93     9593   5898   7165    113   -582    630       C  
ATOM    705  NZ  LYS A  93      35.514   4.218  21.689  1.00 61.89           N  
ANISOU  705  NZ  LYS A  93     9903   6178   7435      1   -618    651       N  
ATOM    706  N   GLN A  94      33.528   7.417  15.446  1.00 52.87           N  
ANISOU  706  N   GLN A  94     8959   5028   6102    364   -516    307       N  
ATOM    707  CA  GLN A  94      32.594   8.450  15.022  1.00 50.32           C  
ANISOU  707  CA  GLN A  94     8687   4708   5722    390   -553    241       C  
ATOM    708  C   GLN A  94      32.197   9.386  16.163  1.00 52.16           C  
ANISOU  708  C   GLN A  94     8855   5009   5953    322   -558    249       C  
ATOM    709  O   GLN A  94      32.341   9.064  17.340  1.00 50.97           O  
ANISOU  709  O   GLN A  94     8618   4902   5845    241   -541    297       O  
ATOM    710  CB  GLN A  94      31.326   7.811  14.519  1.00 48.46           C  
ANISOU  710  CB  GLN A  94     8462   4437   5514    425   -631    153       C  
ATOM    711  CG  GLN A  94      31.524   7.000  13.284  1.00 49.25           C  
ANISOU  711  CG  GLN A  94     8640   4466   5608    502   -640    129       C  
ATOM    712  CD  GLN A  94      30.310   6.166  12.956  1.00 50.95           C  
ANISOU  712  CD  GLN A  94     8842   4649   5869    523   -718     44       C  
ATOM    713  OE1 GLN A  94      29.161   6.581  13.239  1.00 52.10           O  
ANISOU  713  OE1 GLN A  94     8948   4818   6028    510   -776    -36       O  
ATOM    714  NE2 GLN A  94      30.545   4.967  12.365  1.00 48.47           N  
ANISOU  714  NE2 GLN A  94     8548   4280   5587    556   -721     45       N  
ATOM    715  N   GLU A  95      31.691  10.556  15.799  1.00 55.53           N  
ANISOU  715  N   GLU A  95     9338   5437   6322    356   -589    197       N  
ATOM    716  CA  GLU A  95      31.128  11.476  16.788  1.00 59.43           C  
ANISOU  716  CA  GLU A  95     9769   5994   6819    305   -609    175       C  
ATOM    717  C   GLU A  95      29.750  10.932  17.152  1.00 61.76           C  
ANISOU  717  C   GLU A  95     9983   6308   7175    281   -672     79       C  
ATOM    718  O   GLU A  95      29.097  10.294  16.336  1.00 63.03           O  
ANISOU  718  O   GLU A  95    10172   6422   7354    336   -724      9       O  
ATOM    719  CB  GLU A  95      31.075  12.920  16.250  1.00 58.41           C  
ANISOU  719  CB  GLU A  95     9740   5845   6609    358   -637    143       C  
ATOM    720  CG  GLU A  95      32.462  13.561  16.099  1.00 59.22           C  
ANISOU  720  CG  GLU A  95     9909   5942   6648    342   -550    233       C  
ATOM    721  CD  GLU A  95      33.192  13.840  17.443  1.00 61.86           C  
ANISOU  721  CD  GLU A  95    10136   6355   7014    251   -486    311       C  
ATOM    722  OE1 GLU A  95      32.682  13.452  18.531  1.00 62.64           O  
ANISOU  722  OE1 GLU A  95    10120   6508   7173    192   -502    310       O  
ATOM    723  OE2 GLU A  95      34.309  14.443  17.425  1.00 63.15           O  
ANISOU  723  OE2 GLU A  95    10332   6524   7137    229   -414    370       O  
ATOM    724  N   PRO A  96      29.325  11.112  18.390  1.00 60.54           N  
ANISOU  724  N   PRO A  96     9724   6226   7053    188   -660     70       N  
ATOM    725  CA  PRO A  96      29.955  11.745  19.530  1.00 59.64           C  
ANISOU  725  CA  PRO A  96     9561   6174   6925    110   -607    145       C  
ATOM    726  C   PRO A  96      30.981  10.899  20.263  1.00 56.85           C  
ANISOU  726  C   PRO A  96     9182   5826   6591     40   -546    265       C  
ATOM    727  O   PRO A  96      31.646  11.407  21.164  1.00 57.42           O  
ANISOU  727  O   PRO A  96     9224   5943   6651    -15   -507    333       O  
ATOM    728  CB  PRO A  96      28.767  11.995  20.470  1.00 61.94           C  
ANISOU  728  CB  PRO A  96     9749   6534   7250     35   -629     49       C  
ATOM    729  CG  PRO A  96      27.841  10.864  20.184  1.00 63.03           C  
ANISOU  729  CG  PRO A  96     9856   6653   7442     20   -657    -31       C  
ATOM    730  CD  PRO A  96      28.020  10.517  18.729  1.00 61.86           C  
ANISOU  730  CD  PRO A  96     9807   6419   7280    142   -699    -40       C  
ATOM    731  N   GLU A  97      31.092   9.618  19.943  1.00 56.22           N  
ANISOU  731  N   GLU A  97     9117   5698   6546     44   -550    285       N  
ATOM    732  CA  GLU A  97      31.995   8.744  20.713  1.00 57.14           C  
ANISOU  732  CA  GLU A  97     9218   5805   6686    -16   -521    387       C  
ATOM    733  C   GLU A  97      33.449   9.215  20.621  1.00 53.65           C  
ANISOU  733  C   GLU A  97     8795   5363   6227     25   -481    466       C  
ATOM    734  O   GLU A  97      34.210   9.091  21.562  1.00 52.33           O  
ANISOU  734  O   GLU A  97     8596   5215   6071    -27   -467    539       O  
ATOM    735  CB  GLU A  97      31.868   7.274  20.287  1.00 59.88           C  
ANISOU  735  CB  GLU A  97     9594   6085   7075     -5   -548    386       C  
ATOM    736  CG  GLU A  97      30.619   6.563  20.815  1.00 65.18           C  
ANISOU  736  CG  GLU A  97    10234   6760   7770    -99   -570    326       C  
ATOM    737  CD  GLU A  97      29.384   6.595  19.882  1.00 72.05           C  
ANISOU  737  CD  GLU A  97    11097   7623   8656    -50   -606    195       C  
ATOM    738  OE1 GLU A  97      29.482   7.010  18.697  1.00 75.83           O  
ANISOU  738  OE1 GLU A  97    11623   8071   9119     69   -630    158       O  
ATOM    739  OE2 GLU A  97      28.286   6.184  20.342  1.00 74.50           O  
ANISOU  739  OE2 GLU A  97    11360   7955   8993   -139   -612    117       O  
ATOM    740  N   ARG A  98      33.821   9.778  19.482  1.00 53.82           N  
ANISOU  740  N   ARG A  98     8873   5361   6215    111   -464    442       N  
ATOM    741  CA  ARG A  98      35.182  10.268  19.278  1.00 52.79           C  
ANISOU  741  CA  ARG A  98     8756   5235   6066    135   -407    493       C  
ATOM    742  C   ARG A  98      35.558  11.326  20.300  1.00 51.60           C  
ANISOU  742  C   ARG A  98     8561   5149   5896     74   -379    532       C  
ATOM    743  O   ARG A  98      36.619  11.245  20.886  1.00 51.28           O  
ANISOU  743  O   ARG A  98     8478   5127   5879     51   -351    589       O  
ATOM    744  CB  ARG A  98      35.334  10.835  17.872  1.00 51.50           C  
ANISOU  744  CB  ARG A  98     8690   5034   5845    211   -381    448       C  
ATOM    745  CG  ARG A  98      36.752  11.224  17.527  1.00 50.63           C  
ANISOU  745  CG  ARG A  98     8594   4929   5715    218   -299    479       C  
ATOM    746  CD  ARG A  98      36.889  11.570  16.062  1.00 50.75           C  
ANISOU  746  CD  ARG A  98     8731   4893   5658    274   -264    433       C  
ATOM    747  NE  ARG A  98      36.217  12.814  15.761  1.00 50.17           N  
ANISOU  747  NE  ARG A  98     8753   4810   5500    278   -286    406       N  
ATOM    748  CZ  ARG A  98      36.460  13.582  14.709  1.00 50.32           C  
ANISOU  748  CZ  ARG A  98     8913   4783   5422    300   -251    382       C  
ATOM    749  NH1 ARG A  98      35.809  14.748  14.578  1.00 52.14           N  
ANISOU  749  NH1 ARG A  98     9243   4992   5577    307   -299    359       N  
ATOM    750  NH2 ARG A  98      37.372  13.237  13.825  1.00 50.08           N  
ANISOU  750  NH2 ARG A  98     8936   4726   5365    307   -169    374       N  
ATOM    751  N   ASN A  99      34.688  12.310  20.525  1.00 52.96           N  
ANISOU  751  N   ASN A  99     8738   5353   6031     56   -398    492       N  
ATOM    752  CA  ASN A  99      34.939  13.306  21.583  1.00 53.45           C  
ANISOU  752  CA  ASN A  99     8753   5478   6077     -6   -379    524       C  
ATOM    753  C   ASN A  99      34.908  12.705  22.975  1.00 52.60           C  
ANISOU  753  C   ASN A  99     8568   5409   6007    -95   -389    570       C  
ATOM    754  O   ASN A  99      35.774  13.021  23.785  1.00 52.82           O  
ANISOU  754  O   ASN A  99     8563   5470   6038   -134   -365    631       O  
ATOM    755  CB  ASN A  99      33.957  14.479  21.519  1.00 55.46           C  
ANISOU  755  CB  ASN A  99     9029   5753   6289      2   -411    454       C  
ATOM    756  CG  ASN A  99      34.392  15.662  22.386  1.00 54.75           C  
ANISOU  756  CG  ASN A  99     8910   5718   6172    -46   -385    486       C  
ATOM    757  OD1 ASN A  99      35.517  16.153  22.274  1.00 56.38           O  
ANISOU  757  OD1 ASN A  99     9141   5924   6358    -46   -333    539       O  
ATOM    758  ND2 ASN A  99      33.492  16.132  23.245  1.00 53.45           N  
ANISOU  758  ND2 ASN A  99     8690   5607   6014    -93   -417    441       N  
ATOM    759  N   GLU A 100      33.947  11.834  23.261  1.00 52.55           N  
ANISOU  759  N   GLU A 100     8546   5396   6026   -134   -423    540       N  
ATOM    760  CA  GLU A 100      33.944  11.154  24.560  1.00 56.14           C  
ANISOU  760  CA  GLU A 100     8965   5869   6496   -236   -430    590       C  
ATOM    761  C   GLU A 100      35.283  10.496  24.833  1.00 54.48           C  
ANISOU  761  C   GLU A 100     8765   5623   6310   -223   -434    679       C  
ATOM    762  O   GLU A 100      35.786  10.529  25.952  1.00 55.87           O  
ANISOU  762  O   GLU A 100     8925   5822   6483   -285   -440    738       O  
ATOM    763  CB  GLU A 100      32.838  10.123  24.678  1.00 60.66           C  
ANISOU  763  CB  GLU A 100     9540   6421   7087   -292   -454    543       C  
ATOM    764  CG  GLU A 100      31.416  10.679  24.608  1.00 66.68           C  
ANISOU  764  CG  GLU A 100    10262   7230   7844   -319   -458    425       C  
ATOM    765  CD  GLU A 100      30.355   9.590  24.369  1.00 77.15           C  
ANISOU  765  CD  GLU A 100    11587   8528   9200   -359   -476    353       C  
ATOM    766  OE1 GLU A 100      30.670   8.354  24.501  1.00 83.35           O  
ANISOU  766  OE1 GLU A 100    12416   9255  10000   -394   -484    413       O  
ATOM    767  OE2 GLU A 100      29.190   9.970  24.070  1.00 80.56           O  
ANISOU  767  OE2 GLU A 100    11973   8992   9645   -355   -490    226       O  
ATOM    768  N   CYS A 101      35.879   9.965  23.779  1.00 56.28           N  
ANISOU  768  N   CYS A 101     9022   5798   6565   -133   -435    676       N  
ATOM    769  CA  CYS A 101      37.152   9.273  23.846  1.00 57.22           C  
ANISOU  769  CA  CYS A 101     9136   5879   6725    -97   -448    727       C  
ATOM    770  C   CYS A 101      38.306  10.231  24.119  1.00 57.14           C  
ANISOU  770  C   CYS A 101     9083   5913   6714    -85   -409    751       C  
ATOM    771  O   CYS A 101      39.109   9.977  25.043  1.00 56.09           O  
ANISOU  771  O   CYS A 101     8921   5782   6608   -108   -441    800       O  
ATOM    772  CB  CYS A 101      37.396   8.578  22.517  1.00 60.51           C  
ANISOU  772  CB  CYS A 101     9584   6238   7170     -3   -446    689       C  
ATOM    773  SG  CYS A 101      38.855   7.518  22.493  1.00 67.37           S  
ANISOU  773  SG  CYS A 101    10432   7054   8111     59   -480    714       S  
ATOM    774  N   PHE A 102      38.373  11.317  23.323  1.00 51.74           N  
ANISOU  774  N   PHE A 102     8407   5257   5994    -53   -349    714       N  
ATOM    775  CA  PHE A 102      39.355  12.373  23.522  1.00 51.66           C  
ANISOU  775  CA  PHE A 102     8364   5292   5973    -61   -296    726       C  
ATOM    776  C   PHE A 102      39.304  13.003  24.919  1.00 51.22           C  
ANISOU  776  C   PHE A 102     8266   5291   5905   -138   -313    769       C  
ATOM    777  O   PHE A 102      40.312  13.149  25.600  1.00 50.28           O  
ANISOU  777  O   PHE A 102     8097   5194   5813   -152   -313    800       O  
ATOM    778  CB  PHE A 102      39.166  13.505  22.523  1.00 52.02           C  
ANISOU  778  CB  PHE A 102     8465   5343   5956    -38   -237    682       C  
ATOM    779  CG  PHE A 102      39.712  13.227  21.162  1.00 52.28           C  
ANISOU  779  CG  PHE A 102     8546   5334   5984     24   -189    642       C  
ATOM    780  CD1 PHE A 102      40.973  12.706  20.986  1.00 53.02           C  
ANISOU  780  CD1 PHE A 102     8588   5425   6132     46   -152    636       C  
ATOM    781  CD2 PHE A 102      38.966  13.530  20.047  1.00 53.42           C  
ANISOU  781  CD2 PHE A 102     8789   5440   6068     61   -183    598       C  
ATOM    782  CE1 PHE A 102      41.469  12.446  19.724  1.00 52.96           C  
ANISOU  782  CE1 PHE A 102     8620   5386   6116     92    -92    583       C  
ATOM    783  CE2 PHE A 102      39.460  13.296  18.774  1.00 54.42           C  
ANISOU  783  CE2 PHE A 102     8979   5524   6173    107   -131    560       C  
ATOM    784  CZ  PHE A 102      40.716  12.739  18.620  1.00 54.30           C  
ANISOU  784  CZ  PHE A 102     8904   5516   6211    116    -76    551       C  
ATOM    785  N   LEU A 103      38.127  13.403  25.332  1.00 49.79           N  
ANISOU  785  N   LEU A 103     8099   5136   5685   -186   -329    755       N  
ATOM    786  CA  LEU A 103      37.958  13.867  26.690  1.00 50.30           C  
ANISOU  786  CA  LEU A 103     8127   5253   5733   -269   -343    788       C  
ATOM    787  C   LEU A 103      38.549  12.868  27.693  1.00 50.44           C  
ANISOU  787  C   LEU A 103     8134   5249   5782   -306   -393    850       C  
ATOM    788  O   LEU A 103      39.195  13.254  28.659  1.00 51.16           O  
ANISOU  788  O   LEU A 103     8196   5371   5872   -343   -404    891       O  
ATOM    789  CB  LEU A 103      36.453  14.091  26.977  1.00 50.87           C  
ANISOU  789  CB  LEU A 103     8203   5352   5772   -322   -356    738       C  
ATOM    790  CG  LEU A 103      35.855  15.338  26.324  1.00 48.84           C  
ANISOU  790  CG  LEU A 103     7960   5119   5480   -286   -339    670       C  
ATOM    791  CD1 LEU A 103      34.353  15.400  26.542  1.00 49.57           C  
ANISOU  791  CD1 LEU A 103     8035   5238   5564   -323   -366    588       C  
ATOM    792  CD2 LEU A 103      36.553  16.508  26.945  1.00 47.96           C  
ANISOU  792  CD2 LEU A 103     7824   5054   5346   -312   -312    700       C  
ATOM    793  N   SER A 104      38.353  11.577  27.470  1.00 50.76           N  
ANISOU  793  N   SER A 104     8211   5228   5849   -292   -436    857       N  
ATOM    794  CA  SER A 104      38.790  10.607  28.475  1.00 50.63           C  
ANISOU  794  CA  SER A 104     8220   5170   5848   -331   -507    918       C  
ATOM    795  C   SER A 104      40.307  10.499  28.579  1.00 51.24           C  
ANISOU  795  C   SER A 104     8262   5229   5980   -264   -540    940       C  
ATOM    796  O   SER A 104      40.764   9.914  29.524  1.00 52.41           O  
ANISOU  796  O   SER A 104     8436   5342   6136   -288   -617    987       O  
ATOM    797  CB  SER A 104      38.202   9.229  28.229  1.00 49.33           C  
ANISOU  797  CB  SER A 104     8121   4929   5694   -338   -554    919       C  
ATOM    798  OG  SER A 104      39.068   8.473  27.400  1.00 53.20           O  
ANISOU  798  OG  SER A 104     8611   5357   6245   -233   -586    911       O  
ATOM    799  N   HIS A 105      41.079  11.044  27.634  1.00 52.12           N  
ANISOU  799  N   HIS A 105     8319   5360   6125   -187   -484    897       N  
ATOM    800  CA  HIS A 105      42.559  11.074  27.751  1.00 54.80           C  
ANISOU  800  CA  HIS A 105     8592   5701   6527   -132   -500    888       C  
ATOM    801  C   HIS A 105      43.156  12.391  28.277  1.00 54.37           C  
ANISOU  801  C   HIS A 105     8476   5722   6460   -166   -452    888       C  
ATOM    802  O   HIS A 105      44.378  12.519  28.328  1.00 54.71           O  
ANISOU  802  O   HIS A 105     8447   5777   6562   -126   -454    860       O  
ATOM    803  CB  HIS A 105      43.237  10.774  26.400  1.00 57.37           C  
ANISOU  803  CB  HIS A 105     8885   6006   6906    -41   -454    819       C  
ATOM    804  CG  HIS A 105      43.095   9.352  25.942  1.00 58.56           C  
ANISOU  804  CG  HIS A 105     9077   6077   7098     15   -521    810       C  
ATOM    805  ND1 HIS A 105      41.960   8.884  25.315  1.00 59.52           N  
ANISOU  805  ND1 HIS A 105     9268   6163   7182      8   -513    809       N  
ATOM    806  CD2 HIS A 105      43.949   8.303  26.005  1.00 59.74           C  
ANISOU  806  CD2 HIS A 105     9206   6168   7326     86   -605    790       C  
ATOM    807  CE1 HIS A 105      42.121   7.609  25.010  1.00 61.50           C  
ANISOU  807  CE1 HIS A 105     9545   6339   7483     64   -581    799       C  
ATOM    808  NE2 HIS A 105      43.318   7.230  25.424  1.00 60.68           N  
ANISOU  808  NE2 HIS A 105     9391   6216   7449    115   -643    788       N  
ATOM    809  N   LYS A 106      42.314  13.362  28.638  1.00 53.15           N  
ANISOU  809  N   LYS A 106     8341   5618   6237   -235   -411    905       N  
ATOM    810  CA  LYS A 106      42.761  14.582  29.328  1.00 51.78           C  
ANISOU  810  CA  LYS A 106     8120   5508   6044   -278   -380    913       C  
ATOM    811  C   LYS A 106      43.432  14.223  30.648  1.00 52.03           C  
ANISOU  811  C   LYS A 106     8131   5537   6101   -301   -467    957       C  
ATOM    812  O   LYS A 106      42.868  13.521  31.475  1.00 52.21           O  
ANISOU  812  O   LYS A 106     8214   5528   6095   -346   -539   1004       O  
ATOM    813  CB  LYS A 106      41.588  15.523  29.596  1.00 51.76           C  
ANISOU  813  CB  LYS A 106     8149   5551   5966   -345   -346    916       C  
ATOM    814  CG  LYS A 106      41.240  16.426  28.413  1.00 52.75           C  
ANISOU  814  CG  LYS A 106     8297   5686   6059   -316   -269    866       C  
ATOM    815  CD  LYS A 106      40.023  17.289  28.711  1.00 53.97           C  
ANISOU  815  CD  LYS A 106     8478   5876   6152   -363   -265    849       C  
ATOM    816  CE  LYS A 106      39.937  18.480  27.773  1.00 54.68           C  
ANISOU  816  CE  LYS A 106     8607   5968   6202   -336   -212    806       C  
ATOM    817  NZ  LYS A 106      38.657  19.258  27.857  1.00 55.82           N  
ANISOU  817  NZ  LYS A 106     8782   6131   6297   -352   -232    763       N  
ATOM    818  N   ASP A 107      44.644  14.707  30.836  1.00 52.12           N  
ANISOU  818  N   ASP A 107     8066   5576   6162   -274   -462    935       N  
ATOM    819  CA  ASP A 107      45.417  14.383  32.003  1.00 53.49           C  
ANISOU  819  CA  ASP A 107     8218   5737   6368   -275   -563    962       C  
ATOM    820  C   ASP A 107      45.208  15.432  33.117  1.00 55.34           C  
ANISOU  820  C   ASP A 107     8450   6031   6545   -357   -557    999       C  
ATOM    821  O   ASP A 107      45.598  16.620  32.975  1.00 52.40           O  
ANISOU  821  O   ASP A 107     8016   5721   6173   -372   -481    969       O  
ATOM    822  CB  ASP A 107      46.871  14.319  31.589  1.00 55.51           C  
ANISOU  822  CB  ASP A 107     8369   5995   6726   -195   -566    890       C  
ATOM    823  CG  ASP A 107      47.712  13.567  32.571  1.00 59.70           C  
ANISOU  823  CG  ASP A 107     8885   6481   7316   -152   -715    896       C  
ATOM    824  OD1 ASP A 107      47.344  13.490  33.759  1.00 58.95           O  
ANISOU  824  OD1 ASP A 107     8863   6370   7166   -206   -799    966       O  
ATOM    825  OD2 ASP A 107      48.764  13.051  32.141  1.00 66.12           O  
ANISOU  825  OD2 ASP A 107     9618   7273   8231    -63   -751    818       O  
ATOM    826  N   ASP A 108      44.580  15.008  34.219  1.00 55.31           N  
ANISOU  826  N   ASP A 108     8525   6006   6483   -422   -632   1060       N  
ATOM    827  CA  ASP A 108      44.377  15.899  35.348  1.00 55.51           C  
ANISOU  827  CA  ASP A 108     8555   6087   6450   -504   -631   1091       C  
ATOM    828  C   ASP A 108      45.667  16.109  36.156  1.00 60.10           C  
ANISOU  828  C   ASP A 108     9084   6672   7078   -475   -707   1091       C  
ATOM    829  O   ASP A 108      45.689  16.915  37.087  1.00 61.17           O  
ANISOU  829  O   ASP A 108     9213   6855   7173   -534   -710   1111       O  
ATOM    830  CB  ASP A 108      43.226  15.428  36.228  1.00 54.52           C  
ANISOU  830  CB  ASP A 108     8536   5945   6233   -604   -663   1143       C  
ATOM    831  CG  ASP A 108      41.858  15.763  35.637  1.00 55.98           C  
ANISOU  831  CG  ASP A 108     8733   6167   6371   -652   -569   1113       C  
ATOM    832  OD1 ASP A 108      41.492  16.964  35.551  1.00 55.16           O  
ANISOU  832  OD1 ASP A 108     8580   6133   6244   -676   -497   1080       O  
ATOM    833  OD2 ASP A 108      41.122  14.819  35.266  1.00 59.91           O  
ANISOU  833  OD2 ASP A 108     9291   6617   6857   -664   -577   1114       O  
ATOM    834  N   SER A 109      46.743  15.410  35.799  1.00 62.13           N  
ANISOU  834  N   SER A 109     9295   6882   7429   -380   -773   1054       N  
ATOM    835  CA  SER A 109      48.033  15.612  36.460  1.00 66.53           C  
ANISOU  835  CA  SER A 109     9778   7446   8054   -335   -854   1024       C  
ATOM    836  C   SER A 109      49.178  15.385  35.477  1.00 66.42           C  
ANISOU  836  C   SER A 109     9642   7429   8165   -231   -838    924       C  
ATOM    837  O   SER A 109      49.824  14.346  35.500  1.00 74.37           O  
ANISOU  837  O   SER A 109    10644   8368   9245   -146   -956    893       O  
ATOM    838  CB  SER A 109      48.171  14.675  37.652  1.00 68.67           C  
ANISOU  838  CB  SER A 109    10154   7636   8301   -334  -1030   1079       C  
ATOM    839  OG  SER A 109      48.275  13.348  37.198  1.00 77.51           O  
ANISOU  839  OG  SER A 109    11325   8661   9463   -261  -1116   1072       O  
ATOM    840  N   PRO A 110      49.423  16.367  34.601  1.00 64.42           N  
ANISOU  840  N   PRO A 110     9297   7246   7932   -243   -691    864       N  
ATOM    841  CA  PRO A 110      50.365  16.251  33.491  1.00 63.89           C  
ANISOU  841  CA  PRO A 110     9120   7191   7965   -176   -627    756       C  
ATOM    842  C   PRO A 110      51.843  16.155  33.859  1.00 69.05           C  
ANISOU  842  C   PRO A 110     9637   7855   8742   -110   -700    657       C  
ATOM    843  O   PRO A 110      52.642  15.726  33.035  1.00 66.45           O  
ANISOU  843  O   PRO A 110     9212   7525   8511    -43   -675    549       O  
ATOM    844  CB  PRO A 110      50.145  17.529  32.731  1.00 62.99           C  
ANISOU  844  CB  PRO A 110     8985   7145   7804   -243   -452    735       C  
ATOM    845  CG  PRO A 110      48.774  17.956  33.102  1.00 61.94           C  
ANISOU  845  CG  PRO A 110     8968   7014   7551   -315   -438    831       C  
ATOM    846  CD  PRO A 110      48.679  17.628  34.540  1.00 60.90           C  
ANISOU  846  CD  PRO A 110     8872   6866   7401   -332   -571    894       C  
ATOM    847  N   ASP A 111      52.217  16.540  35.075  1.00 76.80           N  
ANISOU  847  N   ASP A 111    10605   8850   9725   -127   -792    678       N  
ATOM    848  CA  ASP A 111      53.627  16.465  35.477  1.00 83.26           C  
ANISOU  848  CA  ASP A 111    11284   9679  10671    -55   -882    567       C  
ATOM    849  C   ASP A 111      54.451  17.314  34.485  1.00 83.38           C  
ANISOU  849  C   ASP A 111    11141   9779  10759    -75   -707    437       C  
ATOM    850  O   ASP A 111      55.455  16.871  33.896  1.00 82.75           O  
ANISOU  850  O   ASP A 111    10930   9707  10806     -4   -706    297       O  
ATOM    851  CB  ASP A 111      54.105  14.996  35.552  1.00 90.43           C  
ANISOU  851  CB  ASP A 111    12198  10493  11666     70  -1061    524       C  
ATOM    852  CG  ASP A 111      53.097  14.072  36.292  1.00 97.58           C  
ANISOU  852  CG  ASP A 111    13307  11298  12470     62  -1201    664       C  
ATOM    853  OD1 ASP A 111      52.724  14.394  37.450  1.00103.17           O  
ANISOU  853  OD1 ASP A 111    14109  11998  13093      0  -1271    754       O  
ATOM    854  OD2 ASP A 111      52.687  13.021  35.726  1.00103.49           O  
ANISOU  854  OD2 ASP A 111    14128  11976  13220    107  -1236    679       O  
ATOM    855  N   LEU A 112      53.964  18.538  34.293  1.00 77.12           N  
ANISOU  855  N   LEU A 112    10377   9046   9880   -182   -558    480       N  
ATOM    856  CA  LEU A 112      54.650  19.549  33.528  1.00 73.47           C  
ANISOU  856  CA  LEU A 112     9809   8657   9450   -239   -386    379       C  
ATOM    857  C   LEU A 112      55.421  20.404  34.532  1.00 75.25           C  
ANISOU  857  C   LEU A 112     9942   8935   9716   -271   -421    342       C  
ATOM    858  O   LEU A 112      54.995  20.559  35.676  1.00 71.24           O  
ANISOU  858  O   LEU A 112     9501   8414   9154   -282   -530    435       O  
ATOM    859  CB  LEU A 112      53.635  20.387  32.751  1.00 70.59           C  
ANISOU  859  CB  LEU A 112     9562   8305   8955   -331   -228    450       C  
ATOM    860  CG  LEU A 112      52.927  19.672  31.593  1.00 68.36           C  
ANISOU  860  CG  LEU A 112     9364   7976   8633   -304   -175    467       C  
ATOM    861  CD1 LEU A 112      51.704  20.455  31.165  1.00 64.17           C  
ANISOU  861  CD1 LEU A 112     8977   7441   7965   -377    -85    557       C  
ATOM    862  CD2 LEU A 112      53.870  19.479  30.416  1.00 69.16           C  
ANISOU  862  CD2 LEU A 112     9367   8097   8814   -290    -61    327       C  
ATOM    863  N   PRO A 113      56.573  20.944  34.119  1.00 79.02           N  
ANISOU  863  N   PRO A 113    10262   9473  10289   -293   -325    195       N  
ATOM    864  CA  PRO A 113      57.406  21.687  35.054  1.00 80.75           C  
ANISOU  864  CA  PRO A 113    10373   9742  10567   -316   -367    138       C  
ATOM    865  C   PRO A 113      56.685  22.859  35.701  1.00 80.89           C  
ANISOU  865  C   PRO A 113    10492   9782  10462   -414   -328    256       C  
ATOM    866  O   PRO A 113      55.929  23.555  35.026  1.00 79.51           O  
ANISOU  866  O   PRO A 113    10416   9613  10180   -496   -188    316       O  
ATOM    867  CB  PRO A 113      58.569  22.196  34.191  1.00 82.43           C  
ANISOU  867  CB  PRO A 113    10416  10024  10881   -361   -206    -46       C  
ATOM    868  CG  PRO A 113      58.222  21.904  32.779  1.00 81.47           C  
ANISOU  868  CG  PRO A 113    10347   9889  10719   -385    -56    -64       C  
ATOM    869  CD  PRO A 113      57.172  20.845  32.777  1.00 81.52           C  
ANISOU  869  CD  PRO A 113    10494   9816  10664   -304   -171     63       C  
ATOM    870  N   LYS A 114      56.897  23.053  37.002  1.00 82.22           N  
ANISOU  870  N   LYS A 114    10643   9956  10642   -400   -465    284       N  
ATOM    871  CA  LYS A 114      56.345  24.212  37.690  1.00 81.66           C  
ANISOU  871  CA  LYS A 114    10645   9915  10469   -491   -432    373       C  
ATOM    872  C   LYS A 114      56.992  25.428  37.062  1.00 82.87           C  
ANISOU  872  C   LYS A 114    10711  10132  10643   -586   -252    280       C  
ATOM    873  O   LYS A 114      58.209  25.438  36.849  1.00 88.60           O  
ANISOU  873  O   LYS A 114    11273  10896  11496   -576   -223    129       O  
ATOM    874  CB  LYS A 114      56.634  24.166  39.197  1.00 79.16           C  
ANISOU  874  CB  LYS A 114    10315   9593  10169   -457   -613    399       C  
ATOM    875  N   LEU A 115      56.181  26.431  36.730  1.00 81.09           N  
ANISOU  875  N   LEU A 115    10600   9913  10296   -681   -133    356       N  
ATOM    876  CA  LEU A 115      56.683  27.657  36.114  1.00 77.49           C  
ANISOU  876  CA  LEU A 115    10112   9499   9831   -790     40    285       C  
ATOM    877  C   LEU A 115      57.266  28.537  37.208  1.00 77.52           C  
ANISOU  877  C   LEU A 115    10039   9548   9867   -831     -5    260       C  
ATOM    878  O   LEU A 115      56.641  28.742  38.253  1.00 72.31           O  
ANISOU  878  O   LEU A 115     9446   8882   9147   -820   -113    358       O  
ATOM    879  CB  LEU A 115      55.568  28.390  35.358  1.00 74.57           C  
ANISOU  879  CB  LEU A 115     9921   9099   9315   -862    153    376       C  
ATOM    880  N   LYS A 116      58.481  29.023  36.975  1.00 81.10           N  
ANISOU  880  N   LYS A 116    10345  10051  10418   -882     82    115       N  
ATOM    881  CA  LYS A 116      59.163  29.921  37.911  1.00 85.05           C  
ANISOU  881  CA  LYS A 116    10755  10599  10962   -929     55     66       C  
ATOM    882  C   LYS A 116      59.323  31.289  37.232  1.00 85.24           C  
ANISOU  882  C   LYS A 116    10818  10643  10925  -1081    255     32       C  
ATOM    883  O   LYS A 116      60.278  31.512  36.488  1.00 91.08           O  
ANISOU  883  O   LYS A 116    11453  11416  11736  -1152    395   -111       O  
ATOM    884  CB  LYS A 116      60.524  29.337  38.326  1.00 84.57           C  
ANISOU  884  CB  LYS A 116    10473  10577  11081   -861    -30    -98       C  
ATOM    885  N   PRO A 117      58.380  32.209  37.471  1.00 84.90           N  
ANISOU  885  N   PRO A 117    10934  10575  10748  -1138    270    154       N  
ATOM    886  CA  PRO A 117      58.358  33.414  36.645  1.00 85.92           C  
ANISOU  886  CA  PRO A 117    11160  10693  10794  -1277    449    139       C  
ATOM    887  C   PRO A 117      59.579  34.289  36.859  1.00 87.62           C  
ANISOU  887  C   PRO A 117    11242  10962  11087  -1380    535      8       C  
ATOM    888  O   PRO A 117      59.919  34.595  37.999  1.00 87.12           O  
ANISOU  888  O   PRO A 117    11091  10935  11077  -1361    432     -2       O  
ATOM    889  CB  PRO A 117      57.086  34.134  37.106  1.00 83.86           C  
ANISOU  889  CB  PRO A 117    11077  10392  10393  -1283    393    285       C  
ATOM    890  CG  PRO A 117      56.878  33.675  38.503  1.00 83.97           C  
ANISOU  890  CG  PRO A 117    11029  10432  10444  -1193    209    337       C  
ATOM    891  CD  PRO A 117      57.361  32.249  38.535  1.00 84.87           C  
ANISOU  891  CD  PRO A 117    11028  10553  10664  -1088    125    291       C  
ATOM    892  N   ASP A 118      60.234  34.676  35.765  1.00 90.87           N  
ANISOU  892  N   ASP A 118    11646  11378  11503  -1497    727    -99       N  
ATOM    893  CA  ASP A 118      61.360  35.611  35.820  1.00 92.10           C  
ANISOU  893  CA  ASP A 118    11691  11582  11719  -1632    847   -236       C  
ATOM    894  C   ASP A 118      60.948  36.975  35.255  1.00 88.68           C  
ANISOU  894  C   ASP A 118    11468  11095  11131  -1789    989   -180       C  
ATOM    895  O   ASP A 118      60.673  37.090  34.058  1.00 91.64           O  
ANISOU  895  O   ASP A 118    11995  11417  11408  -1865   1127   -170       O  
ATOM    896  CB  ASP A 118      62.563  35.063  35.044  1.00 96.97           C  
ANISOU  896  CB  ASP A 118    12127  12253  12464  -1675    977   -435       C  
ATOM    897  CG  ASP A 118      63.856  35.792  35.382  1.00101.06           C  
ANISOU  897  CG  ASP A 118    12459  12845  13096  -1788   1063   -613       C  
ATOM    898  OD1 ASP A 118      64.617  35.271  36.234  1.00 99.78           O  
ANISOU  898  OD1 ASP A 118    12070  12743  13097  -1694    934   -719       O  
ATOM    899  OD2 ASP A 118      64.093  36.891  34.816  1.00108.16           O  
ANISOU  899  OD2 ASP A 118    13449  13732  13916  -1973   1249   -648       O  
ATOM    900  N   PRO A 119      60.917  38.014  36.107  1.00 83.55           N  
ANISOU  900  N   PRO A 119    10843  10449  10455  -1838    947   -146       N  
ATOM    901  CA  PRO A 119      60.460  39.366  35.747  1.00 82.32           C  
ANISOU  901  CA  PRO A 119    10903  10225  10150  -1971   1040    -83       C  
ATOM    902  C   PRO A 119      61.089  39.972  34.512  1.00 83.21           C  
ANISOU  902  C   PRO A 119    11100  10308  10207  -2158   1273   -178       C  
ATOM    903  O   PRO A 119      60.389  40.604  33.733  1.00 82.13           O  
ANISOU  903  O   PRO A 119    11219  10077   9910  -2229   1339    -97       O  
ATOM    904  CB  PRO A 119      60.851  40.194  36.962  1.00 83.50           C  
ANISOU  904  CB  PRO A 119    10963  10415  10348  -1997    968   -101       C  
ATOM    905  CG  PRO A 119      60.770  39.233  38.085  1.00 83.60           C  
ANISOU  905  CG  PRO A 119    10818  10483  10464  -1827    770    -77       C  
ATOM    906  CD  PRO A 119      61.250  37.923  37.535  1.00 83.86           C  
ANISOU  906  CD  PRO A 119    10719  10546  10598  -1755    783   -158       C  
ATOM    907  N   ASN A 120      62.400  39.802  34.364  1.00 87.30           N  
ANISOU  907  N   ASN A 120    11410  10903  10855  -2240   1390   -359       N  
ATOM    908  CA  ASN A 120      63.110  40.254  33.174  1.00 92.06           C  
ANISOU  908  CA  ASN A 120    12072  11492  11414  -2440   1637   -478       C  
ATOM    909  C   ASN A 120      62.590  39.602  31.924  1.00 91.94           C  
ANISOU  909  C   ASN A 120    12209  11421  11305  -2431   1715   -440       C  
ATOM    910  O   ASN A 120      62.097  40.289  31.029  1.00 93.74           O  
ANISOU  910  O   ASN A 120    12709  11549  11356  -2546   1822   -374       O  
ATOM    911  CB  ASN A 120      64.607  39.946  33.258  1.00 96.30           C  
ANISOU  911  CB  ASN A 120    12307  12145  12140  -2508   1741   -712       C  
ATOM    912  CG  ASN A 120      65.408  41.095  33.822  1.00 99.59           C  
ANISOU  912  CG  ASN A 120    12651  12595  12594  -2659   1813   -807       C  
ATOM    913  OD1 ASN A 120      64.891  41.925  34.590  1.00 97.62           O  
ANISOU  913  OD1 ASN A 120    12509  12305  12278  -2650   1711   -690       O  
ATOM    914  ND2 ASN A 120      66.686  41.151  33.445  1.00101.48           N  
ANISOU  914  ND2 ASN A 120    12700  12913  12946  -2803   1992  -1034       N  
ATOM    915  N   THR A 121      62.714  38.278  31.864  1.00 89.10           N  
ANISOU  915  N   THR A 121    11683  11114  11059  -2291   1652   -485       N  
ATOM    916  CA  THR A 121      62.369  37.554  30.650  1.00 89.46           C  
ANISOU  916  CA  THR A 121    11837  11117  11036  -2283   1736   -477       C  
ATOM    917  C   THR A 121      60.893  37.768  30.346  1.00 85.52           C  
ANISOU  917  C   THR A 121    11636  10503  10355  -2220   1646   -271       C  
ATOM    918  O   THR A 121      60.513  37.874  29.183  1.00 85.72           O  
ANISOU  918  O   THR A 121    11875  10451  10244  -2293   1757   -244       O  
ATOM    919  CB  THR A 121      62.675  36.034  30.720  1.00 90.12           C  
ANISOU  919  CB  THR A 121    11693  11269  11278  -2120   1651   -553       C  
ATOM    920  OG1 THR A 121      61.702  35.385  31.533  1.00 95.90           O  
ANISOU  920  OG1 THR A 121    12442  11979  12018  -1920   1415   -399       O  
ATOM    921  CG2 THR A 121      64.061  35.757  31.284  1.00 92.38           C  
ANISOU  921  CG2 THR A 121    11653  11671  11777  -2128   1668   -765       C  
ATOM    922  N   LEU A 122      60.061  37.825  31.381  1.00 81.47           N  
ANISOU  922  N   LEU A 122    11139   9978   9839  -2087   1445   -140       N  
ATOM    923  CA  LEU A 122      58.633  38.012  31.158  1.00 81.46           C  
ANISOU  923  CA  LEU A 122    11389   9876   9685  -2017   1348     28       C  
ATOM    924  C   LEU A 122      58.372  39.422  30.619  1.00 82.19           C  
ANISOU  924  C   LEU A 122    11747   9871   9609  -2171   1442     67       C  
ATOM    925  O   LEU A 122      57.608  39.602  29.655  1.00 82.06           O  
ANISOU  925  O   LEU A 122    11985   9752   9444  -2188   1469    135       O  
ATOM    926  CB  LEU A 122      57.810  37.707  32.423  1.00 78.12           C  
ANISOU  926  CB  LEU A 122    10905   9475   9302  -1851   1124    137       C  
ATOM    927  CG  LEU A 122      57.707  36.221  32.830  1.00 80.08           C  
ANISOU  927  CG  LEU A 122    10984   9777   9667  -1686   1001    141       C  
ATOM    928  CD1 LEU A 122      57.235  36.073  34.280  1.00 78.88           C  
ANISOU  928  CD1 LEU A 122    10751   9660   9561  -1573    806    218       C  
ATOM    929  CD2 LEU A 122      56.825  35.375  31.906  1.00 77.78           C  
ANISOU  929  CD2 LEU A 122    10819   9428   9307  -1609    989    205       C  
ATOM    930  N   CYS A 123      59.007  40.421  31.221  1.00 80.78           N  
ANISOU  930  N   CYS A 123    11527   9714   9450  -2281   1482     21       N  
ATOM    931  CA  CYS A 123      58.806  41.794  30.759  1.00 81.47           C  
ANISOU  931  CA  CYS A 123    11883   9696   9377  -2433   1562     56       C  
ATOM    932  C   CYS A 123      59.386  42.022  29.354  1.00 81.07           C  
ANISOU  932  C   CYS A 123    11987   9589   9226  -2622   1790    -23       C  
ATOM    933  O   CYS A 123      58.881  42.860  28.611  1.00 81.41           O  
ANISOU  933  O   CYS A 123    12343   9502   9087  -2716   1833     39       O  
ATOM    934  CB  CYS A 123      59.350  42.814  31.769  1.00 82.64           C  
ANISOU  934  CB  CYS A 123    11951   9879   9571  -2510   1549     24       C  
ATOM    935  SG  CYS A 123      58.196  43.203  33.117  1.00 80.77           S  
ANISOU  935  SG  CYS A 123    11735   9630   9325  -2344   1294    163       S  
ATOM    936  N   ASP A 124      60.429  41.279  28.989  1.00 81.50           N  
ANISOU  936  N   ASP A 124    11835   9736   9393  -2677   1931   -168       N  
ATOM    937  CA  ASP A 124      60.971  41.341  27.631  1.00 84.44           C  
ANISOU  937  CA  ASP A 124    12341  10069   9672  -2860   2163   -259       C  
ATOM    938  C   ASP A 124      59.940  40.778  26.653  1.00 83.68           C  
ANISOU  938  C   ASP A 124    12474   9877   9445  -2773   2120   -155       C  
ATOM    939  O   ASP A 124      59.555  41.446  25.681  1.00 84.66           O  
ANISOU  939  O   ASP A 124    12924   9871   9372  -2891   2201   -106       O  
ATOM    940  CB  ASP A 124      62.301  40.573  27.507  1.00 86.64           C  
ANISOU  940  CB  ASP A 124    12306  10485  10126  -2920   2314   -465       C  
ATOM    941  CG  ASP A 124      63.478  41.264  28.236  1.00 90.28           C  
ANISOU  941  CG  ASP A 124    12560  11035  10706  -3055   2402   -610       C  
ATOM    942  OD1 ASP A 124      63.474  42.510  28.419  1.00 92.62           O  
ANISOU  942  OD1 ASP A 124    13020  11268  10902  -3194   2441   -573       O  
ATOM    943  OD2 ASP A 124      64.433  40.548  28.621  1.00 91.95           O  
ANISOU  943  OD2 ASP A 124    12439  11378  11118  -3020   2424   -774       O  
ATOM    944  N   GLU A 125      59.464  39.569  26.948  1.00 82.89           N  
ANISOU  944  N   GLU A 125    12216   9830   9448  -2564   1978   -118       N  
ATOM    945  CA  GLU A 125      58.487  38.863  26.101  1.00 82.07           C  
ANISOU  945  CA  GLU A 125    12283   9651   9250  -2458   1922    -31       C  
ATOM    946  C   GLU A 125      57.223  39.695  25.884  1.00 79.50           C  
ANISOU  946  C   GLU A 125    12290   9178   8738  -2430   1808    121       C  
ATOM    947  O   GLU A 125      56.650  39.717  24.786  1.00 79.44           O  
ANISOU  947  O   GLU A 125    12546   9061   8577  -2453   1839    165       O  
ATOM    948  CB  GLU A 125      58.136  37.493  26.710  1.00 81.54           C  
ANISOU  948  CB  GLU A 125    11982   9666   9336  -2235   1760     -8       C  
ATOM    949  CG  GLU A 125      59.279  36.468  26.702  1.00 82.73           C  
ANISOU  949  CG  GLU A 125    11831   9938   9665  -2229   1847   -167       C  
ATOM    950  CD  GLU A 125      58.982  35.196  27.503  1.00 83.36           C  
ANISOU  950  CD  GLU A 125    11693  10084   9897  -2009   1656   -138       C  
ATOM    951  OE1 GLU A 125      59.585  34.140  27.196  1.00 84.74           O  
ANISOU  951  OE1 GLU A 125    11690  10320  10186  -1963   1694   -245       O  
ATOM    952  OE2 GLU A 125      58.142  35.222  28.434  1.00 82.30           O  
ANISOU  952  OE2 GLU A 125    11571   9936   9764  -1884   1468    -14       O  
ATOM    953  N   PHE A 126      56.827  40.406  26.931  1.00 76.81           N  
ANISOU  953  N   PHE A 126    11938   8834   8412  -2380   1671    188       N  
ATOM    954  CA  PHE A 126      55.640  41.242  26.904  1.00 76.61           C  
ANISOU  954  CA  PHE A 126    12190   8679   8238  -2333   1535    310       C  
ATOM    955  C   PHE A 126      55.792  42.451  25.977  1.00 81.60           C  
ANISOU  955  C   PHE A 126    13157   9170   8676  -2527   1656    308       C  
ATOM    956  O   PHE A 126      54.945  42.680  25.110  1.00 84.77           O  
ANISOU  956  O   PHE A 126    13858   9434   8918  -2508   1608    375       O  
ATOM    957  CB  PHE A 126      55.317  41.705  28.322  1.00 73.07           C  
ANISOU  957  CB  PHE A 126    11616   8279   7869  -2246   1376    356       C  
ATOM    958  CG  PHE A 126      54.152  42.647  28.402  1.00 71.26           C  
ANISOU  958  CG  PHE A 126    11641   7926   7507  -2195   1230    453       C  
ATOM    959  CD1 PHE A 126      54.350  44.011  28.515  1.00 70.61           C  
ANISOU  959  CD1 PHE A 126    11727   7766   7334  -2321   1255    455       C  
ATOM    960  CD2 PHE A 126      52.861  42.169  28.381  1.00 70.17           C  
ANISOU  960  CD2 PHE A 126    11567   7750   7343  -2019   1061    529       C  
ATOM    961  CE1 PHE A 126      53.278  44.882  28.603  1.00 69.73           C  
ANISOU  961  CE1 PHE A 126    11847   7536   7111  -2258   1100    529       C  
ATOM    962  CE2 PHE A 126      51.784  43.033  28.451  1.00 71.26           C  
ANISOU  962  CE2 PHE A 126    11922   7779   7376  -1960    915    590       C  
ATOM    963  CZ  PHE A 126      51.997  44.401  28.551  1.00 69.69           C  
ANISOU  963  CZ  PHE A 126    11895   7496   7087  -2075    928    589       C  
ATOM    964  N   LYS A 127      56.853  43.236  26.169  1.00 84.98           N  
ANISOU  964  N   LYS A 127    13549   9624   9115  -2715   1804    228       N  
ATOM    965  CA  LYS A 127      57.117  44.379  25.275  1.00 88.39           C  
ANISOU  965  CA  LYS A 127    14316   9916   9352  -2935   1942    219       C  
ATOM    966  C   LYS A 127      57.256  43.874  23.838  1.00 87.74           C  
ANISOU  966  C   LYS A 127    14410   9774   9154  -3026   2095    184       C  
ATOM    967  O   LYS A 127      56.729  44.477  22.903  1.00 85.10           O  
ANISOU  967  O   LYS A 127    14454   9271   8609  -3097   2099    242       O  
ATOM    968  CB  LYS A 127      58.379  45.161  25.680  1.00 87.13           C  
ANISOU  968  CB  LYS A 127    14050   9814   9240  -3148   2112    112       C  
ATOM    969  N   ALA A 128      57.945  42.748  23.682  1.00 86.48           N  
ANISOU  969  N   ALA A 128    13980   9747   9130  -3013   2204     85       N  
ATOM    970  CA  ALA A 128      58.238  42.226  22.366  1.00 89.63           C  
ANISOU  970  CA  ALA A 128    14503  10114   9437  -3115   2376     25       C  
ATOM    971  C   ALA A 128      56.944  41.942  21.602  1.00 91.06           C  
ANISOU  971  C   ALA A 128    14967  10159   9472  -2978   2232    148       C  
ATOM    972  O   ALA A 128      56.768  42.432  20.481  1.00 89.67           O  
ANISOU  972  O   ALA A 128    15147   9838   9085  -3106   2314    167       O  
ATOM    973  CB  ALA A 128      59.094  40.973  22.475  1.00 89.71           C  
ANISOU  973  CB  ALA A 128    14136  10298   9649  -3076   2473   -109       C  
ATOM    974  N   ASP A 129      56.038  41.165  22.208  1.00 87.83           N  
ANISOU  974  N   ASP A 129    14411   9793   9169  -2726   2016    224       N  
ATOM    975  CA  ASP A 129      54.805  40.783  21.533  1.00 83.86           C  
ANISOU  975  CA  ASP A 129    14126   9180   8557  -2581   1872    319       C  
ATOM    976  C   ASP A 129      53.700  40.475  22.526  1.00 82.39           C  
ANISOU  976  C   ASP A 129    13816   9020   8467  -2338   1613    410       C  
ATOM    977  O   ASP A 129      53.580  39.351  23.020  1.00 85.34           O  
ANISOU  977  O   ASP A 129    13919   9508   8997  -2191   1548    403       O  
ATOM    978  CB  ASP A 129      55.059  39.590  20.601  1.00 83.81           C  
ANISOU  978  CB  ASP A 129    14061   9214   8568  -2570   1982    259       C  
ATOM    979  CG  ASP A 129      53.864  39.276  19.706  1.00 84.24           C  
ANISOU  979  CG  ASP A 129    14385   9138   8486  -2452   1857    344       C  
ATOM    980  OD1 ASP A 129      52.815  39.939  19.856  1.00 79.77           O  
ANISOU  980  OD1 ASP A 129    14028   8456   7826  -2362   1671    440       O  
ATOM    981  OD2 ASP A 129      53.971  38.359  18.848  1.00 87.00           O  
ANISOU  981  OD2 ASP A 129    14731   9500   8825  -2444   1938    303       O  
ATOM    982  N   GLU A 130      52.860  41.476  22.767  1.00 83.37           N  
ANISOU  982  N   GLU A 130    14158   9030   8489  -2301   1464    488       N  
ATOM    983  CA  GLU A 130      51.764  41.395  23.739  1.00 81.62           C  
ANISOU  983  CA  GLU A 130    13839   8829   8344  -2095   1226    557       C  
ATOM    984  C   GLU A 130      50.691  40.336  23.445  1.00 81.97           C  
ANISOU  984  C   GLU A 130    13863   8870   8413  -1901   1089    595       C  
ATOM    985  O   GLU A 130      50.256  39.630  24.360  1.00 81.75           O  
ANISOU  985  O   GLU A 130    13589   8945   8525  -1754    976    611       O  
ATOM    986  CB  GLU A 130      51.083  42.758  23.881  1.00 83.65           C  
ANISOU  986  CB  GLU A 130    14365   8946   8471  -2102   1099    609       C  
ATOM    987  CG  GLU A 130      51.959  43.824  24.537  1.00 90.81           C  
ANISOU  987  CG  GLU A 130    15247   9870   9386  -2258   1185    582       C  
ATOM    988  CD  GLU A 130      51.176  45.032  25.050  1.00 94.02           C  
ANISOU  988  CD  GLU A 130    15834  10170   9718  -2212   1009    631       C  
ATOM    989  OE1 GLU A 130      50.035  44.849  25.538  1.00 97.76           O  
ANISOU  989  OE1 GLU A 130    16269  10643  10233  -2019    804    668       O  
ATOM    990  OE2 GLU A 130      51.708  46.163  24.973  1.00 91.53           O  
ANISOU  990  OE2 GLU A 130    15697   9772   9308  -2374   1079    621       O  
ATOM    991  N   LYS A 131      50.235  40.233  22.201  1.00 79.92           N  
ANISOU  991  N   LYS A 131    13869   8487   8010  -1904   1094    608       N  
ATOM    992  CA  LYS A 131      49.208  39.237  21.875  1.00 78.15           C  
ANISOU  992  CA  LYS A 131    13628   8256   7810  -1723    964    634       C  
ATOM    993  C   LYS A 131      49.769  37.812  22.055  1.00 76.34           C  
ANISOU  993  C   LYS A 131    13086   8178   7741  -1683   1050    595       C  
ATOM    994  O   LYS A 131      49.076  36.933  22.576  1.00 75.94           O  
ANISOU  994  O   LYS A 131    12863   8193   7799  -1522    925    617       O  
ATOM    995  CB  LYS A 131      48.626  39.453  20.459  1.00 81.06           C  
ANISOU  995  CB  LYS A 131    14367   8448   7983  -1733    942    650       C  
ATOM    996  CG  LYS A 131      47.446  38.550  20.067  1.00 81.68           C  
ANISOU  996  CG  LYS A 131    14458   8502   8076  -1541    785    670       C  
ATOM    997  CD  LYS A 131      46.128  38.922  20.742  1.00 81.40           C  
ANISOU  997  CD  LYS A 131    14432   8430   8066  -1369    538    698       C  
ATOM    998  N   LYS A 132      51.016  37.584  21.644  1.00 74.99           N  
ANISOU  998  N   LYS A 132    12843   8062   7589  -1830   1259    526       N  
ATOM    999  CA  LYS A 132      51.659  36.272  21.804  1.00 73.31           C  
ANISOU  999  CA  LYS A 132    12332   7985   7536  -1790   1334    469       C  
ATOM   1000  C   LYS A 132      51.869  35.959  23.294  1.00 71.06           C  
ANISOU 1000  C   LYS A 132    11725   7836   7438  -1709   1251    470       C  
ATOM   1001  O   LYS A 132      51.731  34.822  23.735  1.00 65.61           O  
ANISOU 1001  O   LYS A 132    10822   7229   6878  -1586   1184    469       O  
ATOM   1002  CB  LYS A 132      52.991  36.239  21.057  1.00 75.71           C  
ANISOU 1002  CB  LYS A 132    12623   8320   7823  -1977   1581    364       C  
ATOM   1003  CG  LYS A 132      53.812  34.969  21.243  1.00 77.99           C  
ANISOU 1003  CG  LYS A 132    12589   8752   8292  -1941   1658    275       C  
ATOM   1004  CD  LYS A 132      55.173  35.107  20.545  1.00 84.38           C  
ANISOU 1004  CD  LYS A 132    13372   9600   9088  -2146   1916    139       C  
ATOM   1005  CE  LYS A 132      55.804  33.772  20.144  1.00 86.81           C  
ANISOU 1005  CE  LYS A 132    13458  10004   9521  -2107   2002     32       C  
ATOM   1006  NZ  LYS A 132      56.289  32.909  21.258  1.00 86.62           N  
ANISOU 1006  NZ  LYS A 132    13062  10120   9732  -1985   1922    -18       N  
ATOM   1007  N   PHE A 133      52.211  36.982  24.062  1.00 69.97           N  
ANISOU 1007  N   PHE A 133    11572   7709   7303  -1784   1252    473       N  
ATOM   1008  CA  PHE A 133      52.413  36.836  25.505  1.00 67.43           C  
ANISOU 1008  CA  PHE A 133    10979   7503   7137  -1718   1168    476       C  
ATOM   1009  C   PHE A 133      51.151  36.309  26.177  1.00 63.82           C  
ANISOU 1009  C   PHE A 133    10474   7054   6719  -1534    963    554       C  
ATOM   1010  O   PHE A 133      51.177  35.369  26.973  1.00 64.63           O  
ANISOU 1010  O   PHE A 133    10348   7254   6956  -1439    898    555       O  
ATOM   1011  CB  PHE A 133      52.773  38.209  26.081  1.00 66.76           C  
ANISOU 1011  CB  PHE A 133    10955   7400   7012  -1830   1188    476       C  
ATOM   1012  CG  PHE A 133      53.164  38.184  27.525  1.00 64.99           C  
ANISOU 1012  CG  PHE A 133    10466   7291   6935  -1791   1124    466       C  
ATOM   1013  CD1 PHE A 133      54.436  37.775  27.906  1.00 65.51           C  
ANISOU 1013  CD1 PHE A 133    10287   7468   7135  -1852   1229    374       C  
ATOM   1014  CD2 PHE A 133      52.270  38.598  28.501  1.00 62.04           C  
ANISOU 1014  CD2 PHE A 133    10091   6915   6565  -1695    955    536       C  
ATOM   1015  CE1 PHE A 133      54.813  37.783  29.242  1.00 64.32           C  
ANISOU 1015  CE1 PHE A 133     9913   7414   7113  -1813   1153    363       C  
ATOM   1016  CE2 PHE A 133      52.640  38.603  29.829  1.00 61.88           C  
ANISOU 1016  CE2 PHE A 133     9851   6996   6665  -1669    897    528       C  
ATOM   1017  CZ  PHE A 133      53.910  38.191  30.202  1.00 62.39           C  
ANISOU 1017  CZ  PHE A 133     9690   7161   6856  -1725    990    448       C  
ATOM   1018  N   TRP A 134      50.052  36.962  25.841  1.00 61.25           N  
ANISOU 1018  N   TRP A 134    10380   6620   6271  -1492    861    608       N  
ATOM   1019  CA  TRP A 134      48.720  36.616  26.278  1.00 61.07           C  
ANISOU 1019  CA  TRP A 134    10352   6589   6262  -1334    678    659       C  
ATOM   1020  C   TRP A 134      48.399  35.204  25.894  1.00 63.62           C  
ANISOU 1020  C   TRP A 134    10584   6945   6645  -1236    660    659       C  
ATOM   1021  O   TRP A 134      47.946  34.408  26.718  1.00 63.60           O  
ANISOU 1021  O   TRP A 134    10406   7018   6743  -1135    564    678       O  
ATOM   1022  CB  TRP A 134      47.802  37.585  25.586  1.00 61.16           C  
ANISOU 1022  CB  TRP A 134    10664   6456   6120  -1323    598    682       C  
ATOM   1023  CG  TRP A 134      46.343  37.542  25.874  1.00 58.37           C  
ANISOU 1023  CG  TRP A 134    10349   6071   5760  -1173    406    705       C  
ATOM   1024  CD1 TRP A 134      45.652  38.203  26.884  1.00 58.64           C  
ANISOU 1024  CD1 TRP A 134    10341   6121   5817  -1116    275    711       C  
ATOM   1025  CD2 TRP A 134      45.329  36.940  25.042  1.00 58.99           C  
ANISOU 1025  CD2 TRP A 134    10540   6082   5793  -1065    320    706       C  
ATOM   1026  NE1 TRP A 134      44.304  37.988  26.781  1.00 57.84           N  
ANISOU 1026  NE1 TRP A 134    10291   5982   5703   -982    122    703       N  
ATOM   1027  CE2 TRP A 134      44.041  37.246  25.673  1.00 59.01           C  
ANISOU 1027  CE2 TRP A 134    10537   6074   5810   -944    136    700       C  
ATOM   1028  CE3 TRP A 134      45.349  36.170  23.887  1.00 58.34           C  
ANISOU 1028  CE3 TRP A 134    10547   5952   5666  -1055    375    699       C  
ATOM   1029  CZ2 TRP A 134      42.846  36.776  25.152  1.00 56.45           C  
ANISOU 1029  CZ2 TRP A 134    10284   5699   5467   -819     13    681       C  
ATOM   1030  CZ3 TRP A 134      44.142  35.708  23.382  1.00 56.27           C  
ANISOU 1030  CZ3 TRP A 134    10368   5632   5378   -926    244    695       C  
ATOM   1031  CH2 TRP A 134      42.925  35.992  24.010  1.00 55.75           C  
ANISOU 1031  CH2 TRP A 134    10283   5562   5338   -810     67    682       C  
ATOM   1032  N   GLY A 135      48.677  34.856  24.643  1.00 65.65           N  
ANISOU 1032  N   GLY A 135    10963   7145   6835  -1276    759    634       N  
ATOM   1033  CA  GLY A 135      48.427  33.501  24.153  1.00 65.17           C  
ANISOU 1033  CA  GLY A 135    10828   7106   6825  -1188    750    627       C  
ATOM   1034  C   GLY A 135      49.166  32.406  24.904  1.00 64.95           C  
ANISOU 1034  C   GLY A 135    10509   7206   6964  -1158    775    601       C  
ATOM   1035  O   GLY A 135      48.609  31.349  25.172  1.00 65.13           O  
ANISOU 1035  O   GLY A 135    10428   7260   7057  -1046    686    621       O  
ATOM   1036  N   LYS A 136      50.412  32.670  25.275  1.00 66.52           N  
ANISOU 1036  N   LYS A 136    10579   7470   7225  -1257    886    548       N  
ATOM   1037  CA  LYS A 136      51.223  31.697  25.992  1.00 67.42           C  
ANISOU 1037  CA  LYS A 136    10422   7693   7501  -1222    892    505       C  
ATOM   1038  C   LYS A 136      50.706  31.511  27.424  1.00 63.22           C  
ANISOU 1038  C   LYS A 136     9755   7217   7049  -1132    735    562       C  
ATOM   1039  O   LYS A 136      50.702  30.398  27.955  1.00 62.96           O  
ANISOU 1039  O   LYS A 136     9569   7235   7117  -1045    663    567       O  
ATOM   1040  CB  LYS A 136      52.705  32.099  25.976  1.00 73.45           C  
ANISOU 1040  CB  LYS A 136    11079   8513   8317  -1353   1048    407       C  
ATOM   1041  CG  LYS A 136      53.629  31.055  26.581  1.00 78.11           C  
ANISOU 1041  CG  LYS A 136    11391   9205   9083  -1305   1043    335       C  
ATOM   1042  CD  LYS A 136      54.920  30.802  25.797  1.00 83.09           C  
ANISOU 1042  CD  LYS A 136    11930   9875   9765  -1400   1222    194       C  
ATOM   1043  CE  LYS A 136      55.577  29.492  26.272  1.00 84.79           C  
ANISOU 1043  CE  LYS A 136    11885  10172  10161  -1297   1165    120       C  
ATOM   1044  NZ  LYS A 136      56.912  29.163  25.683  1.00 88.55           N  
ANISOU 1044  NZ  LYS A 136    12209  10707  10727  -1371   1322    -53       N  
ATOM   1045  N   TYR A 137      50.211  32.574  28.033  1.00 58.82           N  
ANISOU 1045  N   TYR A 137     9272   6641   6435  -1154    677    605       N  
ATOM   1046  CA  TYR A 137      49.575  32.417  29.342  1.00 56.14           C  
ANISOU 1046  CA  TYR A 137     8830   6352   6150  -1077    534    655       C  
ATOM   1047  C   TYR A 137      48.338  31.507  29.232  1.00 53.15           C  
ANISOU 1047  C   TYR A 137     8483   5951   5762   -964    427    699       C  
ATOM   1048  O   TYR A 137      48.241  30.518  29.940  1.00 55.35           O  
ANISOU 1048  O   TYR A 137     8627   6281   6123   -902    358    715       O  
ATOM   1049  CB  TYR A 137      49.207  33.784  29.955  1.00 55.71           C  
ANISOU 1049  CB  TYR A 137     8856   6279   6032  -1120    493    679       C  
ATOM   1050  CG  TYR A 137      48.488  33.669  31.265  1.00 53.91           C  
ANISOU 1050  CG  TYR A 137     8534   6104   5845  -1054    360    719       C  
ATOM   1051  CD1 TYR A 137      49.189  33.578  32.454  1.00 57.10           C  
ANISOU 1051  CD1 TYR A 137     8768   6590   6337  -1069    338    715       C  
ATOM   1052  CD2 TYR A 137      47.105  33.601  31.316  1.00 53.32           C  
ANISOU 1052  CD2 TYR A 137     8539   5999   5722   -978    256    750       C  
ATOM   1053  CE1 TYR A 137      48.528  33.428  33.664  1.00 56.75           C  
ANISOU 1053  CE1 TYR A 137     8656   6593   6314  -1022    223    751       C  
ATOM   1054  CE2 TYR A 137      46.432  33.464  32.508  1.00 52.50           C  
ANISOU 1054  CE2 TYR A 137     8348   5951   5649   -936    153    772       C  
ATOM   1055  CZ  TYR A 137      47.152  33.373  33.678  1.00 55.78           C  
ANISOU 1055  CZ  TYR A 137     8615   6445   6136   -964    142    778       C  
ATOM   1056  OH  TYR A 137      46.494  33.243  34.872  1.00 60.83           O  
ANISOU 1056  OH  TYR A 137     9187   7136   6788   -939     50    800       O  
ATOM   1057  N   LEU A 138      47.390  31.839  28.359  1.00 51.29           N  
ANISOU 1057  N   LEU A 138     8432   5631   5424   -940    405    712       N  
ATOM   1058  CA  LEU A 138      46.298  30.919  28.039  1.00 51.38           C  
ANISOU 1058  CA  LEU A 138     8471   5620   5432   -840    322    731       C  
ATOM   1059  C   LEU A 138      46.800  29.475  27.872  1.00 52.08           C  
ANISOU 1059  C   LEU A 138     8433   5746   5610   -802    349    721       C  
ATOM   1060  O   LEU A 138      46.193  28.536  28.344  1.00 51.95           O  
ANISOU 1060  O   LEU A 138     8343   5754   5643   -733    265    744       O  
ATOM   1061  CB  LEU A 138      45.609  31.354  26.742  1.00 50.86           C  
ANISOU 1061  CB  LEU A 138     8630   5446   5249   -827    324    721       C  
ATOM   1062  CG  LEU A 138      44.747  32.603  26.859  1.00 50.30           C  
ANISOU 1062  CG  LEU A 138     8706   5314   5091   -820    241    724       C  
ATOM   1063  CD1 LEU A 138      43.997  32.849  25.563  1.00 48.78           C  
ANISOU 1063  CD1 LEU A 138     8746   5001   4786   -782    208    710       C  
ATOM   1064  CD2 LEU A 138      43.756  32.455  28.020  1.00 48.75           C  
ANISOU 1064  CD2 LEU A 138     8396   5177   4948   -751    114    732       C  
ATOM   1065  N   TYR A 139      47.910  29.315  27.177  1.00 52.95           N  
ANISOU 1065  N   TYR A 139     8524   5857   5739   -855    467    676       N  
ATOM   1066  CA  TYR A 139      48.436  28.019  26.872  1.00 53.66           C  
ANISOU 1066  CA  TYR A 139     8504   5972   5912   -814    492    646       C  
ATOM   1067  C   TYR A 139      48.945  27.342  28.117  1.00 55.06           C  
ANISOU 1067  C   TYR A 139     8483   6226   6212   -781    425    650       C  
ATOM   1068  O   TYR A 139      48.632  26.169  28.355  1.00 59.57           O  
ANISOU 1068  O   TYR A 139     8990   6803   6840   -704    348    668       O  
ATOM   1069  CB  TYR A 139      49.540  28.178  25.800  1.00 55.46           C  
ANISOU 1069  CB  TYR A 139     8759   6188   6125   -894    653    570       C  
ATOM   1070  CG  TYR A 139      50.464  27.001  25.592  1.00 55.15           C  
ANISOU 1070  CG  TYR A 139     8562   6195   6200   -867    698    502       C  
ATOM   1071  CD1 TYR A 139      50.065  25.894  24.858  1.00 54.09           C  
ANISOU 1071  CD1 TYR A 139     8449   6029   6073   -792    678    498       C  
ATOM   1072  CD2 TYR A 139      51.751  27.011  26.114  1.00 56.06           C  
ANISOU 1072  CD2 TYR A 139     8500   6381   6420   -911    753    427       C  
ATOM   1073  CE1 TYR A 139      50.930  24.829  24.656  1.00 55.02           C  
ANISOU 1073  CE1 TYR A 139     8422   6184   6301   -759    711    423       C  
ATOM   1074  CE2 TYR A 139      52.618  25.942  25.927  1.00 55.93           C  
ANISOU 1074  CE2 TYR A 139     8327   6404   6520   -872    778    341       C  
ATOM   1075  CZ  TYR A 139      52.204  24.859  25.200  1.00 55.44           C  
ANISOU 1075  CZ  TYR A 139     8294   6307   6462   -795    756    341       C  
ATOM   1076  OH  TYR A 139      53.051  23.807  25.038  1.00 57.13           O  
ANISOU 1076  OH  TYR A 139     8354   6556   6799   -747    766    247       O  
ATOM   1077  N   GLU A 140      49.755  28.028  28.919  1.00 56.81           N  
ANISOU 1077  N   GLU A 140     8615   6498   6473   -839    445    631       N  
ATOM   1078  CA  GLU A 140      50.429  27.302  30.002  1.00 57.70           C  
ANISOU 1078  CA  GLU A 140     8546   6673   6706   -802    375    619       C  
ATOM   1079  C   GLU A 140      49.450  26.916  31.102  1.00 57.50           C  
ANISOU 1079  C   GLU A 140     8516   6654   6676   -747    232    699       C  
ATOM   1080  O   GLU A 140      49.622  25.855  31.747  1.00 58.26           O  
ANISOU 1080  O   GLU A 140     8522   6767   6846   -690    145    709       O  
ATOM   1081  CB  GLU A 140      51.667  28.020  30.532  1.00 60.19           C  
ANISOU 1081  CB  GLU A 140     8748   7042   7080   -873    431    557       C  
ATOM   1082  CG  GLU A 140      52.841  28.088  29.527  1.00 65.34           C  
ANISOU 1082  CG  GLU A 140     9354   7704   7768   -937    584    446       C  
ATOM   1083  CD  GLU A 140      53.752  26.832  29.405  1.00 67.03           C  
ANISOU 1083  CD  GLU A 140     9400   7951   8117   -874    576    357       C  
ATOM   1084  OE1 GLU A 140      53.448  25.719  29.882  1.00 65.58           O  
ANISOU 1084  OE1 GLU A 140     9164   7762   7992   -769    447    390       O  
ATOM   1085  OE2 GLU A 140      54.841  26.972  28.810  1.00 75.02           O  
ANISOU 1085  OE2 GLU A 140    10331   8994   9180   -936    703    237       O  
ATOM   1086  N   ILE A 141      48.393  27.707  31.281  1.00 53.48           N  
ANISOU 1086  N   ILE A 141     8114   6128   6078   -763    204    745       N  
ATOM   1087  CA  ILE A 141      47.366  27.336  32.249  1.00 51.77           C  
ANISOU 1087  CA  ILE A 141     7895   5926   5849   -728     90    801       C  
ATOM   1088  C   ILE A 141      46.458  26.246  31.688  1.00 51.36           C  
ANISOU 1088  C   ILE A 141     7893   5835   5787   -666     51    819       C  
ATOM   1089  O   ILE A 141      46.071  25.313  32.399  1.00 51.68           O  
ANISOU 1089  O   ILE A 141     7894   5887   5856   -637    -29    851       O  
ATOM   1090  CB  ILE A 141      46.478  28.531  32.636  1.00 51.35           C  
ANISOU 1090  CB  ILE A 141     7920   5873   5716   -760     68    818       C  
ATOM   1091  CG1 ILE A 141      47.299  29.638  33.306  1.00 53.05           C  
ANISOU 1091  CG1 ILE A 141     8092   6126   5939   -825     96    805       C  
ATOM   1092  CG2 ILE A 141      45.360  28.099  33.561  1.00 49.01           C  
ANISOU 1092  CG2 ILE A 141     7615   5601   5407   -738    -29    852       C  
ATOM   1093  CD1 ILE A 141      48.048  29.204  34.542  1.00 51.60           C  
ANISOU 1093  CD1 ILE A 141     7773   6001   5832   -828     42    814       C  
ATOM   1094  N   ALA A 142      46.085  26.368  30.421  1.00 50.71           N  
ANISOU 1094  N   ALA A 142     7912   5700   5654   -652    106    798       N  
ATOM   1095  CA  ALA A 142      45.144  25.423  29.845  1.00 51.53           C  
ANISOU 1095  CA  ALA A 142     8068   5766   5746   -592     66    806       C  
ATOM   1096  C   ALA A 142      45.735  24.003  29.773  1.00 52.55           C  
ANISOU 1096  C   ALA A 142     8116   5894   5956   -549     51    804       C  
ATOM   1097  O   ALA A 142      45.044  23.019  30.057  1.00 48.71           O  
ANISOU 1097  O   ALA A 142     7627   5397   5484   -513    -20    831       O  
ATOM   1098  CB  ALA A 142      44.677  25.888  28.480  1.00 50.12           C  
ANISOU 1098  CB  ALA A 142     8030   5523   5490   -581    115    780       C  
ATOM   1099  N   ARG A 143      47.018  23.880  29.458  1.00 53.76           N  
ANISOU 1099  N   ARG A 143     8201   6059   6168   -558    114    762       N  
ATOM   1100  CA  ARG A 143      47.574  22.532  29.404  1.00 55.21           C  
ANISOU 1100  CA  ARG A 143     8304   6235   6437   -501     80    744       C  
ATOM   1101  C   ARG A 143      47.766  21.891  30.779  1.00 56.17           C  
ANISOU 1101  C   ARG A 143     8342   6379   6619   -483    -36    780       C  
ATOM   1102  O   ARG A 143      47.895  20.655  30.879  1.00 59.57           O  
ANISOU 1102  O   ARG A 143     8744   6783   7106   -426   -106    783       O  
ATOM   1103  CB  ARG A 143      48.825  22.465  28.538  1.00 56.25           C  
ANISOU 1103  CB  ARG A 143     8376   6372   6623   -506    180    660       C  
ATOM   1104  CG  ARG A 143      50.062  23.169  29.030  1.00 57.85           C  
ANISOU 1104  CG  ARG A 143     8470   6629   6881   -558    228    605       C  
ATOM   1105  CD  ARG A 143      50.977  23.368  27.820  1.00 59.01           C  
ANISOU 1105  CD  ARG A 143     8603   6778   7040   -597    376    506       C  
ATOM   1106  NE  ARG A 143      52.400  23.237  28.140  1.00 60.73           N  
ANISOU 1106  NE  ARG A 143     8648   7050   7377   -606    405    405       N  
ATOM   1107  CZ  ARG A 143      53.173  22.202  27.838  1.00 60.67           C  
ANISOU 1107  CZ  ARG A 143     8525   7051   7477   -546    396    316       C  
ATOM   1108  NH1 ARG A 143      54.448  22.210  28.193  1.00 62.78           N  
ANISOU 1108  NH1 ARG A 143     8622   7372   7860   -553    412    203       N  
ATOM   1109  NH2 ARG A 143      52.700  21.165  27.184  1.00 60.95           N  
ANISOU 1109  NH2 ARG A 143     8604   7041   7512   -476    366    325       N  
ATOM   1110  N   ARG A 144      47.728  22.700  31.835  1.00 53.18           N  
ANISOU 1110  N   ARG A 144     7947   6041   6220   -530    -65    809       N  
ATOM   1111  CA  ARG A 144      47.784  22.175  33.201  1.00 53.25           C  
ANISOU 1111  CA  ARG A 144     7914   6063   6257   -525   -181    851       C  
ATOM   1112  C   ARG A 144      46.435  21.981  33.864  1.00 52.20           C  
ANISOU 1112  C   ARG A 144     7860   5923   6050   -550   -241    915       C  
ATOM   1113  O   ARG A 144      46.335  21.295  34.873  1.00 53.80           O  
ANISOU 1113  O   ARG A 144     8066   6120   6257   -555   -334    956       O  
ATOM   1114  CB  ARG A 144      48.608  23.109  34.073  1.00 54.05           C  
ANISOU 1114  CB  ARG A 144     7943   6215   6380   -567   -182    836       C  
ATOM   1115  CG  ARG A 144      50.074  23.094  33.679  1.00 54.31           C  
ANISOU 1115  CG  ARG A 144     7863   6263   6510   -547   -140    751       C  
ATOM   1116  CD  ARG A 144      50.850  24.092  34.481  1.00 53.02           C  
ANISOU 1116  CD  ARG A 144     7625   6151   6369   -595   -134    726       C  
ATOM   1117  NE  ARG A 144      52.260  23.993  34.177  1.00 54.63           N  
ANISOU 1117  NE  ARG A 144     7698   6377   6683   -578    -98    621       N  
ATOM   1118  CZ  ARG A 144      52.818  24.450  33.053  1.00 55.53           C  
ANISOU 1118  CZ  ARG A 144     7786   6504   6810   -615     45    540       C  
ATOM   1119  NH1 ARG A 144      52.068  24.996  32.093  1.00 55.88           N  
ANISOU 1119  NH1 ARG A 144     7953   6524   6757   -660    149    568       N  
ATOM   1120  NH2 ARG A 144      54.125  24.345  32.879  1.00 54.99           N  
ANISOU 1120  NH2 ARG A 144     7575   6467   6852   -610     81    421       N  
ATOM   1121  N   HIS A 145      45.416  22.616  33.319  1.00 50.51           N  
ANISOU 1121  N   HIS A 145     7715   5710   5768   -570   -191    914       N  
ATOM   1122  CA  HIS A 145      44.075  22.547  33.850  1.00 48.82           C  
ANISOU 1122  CA  HIS A 145     7555   5502   5492   -600   -231    941       C  
ATOM   1123  C   HIS A 145      43.174  22.297  32.663  1.00 49.42           C  
ANISOU 1123  C   HIS A 145     7697   5540   5542   -565   -199    915       C  
ATOM   1124  O   HIS A 145      42.615  23.236  32.055  1.00 48.18           O  
ANISOU 1124  O   HIS A 145     7588   5381   5339   -566   -161    884       O  
ATOM   1125  CB  HIS A 145      43.751  23.866  34.528  1.00 49.47           C  
ANISOU 1125  CB  HIS A 145     7637   5634   5526   -655   -217    936       C  
ATOM   1126  CG  HIS A 145      44.682  24.195  35.644  1.00 49.75           C  
ANISOU 1126  CG  HIS A 145     7609   5706   5585   -687   -248    956       C  
ATOM   1127  ND1 HIS A 145      44.563  23.629  36.889  1.00 49.65           N  
ANISOU 1127  ND1 HIS A 145     7594   5708   5563   -720   -325    996       N  
ATOM   1128  CD2 HIS A 145      45.769  25.000  35.698  1.00 51.18           C  
ANISOU 1128  CD2 HIS A 145     7737   5909   5799   -696   -215    936       C  
ATOM   1129  CE1 HIS A 145      45.528  24.070  37.672  1.00 50.79           C  
ANISOU 1129  CE1 HIS A 145     7685   5879   5734   -735   -351   1001       C  
ATOM   1130  NE2 HIS A 145      46.267  24.919  36.979  1.00 53.12           N  
ANISOU 1130  NE2 HIS A 145     7937   6185   6062   -721   -283    961       N  
ATOM   1131  N   PRO A 146      43.060  21.031  32.272  1.00 49.71           N  
ANISOU 1131  N   PRO A 146     7745   5534   5607   -527   -227    924       N  
ATOM   1132  CA  PRO A 146      42.375  20.719  31.003  1.00 49.73           C  
ANISOU 1132  CA  PRO A 146     7807   5494   5595   -483   -198    892       C  
ATOM   1133  C   PRO A 146      40.865  20.949  31.051  1.00 50.50           C  
ANISOU 1133  C   PRO A 146     7951   5599   5639   -502   -218    871       C  
ATOM   1134  O   PRO A 146      40.202  20.857  30.007  1.00 50.81           O  
ANISOU 1134  O   PRO A 146     8043   5602   5661   -459   -207    833       O  
ATOM   1135  CB  PRO A 146      42.700  19.243  30.767  1.00 50.74           C  
ANISOU 1135  CB  PRO A 146     7926   5577   5776   -440   -235    906       C  
ATOM   1136  CG  PRO A 146      43.211  18.749  32.088  1.00 52.45           C  
ANISOU 1136  CG  PRO A 146     8104   5806   6019   -470   -307    951       C  
ATOM   1137  CD  PRO A 146      43.825  19.902  32.798  1.00 49.90           C  
ANISOU 1137  CD  PRO A 146     7733   5536   5689   -508   -289    952       C  
ATOM   1138  N   TYR A 147      40.331  21.240  32.242  1.00 49.73           N  
ANISOU 1138  N   TYR A 147     7830   5549   5517   -565   -248    880       N  
ATOM   1139  CA  TYR A 147      38.922  21.567  32.404  1.00 48.70           C  
ANISOU 1139  CA  TYR A 147     7715   5442   5346   -591   -261    830       C  
ATOM   1140  C   TYR A 147      38.716  23.002  32.827  1.00 46.35           C  
ANISOU 1140  C   TYR A 147     7406   5190   5015   -615   -253    797       C  
ATOM   1141  O   TYR A 147      37.626  23.391  33.259  1.00 44.00           O  
ANISOU 1141  O   TYR A 147     7095   4929   4693   -644   -270    740       O  
ATOM   1142  CB  TYR A 147      38.280  20.622  33.390  1.00 50.70           C  
ANISOU 1142  CB  TYR A 147     7957   5715   5593   -661   -292    844       C  
ATOM   1143  CG  TYR A 147      38.265  19.218  32.859  1.00 56.27           C  
ANISOU 1143  CG  TYR A 147     8692   6361   6326   -635   -310    865       C  
ATOM   1144  CD1 TYR A 147      39.332  18.349  33.091  1.00 56.87           C  
ANISOU 1144  CD1 TYR A 147     8775   6399   6436   -621   -339    931       C  
ATOM   1145  CD2 TYR A 147      37.183  18.743  32.099  1.00 58.26           C  
ANISOU 1145  CD2 TYR A 147     8968   6591   6578   -615   -309    808       C  
ATOM   1146  CE1 TYR A 147      39.314  17.053  32.591  1.00 58.21           C  
ANISOU 1146  CE1 TYR A 147     8978   6505   6633   -590   -367    945       C  
ATOM   1147  CE2 TYR A 147      37.163  17.444  31.618  1.00 57.77           C  
ANISOU 1147  CE2 TYR A 147     8937   6471   6542   -594   -328    827       C  
ATOM   1148  CZ  TYR A 147      38.236  16.611  31.852  1.00 58.06           C  
ANISOU 1148  CZ  TYR A 147     8987   6467   6608   -581   -355    898       C  
ATOM   1149  OH  TYR A 147      38.223  15.320  31.363  1.00 61.60           O  
ANISOU 1149  OH  TYR A 147     9472   6849   7083   -552   -384    912       O  
ATOM   1150  N   PHE A 148      39.736  23.824  32.664  1.00 45.31           N  
ANISOU 1150  N   PHE A 148     7276   5055   4885   -602   -225    818       N  
ATOM   1151  CA  PHE A 148      39.582  25.185  33.130  1.00 46.64           C  
ANISOU 1151  CA  PHE A 148     7441   5259   5020   -628   -224    791       C  
ATOM   1152  C   PHE A 148      38.464  25.885  32.321  1.00 47.84           C  
ANISOU 1152  C   PHE A 148     7655   5385   5139   -582   -246    712       C  
ATOM   1153  O   PHE A 148      38.353  25.704  31.096  1.00 46.93           O  
ANISOU 1153  O   PHE A 148     7609   5206   5016   -522   -242    694       O  
ATOM   1154  CB  PHE A 148      40.907  25.924  33.060  1.00 47.38           C  
ANISOU 1154  CB  PHE A 148     7531   5349   5122   -635   -184    823       C  
ATOM   1155  CG  PHE A 148      40.946  27.162  33.893  1.00 49.49           C  
ANISOU 1155  CG  PHE A 148     7780   5659   5363   -678   -190    812       C  
ATOM   1156  CD1 PHE A 148      40.212  28.281  33.527  1.00 50.71           C  
ANISOU 1156  CD1 PHE A 148     7994   5799   5474   -660   -204    756       C  
ATOM   1157  CD2 PHE A 148      41.701  27.211  35.060  1.00 49.06           C  
ANISOU 1157  CD2 PHE A 148     7658   5654   5328   -729   -196    851       C  
ATOM   1158  CE1 PHE A 148      40.237  29.420  34.310  1.00 50.56           C  
ANISOU 1158  CE1 PHE A 148     7961   5817   5434   -696   -217    741       C  
ATOM   1159  CE2 PHE A 148      41.739  28.346  35.831  1.00 48.86           C  
ANISOU 1159  CE2 PHE A 148     7616   5669   5279   -768   -202    838       C  
ATOM   1160  CZ  PHE A 148      41.012  29.452  35.457  1.00 49.58           C  
ANISOU 1160  CZ  PHE A 148     7761   5748   5330   -754   -209    783       C  
ATOM   1161  N   TYR A 149      37.622  26.636  33.043  1.00 48.98           N  
ANISOU 1161  N   TYR A 149     7772   5574   5263   -607   -278    655       N  
ATOM   1162  CA  TYR A 149      36.481  27.402  32.506  1.00 48.60           C  
ANISOU 1162  CA  TYR A 149     7765   5506   5193   -555   -329    554       C  
ATOM   1163  C   TYR A 149      37.010  28.399  31.490  1.00 50.41           C  
ANISOU 1163  C   TYR A 149     8108   5659   5385   -503   -330    559       C  
ATOM   1164  O   TYR A 149      37.596  29.413  31.864  1.00 54.35           O  
ANISOU 1164  O   TYR A 149     8623   6165   5862   -529   -319    577       O  
ATOM   1165  CB  TYR A 149      35.802  28.143  33.666  1.00 49.48           C  
ANISOU 1165  CB  TYR A 149     7808   5692   5298   -601   -355    490       C  
ATOM   1166  CG  TYR A 149      34.392  28.701  33.486  1.00 49.38           C  
ANISOU 1166  CG  TYR A 149     7788   5688   5288   -555   -422    348       C  
ATOM   1167  CD1 TYR A 149      33.878  29.621  34.420  1.00 49.31           C  
ANISOU 1167  CD1 TYR A 149     7720   5742   5275   -584   -449    270       C  
ATOM   1168  CD2 TYR A 149      33.582  28.325  32.436  1.00 48.24           C  
ANISOU 1168  CD2 TYR A 149     7683   5491   5155   -479   -467    276       C  
ATOM   1169  CE1 TYR A 149      32.605  30.130  34.314  1.00 48.97           C  
ANISOU 1169  CE1 TYR A 149     7646   5713   5248   -536   -519    114       C  
ATOM   1170  CE2 TYR A 149      32.306  28.840  32.321  1.00 49.43           C  
ANISOU 1170  CE2 TYR A 149     7808   5650   5321   -427   -545    124       C  
ATOM   1171  CZ  TYR A 149      31.819  29.728  33.270  1.00 49.92           C  
ANISOU 1171  CZ  TYR A 149     7799   5780   5388   -455   -571     37       C  
ATOM   1172  OH  TYR A 149      30.551  30.252  33.150  1.00 50.89           O  
ANISOU 1172  OH  TYR A 149     7881   5915   5541   -392   -658   -142       O  
ATOM   1173  N   ALA A 150      36.808  28.112  30.206  1.00 49.49           N  
ANISOU 1173  N   ALA A 150     8085   5466   5253   -437   -342    542       N  
ATOM   1174  CA  ALA A 150      37.517  28.805  29.155  1.00 48.44           C  
ANISOU 1174  CA  ALA A 150     8087   5249   5068   -412   -320    566       C  
ATOM   1175  C   ALA A 150      37.322  30.321  29.193  1.00 49.51           C  
ANISOU 1175  C   ALA A 150     8309   5351   5152   -402   -369    525       C  
ATOM   1176  O   ALA A 150      38.296  31.074  29.202  1.00 51.57           O  
ANISOU 1176  O   ALA A 150     8621   5593   5380   -448   -318    572       O  
ATOM   1177  CB  ALA A 150      37.097  28.254  27.810  1.00 48.90           C  
ANISOU 1177  CB  ALA A 150     8248   5227   5106   -341   -341    540       C  
ATOM   1178  N   PRO A 151      36.078  30.783  29.227  1.00 49.18           N  
ANISOU 1178  N   PRO A 151     8280   5299   5106   -343   -471    426       N  
ATOM   1179  CA  PRO A 151      35.881  32.207  29.297  1.00 51.57           C  
ANISOU 1179  CA  PRO A 151     8670   5560   5364   -323   -537    380       C  
ATOM   1180  C   PRO A 151      36.551  32.887  30.502  1.00 50.91           C  
ANISOU 1180  C   PRO A 151     8505   5549   5291   -403   -494    418       C  
ATOM   1181  O   PRO A 151      37.059  33.994  30.338  1.00 51.58           O  
ANISOU 1181  O   PRO A 151     8697   5579   5324   -417   -499    433       O  
ATOM   1182  CB  PRO A 151      34.362  32.353  29.417  1.00 51.79           C  
ANISOU 1182  CB  PRO A 151     8658   5598   5420   -244   -660    240       C  
ATOM   1183  CG  PRO A 151      33.827  31.112  28.864  1.00 52.11           C  
ANISOU 1183  CG  PRO A 151     8663   5641   5496   -210   -658    220       C  
ATOM   1184  CD  PRO A 151      34.805  30.077  29.329  1.00 51.49           C  
ANISOU 1184  CD  PRO A 151     8493   5625   5444   -298   -534    337       C  
ATOM   1185  N   GLU A 152      36.565  32.254  31.673  1.00 48.92           N  
ANISOU 1185  N   GLU A 152     8086   5408   5094   -460   -455    434       N  
ATOM   1186  CA  GLU A 152      37.191  32.886  32.805  1.00 50.42           C  
ANISOU 1186  CA  GLU A 152     8208   5661   5288   -532   -424    468       C  
ATOM   1187  C   GLU A 152      38.644  32.958  32.503  1.00 51.13           C  
ANISOU 1187  C   GLU A 152     8343   5721   5363   -581   -338    566       C  
ATOM   1188  O   GLU A 152      39.279  33.969  32.806  1.00 53.77           O  
ANISOU 1188  O   GLU A 152     8709   6048   5673   -619   -324    583       O  
ATOM   1189  CB  GLU A 152      37.026  32.162  34.119  1.00 53.81           C  
ANISOU 1189  CB  GLU A 152     8480   6203   5763   -595   -398    475       C  
ATOM   1190  CG  GLU A 152      35.825  32.597  34.924  1.00 58.97           C  
ANISOU 1190  CG  GLU A 152     9061   6919   6426   -593   -458    362       C  
ATOM   1191  CD  GLU A 152      35.865  34.045  35.405  1.00 60.78           C  
ANISOU 1191  CD  GLU A 152     9311   7149   6632   -592   -500    319       C  
ATOM   1192  OE1 GLU A 152      36.575  34.372  36.392  1.00 58.75           O  
ANISOU 1192  OE1 GLU A 152     9002   6948   6372   -663   -461    371       O  
ATOM   1193  OE2 GLU A 152      35.117  34.852  34.810  1.00 65.18           O  
ANISOU 1193  OE2 GLU A 152     9942   7648   7175   -513   -587    224       O  
ATOM   1194  N   LEU A 153      39.179  31.935  31.846  1.00 48.17           N  
ANISOU 1194  N   LEU A 153     7972   5328   5004   -580   -281    617       N  
ATOM   1195  CA  LEU A 153      40.583  31.978  31.503  1.00 46.88           C  
ANISOU 1195  CA  LEU A 153     7831   5143   4836   -629   -191    683       C  
ATOM   1196  C   LEU A 153      40.927  33.191  30.608  1.00 49.49           C  
ANISOU 1196  C   LEU A 153     8332   5381   5091   -637   -177    672       C  
ATOM   1197  O   LEU A 153      41.982  33.802  30.774  1.00 50.03           O  
ANISOU 1197  O   LEU A 153     8407   5452   5150   -706   -110    701       O  
ATOM   1198  CB  LEU A 153      40.985  30.696  30.833  1.00 45.29           C  
ANISOU 1198  CB  LEU A 153     7610   4931   4667   -614   -141    715       C  
ATOM   1199  CG  LEU A 153      42.465  30.497  30.579  1.00 44.37           C  
ANISOU 1199  CG  LEU A 153     7470   4816   4573   -664    -42    757       C  
ATOM   1200  CD1 LEU A 153      43.260  30.787  31.824  1.00 42.35           C  
ANISOU 1200  CD1 LEU A 153     7095   4634   4361   -723    -28    781       C  
ATOM   1201  CD2 LEU A 153      42.675  29.088  30.048  1.00 43.04           C  
ANISOU 1201  CD2 LEU A 153     7260   4644   4449   -632    -16    771       C  
ATOM   1202  N   LEU A 154      40.038  33.565  29.691  1.00 50.08           N  
ANISOU 1202  N   LEU A 154     8553   5368   5108   -571   -246    624       N  
ATOM   1203  CA  LEU A 154      40.277  34.763  28.888  1.00 52.30           C  
ANISOU 1203  CA  LEU A 154     9036   5540   5296   -584   -253    616       C  
ATOM   1204  C   LEU A 154      40.413  35.976  29.804  1.00 53.64           C  
ANISOU 1204  C   LEU A 154     9195   5729   5456   -624   -282    605       C  
ATOM   1205  O   LEU A 154      41.307  36.803  29.643  1.00 53.01           O  
ANISOU 1205  O   LEU A 154     9204   5607   5329   -698   -221    634       O  
ATOM   1206  CB  LEU A 154      39.137  34.984  27.894  1.00 52.89           C  
ANISOU 1206  CB  LEU A 154     9277   5508   5310   -486   -366    555       C  
ATOM   1207  CG  LEU A 154      38.952  33.960  26.766  1.00 52.15           C  
ANISOU 1207  CG  LEU A 154     9244   5367   5203   -441   -350    558       C  
ATOM   1208  CD1 LEU A 154      37.808  34.431  25.876  1.00 54.30           C  
ANISOU 1208  CD1 LEU A 154     9699   5523   5410   -338   -492    484       C  
ATOM   1209  CD2 LEU A 154      40.204  33.750  25.935  1.00 51.51           C  
ANISOU 1209  CD2 LEU A 154     9247   5246   5076   -520   -211    619       C  
ATOM   1210  N   TYR A 155      39.513  36.067  30.779  1.00 55.02           N  
ANISOU 1210  N   TYR A 155     9258   5972   5677   -582   -368    555       N  
ATOM   1211  CA  TYR A 155      39.519  37.162  31.744  1.00 54.29           C  
ANISOU 1211  CA  TYR A 155     9137   5908   5583   -611   -406    532       C  
ATOM   1212  C   TYR A 155      40.846  37.247  32.520  1.00 54.78           C  
ANISOU 1212  C   TYR A 155     9101   6038   5673   -715   -299    602       C  
ATOM   1213  O   TYR A 155      41.421  38.307  32.672  1.00 58.04           O  
ANISOU 1213  O   TYR A 155     9581   6420   6052   -767   -284    610       O  
ATOM   1214  CB  TYR A 155      38.356  36.988  32.703  1.00 54.11           C  
ANISOU 1214  CB  TYR A 155     8977   5970   5614   -562   -491    455       C  
ATOM   1215  CG  TYR A 155      38.467  37.790  33.971  1.00 55.26           C  
ANISOU 1215  CG  TYR A 155     9033   6186   5776   -606   -504    437       C  
ATOM   1216  CD1 TYR A 155      38.063  39.120  34.032  1.00 54.91           C  
ANISOU 1216  CD1 TYR A 155     9083   6085   5694   -575   -594    372       C  
ATOM   1217  CD2 TYR A 155      38.940  37.203  35.124  1.00 56.02           C  
ANISOU 1217  CD2 TYR A 155     8963   6399   5923   -675   -441    481       C  
ATOM   1218  CE1 TYR A 155      38.145  39.828  35.220  1.00 56.17           C  
ANISOU 1218  CE1 TYR A 155     9155   6315   5873   -614   -607    350       C  
ATOM   1219  CE2 TYR A 155      39.023  37.902  36.305  1.00 56.09           C  
ANISOU 1219  CE2 TYR A 155     8895   6474   5942   -717   -454    462       C  
ATOM   1220  CZ  TYR A 155      38.629  39.200  36.354  1.00 56.90           C  
ANISOU 1220  CZ  TYR A 155     9075   6531   6012   -688   -531    396       C  
ATOM   1221  OH  TYR A 155      38.763  39.849  37.561  1.00 62.13           O  
ANISOU 1221  OH  TYR A 155     9654   7266   6688   -734   -538    378       O  
ATOM   1222  N   TYR A 156      41.348  36.121  32.990  1.00 53.23           N  
ANISOU 1222  N   TYR A 156     8754   5928   5542   -744   -234    646       N  
ATOM   1223  CA  TYR A 156      42.604  36.116  33.708  1.00 51.46           C  
ANISOU 1223  CA  TYR A 156     8430   5766   5358   -826   -153    695       C  
ATOM   1224  C   TYR A 156      43.732  36.517  32.807  1.00 50.66           C  
ANISOU 1224  C   TYR A 156     8426   5599   5223   -886    -58    718       C  
ATOM   1225  O   TYR A 156      44.650  37.188  33.245  1.00 51.24           O  
ANISOU 1225  O   TYR A 156     8474   5692   5304   -960     -7    728       O  
ATOM   1226  CB  TYR A 156      42.862  34.749  34.353  1.00 53.15           C  
ANISOU 1226  CB  TYR A 156     8482   6065   5646   -828   -131    729       C  
ATOM   1227  CG  TYR A 156      42.020  34.547  35.588  1.00 54.07           C  
ANISOU 1227  CG  TYR A 156     8498   6263   5785   -820   -199    710       C  
ATOM   1228  CD1 TYR A 156      42.130  35.415  36.671  1.00 58.18           C  
ANISOU 1228  CD1 TYR A 156     8972   6832   6302   -860   -222    699       C  
ATOM   1229  CD2 TYR A 156      41.119  33.524  35.667  1.00 55.67           C  
ANISOU 1229  CD2 TYR A 156     8657   6490   6004   -784   -232    696       C  
ATOM   1230  CE1 TYR A 156      41.353  35.266  37.802  1.00 60.70           C  
ANISOU 1230  CE1 TYR A 156     9208   7227   6630   -868   -271    670       C  
ATOM   1231  CE2 TYR A 156      40.341  33.352  36.783  1.00 59.23           C  
ANISOU 1231  CE2 TYR A 156     9025   7015   6463   -801   -274    666       C  
ATOM   1232  CZ  TYR A 156      40.455  34.224  37.854  1.00 62.47           C  
ANISOU 1232  CZ  TYR A 156     9394   7478   6865   -844   -291    652       C  
ATOM   1233  OH  TYR A 156      39.678  34.031  38.980  1.00 63.85           O  
ANISOU 1233  OH  TYR A 156     9491   7731   7036   -876   -320    615       O  
ATOM   1234  N   ALA A 157      43.669  36.122  31.542  1.00 50.94           N  
ANISOU 1234  N   ALA A 157     8576   5559   5218   -863    -26    718       N  
ATOM   1235  CA  ALA A 157      44.744  36.435  30.614  1.00 49.98           C  
ANISOU 1235  CA  ALA A 157     8557   5379   5055   -941     88    728       C  
ATOM   1236  C   ALA A 157      44.797  37.934  30.457  1.00 52.34           C  
ANISOU 1236  C   ALA A 157     9022   5597   5267   -992     76    715       C  
ATOM   1237  O   ALA A 157      45.859  38.529  30.593  1.00 53.33           O  
ANISOU 1237  O   ALA A 157     9145   5729   5389  -1095    166    719       O  
ATOM   1238  CB  ALA A 157      44.544  35.745  29.297  1.00 49.12           C  
ANISOU 1238  CB  ALA A 157     8557   5200   4905   -908    118    726       C  
ATOM   1239  N   ASN A 158      43.645  38.563  30.239  1.00 54.72           N  
ANISOU 1239  N   ASN A 158     9462   5824   5506   -921    -47    688       N  
ATOM   1240  CA  ASN A 158      43.576  40.018  30.287  1.00 55.30           C  
ANISOU 1240  CA  ASN A 158     9693   5816   5503   -953    -94    671       C  
ATOM   1241  C   ASN A 158      44.221  40.562  31.561  1.00 54.98           C  
ANISOU 1241  C   ASN A 158     9506   5865   5520  -1019    -68    678       C  
ATOM   1242  O   ASN A 158      45.186  41.319  31.482  1.00 63.20           O  
ANISOU 1242  O   ASN A 158    10609   6876   6527  -1125     15    689       O  
ATOM   1243  CB  ASN A 158      42.141  40.511  30.199  1.00 56.50           C  
ANISOU 1243  CB  ASN A 158     9951   5900   5616   -836   -267    618       C  
ATOM   1244  CG  ASN A 158      41.540  40.394  28.808  1.00 59.92           C  
ANISOU 1244  CG  ASN A 158    10604   6200   5962   -775   -319    602       C  
ATOM   1245  OD1 ASN A 158      42.199  40.019  27.821  1.00 61.27           O  
ANISOU 1245  OD1 ASN A 158    10880   6319   6081   -832   -216    637       O  
ATOM   1246  ND2 ASN A 158      40.259  40.751  28.720  1.00 63.86           N  
ANISOU 1246  ND2 ASN A 158    11179   6642   6444   -655   -488    533       N  
ATOM   1247  N   LYS A 159      43.720  40.179  32.726  1.00 53.06           N  
ANISOU 1247  N   LYS A 159     9074   5730   5356   -967   -132    666       N  
ATOM   1248  CA  LYS A 159      44.324  40.621  33.983  1.00 54.71           C  
ANISOU 1248  CA  LYS A 159     9144   6027   5618  -1025   -115    672       C  
ATOM   1249  C   LYS A 159      45.839  40.460  33.998  1.00 55.94           C  
ANISOU 1249  C   LYS A 159     9227   6218   5809  -1132     22    702       C  
ATOM   1250  O   LYS A 159      46.558  41.432  34.234  1.00 60.52           O  
ANISOU 1250  O   LYS A 159     9842   6782   6371  -1216     62    697       O  
ATOM   1251  CB  LYS A 159      43.721  39.937  35.219  1.00 53.37           C  
ANISOU 1251  CB  LYS A 159     8778   5978   5523   -975   -175    663       C  
ATOM   1252  CG  LYS A 159      42.864  40.872  36.089  1.00 55.54           C  
ANISOU 1252  CG  LYS A 159     9048   6268   5785   -943   -281    610       C  
ATOM   1253  CD  LYS A 159      43.099  40.770  37.624  1.00 58.02           C  
ANISOU 1253  CD  LYS A 159     9179   6707   6157   -979   -284    615       C  
ATOM   1254  N   TYR A 160      46.319  39.256  33.757  1.00 53.92           N  
ANISOU 1254  N   TYR A 160     8866   6012   5611  -1129     88    720       N  
ATOM   1255  CA  TYR A 160      47.755  38.993  33.686  1.00 56.44           C  
ANISOU 1255  CA  TYR A 160     9094   6369   5981  -1217    212    720       C  
ATOM   1256  C   TYR A 160      48.445  40.063  32.884  1.00 59.53           C  
ANISOU 1256  C   TYR A 160     9647   6675   6296  -1325    306    701       C  
ATOM   1257  O   TYR A 160      49.404  40.662  33.337  1.00 63.78           O  
ANISOU 1257  O   TYR A 160    10127   7243   6862  -1417    370    682       O  
ATOM   1258  CB  TYR A 160      47.983  37.671  32.973  1.00 56.59           C  
ANISOU 1258  CB  TYR A 160     9062   6401   6040  -1186    265    724       C  
ATOM   1259  CG  TYR A 160      49.353  37.048  33.081  1.00 57.11           C  
ANISOU 1259  CG  TYR A 160     8970   6533   6197  -1241    365    701       C  
ATOM   1260  CD1 TYR A 160      49.850  36.624  34.302  1.00 56.73           C  
ANISOU 1260  CD1 TYR A 160     8727   6579   6247  -1227    324    700       C  
ATOM   1261  CD2 TYR A 160      50.118  36.802  31.940  1.00 57.28           C  
ANISOU 1261  CD2 TYR A 160     9037   6519   6206  -1299    491    666       C  
ATOM   1262  CE1 TYR A 160      51.083  35.979  34.389  1.00 57.84           C  
ANISOU 1262  CE1 TYR A 160     8715   6776   6486  -1255    389    658       C  
ATOM   1263  CE2 TYR A 160      51.354  36.187  32.020  1.00 57.41           C  
ANISOU 1263  CE2 TYR A 160     8887   6603   6323  -1339    577    615       C  
ATOM   1264  CZ  TYR A 160      51.831  35.756  33.240  1.00 58.05           C  
ANISOU 1264  CZ  TYR A 160     8766   6775   6516  -1307    516    608       C  
ATOM   1265  OH  TYR A 160      53.066  35.117  33.319  1.00 58.08           O  
ANISOU 1265  OH  TYR A 160     8595   6840   6632  -1328    576    538       O  
ATOM   1266  N   ASN A 161      47.942  40.305  31.679  1.00 62.54           N  
ANISOU 1266  N   ASN A 161    10245   6942   6575  -1320    311    703       N  
ATOM   1267  CA  ASN A 161      48.530  41.301  30.794  1.00 63.65           C  
ANISOU 1267  CA  ASN A 161    10594   6978   6613  -1438    404    690       C  
ATOM   1268  C   ASN A 161      48.515  42.679  31.417  1.00 61.89           C  
ANISOU 1268  C   ASN A 161    10449   6717   6348  -1487    356    685       C  
ATOM   1269  O   ASN A 161      49.502  43.392  31.335  1.00 65.54           O  
ANISOU 1269  O   ASN A 161    10952   7161   6788  -1622    463    667       O  
ATOM   1270  CB  ASN A 161      47.849  41.309  29.412  1.00 66.01           C  
ANISOU 1270  CB  ASN A 161    11149   7141   6789  -1411    387    698       C  
ATOM   1271  CG  ASN A 161      48.578  40.442  28.392  1.00 70.71           C  
ANISOU 1271  CG  ASN A 161    11747   7738   7381  -1468    533    685       C  
ATOM   1272  OD1 ASN A 161      49.133  39.380  28.717  1.00 70.62           O  
ANISOU 1272  OD1 ASN A 161    11509   7838   7486  -1453    590    672       O  
ATOM   1273  ND2 ASN A 161      48.585  40.898  27.142  1.00 76.44           N  
ANISOU 1273  ND2 ASN A 161    12743   8333   7969  -1535    588    683       N  
ATOM   1274  N   GLY A 162      47.416  43.049  32.064  1.00 59.91           N  
ANISOU 1274  N   GLY A 162    10210   6460   6094  -1384    199    689       N  
ATOM   1275  CA  GLY A 162      47.320  44.371  32.710  1.00 59.85           C  
ANISOU 1275  CA  GLY A 162    10274   6416   6052  -1415    134    677       C  
ATOM   1276  C   GLY A 162      48.396  44.623  33.765  1.00 59.01           C  
ANISOU 1276  C   GLY A 162     9978   6413   6028  -1505    207    669       C  
ATOM   1277  O   GLY A 162      48.884  45.744  33.922  1.00 61.60           O  
ANISOU 1277  O   GLY A 162    10396   6695   6316  -1598    232    657       O  
ATOM   1278  N   VAL A 163      48.758  43.567  34.486  1.00 57.80           N  
ANISOU 1278  N   VAL A 163     9576   6394   5991  -1474    230    673       N  
ATOM   1279  CA  VAL A 163      49.823  43.627  35.447  1.00 57.40           C  
ANISOU 1279  CA  VAL A 163     9337   6443   6030  -1544    285    656       C  
ATOM   1280  C   VAL A 163      51.123  43.976  34.733  1.00 61.69           C  
ANISOU 1280  C   VAL A 163     9921   6956   6561  -1692    449    624       C  
ATOM   1281  O   VAL A 163      51.784  44.958  35.099  1.00 64.89           O  
ANISOU 1281  O   VAL A 163    10340   7353   6960  -1793    490    598       O  
ATOM   1282  CB  VAL A 163      49.991  42.316  36.207  1.00 55.43           C  
ANISOU 1282  CB  VAL A 163     8847   6319   5895  -1477    266    664       C  
ATOM   1283  CG1 VAL A 163      51.268  42.400  37.020  1.00 55.15           C  
ANISOU 1283  CG1 VAL A 163     8636   6369   5951  -1552    322    632       C  
ATOM   1284  CG2 VAL A 163      48.788  42.058  37.109  1.00 51.03           C  
ANISOU 1284  CG2 VAL A 163     8239   5805   5345  -1366    124    685       C  
ATOM   1285  N   PHE A 164      51.460  43.232  33.680  1.00 62.70           N  
ANISOU 1285  N   PHE A 164    10079   7063   6679  -1716    548    614       N  
ATOM   1286  CA  PHE A 164      52.688  43.518  32.919  1.00 65.51           C  
ANISOU 1286  CA  PHE A 164    10474   7397   7021  -1875    727    562       C  
ATOM   1287  C   PHE A 164      52.709  44.909  32.299  1.00 67.02           C  
ANISOU 1287  C   PHE A 164    10939   7455   7072  -1998    772    561       C  
ATOM   1288  O   PHE A 164      53.734  45.570  32.345  1.00 68.52           O  
ANISOU 1288  O   PHE A 164    11119   7650   7267  -2149    890    512       O  
ATOM   1289  CB  PHE A 164      53.006  42.419  31.899  1.00 63.92           C  
ANISOU 1289  CB  PHE A 164    10251   7203   6833  -1876    828    540       C  
ATOM   1290  CG  PHE A 164      53.578  41.210  32.539  1.00 63.90           C  
ANISOU 1290  CG  PHE A 164     9959   7333   6986  -1812    827    508       C  
ATOM   1291  CD1 PHE A 164      52.750  40.215  33.013  1.00 64.54           C  
ANISOU 1291  CD1 PHE A 164     9948   7457   7117  -1658    697    556       C  
ATOM   1292  CD2 PHE A 164      54.935  41.115  32.779  1.00 65.14           C  
ANISOU 1292  CD2 PHE A 164     9933   7570   7245  -1906    940    421       C  
ATOM   1293  CE1 PHE A 164      53.269  39.119  33.680  1.00 65.26           C  
ANISOU 1293  CE1 PHE A 164     9800   7654   7343  -1597    673    533       C  
ATOM   1294  CE2 PHE A 164      55.469  40.028  33.439  1.00 66.85           C  
ANISOU 1294  CE2 PHE A 164     9892   7898   7612  -1830    906    383       C  
ATOM   1295  CZ  PHE A 164      54.635  39.022  33.894  1.00 66.49           C  
ANISOU 1295  CZ  PHE A 164     9784   7879   7602  -1674    766    446       C  
ATOM   1296  N   GLN A 165      51.584  45.364  31.767  1.00 69.75           N  
ANISOU 1296  N   GLN A 165    11529   7676   7295  -1935    667    608       N  
ATOM   1297  CA  GLN A 165      51.516  46.700  31.191  1.00 77.11           C  
ANISOU 1297  CA  GLN A 165    12761   8456   8081  -2038    676    613       C  
ATOM   1298  C   GLN A 165      51.878  47.770  32.221  1.00 79.75           C  
ANISOU 1298  C   GLN A 165    13048   8809   8442  -2098    647    598       C  
ATOM   1299  O   GLN A 165      52.599  48.718  31.933  1.00 80.90           O  
ANISOU 1299  O   GLN A 165    13334   8885   8520  -2261    746    575       O  
ATOM   1300  CB  GLN A 165      50.119  46.983  30.660  1.00 82.24           C  
ANISOU 1300  CB  GLN A 165    13657   8973   8619  -1914    510    653       C  
ATOM   1301  CG  GLN A 165      50.031  48.249  29.813  1.00 87.40           C  
ANISOU 1301  CG  GLN A 165    14682   9431   9095  -2015    505    662       C  
ATOM   1302  CD  GLN A 165      48.605  48.649  29.510  1.00 92.58           C  
ANISOU 1302  CD  GLN A 165    15560   9956   9662  -1863    291    682       C  
ATOM   1303  OE1 GLN A 165      47.649  48.076  30.050  1.00 99.02           O  
ANISOU 1303  OE1 GLN A 165    16226  10840  10558  -1689    152    678       O  
ATOM   1304  NE2 GLN A 165      48.448  49.637  28.638  1.00 98.50           N  
ANISOU 1304  NE2 GLN A 165    16675  10509  10242  -1932    260    692       N  
ATOM   1305  N   GLU A 166      51.365  47.593  33.426  1.00 80.56           N  
ANISOU 1305  N   GLU A 166    12960   9009   8641  -1973    515    607       N  
ATOM   1306  CA  GLU A 166      51.590  48.509  34.516  1.00 81.25           C  
ANISOU 1306  CA  GLU A 166    12981   9127   8763  -2003    467    592       C  
ATOM   1307  C   GLU A 166      53.005  48.352  35.055  1.00 79.81           C  
ANISOU 1307  C   GLU A 166    12575   9059   8689  -2122    605    543       C  
ATOM   1308  O   GLU A 166      53.776  49.293  35.081  1.00 83.23           O  
ANISOU 1308  O   GLU A 166    13070   9457   9097  -2267    687    510       O  
ATOM   1309  CB  GLU A 166      50.568  48.189  35.606  1.00 84.30           C  
ANISOU 1309  CB  GLU A 166    13222   9592   9215  -1834    294    609       C  
ATOM   1310  CG  GLU A 166      50.518  49.153  36.777  1.00 89.42           C  
ANISOU 1310  CG  GLU A 166    13820  10268   9888  -1836    211    593       C  
ATOM   1311  CD  GLU A 166      49.767  48.553  37.962  1.00 90.16           C  
ANISOU 1311  CD  GLU A 166    13708  10482  10065  -1698     88    596       C  
ATOM   1312  OE1 GLU A 166      48.524  48.374  37.859  1.00 85.85           O  
ANISOU 1312  OE1 GLU A 166    13224   9908   9487  -1576    -29    599       O  
ATOM   1313  OE2 GLU A 166      50.428  48.246  38.986  1.00 85.19           O  
ANISOU 1313  OE2 GLU A 166    12862   9975   9532  -1717    110    586       O  
ATOM   1314  N   CYS A 167      53.346  47.149  35.475  1.00 78.01           N  
ANISOU 1314  N   CYS A 167    12090   8963   8585  -2060    623    530       N  
ATOM   1315  CA  CYS A 167      54.547  46.940  36.249  1.00 76.97           C  
ANISOU 1315  CA  CYS A 167    11710   8952   8582  -2124    696    471       C  
ATOM   1316  C   CYS A 167      55.863  46.969  35.475  1.00 79.51           C  
ANISOU 1316  C   CYS A 167    12011   9276   8921  -2295    898    391       C  
ATOM   1317  O   CYS A 167      56.891  47.244  36.077  1.00 82.70           O  
ANISOU 1317  O   CYS A 167    12253   9754   9415  -2381    959    320       O  
ATOM   1318  CB  CYS A 167      54.457  45.620  37.007  1.00 78.92           C  
ANISOU 1318  CB  CYS A 167    11707   9325   8953  -1989    621    479       C  
ATOM   1319  SG  CYS A 167      53.374  45.653  38.453  1.00 81.97           S  
ANISOU 1319  SG  CYS A 167    12020   9767   9360  -1844    418    533       S  
ATOM   1320  N   CYS A 168      55.882  46.675  34.175  1.00 80.37           N  
ANISOU 1320  N   CYS A 168    12269   9314   8952  -2351   1006    387       N  
ATOM   1321  CA  CYS A 168      57.175  46.671  33.452  1.00 83.68           C  
ANISOU 1321  CA  CYS A 168    12651   9751   9391  -2532   1221    287       C  
ATOM   1322  C   CYS A 168      57.768  48.088  33.279  1.00 87.09           C  
ANISOU 1322  C   CYS A 168    13248  10103   9738  -2735   1327    249       C  
ATOM   1323  O   CYS A 168      58.946  48.236  32.945  1.00 89.61           O  
ANISOU 1323  O   CYS A 168    13497  10459  10094  -2909   1512    143       O  
ATOM   1324  CB  CYS A 168      57.100  45.947  32.097  1.00 84.74           C  
ANISOU 1324  CB  CYS A 168    12901   9837   9459  -2554   1326    282       C  
ATOM   1325  SG  CYS A 168      56.666  44.176  32.171  1.00 84.10           S  
ANISOU 1325  SG  CYS A 168    12609   9853   9493  -2349   1239    303       S  
ATOM   1326  N   GLN A 169      56.951  49.116  33.510  1.00 86.62           N  
ANISOU 1326  N   GLN A 169    13406   9935   9569  -2714   1209    323       N  
ATOM   1327  CA  GLN A 169      57.403  50.506  33.509  1.00 88.28           C  
ANISOU 1327  CA  GLN A 169    13787  10058   9697  -2890   1273    299       C  
ATOM   1328  C   GLN A 169      58.240  50.842  34.755  1.00 87.85           C  
ANISOU 1328  C   GLN A 169    13472  10124   9785  -2926   1274    232       C  
ATOM   1329  O   GLN A 169      59.224  51.568  34.672  1.00 88.46           O  
ANISOU 1329  O   GLN A 169    13557  10193   9860  -3120   1417    152       O  
ATOM   1330  CB  GLN A 169      56.187  51.440  33.441  1.00 88.49           C  
ANISOU 1330  CB  GLN A 169    14118   9928   9576  -2820   1108    392       C  
ATOM   1331  N   ALA A 170      57.848  50.273  35.891  1.00 84.97           N  
ANISOU 1331  N   ALA A 170    12880   9867   9537  -2746   1117    258       N  
ATOM   1332  CA  ALA A 170      58.382  50.606  37.206  1.00 83.59           C  
ANISOU 1332  CA  ALA A 170    12486   9792   9481  -2740   1061    215       C  
ATOM   1333  C   ALA A 170      59.897  50.408  37.373  1.00 83.37           C  
ANISOU 1333  C   ALA A 170    12216   9873   9589  -2872   1215     80       C  
ATOM   1334  O   ALA A 170      60.539  49.778  36.547  1.00 82.92           O  
ANISOU 1334  O   ALA A 170    12104   9843   9560  -2945   1362     10       O  
ATOM   1335  CB  ALA A 170      57.630  49.796  38.257  1.00 80.90           C  
ANISOU 1335  CB  ALA A 170    11971   9545   9225  -2523    873    271       C  
ATOM   1336  N   GLU A 171      60.447  50.938  38.470  1.00 84.86           N  
ANISOU 1336  N   GLU A 171    12248  10129   9867  -2894   1172     30       N  
ATOM   1337  CA  GLU A 171      61.898  50.898  38.727  1.00 84.78           C  
ANISOU 1337  CA  GLU A 171    11995  10221   9997  -3019   1300   -122       C  
ATOM   1338  C   GLU A 171      62.352  49.492  39.098  1.00 82.92           C  
ANISOU 1338  C   GLU A 171    11457  10122   9928  -2889   1260   -182       C  
ATOM   1339  O   GLU A 171      63.314  48.969  38.539  1.00 83.22           O  
ANISOU 1339  O   GLU A 171    11352  10216  10051  -2972   1404   -308       O  
ATOM   1340  CB  GLU A 171      62.269  51.875  39.846  1.00 84.64           C  
ANISOU 1340  CB  GLU A 171    11905  10229  10027  -3061   1237   -154       C  
ATOM   1341  N   ASP A 172      61.657  48.896  40.061  1.00 79.76           N  
ANISOU 1341  N   ASP A 172    10966   9769   9570  -2690   1061   -102       N  
ATOM   1342  CA  ASP A 172      61.855  47.498  40.408  1.00 77.79           C  
ANISOU 1342  CA  ASP A 172    10489   9619   9449  -2543    986   -128       C  
ATOM   1343  C   ASP A 172      60.666  46.679  39.881  1.00 74.89           C  
ANISOU 1343  C   ASP A 172    10256   9203   8996  -2411    917     -5       C  
ATOM   1344  O   ASP A 172      59.674  46.462  40.589  1.00 71.56           O  
ANISOU 1344  O   ASP A 172     9870   8780   8540  -2271    754    100       O  
ATOM   1345  CB  ASP A 172      62.032  47.342  41.925  1.00 78.44           C  
ANISOU 1345  CB  ASP A 172    10378   9788   9639  -2432    813   -137       C  
ATOM   1346  CG  ASP A 172      62.445  45.924  42.336  1.00 82.31           C  
ANISOU 1346  CG  ASP A 172    10637  10369  10270  -2293    724   -185       C  
ATOM   1347  OD1 ASP A 172      62.201  44.959  41.569  1.00 83.22           O  
ANISOU 1347  OD1 ASP A 172    10765  10474  10380  -2236    753   -167       O  
ATOM   1348  OD2 ASP A 172      63.005  45.771  43.442  1.00 83.50           O  
ANISOU 1348  OD2 ASP A 172    10605  10591  10531  -2234    611   -241       O  
ATOM   1349  N   LYS A 173      60.793  46.254  38.623  1.00 73.57           N  
ANISOU 1349  N   LYS A 173    10162   8999   8792  -2469   1054    -30       N  
ATOM   1350  CA  LYS A 173      59.871  45.341  37.965  1.00 70.40           C  
ANISOU 1350  CA  LYS A 173     9858   8560   8330  -2355   1014     57       C  
ATOM   1351  C   LYS A 173      59.336  44.262  38.923  1.00 70.55           C  
ANISOU 1351  C   LYS A 173     9734   8647   8426  -2157    827    116       C  
ATOM   1352  O   LYS A 173      58.120  44.106  39.118  1.00 66.41           O  
ANISOU 1352  O   LYS A 173     9328   8084   7821  -2049    710    231       O  
ATOM   1353  CB  LYS A 173      60.595  44.647  36.798  1.00 71.83           C  
ANISOU 1353  CB  LYS A 173     9993   8753   8544  -2428   1181    -37       C  
ATOM   1354  CG  LYS A 173      60.922  45.521  35.592  1.00 73.48           C  
ANISOU 1354  CG  LYS A 173    10409   8875   8636  -2634   1385    -78       C  
ATOM   1355  N   GLY A 174      60.259  43.520  39.528  1.00 73.03           N  
ANISOU 1355  N   GLY A 174     9797   9058   8894  -2114    796     25       N  
ATOM   1356  CA  GLY A 174      59.907  42.363  40.351  1.00 73.74           C  
ANISOU 1356  CA  GLY A 174     9766   9200   9053  -1940    626     70       C  
ATOM   1357  C   GLY A 174      59.059  42.699  41.560  1.00 73.32           C  
ANISOU 1357  C   GLY A 174     9758   9149   8951  -1860    461    171       C  
ATOM   1358  O   GLY A 174      58.069  42.029  41.839  1.00 72.94           O  
ANISOU 1358  O   GLY A 174     9765   9092   8858  -1747    351    267       O  
ATOM   1359  N   ALA A 175      59.436  43.754  42.274  1.00 74.33           N  
ANISOU 1359  N   ALA A 175     9866   9292   9086  -1930    451    140       N  
ATOM   1360  CA  ALA A 175      58.719  44.146  43.484  1.00 73.48           C  
ANISOU 1360  CA  ALA A 175     9790   9195   8935  -1866    303    217       C  
ATOM   1361  C   ALA A 175      57.247  44.454  43.189  1.00 71.68           C  
ANISOU 1361  C   ALA A 175     9775   8898   8564  -1829    270    332       C  
ATOM   1362  O   ALA A 175      56.363  44.158  44.004  1.00 65.60           O  
ANISOU 1362  O   ALA A 175     9021   8147   7759  -1736    142    402       O  
ATOM   1363  CB  ALA A 175      59.405  45.351  44.112  1.00 73.37           C  
ANISOU 1363  CB  ALA A 175     9734   9197   8945  -1965    321    154       C  
ATOM   1364  N   CYS A 176      57.009  45.022  42.000  1.00 74.15           N  
ANISOU 1364  N   CYS A 176    10252   9129   8793  -1907    385    338       N  
ATOM   1365  CA  CYS A 176      55.678  45.420  41.542  1.00 75.13           C  
ANISOU 1365  CA  CYS A 176    10590   9170   8785  -1873    351    422       C  
ATOM   1366  C   CYS A 176      54.806  44.216  41.195  1.00 71.62           C  
ANISOU 1366  C   CYS A 176    10161   8726   8324  -1756    299    480       C  
ATOM   1367  O   CYS A 176      53.679  44.108  41.680  1.00 69.42           O  
ANISOU 1367  O   CYS A 176     9934   8447   7995  -1669    191    539       O  
ATOM   1368  CB  CYS A 176      55.787  46.344  40.314  1.00 80.58           C  
ANISOU 1368  CB  CYS A 176    11477   9755   9385  -1994    479    405       C  
ATOM   1369  SG  CYS A 176      54.238  47.079  39.692  1.00 90.29           S  
ANISOU 1369  SG  CYS A 176    13001  10856  10451  -1951    411    484       S  
ATOM   1370  N   LEU A 177      55.333  43.313  40.372  1.00 69.39           N  
ANISOU 1370  N   LEU A 177     9827   8450   8089  -1758    379    452       N  
ATOM   1371  CA  LEU A 177      54.501  42.275  39.751  1.00 68.06           C  
ANISOU 1371  CA  LEU A 177     9711   8258   7889  -1665    353    504       C  
ATOM   1372  C   LEU A 177      54.470  40.939  40.475  1.00 67.77           C  
ANISOU 1372  C   LEU A 177     9522   8294   7935  -1557    257    522       C  
ATOM   1373  O   LEU A 177      53.443  40.239  40.438  1.00 66.10           O  
ANISOU 1373  O   LEU A 177     9362   8070   7682  -1471    189    583       O  
ATOM   1374  CB  LEU A 177      54.878  42.070  38.281  1.00 66.21           C  
ANISOU 1374  CB  LEU A 177     9558   7968   7631  -1727    494    472       C  
ATOM   1375  CG  LEU A 177      56.264  41.549  37.939  1.00 69.25           C  
ANISOU 1375  CG  LEU A 177     9783   8405   8125  -1788    606    373       C  
ATOM   1376  CD1 LEU A 177      56.288  40.024  37.945  1.00 69.04           C  
ANISOU 1376  CD1 LEU A 177     9625   8425   8181  -1675    554    373       C  
ATOM   1377  CD2 LEU A 177      56.700  42.133  36.591  1.00 70.64           C  
ANISOU 1377  CD2 LEU A 177    10098   8511   8232  -1926    783    326       C  
ATOM   1378  N   LEU A 178      55.571  40.568  41.126  1.00 68.70           N  
ANISOU 1378  N   LEU A 178     9460   8479   8165  -1562    243    461       N  
ATOM   1379  CA  LEU A 178      55.629  39.238  41.744  1.00 67.66           C  
ANISOU 1379  CA  LEU A 178     9209   8393   8105  -1458    138    475       C  
ATOM   1380  C   LEU A 178      54.490  39.011  42.736  1.00 65.34           C  
ANISOU 1380  C   LEU A 178     8968   8110   7748  -1386      3    563       C  
ATOM   1381  O   LEU A 178      53.853  37.979  42.688  1.00 62.66           O  
ANISOU 1381  O   LEU A 178     8649   7764   7395  -1313    -50    611       O  
ATOM   1382  CB  LEU A 178      56.990  38.950  42.380  1.00 69.52           C  
ANISOU 1382  CB  LEU A 178     9250   8690   8475  -1459    110    382       C  
ATOM   1383  CG  LEU A 178      58.092  38.591  41.380  1.00 70.30           C  
ANISOU 1383  CG  LEU A 178     9248   8796   8666  -1500    231    271       C  
ATOM   1384  CD1 LEU A 178      59.435  38.486  42.088  1.00 70.42           C  
ANISOU 1384  CD1 LEU A 178     9055   8876   8827  -1501    192    150       C  
ATOM   1385  CD2 LEU A 178      57.773  37.283  40.675  1.00 68.15           C  
ANISOU 1385  CD2 LEU A 178     8984   8504   8407  -1416    223    292       C  
ATOM   1386  N   PRO A 179      54.192  40.001  43.605  1.00 68.74           N  
ANISOU 1386  N   PRO A 179     9429   8556   8135  -1417    -41    577       N  
ATOM   1387  CA  PRO A 179      53.017  39.849  44.496  1.00 66.23           C  
ANISOU 1387  CA  PRO A 179     9166   8253   7744  -1367   -147    644       C  
ATOM   1388  C   PRO A 179      51.723  39.768  43.711  1.00 63.14           C  
ANISOU 1388  C   PRO A 179     8908   7814   7267  -1340   -126    687       C  
ATOM   1389  O   PRO A 179      50.846  38.979  44.043  1.00 64.52           O  
ANISOU 1389  O   PRO A 179     9102   8002   7411  -1286   -188    728       O  
ATOM   1390  CB  PRO A 179      53.032  41.117  45.354  1.00 63.67           C  
ANISOU 1390  CB  PRO A 179     8851   7950   7392  -1418   -173    628       C  
ATOM   1391  CG  PRO A 179      54.410  41.653  45.220  1.00 67.34           C  
ANISOU 1391  CG  PRO A 179     9225   8423   7937  -1483   -112    557       C  
ATOM   1392  CD  PRO A 179      54.869  41.288  43.832  1.00 67.89           C  
ANISOU 1392  CD  PRO A 179     9305   8453   8037  -1506      5    525       C  
ATOM   1393  N   LYS A 180      51.616  40.567  42.666  1.00 61.96           N  
ANISOU 1393  N   LYS A 180     8859   7606   7078  -1380    -41    669       N  
ATOM   1394  CA  LYS A 180      50.388  40.596  41.886  1.00 60.80           C  
ANISOU 1394  CA  LYS A 180     8848   7402   6850  -1344    -41    695       C  
ATOM   1395  C   LYS A 180      50.084  39.287  41.142  1.00 58.09           C  
ANISOU 1395  C   LYS A 180     8506   7045   6521  -1285    -29    720       C  
ATOM   1396  O   LYS A 180      48.937  38.890  41.085  1.00 57.62           O  
ANISOU 1396  O   LYS A 180     8502   6977   6416  -1232    -76    744       O  
ATOM   1397  CB  LYS A 180      50.391  41.774  40.914  1.00 60.97           C  
ANISOU 1397  CB  LYS A 180     9012   7341   6813  -1400     29    673       C  
ATOM   1398  CG  LYS A 180      50.164  43.121  41.571  1.00 59.88           C  
ANISOU 1398  CG  LYS A 180     8925   7194   6633  -1436    -12    655       C  
ATOM   1399  CD  LYS A 180      50.158  44.223  40.509  1.00 62.67           C  
ANISOU 1399  CD  LYS A 180     9459   7439   6913  -1493     45    638       C  
ATOM   1400  CE  LYS A 180      50.656  45.563  41.038  1.00 63.27           C  
ANISOU 1400  CE  LYS A 180     9562   7500   6976  -1572     47    609       C  
ATOM   1401  NZ  LYS A 180      49.609  46.188  41.900  1.00 61.73           N  
ANISOU 1401  NZ  LYS A 180     9394   7316   6743  -1514    -72    605       N  
ATOM   1402  N   ILE A 181      51.085  38.612  40.592  1.00 58.56           N  
ANISOU 1402  N   ILE A 181     8497   7105   6647  -1295     33    700       N  
ATOM   1403  CA  ILE A 181      50.813  37.336  39.921  1.00 60.58           C  
ANISOU 1403  CA  ILE A 181     8750   7346   6919  -1235     37    720       C  
ATOM   1404  C   ILE A 181      50.672  36.179  40.916  1.00 62.67           C  
ANISOU 1404  C   ILE A 181     8924   7661   7225  -1175    -63    752       C  
ATOM   1405  O   ILE A 181      50.027  35.195  40.599  1.00 66.51           O  
ANISOU 1405  O   ILE A 181     9437   8133   7700  -1122    -88    782       O  
ATOM   1406  CB  ILE A 181      51.819  36.980  38.781  1.00 63.47           C  
ANISOU 1406  CB  ILE A 181     9092   7688   7336  -1263    147    674       C  
ATOM   1407  CG1 ILE A 181      53.221  36.659  39.333  1.00 66.22           C  
ANISOU 1407  CG1 ILE A 181     9268   8094   7799  -1281    153    615       C  
ATOM   1408  CG2 ILE A 181      51.867  38.078  37.712  1.00 60.90           C  
ANISOU 1408  CG2 ILE A 181     8906   7296   6939  -1341    254    650       C  
ATOM   1409  CD1 ILE A 181      54.316  36.575  38.269  1.00 67.21           C  
ANISOU 1409  CD1 ILE A 181     9346   8209   7980  -1336    284    532       C  
ATOM   1410  N   GLU A 182      51.263  36.287  42.109  1.00 65.02           N  
ANISOU 1410  N   GLU A 182     9131   8010   7563  -1187   -126    745       N  
ATOM   1411  CA  GLU A 182      51.087  35.279  43.157  1.00 65.72           C  
ANISOU 1411  CA  GLU A 182     9176   8131   7665  -1142   -236    782       C  
ATOM   1412  C   GLU A 182      49.646  35.328  43.662  1.00 66.33           C  
ANISOU 1412  C   GLU A 182     9339   8215   7647  -1140   -280    826       C  
ATOM   1413  O   GLU A 182      49.016  34.287  43.859  1.00 65.50           O  
ANISOU 1413  O   GLU A 182     9258   8107   7521  -1109   -326    862       O  
ATOM   1414  CB  GLU A 182      52.066  35.502  44.321  1.00 68.43           C  
ANISOU 1414  CB  GLU A 182     9422   8517   8061  -1157   -304    757       C  
ATOM   1415  CG  GLU A 182      52.330  34.299  45.223  1.00 69.56           C  
ANISOU 1415  CG  GLU A 182     9527   8668   8234  -1106   -427    783       C  
ATOM   1416  N   THR A 183      49.118  36.537  43.828  1.00 64.29           N  
ANISOU 1416  N   THR A 183     9128   7965   7336  -1176   -262    810       N  
ATOM   1417  CA  THR A 183      47.721  36.714  44.200  1.00 63.85           C  
ANISOU 1417  CA  THR A 183     9137   7923   7202  -1174   -293    818       C  
ATOM   1418  C   THR A 183      46.789  36.163  43.150  1.00 62.11           C  
ANISOU 1418  C   THR A 183     8982   7660   6955  -1133   -266    820       C  
ATOM   1419  O   THR A 183      45.925  35.350  43.450  1.00 62.53           O  
ANISOU 1419  O   THR A 183     9047   7730   6981  -1119   -299    835       O  
ATOM   1420  CB  THR A 183      47.396  38.193  44.448  1.00 64.64           C  
ANISOU 1420  CB  THR A 183     9270   8028   7260  -1207   -288    780       C  
ATOM   1421  OG1 THR A 183      47.921  38.553  45.737  1.00 66.37           O  
ANISOU 1421  OG1 THR A 183     9429   8301   7487  -1243   -335    779       O  
ATOM   1422  CG2 THR A 183      45.879  38.444  44.438  1.00 61.58           C  
ANISOU 1422  CG2 THR A 183     8946   7644   6808  -1188   -310    753       C  
ATOM   1423  N   MET A 184      46.968  36.594  41.917  1.00 60.72           N  
ANISOU 1423  N   MET A 184     8860   7427   6784  -1123   -204    803       N  
ATOM   1424  CA  MET A 184      46.124  36.108  40.849  1.00 61.95           C  
ANISOU 1424  CA  MET A 184     9089   7536   6914  -1078   -186    801       C  
ATOM   1425  C   MET A 184      46.245  34.582  40.734  1.00 62.20           C  
ANISOU 1425  C   MET A 184     9078   7571   6983  -1046   -195    835       C  
ATOM   1426  O   MET A 184      45.235  33.876  40.638  1.00 59.80           O  
ANISOU 1426  O   MET A 184     8802   7266   6654  -1018   -220    841       O  
ATOM   1427  CB  MET A 184      46.477  36.792  39.525  1.00 62.62           C  
ANISOU 1427  CB  MET A 184     9262   7546   6985  -1083   -117    781       C  
ATOM   1428  CG  MET A 184      45.808  36.128  38.333  1.00 68.22           C  
ANISOU 1428  CG  MET A 184    10049   8199   7673  -1031   -101    782       C  
ATOM   1429  SD  MET A 184      45.809  37.059  36.790  1.00 66.32           S  
ANISOU 1429  SD  MET A 184     9979   7850   7371  -1038    -44    757       S  
ATOM   1430  CE  MET A 184      47.395  37.870  36.906  1.00 68.54           C  
ANISOU 1430  CE  MET A 184    10227   8136   7678  -1135     43    750       C  
ATOM   1431  N   ARG A 185      47.476  34.071  40.761  1.00 62.66           N  
ANISOU 1431  N   ARG A 185     9066   7635   7108  -1049   -180    847       N  
ATOM   1432  CA  ARG A 185      47.709  32.635  40.601  1.00 60.67           C  
ANISOU 1432  CA  ARG A 185     8780   7373   6899  -1008   -203    871       C  
ATOM   1433  C   ARG A 185      46.910  31.824  41.594  1.00 60.27           C  
ANISOU 1433  C   ARG A 185     8737   7348   6815  -1006   -281    908       C  
ATOM   1434  O   ARG A 185      46.483  30.722  41.270  1.00 65.56           O  
ANISOU 1434  O   ARG A 185     9430   7994   7486   -976   -297    929       O  
ATOM   1435  CB  ARG A 185      49.191  32.283  40.697  1.00 60.19           C  
ANISOU 1435  CB  ARG A 185     8623   7320   6927  -1004   -201    853       C  
ATOM   1436  CG  ARG A 185      49.445  30.785  40.716  1.00 61.81           C  
ANISOU 1436  CG  ARG A 185     8795   7509   7181   -949   -257    872       C  
ATOM   1437  CD  ARG A 185      50.908  30.401  40.488  1.00 64.37           C  
ANISOU 1437  CD  ARG A 185     9012   7833   7612   -924   -252    820       C  
ATOM   1438  NE  ARG A 185      51.118  28.947  40.585  1.00 67.99           N  
ANISOU 1438  NE  ARG A 185     9449   8265   8120   -858   -335    833       N  
ATOM   1439  N   GLU A 186      46.700  32.342  42.796  1.00 58.88           N  
ANISOU 1439  N   GLU A 186     8551   7218   6603  -1048   -326    912       N  
ATOM   1440  CA  GLU A 186      45.872  31.628  43.772  1.00 58.22           C  
ANISOU 1440  CA  GLU A 186     8496   7160   6466  -1074   -383    940       C  
ATOM   1441  C   GLU A 186      44.401  31.653  43.369  1.00 55.01           C  
ANISOU 1441  C   GLU A 186     8141   6757   6005  -1079   -354    913       C  
ATOM   1442  O   GLU A 186      43.684  30.653  43.509  1.00 51.61           O  
ANISOU 1442  O   GLU A 186     7740   6322   5547  -1090   -370    928       O  
ATOM   1443  CB  GLU A 186      46.037  32.200  45.179  1.00 62.24           C  
ANISOU 1443  CB  GLU A 186     8989   7720   6941  -1128   -431    943       C  
ATOM   1444  CG  GLU A 186      47.403  31.927  45.801  1.00 70.69           C  
ANISOU 1444  CG  GLU A 186    10009   8786   8065  -1117   -494    964       C  
ATOM   1445  CD  GLU A 186      47.508  30.556  46.462  1.00 82.44           C  
ANISOU 1445  CD  GLU A 186    11537  10247   9538  -1111   -582   1013       C  
ATOM   1446  OE1 GLU A 186      48.110  30.456  47.565  1.00 91.13           O  
ANISOU 1446  OE1 GLU A 186    12641  11355  10630  -1127   -669   1031       O  
ATOM   1447  OE2 GLU A 186      46.979  29.574  45.892  1.00 88.33           O  
ANISOU 1447  OE2 GLU A 186    12327  10957  10277  -1091   -575   1034       O  
ATOM   1448  N   LYS A 187      43.940  32.782  42.849  1.00 53.78           N  
ANISOU 1448  N   LYS A 187     7999   6600   5834  -1071   -319    863       N  
ATOM   1449  CA  LYS A 187      42.559  32.847  42.404  1.00 55.28           C  
ANISOU 1449  CA  LYS A 187     8227   6790   5987  -1058   -309    812       C  
ATOM   1450  C   LYS A 187      42.345  31.855  41.238  1.00 52.26           C  
ANISOU 1450  C   LYS A 187     7876   6353   5627  -1007   -290    825       C  
ATOM   1451  O   LYS A 187      41.314  31.163  41.177  1.00 53.34           O  
ANISOU 1451  O   LYS A 187     8027   6496   5745  -1008   -297    803       O  
ATOM   1452  CB  LYS A 187      42.157  34.268  42.045  1.00 59.23           C  
ANISOU 1452  CB  LYS A 187     8753   7282   6469  -1042   -304    749       C  
ATOM   1453  CG  LYS A 187      42.213  35.214  43.238  1.00 64.19           C  
ANISOU 1453  CG  LYS A 187     9347   7968   7074  -1091   -327    726       C  
ATOM   1454  CD  LYS A 187      41.631  36.591  42.906  1.00 71.75           C  
ANISOU 1454  CD  LYS A 187    10342   8909   8012  -1067   -341    650       C  
ATOM   1455  CE  LYS A 187      42.483  37.779  43.390  1.00 78.73           C  
ANISOU 1455  CE  LYS A 187    11221   9797   8897  -1096   -345    654       C  
ATOM   1456  NZ  LYS A 187      43.259  38.473  42.299  1.00 84.14           N  
ANISOU 1456  NZ  LYS A 187    11976  10400   9595  -1076   -314    669       N  
ATOM   1457  N   VAL A 188      43.343  31.731  40.374  1.00 46.65           N  
ANISOU 1457  N   VAL A 188     7171   5594   4960   -972   -261    853       N  
ATOM   1458  CA  VAL A 188      43.245  30.843  39.235  1.00 45.48           C  
ANISOU 1458  CA  VAL A 188     7054   5393   4832   -922   -239    862       C  
ATOM   1459  C   VAL A 188      43.195  29.392  39.690  1.00 46.48           C  
ANISOU 1459  C   VAL A 188     7161   5524   4974   -927   -272    903       C  
ATOM   1460  O   VAL A 188      42.267  28.648  39.334  1.00 44.82           O  
ANISOU 1460  O   VAL A 188     6981   5300   4748   -914   -277    893       O  
ATOM   1461  CB  VAL A 188      44.389  31.080  38.240  1.00 44.52           C  
ANISOU 1461  CB  VAL A 188     6940   5226   4750   -900   -186    867       C  
ATOM   1462  CG1 VAL A 188      44.402  29.985  37.190  1.00 43.09           C  
ANISOU 1462  CG1 VAL A 188     6781   4998   4594   -852   -165    877       C  
ATOM   1463  CG2 VAL A 188      44.251  32.471  37.608  1.00 44.78           C  
ANISOU 1463  CG2 VAL A 188     7042   5229   4744   -905   -153    829       C  
ATOM   1464  N   LEU A 189      44.161  28.980  40.502  1.00 47.09           N  
ANISOU 1464  N   LEU A 189     7198   5615   5080   -945   -307    944       N  
ATOM   1465  CA  LEU A 189      44.082  27.632  41.048  1.00 48.97           C  
ANISOU 1465  CA  LEU A 189     7451   5841   5316   -953   -360    987       C  
ATOM   1466  C   LEU A 189      42.708  27.310  41.696  1.00 47.27           C  
ANISOU 1466  C   LEU A 189     7279   5653   5028  -1014   -370    978       C  
ATOM   1467  O   LEU A 189      42.137  26.277  41.420  1.00 49.20           O  
ANISOU 1467  O   LEU A 189     7561   5869   5264  -1014   -375    988       O  
ATOM   1468  CB  LEU A 189      45.233  27.366  42.007  1.00 50.86           C  
ANISOU 1468  CB  LEU A 189     7658   6083   5583   -961   -426   1022       C  
ATOM   1469  CG  LEU A 189      46.643  27.309  41.371  1.00 52.40           C  
ANISOU 1469  CG  LEU A 189     7787   6252   5871   -901   -421   1008       C  
ATOM   1470  CD1 LEU A 189      47.601  26.912  42.479  1.00 52.79           C  
ANISOU 1470  CD1 LEU A 189     7807   6302   5950   -900   -520   1028       C  
ATOM   1471  CD2 LEU A 189      46.809  26.391  40.146  1.00 50.40           C  
ANISOU 1471  CD2 LEU A 189     7535   5946   5667   -838   -396    999       C  
ATOM   1472  N   THR A 190      42.144  28.207  42.483  1.00 47.81           N  
ANISOU 1472  N   THR A 190     7339   5779   5048  -1070   -362    945       N  
ATOM   1473  CA  THR A 190      40.804  27.968  43.051  1.00 50.51           C  
ANISOU 1473  CA  THR A 190     7704   6160   5326  -1140   -351    905       C  
ATOM   1474  C   THR A 190      39.748  27.753  41.968  1.00 51.19           C  
ANISOU 1474  C   THR A 190     7796   6229   5424  -1103   -317    846       C  
ATOM   1475  O   THR A 190      39.029  26.752  41.956  1.00 53.71           O  
ANISOU 1475  O   THR A 190     8141   6540   5724  -1136   -311    840       O  
ATOM   1476  CB  THR A 190      40.340  29.150  43.912  1.00 51.05           C  
ANISOU 1476  CB  THR A 190     7743   6300   5352  -1194   -340    849       C  
ATOM   1477  OG1 THR A 190      41.273  29.345  44.975  1.00 54.15           O  
ANISOU 1477  OG1 THR A 190     8136   6709   5729  -1231   -378    900       O  
ATOM   1478  CG2 THR A 190      38.936  28.925  44.485  1.00 49.77           C  
ANISOU 1478  CG2 THR A 190     7586   6192   5132  -1277   -313    777       C  
ATOM   1479  N   SER A 191      39.698  28.692  41.037  1.00 50.88           N  
ANISOU 1479  N   SER A 191     7744   6176   5412  -1035   -300    800       N  
ATOM   1480  CA  SER A 191      38.833  28.612  39.855  1.00 49.70           C  
ANISOU 1480  CA  SER A 191     7613   5993   5277   -976   -288    740       C  
ATOM   1481  C   SER A 191      38.876  27.231  39.177  1.00 51.21           C  
ANISOU 1481  C   SER A 191     7833   6134   5492   -951   -285    782       C  
ATOM   1482  O   SER A 191      37.853  26.633  38.858  1.00 53.02           O  
ANISOU 1482  O   SER A 191     8068   6361   5715   -955   -281    734       O  
ATOM   1483  CB  SER A 191      39.306  29.688  38.865  1.00 48.17           C  
ANISOU 1483  CB  SER A 191     7446   5757   5102   -904   -283    726       C  
ATOM   1484  OG  SER A 191      38.425  29.828  37.794  1.00 49.73           O  
ANISOU 1484  OG  SER A 191     7682   5915   5299   -842   -291    659       O  
ATOM   1485  N   SER A 192      40.092  26.751  38.937  1.00 50.66           N  
ANISOU 1485  N   SER A 192     7771   6023   5455   -922   -290    858       N  
ATOM   1486  CA  SER A 192      40.334  25.503  38.252  1.00 48.50           C  
ANISOU 1486  CA  SER A 192     7522   5693   5213   -885   -295    895       C  
ATOM   1487  C   SER A 192      39.537  24.455  38.941  1.00 50.12           C  
ANISOU 1487  C   SER A 192     7748   5908   5386   -951   -313    901       C  
ATOM   1488  O   SER A 192      38.807  23.697  38.321  1.00 51.95           O  
ANISOU 1488  O   SER A 192     8004   6114   5623   -938   -306    878       O  
ATOM   1489  CB  SER A 192      41.814  25.175  38.368  1.00 49.19           C  
ANISOU 1489  CB  SER A 192     7591   5755   5344   -861   -313    957       C  
ATOM   1490  OG  SER A 192      42.186  24.131  37.530  1.00 50.05           O  
ANISOU 1490  OG  SER A 192     7714   5807   5496   -807   -317    976       O  
ATOM   1491  N   ALA A 193      39.661  24.452  40.261  1.00 51.95           N  
ANISOU 1491  N   ALA A 193     7984   6177   5577  -1032   -335    929       N  
ATOM   1492  CA  ALA A 193      39.131  23.400  41.090  1.00 52.10           C  
ANISOU 1492  CA  ALA A 193     8056   6194   5546  -1121   -352    952       C  
ATOM   1493  C   ALA A 193      37.634  23.529  41.114  1.00 52.65           C  
ANISOU 1493  C   ALA A 193     8111   6313   5580  -1184   -303    859       C  
ATOM   1494  O   ALA A 193      36.921  22.555  41.102  1.00 56.70           O  
ANISOU 1494  O   ALA A 193     8661   6809   6072  -1236   -291    847       O  
ATOM   1495  CB  ALA A 193      39.712  23.507  42.494  1.00 51.40           C  
ANISOU 1495  CB  ALA A 193     7996   6127   5409  -1195   -391   1003       C  
ATOM   1496  N   ARG A 194      37.161  24.756  41.108  1.00 54.10           N  
ANISOU 1496  N   ARG A 194     8237   6555   5765  -1174   -278    780       N  
ATOM   1497  CA  ARG A 194      35.741  25.023  41.207  1.00 54.40           C  
ANISOU 1497  CA  ARG A 194     8235   6651   5782  -1225   -241    658       C  
ATOM   1498  C   ARG A 194      35.007  24.448  40.015  1.00 51.32           C  
ANISOU 1498  C   ARG A 194     7842   6223   5433  -1166   -236    603       C  
ATOM   1499  O   ARG A 194      33.921  23.893  40.160  1.00 53.27           O  
ANISOU 1499  O   ARG A 194     8075   6499   5667  -1235   -206    525       O  
ATOM   1500  CB  ARG A 194      35.549  26.528  41.333  1.00 57.56           C  
ANISOU 1500  CB  ARG A 194     8577   7105   6189  -1195   -242    580       C  
ATOM   1501  CG  ARG A 194      34.172  27.007  41.765  1.00 59.83           C  
ANISOU 1501  CG  ARG A 194     8800   7473   6460  -1254   -214    429       C  
ATOM   1502  CD  ARG A 194      34.288  28.351  42.500  1.00 57.65           C  
ANISOU 1502  CD  ARG A 194     8482   7255   6167  -1263   -222    384       C  
ATOM   1503  NE  ARG A 194      34.538  28.154  43.927  1.00 59.12           N  
ANISOU 1503  NE  ARG A 194     8684   7494   6286  -1393   -195    426       N  
ATOM   1504  CZ  ARG A 194      35.037  29.060  44.755  1.00 61.08           C  
ANISOU 1504  CZ  ARG A 194     8920   7781   6508  -1416   -206    439       C  
ATOM   1505  NH1 ARG A 194      35.382  30.275  44.303  1.00 70.96           N  
ANISOU 1505  NH1 ARG A 194    10142   9021   7798  -1320   -241    416       N  
ATOM   1506  NH2 ARG A 194      35.207  28.756  46.033  1.00 58.12           N  
ANISOU 1506  NH2 ARG A 194     8578   7445   6059  -1539   -186    476       N  
ATOM   1507  N   GLN A 195      35.629  24.548  38.845  1.00 49.19           N  
ANISOU 1507  N   GLN A 195     7590   5889   5211  -1047   -259    640       N  
ATOM   1508  CA  GLN A 195      35.064  24.051  37.577  1.00 47.93           C  
ANISOU 1508  CA  GLN A 195     7442   5681   5088   -973   -264    596       C  
ATOM   1509  C   GLN A 195      35.273  22.542  37.424  1.00 51.07           C  
ANISOU 1509  C   GLN A 195     7887   6027   5492   -996   -264    666       C  
ATOM   1510  O   GLN A 195      34.534  21.859  36.673  1.00 51.27           O  
ANISOU 1510  O   GLN A 195     7918   6024   5537   -974   -261    618       O  
ATOM   1511  CB  GLN A 195      35.761  24.764  36.425  1.00 45.35           C  
ANISOU 1511  CB  GLN A 195     7141   5298   4791   -853   -282    616       C  
ATOM   1512  CG  GLN A 195      35.239  24.530  35.026  1.00 45.53           C  
ANISOU 1512  CG  GLN A 195     7196   5263   4839   -763   -296    565       C  
ATOM   1513  CD  GLN A 195      33.800  24.983  34.823  1.00 47.86           C  
ANISOU 1513  CD  GLN A 195     7457   5588   5139   -747   -322    420       C  
ATOM   1514  OE1 GLN A 195      33.260  25.775  35.599  1.00 49.49           O  
ANISOU 1514  OE1 GLN A 195     7611   5859   5333   -787   -327    345       O  
ATOM   1515  NE2 GLN A 195      33.166  24.470  33.773  1.00 46.53           N  
ANISOU 1515  NE2 GLN A 195     7311   5374   4994   -683   -344    367       N  
ATOM   1516  N   ARG A 196      36.316  22.021  38.070  1.00 50.53           N  
ANISOU 1516  N   ARG A 196     7856   5934   5410  -1027   -280    774       N  
ATOM   1517  CA  ARG A 196      36.614  20.615  37.917  1.00 50.06           C  
ANISOU 1517  CA  ARG A 196     7854   5808   5357  -1034   -302    841       C  
ATOM   1518  C   ARG A 196      35.547  19.864  38.669  1.00 50.67           C  
ANISOU 1518  C   ARG A 196     7961   5908   5382  -1163   -279    806       C  
ATOM   1519  O   ARG A 196      35.122  18.793  38.217  1.00 50.21           O  
ANISOU 1519  O   ARG A 196     7942   5803   5332  -1173   -280    804       O  
ATOM   1520  CB  ARG A 196      38.001  20.252  38.422  1.00 49.93           C  
ANISOU 1520  CB  ARG A 196     7873   5752   5348  -1019   -350    947       C  
ATOM   1521  CG  ARG A 196      38.375  18.801  38.157  1.00 51.00           C  
ANISOU 1521  CG  ARG A 196     8075   5803   5501  -1001   -395   1007       C  
ATOM   1522  CD  ARG A 196      38.745  18.623  36.691  1.00 51.99           C  
ANISOU 1522  CD  ARG A 196     8175   5882   5696   -877   -389    993       C  
ATOM   1523  NE  ARG A 196      38.981  17.238  36.299  1.00 52.14           N  
ANISOU 1523  NE  ARG A 196     8249   5821   5741   -848   -432   1031       N  
ATOM   1524  CZ  ARG A 196      38.028  16.343  36.064  1.00 52.87           C  
ANISOU 1524  CZ  ARG A 196     8388   5885   5817   -888   -426   1011       C  
ATOM   1525  NH1 ARG A 196      36.737  16.642  36.224  1.00 53.41           N  
ANISOU 1525  NH1 ARG A 196     8442   6005   5847   -966   -375    941       N  
ATOM   1526  NH2 ARG A 196      38.367  15.129  35.665  1.00 52.38           N  
ANISOU 1526  NH2 ARG A 196     8380   5741   5783   -851   -473   1048       N  
ATOM   1527  N   LEU A 197      35.078  20.455  39.775  1.00 50.12           N  
ANISOU 1527  N   LEU A 197     7873   5913   5258  -1268   -250    766       N  
ATOM   1528  CA  LEU A 197      33.943  19.903  40.529  1.00 51.14           C  
ANISOU 1528  CA  LEU A 197     8022   6082   5328  -1421   -201    702       C  
ATOM   1529  C   LEU A 197      32.654  20.015  39.733  1.00 51.91           C  
ANISOU 1529  C   LEU A 197     8042   6217   5467  -1406   -160    557       C  
ATOM   1530  O   LEU A 197      31.830  19.115  39.755  1.00 54.37           O  
ANISOU 1530  O   LEU A 197     8373   6523   5762  -1494   -125    510       O  
ATOM   1531  CB  LEU A 197      33.783  20.589  41.880  1.00 51.74           C  
ANISOU 1531  CB  LEU A 197     8091   6236   5333  -1540   -170    678       C  
ATOM   1532  CG  LEU A 197      32.522  20.235  42.648  1.00 52.89           C  
ANISOU 1532  CG  LEU A 197     8238   6445   5413  -1716    -92    576       C  
ATOM   1533  CD1 LEU A 197      32.372  18.726  42.801  1.00 52.02           C  
ANISOU 1533  CD1 LEU A 197     8251   6262   5254  -1818    -86    636       C  
ATOM   1534  CD2 LEU A 197      32.570  20.950  43.993  1.00 52.76           C  
ANISOU 1534  CD2 LEU A 197     8226   6501   5319  -1828    -63    565       C  
ATOM   1535  N   ARG A 198      32.494  21.091  38.979  1.00 52.41           N  
ANISOU 1535  N   ARG A 198     8025   6304   5583  -1290   -175    483       N  
ATOM   1536  CA  ARG A 198      31.372  21.158  38.049  1.00 52.12           C  
ANISOU 1536  CA  ARG A 198     7925   6280   5597  -1239   -170    345       C  
ATOM   1537  C   ARG A 198      31.384  20.058  36.989  1.00 51.56           C  
ANISOU 1537  C   ARG A 198     7901   6127   5561  -1180   -189    379       C  
ATOM   1538  O   ARG A 198      30.388  19.347  36.832  1.00 51.76           O  
ANISOU 1538  O   ARG A 198     7908   6163   5598  -1237   -163    292       O  
ATOM   1539  CB  ARG A 198      31.314  22.502  37.383  1.00 52.09           C  
ANISOU 1539  CB  ARG A 198     7869   6290   5634  -1111   -209    273       C  
ATOM   1540  CG  ARG A 198      30.888  23.573  38.346  1.00 52.75           C  
ANISOU 1540  CG  ARG A 198     7883   6464   5694  -1170   -192    183       C  
ATOM   1541  CD  ARG A 198      30.506  24.847  37.629  1.00 55.37           C  
ANISOU 1541  CD  ARG A 198     8169   6799   6068  -1044   -248     74       C  
ATOM   1542  NE  ARG A 198      30.551  25.933  38.596  1.00 55.53           N  
ANISOU 1542  NE  ARG A 198     8145   6889   6064  -1085   -242     35       N  
ATOM   1543  CZ  ARG A 198      31.490  26.854  38.680  1.00 53.13           C  
ANISOU 1543  CZ  ARG A 198     7876   6565   5747  -1032   -270    115       C  
ATOM   1544  NH1 ARG A 198      32.500  26.912  37.818  1.00 52.89           N  
ANISOU 1544  NH1 ARG A 198     7921   6448   5725   -938   -299    230       N  
ATOM   1545  NH2 ARG A 198      31.394  27.734  39.661  1.00 55.91           N  
ANISOU 1545  NH2 ARG A 198     8181   6987   6076  -1085   -261     65       N  
ATOM   1546  N   CYS A 199      32.494  19.885  36.287  1.00 50.37           N  
ANISOU 1546  N   CYS A 199     7807   5900   5432  -1074   -229    495       N  
ATOM   1547  CA  CYS A 199      32.559  18.807  35.288  1.00 52.71           C  
ANISOU 1547  CA  CYS A 199     8148   6117   5761  -1016   -247    526       C  
ATOM   1548  C   CYS A 199      32.443  17.400  35.889  1.00 54.46           C  
ANISOU 1548  C   CYS A 199     8433   6306   5951  -1131   -233    578       C  
ATOM   1549  O   CYS A 199      31.798  16.539  35.314  1.00 55.23           O  
ANISOU 1549  O   CYS A 199     8544   6372   6070  -1138   -229    537       O  
ATOM   1550  CB  CYS A 199      33.830  18.880  34.475  1.00 51.95           C  
ANISOU 1550  CB  CYS A 199     8092   5953   5692   -893   -280    625       C  
ATOM   1551  SG  CYS A 199      34.013  20.438  33.571  1.00 52.44           S  
ANISOU 1551  SG  CYS A 199     8130   6022   5772   -769   -294    574       S  
ATOM   1552  N   ALA A 200      33.047  17.181  37.047  1.00 54.57           N  
ANISOU 1552  N   ALA A 200     8501   6322   5910  -1224   -234    666       N  
ATOM   1553  CA  ALA A 200      32.943  15.884  37.719  1.00 55.46           C  
ANISOU 1553  CA  ALA A 200     8714   6388   5973  -1348   -233    722       C  
ATOM   1554  C   ALA A 200      31.489  15.585  38.073  1.00 57.73           C  
ANISOU 1554  C   ALA A 200     8976   6730   6228  -1493   -161    599       C  
ATOM   1555  O   ALA A 200      31.023  14.470  37.889  1.00 58.45           O  
ANISOU 1555  O   ALA A 200     9125   6771   6311  -1557   -150    594       O  
ATOM   1556  CB  ALA A 200      33.822  15.849  38.960  1.00 54.09           C  
ANISOU 1556  CB  ALA A 200     8620   6201   5732  -1419   -263    829       C  
ATOM   1557  N   SER A 201      30.767  16.590  38.555  1.00 60.79           N  
ANISOU 1557  N   SER A 201     9272   7222   6606  -1547   -109    485       N  
ATOM   1558  CA  SER A 201      29.358  16.428  38.900  1.00 62.46           C  
ANISOU 1558  CA  SER A 201     9426   7505   6800  -1688    -29    329       C  
ATOM   1559  C   SER A 201      28.571  15.920  37.719  1.00 65.75           C  
ANISOU 1559  C   SER A 201     9792   7898   7291  -1623    -33    232       C  
ATOM   1560  O   SER A 201      27.893  14.912  37.815  1.00 69.17           O  
ANISOU 1560  O   SER A 201    10260   8316   7706  -1742     11    191       O  
ATOM   1561  CB  SER A 201      28.755  17.757  39.365  1.00 60.71           C  
ANISOU 1561  CB  SER A 201     9080   7402   6586  -1705      9    192       C  
ATOM   1562  OG  SER A 201      29.461  18.224  40.477  1.00 59.33           O  
ANISOU 1562  OG  SER A 201     8954   7250   6340  -1769     13    278       O  
ATOM   1563  N   ILE A 202      28.655  16.616  36.590  1.00 65.51           N  
ANISOU 1563  N   ILE A 202     9969   7229   7691   -133    432    254       N  
ATOM   1564  CA  ILE A 202      27.810  16.236  35.455  1.00 68.98           C  
ANISOU 1564  CA  ILE A 202    10540   7558   8112   -166    420    119       C  
ATOM   1565  C   ILE A 202      28.243  14.868  34.937  1.00 64.39           C  
ANISOU 1565  C   ILE A 202    10084   6810   7571   -147    573    173       C  
ATOM   1566  O   ILE A 202      27.416  14.057  34.601  1.00 63.58           O  
ANISOU 1566  O   ILE A 202    10063   6627   7469   -220    599     89       O  
ATOM   1567  CB  ILE A 202      27.754  17.295  34.306  1.00 73.01           C  
ANISOU 1567  CB  ILE A 202    11120   8060   8562   -137    336     23       C  
ATOM   1568  CG1 ILE A 202      29.000  17.263  33.432  1.00 76.25           C  
ANISOU 1568  CG1 ILE A 202    11630   8371   8972    -52    425     95       C  
ATOM   1569  CG2 ILE A 202      27.586  18.707  34.859  1.00 68.49           C  
ANISOU 1569  CG2 ILE A 202    10437   7628   7958   -132    222     -2       C  
ATOM   1570  CD1 ILE A 202      28.958  18.266  32.303  1.00 84.26           C  
ANISOU 1570  CD1 ILE A 202    12721   9372   9922    -25    350      8       C  
ATOM   1571  N   GLN A 203      29.537  14.606  34.913  1.00 64.29           N  
ANISOU 1571  N   GLN A 203    10085   6748   7594    -54    685    317       N  
ATOM   1572  CA  GLN A 203      30.017  13.365  34.352  1.00 68.29           C  
ANISOU 1572  CA  GLN A 203    10726   7076   8145    -16    857    375       C  
ATOM   1573  C   GLN A 203      29.648  12.137  35.202  1.00 68.46           C  
ANISOU 1573  C   GLN A 203    10735   7053   8225    -54    953    435       C  
ATOM   1574  O   GLN A 203      29.288  11.092  34.662  1.00 68.74           O  
ANISOU 1574  O   GLN A 203    10916   6928   8276    -91   1062    386       O  
ATOM   1575  CB  GLN A 203      31.520  13.414  34.130  1.00 72.86           C  
ANISOU 1575  CB  GLN A 203    11306   7623   8755    111    964    535       C  
ATOM   1576  CG  GLN A 203      31.968  12.452  33.035  1.00 81.19           C  
ANISOU 1576  CG  GLN A 203    12551   8462   9834    161   1137    543       C  
ATOM   1577  CD  GLN A 203      33.464  12.217  33.054  1.00 86.21           C  
ANISOU 1577  CD  GLN A 203    13163   9066  10528    302   1282    744       C  
ATOM   1578  OE1 GLN A 203      33.983  11.493  33.916  1.00 82.01           O  
ANISOU 1578  OE1 GLN A 203    12551   8543  10065    361   1387    915       O  
ATOM   1579  NE2 GLN A 203      34.175  12.844  32.104  1.00 92.43           N  
ANISOU 1579  NE2 GLN A 203    14010   9825  11286    362   1290    736       N  
ATOM   1580  N   LYS A 204      29.685  12.285  36.518  1.00 65.75           N  
ANISOU 1580  N   LYS A 204    10227   6851   7903    -59    914    531       N  
ATOM   1581  CA  LYS A 204      29.477  11.159  37.430  1.00 66.97           C  
ANISOU 1581  CA  LYS A 204    10356   6976   8115    -81   1012    620       C  
ATOM   1582  C   LYS A 204      28.092  11.152  38.083  1.00 64.51           C  
ANISOU 1582  C   LYS A 204     9989   6741   7782   -211    912    499       C  
ATOM   1583  O   LYS A 204      27.723  10.162  38.663  1.00 66.83           O  
ANISOU 1583  O   LYS A 204    10292   6984   8115   -250    995    538       O  
ATOM   1584  CB  LYS A 204      30.531  11.167  38.563  1.00 66.55           C  
ANISOU 1584  CB  LYS A 204    10149   7040   8097      2   1053    843       C  
ATOM   1585  CG  LYS A 204      31.991  11.213  38.112  1.00 67.05           C  
ANISOU 1585  CG  LYS A 204    10219   7071   8187    138   1151   1001       C  
ATOM   1586  CD  LYS A 204      32.477   9.938  37.418  1.00 66.46           C  
ANISOU 1586  CD  LYS A 204    10300   6771   8181    222   1366   1079       C  
ATOM   1587  N   PHE A 205      27.348  12.249  38.044  1.00 61.95           N  
ANISOU 1587  N   PHE A 205     9599   6539   7399   -270    746    365       N  
ATOM   1588  CA  PHE A 205      26.051  12.290  38.732  1.00 62.46           C  
ANISOU 1588  CA  PHE A 205     9588   6694   7450   -382    658    265       C  
ATOM   1589  C   PHE A 205      24.953  12.942  37.911  1.00 62.40           C  
ANISOU 1589  C   PHE A 205     9612   6711   7387   -452    532     74       C  
ATOM   1590  O   PHE A 205      23.872  13.211  38.435  1.00 64.58           O  
ANISOU 1590  O   PHE A 205     9801   7087   7648   -532    443     -9       O  
ATOM   1591  CB  PHE A 205      26.175  13.035  40.065  1.00 62.15           C  
ANISOU 1591  CB  PHE A 205     9371   6841   7401   -382    585    337       C  
ATOM   1592  CG  PHE A 205      27.204  12.454  41.001  1.00 63.26           C  
ANISOU 1592  CG  PHE A 205     9448   7006   7581   -324    686    543       C  
ATOM   1593  CD1 PHE A 205      26.828  11.685  42.078  1.00 62.65           C  
ANISOU 1593  CD1 PHE A 205     9312   6962   7532   -372    733    610       C  
ATOM   1594  CD2 PHE A 205      28.547  12.708  40.816  1.00 63.14           C  
ANISOU 1594  CD2 PHE A 205     9422   6997   7571   -221    732    679       C  
ATOM   1595  CE1 PHE A 205      27.782  11.157  42.936  1.00 63.92           C  
ANISOU 1595  CE1 PHE A 205     9404   7161   7723   -311    823    820       C  
ATOM   1596  CE2 PHE A 205      29.498  12.191  41.673  1.00 63.01           C  
ANISOU 1596  CE2 PHE A 205     9324   7030   7586   -163    818    889       C  
ATOM   1597  CZ  PHE A 205      29.118  11.405  42.729  1.00 62.20           C  
ANISOU 1597  CZ  PHE A 205     9164   6961   7509   -204    863    964       C  
ATOM   1598  N   GLY A 206      25.230  13.214  36.640  1.00 62.00           N  
ANISOU 1598  N   GLY A 206     9676   6578   7304   -417    525     16       N  
ATOM   1599  CA  GLY A 206      24.272  13.855  35.766  1.00 66.03           C  
ANISOU 1599  CA  GLY A 206    10215   7122   7753   -471    403   -143       C  
ATOM   1600  C   GLY A 206      24.054  15.345  36.001  1.00 70.44           C  
ANISOU 1600  C   GLY A 206    10656   7832   8277   -436    261   -178       C  
ATOM   1601  O   GLY A 206      24.336  15.881  37.082  1.00 70.31           O  
ANISOU 1601  O   GLY A 206    10517   7919   8277   -411    242   -109       O  
ATOM   1602  N   GLU A 207      23.535  15.998  34.959  1.00 76.47           N  
ANISOU 1602  N   GLU A 207    11467   8605   8985   -440    170   -284       N  
ATOM   1603  CA  GLU A 207      23.120  17.400  34.989  1.00 78.53           C  
ANISOU 1603  CA  GLU A 207    11640   8987   9210   -405     43   -333       C  
ATOM   1604  C   GLU A 207      22.344  17.739  36.244  1.00 77.40           C  
ANISOU 1604  C   GLU A 207    11342   8976   9090   -443     -6   -342       C  
ATOM   1605  O   GLU A 207      22.601  18.739  36.885  1.00 78.01           O  
ANISOU 1605  O   GLU A 207    11339   9134   9165   -397    -39   -314       O  
ATOM   1606  CB  GLU A 207      22.205  17.702  33.801  1.00 82.82           C  
ANISOU 1606  CB  GLU A 207    12236   9540   9693   -435    -51   -450       C  
ATOM   1607  CG  GLU A 207      22.865  17.644  32.435  1.00 89.17           C  
ANISOU 1607  CG  GLU A 207    13198  10231  10450   -399    -23   -461       C  
ATOM   1608  CD  GLU A 207      21.985  18.229  31.336  1.00 97.55           C  
ANISOU 1608  CD  GLU A 207    14287  11343  11434   -419   -142   -560       C  
ATOM   1609  OE1 GLU A 207      20.932  18.832  31.673  1.00 96.99           O  
ANISOU 1609  OE1 GLU A 207    14094  11402  11355   -436   -247   -605       O  
ATOM   1610  OE2 GLU A 207      22.348  18.083  30.136  1.00 96.08           O  
ANISOU 1610  OE2 GLU A 207    14241  11071  11193   -415   -126   -585       O  
ATOM   1611  N   ARG A 208      21.361  16.910  36.564  1.00 80.29           N  
ANISOU 1611  N   ARG A 208    11676   9359   9472   -539     -5   -389       N  
ATOM   1612  CA  ARG A 208      20.495  17.137  37.713  1.00 81.06           C  
ANISOU 1612  CA  ARG A 208    11629   9579   9589   -585    -44   -406       C  
ATOM   1613  C   ARG A 208      21.277  17.628  38.942  1.00 80.67           C  
ANISOU 1613  C   ARG A 208    11501   9589   9563   -541     -8   -310       C  
ATOM   1614  O   ARG A 208      20.824  18.529  39.661  1.00 76.31           O  
ANISOU 1614  O   ARG A 208    10847   9145   9002   -536    -59   -335       O  
ATOM   1615  CB  ARG A 208      19.747  15.843  38.032  1.00 86.54           C  
ANISOU 1615  CB  ARG A 208    12322  10250  10309   -699      3   -429       C  
ATOM   1616  CG  ARG A 208      18.640  15.967  39.062  1.00 90.73           C  
ANISOU 1616  CG  ARG A 208    12707  10909  10857   -763    -39   -465       C  
ATOM   1617  CD  ARG A 208      17.764  14.714  39.053  1.00 97.16           C  
ANISOU 1617  CD  ARG A 208    13539  11695  11684   -895     -4   -513       C  
ATOM   1618  NE  ARG A 208      16.720  14.771  40.074  1.00 97.34           N  
ANISOU 1618  NE  ARG A 208    13417  11842  11727   -960    -33   -540       N  
ATOM   1619  CZ  ARG A 208      16.873  14.432  41.354  1.00 99.35           C  
ANISOU 1619  CZ  ARG A 208    13609  12122  12017   -979     33   -472       C  
ATOM   1620  NH1 ARG A 208      18.043  13.984  41.808  1.00 98.12           N  
ANISOU 1620  NH1 ARG A 208    13511  11886  11883   -936    127   -358       N  
ATOM   1621  NH2 ARG A 208      15.842  14.539  42.193  1.00100.54           N  
ANISOU 1621  NH2 ARG A 208    13633  12389  12181  -1042      6   -509       N  
ATOM   1622  N   ALA A 209      22.458  17.049  39.165  1.00 79.36           N  
ANISOU 1622  N   ALA A 209    11383   9354   9418   -511     85   -198       N  
ATOM   1623  CA  ALA A 209      23.280  17.394  40.319  1.00 78.05           C  
ANISOU 1623  CA  ALA A 209    11137   9262   9258   -488    116    -90       C  
ATOM   1624  C   ALA A 209      23.843  18.805  40.221  1.00 79.97           C  
ANISOU 1624  C   ALA A 209    11363   9562   9461   -429     63    -94       C  
ATOM   1625  O   ALA A 209      23.938  19.518  41.228  1.00 75.65           O  
ANISOU 1625  O   ALA A 209    10729   9120   8894   -447     47    -73       O  
ATOM   1626  CB  ALA A 209      24.415  16.399  40.453  1.00 80.07           C  
ANISOU 1626  CB  ALA A 209    11437   9439   9545   -458    229     50       C  
ATOM   1627  N   LEU A 210      24.234  19.198  39.010  1.00 76.18           N  
ANISOU 1627  N   LEU A 210    10977   9007   8961   -368     46   -122       N  
ATOM   1628  CA  LEU A 210      24.727  20.544  38.773  1.00 77.36           C  
ANISOU 1628  CA  LEU A 210    11131   9190   9072   -314      2   -134       C  
ATOM   1629  C   LEU A 210      23.601  21.585  38.889  1.00 76.71           C  
ANISOU 1629  C   LEU A 210    10998   9181   8969   -320    -80   -243       C  
ATOM   1630  O   LEU A 210      23.801  22.660  39.477  1.00 75.20           O  
ANISOU 1630  O   LEU A 210    10767   9054   8753   -312    -92   -245       O  
ATOM   1631  CB  LEU A 210      25.413  20.631  37.403  1.00 80.32           C  
ANISOU 1631  CB  LEU A 210    11628   9460   9431   -247     13   -131       C  
ATOM   1632  CG  LEU A 210      26.108  21.950  37.036  1.00 80.71           C  
ANISOU 1632  CG  LEU A 210    11703   9522   9441   -190    -14   -130       C  
ATOM   1633  CD1 LEU A 210      27.241  22.261  37.997  1.00 82.31           C  
ANISOU 1633  CD1 LEU A 210    11844   9792   9637   -201     32    -22       C  
ATOM   1634  CD2 LEU A 210      26.636  21.862  35.620  1.00 80.49           C  
ANISOU 1634  CD2 LEU A 210    11802   9383   9397   -130      2   -133       C  
ATOM   1635  N   LYS A 211      22.423  21.270  38.349  1.00 74.18           N  
ANISOU 1635  N   LYS A 211    10678   8852   8654   -339   -128   -328       N  
ATOM   1636  CA  LYS A 211      21.257  22.154  38.509  1.00 74.87           C  
ANISOU 1636  CA  LYS A 211    10693   9020   8733   -333   -197   -413       C  
ATOM   1637  C   LYS A 211      21.042  22.452  39.984  1.00 69.59           C  
ANISOU 1637  C   LYS A 211     9920   8444   8076   -375   -171   -399       C  
ATOM   1638  O   LYS A 211      20.987  23.597  40.397  1.00 69.11           O  
ANISOU 1638  O   LYS A 211     9833   8429   7997   -346   -177   -422       O  
ATOM   1639  CB  LYS A 211      19.996  21.521  37.930  1.00 76.62           C  
ANISOU 1639  CB  LYS A 211    10895   9255   8961   -373   -249   -485       C  
ATOM   1640  CG  LYS A 211      20.055  21.389  36.422  1.00 80.98           C  
ANISOU 1640  CG  LYS A 211    11554   9736   9479   -345   -288   -515       C  
ATOM   1641  CD  LYS A 211      18.685  21.321  35.755  1.00 83.97           C  
ANISOU 1641  CD  LYS A 211    11891  10176   9837   -377   -375   -594       C  
ATOM   1642  CE  LYS A 211      18.842  21.263  34.230  1.00 86.99           C  
ANISOU 1642  CE  LYS A 211    12391  10497  10163   -357   -416   -620       C  
ATOM   1643  NZ  LYS A 211      17.640  20.760  33.500  1.00 88.63           N  
ANISOU 1643  NZ  LYS A 211    12574  10766  10334   -435   -494   -688       N  
ATOM   1644  N   ALA A 212      20.970  21.407  40.783  1.00 68.81           N  
ANISOU 1644  N   ALA A 212     9775   8365   8003   -448   -128   -360       N  
ATOM   1645  CA  ALA A 212      20.691  21.580  42.186  1.00 72.13           C  
ANISOU 1645  CA  ALA A 212    10100   8881   8427   -502   -102   -348       C  
ATOM   1646  C   ALA A 212      21.709  22.546  42.825  1.00 75.80           C  
ANISOU 1646  C   ALA A 212    10569   9382   8851   -490    -76   -301       C  
ATOM   1647  O   ALA A 212      21.321  23.463  43.564  1.00 74.26           O  
ANISOU 1647  O   ALA A 212    10328   9255   8634   -505    -73   -344       O  
ATOM   1648  CB  ALA A 212      20.685  20.233  42.892  1.00 70.23           C  
ANISOU 1648  CB  ALA A 212     9826   8643   8214   -577    -51   -288       C  
ATOM   1649  N   TRP A 213      22.994  22.360  42.514  1.00 75.66           N  
ANISOU 1649  N   TRP A 213    10608   9320   8819   -469    -48   -215       N  
ATOM   1650  CA  TRP A 213      24.040  23.252  43.008  1.00 78.06           C  
ANISOU 1650  CA  TRP A 213    10915   9669   9074   -476    -28   -166       C  
ATOM   1651  C   TRP A 213      23.696  24.673  42.675  1.00 74.05           C  
ANISOU 1651  C   TRP A 213    10442   9155   8537   -438    -56   -258       C  
ATOM   1652  O   TRP A 213      23.672  25.538  43.549  1.00 77.01           O  
ANISOU 1652  O   TRP A 213    10792   9596   8874   -481    -36   -283       O  
ATOM   1653  CB  TRP A 213      25.393  22.894  42.403  1.00 89.25           C  
ANISOU 1653  CB  TRP A 213    12389  11035  10488   -439      0    -63       C  
ATOM   1654  CG  TRP A 213      26.572  23.598  43.046  1.00 99.62           C  
ANISOU 1654  CG  TRP A 213    13680  12425  11745   -476     22     12       C  
ATOM   1655  CD1 TRP A 213      27.036  24.884  42.782  1.00102.53           C  
ANISOU 1655  CD1 TRP A 213    14096  12797  12065   -468     10    -26       C  
ATOM   1656  CD2 TRP A 213      27.490  23.060  44.072  1.00110.16           C  
ANISOU 1656  CD2 TRP A 213    14939  13859  13057   -537     60    149       C  
ATOM   1657  NE1 TRP A 213      28.131  25.177  43.559  1.00113.54           N  
ANISOU 1657  NE1 TRP A 213    15449  14288  13404   -538     36     63       N  
ATOM   1658  CE2 TRP A 213      28.461  24.126  44.355  1.00115.05           C  
ANISOU 1658  CE2 TRP A 213    15557  14552  13605   -580     59    178       C  
ATOM   1659  CE3 TRP A 213      27.593  21.851  44.763  1.00116.18           C  
ANISOU 1659  CE3 TRP A 213    15637  14661  13847   -564     96    256       C  
ATOM   1660  CZ2 TRP A 213      29.490  23.966  45.301  1.00120.75           C  
ANISOU 1660  CZ2 TRP A 213    16198  15406  14275   -655     80    311       C  
ATOM   1661  CZ3 TRP A 213      28.628  21.695  45.708  1.00121.76           C  
ANISOU 1661  CZ3 TRP A 213    16263  15491  14509   -618    122    401       C  
ATOM   1662  CH2 TRP A 213      29.556  22.730  45.972  1.00126.14           C  
ANISOU 1662  CH2 TRP A 213    16802  16139  14986   -667    107    429       C  
ATOM   1663  N   SER A 214      23.411  24.914  41.408  1.00 68.04           N  
ANISOU 1663  N   SER A 214     9749   8314   7790   -358    -94   -306       N  
ATOM   1664  CA  SER A 214      23.110  26.249  40.916  1.00 69.14           C  
ANISOU 1664  CA  SER A 214     9933   8429   7907   -296   -114   -377       C  
ATOM   1665  C   SER A 214      21.884  26.900  41.559  1.00 67.28           C  
ANISOU 1665  C   SER A 214     9635   8247   7680   -298   -115   -456       C  
ATOM   1666  O   SER A 214      21.963  28.032  42.052  1.00 68.81           O  
ANISOU 1666  O   SER A 214     9848   8453   7844   -298    -78   -487       O  
ATOM   1667  CB  SER A 214      22.929  26.195  39.403  1.00 69.95           C  
ANISOU 1667  CB  SER A 214    10111   8448   8020   -212   -161   -401       C  
ATOM   1668  OG  SER A 214      24.169  25.859  38.825  1.00 70.58           O  
ANISOU 1668  OG  SER A 214    10262   8469   8086   -201   -139   -332       O  
ATOM   1669  N   VAL A 215      20.761  26.190  41.554  1.00 63.00           N  
ANISOU 1669  N   VAL A 215     9025   7735   7179   -303   -146   -488       N  
ATOM   1670  CA  VAL A 215      19.586  26.634  42.291  1.00 62.79           C  
ANISOU 1670  CA  VAL A 215     8916   7773   7169   -308   -134   -547       C  
ATOM   1671  C   VAL A 215      19.970  27.157  43.704  1.00 64.43           C  
ANISOU 1671  C   VAL A 215     9103   8034   7342   -383    -62   -543       C  
ATOM   1672  O   VAL A 215      19.526  28.209  44.132  1.00 65.78           O  
ANISOU 1672  O   VAL A 215     9276   8216   7502   -361    -21   -597       O  
ATOM   1673  CB  VAL A 215      18.560  25.488  42.429  1.00 62.30           C  
ANISOU 1673  CB  VAL A 215     8763   7759   7149   -352   -163   -560       C  
ATOM   1674  CG1 VAL A 215      17.454  25.880  43.411  1.00 63.14           C  
ANISOU 1674  CG1 VAL A 215     8770   7947   7275   -370   -134   -609       C  
ATOM   1675  CG2 VAL A 215      17.963  25.128  41.081  1.00 56.64           C  
ANISOU 1675  CG2 VAL A 215     8060   7012   6448   -301   -237   -584       C  
ATOM   1676  N   ALA A 216      20.802  26.415  44.424  1.00 65.38           N  
ANISOU 1676  N   ALA A 216     9210   8191   7441   -472    -39   -475       N  
ATOM   1677  CA  ALA A 216      21.252  26.845  45.734  1.00 65.34           C  
ANISOU 1677  CA  ALA A 216     9187   8257   7382   -565     19   -462       C  
ATOM   1678  C   ALA A 216      22.001  28.145  45.607  1.00 68.08           C  
ANISOU 1678  C   ALA A 216     9621   8572   7674   -555     49   -483       C  
ATOM   1679  O   ALA A 216      21.671  29.143  46.249  1.00 71.45           O  
ANISOU 1679  O   ALA A 216    10067   9013   8068   -580    104   -547       O  
ATOM   1680  CB  ALA A 216      22.149  25.805  46.344  1.00 66.44           C  
ANISOU 1680  CB  ALA A 216     9294   8450   7503   -648     27   -357       C  
ATOM   1681  N   ARG A 217      23.018  28.125  44.761  1.00 70.41           N  
ANISOU 1681  N   ARG A 217     9979   8815   7957   -523     25   -431       N  
ATOM   1682  CA  ARG A 217      23.941  29.228  44.670  1.00 71.11           C  
ANISOU 1682  CA  ARG A 217    10151   8881   7986   -540     57   -435       C  
ATOM   1683  C   ARG A 217      23.214  30.527  44.320  1.00 69.06           C  
ANISOU 1683  C   ARG A 217     9958   8552   7729   -467     88   -533       C  
ATOM   1684  O   ARG A 217      23.436  31.553  44.967  1.00 67.30           O  
ANISOU 1684  O   ARG A 217     9787   8333   7451   -525    155   -577       O  
ATOM   1685  CB  ARG A 217      25.031  28.918  43.653  1.00 77.40           C  
ANISOU 1685  CB  ARG A 217    10998   9627   8783   -499     27   -361       C  
ATOM   1686  CG  ARG A 217      26.394  29.482  44.030  1.00 84.65           C  
ANISOU 1686  CG  ARG A 217    11950  10588   9627   -584     59   -308       C  
ATOM   1687  CD  ARG A 217      27.441  29.124  42.993  1.00 87.25           C  
ANISOU 1687  CD  ARG A 217    12317  10868   9966   -531     39   -227       C  
ATOM   1688  NE  ARG A 217      27.129  29.733  41.693  1.00 93.99           N  
ANISOU 1688  NE  ARG A 217    13267  11600  10846   -417     22   -287       N  
ATOM   1689  CZ  ARG A 217      27.599  30.906  41.255  1.00 98.92           C  
ANISOU 1689  CZ  ARG A 217    13983  12171  11429   -405     48   -320       C  
ATOM   1690  NH1 ARG A 217      28.424  31.643  42.003  1.00 97.07           N  
ANISOU 1690  NH1 ARG A 217    13764  11994  11123   -517     93   -310       N  
ATOM   1691  NH2 ARG A 217      27.243  31.353  40.047  1.00 97.55           N  
ANISOU 1691  NH2 ARG A 217    13893  11891  11281   -290     29   -361       N  
ATOM   1692  N   LEU A 218      22.330  30.471  43.329  1.00 67.45           N  
ANISOU 1692  N   LEU A 218     9754   8288   7585   -345     45   -564       N  
ATOM   1693  CA  LEU A 218      21.681  31.677  42.806  1.00 68.56           C  
ANISOU 1693  CA  LEU A 218     9956   8358   7737   -242     73   -629       C  
ATOM   1694  C   LEU A 218      20.564  32.228  43.700  1.00 67.63           C  
ANISOU 1694  C   LEU A 218     9792   8268   7634   -239    137   -695       C  
ATOM   1695  O   LEU A 218      20.392  33.443  43.815  1.00 64.99           O  
ANISOU 1695  O   LEU A 218     9530   7877   7285   -200    215   -744       O  
ATOM   1696  CB  LEU A 218      21.135  31.429  41.396  1.00 65.13           C  
ANISOU 1696  CB  LEU A 218     9525   7872   7349   -114     -4   -621       C  
ATOM   1697  CG  LEU A 218      22.143  31.072  40.300  1.00 65.65           C  
ANISOU 1697  CG  LEU A 218     9663   7883   7400    -92    -51   -569       C  
ATOM   1698  CD1 LEU A 218      21.531  31.367  38.928  1.00 65.63           C  
ANISOU 1698  CD1 LEU A 218     9698   7823   7418     39   -106   -581       C  
ATOM   1699  CD2 LEU A 218      23.442  31.851  40.431  1.00 66.32           C  
ANISOU 1699  CD2 LEU A 218     9842   7929   7426   -139      3   -549       C  
ATOM   1700  N   SER A 219      19.789  31.340  44.300  1.00 68.37           N  
ANISOU 1700  N   SER A 219     9774   8442   7763   -275    117   -695       N  
ATOM   1701  CA  SER A 219      18.777  31.749  45.268  1.00 71.59           C  
ANISOU 1701  CA  SER A 219    10128   8889   8185   -284    189   -752       C  
ATOM   1702  C   SER A 219      19.376  32.437  46.492  1.00 73.84           C  
ANISOU 1702  C   SER A 219    10473   9189   8394   -405    291   -784       C  
ATOM   1703  O   SER A 219      18.776  33.366  47.025  1.00 77.25           O  
ANISOU 1703  O   SER A 219    10935   9595   8822   -386    389   -849       O  
ATOM   1704  CB  SER A 219      17.984  30.545  45.719  1.00 71.46           C  
ANISOU 1704  CB  SER A 219     9980   8962   8210   -325    148   -739       C  
ATOM   1705  OG  SER A 219      17.612  29.795  44.592  1.00 75.21           O  
ANISOU 1705  OG  SER A 219    10414   9428   8733   -255     51   -711       O  
ATOM   1706  N   GLN A 220      20.555  31.989  46.928  1.00 74.37           N  
ANISOU 1706  N   GLN A 220    10557   9303   8397   -531    274   -735       N  
ATOM   1707  CA  GLN A 220      21.325  32.721  47.935  1.00 75.44           C  
ANISOU 1707  CA  GLN A 220    10763   9466   8436   -668    357   -759       C  
ATOM   1708  C   GLN A 220      21.688  34.110  47.415  1.00 76.55           C  
ANISOU 1708  C   GLN A 220    11043   9495   8546   -625    423   -811       C  
ATOM   1709  O   GLN A 220      21.473  35.102  48.108  1.00 83.57           O  
ANISOU 1709  O   GLN A 220    12008  10354   9392   -672    535   -886       O  
ATOM   1710  CB  GLN A 220      22.619  31.991  48.310  1.00 76.61           C  
ANISOU 1710  CB  GLN A 220    10887   9702   8518   -799    311   -670       C  
ATOM   1711  CG  GLN A 220      22.491  30.934  49.397  1.00 79.55           C  
ANISOU 1711  CG  GLN A 220    11152  10200   8874   -903    297   -622       C  
ATOM   1712  CD  GLN A 220      23.845  30.369  49.821  1.00 80.16           C  
ANISOU 1712  CD  GLN A 220    11204  10376   8877  -1024    263   -513       C  
ATOM   1713  OE1 GLN A 220      24.836  30.523  49.117  1.00 83.29           O  
ANISOU 1713  OE1 GLN A 220    11643  10746   9258  -1009    234   -463       O  
ATOM   1714  NE2 GLN A 220      23.888  29.713  50.974  1.00 77.83           N  
ANISOU 1714  NE2 GLN A 220    10832  10205   8536  -1141    269   -466       N  
ATOM   1715  N   LYS A 221      22.244  34.174  46.204  1.00 75.14           N  
ANISOU 1715  N   LYS A 221    10913   9249   8389   -541    365   -771       N  
ATOM   1716  CA  LYS A 221      22.689  35.447  45.610  1.00 75.81           C  
ANISOU 1716  CA  LYS A 221    11139   9220   8445   -499    426   -807       C  
ATOM   1717  C   LYS A 221      21.521  36.369  45.284  1.00 73.42           C  
ANISOU 1717  C   LYS A 221    10879   8818   8199   -352    498   -871       C  
ATOM   1718  O   LYS A 221      21.622  37.577  45.458  1.00 71.37           O  
ANISOU 1718  O   LYS A 221    10745   8470   7904   -357    613   -929       O  
ATOM   1719  CB  LYS A 221      23.466  35.226  44.301  1.00 79.47           C  
ANISOU 1719  CB  LYS A 221    11637   9635   8924   -428    345   -744       C  
ATOM   1720  CG  LYS A 221      24.940  34.888  44.442  1.00 81.99           C  
ANISOU 1720  CG  LYS A 221    11967  10012   9174   -557    318   -678       C  
ATOM   1721  CD  LYS A 221      25.601  34.792  43.066  1.00 83.21           C  
ANISOU 1721  CD  LYS A 221    12168  10097   9351   -466    260   -625       C  
ATOM   1722  N   PHE A 222      20.429  35.786  44.797  1.00 72.02           N  
ANISOU 1722  N   PHE A 222    10599   8659   8108   -224    436   -854       N  
ATOM   1723  CA  PHE A 222      19.266  36.538  44.324  1.00 72.89           C  
ANISOU 1723  CA  PHE A 222    10713   8698   8282    -54    485   -882       C  
ATOM   1724  C   PHE A 222      17.984  36.171  45.065  1.00 71.95           C  
ANISOU 1724  C   PHE A 222    10469   8652   8217    -31    510   -906       C  
ATOM   1725  O   PHE A 222      16.987  35.800  44.451  1.00 71.21           O  
ANISOU 1725  O   PHE A 222    10272   8589   8196     92    448   -879       O  
ATOM   1726  CB  PHE A 222      19.037  36.267  42.836  1.00 70.91           C  
ANISOU 1726  CB  PHE A 222    10440   8420   8084     95    375   -826       C  
ATOM   1727  CG  PHE A 222      20.252  36.411  41.993  1.00 69.07           C  
ANISOU 1727  CG  PHE A 222    10312   8126   7807     79    335   -792       C  
ATOM   1728  CD1 PHE A 222      21.086  37.494  42.130  1.00 68.27           C  
ANISOU 1728  CD1 PHE A 222    10357   7936   7648     35    432   -821       C  
ATOM   1729  CD2 PHE A 222      20.534  35.472  41.008  1.00 70.74           C  
ANISOU 1729  CD2 PHE A 222    10482   8363   8032    107    210   -735       C  
ATOM   1730  CE1 PHE A 222      22.201  37.631  41.324  1.00 67.67           C  
ANISOU 1730  CE1 PHE A 222    10370   7809   7534     20    398   -786       C  
ATOM   1731  CE2 PHE A 222      21.647  35.607  40.197  1.00 65.56           C  
ANISOU 1731  CE2 PHE A 222     9922   7648   7339    101    184   -702       C  
ATOM   1732  CZ  PHE A 222      22.489  36.678  40.365  1.00 64.23           C  
ANISOU 1732  CZ  PHE A 222     9885   7404   7118     58    275   -723       C  
ATOM   1733  N   PRO A 223      17.985  36.301  46.385  1.00 75.35           N  
ANISOU 1733  N   PRO A 223    10906   9120   8605   -157    605   -956       N  
ATOM   1734  CA  PRO A 223      16.803  35.886  47.146  1.00 76.41           C  
ANISOU 1734  CA  PRO A 223    10917   9329   8786   -146    635   -977       C  
ATOM   1735  C   PRO A 223      15.542  36.585  46.680  1.00 76.25           C  
ANISOU 1735  C   PRO A 223    10862   9259   8849     47    693   -985       C  
ATOM   1736  O   PRO A 223      14.445  36.041  46.810  1.00 78.11           O  
ANISOU 1736  O   PRO A 223    10954   9575   9150    102    667   -972       O  
ATOM   1737  CB  PRO A 223      17.150  36.281  48.588  1.00 75.43           C  
ANISOU 1737  CB  PRO A 223    10859   9223   8580   -312    761  -1042       C  
ATOM   1738  CG  PRO A 223      18.242  37.281  48.466  1.00 76.20           C  
ANISOU 1738  CG  PRO A 223    11130   9225   8598   -371    827  -1070       C  
ATOM   1739  CD  PRO A 223      19.009  36.913  47.243  1.00 75.09           C  
ANISOU 1739  CD  PRO A 223    10996   9065   8468   -320    697  -1000       C  
ATOM   1740  N   LYS A 224      15.709  37.780  46.136  1.00 79.85           N  
ANISOU 1740  N   LYS A 224    11446   9587   9304    150    775   -996       N  
ATOM   1741  CA  LYS A 224      14.592  38.584  45.658  1.00 86.11           C  
ANISOU 1741  CA  LYS A 224    12218  10323  10177    356    848   -982       C  
ATOM   1742  C   LYS A 224      13.909  37.971  44.425  1.00 84.63           C  
ANISOU 1742  C   LYS A 224    11893  10203  10059    501    693   -900       C  
ATOM   1743  O   LYS A 224      12.754  38.263  44.155  1.00 84.51           O  
ANISOU 1743  O   LYS A 224    11783  10212  10117    659    718   -867       O  
ATOM   1744  CB  LYS A 224      15.079  40.019  45.382  1.00 92.37           C  
ANISOU 1744  CB  LYS A 224    13208  10946  10943    422    987  -1008       C  
ATOM   1745  CG  LYS A 224      14.202  40.841  44.446  1.00 98.63           C  
ANISOU 1745  CG  LYS A 224    13995  11662  11817    671   1031   -952       C  
ATOM   1746  CD  LYS A 224      14.814  42.194  44.114  1.00103.73           C  
ANISOU 1746  CD  LYS A 224    14857  12122  12432    726   1170   -971       C  
ATOM   1747  CE  LYS A 224      14.277  42.723  42.781  1.00107.62           C  
ANISOU 1747  CE  LYS A 224    15337  12562  12991    970   1139   -876       C  
ATOM   1748  NZ  LYS A 224      12.947  42.148  42.402  1.00107.74           N  
ANISOU 1748  NZ  LYS A 224    15130  12712  13094   1122   1047   -799       N  
ATOM   1749  N   ALA A 225      14.606  37.113  43.690  1.00 83.84           N  
ANISOU 1749  N   ALA A 225    11780  10144   9932    443    538   -864       N  
ATOM   1750  CA  ALA A 225      14.055  36.572  42.443  1.00 84.52           C  
ANISOU 1750  CA  ALA A 225    11765  10289  10061    556    393   -796       C  
ATOM   1751  C   ALA A 225      12.965  35.513  42.680  1.00 85.51           C  
ANISOU 1751  C   ALA A 225    11693  10562  10237    538    315   -782       C  
ATOM   1752  O   ALA A 225      13.067  34.704  43.598  1.00 85.51           O  
ANISOU 1752  O   ALA A 225    11643  10625  10223    395    314   -813       O  
ATOM   1753  CB  ALA A 225      15.180  36.003  41.584  1.00 78.54           C  
ANISOU 1753  CB  ALA A 225    11078   9510   9254    491    276   -770       C  
ATOM   1754  N   GLU A 226      11.922  35.523  41.852  1.00 86.69           N  
ANISOU 1754  N   GLU A 226    11725  10775  10436    679    250   -728       N  
ATOM   1755  CA  GLU A 226      10.911  34.466  41.883  1.00 88.20           C  
ANISOU 1755  CA  GLU A 226    11725  11120  10666    647    156   -710       C  
ATOM   1756  C   GLU A 226      11.522  33.168  41.369  1.00 85.10           C  
ANISOU 1756  C   GLU A 226    11331  10769  10233    513     12   -708       C  
ATOM   1757  O   GLU A 226      12.450  33.193  40.570  1.00 80.80           O  
ANISOU 1757  O   GLU A 226    10903  10153   9646    509    -40   -694       O  
ATOM   1758  CB  GLU A 226       9.686  34.834  41.033  1.00 93.14           C  
ANISOU 1758  CB  GLU A 226    12218  11827  11344    823    111   -640       C  
ATOM   1759  CG  GLU A 226       8.783  35.905  41.635  1.00 96.42           C  
ANISOU 1759  CG  GLU A 226    12584  12229  11822    971    265   -626       C  
ATOM   1760  CD  GLU A 226       8.309  35.568  43.048  1.00104.04           C  
ANISOU 1760  CD  GLU A 226    13473  13242  12815    875    364   -683       C  
ATOM   1761  OE1 GLU A 226       8.168  34.362  43.374  1.00106.60           O  
ANISOU 1761  OE1 GLU A 226    13700  13672  13131    729    277   -704       O  
ATOM   1762  OE2 GLU A 226       8.086  36.511  43.843  1.00106.57           O  
ANISOU 1762  OE2 GLU A 226    13842  13487  13162    942    541   -708       O  
ATOM   1763  N   PHE A 227      10.997  32.038  41.837  1.00 83.17           N  
ANISOU 1763  N   PHE A 227    10963  10632  10005    403    -38   -721       N  
ATOM   1764  CA  PHE A 227      11.526  30.725  41.470  1.00 80.54           C  
ANISOU 1764  CA  PHE A 227    10637  10324   9640    269   -146   -721       C  
ATOM   1765  C   PHE A 227      11.502  30.451  39.967  1.00 79.40           C  
ANISOU 1765  C   PHE A 227    10503  10192   9472    317   -274   -684       C  
ATOM   1766  O   PHE A 227      12.310  29.681  39.455  1.00 75.47           O  
ANISOU 1766  O   PHE A 227    10085   9655   8936    234   -335   -685       O  
ATOM   1767  CB  PHE A 227      10.766  29.623  42.208  1.00 80.43           C  
ANISOU 1767  CB  PHE A 227    10484  10421   9653    154   -162   -739       C  
ATOM   1768  CG  PHE A 227      11.287  28.240  41.932  1.00 77.63           C  
ANISOU 1768  CG  PHE A 227    10153  10072   9272     14   -243   -739       C  
ATOM   1769  CD1 PHE A 227      12.624  27.938  42.132  1.00 74.16           C  
ANISOU 1769  CD1 PHE A 227     9846   9540   8794    -59   -221   -736       C  
ATOM   1770  CD2 PHE A 227      10.443  27.245  41.465  1.00 76.74           C  
ANISOU 1770  CD2 PHE A 227     9931  10057   9171    -46   -332   -738       C  
ATOM   1771  CE1 PHE A 227      13.113  26.673  41.857  1.00 73.70           C  
ANISOU 1771  CE1 PHE A 227     9814   9469   8717   -167   -274   -725       C  
ATOM   1772  CE2 PHE A 227      10.925  25.976  41.199  1.00 75.61           C  
ANISOU 1772  CE2 PHE A 227     9833   9893   9003   -174   -382   -742       C  
ATOM   1773  CZ  PHE A 227      12.260  25.690  41.400  1.00 74.14           C  
ANISOU 1773  CZ  PHE A 227     9783   9598   8788   -224   -346   -732       C  
ATOM   1774  N   VAL A 228      10.574  31.084  39.263  1.00 85.34           N  
ANISOU 1774  N   VAL A 228    11175  11003  10246    453   -309   -646       N  
ATOM   1775  CA  VAL A 228      10.527  31.002  37.799  1.00 86.45           C  
ANISOU 1775  CA  VAL A 228    11331  11167  10348    505   -430   -604       C  
ATOM   1776  C   VAL A 228      11.862  31.483  37.211  1.00 85.33           C  
ANISOU 1776  C   VAL A 228    11385  10878  10159    532   -415   -601       C  
ATOM   1777  O   VAL A 228      12.516  30.747  36.475  1.00 87.44           O  
ANISOU 1777  O   VAL A 228    11726  11118  10379    457   -490   -605       O  
ATOM   1778  CB  VAL A 228       9.372  31.848  37.205  1.00 91.49           C  
ANISOU 1778  CB  VAL A 228    11850  11898  11014    675   -455   -539       C  
ATOM   1779  CG1 VAL A 228       9.026  31.352  35.806  1.00 90.32           C  
ANISOU 1779  CG1 VAL A 228    11661  11845  10812    671   -612   -498       C  
ATOM   1780  CG2 VAL A 228       8.135  31.830  38.105  1.00 92.99           C  
ANISOU 1780  CG2 VAL A 228    11853  12210  11270    692   -406   -535       C  
ATOM   1781  N   GLU A 229      12.276  32.700  37.570  1.00 86.52           N  
ANISOU 1781  N   GLU A 229    11625  10927  10320    629   -305   -598       N  
ATOM   1782  CA  GLU A 229      13.554  33.274  37.103  1.00 85.91           C  
ANISOU 1782  CA  GLU A 229    11733  10711  10199    647   -275   -596       C  
ATOM   1783  C   GLU A 229      14.776  32.410  37.421  1.00 81.11           C  
ANISOU 1783  C   GLU A 229    11213  10051   9555    491   -279   -628       C  
ATOM   1784  O   GLU A 229      15.580  32.107  36.527  1.00 82.02           O  
ANISOU 1784  O   GLU A 229    11422  10114   9627    473   -334   -612       O  
ATOM   1785  CB  GLU A 229      13.788  34.671  37.693  1.00 90.06           C  
ANISOU 1785  CB  GLU A 229    12346  11132  10740    738   -129   -604       C  
ATOM   1786  CG  GLU A 229      13.293  35.824  36.836  1.00 98.24           C  
ANISOU 1786  CG  GLU A 229    13405  12133  11788    932   -112   -546       C  
ATOM   1787  CD  GLU A 229      14.077  35.985  35.545  1.00104.80           C  
ANISOU 1787  CD  GLU A 229    14358  12898  12564    969   -183   -510       C  
ATOM   1788  OE1 GLU A 229      14.985  35.167  35.291  1.00106.43           O  
ANISOU 1788  OE1 GLU A 229    14627  13086  12726    846   -243   -533       O  
ATOM   1789  OE2 GLU A 229      13.781  36.932  34.781  1.00113.80           O  
ANISOU 1789  OE2 GLU A 229    15533  14003  13704   1129   -169   -451       O  
ATOM   1790  N   VAL A 230      14.928  32.039  38.690  1.00 73.42           N  
ANISOU 1790  N   VAL A 230    10208   9092   8596    385   -213   -663       N  
ATOM   1791  CA  VAL A 230      16.082  31.255  39.115  1.00 68.51           C  
ANISOU 1791  CA  VAL A 230     9652   8436   7944    249   -206   -671       C  
ATOM   1792  C   VAL A 230      16.157  30.037  38.231  1.00 70.45           C  
ANISOU 1792  C   VAL A 230     9885   8707   8177    198   -311   -652       C  
ATOM   1793  O   VAL A 230      17.232  29.647  37.797  1.00 72.25           O  
ANISOU 1793  O   VAL A 230    10209   8869   8372    156   -322   -634       O  
ATOM   1794  CB  VAL A 230      16.003  30.834  40.603  1.00 68.25           C  
ANISOU 1794  CB  VAL A 230     9554   8452   7925    136   -138   -697       C  
ATOM   1795  CG1 VAL A 230      16.870  29.623  40.908  1.00 64.05           C  
ANISOU 1795  CG1 VAL A 230     9038   7926   7373      3   -162   -678       C  
ATOM   1796  CG2 VAL A 230      16.377  31.993  41.522  1.00 69.38           C  
ANISOU 1796  CG2 VAL A 230     9766   8545   8052    141    -16   -725       C  
ATOM   1797  N   THR A 231      15.006  29.463  37.913  1.00 71.32           N  
ANISOU 1797  N   THR A 231     9880   8911   8309    199   -381   -657       N  
ATOM   1798  CA  THR A 231      14.994  28.284  37.072  1.00 71.64           C  
ANISOU 1798  CA  THR A 231     9922   8971   8327    128   -471   -654       C  
ATOM   1799  C   THR A 231      15.518  28.577  35.678  1.00 73.03           C  
ANISOU 1799  C   THR A 231    10209   9086   8454    193   -526   -632       C  
ATOM   1800  O   THR A 231      16.316  27.781  35.143  1.00 73.85           O  
ANISOU 1800  O   THR A 231    10403   9131   8527    127   -544   -629       O  
ATOM   1801  CB  THR A 231      13.601  27.658  36.957  1.00 73.02           C  
ANISOU 1801  CB  THR A 231     9948   9276   8521     96   -540   -667       C  
ATOM   1802  OG1 THR A 231      13.054  27.491  38.275  1.00 77.52           O  
ANISOU 1802  OG1 THR A 231    10413   9904   9139     46   -478   -686       O  
ATOM   1803  CG2 THR A 231      13.703  26.291  36.247  1.00 70.09           C  
ANISOU 1803  CG2 THR A 231     9606   8907   8117    -23   -608   -680       C  
ATOM   1804  N   LYS A 232      15.085  29.692  35.074  1.00 70.54           N  
ANISOU 1804  N   LYS A 232     9893   8778   8131    326   -544   -610       N  
ATOM   1805  CA  LYS A 232      15.612  30.025  33.758  1.00 67.85           C  
ANISOU 1805  CA  LYS A 232     9665   8378   7736    389   -593   -584       C  
ATOM   1806  C   LYS A 232      17.111  30.254  33.879  1.00 66.19           C  
ANISOU 1806  C   LYS A 232     9605   8036   7508    370   -520   -580       C  
ATOM   1807  O   LYS A 232      17.890  29.756  33.060  1.00 60.60           O  
ANISOU 1807  O   LYS A 232     8995   7269   6759    338   -546   -572       O  
ATOM   1808  CB  LYS A 232      14.964  31.237  33.114  1.00 70.91           C  
ANISOU 1808  CB  LYS A 232    10035   8790   8118    548   -613   -543       C  
ATOM   1809  CG  LYS A 232      15.872  31.770  32.011  1.00 73.26           C  
ANISOU 1809  CG  LYS A 232    10488   8987   8359    610   -624   -515       C  
ATOM   1810  CD  LYS A 232      15.276  32.848  31.144  1.00 77.71           C  
ANISOU 1810  CD  LYS A 232    11048   9573   8904    770   -656   -457       C  
ATOM   1811  CE  LYS A 232      16.373  33.449  30.278  1.00 79.54           C  
ANISOU 1811  CE  LYS A 232    11458   9679   9085    821   -636   -435       C  
ATOM   1812  NZ  LYS A 232      17.068  32.418  29.465  1.00 78.75           N  
ANISOU 1812  NZ  LYS A 232    11440   9558   8925    715   -698   -453       N  
ATOM   1813  N   LEU A 233      17.513  31.006  34.904  1.00 66.57           N  
ANISOU 1813  N   LEU A 233     9668   8043   7582    382   -423   -587       N  
ATOM   1814  CA  LEU A 233      18.933  31.260  35.128  1.00 65.86           C  
ANISOU 1814  CA  LEU A 233     9700   7855   7470    345   -354   -579       C  
ATOM   1815  C   LEU A 233      19.713  29.957  35.263  1.00 64.34           C  
ANISOU 1815  C   LEU A 233     9520   7655   7270    227   -363   -570       C  
ATOM   1816  O   LEU A 233      20.789  29.815  34.696  1.00 62.09           O  
ANISOU 1816  O   LEU A 233     9336   7299   6955    217   -353   -544       O  
ATOM   1817  CB  LEU A 233      19.158  32.136  36.357  1.00 65.90           C  
ANISOU 1817  CB  LEU A 233     9707   7841   7490    334   -249   -597       C  
ATOM   1818  CG  LEU A 233      18.796  33.630  36.265  1.00 68.29           C  
ANISOU 1818  CG  LEU A 233    10056   8094   7796    456   -188   -602       C  
ATOM   1819  CD1 LEU A 233      19.445  34.345  37.443  1.00 68.41           C  
ANISOU 1819  CD1 LEU A 233    10126   8065   7802    392    -68   -632       C  
ATOM   1820  CD2 LEU A 233      19.232  34.298  34.958  1.00 66.35           C  
ANISOU 1820  CD2 LEU A 233     9927   7768   7516    555   -212   -569       C  
ATOM   1821  N   VAL A 234      19.149  28.991  35.979  1.00 65.24           N  
ANISOU 1821  N   VAL A 234     9534   7840   7415    145   -373   -584       N  
ATOM   1822  CA  VAL A 234      19.856  27.743  36.225  1.00 63.55           C  
ANISOU 1822  CA  VAL A 234     9333   7609   7202     43   -360   -563       C  
ATOM   1823  C   VAL A 234      19.991  26.917  34.956  1.00 64.42           C  
ANISOU 1823  C   VAL A 234     9511   7679   7288     37   -413   -558       C  
ATOM   1824  O   VAL A 234      21.080  26.414  34.650  1.00 68.84           O  
ANISOU 1824  O   VAL A 234    10157   8166   7835     12   -379   -524       O  
ATOM   1825  CB  VAL A 234      19.192  26.935  37.347  1.00 65.50           C  
ANISOU 1825  CB  VAL A 234     9465   7934   7488    -44   -345   -577       C  
ATOM   1826  CG1 VAL A 234      19.827  25.561  37.454  1.00 67.44           C  
ANISOU 1826  CG1 VAL A 234     9732   8152   7740   -134   -326   -544       C  
ATOM   1827  CG2 VAL A 234      19.321  27.686  38.679  1.00 66.11           C  
ANISOU 1827  CG2 VAL A 234     9502   8043   7574    -61   -274   -581       C  
ATOM   1828  N   THR A 235      18.899  26.798  34.204  1.00 64.89           N  
ANISOU 1828  N   THR A 235     9530   7790   7335     56   -492   -589       N  
ATOM   1829  CA  THR A 235      18.929  26.132  32.907  1.00 62.89           C  
ANISOU 1829  CA  THR A 235     9354   7505   7035     38   -547   -596       C  
ATOM   1830  C   THR A 235      20.038  26.699  32.041  1.00 59.79           C  
ANISOU 1830  C   THR A 235     9101   7013   6603    104   -526   -567       C  
ATOM   1831  O   THR A 235      20.846  25.960  31.513  1.00 60.27           O  
ANISOU 1831  O   THR A 235     9258   6997   6644     66   -498   -554       O  
ATOM   1832  CB  THR A 235      17.588  26.279  32.153  1.00 66.36           C  
ANISOU 1832  CB  THR A 235     9723   8044   7446     59   -649   -623       C  
ATOM   1833  OG1 THR A 235      16.600  25.457  32.774  1.00 67.80           O  
ANISOU 1833  OG1 THR A 235     9784   8318   7658    -32   -671   -653       O  
ATOM   1834  CG2 THR A 235      17.721  25.890  30.674  1.00 65.08           C  
ANISOU 1834  CG2 THR A 235     9667   7852   7210     45   -709   -631       C  
ATOM   1835  N   ASP A 236      20.063  28.017  31.896  1.00 60.38           N  
ANISOU 1835  N   ASP A 236     9191   7082   6668    206   -528   -554       N  
ATOM   1836  CA  ASP A 236      21.056  28.670  31.055  1.00 58.49           C  
ANISOU 1836  CA  ASP A 236     9084   6752   6388    269   -506   -526       C  
ATOM   1837  C   ASP A 236      22.468  28.424  31.596  1.00 57.06           C  
ANISOU 1837  C   ASP A 236     8962   6496   6222    225   -416   -494       C  
ATOM   1838  O   ASP A 236      23.368  28.035  30.848  1.00 57.03           O  
ANISOU 1838  O   ASP A 236     9059   6418   6191    220   -394   -470       O  
ATOM   1839  CB  ASP A 236      20.779  30.157  30.968  1.00 58.66           C  
ANISOU 1839  CB  ASP A 236     9111   6772   6404    383   -504   -516       C  
ATOM   1840  CG  ASP A 236      19.579  30.494  30.084  1.00 64.35           C  
ANISOU 1840  CG  ASP A 236     9789   7564   7096    458   -597   -515       C  
ATOM   1841  OD1 ASP A 236      19.330  31.719  29.918  1.00 69.45           O  
ANISOU 1841  OD1 ASP A 236    10448   8200   7741    573   -586   -491       O  
ATOM   1842  OD2 ASP A 236      18.884  29.577  29.565  1.00 62.37           O  
ANISOU 1842  OD2 ASP A 236     9494   7383   6821    402   -676   -533       O  
ATOM   1843  N   LEU A 237      22.655  28.603  32.902  1.00 57.16           N  
ANISOU 1843  N   LEU A 237     8906   6539   6273    188   -362   -487       N  
ATOM   1844  CA  LEU A 237      23.985  28.453  33.498  1.00 54.88           C  
ANISOU 1844  CA  LEU A 237     8648   6214   5990    141   -286   -439       C  
ATOM   1845  C   LEU A 237      24.466  27.001  33.455  1.00 54.66           C  
ANISOU 1845  C   LEU A 237     8624   6166   5979     77   -264   -405       C  
ATOM   1846  O   LEU A 237      25.646  26.740  33.293  1.00 52.45           O  
ANISOU 1846  O   LEU A 237     8400   5835   5694     71   -209   -348       O  
ATOM   1847  CB  LEU A 237      23.985  28.968  34.918  1.00 54.13           C  
ANISOU 1847  CB  LEU A 237     8476   6176   5915     98   -240   -441       C  
ATOM   1848  CG  LEU A 237      25.335  28.854  35.628  1.00 54.83           C  
ANISOU 1848  CG  LEU A 237     8573   6265   5995     32   -172   -380       C  
ATOM   1849  CD1 LEU A 237      26.334  29.780  34.945  1.00 51.26           C  
ANISOU 1849  CD1 LEU A 237     8225   5746   5503     73   -144   -358       C  
ATOM   1850  CD2 LEU A 237      25.168  29.127  37.121  1.00 53.37           C  
ANISOU 1850  CD2 LEU A 237     8302   6161   5816    -41   -137   -388       C  
ATOM   1851  N   THR A 238      23.547  26.057  33.582  1.00 55.38           N  
ANISOU 1851  N   THR A 238     8657   6294   6092     31   -296   -435       N  
ATOM   1852  CA  THR A 238      23.904  24.655  33.459  1.00 56.39           C  
ANISOU 1852  CA  THR A 238     8810   6379   6236    -27   -259   -407       C  
ATOM   1853  C   THR A 238      24.359  24.298  32.051  1.00 59.14           C  
ANISOU 1853  C   THR A 238     9290   6633   6546      1   -255   -409       C  
ATOM   1854  O   THR A 238      25.301  23.497  31.873  1.00 61.40           O  
ANISOU 1854  O   THR A 238     9640   6844   6844    -11   -179   -356       O  
ATOM   1855  CB  THR A 238      22.727  23.744  33.865  1.00 57.03           C  
ANISOU 1855  CB  THR A 238     8812   6514   6341    -98   -289   -451       C  
ATOM   1856  OG1 THR A 238      22.418  23.971  35.250  1.00 59.14           O  
ANISOU 1856  OG1 THR A 238     8963   6864   6644   -129   -274   -443       O  
ATOM   1857  CG2 THR A 238      23.080  22.273  33.677  1.00 53.87           C  
ANISOU 1857  CG2 THR A 238     8466   6044   5958   -160   -230   -427       C  
ATOM   1858  N   LYS A 239      23.706  24.884  31.050  1.00 60.45           N  
ANISOU 1858  N   LYS A 239     9498   6805   6665     41   -330   -459       N  
ATOM   1859  CA  LYS A 239      24.043  24.573  29.659  1.00 61.56           C  
ANISOU 1859  CA  LYS A 239     9773   6865   6752     55   -333   -469       C  
ATOM   1860  C   LYS A 239      25.434  25.104  29.399  1.00 60.74           C  
ANISOU 1860  C   LYS A 239     9752   6686   6642    114   -263   -409       C  
ATOM   1861  O   LYS A 239      26.250  24.420  28.781  1.00 60.76           O  
ANISOU 1861  O   LYS A 239     9851   6599   6634    110   -197   -382       O  
ATOM   1862  CB  LYS A 239      23.030  25.163  28.666  1.00 60.73           C  
ANISOU 1862  CB  LYS A 239     9682   6809   6583     85   -439   -522       C  
ATOM   1863  CG  LYS A 239      23.380  24.869  27.216  1.00 62.79           C  
ANISOU 1863  CG  LYS A 239    10091   6995   6770     86   -443   -535       C  
ATOM   1864  CD  LYS A 239      22.377  25.407  26.182  1.00 62.28           C  
ANISOU 1864  CD  LYS A 239    10035   7001   6626    108   -559   -572       C  
ATOM   1865  N   VAL A 240      25.704  26.304  29.906  1.00 56.81           N  
ANISOU 1865  N   VAL A 240     9216   6220   6151    163   -266   -389       N  
ATOM   1866  CA  VAL A 240      27.023  26.906  29.776  1.00 55.14           C  
ANISOU 1866  CA  VAL A 240     9067   5954   5931    201   -201   -332       C  
ATOM   1867  C   VAL A 240      28.074  25.919  30.278  1.00 53.52           C  
ANISOU 1867  C   VAL A 240     8850   5721   5765    162   -110   -259       C  
ATOM   1868  O   VAL A 240      29.052  25.609  29.577  1.00 53.22           O  
ANISOU 1868  O   VAL A 240     8899   5607   5717    186    -47   -212       O  
ATOM   1869  CB  VAL A 240      27.103  28.249  30.549  1.00 53.50           C  
ANISOU 1869  CB  VAL A 240     8810   5793   5726    223   -202   -329       C  
ATOM   1870  CG1 VAL A 240      28.534  28.726  30.694  1.00 52.07           C  
ANISOU 1870  CG1 VAL A 240     8668   5579   5537    222   -127   -265       C  
ATOM   1871  CG2 VAL A 240      26.273  29.310  29.863  1.00 53.13           C  
ANISOU 1871  CG2 VAL A 240     8799   5745   5642    295   -265   -376       C  
ATOM   1872  N   HIS A 241      27.864  25.402  31.478  1.00 52.10           N  
ANISOU 1872  N   HIS A 241     8561   5604   5630    108    -95   -238       N  
ATOM   1873  CA  HIS A 241      28.842  24.484  32.045  1.00 53.54           C  
ANISOU 1873  CA  HIS A 241     8715   5774   5852     83     -7   -145       C  
ATOM   1874  C   HIS A 241      28.921  23.155  31.284  1.00 54.98           C  
ANISOU 1874  C   HIS A 241     8981   5860   6049     82     48   -136       C  
ATOM   1875  O   HIS A 241      30.016  22.699  30.949  1.00 54.81           O  
ANISOU 1875  O   HIS A 241     9010   5772   6041    114    139    -57       O  
ATOM   1876  CB  HIS A 241      28.606  24.302  33.527  1.00 54.31           C  
ANISOU 1876  CB  HIS A 241     8680   5971   5985     24     -5   -117       C  
ATOM   1877  CG  HIS A 241      28.916  25.538  34.319  1.00 58.81           C  
ANISOU 1877  CG  HIS A 241     9192   6621   6533      9    -20   -109       C  
ATOM   1878  ND1 HIS A 241      30.128  26.197  34.236  1.00 58.35           N  
ANISOU 1878  ND1 HIS A 241     9156   6563   6450     20     21    -47       N  
ATOM   1879  CD2 HIS A 241      28.167  26.238  35.200  1.00 60.36           C  
ANISOU 1879  CD2 HIS A 241     9317   6895   6723    -26    -59   -161       C  
ATOM   1880  CE1 HIS A 241      30.101  27.254  35.024  1.00 59.40           C  
ANISOU 1880  CE1 HIS A 241     9246   6768   6556    -20      5    -69       C  
ATOM   1881  NE2 HIS A 241      28.928  27.298  35.625  1.00 61.42           N  
ANISOU 1881  NE2 HIS A 241     9448   7065   6823    -44    -38   -138       N  
ATOM   1882  N   LYS A 242      27.783  22.551  30.970  1.00 53.66           N  
ANISOU 1882  N   LYS A 242     8832   5682   5875     42      4   -216       N  
ATOM   1883  CA  LYS A 242      27.804  21.312  30.200  1.00 53.75           C  
ANISOU 1883  CA  LYS A 242     8948   5588   5886     19     67   -227       C  
ATOM   1884  C   LYS A 242      28.616  21.503  28.934  1.00 53.45           C  
ANISOU 1884  C   LYS A 242     9051   5452   5806     75    111   -217       C  
ATOM   1885  O   LYS A 242      29.417  20.661  28.571  1.00 55.12           O  
ANISOU 1885  O   LYS A 242     9343   5563   6037     91    225   -164       O  
ATOM   1886  CB  LYS A 242      26.383  20.876  29.855  1.00 55.96           C  
ANISOU 1886  CB  LYS A 242     9238   5889   6137    -53     -9   -334       C  
ATOM   1887  CG  LYS A 242      26.286  19.534  29.156  1.00 60.74           C  
ANISOU 1887  CG  LYS A 242     9963   6383   6731   -111     64   -364       C  
ATOM   1888  CD  LYS A 242      24.912  19.282  28.525  1.00 61.54           C  
ANISOU 1888  CD  LYS A 242    10089   6522   6772   -201    -30   -481       C  
ATOM   1889  N   GLU A 243      28.451  22.640  28.283  1.00 54.74           N  
ANISOU 1889  N   GLU A 243     9245   5641   5914    112     33   -260       N  
ATOM   1890  CA  GLU A 243      29.212  22.928  27.069  1.00 53.91           C  
ANISOU 1890  CA  GLU A 243     9276   5449   5760    164     71   -251       C  
ATOM   1891  C   GLU A 243      30.721  23.030  27.304  1.00 50.34           C  
ANISOU 1891  C   GLU A 243     8822   4960   5346    217    180   -139       C  
ATOM   1892  O   GLU A 243      31.508  22.375  26.624  1.00 46.97           O  
ANISOU 1892  O   GLU A 243     8495   4431   4921    243    284   -100       O  
ATOM   1893  CB  GLU A 243      28.700  24.197  26.389  1.00 57.83           C  
ANISOU 1893  CB  GLU A 243     9799   5985   6189    199    -35   -306       C  
ATOM   1894  CG  GLU A 243      27.300  24.118  25.788  1.00 63.54           C  
ANISOU 1894  CG  GLU A 243    10536   6751   6854    159   -144   -401       C  
ATOM   1895  CD  GLU A 243      27.168  23.141  24.633  1.00 70.82           C  
ANISOU 1895  CD  GLU A 243    11599   7593   7716    107   -118   -449       C  
ATOM   1896  OE1 GLU A 243      28.169  22.856  23.924  1.00 76.87           O  
ANISOU 1896  OE1 GLU A 243    12491   8251   8465    133    -21   -418       O  
ATOM   1897  OE2 GLU A 243      26.031  22.663  24.416  1.00 82.03           O  
ANISOU 1897  OE2 GLU A 243    13008   9062   9098     32   -191   -520       O  
ATOM   1898  N   CYS A 244      31.128  23.814  28.293  1.00 51.25           N  
ANISOU 1898  N   CYS A 244     8822   5163   5488    226    164    -85       N  
ATOM   1899  CA  CYS A 244      32.565  23.892  28.637  1.00 51.06           C  
ANISOU 1899  CA  CYS A 244     8765   5140   5496    259    258     35       C  
ATOM   1900  C   CYS A 244      33.127  22.525  29.019  1.00 49.47           C  
ANISOU 1900  C   CYS A 244     8541   4899   5358    262    372    128       C  
ATOM   1901  O   CYS A 244      34.204  22.138  28.575  1.00 47.88           O  
ANISOU 1901  O   CYS A 244     8385   4632   5175    313    481    215       O  
ATOM   1902  CB  CYS A 244      32.822  24.892  29.760  1.00 54.65           C  
ANISOU 1902  CB  CYS A 244     9094   5715   5955    233    218     70       C  
ATOM   1903  SG  CYS A 244      33.416  26.498  29.178  1.00 60.49           S  
ANISOU 1903  SG  CYS A 244     9893   6456   6636    261    196     56       S  
ATOM   1904  N   CYS A 245      32.377  21.775  29.817  1.00 48.28           N  
ANISOU 1904  N   CYS A 245     8323   4779   5243    214    358    114       N  
ATOM   1905  CA  CYS A 245      32.845  20.478  30.276  1.00 48.91           C  
ANISOU 1905  CA  CYS A 245     8380   4816   5387    223    474    213       C  
ATOM   1906  C   CYS A 245      33.006  19.456  29.167  1.00 50.38           C  
ANISOU 1906  C   CYS A 245     8727   4839   5577    252    584    199       C  
ATOM   1907  O   CYS A 245      33.954  18.672  29.196  1.00 50.23           O  
ANISOU 1907  O   CYS A 245     8721   4754   5609    307    725    316       O  
ATOM   1908  CB  CYS A 245      31.958  19.976  31.396  1.00 50.26           C  
ANISOU 1908  CB  CYS A 245     8450   5057   5589    158    434    197       C  
ATOM   1909  SG  CYS A 245      32.158  20.984  32.916  1.00 50.65           S  
ANISOU 1909  SG  CYS A 245     8309   5296   5638    123    358    256       S  
ATOM   1910  N   HIS A 246      32.151  19.520  28.147  1.00 52.82           N  
ANISOU 1910  N   HIS A 246     9160   5086   5824    217    528     64       N  
ATOM   1911  CA  HIS A 246      32.297  18.663  26.937  1.00 55.08           C  
ANISOU 1911  CA  HIS A 246     9631   5211   6086    223    633     27       C  
ATOM   1912  C   HIS A 246      33.250  19.176  25.874  1.00 51.68           C  
ANISOU 1912  C   HIS A 246     9305   4714   5618    292    688     51       C  
ATOM   1913  O   HIS A 246      33.369  18.588  24.818  1.00 52.35           O  
ANISOU 1913  O   HIS A 246     9555   4667   5669    292    775     11       O  
ATOM   1914  CB  HIS A 246      30.933  18.376  26.316  1.00 58.01           C  
ANISOU 1914  CB  HIS A 246    10090   5561   6390    127    549   -127       C  
ATOM   1915  CG  HIS A 246      30.166  17.399  27.120  1.00 65.84           C  
ANISOU 1915  CG  HIS A 246    11032   6559   7425     53    563   -144       C  
ATOM   1916  ND1 HIS A 246      29.826  16.150  26.641  1.00 74.10           N  
ANISOU 1916  ND1 HIS A 246    12213   7476   8465    -12    662   -194       N  
ATOM   1917  CD2 HIS A 246      29.801  17.422  28.426  1.00 68.01           C  
ANISOU 1917  CD2 HIS A 246    11145   6940   7754     33    516   -105       C  
ATOM   1918  CE1 HIS A 246      29.217  15.472  27.598  1.00 75.27           C  
ANISOU 1918  CE1 HIS A 246    12282   7655   8663    -71    666   -190       C  
ATOM   1919  NE2 HIS A 246      29.187  16.224  28.689  1.00 73.95           N  
ANISOU 1919  NE2 HIS A 246    11931   7633   8533    -41    575   -134       N  
ATOM   1920  N   GLY A 247      33.930  20.270  26.155  1.00 49.97           N  
ANISOU 1920  N   GLY A 247     9000   4585   5402    339    646    113       N  
ATOM   1921  CA  GLY A 247      34.950  20.761  25.250  1.00 51.99           C  
ANISOU 1921  CA  GLY A 247     9339   4784   5630    405    711    153       C  
ATOM   1922  C   GLY A 247      34.462  21.676  24.137  1.00 52.61           C  
ANISOU 1922  C   GLY A 247     9531   4849   5611    393    615     42       C  
ATOM   1923  O   GLY A 247      35.246  22.021  23.248  1.00 51.98           O  
ANISOU 1923  O   GLY A 247     9545   4706   5498    442    675     64       O  
ATOM   1924  N   ASP A 248      33.192  22.094  24.189  1.00 54.46           N  
ANISOU 1924  N   ASP A 248     9746   5148   5799    336    470    -66       N  
ATOM   1925  CA  ASP A 248      32.660  23.046  23.220  1.00 55.41           C  
ANISOU 1925  CA  ASP A 248     9949   5279   5826    336    366   -151       C  
ATOM   1926  C   ASP A 248      32.826  24.455  23.809  1.00 53.36           C  
ANISOU 1926  C   ASP A 248     9584   5121   5571    368    287   -121       C  
ATOM   1927  O   ASP A 248      31.855  25.124  24.189  1.00 52.05           O  
ANISOU 1927  O   ASP A 248     9351   5039   5387    349    168   -177       O  
ATOM   1928  CB  ASP A 248      31.206  22.733  22.860  1.00 58.70           C  
ANISOU 1928  CB  ASP A 248    10400   5721   6184    263    259   -267       C  
ATOM   1929  CG  ASP A 248      30.728  23.454  21.581  1.00 64.11           C  
ANISOU 1929  CG  ASP A 248    11198   6404   6755    266    172   -338       C  
ATOM   1930  OD1 ASP A 248      31.343  24.502  21.201  1.00 61.13           O  
ANISOU 1930  OD1 ASP A 248    10846   6026   6353    333    167   -303       O  
ATOM   1931  OD2 ASP A 248      29.744  22.948  20.952  1.00 72.74           O  
ANISOU 1931  OD2 ASP A 248    12357   7503   7778    194    112   -425       O  
ATOM   1932  N   LEU A 249      34.073  24.925  23.798  1.00 51.05           N  
ANISOU 1932  N   LEU A 249     9289   4813   5296    416    365    -35       N  
ATOM   1933  CA  LEU A 249      34.434  26.196  24.416  1.00 51.04           C  
ANISOU 1933  CA  LEU A 249     9200   4894   5297    425    321     -2       C  
ATOM   1934  C   LEU A 249      33.804  27.439  23.766  1.00 49.82           C  
ANISOU 1934  C   LEU A 249     9112   4748   5070    444    222    -75       C  
ATOM   1935  O   LEU A 249      33.464  28.404  24.461  1.00 49.36           O  
ANISOU 1935  O   LEU A 249     8978   4762   5015    435    159    -88       O  
ATOM   1936  CB  LEU A 249      35.962  26.358  24.419  1.00 50.21           C  
ANISOU 1936  CB  LEU A 249     9084   4776   5217    457    433    109       C  
ATOM   1937  CG  LEU A 249      36.720  25.219  25.081  1.00 49.58           C  
ANISOU 1937  CG  LEU A 249     8921   4701   5215    462    542    217       C  
ATOM   1938  CD1 LEU A 249      38.196  25.579  25.098  1.00 49.28           C  
ANISOU 1938  CD1 LEU A 249     8844   4686   5195    493    636    339       C  
ATOM   1939  CD2 LEU A 249      36.202  24.952  26.487  1.00 46.09           C  
ANISOU 1939  CD2 LEU A 249     8326   4364   4821    411    491    233       C  
ATOM   1940  N   LEU A 250      33.659  27.420  22.449  1.00 47.69           N  
ANISOU 1940  N   LEU A 250     8987   4402   4732    470    219   -117       N  
ATOM   1941  CA  LEU A 250      33.028  28.529  21.765  1.00 47.95           C  
ANISOU 1941  CA  LEU A 250     9084   4445   4692    500    127   -168       C  
ATOM   1942  C   LEU A 250      31.586  28.609  22.203  1.00 48.67           C  
ANISOU 1942  C   LEU A 250     9097   4615   4778    479      6   -233       C  
ATOM   1943  O   LEU A 250      31.120  29.663  22.580  1.00 51.24           O  
ANISOU 1943  O   LEU A 250     9374   4993   5102    505    -55   -242       O  
ATOM   1944  CB  LEU A 250      33.111  28.377  20.253  1.00 47.38           C  
ANISOU 1944  CB  LEU A 250     9182   4290   4532    522    143   -194       C  
ATOM   1945  CG  LEU A 250      34.526  28.187  19.722  1.00 46.88           C  
ANISOU 1945  CG  LEU A 250     9202   4139   4473    547    280   -130       C  
ATOM   1946  CD1 LEU A 250      34.535  27.584  18.314  1.00 48.42           C  
ANISOU 1946  CD1 LEU A 250     9572   4240   4584    547    320   -169       C  
ATOM   1947  CD2 LEU A 250      35.240  29.517  19.753  1.00 44.71           C  
ANISOU 1947  CD2 LEU A 250     8926   3873   4190    584    292    -85       C  
ATOM   1948  N   GLU A 251      30.867  27.501  22.220  1.00 51.24           N  
ANISOU 1948  N   GLU A 251     9409   4952   5109    429    -17   -275       N  
ATOM   1949  CA  GLU A 251      29.452  27.590  22.599  1.00 53.19           C  
ANISOU 1949  CA  GLU A 251     9570   5291   5350    405   -135   -332       C  
ATOM   1950  C   GLU A 251      29.316  27.967  24.057  1.00 53.91           C  
ANISOU 1950  C   GLU A 251     9509   5456   5521    398   -143   -312       C  
ATOM   1951  O   GLU A 251      28.394  28.672  24.425  1.00 56.80           O  
ANISOU 1951  O   GLU A 251     9804   5893   5885    415   -223   -340       O  
ATOM   1952  CB  GLU A 251      28.669  26.315  22.305  1.00 54.62           C  
ANISOU 1952  CB  GLU A 251     9769   5474   5510    329   -158   -389       C  
ATOM   1953  CG  GLU A 251      27.186  26.588  22.368  1.00 57.20           C  
ANISOU 1953  CG  GLU A 251    10016   5912   5807    310   -294   -444       C  
ATOM   1954  CD  GLU A 251      26.281  25.441  21.965  1.00 61.53           C  
ANISOU 1954  CD  GLU A 251    10583   6484   6311    211   -336   -510       C  
ATOM   1955  OE1 GLU A 251      25.060  25.628  22.171  1.00 69.76           O  
ANISOU 1955  OE1 GLU A 251    11526   7640   7339    189   -447   -544       O  
ATOM   1956  OE2 GLU A 251      26.739  24.378  21.488  1.00 71.21           O  
ANISOU 1956  OE2 GLU A 251    11918   7620   7519    151   -253   -529       O  
ATOM   1957  N   CYS A 252      30.242  27.493  24.888  1.00 55.82           N  
ANISOU 1957  N   CYS A 252     9698   5685   5827    374    -53   -255       N  
ATOM   1958  CA  CYS A 252      30.273  27.845  26.308  1.00 53.24           C  
ANISOU 1958  CA  CYS A 252     9233   5435   5560    350    -52   -229       C  
ATOM   1959  C   CYS A 252      30.435  29.371  26.409  1.00 50.89           C  
ANISOU 1959  C   CYS A 252     8942   5153   5239    389    -70   -227       C  
ATOM   1960  O   CYS A 252      29.641  30.029  27.071  1.00 52.11           O  
ANISOU 1960  O   CYS A 252     9028   5368   5404    390   -121   -261       O  
ATOM   1961  CB  CYS A 252      31.416  27.089  26.988  1.00 54.03           C  
ANISOU 1961  CB  CYS A 252     9286   5526   5715    322     51   -145       C  
ATOM   1962  SG  CYS A 252      31.743  27.534  28.701  1.00 58.10           S  
ANISOU 1962  SG  CYS A 252     9643   6153   6280    273     61    -94       S  
ATOM   1963  N   ALA A 253      31.410  29.924  25.699  1.00 47.52           N  
ANISOU 1963  N   ALA A 253     8611   4666   4781    423    -19   -192       N  
ATOM   1964  CA  ALA A 253      31.664  31.369  25.742  1.00 50.94           C  
ANISOU 1964  CA  ALA A 253     9074   5093   5189    450    -15   -190       C  
ATOM   1965  C   ALA A 253      30.465  32.194  25.288  1.00 52.82           C  
ANISOU 1965  C   ALA A 253     9344   5335   5391    510    -97   -244       C  
ATOM   1966  O   ALA A 253      30.069  33.166  25.941  1.00 54.97           O  
ANISOU 1966  O   ALA A 253     9580   5633   5674    522   -105   -260       O  
ATOM   1967  CB  ALA A 253      32.886  31.743  24.929  1.00 47.44           C  
ANISOU 1967  CB  ALA A 253     8735   4579   4712    471     57   -142       C  
ATOM   1968  N   ASP A 254      29.877  31.796  24.176  1.00 57.20           N  
ANISOU 1968  N   ASP A 254     9968   5868   5899    547   -152   -268       N  
ATOM   1969  CA  ASP A 254      28.760  32.521  23.613  1.00 59.76           C  
ANISOU 1969  CA  ASP A 254    10312   6215   6181    614   -237   -295       C  
ATOM   1970  C   ASP A 254      27.581  32.406  24.575  1.00 57.26           C  
ANISOU 1970  C   ASP A 254     9856   5989   5909    601   -296   -328       C  
ATOM   1971  O   ASP A 254      26.955  33.401  24.932  1.00 52.49           O  
ANISOU 1971  O   ASP A 254     9218   5409   5316    656   -314   -332       O  
ATOM   1972  CB  ASP A 254      28.424  31.947  22.238  1.00 64.85           C  
ANISOU 1972  CB  ASP A 254    11049   6843   6749    628   -290   -309       C  
ATOM   1973  CG  ASP A 254      27.357  32.736  21.509  1.00 75.77           C  
ANISOU 1973  CG  ASP A 254    12450   8267   8073    705   -384   -312       C  
ATOM   1974  OD1 ASP A 254      26.885  33.763  22.058  1.00 72.83           O  
ANISOU 1974  OD1 ASP A 254    12024   7917   7729    767   -393   -299       O  
ATOM   1975  OD2 ASP A 254      27.008  32.312  20.366  1.00 83.08           O  
ANISOU 1975  OD2 ASP A 254    13448   9202   8917    703   -441   -322       O  
ATOM   1976  N   ASP A 255      27.303  31.187  25.017  1.00 56.70           N  
ANISOU 1976  N   ASP A 255     9712   5962   5870    529   -311   -349       N  
ATOM   1977  CA  ASP A 255      26.148  30.951  25.871  1.00 58.93           C  
ANISOU 1977  CA  ASP A 255     9861   6336   6193    507   -367   -381       C  
ATOM   1978  C   ASP A 255      26.250  31.731  27.180  1.00 58.98           C  
ANISOU 1978  C   ASP A 255     9790   6366   6255    505   -320   -376       C  
ATOM   1979  O   ASP A 255      25.240  32.203  27.726  1.00 57.50           O  
ANISOU 1979  O   ASP A 255     9520   6238   6090    533   -355   -398       O  
ATOM   1980  CB  ASP A 255      26.006  29.462  26.140  1.00 57.21           C  
ANISOU 1980  CB  ASP A 255     9596   6141   5999    417   -368   -401       C  
ATOM   1981  N   ARG A 256      27.486  31.924  27.645  1.00 61.12           N  
ANISOU 1981  N   ARG A 256    10089   6593   6539    470   -235   -343       N  
ATOM   1982  CA  ARG A 256      27.732  32.669  28.879  1.00 59.23           C  
ANISOU 1982  CA  ARG A 256     9795   6380   6331    438   -183   -343       C  
ATOM   1983  C   ARG A 256      27.544  34.156  28.683  1.00 57.11           C  
ANISOU 1983  C   ARG A 256     9593   6067   6040    508   -163   -353       C  
ATOM   1984  O   ARG A 256      26.988  34.824  29.538  1.00 58.79           O  
ANISOU 1984  O   ARG A 256     9758   6305   6275    511   -143   -379       O  
ATOM   1985  CB  ARG A 256      29.147  32.422  29.367  1.00 58.80           C  
ANISOU 1985  CB  ARG A 256     9744   6315   6284    364   -105   -294       C  
ATOM   1986  CG  ARG A 256      29.387  32.873  30.795  1.00 57.50           C  
ANISOU 1986  CG  ARG A 256     9501   6208   6137    287    -61   -294       C  
ATOM   1987  CD  ARG A 256      30.852  33.176  30.975  1.00 59.73           C  
ANISOU 1987  CD  ARG A 256     9814   6483   6398    227     11   -240       C  
ATOM   1988  NE  ARG A 256      31.270  33.330  32.362  1.00 58.63           N  
ANISOU 1988  NE  ARG A 256     9588   6427   6261    119     49   -226       N  
ATOM   1989  CZ  ARG A 256      32.425  33.880  32.731  1.00 60.75           C  
ANISOU 1989  CZ  ARG A 256     9869   6719   6495     41    108   -186       C  
ATOM   1990  NH1 ARG A 256      33.279  34.379  31.830  1.00 62.69           N  
ANISOU 1990  NH1 ARG A 256    10209   6899   6711     65    142   -159       N  
ATOM   1991  NH2 ARG A 256      32.724  33.949  34.020  1.00 64.39           N  
ANISOU 1991  NH2 ARG A 256    10244   7278   6943    -74    131   -174       N  
ATOM   1992  N   ALA A 257      28.016  34.684  27.560  1.00 57.06           N  
ANISOU 1992  N   ALA A 257     9707   5986   5987    567   -154   -331       N  
ATOM   1993  CA  ALA A 257      27.825  36.114  27.278  1.00 56.36           C  
ANISOU 1993  CA  ALA A 257     9701   5838   5877    647   -124   -332       C  
ATOM   1994  C   ALA A 257      26.352  36.416  27.120  1.00 57.50           C  
ANISOU 1994  C   ALA A 257     9794   6022   6031    743   -189   -346       C  
ATOM   1995  O   ALA A 257      25.884  37.437  27.620  1.00 60.45           O  
ANISOU 1995  O   ALA A 257    10170   6376   6424    793   -144   -355       O  
ATOM   1996  CB  ALA A 257      28.610  36.577  26.081  1.00 51.44           C  
ANISOU 1996  CB  ALA A 257     9218   5128   5199    692   -100   -299       C  
ATOM   1997  N   ASP A 258      25.612  35.511  26.484  1.00 59.06           N  
ANISOU 1997  N   ASP A 258     9943   6281   6215    759   -285   -347       N  
ATOM   1998  CA  ASP A 258      24.178  35.714  26.343  1.00 63.28           C  
ANISOU 1998  CA  ASP A 258    10400   6888   6757    841   -358   -347       C  
ATOM   1999  C   ASP A 258      23.551  35.797  27.707  1.00 63.85           C  
ANISOU 1999  C   ASP A 258    10350   7013   6895    815   -329   -378       C  
ATOM   2000  O   ASP A 258      22.703  36.661  27.944  1.00 66.77           O  
ANISOU 2000  O   ASP A 258    10687   7395   7287    907   -316   -369       O  
ATOM   2001  CB  ASP A 258      23.492  34.593  25.578  1.00 65.73           C  
ANISOU 2001  CB  ASP A 258    10661   7279   7033    818   -470   -353       C  
ATOM   2002  CG  ASP A 258      23.844  34.570  24.101  1.00 69.07           C  
ANISOU 2002  CG  ASP A 258    11207   7663   7372    852   -509   -325       C  
ATOM   2003  OD1 ASP A 258      24.529  35.505  23.624  1.00 77.24           O  
ANISOU 2003  OD1 ASP A 258    12358   8609   8381    913   -455   -294       O  
ATOM   2004  OD2 ASP A 258      23.427  33.588  23.417  1.00 74.53           O  
ANISOU 2004  OD2 ASP A 258    11887   8414   8019    803   -590   -340       O  
ATOM   2005  N   LEU A 259      23.986  34.919  28.611  1.00 63.10           N  
ANISOU 2005  N   LEU A 259    10194   6949   6831    697   -309   -405       N  
ATOM   2006  CA  LEU A 259      23.399  34.868  29.951  1.00 62.22           C  
ANISOU 2006  CA  LEU A 259     9967   6899   6775    655   -282   -436       C  
ATOM   2007  C   LEU A 259      23.659  36.144  30.730  1.00 62.30           C  
ANISOU 2007  C   LEU A 259    10022   6850   6797    674   -177   -448       C  
ATOM   2008  O   LEU A 259      22.801  36.596  31.466  1.00 65.72           O  
ANISOU 2008  O   LEU A 259    10391   7314   7267    706   -149   -469       O  
ATOM   2009  CB  LEU A 259      23.889  33.661  30.743  1.00 61.04           C  
ANISOU 2009  CB  LEU A 259     9751   6793   6648    526   -277   -449       C  
ATOM   2010  CG  LEU A 259      23.419  33.620  32.215  1.00 61.95           C  
ANISOU 2010  CG  LEU A 259     9757   6973   6810    466   -240   -478       C  
ATOM   2011  CD1 LEU A 259      21.909  33.420  32.267  1.00 61.08           C  
ANISOU 2011  CD1 LEU A 259     9534   6943   6729    516   -303   -498       C  
ATOM   2012  CD2 LEU A 259      24.142  32.557  33.041  1.00 57.39           C  
ANISOU 2012  CD2 LEU A 259     9128   6431   6246    341   -220   -470       C  
ATOM   2013  N   ALA A 260      24.831  36.735  30.562  1.00 61.82           N  
ANISOU 2013  N   ALA A 260    10079   6704   6704    647   -109   -436       N  
ATOM   2014  CA  ALA A 260      25.116  38.001  31.218  1.00 60.57           C  
ANISOU 2014  CA  ALA A 260     9993   6478   6545    645      3   -456       C  
ATOM   2015  C   ALA A 260      24.230  39.131  30.665  1.00 62.75           C  
ANISOU 2015  C   ALA A 260    10323   6693   6826    801     27   -443       C  
ATOM   2016  O   ALA A 260      23.645  39.894  31.451  1.00 62.08           O  
ANISOU 2016  O   ALA A 260    10229   6588   6771    832    106   -469       O  
ATOM   2017  CB  ALA A 260      26.583  38.337  31.082  1.00 60.72           C  
ANISOU 2017  CB  ALA A 260    10121   6430   6520    565     65   -444       C  
ATOM   2018  N   LYS A 261      24.105  39.224  29.331  1.00 61.80           N  
ANISOU 2018  N   LYS A 261    10259   6546   6677    905    -33   -395       N  
ATOM   2019  CA  LYS A 261      23.204  40.214  28.722  1.00 61.82           C  
ANISOU 2019  CA  LYS A 261    10295   6510   6684   1073    -22   -355       C  
ATOM   2020  C   LYS A 261      21.813  40.043  29.334  1.00 62.50           C  
ANISOU 2020  C   LYS A 261    10231   6692   6826   1131    -51   -360       C  
ATOM   2021  O   LYS A 261      21.249  41.004  29.878  1.00 65.94           O  
ANISOU 2021  O   LYS A 261    10675   7082   7298   1213     44   -360       O  
ATOM   2022  CB  LYS A 261      23.158  40.149  27.176  1.00 60.00           C  
ANISOU 2022  CB  LYS A 261    10122   6275   6401   1166   -109   -293       C  
ATOM   2023  N   TYR A 262      21.287  38.823  29.344  1.00 60.63           N  
ANISOU 2023  N   TYR A 262     9860   6581   6598   1080   -164   -368       N  
ATOM   2024  CA  TYR A 262      19.953  38.625  29.900  1.00 63.48           C  
ANISOU 2024  CA  TYR A 262    10064   7046   7010   1126   -194   -369       C  
ATOM   2025  C   TYR A 262      19.874  39.070  31.375  1.00 65.49           C  
ANISOU 2025  C   TYR A 262    10294   7274   7316   1080    -72   -421       C  
ATOM   2026  O   TYR A 262      18.908  39.725  31.789  1.00 64.70           O  
ANISOU 2026  O   TYR A 262    10139   7183   7260   1183    -16   -409       O  
ATOM   2027  CB  TYR A 262      19.500  37.176  29.766  1.00 64.35           C  
ANISOU 2027  CB  TYR A 262    10046   7289   7116   1041   -322   -382       C  
ATOM   2028  CG  TYR A 262      18.178  36.889  30.432  1.00 66.95           C  
ANISOU 2028  CG  TYR A 262    10202   7737   7498   1063   -351   -387       C  
ATOM   2029  CD1 TYR A 262      16.978  37.012  29.738  1.00 67.96           C  
ANISOU 2029  CD1 TYR A 262    10230   7965   7625   1179   -433   -329       C  
ATOM   2030  CD2 TYR A 262      18.129  36.499  31.766  1.00 69.72           C  
ANISOU 2030  CD2 TYR A 262    10481   8114   7895    965   -295   -442       C  
ATOM   2031  CE1 TYR A 262      15.771  36.743  30.356  1.00 71.74           C  
ANISOU 2031  CE1 TYR A 262    10536   8567   8156   1196   -455   -327       C  
ATOM   2032  CE2 TYR A 262      16.928  36.245  32.400  1.00 70.86           C  
ANISOU 2032  CE2 TYR A 262    10468   8367   8090    982   -311   -447       C  
ATOM   2033  CZ  TYR A 262      15.754  36.361  31.695  1.00 73.87           C  
ANISOU 2033  CZ  TYR A 262    10745   8846   8477   1097   -389   -391       C  
ATOM   2034  OH  TYR A 262      14.570  36.098  32.343  1.00 80.08           O  
ANISOU 2034  OH  TYR A 262    11359   9751   9315   1110   -400   -391       O  
ATOM   2035  N   ILE A 263      20.880  38.720  32.167  1.00 62.90           N  
ANISOU 2035  N   ILE A 263    10004   6920   6976    927    -25   -473       N  
ATOM   2036  CA  ILE A 263      20.864  39.133  33.558  1.00 65.17           C  
ANISOU 2036  CA  ILE A 263    10281   7192   7290    860     89   -526       C  
ATOM   2037  C   ILE A 263      20.808  40.660  33.677  1.00 68.73           C  
ANISOU 2037  C   ILE A 263    10854   7515   7744    953    231   -529       C  
ATOM   2038  O   ILE A 263      19.952  41.198  34.374  1.00 73.44           O  
ANISOU 2038  O   ILE A 263    11413   8107   8384   1013    314   -546       O  
ATOM   2039  CB  ILE A 263      22.027  38.514  34.358  1.00 62.44           C  
ANISOU 2039  CB  ILE A 263     9949   6861   6915    671    107   -564       C  
ATOM   2040  CG1 ILE A 263      21.705  37.041  34.652  1.00 61.55           C  
ANISOU 2040  CG1 ILE A 263     9691   6873   6822    594      6   -565       C  
ATOM   2041  CG2 ILE A 263      22.236  39.265  35.656  1.00 61.52           C  
ANISOU 2041  CG2 ILE A 263     9874   6708   6794    590    242   -620       C  
ATOM   2042  CD1 ILE A 263      22.840  36.253  35.238  1.00 59.24           C  
ANISOU 2042  CD1 ILE A 263     9396   6607   6504    435      7   -569       C  
ATOM   2043  N   CYS A 264      21.664  41.371  32.959  1.00 69.44           N  
ANISOU 2043  N   CYS A 264    11098   7494   7793    975    272   -510       N  
ATOM   2044  CA  CYS A 264      21.637  42.837  33.034  1.00 71.62           C  
ANISOU 2044  CA  CYS A 264    11514   7626   8071   1061    426   -513       C  
ATOM   2045  C   CYS A 264      20.333  43.468  32.549  1.00 75.54           C  
ANISOU 2045  C   CYS A 264    11972   8110   8618   1280    443   -450       C  
ATOM   2046  O   CYS A 264      19.891  44.474  33.096  1.00 80.90           O  
ANISOU 2046  O   CYS A 264    12711   8698   9331   1354    592   -462       O  
ATOM   2047  CB  CYS A 264      22.810  43.437  32.277  1.00 69.25           C  
ANISOU 2047  CB  CYS A 264    11387   7210   7714   1037    464   -498       C  
ATOM   2048  SG  CYS A 264      24.374  42.891  32.994  1.00 69.48           S  
ANISOU 2048  SG  CYS A 264    11450   7263   7686    782    473   -557       S  
ATOM   2049  N   ASP A 265      19.707  42.871  31.545  1.00 77.88           N  
ANISOU 2049  N   ASP A 265    12168   8504   8918   1380    297   -379       N  
ATOM   2050  CA  ASP A 265      18.468  43.420  30.998  1.00 78.78           C  
ANISOU 2050  CA  ASP A 265    12218   8642   9073   1593    293   -293       C  
ATOM   2051  C   ASP A 265      17.285  43.247  31.927  1.00 75.70           C  
ANISOU 2051  C   ASP A 265    11666   8343   8752   1632    319   -303       C  
ATOM   2052  O   ASP A 265      16.286  43.932  31.766  1.00 78.20           O  
ANISOU 2052  O   ASP A 265    11935   8659   9116   1816    370   -232       O  
ATOM   2053  CB  ASP A 265      18.141  42.785  29.637  1.00 81.71           C  
ANISOU 2053  CB  ASP A 265    12518   9121   9406   1662    114   -212       C  
ATOM   2054  CG  ASP A 265      19.066  43.268  28.532  1.00 85.38           C  
ANISOU 2054  CG  ASP A 265    13154   9481   9807   1690    113   -174       C  
ATOM   2055  OD1 ASP A 265      20.063  43.973  28.831  1.00 94.36           O  
ANISOU 2055  OD1 ASP A 265    14456  10468  10928   1633    239   -216       O  
ATOM   2056  OD2 ASP A 265      18.806  42.951  27.358  1.00 86.84           O  
ANISOU 2056  OD2 ASP A 265    13311   9737   9948   1758    -13   -103       O  
ATOM   2057  N   ASN A 266      17.393  42.327  32.882  1.00 76.46           N  
ANISOU 2057  N   ASN A 266    11674   8521   8856   1468    289   -381       N  
ATOM   2058  CA  ASN A 266      16.291  42.007  33.786  1.00 78.39           C  
ANISOU 2058  CA  ASN A 266    11755   8867   9163   1482    304   -396       C  
ATOM   2059  C   ASN A 266      16.696  42.192  35.241  1.00 81.02           C  
ANISOU 2059  C   ASN A 266    12139   9142   9504   1345    444   -495       C  
ATOM   2060  O   ASN A 266      16.064  41.613  36.139  1.00 88.04           O  
ANISOU 2060  O   ASN A 266    12897  10128  10428   1289    441   -529       O  
ATOM   2061  CB  ASN A 266      15.829  40.553  33.592  1.00 77.75           C  
ANISOU 2061  CB  ASN A 266    11494   8970   9079   1402    123   -392       C  
ATOM   2062  CG  ASN A 266      15.394  40.244  32.175  1.00 79.70           C  
ANISOU 2062  CG  ASN A 266    11684   9301   9297   1500    -28   -304       C  
ATOM   2063  OD1 ASN A 266      14.338  40.691  31.710  1.00 77.25           O  
ANISOU 2063  OD1 ASN A 266    11282   9053   9016   1667    -46   -220       O  
ATOM   2064  ND2 ASN A 266      16.203  39.446  31.485  1.00 78.40           N  
ANISOU 2064  ND2 ASN A 266    11569   9149   9070   1392   -137   -319       N  
ATOM   2065  N   GLN A 267      17.737  42.985  35.493  1.00 77.28           N  
ANISOU 2065  N   GLN A 267    11855   8520   8989   1277    566   -541       N  
ATOM   2066  CA  GLN A 267      18.229  43.132  36.855  1.00 77.85           C  
ANISOU 2066  CA  GLN A 267    11983   8553   9042   1112    688   -638       C  
ATOM   2067  C   GLN A 267      17.135  43.577  37.838  1.00 81.66           C  
ANISOU 2067  C   GLN A 267    12408   9035   9585   1179    819   -664       C  
ATOM   2068  O   GLN A 267      17.181  43.214  39.013  1.00 81.05           O  
ANISOU 2068  O   GLN A 267    12294   9003   9497   1034    863   -737       O  
ATOM   2069  CB  GLN A 267      19.485  44.017  36.937  1.00 75.97           C  
ANISOU 2069  CB  GLN A 267    11963   8162   8740   1016    806   -684       C  
ATOM   2070  CG  GLN A 267      19.381  45.434  36.399  1.00 76.97           C  
ANISOU 2070  CG  GLN A 267    12255   8112   8878   1171    952   -654       C  
ATOM   2071  CD  GLN A 267      20.740  46.110  36.314  1.00 75.31           C  
ANISOU 2071  CD  GLN A 267    12251   7771   8592   1044   1036   -698       C  
ATOM   2072  OE1 GLN A 267      21.365  46.429  37.341  1.00 79.84           O  
ANISOU 2072  OE1 GLN A 267    12916   8302   9118    865   1149   -788       O  
ATOM   2073  NE2 GLN A 267      21.218  46.305  35.093  1.00 68.37           N  
ANISOU 2073  NE2 GLN A 267    11444   6841   7692   1120    977   -633       N  
ATOM   2074  N   ASP A 268      16.122  44.289  37.351  1.00 84.61           N  
ANISOU 2074  N   ASP A 268    12756   9371  10021   1401    875   -593       N  
ATOM   2075  CA  ASP A 268      15.007  44.682  38.208  1.00 90.67           C  
ANISOU 2075  CA  ASP A 268    13451  10143  10857   1492   1007   -601       C  
ATOM   2076  C   ASP A 268      14.244  43.489  38.800  1.00 89.59           C  
ANISOU 2076  C   ASP A 268    13090  10197  10752   1426    897   -613       C  
ATOM   2077  O   ASP A 268      13.777  43.567  39.924  1.00 91.24           O  
ANISOU 2077  O   ASP A 268    13266  10415  10987   1384   1011   -669       O  
ATOM   2078  CB  ASP A 268      14.054  45.649  37.479  1.00 97.28           C  
ANISOU 2078  CB  ASP A 268    14283  10916  11762   1770   1087   -493       C  
ATOM   2079  CG  ASP A 268      14.641  47.077  37.338  1.00101.72           C  
ANISOU 2079  CG  ASP A 268    15100  11242  12309   1837   1290   -502       C  
ATOM   2080  OD1 ASP A 268      15.495  47.478  38.167  1.00 99.20           O  
ANISOU 2080  OD1 ASP A 268    14949  10804  11936   1665   1422   -614       O  
ATOM   2081  OD2 ASP A 268      14.241  47.802  36.391  1.00103.44           O  
ANISOU 2081  OD2 ASP A 268    15350  11394  12560   2056   1319   -392       O  
ATOM   2082  N   THR A 269      14.144  42.379  38.076  1.00 89.81           N  
ANISOU 2082  N   THR A 269    12979  10373  10772   1401    687   -567       N  
ATOM   2083  CA  THR A 269      13.531  41.162  38.639  1.00 85.51           C  
ANISOU 2083  CA  THR A 269    12239  10001  10249   1307    584   -586       C  
ATOM   2084  C   THR A 269      14.527  40.068  39.062  1.00 81.03           C  
ANISOU 2084  C   THR A 269    11683   9484   9621   1073    492   -651       C  
ATOM   2085  O   THR A 269      14.133  38.908  39.213  1.00 78.49           O  
ANISOU 2085  O   THR A 269    11212   9301   9311    998    376   -651       O  
ATOM   2086  CB  THR A 269      12.575  40.542  37.629  1.00 86.09           C  
ANISOU 2086  CB  THR A 269    12132  10225  10354   1422    419   -492       C  
ATOM   2087  OG1 THR A 269      13.333  40.119  36.499  1.00 88.55           O  
ANISOU 2087  OG1 THR A 269    12502  10537  10607   1388    278   -464       O  
ATOM   2088  CG2 THR A 269      11.529  41.557  37.184  1.00 89.36           C  
ANISOU 2088  CG2 THR A 269    12500  10623  10831   1671    497   -398       C  
ATOM   2089  N   ILE A 270      15.797  40.435  39.262  1.00 80.39           N  
ANISOU 2089  N   ILE A 270    11773   9295   9478    960    549   -699       N  
ATOM   2090  CA  ILE A 270      16.830  39.503  39.732  1.00 74.87           C  
ANISOU 2090  CA  ILE A 270    11083   8642   8720    750    483   -742       C  
ATOM   2091  C   ILE A 270      17.579  40.029  40.940  1.00 73.31           C  
ANISOU 2091  C   ILE A 270    11001   8381   8472    600    624   -820       C  
ATOM   2092  O   ILE A 270      17.681  39.322  41.942  1.00 75.02           O  
ANISOU 2092  O   ILE A 270    11151   8683   8670    453    617   -857       O  
ATOM   2093  CB  ILE A 270      17.892  39.204  38.670  1.00 74.07           C  
ANISOU 2093  CB  ILE A 270    11061   8512   8572    721    380   -707       C  
ATOM   2094  CG1 ILE A 270      17.264  38.569  37.432  1.00 76.55           C  
ANISOU 2094  CG1 ILE A 270    11276   8900   8911    832    228   -638       C  
ATOM   2095  CG2 ILE A 270      18.940  38.255  39.237  1.00 70.05           C  
ANISOU 2095  CG2 ILE A 270    10547   8056   8013    521    330   -733       C  
ATOM   2096  CD1 ILE A 270      18.216  38.448  36.260  1.00 75.12           C  
ANISOU 2096  CD1 ILE A 270    11192   8669   8681    832    149   -603       C  
ATOM   2097  N   SER A 271      18.142  41.234  40.846  1.00 73.41           N  
ANISOU 2097  N   SER A 271    11191   8249   8453    619    750   -843       N  
ATOM   2098  CA  SER A 271      18.889  41.807  41.986  1.00 75.72           C  
ANISOU 2098  CA  SER A 271    11609   8483   8676    448    891   -927       C  
ATOM   2099  C   SER A 271      19.228  43.292  41.905  1.00 74.40           C  
ANISOU 2099  C   SER A 271    11651   8135   8482    486   1067   -963       C  
ATOM   2100  O   SER A 271      19.481  43.834  40.831  1.00 77.64           O  
ANISOU 2100  O   SER A 271    12147   8453   8901    599   1059   -916       O  
ATOM   2101  CB  SER A 271      20.195  41.041  42.211  1.00 74.74           C  
ANISOU 2101  CB  SER A 271    11492   8433   8475    243    800   -932       C  
ATOM   2102  OG  SER A 271      20.976  41.665  43.216  1.00 77.07           O  
ANISOU 2102  OG  SER A 271    11909   8689   8685     63    925  -1004       O  
ATOM   2103  N   SER A 272      19.285  43.923  43.070  1.00 73.26           N  
ANISOU 2103  N   SER A 272    11600   7938   8296    371   1234  -1050       N  
ATOM   2104  CA  SER A 272      19.644  45.332  43.176  1.00 74.91           C  
ANISOU 2104  CA  SER A 272    12033   7961   8467    366   1433  -1105       C  
ATOM   2105  C   SER A 272      21.141  45.559  43.250  1.00 74.63           C  
ANISOU 2105  C   SER A 272    12136   7899   8320    153   1435  -1144       C  
ATOM   2106  O   SER A 272      21.577  46.700  43.202  1.00 75.76           O  
ANISOU 2106  O   SER A 272    12479   7884   8422    127   1590  -1190       O  
ATOM   2107  CB  SER A 272      19.004  45.967  44.421  1.00 75.72           C  
ANISOU 2107  CB  SER A 272    12199   8006   8565    324   1637  -1193       C  
ATOM   2108  OG  SER A 272      19.690  45.590  45.604  1.00 72.17           O  
ANISOU 2108  OG  SER A 272    11763   7645   8014     54   1647  -1274       O  
ATOM   2109  N   LYS A 273      21.929  44.494  43.362  1.00 77.03           N  
ANISOU 2109  N   LYS A 273    12336   8356   8577      1   1275  -1121       N  
ATOM   2110  CA  LYS A 273      23.383  44.628  43.544  1.00 78.87           C  
ANISOU 2110  CA  LYS A 273    12666   8602   8698   -218   1271  -1145       C  
ATOM   2111  C   LYS A 273      24.210  44.498  42.245  1.00 76.67           C  
ANISOU 2111  C   LYS A 273    12409   8301   8421   -163   1162  -1070       C  
ATOM   2112  O   LYS A 273      25.434  44.379  42.301  1.00 76.42           O  
ANISOU 2112  O   LYS A 273    12411   8316   8309   -334   1127  -1066       O  
ATOM   2113  CB  LYS A 273      23.862  43.596  44.575  1.00 80.95           C  
ANISOU 2113  CB  LYS A 273    12804   9055   8898   -428   1184  -1152       C  
ATOM   2114  N   LEU A 274      23.557  44.536  41.085  1.00 76.35           N  
ANISOU 2114  N   LEU A 274    12346   8198   8466     70   1111  -1005       N  
ATOM   2115  CA  LEU A 274      24.239  44.277  39.807  1.00 75.53           C  
ANISOU 2115  CA  LEU A 274    12250   8084   8363    130    997   -931       C  
ATOM   2116  C   LEU A 274      24.654  45.539  39.009  1.00 80.12           C  
ANISOU 2116  C   LEU A 274    13033   8484   8926    198   1108   -931       C  
ATOM   2117  O   LEU A 274      25.384  45.435  38.024  1.00 82.28           O  
ANISOU 2117  O   LEU A 274    13339   8742   9183    218   1035   -878       O  
ATOM   2118  CB  LEU A 274      23.343  43.417  38.916  1.00 73.66           C  
ANISOU 2118  CB  LEU A 274    11863   7913   8211    321    850   -852       C  
ATOM   2119  CG  LEU A 274      22.927  42.003  39.327  1.00 71.75           C  
ANISOU 2119  CG  LEU A 274    11421   7841   7999    282    715   -832       C  
ATOM   2120  CD1 LEU A 274      21.541  41.673  38.790  1.00 71.79           C  
ANISOU 2120  CD1 LEU A 274    11308   7878   8091    477    651   -791       C  
ATOM   2121  CD2 LEU A 274      23.928  40.978  38.823  1.00 69.78           C  
ANISOU 2121  CD2 LEU A 274    11118   7675   7720    198    579   -781       C  
ATOM   2122  N   LYS A 275      24.174  46.716  39.396  1.00 82.57           N  
ANISOU 2122  N   LYS A 275    13484   8647   9240    242   1295   -986       N  
ATOM   2123  CA  LYS A 275      24.433  47.933  38.635  1.00 82.70           C  
ANISOU 2123  CA  LYS A 275    13701   8473   9250    329   1419   -978       C  
ATOM   2124  C   LYS A 275      25.897  48.069  38.178  1.00 81.80           C  
ANISOU 2124  C   LYS A 275    13686   8344   9052    174   1393   -976       C  
ATOM   2125  O   LYS A 275      26.164  48.246  36.982  1.00 87.17           O  
ANISOU 2125  O   LYS A 275    14414   8960   9745    290   1348   -909       O  
ATOM   2126  CB  LYS A 275      23.999  49.160  39.459  1.00 82.41           C  
ANISOU 2126  CB  LYS A 275    13832   8274   9204    317   1663  -1064       C  
ATOM   2127  N   GLU A 276      26.841  47.979  39.114  1.00 79.65           N  
ANISOU 2127  N   GLU A 276    13435   8141   8687    -91   1419  -1043       N  
ATOM   2128  CA  GLU A 276      28.265  48.181  38.787  1.00 78.70           C  
ANISOU 2128  CA  GLU A 276    13400   8021   8481   -259   1409  -1039       C  
ATOM   2129  C   GLU A 276      28.787  47.076  37.856  1.00 77.00           C  
ANISOU 2129  C   GLU A 276    13042   7928   8288   -209   1210   -939       C  
ATOM   2130  O   GLU A 276      29.562  47.344  36.930  1.00 82.32           O  
ANISOU 2130  O   GLU A 276    13793   8545   8940   -198   1198   -898       O  
ATOM   2131  CB  GLU A 276      29.130  48.295  40.053  1.00 74.82           C  
ANISOU 2131  CB  GLU A 276    12938   7614   7874   -568   1471  -1121       C  
ATOM   2132  N   CYS A 277      28.335  45.850  38.088  1.00 72.61           N  
ANISOU 2132  N   CYS A 277    12287   7525   7775   -176   1070   -901       N  
ATOM   2133  CA  CYS A 277      28.650  44.726  37.213  1.00 71.50           C  
ANISOU 2133  CA  CYS A 277    12018   7483   7666   -109    898   -811       C  
ATOM   2134  C   CYS A 277      28.216  44.958  35.782  1.00 70.76           C  
ANISOU 2134  C   CYS A 277    11976   7285   7625    114    864   -752       C  
ATOM   2135  O   CYS A 277      28.953  44.644  34.837  1.00 63.21           O  
ANISOU 2135  O   CYS A 277    11029   6334   6654    129    793   -695       O  
ATOM   2136  CB  CYS A 277      27.937  43.456  37.673  1.00 68.39           C  
ANISOU 2136  CB  CYS A 277    11426   7237   7323    -81    779   -789       C  
ATOM   2137  SG  CYS A 277      28.706  42.595  39.023  1.00 73.50           S  
ANISOU 2137  SG  CYS A 277    11950   8068   7907   -329    741   -798       S  
ATOM   2138  N   CYS A 278      26.998  45.469  35.633  1.00 71.42           N  
ANISOU 2138  N   CYS A 278    12082   7287   7767    289    913   -759       N  
ATOM   2139  CA  CYS A 278      26.360  45.497  34.330  1.00 72.51           C  
ANISOU 2139  CA  CYS A 278    12221   7373   7955    514    850   -685       C  
ATOM   2140  C   CYS A 278      26.767  46.697  33.510  1.00 74.81           C  
ANISOU 2140  C   CYS A 278    12709   7493   8221    583    956   -668       C  
ATOM   2141  O   CYS A 278      26.230  46.911  32.433  1.00 71.44           O  
ANISOU 2141  O   CYS A 278    12305   7014   7826    775    921   -599       O  
ATOM   2142  CB  CYS A 278      24.854  45.416  34.493  1.00 72.86           C  
ANISOU 2142  CB  CYS A 278    12169   7441   8075    680    840   -673       C  
ATOM   2143  SG  CYS A 278      24.341  43.726  34.862  1.00 73.62           S  
ANISOU 2143  SG  CYS A 278    12020   7746   8205    642    661   -659       S  
ATOM   2144  N   ASP A 279      27.731  47.466  34.016  1.00 80.24           N  
ANISOU 2144  N   ASP A 279    13539   8103   8844    415   1082   -726       N  
ATOM   2145  CA  ASP A 279      28.308  48.564  33.258  1.00 86.97           C  
ANISOU 2145  CA  ASP A 279    14591   8790   9663    444   1190   -714       C  
ATOM   2146  C   ASP A 279      29.688  48.205  32.749  1.00 85.64           C  
ANISOU 2146  C   ASP A 279    14438   8669   9433    307   1126   -690       C  
ATOM   2147  O   ASP A 279      30.319  48.996  32.035  1.00 93.93           O  
ANISOU 2147  O   ASP A 279    15644   9597  10448    311   1201   -674       O  
ATOM   2148  CB  ASP A 279      28.368  49.835  34.107  1.00 91.21           C  
ANISOU 2148  CB  ASP A 279    15309   9179  10169    351   1408   -801       C  
ATOM   2149  CG  ASP A 279      26.994  50.467  34.312  1.00 95.26           C  
ANISOU 2149  CG  ASP A 279    15854   9588  10754    547   1516   -803       C  
ATOM   2150  OD1 ASP A 279      26.057  50.149  33.537  1.00 92.10           O  
ANISOU 2150  OD1 ASP A 279    15359   9212  10424    778   1426   -716       O  
ATOM   2151  OD2 ASP A 279      26.859  51.284  35.252  1.00 97.16           O  
ANISOU 2151  OD2 ASP A 279    16213   9726  10976    464   1698   -888       O  
ATOM   2152  N   LYS A 280      30.146  47.005  33.074  1.00 75.35           N  
ANISOU 2152  N   LYS A 280    12970   7539   8120    197    996   -677       N  
ATOM   2153  CA  LYS A 280      31.501  46.635  32.733  1.00 72.94           C  
ANISOU 2153  CA  LYS A 280    12661   7293   7761     61    952   -647       C  
ATOM   2154  C   LYS A 280      31.584  45.993  31.344  1.00 68.43           C  
ANISOU 2154  C   LYS A 280    12057   6731   7215    208    835   -560       C  
ATOM   2155  O   LYS A 280      30.579  45.512  30.804  1.00 62.98           O  
ANISOU 2155  O   LYS A 280    11298   6055   6578    382    749   -526       O  
ATOM   2156  CB  LYS A 280      32.059  45.712  33.816  1.00 76.23           C  
ANISOU 2156  CB  LYS A 280    12925   7890   8151   -131    891   -660       C  
ATOM   2157  CG  LYS A 280      31.946  46.305  35.218  1.00 82.03           C  
ANISOU 2157  CG  LYS A 280    13694   8632   8844   -294   1002   -750       C  
ATOM   2158  CD  LYS A 280      32.792  45.563  36.253  1.00 86.39           C  
ANISOU 2158  CD  LYS A 280    14115   9372   9338   -522    952   -750       C  
ATOM   2159  CE  LYS A 280      33.377  46.483  37.312  1.00 88.25           C  
ANISOU 2159  CE  LYS A 280    14454   9602   9475   -762   1083   -833       C  
ATOM   2160  NZ  LYS A 280      32.293  47.315  37.899  1.00 92.77           N  
ANISOU 2160  NZ  LYS A 280    15135  10049  10063   -714   1210   -926       N  
ATOM   2161  N   PRO A 281      32.794  45.973  30.769  1.00 68.50           N  
ANISOU 2161  N   PRO A 281    12111   6739   7177    126    834   -526       N  
ATOM   2162  CA  PRO A 281      33.103  45.262  29.512  1.00 66.73           C  
ANISOU 2162  CA  PRO A 281    11860   6533   6961    227    735   -449       C  
ATOM   2163  C   PRO A 281      32.832  43.773  29.615  1.00 66.69           C  
ANISOU 2163  C   PRO A 281    11670   6674   6995    246    598   -417       C  
ATOM   2164  O   PRO A 281      32.772  43.230  30.727  1.00 65.51           O  
ANISOU 2164  O   PRO A 281    11402   6633   6857    142    579   -443       O  
ATOM   2165  CB  PRO A 281      34.605  45.483  29.326  1.00 67.23           C  
ANISOU 2165  CB  PRO A 281    11979   6600   6965     76    786   -429       C  
ATOM   2166  CG  PRO A 281      34.973  46.619  30.206  1.00 68.33           C  
ANISOU 2166  CG  PRO A 281    12225   6681   7056    -80    923   -497       C  
ATOM   2167  CD  PRO A 281      33.975  46.661  31.323  1.00 69.34           C  
ANISOU 2167  CD  PRO A 281    12301   6833   7211    -87    940   -561       C  
ATOM   2168  N   LEU A 282      32.736  43.115  28.461  1.00 67.44           N  
ANISOU 2168  N   LEU A 282    11752   6769   7102    364    513   -363       N  
ATOM   2169  CA  LEU A 282      32.114  41.794  28.357  1.00 67.22           C  
ANISOU 2169  CA  LEU A 282    11584   6842   7115    421    392   -342       C  
ATOM   2170  C   LEU A 282      32.684  40.730  29.290  1.00 64.38           C  
ANISOU 2170  C   LEU A 282    11080   6614   6769    285    361   -335       C  
ATOM   2171  O   LEU A 282      31.961  40.178  30.112  1.00 67.54           O  
ANISOU 2171  O   LEU A 282    11369   7091   7204    271    321   -359       O  
ATOM   2172  CB  LEU A 282      32.172  41.331  26.901  1.00 71.96           C  
ANISOU 2172  CB  LEU A 282    12230   7411   7702    531    328   -291       C  
ATOM   2173  CG  LEU A 282      31.509  40.013  26.494  1.00 73.97           C  
ANISOU 2173  CG  LEU A 282    12380   7743   7981    591    211   -275       C  
ATOM   2174  CD1 LEU A 282      30.859  40.189  25.121  1.00 77.53           C  
ANISOU 2174  CD1 LEU A 282    12914   8140   8405    737    157   -249       C  
ATOM   2175  CD2 LEU A 282      32.521  38.867  26.498  1.00 67.14           C  
ANISOU 2175  CD2 LEU A 282    11452   6940   7119    502    198   -242       C  
ATOM   2176  N   LEU A 283      33.971  40.444  29.190  1.00 64.31           N  
ANISOU 2176  N   LEU A 283    11065   6638   6733    189    385   -291       N  
ATOM   2177  CA  LEU A 283      34.559  39.423  30.066  1.00 62.75           C  
ANISOU 2177  CA  LEU A 283    10719   6574   6548     75    360   -258       C  
ATOM   2178  C   LEU A 283      34.470  39.802  31.536  1.00 67.13           C  
ANISOU 2178  C   LEU A 283    11216   7202   7090    -59    397   -302       C  
ATOM   2179  O   LEU A 283      34.168  38.955  32.378  1.00 76.91           O  
ANISOU 2179  O   LEU A 283    12324   8545   8354   -101    352   -295       O  
ATOM   2180  CB  LEU A 283      36.005  39.138  29.698  1.00 62.47           C  
ANISOU 2180  CB  LEU A 283    10678   6571   6487      5    391   -184       C  
ATOM   2181  CG  LEU A 283      36.118  38.328  28.406  1.00 64.70           C  
ANISOU 2181  CG  LEU A 283    10986   6809   6789    123    353   -135       C  
ATOM   2182  CD1 LEU A 283      37.553  38.220  27.916  1.00 65.20           C  
ANISOU 2182  CD1 LEU A 283    11062   6883   6829     73    408    -60       C  
ATOM   2183  CD2 LEU A 283      35.475  36.962  28.594  1.00 63.46           C  
ANISOU 2183  CD2 LEU A 283    10716   6714   6683    167    280   -123       C  
ATOM   2184  N   GLU A 284      34.712  41.076  31.834  1.00 71.55           N  
ANISOU 2184  N   GLU A 284    11884   7699   7602   -132    486   -349       N  
ATOM   2185  CA  GLU A 284      34.740  41.586  33.205  1.00 70.02           C  
ANISOU 2185  CA  GLU A 284    11669   7564   7372   -289    542   -403       C  
ATOM   2186  C   GLU A 284      33.336  41.585  33.787  1.00 67.94           C  
ANISOU 2186  C   GLU A 284    11378   7286   7151   -215    529   -465       C  
ATOM   2187  O   GLU A 284      33.149  41.366  34.984  1.00 64.72           O  
ANISOU 2187  O   GLU A 284    10887   6971   6732   -323    533   -494       O  
ATOM   2188  CB  GLU A 284      35.312  43.005  33.223  1.00 75.50           C  
ANISOU 2188  CB  GLU A 284    12523   8164   8000   -385    660   -450       C  
ATOM   2189  CG  GLU A 284      36.037  43.407  34.497  1.00 82.89           C  
ANISOU 2189  CG  GLU A 284    13435   9198   8860   -626    721   -482       C  
ATOM   2190  CD  GLU A 284      36.294  44.915  34.594  1.00 95.82           C  
ANISOU 2190  CD  GLU A 284    15265  10711  10432   -725    859   -559       C  
ATOM   2191  OE1 GLU A 284      36.578  45.567  33.549  1.00101.14           O  
ANISOU 2191  OE1 GLU A 284    16072  11253  11102   -652    907   -548       O  
ATOM   2192  OE2 GLU A 284      36.225  45.452  35.731  1.00103.57           O  
ANISOU 2192  OE2 GLU A 284    16274  11722  11358   -886    930   -633       O  
ATOM   2193  N   LYS A 285      32.347  41.840  32.933  1.00 66.63           N  
ANISOU 2193  N   LYS A 285    11276   7013   7028    -33    512   -478       N  
ATOM   2194  CA  LYS A 285      30.950  41.819  33.351  1.00 64.63           C  
ANISOU 2194  CA  LYS A 285    10979   6753   6823     61    497   -521       C  
ATOM   2195  C   LYS A 285      30.539  40.483  33.947  1.00 64.30           C  
ANISOU 2195  C   LYS A 285    10763   6849   6820     40    403   -504       C  
ATOM   2196  O   LYS A 285      29.859  40.462  34.966  1.00 66.41           O  
ANISOU 2196  O   LYS A 285    10970   7163   7101      1    420   -549       O  
ATOM   2197  CB  LYS A 285      30.035  42.169  32.188  1.00 62.09           C  
ANISOU 2197  CB  LYS A 285    10725   6328   6536    267    474   -507       C  
ATOM   2198  CG  LYS A 285      28.569  41.917  32.479  1.00 64.03           C  
ANISOU 2198  CG  LYS A 285    10885   6603   6840    379    433   -527       C  
ATOM   2199  CD  LYS A 285      27.638  42.758  31.620  1.00 67.64           C  
ANISOU 2199  CD  LYS A 285    11426   6954   7320    569    455   -512       C  
ATOM   2200  CE  LYS A 285      27.904  42.577  30.130  1.00 71.76           C  
ANISOU 2200  CE  LYS A 285    12002   7441   7824    670    385   -448       C  
ATOM   2201  NZ  LYS A 285      26.956  43.361  29.282  1.00 74.86           N  
ANISOU 2201  NZ  LYS A 285    12459   7753   8230    863    394   -413       N  
ATOM   2202  N   SER A 286      30.945  39.377  33.319  1.00 67.99           N  
ANISOU 2202  N   SER A 286    11159   7369   7304     65    317   -440       N  
ATOM   2203  CA  SER A 286      30.522  38.024  33.748  1.00 70.34           C  
ANISOU 2203  CA  SER A 286    11307   7777   7644     58    235   -418       C  
ATOM   2204  C   SER A 286      31.173  37.602  35.051  1.00 68.93           C  
ANISOU 2204  C   SER A 286    11030   7717   7442   -108    254   -404       C  
ATOM   2205  O   SER A 286      30.498  37.129  35.963  1.00 75.17           O  
ANISOU 2205  O   SER A 286    11725   8580   8254   -140    235   -426       O  
ATOM   2206  CB  SER A 286      30.825  36.972  32.674  1.00 74.09           C  
ANISOU 2206  CB  SER A 286    11761   8253   8139    127    165   -356       C  
ATOM   2207  OG  SER A 286      30.022  37.180  31.523  1.00 78.92           O  
ANISOU 2207  OG  SER A 286    12440   8785   8762    272    125   -369       O  
ATOM   2208  N   HIS A 287      32.487  37.765  35.124  1.00 66.49           N  
ANISOU 2208  N   HIS A 287    10737   7440   7085   -215    290   -359       N  
ATOM   2209  CA  HIS A 287      33.224  37.595  36.363  1.00 67.91           C  
ANISOU 2209  CA  HIS A 287    10831   7752   7220   -390    312   -334       C  
ATOM   2210  C   HIS A 287      32.537  38.331  37.502  1.00 68.86           C  
ANISOU 2210  C   HIS A 287    10968   7886   7311   -473    363   -422       C  
ATOM   2211  O   HIS A 287      32.264  37.739  38.546  1.00 72.45           O  
ANISOU 2211  O   HIS A 287    11314   8448   7764   -547    343   -420       O  
ATOM   2212  CB  HIS A 287      34.645  38.135  36.197  1.00 70.84           C  
ANISOU 2212  CB  HIS A 287    11246   8143   7527   -501    361   -289       C  
ATOM   2213  CG  HIS A 287      35.536  37.880  37.368  1.00 71.83           C  
ANISOU 2213  CG  HIS A 287    11260   8438   7593   -690    368   -238       C  
ATOM   2214  ND1 HIS A 287      36.144  36.658  37.581  1.00 71.82           N  
ANISOU 2214  ND1 HIS A 287    11110   8564   7613   -704    318   -123       N  
ATOM   2215  CD2 HIS A 287      35.934  38.687  38.381  1.00 67.89           C  
ANISOU 2215  CD2 HIS A 287    10780   8009   7007   -877    423   -279       C  
ATOM   2216  CE1 HIS A 287      36.865  36.721  38.687  1.00 74.14           C  
ANISOU 2216  CE1 HIS A 287    11317   9016   7835   -885    330    -83       C  
ATOM   2217  NE2 HIS A 287      36.761  37.942  39.187  1.00 71.53           N  
ANISOU 2217  NE2 HIS A 287    11089   8659   7432  -1005    389   -182       N  
ATOM   2218  N   CYS A 288      32.248  39.615  37.285  1.00 68.88           N  
ANISOU 2218  N   CYS A 288    11115   7767   7291   -454    442   -498       N  
ATOM   2219  CA  CYS A 288      31.642  40.474  38.301  1.00 66.72           C  
ANISOU 2219  CA  CYS A 288    10893   7472   6984   -529    525   -590       C  
ATOM   2220  C   CYS A 288      30.315  39.910  38.764  1.00 67.91           C  
ANISOU 2220  C   CYS A 288    10956   7648   7198   -442    489   -619       C  
ATOM   2221  O   CYS A 288      30.033  39.904  39.965  1.00 65.09           O  
ANISOU 2221  O   CYS A 288    10554   7364   6814   -551    522   -661       O  
ATOM   2222  CB  CYS A 288      31.417  41.877  37.760  1.00 69.22           C  
ANISOU 2222  CB  CYS A 288    11396   7617   7288   -471    629   -655       C  
ATOM   2223  SG  CYS A 288      30.703  43.056  38.944  1.00 75.76           S  
ANISOU 2223  SG  CYS A 288    12329   8378   8077   -556    776   -776       S  
ATOM   2224  N   ILE A 289      29.494  39.437  37.825  1.00 66.58           N  
ANISOU 2224  N   ILE A 289    10762   7428   7106   -257    422   -598       N  
ATOM   2225  CA  ILE A 289      28.215  38.827  38.200  1.00 67.51           C  
ANISOU 2225  CA  ILE A 289    10780   7586   7286   -179    379   -618       C  
ATOM   2226  C   ILE A 289      28.469  37.571  39.040  1.00 68.61           C  
ANISOU 2226  C   ILE A 289    10770   7875   7425   -285    317   -576       C  
ATOM   2227  O   ILE A 289      27.855  37.383  40.098  1.00 65.97           O  
ANISOU 2227  O   ILE A 289    10367   7606   7092   -342    333   -611       O  
ATOM   2228  CB  ILE A 289      27.368  38.416  36.978  1.00 68.08           C  
ANISOU 2228  CB  ILE A 289    10835   7608   7425     12    300   -592       C  
ATOM   2229  CG1 ILE A 289      26.843  39.648  36.225  1.00 65.43           C  
ANISOU 2229  CG1 ILE A 289    10628   7136   7097    146    360   -619       C  
ATOM   2230  CG2 ILE A 289      26.216  37.507  37.422  1.00 66.80           C  
ANISOU 2230  CG2 ILE A 289    10536   7526   7319     52    238   -600       C  
ATOM   2231  CD1 ILE A 289      26.388  39.357  34.811  1.00 59.50           C  
ANISOU 2231  CD1 ILE A 289     9882   6345   6379    310    275   -573       C  
ATOM   2232  N   ALA A 290      29.379  36.720  38.560  1.00 67.38           N  
ANISOU 2232  N   ALA A 290    10567   7765   7267   -303    257   -494       N  
ATOM   2233  CA  ALA A 290      29.698  35.469  39.253  1.00 67.37           C  
ANISOU 2233  CA  ALA A 290    10429   7895   7273   -382    208   -430       C  
ATOM   2234  C   ALA A 290      30.188  35.661  40.674  1.00 67.37           C  
ANISOU 2234  C   ALA A 290    10383   8011   7204   -563    251   -433       C  
ATOM   2235  O   ALA A 290      30.052  34.755  41.463  1.00 73.63           O  
ANISOU 2235  O   ALA A 290    11061   8910   8005   -617    220   -395       O  
ATOM   2236  CB  ALA A 290      30.707  34.632  38.476  1.00 64.66           C  
ANISOU 2236  CB  ALA A 290    10060   7568   6941   -362    166   -331       C  
ATOM   2237  N   GLU A 291      30.756  36.813  41.007  1.00 68.72           N  
ANISOU 2237  N   GLU A 291    10648   8165   7300   -669    326   -476       N  
ATOM   2238  CA  GLU A 291      31.247  37.041  42.363  1.00 72.14           C  
ANISOU 2238  CA  GLU A 291    11045   8721   7643   -871    367   -485       C  
ATOM   2239  C   GLU A 291      30.499  38.181  43.034  1.00 70.67           C  
ANISOU 2239  C   GLU A 291    10963   8468   7420   -920    465   -611       C  
ATOM   2240  O   GLU A 291      31.034  38.861  43.913  1.00 71.28           O  
ANISOU 2240  O   GLU A 291    11088   8599   7396  -1105    532   -650       O  
ATOM   2241  CB  GLU A 291      32.764  37.284  42.350  1.00 76.72           C  
ANISOU 2241  CB  GLU A 291    11631   9377   8142  -1010    376   -418       C  
ATOM   2242  CG  GLU A 291      33.555  35.994  42.582  1.00 82.99           C  
ANISOU 2242  CG  GLU A 291    12263  10329   8942  -1044    301   -275       C  
ATOM   2243  CD  GLU A 291      34.997  36.054  42.078  1.00 92.38           C  
ANISOU 2243  CD  GLU A 291    13439  11571  10091  -1101    298   -178       C  
ATOM   2244  OE1 GLU A 291      35.599  37.172  42.125  1.00 99.10           O  
ANISOU 2244  OE1 GLU A 291    14384  12410  10860  -1221    356   -225       O  
ATOM   2245  OE2 GLU A 291      35.513  34.982  41.634  1.00 78.85           O  
ANISOU 2245  OE2 GLU A 291    11625   9905   8428  -1026    250    -55       O  
ATOM   2246  N   VAL A 292      29.246  38.376  42.642  1.00 67.94           N  
ANISOU 2246  N   VAL A 292    10652   8012   7151   -760    479   -670       N  
ATOM   2247  CA  VAL A 292      28.523  39.562  43.067  1.00 70.82           C  
ANISOU 2247  CA  VAL A 292    11135   8276   7497   -763    597   -780       C  
ATOM   2248  C   VAL A 292      28.109  39.431  44.511  1.00 74.33           C  
ANISOU 2248  C   VAL A 292    11527   8819   7898   -897    640   -828       C  
ATOM   2249  O   VAL A 292      27.971  38.315  45.015  1.00 75.63           O  
ANISOU 2249  O   VAL A 292    11547   9110   8078   -923    561   -774       O  
ATOM   2250  CB  VAL A 292      27.270  39.793  42.230  1.00 67.89           C  
ANISOU 2250  CB  VAL A 292    10792   7776   7226   -536    601   -806       C  
ATOM   2251  CG1 VAL A 292      26.268  38.678  42.461  1.00 63.86           C  
ANISOU 2251  CG1 VAL A 292    10128   7346   6789   -458    520   -783       C  
ATOM   2252  CG2 VAL A 292      26.663  41.128  42.588  1.00 72.60           C  
ANISOU 2252  CG2 VAL A 292    11528   8248   7807   -521    751   -903       C  
ATOM   2253  N   GLU A 293      27.910  40.570  45.166  1.00 75.97           N  
ANISOU 2253  N   GLU A 293    11863   8957   8045   -983    775   -929       N  
ATOM   2254  CA  GLU A 293      27.386  40.585  46.526  1.00 81.02           C  
ANISOU 2254  CA  GLU A 293    12480   9668   8636  -1105    840   -993       C  
ATOM   2255  C   GLU A 293      25.934  40.095  46.567  1.00 79.26           C  
ANISOU 2255  C   GLU A 293    12170   9423   8521   -935    827  -1006       C  
ATOM   2256  O   GLU A 293      25.120  40.455  45.726  1.00 81.01           O  
ANISOU 2256  O   GLU A 293    12427   9520   8833   -736    846  -1018       O  
ATOM   2257  CB  GLU A 293      27.490  41.998  47.129  1.00 85.44           C  
ANISOU 2257  CB  GLU A 293    13230  10130   9104  -1236   1014  -1111       C  
ATOM   2258  CG  GLU A 293      27.258  42.061  48.636  1.00 88.78           C  
ANISOU 2258  CG  GLU A 293    13651  10646   9435  -1427   1091  -1182       C  
ATOM   2259  CD  GLU A 293      27.396  43.467  49.213  1.00 90.88           C  
ANISOU 2259  CD  GLU A 293    14132  10800   9598  -1576   1283  -1311       C  
ATOM   2260  OE1 GLU A 293      27.418  44.439  48.426  1.00 89.52           O  
ANISOU 2260  OE1 GLU A 293    14114  10447   9453  -1486   1374  -1349       O  
ATOM   2261  OE2 GLU A 293      27.465  43.593  50.459  1.00 87.86           O  
ANISOU 2261  OE2 GLU A 293    13773  10506   9103  -1786   1350  -1376       O  
ATOM   2262  N   LYS A 294      25.623  39.294  47.574  1.00 80.79           N  
ANISOU 2262  N   LYS A 294    12246   9751   8698  -1021    796   -997       N  
ATOM   2263  CA  LYS A 294      24.292  38.748  47.745  1.00 80.59           C  
ANISOU 2263  CA  LYS A 294    12123   9733   8766   -893    783  -1007       C  
ATOM   2264  C   LYS A 294      23.323  39.883  48.030  1.00 83.43           C  
ANISOU 2264  C   LYS A 294    12594   9963   9145   -826    942  -1111       C  
ATOM   2265  O   LYS A 294      23.661  40.816  48.754  1.00 87.80           O  
ANISOU 2265  O   LYS A 294    13280  10475   9604   -967   1074  -1191       O  
ATOM   2266  CB  LYS A 294      24.280  37.730  48.884  1.00 80.13           C  
ANISOU 2266  CB  LYS A 294    11934   9844   8669  -1028    736   -977       C  
ATOM   2267  CG  LYS A 294      25.382  36.684  48.737  1.00 82.74           C  
ANISOU 2267  CG  LYS A 294    12165  10302   8969  -1105    608   -860       C  
ATOM   2268  CD  LYS A 294      25.300  35.539  49.740  1.00 82.08           C  
ANISOU 2268  CD  LYS A 294    11940  10382   8865  -1203    554   -803       C  
ATOM   2269  CE  LYS A 294      26.514  34.615  49.635  1.00 79.86           C  
ANISOU 2269  CE  LYS A 294    11572  10222   8551  -1274    452   -670       C  
ATOM   2270  N   ASP A 295      22.132  39.811  47.435  1.00 84.21           N  
ANISOU 2270  N   ASP A 295    12640   9998   9360   -614    935  -1105       N  
ATOM   2271  CA  ASP A 295      21.082  40.810  47.634  1.00 82.59           C  
ANISOU 2271  CA  ASP A 295    12514   9672   9197   -505   1091  -1178       C  
ATOM   2272  C   ASP A 295      20.458  40.601  49.011  1.00 82.50           C  
ANISOU 2272  C   ASP A 295    12452   9737   9156   -610   1170  -1236       C  
ATOM   2273  O   ASP A 295      20.636  39.552  49.632  1.00 79.05           O  
ANISOU 2273  O   ASP A 295    11893   9451   8690   -725   1077  -1203       O  
ATOM   2274  CB  ASP A 295      20.008  40.682  46.542  1.00 85.98           C  
ANISOU 2274  CB  ASP A 295    12863  10050   9757   -244   1038  -1126       C  
ATOM   2275  CG  ASP A 295      19.256  41.981  46.276  1.00 90.88           C  
ANISOU 2275  CG  ASP A 295    13600  10505  10424    -83   1201  -1166       C  
ATOM   2276  OD1 ASP A 295      19.779  43.066  46.582  1.00 97.04           O  
ANISOU 2276  OD1 ASP A 295    14565  11168  11139   -159   1351  -1231       O  
ATOM   2277  OD2 ASP A 295      18.140  41.919  45.723  1.00 96.68           O  
ANISOU 2277  OD2 ASP A 295    14243  11231  11261    120   1183  -1124       O  
ATOM   2278  N   ALA A 296      19.736  41.607  49.488  1.00 80.31           N  
ANISOU 2278  N   ALA A 296    12278   9349   8886   -567   1353  -1318       N  
ATOM   2279  CA  ALA A 296      19.061  41.521  50.766  1.00 79.75           C  
ANISOU 2279  CA  ALA A 296    12178   9334   8791   -654   1454  -1382       C  
ATOM   2280  C   ALA A 296      17.875  40.570  50.630  1.00 83.04           C  
ANISOU 2280  C   ALA A 296    12391   9836   9325   -503   1367  -1326       C  
ATOM   2281  O   ALA A 296      17.331  40.399  49.544  1.00 82.82           O  
ANISOU 2281  O   ALA A 296    12286   9780   9403   -302   1288  -1262       O  
ATOM   2282  CB  ALA A 296      18.598  42.902  51.217  1.00 78.90           C  
ANISOU 2282  CB  ALA A 296    12252   9059   8666   -630   1699  -1484       C  
ATOM   2283  N   ILE A 297      17.477  39.970  51.748  1.00 88.42           N  
ANISOU 2283  N   ILE A 297    12988  10629   9977   -615   1385  -1351       N  
ATOM   2284  CA  ILE A 297      16.373  39.024  51.788  1.00 89.55           C  
ANISOU 2284  CA  ILE A 297    12938  10868  10218   -513   1313  -1307       C  
ATOM   2285  C   ILE A 297      15.077  39.800  51.923  1.00 94.26           C  
ANISOU 2285  C   ILE A 297    13541  11375  10899   -348   1476  -1349       C  
ATOM   2286  O   ILE A 297      14.990  40.674  52.779  1.00101.24           O  
ANISOU 2286  O   ILE A 297    14557  12183  11728   -416   1667  -1437       O  
ATOM   2287  CB  ILE A 297      16.463  38.100  53.021  1.00 90.96           C  
ANISOU 2287  CB  ILE A 297    13033  11200  10328   -706   1285  -1315       C  
ATOM   2288  CG1 ILE A 297      17.836  37.423  53.102  1.00 89.72           C  
ANISOU 2288  CG1 ILE A 297    12877  11140  10073   -885   1155  -1263       C  
ATOM   2289  CG2 ILE A 297      15.351  37.062  52.995  1.00 87.16           C  
ANISOU 2289  CG2 ILE A 297    12353  10815   9950   -610   1207  -1266       C  
ATOM   2290  CD1 ILE A 297      17.922  36.334  54.151  1.00 89.41           C  
ANISOU 2290  CD1 ILE A 297    12728  11266   9978  -1045   1099  -1232       C  
ATOM   2291  N   PRO A 298      14.059  39.472  51.111  1.00 97.47           N  
ANISOU 2291  N   PRO A 298    13802  11798  11432   -138   1408  -1284       N  
ATOM   2292  CA  PRO A 298      12.763  40.154  51.220  1.00102.01           C  
ANISOU 2292  CA  PRO A 298    14348  12313  12100     41   1560  -1298       C  
ATOM   2293  C   PRO A 298      12.258  40.211  52.678  1.00106.18           C  
ANISOU 2293  C   PRO A 298    14881  12872  12590    -72   1718  -1378       C  
ATOM   2294  O   PRO A 298      12.496  39.282  53.453  1.00103.99           O  
ANISOU 2294  O   PRO A 298    14532  12724  12254   -247   1646  -1387       O  
ATOM   2295  CB  PRO A 298      11.836  39.309  50.331  1.00101.23           C  
ANISOU 2295  CB  PRO A 298    14029  12317  12117    205   1402  -1202       C  
ATOM   2296  CG  PRO A 298      12.730  38.488  49.460  1.00100.27           C  
ANISOU 2296  CG  PRO A 298    13882  12248  11968    149   1192  -1146       C  
ATOM   2297  CD  PRO A 298      14.002  38.297  50.223  1.00 97.98           C  
ANISOU 2297  CD  PRO A 298    13704  11970  11555    -86   1190  -1193       C  
ATOM   2298  N   GLU A 299      11.561  41.291  53.030  1.00110.48           N  
ANISOU 2298  N   GLU A 299    15514  13295  13169     34   1942  -1428       N  
ATOM   2299  CA  GLU A 299      11.383  41.673  54.436  1.00112.01           C  
ANISOU 2299  CA  GLU A 299    15801  13467  13290   -106   2142  -1531       C  
ATOM   2300  C   GLU A 299      10.522  40.703  55.255  1.00110.88           C  
ANISOU 2300  C   GLU A 299    15473  13481  13177   -150   2116  -1524       C  
ATOM   2301  O   GLU A 299      10.900  40.333  56.368  1.00112.85           O  
ANISOU 2301  O   GLU A 299    15758  13803  13318   -370   2144  -1585       O  
ATOM   2302  CB  GLU A 299      10.816  43.098  54.535  1.00113.32           C  
ANISOU 2302  CB  GLU A 299    16123  13437  13496     41   2415  -1583       C  
ATOM   2303  CG  GLU A 299      11.321  43.876  55.731  1.00112.93           C  
ANISOU 2303  CG  GLU A 299    16306  13291  13312   -165   2637  -1720       C  
ATOM   2304  CD  GLU A 299      10.903  45.335  55.723  1.00117.92           C  
ANISOU 2304  CD  GLU A 299    17134  13691  13980    -22   2925  -1775       C  
ATOM   2305  OE1 GLU A 299      11.255  46.018  54.740  1.00123.47           O  
ANISOU 2305  OE1 GLU A 299    17933  14263  14717    103   2929  -1738       O  
ATOM   2306  OE2 GLU A 299      10.248  45.802  56.697  1.00111.11           O  
ANISOU 2306  OE2 GLU A 299    16340  12767  13109    -36   3160  -1853       O  
ATOM   2307  N   ASN A 300       9.376  40.291  54.720  1.00108.05           N  
ANISOU 2307  N   ASN A 300    14913  13186  12954     47   2062  -1446       N  
ATOM   2308  CA  ASN A 300       8.466  39.436  55.487  1.00109.47           C  
ANISOU 2308  CA  ASN A 300    14916  13508  13169     11   2058  -1441       C  
ATOM   2309  C   ASN A 300       8.115  38.157  54.753  1.00108.32           C  
ANISOU 2309  C   ASN A 300    14541  13520  13097     52   1817  -1343       C  
ATOM   2310  O   ASN A 300       7.073  38.082  54.111  1.00114.43           O  
ANISOU 2310  O   ASN A 300    15154  14334  13989    242   1790  -1275       O  
ATOM   2311  CB  ASN A 300       7.191  40.206  55.877  1.00110.63           C  
ANISOU 2311  CB  ASN A 300    15034  13594  13409    184   2286  -1457       C  
ATOM   2312  N   LEU A 301       8.981  37.146  54.867  1.00105.39           N  
ANISOU 2312  N   LEU A 301    14154  13240  12648   -132   1649  -1331       N  
ATOM   2313  CA  LEU A 301       8.749  35.852  54.221  1.00101.77           C  
ANISOU 2313  CA  LEU A 301    13508  12914  12245   -125   1434  -1249       C  
ATOM   2314  C   LEU A 301       8.109  34.818  55.133  1.00 99.88           C  
ANISOU 2314  C   LEU A 301    13124  12813  12010   -233   1422  -1251       C  
ATOM   2315  O   LEU A 301       8.510  34.671  56.292  1.00 95.07           O  
ANISOU 2315  O   LEU A 301    12584  12230  11308   -409   1494  -1302       O  
ATOM   2316  CB  LEU A 301      10.047  35.290  53.641  1.00 99.53           C  
ANISOU 2316  CB  LEU A 301    13288  12636  11895   -229   1263  -1216       C  
ATOM   2317  CG  LEU A 301      10.364  35.820  52.242  1.00100.20           C  
ANISOU 2317  CG  LEU A 301    13420  12632  12019    -76   1189  -1173       C  
ATOM   2318  CD1 LEU A 301      11.772  35.427  51.825  1.00 93.26           C  
ANISOU 2318  CD1 LEU A 301    12633  11741  11061   -193   1062  -1151       C  
ATOM   2319  CD2 LEU A 301       9.331  35.303  51.246  1.00 98.33           C  
ANISOU 2319  CD2 LEU A 301    12997  12467  11895     85   1076  -1099       C  
ATOM   2320  N   PRO A 302       7.115  34.082  54.600  1.00100.65           N  
ANISOU 2320  N   PRO A 302    13022  13011  12210   -141   1327  -1190       N  
ATOM   2321  CA  PRO A 302       6.517  32.962  55.331  1.00102.39           C  
ANISOU 2321  CA  PRO A 302    13097  13366  12440   -251   1295  -1183       C  
ATOM   2322  C   PRO A 302       7.553  31.908  55.686  1.00100.48           C  
ANISOU 2322  C   PRO A 302    12896  13173  12108   -454   1177  -1170       C  
ATOM   2323  O   PRO A 302       8.456  31.665  54.900  1.00101.51           O  
ANISOU 2323  O   PRO A 302    13084  13272  12214   -465   1050  -1134       O  
ATOM   2324  CB  PRO A 302       5.486  32.383  54.344  1.00102.85           C  
ANISOU 2324  CB  PRO A 302    12949  13516  12612   -123   1175  -1112       C  
ATOM   2325  CG  PRO A 302       5.777  33.009  53.019  1.00101.99           C  
ANISOU 2325  CG  PRO A 302    12885  13331  12534     31   1102  -1072       C  
ATOM   2326  CD  PRO A 302       6.454  34.317  53.302  1.00101.62           C  
ANISOU 2326  CD  PRO A 302    13042  13132  12435     67   1252  -1124       C  
ATOM   2327  N   PRO A 303       7.418  31.270  56.854  1.00104.02           N  
ANISOU 2327  N   PRO A 303    13312  13701  12509   -605   1224  -1189       N  
ATOM   2328  CA  PRO A 303       8.409  30.282  57.256  1.00106.62           C  
ANISOU 2328  CA  PRO A 303    13676  14081  12752   -785   1126  -1157       C  
ATOM   2329  C   PRO A 303       8.275  28.992  56.451  1.00110.85           C  
ANISOU 2329  C   PRO A 303    14089  14679  13351   -783    953  -1082       C  
ATOM   2330  O   PRO A 303       7.186  28.662  55.959  1.00110.86           O  
ANISOU 2330  O   PRO A 303    13946  14727  13448   -696    923  -1068       O  
ATOM   2331  CB  PRO A 303       8.073  30.038  58.724  1.00108.87           C  
ANISOU 2331  CB  PRO A 303    13950  14439  12979   -925   1243  -1193       C  
ATOM   2332  CG  PRO A 303       6.599  30.248  58.794  1.00110.08           C  
ANISOU 2332  CG  PRO A 303    13971  14620  13235   -808   1336  -1216       C  
ATOM   2333  CD  PRO A 303       6.250  31.274  57.750  1.00108.62           C  
ANISOU 2333  CD  PRO A 303    13795  14346  13131   -602   1357  -1221       C  
ATOM   2334  N   LEU A 304       9.384  28.269  56.332  1.00113.54           N  
ANISOU 2334  N   LEU A 304    14487  15021  13632   -884    850  -1033       N  
ATOM   2335  CA  LEU A 304       9.451  27.089  55.477  1.00114.44           C  
ANISOU 2335  CA  LEU A 304    14528  15160  13795   -884    702   -967       C  
ATOM   2336  C   LEU A 304       8.420  26.054  55.903  1.00113.03           C  
ANISOU 2336  C   LEU A 304    14204  15074  13668   -940    700   -955       C  
ATOM   2337  O   LEU A 304       7.737  25.471  55.058  1.00114.47           O  
ANISOU 2337  O   LEU A 304    14285  15281  13928   -889    619   -936       O  
ATOM   2338  CB  LEU A 304      10.865  26.493  55.499  1.00117.38           C  
ANISOU 2338  CB  LEU A 304    14992  15516  14091   -986    630   -906       C  
ATOM   2339  N   THR A 305       8.288  25.860  57.215  1.00113.19           N  
ANISOU 2339  N   THR A 305    14219  15151  13637  -1055    794   -968       N  
ATOM   2340  CA  THR A 305       7.369  24.858  57.763  1.00114.32           C  
ANISOU 2340  CA  THR A 305    14235  15382  13818  -1129    807   -956       C  
ATOM   2341  C   THR A 305       5.979  24.949  57.120  1.00114.25           C  
ANISOU 2341  C   THR A 305    14077  15413  13921  -1019    802   -980       C  
ATOM   2342  O   THR A 305       5.349  23.925  56.868  1.00114.26           O  
ANISOU 2342  O   THR A 305    13967  15472  13973  -1063    742   -954       O  
ATOM   2343  CB  THR A 305       7.241  24.966  59.303  1.00113.96           C  
ANISOU 2343  CB  THR A 305    14206  15393  13699  -1245    940   -982       C  
ATOM   2344  OG1 THR A 305       6.815  26.284  59.661  1.00118.02           O  
ANISOU 2344  OG1 THR A 305    14756  15880  14208  -1172   1071  -1059       O  
ATOM   2345  CG2 THR A 305       8.574  24.661  59.998  1.00109.66           C  
ANISOU 2345  CG2 THR A 305    13778  14853  13033  -1380    925   -934       C  
ATOM   2346  N   ALA A 306       5.525  26.168  56.833  1.00115.31           N  
ANISOU 2346  N   ALA A 306    14209  15515  14089   -879    868  -1021       N  
ATOM   2347  CA  ALA A 306       4.202  26.399  56.238  1.00118.54           C  
ANISOU 2347  CA  ALA A 306    14459  15980  14601   -754    870  -1025       C  
ATOM   2348  C   ALA A 306       3.953  25.540  54.992  1.00119.86           C  
ANISOU 2348  C   ALA A 306    14535  16185  14822   -739    705   -980       C  
ATOM   2349  O   ALA A 306       2.943  24.830  54.906  1.00120.50           O  
ANISOU 2349  O   ALA A 306    14459  16367  14958   -771    676   -968       O  
ATOM   2350  CB  ALA A 306       4.020  27.877  55.910  1.00114.85           C  
ANISOU 2350  CB  ALA A 306    14033  15447  14159   -580    957  -1052       C  
ATOM   2351  N   ASP A 307       4.887  25.589  54.045  1.00118.00           N  
ANISOU 2351  N   ASP A 307    14403  15870  14561   -706    603   -958       N  
ATOM   2352  CA  ASP A 307       4.710  24.944  52.747  1.00117.03           C  
ANISOU 2352  CA  ASP A 307    14223  15769  14476   -684    455   -925       C  
ATOM   2353  C   ASP A 307       5.316  23.526  52.664  1.00111.23           C  
ANISOU 2353  C   ASP A 307    13529  15021  13710   -837    372   -898       C  
ATOM   2354  O   ASP A 307       4.916  22.741  51.807  1.00112.24           O  
ANISOU 2354  O   ASP A 307    13594  15184  13867   -866    273   -884       O  
ATOM   2355  CB  ASP A 307       5.282  25.847  51.635  1.00116.61           C  
ANISOU 2355  CB  ASP A 307    14257  15632  14417   -544    399   -915       C  
ATOM   2356  CG  ASP A 307       4.399  27.076  51.337  1.00117.50           C  
ANISOU 2356  CG  ASP A 307    14292  15767  14584   -365    459   -918       C  
ATOM   2357  OD1 ASP A 307       4.846  27.952  50.574  1.00110.28           O  
ANISOU 2357  OD1 ASP A 307    13461  14776  13665   -242    442   -908       O  
ATOM   2358  OD2 ASP A 307       3.263  27.182  51.847  1.00117.44           O  
ANISOU 2358  OD2 ASP A 307    14140  15852  14629   -338    532   -923       O  
ATOM   2359  N   PHE A 308       6.247  23.184  53.550  1.00103.16           N  
ANISOU 2359  N   PHE A 308    12614  13955  12627   -936    419   -885       N  
ATOM   2360  CA  PHE A 308       6.964  21.903  53.443  1.00100.54           C  
ANISOU 2360  CA  PHE A 308    12339  13590  12270  -1053    358   -839       C  
ATOM   2361  C   PHE A 308       6.846  20.934  54.626  1.00104.42           C  
ANISOU 2361  C   PHE A 308    12804  14127  12742  -1198    421   -817       C  
ATOM   2362  O   PHE A 308       7.534  19.906  54.624  1.00 98.06           O  
ANISOU 2362  O   PHE A 308    12061  13281  11916  -1283    391   -764       O  
ATOM   2363  CB  PHE A 308       8.440  22.185  53.198  1.00100.10           C  
ANISOU 2363  CB  PHE A 308    12440  13438  12156  -1033    332   -806       C  
ATOM   2364  CG  PHE A 308       8.681  23.074  52.031  1.00 97.91           C  
ANISOU 2364  CG  PHE A 308    12208  13104  11891   -900    274   -821       C  
ATOM   2365  CD1 PHE A 308       8.580  22.585  50.740  1.00 96.39           C  
ANISOU 2365  CD1 PHE A 308    12007  12888  11728   -869    169   -810       C  
ATOM   2366  CD2 PHE A 308       8.984  24.411  52.223  1.00 99.75           C  
ANISOU 2366  CD2 PHE A 308    12500  13302  12096   -813    332   -849       C  
ATOM   2367  CE1 PHE A 308       8.782  23.413  49.652  1.00 97.31           C  
ANISOU 2367  CE1 PHE A 308    12166  12958  11848   -745    114   -817       C  
ATOM   2368  CE2 PHE A 308       9.191  25.246  51.144  1.00 99.97           C  
ANISOU 2368  CE2 PHE A 308    12576  13272  12137   -686    286   -856       C  
ATOM   2369  CZ  PHE A 308       9.088  24.747  49.854  1.00 98.99           C  
ANISOU 2369  CZ  PHE A 308    12434  13134  12042   -647    173   -836       C  
ATOM   2370  N   ALA A 309       5.999  21.241  55.621  1.00109.51           N  
ANISOU 2370  N   ALA A 309    13364  14850  13395  -1222    517   -850       N  
ATOM   2371  CA  ALA A 309       5.808  20.358  56.800  1.00108.64           C  
ANISOU 2371  CA  ALA A 309    13227  14791  13262  -1362    585   -828       C  
ATOM   2372  C   ALA A 309       4.394  20.397  57.415  1.00108.28           C  
ANISOU 2372  C   ALA A 309    13030  14847  13263  -1383    663   -871       C  
ATOM   2373  O   ALA A 309       3.775  19.356  57.637  1.00108.11           O  
ANISOU 2373  O   ALA A 309    12932  14877  13270  -1486    664   -858       O  
ATOM   2374  CB  ALA A 309       6.836  20.690  57.873  1.00106.44           C  
ANISOU 2374  CB  ALA A 309    13060  14494  12889  -1413    653   -803       C  
ATOM   2375  N   GLU A 310       3.902  21.596  57.710  1.00108.20           N  
ANISOU 2375  N   GLU A 310    12985  14863  13262  -1287    741   -919       N  
ATOM   2376  CA  GLU A 310       2.551  21.777  58.260  1.00109.25           C  
ANISOU 2376  CA  GLU A 310    12966  15094  13448  -1279    832   -954       C  
ATOM   2377  C   GLU A 310       1.447  21.578  57.203  1.00109.73           C  
ANISOU 2377  C   GLU A 310    12863  15228  13601  -1218    753   -954       C  
ATOM   2378  O   GLU A 310       0.343  21.172  57.535  1.00110.16           O  
ANISOU 2378  O   GLU A 310    12767  15386  13703  -1264    792   -961       O  
ATOM   2379  CB  GLU A 310       2.411  23.159  58.918  1.00105.78           C  
ANISOU 2379  CB  GLU A 310    12558  14642  12990  -1185    966  -1002       C  
ATOM   2380  N   ASP A 311       1.751  21.847  55.938  1.00114.54           N  
ANISOU 2380  N   ASP A 311    13496  15796  14228  -1125    641   -943       N  
ATOM   2381  CA  ASP A 311       0.758  21.733  54.867  1.00120.85           C  
ANISOU 2381  CA  ASP A 311    14140  16682  15095  -1071    553   -936       C  
ATOM   2382  C   ASP A 311       0.332  20.280  54.676  1.00124.42           C  
ANISOU 2382  C   ASP A 311    14523  17194  15558  -1237    484   -925       C  
ATOM   2383  O   ASP A 311       1.166  19.374  54.734  1.00119.83           O  
ANISOU 2383  O   ASP A 311    14064  16532  14934  -1349    454   -911       O  
ATOM   2384  CB  ASP A 311       1.310  22.285  53.542  1.00122.80           C  
ANISOU 2384  CB  ASP A 311    14454  16866  15339   -951    443   -921       C  
ATOM   2385  CG  ASP A 311       0.209  22.660  52.558  1.00123.23           C  
ANISOU 2385  CG  ASP A 311    14334  17033  15455   -847    376   -905       C  
ATOM   2386  OD1 ASP A 311      -0.468  23.688  52.791  1.00121.82           O  
ANISOU 2386  OD1 ASP A 311    14064  16903  15320   -708    459   -900       O  
ATOM   2387  OD2 ASP A 311       0.030  21.935  51.554  1.00121.47           O  
ANISOU 2387  OD2 ASP A 311    14069  16853  15231   -905    246   -892       O  
ATOM   2388  N   LYS A 312      -0.959  20.083  54.404  1.00129.12           N  
ANISOU 2388  N   LYS A 312    14922  17929  16210  -1250    465   -927       N  
ATOM   2389  CA  LYS A 312      -1.575  18.753  54.374  1.00130.19           C  
ANISOU 2389  CA  LYS A 312    14974  18139  16355  -1431    427   -929       C  
ATOM   2390  C   LYS A 312      -1.605  18.081  52.995  1.00129.38           C  
ANISOU 2390  C   LYS A 312    14865  18047  16244  -1489    276   -926       C  
ATOM   2391  O   LYS A 312      -2.118  16.969  52.876  1.00127.67           O  
ANISOU 2391  O   LYS A 312    14595  17885  16030  -1656    247   -937       O  
ATOM   2392  CB  LYS A 312      -3.007  18.845  54.906  1.00135.09           C  
ANISOU 2392  CB  LYS A 312    15369  18926  17033  -1444    495   -933       C  
ATOM   2393  N   ASP A 313      -1.050  18.739  51.973  1.00128.37           N  
ANISOU 2393  N   ASP A 313    14807  17866  16102  -1365    191   -917       N  
ATOM   2394  CA  ASP A 313      -1.049  18.227  50.592  1.00127.17           C  
ANISOU 2394  CA  ASP A 313    14664  17726  15929  -1413     49   -918       C  
ATOM   2395  C   ASP A 313       0.375  18.018  50.057  1.00122.71           C  
ANISOU 2395  C   ASP A 313    14330  16981  15313  -1405      7   -915       C  
ATOM   2396  O   ASP A 313       0.596  17.994  48.838  1.00125.91           O  
ANISOU 2396  O   ASP A 313    14778  17370  15694  -1386   -101   -916       O  
ATOM   2397  CB  ASP A 313      -1.792  19.209  49.670  1.00129.49           C  
ANISOU 2397  CB  ASP A 313    14808  18144  16247  -1263    -28   -895       C  
ATOM   2398  CG  ASP A 313      -3.298  19.225  49.904  1.00134.41           C  
ANISOU 2398  CG  ASP A 313    15170  18979  16922  -1285    -15   -881       C  
ATOM   2399  OD1 ASP A 313      -3.824  18.328  50.594  1.00134.54           O  
ANISOU 2399  OD1 ASP A 313    15121  19051  16948  -1448     33   -901       O  
ATOM   2400  OD2 ASP A 313      -3.966  20.143  49.380  1.00136.45           O  
ANISOU 2400  OD2 ASP A 313    15280  19353  17211  -1133    -49   -839       O  
ATOM   2401  N   VAL A 314       1.332  17.836  50.964  1.00111.77           N  
ANISOU 2401  N   VAL A 314    13088  15474  13908  -1426     93   -906       N  
ATOM   2402  CA  VAL A 314       2.748  17.802  50.596  1.00107.23           C  
ANISOU 2402  CA  VAL A 314    12714  14738  13289  -1393     71   -887       C  
ATOM   2403  C   VAL A 314       3.128  16.616  49.689  1.00107.34           C  
ANISOU 2403  C   VAL A 314    12827  14679  13279  -1511      3   -889       C  
ATOM   2404  O   VAL A 314       3.746  16.810  48.645  1.00105.66           O  
ANISOU 2404  O   VAL A 314    12707  14397  13041  -1452    -71   -887       O  
ATOM   2405  CB  VAL A 314       3.620  17.864  51.864  1.00102.76           C  
ANISOU 2405  CB  VAL A 314    12250  14093  12699  -1400    178   -861       C  
ATOM   2406  CG1 VAL A 314       5.084  17.644  51.543  1.00 99.67           C  
ANISOU 2406  CG1 VAL A 314    12047  13557  12265  -1386    158   -824       C  
ATOM   2407  CG2 VAL A 314       3.428  19.205  52.553  1.00102.17           C  
ANISOU 2407  CG2 VAL A 314    12127  14061  12632  -1275    249   -873       C  
ATOM   2408  N   CYS A 315       2.741  15.402  50.067  1.00113.79           N  
ANISOU 2408  N   CYS A 315    13631  15504  14102  -1680     38   -896       N  
ATOM   2409  CA  CYS A 315       2.988  14.219  49.227  1.00117.08           C  
ANISOU 2409  CA  CYS A 315    14151  15838  14494  -1809     -1   -909       C  
ATOM   2410  C   CYS A 315       2.316  14.376  47.868  1.00119.41           C  
ANISOU 2410  C   CYS A 315    14378  16219  14775  -1818   -123   -950       C  
ATOM   2411  O   CYS A 315       2.913  14.071  46.839  1.00114.31           O  
ANISOU 2411  O   CYS A 315    13859  15483  14092  -1830   -178   -959       O  
ATOM   2412  CB  CYS A 315       2.486  12.924  49.894  1.00121.16           C  
ANISOU 2412  CB  CYS A 315    14656  16358  15024  -2001     72   -915       C  
ATOM   2413  SG  CYS A 315       3.407  12.365  51.358  1.00127.96           S  
ANISOU 2413  SG  CYS A 315    15631  17102  15885  -2025    212   -845       S  
ATOM   2414  N   LYS A 316       1.066  14.839  47.878  1.00125.36           N  
ANISOU 2414  N   LYS A 316    14924  17157  15552  -1813   -160   -967       N  
ATOM   2415  CA  LYS A 316       0.311  15.067  46.647  1.00127.63           C  
ANISOU 2415  CA  LYS A 316    15106  17570  15816  -1819   -286   -988       C  
ATOM   2416  C   LYS A 316       1.108  15.920  45.661  1.00127.99           C  
ANISOU 2416  C   LYS A 316    15252  17547  15832  -1660   -360   -971       C  
ATOM   2417  O   LYS A 316       1.301  15.534  44.503  1.00130.19           O  
ANISOU 2417  O   LYS A 316    15608  17800  16059  -1718   -445   -992       O  
ATOM   2418  N   ASN A 317       1.576  17.072  46.137  1.00122.99           N  
ANISOU 2418  N   ASN A 317    14627  16878  15225  -1471   -319   -937       N  
ATOM   2419  CA  ASN A 317       2.341  18.003  45.302  1.00120.14           C  
ANISOU 2419  CA  ASN A 317    14360  16448  14840  -1309   -374   -917       C  
ATOM   2420  C   ASN A 317       3.705  17.424  44.917  1.00114.18           C  
ANISOU 2420  C   ASN A 317    13838  15502  14045  -1343   -366   -918       C  
ATOM   2421  O   ASN A 317       4.157  17.568  43.777  1.00107.20           O  
ANISOU 2421  O   ASN A 317    13041  14570  13120  -1305   -443   -920       O  
ATOM   2422  CB  ASN A 317       2.524  19.348  46.022  1.00123.72           C  
ANISOU 2422  CB  ASN A 317    14785  16894  15330  -1120   -305   -888       C  
ATOM   2423  CG  ASN A 317       1.196  20.008  46.406  1.00127.31           C  
ANISOU 2423  CG  ASN A 317    15012  17525  15834  -1054   -288   -876       C  
ATOM   2424  OD1 ASN A 317       0.206  19.926  45.679  1.00126.40           O  
ANISOU 2424  OD1 ASN A 317    14744  17562  15719  -1077   -375   -867       O  
ATOM   2425  ND2 ASN A 317       1.178  20.671  47.560  1.00127.99           N  
ANISOU 2425  ND2 ASN A 317    15075  17599  15958   -976   -170   -870       N  
ATOM   2426  N   TYR A 318       4.346  16.763  45.880  1.00108.01           N  
ANISOU 2426  N   TYR A 318    13149  14617  13275  -1411   -268   -908       N  
ATOM   2427  CA  TYR A 318       5.642  16.124  45.660  1.00105.89           C  
ANISOU 2427  CA  TYR A 318    13084  14171  12979  -1437   -238   -889       C  
ATOM   2428  C   TYR A 318       5.541  14.996  44.636  1.00111.07           C  
ANISOU 2428  C   TYR A 318    13817  14783  13601  -1579   -282   -923       C  
ATOM   2429  O   TYR A 318       6.366  14.903  43.726  1.00107.52           O  
ANISOU 2429  O   TYR A 318    13512  14224  13117  -1550   -311   -920       O  
ATOM   2430  CB  TYR A 318       6.214  15.607  46.989  1.00101.73           C  
ANISOU 2430  CB  TYR A 318    12609  13573  12470  -1482   -122   -850       C  
ATOM   2431  CG  TYR A 318       7.368  14.636  46.863  1.00 97.82           C  
ANISOU 2431  CG  TYR A 318    12296  12913  11958  -1533    -73   -811       C  
ATOM   2432  CD1 TYR A 318       8.624  15.056  46.439  1.00 98.61           C  
ANISOU 2432  CD1 TYR A 318    12527  12904  12037  -1426    -79   -770       C  
ATOM   2433  CD2 TYR A 318       7.205  13.298  47.191  1.00 99.22           C  
ANISOU 2433  CD2 TYR A 318    12514  13041  12144  -1685     -9   -806       C  
ATOM   2434  CE1 TYR A 318       9.688  14.165  46.339  1.00100.16           C  
ANISOU 2434  CE1 TYR A 318    12878  12954  12226  -1456    -21   -718       C  
ATOM   2435  CE2 TYR A 318       8.255  12.399  47.092  1.00101.37           C  
ANISOU 2435  CE2 TYR A 318    12954  13151  12410  -1713     57   -755       C  
ATOM   2436  CZ  TYR A 318       9.495  12.834  46.667  1.00102.97           C  
ANISOU 2436  CZ  TYR A 318    13272  13256  12596  -1592     51   -707       C  
ATOM   2437  OH  TYR A 318      10.528  11.924  46.570  1.00105.11           O  
ANISOU 2437  OH  TYR A 318    13698  13371  12869  -1606    129   -641       O  
ATOM   2438  N   GLN A 319       4.527  14.145  44.791  1.00113.34           N  
ANISOU 2438  N   GLN A 319    14016  15154  13894  -1742   -279   -960       N  
ATOM   2439  CA  GLN A 319       4.302  13.034  43.868  1.00112.01           C  
ANISOU 2439  CA  GLN A 319    13925  14950  13682  -1913   -308  -1008       C  
ATOM   2440  C   GLN A 319       4.099  13.516  42.427  1.00113.20           C  
ANISOU 2440  C   GLN A 319    14071  15162  13776  -1884   -437  -1038       C  
ATOM   2441  O   GLN A 319       4.515  12.843  41.480  1.00107.72           O  
ANISOU 2441  O   GLN A 319    13528  14372  13030  -1970   -452  -1070       O  
ATOM   2442  CB  GLN A 319       3.090  12.204  44.314  1.00113.49           C  
ANISOU 2442  CB  GLN A 319    13988  15253  13881  -2104   -289  -1047       C  
ATOM   2443  N   GLU A 320       3.465  14.679  42.273  1.00116.24           N  
ANISOU 2443  N   GLU A 320    14292  15705  14170  -1759   -518  -1022       N  
ATOM   2444  CA  GLU A 320       3.069  15.196  40.961  1.00117.26           C  
ANISOU 2444  CA  GLU A 320    14375  15936  14241  -1728   -650  -1034       C  
ATOM   2445  C   GLU A 320       4.112  16.065  40.259  1.00120.38           C  
ANISOU 2445  C   GLU A 320    14899  16226  14614  -1551   -681  -1004       C  
ATOM   2446  O   GLU A 320       3.948  16.386  39.083  1.00127.34           O  
ANISOU 2446  O   GLU A 320    15782  17166  15435  -1534   -786  -1010       O  
ATOM   2447  CB  GLU A 320       1.739  15.929  41.090  1.00118.94           C  
ANISOU 2447  CB  GLU A 320    14327  16389  14477  -1684   -719  -1015       C  
ATOM   2448  CG  GLU A 320       0.604  14.944  41.330  1.00125.72           C  
ANISOU 2448  CG  GLU A 320    15055  17383  15328  -1904   -724  -1054       C  
ATOM   2449  CD  GLU A 320      -0.656  15.586  41.864  1.00129.30           C  
ANISOU 2449  CD  GLU A 320    15234  18064  15831  -1853   -746  -1020       C  
ATOM   2450  OE1 GLU A 320      -1.195  15.073  42.867  1.00127.50           O  
ANISOU 2450  OE1 GLU A 320    14920  17876  15648  -1949   -668  -1032       O  
ATOM   2451  OE2 GLU A 320      -1.105  16.597  41.285  1.00137.40           O  
ANISOU 2451  OE2 GLU A 320    16128  19225  16851  -1710   -833   -974       O  
ATOM   2452  N   ALA A 321       5.188  16.428  40.956  1.00117.07           N  
ANISOU 2452  N   ALA A 321    14587  15660  14234  -1433   -592   -968       N  
ATOM   2453  CA  ALA A 321       6.286  17.183  40.333  1.00110.21           C  
ANISOU 2453  CA  ALA A 321    13854  14678  13343  -1283   -608   -940       C  
ATOM   2454  C   ALA A 321       7.574  17.076  41.165  1.00 99.24           C  
ANISOU 2454  C   ALA A 321    12603  13118  11984  -1233   -496   -905       C  
ATOM   2455  O   ALA A 321       8.131  18.077  41.584  1.00 91.27           O  
ANISOU 2455  O   ALA A 321    11600  12083  10994  -1088   -470   -869       O  
ATOM   2456  CB  ALA A 321       5.880  18.643  40.138  1.00111.60           C  
ANISOU 2456  CB  ALA A 321    13910  14962  13530  -1103   -667   -908       C  
ATOM   2457  N   LYS A 322       8.046  15.850  41.369  1.00 95.20           N  
ANISOU 2457  N   LYS A 322    12205  12495  11471  -1358   -425   -910       N  
ATOM   2458  CA  LYS A 322       9.091  15.567  42.351  1.00 93.03           C  
ANISOU 2458  CA  LYS A 322    12021  12097  11229  -1331   -314   -855       C  
ATOM   2459  C   LYS A 322      10.235  16.556  42.281  1.00 93.62           C  
ANISOU 2459  C   LYS A 322    12173  12100  11298  -1169   -309   -808       C  
ATOM   2460  O   LYS A 322      10.603  17.154  43.290  1.00 93.35           O  
ANISOU 2460  O   LYS A 322    12104  12077  11287  -1101   -259   -769       O  
ATOM   2461  CB  LYS A 322       9.630  14.136  42.187  1.00 88.70           C  
ANISOU 2461  CB  LYS A 322    11622  11406  10674  -1456   -239   -851       C  
ATOM   2462  N   ASP A 323      10.778  16.752  41.085  1.00 97.30           N  
ANISOU 2462  N   ASP A 323    12745  12499  11726  -1120   -358   -815       N  
ATOM   2463  CA  ASP A 323      11.998  17.550  40.923  1.00 96.80           C  
ANISOU 2463  CA  ASP A 323    12777  12350  11654   -985   -344   -767       C  
ATOM   2464  C   ASP A 323      11.746  19.051  41.061  1.00 91.28           C  
ANISOU 2464  C   ASP A 323    11990  11735  10957   -851   -387   -767       C  
ATOM   2465  O   ASP A 323      12.546  19.760  41.664  1.00 90.47           O  
ANISOU 2465  O   ASP A 323    11917  11595  10862   -769   -340   -728       O  
ATOM   2466  CB  ASP A 323      12.674  17.210  39.602  1.00101.31           C  
ANISOU 2466  CB  ASP A 323    13500  12813  12181   -982   -367   -774       C  
ATOM   2467  CG  ASP A 323      13.157  15.762  39.560  1.00107.40           C  
ANISOU 2467  CG  ASP A 323    14393  13459  12957  -1093   -282   -763       C  
ATOM   2468  OD1 ASP A 323      14.386  15.545  39.574  1.00106.73           O  
ANISOU 2468  OD1 ASP A 323    14425  13249  12880  -1041   -210   -701       O  
ATOM   2469  OD2 ASP A 323      12.311  14.835  39.543  1.00114.26           O  
ANISOU 2469  OD2 ASP A 323    15238  14353  13824  -1233   -277   -810       O  
ATOM   2470  N   ALA A 324      10.622  19.525  40.529  1.00 90.41           N  
ANISOU 2470  N   ALA A 324    11770  11742  10840   -833   -468   -804       N  
ATOM   2471  CA  ALA A 324      10.205  20.925  40.719  1.00 87.80           C  
ANISOU 2471  CA  ALA A 324    11346  11490  10524   -697   -488   -797       C  
ATOM   2472  C   ALA A 324       9.975  21.260  42.203  1.00 85.74           C  
ANISOU 2472  C   ALA A 324    10999  11272  10308   -690   -403   -788       C  
ATOM   2473  O   ALA A 324      10.416  22.290  42.704  1.00 81.86           O  
ANISOU 2473  O   ALA A 324    10526  10757   9822   -590   -357   -772       O  
ATOM   2474  CB  ALA A 324       8.953  21.222  39.910  1.00 84.80           C  
ANISOU 2474  CB  ALA A 324    10840  11247  10131   -681   -586   -817       C  
ATOM   2475  N   PHE A 325       9.262  20.381  42.894  1.00 86.31           N  
ANISOU 2475  N   PHE A 325    10985  11406  10404   -808   -377   -804       N  
ATOM   2476  CA  PHE A 325       8.981  20.563  44.315  1.00 86.54           C  
ANISOU 2476  CA  PHE A 325    10934  11482  10467   -823   -292   -799       C  
ATOM   2477  C   PHE A 325      10.266  20.590  45.147  1.00 80.51           C  
ANISOU 2477  C   PHE A 325    10283  10618   9689   -821   -211   -760       C  
ATOM   2478  O   PHE A 325      10.409  21.420  46.024  1.00 76.33           O  
ANISOU 2478  O   PHE A 325     9736  10107   9161   -771   -152   -755       O  
ATOM   2479  CB  PHE A 325       8.052  19.450  44.801  1.00 90.12           C  
ANISOU 2479  CB  PHE A 325    11290  12010  10942   -968   -279   -820       C  
ATOM   2480  CG  PHE A 325       7.410  19.736  46.116  1.00 90.31           C  
ANISOU 2480  CG  PHE A 325    11197  12117  11000   -978   -203   -823       C  
ATOM   2481  CD1 PHE A 325       6.326  20.595  46.193  1.00 94.39           C  
ANISOU 2481  CD1 PHE A 325    11564  12753  11545   -901   -212   -840       C  
ATOM   2482  CD2 PHE A 325       7.886  19.151  47.277  1.00 90.85           C  
ANISOU 2482  CD2 PHE A 325    11303  12146  11069  -1057   -115   -800       C  
ATOM   2483  CE1 PHE A 325       5.736  20.876  47.413  1.00 99.30           C  
ANISOU 2483  CE1 PHE A 325    12087  13444  12198   -906   -125   -846       C  
ATOM   2484  CE2 PHE A 325       7.303  19.421  48.501  1.00 92.68           C  
ANISOU 2484  CE2 PHE A 325    11438  12456  11321  -1074    -39   -807       C  
ATOM   2485  CZ  PHE A 325       6.224  20.289  48.573  1.00 97.42           C  
ANISOU 2485  CZ  PHE A 325    11900  13165  11952  -1000    -39   -836       C  
ATOM   2486  N   LEU A 326      11.197  19.687  44.854  1.00 79.05           N  
ANISOU 2486  N   LEU A 326    10216  10334   9486   -877   -204   -728       N  
ATOM   2487  CA  LEU A 326      12.481  19.664  45.542  1.00 79.38           C  
ANISOU 2487  CA  LEU A 326    10350  10301   9510   -872   -138   -668       C  
ATOM   2488  C   LEU A 326      13.324  20.878  45.172  1.00 80.58           C  
ANISOU 2488  C   LEU A 326    10572  10411   9634   -755   -150   -657       C  
ATOM   2489  O   LEU A 326      14.039  21.423  46.015  1.00 83.60           O  
ANISOU 2489  O   LEU A 326    10978  10790   9994   -743    -96   -627       O  
ATOM   2490  CB  LEU A 326      13.258  18.383  45.228  1.00 80.25           C  
ANISOU 2490  CB  LEU A 326    10563  10312   9618   -940   -115   -620       C  
ATOM   2491  CG  LEU A 326      12.807  17.068  45.872  1.00 83.88           C  
ANISOU 2491  CG  LEU A 326    10994  10776  10102  -1068    -62   -606       C  
ATOM   2492  CD1 LEU A 326      13.538  15.903  45.214  1.00 85.36           C  
ANISOU 2492  CD1 LEU A 326    11310  10835  10290  -1109    -32   -565       C  
ATOM   2493  CD2 LEU A 326      13.020  17.065  47.390  1.00 79.12           C  
ANISOU 2493  CD2 LEU A 326    10343  10222   9498  -1101     13   -554       C  
ATOM   2494  N   GLY A 327      13.255  21.305  43.915  1.00 76.97           N  
ANISOU 2494  N   GLY A 327    10152   9925   9168   -682   -219   -681       N  
ATOM   2495  CA  GLY A 327      13.887  22.557  43.539  1.00 75.99           C  
ANISOU 2495  CA  GLY A 327    10089   9764   9020   -568   -226   -676       C  
ATOM   2496  C   GLY A 327      13.313  23.682  44.394  1.00 74.08           C  
ANISOU 2496  C   GLY A 327     9771   9587   8787   -518   -182   -704       C  
ATOM   2497  O   GLY A 327      14.045  24.396  45.080  1.00 74.94           O  
ANISOU 2497  O   GLY A 327     9930   9673   8872   -502   -122   -691       O  
ATOM   2498  N   SER A 328      11.993  23.819  44.349  1.00 71.28           N  
ANISOU 2498  N   SER A 328     9297   9321   8466   -500   -204   -740       N  
ATOM   2499  CA  SER A 328      11.273  24.791  45.150  1.00 71.82           C  
ANISOU 2499  CA  SER A 328     9284   9449   8554   -444   -143   -765       C  
ATOM   2500  C   SER A 328      11.754  24.854  46.589  1.00 70.75           C  
ANISOU 2500  C   SER A 328     9168   9314   8402   -514    -44   -762       C  
ATOM   2501  O   SER A 328      12.107  25.920  47.086  1.00 71.64           O  
ANISOU 2501  O   SER A 328     9328   9400   8491   -467     23   -776       O  
ATOM   2502  CB  SER A 328       9.789  24.472  45.138  1.00 74.14           C  
ANISOU 2502  CB  SER A 328     9417   9859   8892   -456   -170   -787       C  
ATOM   2503  OG  SER A 328       9.139  25.254  46.117  1.00 77.00           O  
ANISOU 2503  OG  SER A 328     9702  10275   9281   -414    -82   -806       O  
ATOM   2504  N   PHE A 329      11.767  23.709  47.258  1.00 71.40           N  
ANISOU 2504  N   PHE A 329     9220   9424   8485   -636    -30   -744       N  
ATOM   2505  CA  PHE A 329      12.308  23.617  48.615  1.00 71.48           C  
ANISOU 2505  CA  PHE A 329     9249   9448   8463   -718     53   -725       C  
ATOM   2506  C   PHE A 329      13.682  24.273  48.643  1.00 69.16           C  
ANISOU 2506  C   PHE A 329     9079   9088   8112   -698     72   -695       C  
ATOM   2507  O   PHE A 329      13.916  25.223  49.382  1.00 68.75           O  
ANISOU 2507  O   PHE A 329     9055   9044   8023   -695    139   -717       O  
ATOM   2508  CB  PHE A 329      12.410  22.147  49.046  1.00 75.18           C  
ANISOU 2508  CB  PHE A 329     9698   9930   8936   -840     54   -681       C  
ATOM   2509  CG  PHE A 329      13.085  21.922  50.386  1.00 76.78           C  
ANISOU 2509  CG  PHE A 329     9921  10159   9094   -928    127   -636       C  
ATOM   2510  CD1 PHE A 329      12.330  21.775  51.535  1.00 79.03           C  
ANISOU 2510  CD1 PHE A 329    10123  10524   9379   -998    191   -654       C  
ATOM   2511  CD2 PHE A 329      14.472  21.811  50.486  1.00 75.68           C  
ANISOU 2511  CD2 PHE A 329     9873   9976   8906   -945    131   -564       C  
ATOM   2512  CE1 PHE A 329      12.938  21.551  52.760  1.00 80.23           C  
ANISOU 2512  CE1 PHE A 329    10294  10714   9475  -1089    252   -606       C  
ATOM   2513  CE2 PHE A 329      15.087  21.588  51.708  1.00 77.12           C  
ANISOU 2513  CE2 PHE A 329    10059  10209   9035  -1033    187   -506       C  
ATOM   2514  CZ  PHE A 329      14.319  21.465  52.852  1.00 78.08           C  
ANISOU 2514  CZ  PHE A 329    10108  10412   9148  -1108    245   -528       C  
ATOM   2515  N   LEU A 330      14.581  23.746  47.826  1.00 66.63           N  
ANISOU 2515  N   LEU A 330     8833   8701   7782   -692     20   -648       N  
ATOM   2516  CA  LEU A 330      15.964  24.184  47.811  1.00 65.96           C  
ANISOU 2516  CA  LEU A 330     8852   8566   7646   -686     32   -603       C  
ATOM   2517  C   LEU A 330      16.015  25.680  47.621  1.00 67.47           C  
ANISOU 2517  C   LEU A 330     9090   8731   7814   -605     55   -653       C  
ATOM   2518  O   LEU A 330      16.719  26.387  48.352  1.00 64.22           O  
ANISOU 2518  O   LEU A 330     8730   8325   7346   -643    112   -651       O  
ATOM   2519  CB  LEU A 330      16.738  23.458  46.708  1.00 64.15           C  
ANISOU 2519  CB  LEU A 330     8690   8259   7424   -663    -23   -551       C  
ATOM   2520  CG  LEU A 330      18.247  23.638  46.595  1.00 63.26           C  
ANISOU 2520  CG  LEU A 330     8668   8101   7266   -660    -13   -482       C  
ATOM   2521  CD1 LEU A 330      18.954  23.594  47.933  1.00 62.66           C  
ANISOU 2521  CD1 LEU A 330     8576   8094   7139   -752     43   -424       C  
ATOM   2522  CD2 LEU A 330      18.781  22.554  45.673  1.00 62.85           C  
ANISOU 2522  CD2 LEU A 330     8665   7977   7238   -649    -43   -426       C  
ATOM   2523  N   TYR A 331      15.237  26.154  46.652  1.00 69.29           N  
ANISOU 2523  N   TYR A 331     9305   8938   8085   -500     15   -694       N  
ATOM   2524  CA  TYR A 331      15.124  27.583  46.373  1.00 70.83           C  
ANISOU 2524  CA  TYR A 331     9546   9094   8271   -399     48   -735       C  
ATOM   2525  C   TYR A 331      14.720  28.380  47.607  1.00 70.87           C  
ANISOU 2525  C   TYR A 331     9533   9133   8260   -424    156   -780       C  
ATOM   2526  O   TYR A 331      15.402  29.327  47.987  1.00 68.44           O  
ANISOU 2526  O   TYR A 331     9319   8784   7902   -433    223   -797       O  
ATOM   2527  CB  TYR A 331      14.126  27.808  45.244  1.00 71.64           C  
ANISOU 2527  CB  TYR A 331     9599   9198   8424   -281    -13   -752       C  
ATOM   2528  CG  TYR A 331      13.535  29.191  45.190  1.00 72.60           C  
ANISOU 2528  CG  TYR A 331     9723   9301   8560   -160     45   -786       C  
ATOM   2529  CD1 TYR A 331      14.253  30.259  44.679  1.00 71.54           C  
ANISOU 2529  CD1 TYR A 331     9711   9075   8398    -83     71   -786       C  
ATOM   2530  CD2 TYR A 331      12.242  29.423  45.622  1.00 74.64           C  
ANISOU 2530  CD2 TYR A 331     9864   9630   8867   -116     85   -810       C  
ATOM   2531  CE1 TYR A 331      13.696  31.524  44.603  1.00 76.01           C  
ANISOU 2531  CE1 TYR A 331    10292   9605   8982     39    143   -809       C  
ATOM   2532  CE2 TYR A 331      11.676  30.685  45.553  1.00 78.19           C  
ANISOU 2532  CE2 TYR A 331    10316  10052   9339     16    157   -827       C  
ATOM   2533  CZ  TYR A 331      12.402  31.732  45.041  1.00 77.12           C  
ANISOU 2533  CZ  TYR A 331    10315   9811   9177     96    190   -825       C  
ATOM   2534  OH  TYR A 331      11.830  32.982  44.992  1.00 80.44           O  
ANISOU 2534  OH  TYR A 331    10752  10188   9626    236    282   -835       O  
ATOM   2535  N   GLU A 332      13.619  27.972  48.228  1.00 71.81           N  
ANISOU 2535  N   GLU A 332     9538   9328   8417   -449    180   -801       N  
ATOM   2536  CA  GLU A 332      13.070  28.676  49.390  1.00 74.63           C  
ANISOU 2536  CA  GLU A 332     9873   9719   8765   -468    296   -850       C  
ATOM   2537  C   GLU A 332      13.974  28.623  50.617  1.00 75.42           C  
ANISOU 2537  C   GLU A 332    10035   9839   8782   -611    361   -846       C  
ATOM   2538  O   GLU A 332      14.172  29.631  51.306  1.00 79.95           O  
ANISOU 2538  O   GLU A 332    10680  10391   9306   -631    461   -891       O  
ATOM   2539  CB  GLU A 332      11.705  28.101  49.754  1.00 74.96           C  
ANISOU 2539  CB  GLU A 332     9765   9849   8868   -471    303   -864       C  
ATOM   2540  CG  GLU A 332      10.607  28.396  48.745  1.00 74.73           C  
ANISOU 2540  CG  GLU A 332     9646   9837   8911   -332    257   -868       C  
ATOM   2541  CD  GLU A 332      10.150  29.838  48.778  1.00 75.25           C  
ANISOU 2541  CD  GLU A 332     9735   9861   8995   -198    356   -899       C  
ATOM   2542  OE1 GLU A 332      10.721  30.646  49.542  1.00 75.86           O  
ANISOU 2542  OE1 GLU A 332     9920   9880   9024   -224    466   -934       O  
ATOM   2543  OE2 GLU A 332       9.199  30.159  48.040  1.00 80.32           O  
ANISOU 2543  OE2 GLU A 332    10287  10534   9697    -69    329   -884       O  
ATOM   2544  N   TYR A 333      14.521  27.447  50.885  1.00 76.78           N  
ANISOU 2544  N   TYR A 333    10183  10054   8935   -713    309   -786       N  
ATOM   2545  CA  TYR A 333      15.461  27.280  51.982  1.00 78.12           C  
ANISOU 2545  CA  TYR A 333    10396  10268   9018   -850    350   -754       C  
ATOM   2546  C   TYR A 333      16.726  28.076  51.707  1.00 75.82           C  
ANISOU 2546  C   TYR A 333    10224   9927   8659   -856    351   -741       C  
ATOM   2547  O   TYR A 333      17.285  28.684  52.611  1.00 76.86           O  
ANISOU 2547  O   TYR A 333    10412  10088   8702   -953    418   -757       O  
ATOM   2548  CB  TYR A 333      15.816  25.800  52.171  1.00 79.19           C  
ANISOU 2548  CB  TYR A 333    10479  10451   9158   -929    294   -667       C  
ATOM   2549  CG  TYR A 333      16.152  25.446  53.600  1.00 84.34           C  
ANISOU 2549  CG  TYR A 333    11113  11195   9736  -1071    349   -631       C  
ATOM   2550  CD1 TYR A 333      15.347  24.578  54.332  1.00 86.96           C  
ANISOU 2550  CD1 TYR A 333    11357  11592  10092  -1131    372   -622       C  
ATOM   2551  CD2 TYR A 333      17.258  25.999  54.232  1.00 86.15           C  
ANISOU 2551  CD2 TYR A 333    11413  11457   9861  -1155    377   -605       C  
ATOM   2552  CE1 TYR A 333      15.651  24.259  55.641  1.00 89.63           C  
ANISOU 2552  CE1 TYR A 333    11681  12020  10353  -1261    421   -582       C  
ATOM   2553  CE2 TYR A 333      17.561  25.693  55.541  1.00 86.26           C  
ANISOU 2553  CE2 TYR A 333    11408  11577   9791  -1295    420   -565       C  
ATOM   2554  CZ  TYR A 333      16.762  24.822  56.243  1.00 90.05           C  
ANISOU 2554  CZ  TYR A 333    11803  12115  10296  -1342    442   -550       C  
ATOM   2555  OH  TYR A 333      17.068  24.518  57.554  1.00 97.04           O  
ANISOU 2555  OH  TYR A 333    12672  13112  11088  -1482    483   -502       O  
ATOM   2556  N   SER A 334      17.170  28.067  50.454  1.00 75.17           N  
ANISOU 2556  N   SER A 334    10182   9772   8609   -767    279   -713       N  
ATOM   2557  CA  SER A 334      18.447  28.673  50.105  1.00 74.86           C  
ANISOU 2557  CA  SER A 334    10247   9689   8509   -779    273   -688       C  
ATOM   2558  C   SER A 334      18.368  30.165  50.234  1.00 75.36           C  
ANISOU 2558  C   SER A 334    10399   9698   8537   -752    357   -769       C  
ATOM   2559  O   SER A 334      19.308  30.786  50.733  1.00 77.50           O  
ANISOU 2559  O   SER A 334    10751   9976   8718   -845    402   -772       O  
ATOM   2560  CB  SER A 334      18.895  28.307  48.687  1.00 72.51           C  
ANISOU 2560  CB  SER A 334     9977   9320   8255   -684    186   -643       C  
ATOM   2561  OG  SER A 334      19.301  26.955  48.634  1.00 71.28           O  
ANISOU 2561  OG  SER A 334     9773   9194   8114   -727    133   -558       O  
ATOM   2562  N   ARG A 335      17.262  30.761  49.800  1.00 75.72           N  
ANISOU 2562  N   ARG A 335    10431   9692   8647   -630    388   -830       N  
ATOM   2563  CA  ARG A 335      17.206  32.220  49.795  1.00 79.10           C  
ANISOU 2563  CA  ARG A 335    10963  10039   9052   -580    487   -899       C  
ATOM   2564  C   ARG A 335      17.069  32.815  51.185  1.00 78.44           C  
ANISOU 2564  C   ARG A 335    10917   9986   8900   -693    618   -962       C  
ATOM   2565  O   ARG A 335      17.315  33.997  51.379  1.00 82.13           O  
ANISOU 2565  O   ARG A 335    11506  10381   9320   -701    721  -1022       O  
ATOM   2566  CB  ARG A 335      16.120  32.743  48.873  1.00 81.77           C  
ANISOU 2566  CB  ARG A 335    11276  10313   9480   -395    490   -922       C  
ATOM   2567  CG  ARG A 335      14.688  32.407  49.231  1.00 84.94           C  
ANISOU 2567  CG  ARG A 335    11545  10776   9953   -343    512   -942       C  
ATOM   2568  CD  ARG A 335      13.823  33.425  48.509  1.00 86.15           C  
ANISOU 2568  CD  ARG A 335    11703  10859  10169   -160    561   -962       C  
ATOM   2569  NE  ARG A 335      12.410  33.106  48.478  1.00 85.28           N  
ANISOU 2569  NE  ARG A 335    11440  10819  10143    -73    555   -956       N  
ATOM   2570  CZ  ARG A 335      11.487  33.920  47.989  1.00 88.29           C  
ANISOU 2570  CZ  ARG A 335    11787  11171  10587     96    605   -954       C  
ATOM   2571  NH1 ARG A 335      11.832  35.108  47.503  1.00 88.75           N  
ANISOU 2571  NH1 ARG A 335    11973  11112  10636    200    673   -961       N  
ATOM   2572  NH2 ARG A 335      10.215  33.547  47.989  1.00 93.18           N  
ANISOU 2572  NH2 ARG A 335    12241  11882  11279    163    591   -936       N  
ATOM   2573  N   ARG A 336      16.688  31.989  52.146  1.00 77.82           N  
ANISOU 2573  N   ARG A 336    10747  10010   8811   -788    621   -952       N  
ATOM   2574  CA  ARG A 336      16.556  32.426  53.529  1.00 80.25           C  
ANISOU 2574  CA  ARG A 336    11089  10363   9041   -915    743  -1011       C  
ATOM   2575  C   ARG A 336      17.868  32.335  54.297  1.00 82.73           C  
ANISOU 2575  C   ARG A 336    11464  10748   9221  -1107    736   -980       C  
ATOM   2576  O   ARG A 336      18.032  32.981  55.339  1.00 85.13           O  
ANISOU 2576  O   ARG A 336    11842  11078   9425  -1238    843  -1040       O  
ATOM   2577  CB  ARG A 336      15.471  31.606  54.228  1.00 78.91           C  
ANISOU 2577  CB  ARG A 336    10788  10277   8917   -929    755  -1011       C  
ATOM   2578  CG  ARG A 336      14.100  32.197  53.999  1.00 80.15           C  
ANISOU 2578  CG  ARG A 336    10904  10383   9168   -781    834  -1070       C  
ATOM   2579  CD  ARG A 336      12.967  31.198  54.043  1.00 81.82           C  
ANISOU 2579  CD  ARG A 336    10948  10672   9465   -742    790  -1045       C  
ATOM   2580  NE  ARG A 336      11.819  31.787  53.356  1.00 86.61           N  
ANISOU 2580  NE  ARG A 336    11500  11234  10174   -561    825  -1069       N  
ATOM   2581  CZ  ARG A 336      10.835  31.108  52.783  1.00 91.38           C  
ANISOU 2581  CZ  ARG A 336    11956  11892  10872   -476    752  -1037       C  
ATOM   2582  NH1 ARG A 336      10.824  29.778  52.811  1.00100.92           N  
ANISOU 2582  NH1 ARG A 336    13072  13181  12090   -561    649   -991       N  
ATOM   2583  NH2 ARG A 336       9.853  31.763  52.170  1.00 92.46           N  
ANISOU 2583  NH2 ARG A 336    12036  12004  11090   -308    785  -1044       N  
ATOM   2584  N   HIS A 337      18.810  31.557  53.781  1.00 81.37           N  
ANISOU 2584  N   HIS A 337    11263  10613   9042  -1128    618   -884       N  
ATOM   2585  CA  HIS A 337      20.034  31.293  54.513  1.00 81.73           C  
ANISOU 2585  CA  HIS A 337    11325  10761   8967  -1303    596   -821       C  
ATOM   2586  C   HIS A 337      21.260  31.476  53.640  1.00 80.17           C  
ANISOU 2586  C   HIS A 337    11183  10532   8748  -1291    530   -763       C  
ATOM   2587  O   HIS A 337      21.793  30.513  53.095  1.00 84.60           O  
ANISOU 2587  O   HIS A 337    11678  11120   9345  -1257    432   -658       O  
ATOM   2588  CB  HIS A 337      19.956  29.895  55.132  1.00 85.01           C  
ANISOU 2588  CB  HIS A 337    11616  11297   9389  -1364    537   -729       C  
ATOM   2589  CG  HIS A 337      18.884  29.773  56.179  1.00 88.16           C  
ANISOU 2589  CG  HIS A 337    11968  11745   9783  -1414    615   -785       C  
ATOM   2590  ND1 HIS A 337      19.095  30.104  57.502  1.00 87.93           N  
ANISOU 2590  ND1 HIS A 337    11973  11810   9627  -1586    693   -813       N  
ATOM   2591  CD2 HIS A 337      17.580  29.414  56.087  1.00 86.96           C  
ANISOU 2591  CD2 HIS A 337    11741  11568   9733  -1319    634   -823       C  
ATOM   2592  CE1 HIS A 337      17.977  29.931  58.184  1.00 88.24           C  
ANISOU 2592  CE1 HIS A 337    11964  11868   9693  -1588    762   -866       C  
ATOM   2593  NE2 HIS A 337      17.041  29.513  57.350  1.00 88.73           N  
ANISOU 2593  NE2 HIS A 337    11953  11862   9898  -1425    727   -870       N  
ATOM   2594  N   PRO A 338      21.694  32.732  53.472  1.00 80.43           N  
ANISOU 2594  N   PRO A 338    11342  10493   8723  -1314    596   -832       N  
ATOM   2595  CA  PRO A 338      22.972  33.002  52.808  1.00 82.02           C  
ANISOU 2595  CA  PRO A 338    11601  10681   8880  -1339    547   -779       C  
ATOM   2596  C   PRO A 338      24.137  32.577  53.676  1.00 84.31           C  
ANISOU 2596  C   PRO A 338    11853  11134   9046  -1532    513   -691       C  
ATOM   2597  O   PRO A 338      25.233  32.350  53.180  1.00 87.18           O  
ANISOU 2597  O   PRO A 338    12205  11531   9388  -1549    447   -600       O  
ATOM   2598  CB  PRO A 338      22.994  34.528  52.646  1.00 81.29           C  
ANISOU 2598  CB  PRO A 338    11668  10474   8747  -1344    657   -892       C  
ATOM   2599  CG  PRO A 338      21.630  35.006  53.001  1.00 82.05           C  
ANISOU 2599  CG  PRO A 338    11783  10498   8894  -1269    761   -993       C  
ATOM   2600  CD  PRO A 338      21.005  33.969  53.871  1.00 80.70           C  
ANISOU 2600  CD  PRO A 338    11483  10445   8736  -1315    736   -963       C  
ATOM   2601  N   GLU A 339      23.900  32.498  54.976  1.00 86.22           N  
ANISOU 2601  N   GLU A 339    12072  11484   9202  -1679    563   -713       N  
ATOM   2602  CA  GLU A 339      24.952  32.124  55.894  1.00 90.89           C  
ANISOU 2602  CA  GLU A 339    12618  12259   9659  -1874    528   -620       C  
ATOM   2603  C   GLU A 339      25.354  30.660  55.703  1.00 86.20           C  
ANISOU 2603  C   GLU A 339    11878  11753   9120  -1821    417   -451       C  
ATOM   2604  O   GLU A 339      26.443  30.279  56.087  1.00 94.14           O  
ANISOU 2604  O   GLU A 339    12828  12902  10040  -1931    367   -329       O  
ATOM   2605  CB  GLU A 339      24.552  32.424  57.364  1.00 91.55           C  
ANISOU 2605  CB  GLU A 339    12723  12441   9621  -2054    614   -688       C  
ATOM   2606  CG  GLU A 339      23.527  31.479  58.010  1.00 89.29           C  
ANISOU 2606  CG  GLU A 339    12336  12201   9388  -2021    616   -671       C  
ATOM   2607  CD  GLU A 339      22.064  31.790  57.691  1.00 90.82           C  
ANISOU 2607  CD  GLU A 339    12557  12247   9705  -1867    692   -791       C  
ATOM   2608  OE1 GLU A 339      21.789  32.714  56.901  1.00 95.07           O  
ANISOU 2608  OE1 GLU A 339    13188  12637  10298  -1760    742   -879       O  
ATOM   2609  OE2 GLU A 339      21.169  31.108  58.242  1.00 85.39           O  
ANISOU 2609  OE2 GLU A 339    11789  11597   9059  -1851    707   -789       O  
ATOM   2610  N   TYR A 340      24.479  29.840  55.140  1.00 81.76           N  
ANISOU 2610  N   TYR A 340    11256  11112   8698  -1660    387   -438       N  
ATOM   2611  CA  TYR A 340      24.752  28.402  55.020  1.00 82.23           C  
ANISOU 2611  CA  TYR A 340    11198  11232   8813  -1613    310   -288       C  
ATOM   2612  C   TYR A 340      25.658  28.106  53.841  1.00 79.39           C  
ANISOU 2612  C   TYR A 340    10838  10819   8509  -1513    246   -197       C  
ATOM   2613  O   TYR A 340      25.720  28.874  52.881  1.00 79.43           O  
ANISOU 2613  O   TYR A 340    10926  10706   8547  -1433    250   -267       O  
ATOM   2614  CB  TYR A 340      23.456  27.617  54.834  1.00 81.15           C  
ANISOU 2614  CB  TYR A 340    11009  11026   8799  -1499    311   -319       C  
ATOM   2615  CG  TYR A 340      22.601  27.410  56.067  1.00 82.92           C  
ANISOU 2615  CG  TYR A 340    11191  11329   8985  -1591    365   -358       C  
ATOM   2616  CD1 TYR A 340      21.491  26.591  56.000  1.00 86.34           C  
ANISOU 2616  CD1 TYR A 340    11560  11724   9520  -1513    364   -371       C  
ATOM   2617  CD2 TYR A 340      22.896  27.997  57.287  1.00 86.68           C  
ANISOU 2617  CD2 TYR A 340    11694  11922   9318  -1767    419   -383       C  
ATOM   2618  CE1 TYR A 340      20.687  26.373  57.098  1.00 88.07           C  
ANISOU 2618  CE1 TYR A 340    11738  12014   9711  -1592    419   -404       C  
ATOM   2619  CE2 TYR A 340      22.093  27.780  58.398  1.00 91.00           C  
ANISOU 2619  CE2 TYR A 340    12208  12538   9828  -1849    475   -420       C  
ATOM   2620  CZ  TYR A 340      20.983  26.956  58.292  1.00 91.86           C  
ANISOU 2620  CZ  TYR A 340    12247  12602  10052  -1754    476   -427       C  
ATOM   2621  OH  TYR A 340      20.151  26.704  59.369  1.00 90.40           O  
ANISOU 2621  OH  TYR A 340    12026  12484   9838  -1832    538   -461       O  
ATOM   2622  N   ALA A 341      26.342  26.969  53.916  1.00 80.09           N  
ANISOU 2622  N   ALA A 341    10836  10988   8608  -1510    197    -35       N  
ATOM   2623  CA  ALA A 341      27.203  26.518  52.828  1.00 79.62           C  
ANISOU 2623  CA  ALA A 341    10770  10875   8609  -1406    152     66       C  
ATOM   2624  C   ALA A 341      26.339  25.821  51.795  1.00 76.70           C  
ANISOU 2624  C   ALA A 341    10410  10350   8382  -1240    138     33       C  
ATOM   2625  O   ALA A 341      25.322  25.196  52.133  1.00 75.05           O  
ANISOU 2625  O   ALA A 341    10164  10127   8224  -1223    149      2       O  
ATOM   2626  CB  ALA A 341      28.290  25.578  53.333  1.00 79.73           C  
ANISOU 2626  CB  ALA A 341    10680  11033   8580  -1457    125    268       C  
ATOM   2627  N   VAL A 342      26.739  25.924  50.536  1.00 71.64           N  
ANISOU 2627  N   VAL A 342     9822   9601   7799  -1130    116     36       N  
ATOM   2628  CA  VAL A 342      25.946  25.341  49.454  1.00 73.95           C  
ANISOU 2628  CA  VAL A 342    10138   9750   8208   -989     98     -6       C  
ATOM   2629  C   VAL A 342      25.830  23.814  49.602  1.00 77.34           C  
ANISOU 2629  C   VAL A 342    10499  10188   8697   -965     97    101       C  
ATOM   2630  O   VAL A 342      24.777  23.243  49.318  1.00 78.54           O  
ANISOU 2630  O   VAL A 342    10648  10271   8923   -917     96     43       O  
ATOM   2631  CB  VAL A 342      26.489  25.779  48.077  1.00 72.16           C  
ANISOU 2631  CB  VAL A 342     9993   9413   8013   -889     78    -18       C  
ATOM   2632  CG1 VAL A 342      26.016  24.861  46.971  1.00 69.40           C  
ANISOU 2632  CG1 VAL A 342     9660   8944   7763   -768     56    -16       C  
ATOM   2633  CG2 VAL A 342      26.089  27.228  47.802  1.00 67.61           C  
ANISOU 2633  CG2 VAL A 342     9500   8782   7407   -881     90   -156       C  
ATOM   2634  N   SER A 343      26.877  23.169  50.116  1.00 83.30           N  
ANISOU 2634  N   SER A 343    11195  11036   9418  -1006    105    262       N  
ATOM   2635  CA  SER A 343      26.854  21.719  50.357  1.00 88.33           C  
ANISOU 2635  CA  SER A 343    11775  11675  10110   -981    127    384       C  
ATOM   2636  C   SER A 343      25.852  21.329  51.435  1.00 89.96           C  
ANISOU 2636  C   SER A 343    11930  11943  10308  -1056    144    350       C  
ATOM   2637  O   SER A 343      25.113  20.346  51.274  1.00 99.07           O  
ANISOU 2637  O   SER A 343    13078  13026  11539  -1017    162    349       O  
ATOM   2638  CB  SER A 343      28.244  21.209  50.752  1.00 92.58           C  
ANISOU 2638  CB  SER A 343    12248  12320  10609   -998    139    587       C  
ATOM   2639  OG  SER A 343      29.164  21.459  49.698  1.00101.66           O  
ANISOU 2639  OG  SER A 343    13440  13406  11778   -919    134    627       O  
ATOM   2640  N   VAL A 344      25.852  22.067  52.546  1.00 86.31           N  
ANISOU 2640  N   VAL A 344    11435  11613   9745  -1176    146    324       N  
ATOM   2641  CA  VAL A 344      24.873  21.835  53.610  1.00 83.72           C  
ANISOU 2641  CA  VAL A 344    11064  11347   9398  -1256    171    279       C  
ATOM   2642  C   VAL A 344      23.473  21.942  53.012  1.00 82.33           C  
ANISOU 2642  C   VAL A 344    10924  11048   9308  -1191    174    120       C  
ATOM   2643  O   VAL A 344      22.667  21.017  53.137  1.00 89.36           O  
ANISOU 2643  O   VAL A 344    11782  11909  10261  -1180    190    121       O  
ATOM   2644  CB  VAL A 344      25.024  22.845  54.773  1.00 84.99           C  
ANISOU 2644  CB  VAL A 344    11216  11652   9425  -1402    183    237       C  
ATOM   2645  CG1 VAL A 344      23.776  22.890  55.650  1.00 87.47           C  
ANISOU 2645  CG1 VAL A 344    11514  11992   9731  -1466    222    135       C  
ATOM   2646  CG2 VAL A 344      26.240  22.512  55.621  1.00 82.82           C  
ANISOU 2646  CG2 VAL A 344    10870  11548   9049  -1498    172    416       C  
ATOM   2647  N   LEU A 345      23.207  23.050  52.322  1.00 79.64           N  
ANISOU 2647  N   LEU A 345    10647  10640   8972  -1146    161     -7       N  
ATOM   2648  CA  LEU A 345      21.900  23.282  51.699  1.00 78.01           C  
ANISOU 2648  CA  LEU A 345    10459  10339   8841  -1075    158   -144       C  
ATOM   2649  C   LEU A 345      21.490  22.083  50.838  1.00 75.37           C  
ANISOU 2649  C   LEU A 345    10116   9914   8606   -999    136   -114       C  
ATOM   2650  O   LEU A 345      20.357  21.601  50.934  1.00 77.71           O  
ANISOU 2650  O   LEU A 345    10374  10198   8953  -1003    142   -170       O  
ATOM   2651  CB  LEU A 345      21.903  24.593  50.880  1.00 77.51           C  
ANISOU 2651  CB  LEU A 345    10474  10204   8772  -1010    147   -246       C  
ATOM   2652  CG  LEU A 345      21.926  25.933  51.647  1.00 77.44           C  
ANISOU 2652  CG  LEU A 345    10501  10246   8677  -1083    194   -325       C  
ATOM   2653  CD1 LEU A 345      22.159  27.122  50.723  1.00 77.46           C  
ANISOU 2653  CD1 LEU A 345    10598  10157   8677  -1010    192   -397       C  
ATOM   2654  CD2 LEU A 345      20.626  26.139  52.408  1.00 76.31           C  
ANISOU 2654  CD2 LEU A 345    10321  10128   8544  -1110    243   -420       C  
ATOM   2655  N   LEU A 346      22.422  21.577  50.034  1.00 72.40           N  
ANISOU 2655  N   LEU A 346     9778   9478   8252   -943    120    -26       N  
ATOM   2656  CA  LEU A 346      22.162  20.377  49.221  1.00 74.96           C  
ANISOU 2656  CA  LEU A 346    10120   9704   8659   -887    119      5       C  
ATOM   2657  C   LEU A 346      21.885  19.109  50.039  1.00 75.49           C  
ANISOU 2657  C   LEU A 346    10133   9802   8749   -945    163     85       C  
ATOM   2658  O   LEU A 346      21.009  18.350  49.659  1.00 76.96           O  
ANISOU 2658  O   LEU A 346    10324   9922   8996   -940    169     40       O  
ATOM   2659  CB  LEU A 346      23.298  20.131  48.225  1.00 74.21           C  
ANISOU 2659  CB  LEU A 346    10089   9529   8579   -812    116     87       C  
ATOM   2660  CG  LEU A 346      23.415  21.193  47.121  1.00 75.47           C  
ANISOU 2660  CG  LEU A 346    10319   9623   8732   -741     74     -1       C  
ATOM   2661  CD1 LEU A 346      24.657  20.979  46.264  1.00 73.76           C  
ANISOU 2661  CD1 LEU A 346    10161   9342   8522   -676     83     91       C  
ATOM   2662  CD2 LEU A 346      22.161  21.217  46.258  1.00 77.54           C  
ANISOU 2662  CD2 LEU A 346    10606   9810   9045   -698     39   -128       C  
ATOM   2663  N   ARG A 347      22.596  18.881  51.150  1.00 77.67           N  
ANISOU 2663  N   ARG A 347    10359  10184   8970  -1007    193    206       N  
ATOM   2664  CA  ARG A 347      22.290  17.727  52.037  1.00 84.80           C  
ANISOU 2664  CA  ARG A 347    11210  11122   9887  -1063    241    291       C  
ATOM   2665  C   ARG A 347      20.909  17.848  52.656  1.00 86.93           C  
ANISOU 2665  C   ARG A 347    11438  11429  10162  -1130    246    173       C  
ATOM   2666  O   ARG A 347      20.185  16.869  52.760  1.00 86.74           O  
ANISOU 2666  O   ARG A 347    11400  11367  10191  -1151    278    175       O  
ATOM   2667  CB  ARG A 347      23.293  17.576  53.186  1.00 85.68           C  
ANISOU 2667  CB  ARG A 347    11263  11372   9921  -1122    263    454       C  
ATOM   2668  CG  ARG A 347      24.659  17.064  52.762  1.00 87.64           C  
ANISOU 2668  CG  ARG A 347    11520  11602  10178  -1053    278    625       C  
ATOM   2669  CD  ARG A 347      25.618  16.956  53.938  1.00 85.89           C  
ANISOU 2669  CD  ARG A 347    11214  11552   9867  -1117    288    802       C  
ATOM   2670  NE  ARG A 347      26.969  17.352  53.547  1.00 87.31           N  
ANISOU 2670  NE  ARG A 347    11384  11777  10012  -1076    269    910       N  
ATOM   2671  CZ  ARG A 347      27.742  18.214  54.206  1.00 87.02           C  
ANISOU 2671  CZ  ARG A 347    11295  11907   9861  -1160    231    955       C  
ATOM   2672  NH1 ARG A 347      27.345  18.768  55.347  1.00 88.15           N  
ANISOU 2672  NH1 ARG A 347    11399  12188   9904  -1294    215    904       N  
ATOM   2673  NH2 ARG A 347      28.946  18.504  53.727  1.00 86.16           N  
ANISOU 2673  NH2 ARG A 347    11173  11832   9731  -1120    215   1054       N  
ATOM   2674  N   LEU A 348      20.551  19.057  53.075  1.00 89.31           N  
ANISOU 2674  N   LEU A 348    11724  11802  10409  -1165    228     71       N  
ATOM   2675  CA  LEU A 348      19.222  19.294  53.625  1.00 88.35           C  
ANISOU 2675  CA  LEU A 348    11557  11715  10296  -1213    245    -44       C  
ATOM   2676  C   LEU A 348      18.177  18.894  52.601  1.00 87.55           C  
ANISOU 2676  C   LEU A 348    11462  11515  10289  -1156    224   -135       C  
ATOM   2677  O   LEU A 348      17.198  18.236  52.934  1.00 88.71           O  
ANISOU 2677  O   LEU A 348    11560  11672  10473  -1201    247   -164       O  
ATOM   2678  CB  LEU A 348      19.044  20.761  54.033  1.00 87.52           C  
ANISOU 2678  CB  LEU A 348    11459  11670  10127  -1235    248   -147       C  
ATOM   2679  CG  LEU A 348      20.022  21.247  55.105  1.00 85.14           C  
ANISOU 2679  CG  LEU A 348    11157  11486   9708  -1328    268    -76       C  
ATOM   2680  CD1 LEU A 348      19.574  22.595  55.650  1.00 84.11           C  
ANISOU 2680  CD1 LEU A 348    11048  11397   9513  -1375    302   -203       C  
ATOM   2681  CD2 LEU A 348      20.122  20.224  56.229  1.00 86.62           C  
ANISOU 2681  CD2 LEU A 348    11283  11767   9861  -1418    300     40       C  
ATOM   2682  N   ALA A 349      18.401  19.286  51.350  1.00 85.80           N  
ANISOU 2682  N   ALA A 349    11297  11206  10095  -1068    178   -175       N  
ATOM   2683  CA  ALA A 349      17.534  18.875  50.257  1.00 85.02           C  
ANISOU 2683  CA  ALA A 349    11210  11026  10069  -1026    146   -249       C  
ATOM   2684  C   ALA A 349      17.512  17.352  50.120  1.00 82.39           C  
ANISOU 2684  C   ALA A 349    10892  10632   9781  -1063    177   -181       C  
ATOM   2685  O   ALA A 349      16.443  16.751  49.985  1.00 80.81           O  
ANISOU 2685  O   ALA A 349    10660  10421   9622  -1105    180   -240       O  
ATOM   2686  CB  ALA A 349      18.003  19.514  48.956  1.00 82.21           C  
ANISOU 2686  CB  ALA A 349    10927  10591   9718   -930     94   -281       C  
ATOM   2687  N   LYS A 350      18.694  16.736  50.152  1.00 80.97           N  
ANISOU 2687  N   LYS A 350    10761  10411   9592  -1047    211    -53       N  
ATOM   2688  CA  LYS A 350      18.811  15.282  50.017  1.00 84.48           C  
ANISOU 2688  CA  LYS A 350    11243  10772  10084  -1067    268     28       C  
ATOM   2689  C   LYS A 350      18.107  14.562  51.162  1.00 86.82           C  
ANISOU 2689  C   LYS A 350    11475  11128  10384  -1161    320     52       C  
ATOM   2690  O   LYS A 350      17.424  13.562  50.940  1.00 89.07           O  
ANISOU 2690  O   LYS A 350    11779  11346  10719  -1207    356     32       O  
ATOM   2691  CB  LYS A 350      20.278  14.841  49.938  1.00 85.09           C  
ANISOU 2691  CB  LYS A 350    11371  10806  10154  -1012    310    186       C  
ATOM   2692  CG  LYS A 350      20.485  13.349  49.700  1.00 82.65           C  
ANISOU 2692  CG  LYS A 350    11124  10377   9901  -1009    396    280       C  
ATOM   2693  N   GLU A 351      18.268  15.080  52.379  1.00 91.75           N  
ANISOU 2693  N   GLU A 351    12031  11878  10950  -1203    328     91       N  
ATOM   2694  CA  GLU A 351      17.584  14.527  53.550  1.00 95.07           C  
ANISOU 2694  CA  GLU A 351    12388  12371  11363  -1297    378    111       C  
ATOM   2695  C   GLU A 351      16.082  14.736  53.415  1.00 94.36           C  
ANISOU 2695  C   GLU A 351    12250  12296  11308  -1340    359    -42       C  
ATOM   2696  O   GLU A 351      15.315  13.780  53.466  1.00 98.51           O  
ANISOU 2696  O   GLU A 351    12764  12787  11877  -1400    396    -55       O  
ATOM   2697  CB  GLU A 351      18.084  15.155  54.856  1.00 98.31           C  
ANISOU 2697  CB  GLU A 351    12743  12926  11683  -1344    387    175       C  
ATOM   2698  CG  GLU A 351      17.612  14.438  56.133  1.00104.44           C  
ANISOU 2698  CG  GLU A 351    13465  13780  12439  -1441    448    234       C  
ATOM   2699  CD  GLU A 351      18.352  13.128  56.434  1.00107.67           C  
ANISOU 2699  CD  GLU A 351    13896  14151  12862  -1438    510    419       C  
ATOM   2700  OE1 GLU A 351      19.597  13.155  56.583  1.00110.57           O  
ANISOU 2700  OE1 GLU A 351    14270  14554  13187  -1398    508    561       O  
ATOM   2701  OE2 GLU A 351      17.691  12.069  56.546  1.00100.65           O  
ANISOU 2701  OE2 GLU A 351    13015  13199  12027  -1477    568    431       O  
ATOM   2702  N   TYR A 352      15.669  15.982  53.221  1.00 92.28           N  
ANISOU 2702  N   TYR A 352    11955  12082  11024  -1308    309   -152       N  
ATOM   2703  CA  TYR A 352      14.259  16.288  53.013  1.00 91.41           C  
ANISOU 2703  CA  TYR A 352    11780  12000  10951  -1325    290   -283       C  
ATOM   2704  C   TYR A 352      13.645  15.334  51.982  1.00 89.97           C  
ANISOU 2704  C   TYR A 352    11619  11733  10834  -1339    272   -319       C  
ATOM   2705  O   TYR A 352      12.557  14.792  52.207  1.00 90.99           O  
ANISOU 2705  O   TYR A 352    11686  11892  10995  -1415    290   -367       O  
ATOM   2706  CB  TYR A 352      14.074  17.743  52.567  1.00 87.88           C  
ANISOU 2706  CB  TYR A 352    11322  11580  10489  -1247    242   -377       C  
ATOM   2707  CG  TYR A 352      12.622  18.134  52.406  1.00 85.56           C  
ANISOU 2707  CG  TYR A 352    10940  11335  10235  -1244    228   -489       C  
ATOM   2708  CD1 TYR A 352      11.814  18.345  53.519  1.00 86.33           C  
ANISOU 2708  CD1 TYR A 352    10952  11526  10324  -1301    285   -521       C  
ATOM   2709  CD2 TYR A 352      12.055  18.276  51.149  1.00 83.91           C  
ANISOU 2709  CD2 TYR A 352    10724  11089  10069  -1186    162   -553       C  
ATOM   2710  CE1 TYR A 352      10.486  18.700  53.382  1.00 86.32           C  
ANISOU 2710  CE1 TYR A 352    10852  11580  10366  -1288    281   -609       C  
ATOM   2711  CE2 TYR A 352      10.721  18.620  51.000  1.00 83.70           C  
ANISOU 2711  CE2 TYR A 352    10592  11132  10078  -1180    146   -635       C  
ATOM   2712  CZ  TYR A 352       9.942  18.829  52.117  1.00 85.49           C  
ANISOU 2712  CZ  TYR A 352    10726  11450  10306  -1225    208   -659       C  
ATOM   2713  OH  TYR A 352       8.614  19.176  51.983  1.00 87.19           O  
ANISOU 2713  OH  TYR A 352    10819  11744  10563  -1207    201   -727       O  
ATOM   2714  N   GLU A 353      14.352  15.112  50.875  1.00 86.89           N  
ANISOU 2714  N   GLU A 353    11320  11239  10457  -1281    243   -297       N  
ATOM   2715  CA  GLU A 353      13.884  14.181  49.848  1.00 90.94           C  
ANISOU 2715  CA  GLU A 353    11880  11659  11013  -1312    234   -335       C  
ATOM   2716  C   GLU A 353      13.659  12.770  50.404  1.00 89.71           C  
ANISOU 2716  C   GLU A 353    11741  11462  10884  -1414    319   -279       C  
ATOM   2717  O   GLU A 353      12.592  12.184  50.207  1.00 92.85           O  
ANISOU 2717  O   GLU A 353    12108  11861  11308  -1503    322   -350       O  
ATOM   2718  CB  GLU A 353      14.856  14.106  48.673  1.00 92.25           C  
ANISOU 2718  CB  GLU A 353    12163  11708  11179  -1236    214   -306       C  
ATOM   2719  CG  GLU A 353      14.323  13.259  47.523  1.00 93.55           C  
ANISOU 2719  CG  GLU A 353    12394  11780  11371  -1284    205   -368       C  
ATOM   2720  CD  GLU A 353      15.294  13.133  46.366  1.00 94.58           C  
ANISOU 2720  CD  GLU A 353    12654  11785  11496  -1213    202   -342       C  
ATOM   2721  OE1 GLU A 353      16.503  13.384  46.555  1.00 88.93           O  
ANISOU 2721  OE1 GLU A 353    11981  11039  10770  -1132    230   -245       O  
ATOM   2722  OE2 GLU A 353      14.841  12.764  45.261  1.00 99.18           O  
ANISOU 2722  OE2 GLU A 353    13296  12307  12080  -1248    175   -417       O  
ATOM   2723  N   ALA A 354      14.662  12.231  51.091  1.00 86.59           N  
ANISOU 2723  N   ALA A 354    11391  11032  10478  -1403    389   -145       N  
ATOM   2724  CA  ALA A 354      14.561  10.909  51.720  1.00 84.05           C  
ANISOU 2724  CA  ALA A 354    11093  10660  10181  -1484    487    -66       C  
ATOM   2725  C   ALA A 354      13.380  10.805  52.706  1.00 85.27           C  
ANISOU 2725  C   ALA A 354    11143  10920  10335  -1590    506   -117       C  
ATOM   2726  O   ALA A 354      12.734   9.759  52.799  1.00 82.40           O  
ANISOU 2726  O   ALA A 354    10795  10508  10004  -1685    566   -125       O  
ATOM   2727  CB  ALA A 354      15.863  10.573  52.431  1.00 82.18           C  
ANISOU 2727  CB  ALA A 354    10891  10410   9924  -1433    551    111       C  
ATOM   2728  N   THR A 355      13.110  11.890  53.435  1.00 85.34           N  
ANISOU 2728  N   THR A 355    11055  11065  10306  -1577    468   -153       N  
ATOM   2729  CA  THR A 355      11.975  11.954  54.358  1.00 85.21           C  
ANISOU 2729  CA  THR A 355    10932  11156  10287  -1665    491   -210       C  
ATOM   2730  C   THR A 355      10.669  11.796  53.598  1.00 90.09           C  
ANISOU 2730  C   THR A 355    11500  11778  10951  -1719    455   -338       C  
ATOM   2731  O   THR A 355       9.827  10.987  53.975  1.00 97.69           O  
ANISOU 2731  O   THR A 355    12426  12754  11939  -1827    504   -356       O  
ATOM   2732  CB  THR A 355      11.924  13.288  55.132  1.00 83.04           C  
ANISOU 2732  CB  THR A 355    10580  11011   9960  -1631    467   -243       C  
ATOM   2733  OG1 THR A 355      13.188  13.546  55.758  1.00 77.70           O  
ANISOU 2733  OG1 THR A 355     9947  10353   9223  -1597    483   -130       O  
ATOM   2734  CG2 THR A 355      10.833  13.263  56.198  1.00 77.60           C  
ANISOU 2734  CG2 THR A 355     9791  10427   9268  -1721    516   -286       C  
ATOM   2735  N   LEU A 356      10.511  12.542  52.512  1.00 94.05           N  
ANISOU 2735  N   LEU A 356    11999  12276  11461  -1650    370   -419       N  
ATOM   2736  CA  LEU A 356       9.308  12.413  51.685  1.00100.21           C  
ANISOU 2736  CA  LEU A 356    12719  13084  12272  -1703    320   -528       C  
ATOM   2737  C   LEU A 356       9.127  11.001  51.093  1.00100.64           C  
ANISOU 2737  C   LEU A 356    12856  13032  12351  -1814    356   -529       C  
ATOM   2738  O   LEU A 356       8.042  10.409  51.185  1.00 93.95           O  
ANISOU 2738  O   LEU A 356    11944  12230  11523  -1936    372   -584       O  
ATOM   2739  CB  LEU A 356       9.316  13.453  50.564  1.00 98.84           C  
ANISOU 2739  CB  LEU A 356    12540  12923  12092  -1598    220   -591       C  
ATOM   2740  CG  LEU A 356       9.240  14.908  51.035  1.00 99.19           C  
ANISOU 2740  CG  LEU A 356    12505  13064  12119  -1497    196   -614       C  
ATOM   2741  CD1 LEU A 356       9.051  15.820  49.832  1.00 98.67           C  
ANISOU 2741  CD1 LEU A 356    12429  13007  12055  -1398    103   -674       C  
ATOM   2742  CD2 LEU A 356       8.130  15.120  52.060  1.00 98.58           C  
ANISOU 2742  CD2 LEU A 356    12289  13111  12055  -1550    239   -650       C  
ATOM   2743  N   GLU A 357      10.195  10.467  50.507  1.00101.79           N  
ANISOU 2743  N   GLU A 357    13147  13035  12494  -1776    382   -467       N  
ATOM   2744  CA  GLU A 357      10.144   9.151  49.871  1.00105.38           C  
ANISOU 2744  CA  GLU A 357    13717  13356  12968  -1875    440   -470       C  
ATOM   2745  C   GLU A 357       9.669   8.091  50.858  1.00105.57           C  
ANISOU 2745  C   GLU A 357    13731  13370  13013  -1999    546   -432       C  
ATOM   2746  O   GLU A 357       8.861   7.228  50.500  1.00110.57           O  
ANISOU 2746  O   GLU A 357    14384  13967  13659  -2138    576   -496       O  
ATOM   2747  CB  GLU A 357      11.512   8.763  49.292  1.00109.14           C  
ANISOU 2747  CB  GLU A 357    14355  13670  13443  -1790    486   -384       C  
ATOM   2748  CG  GLU A 357      11.460   7.634  48.260  1.00116.07           C  
ANISOU 2748  CG  GLU A 357    15378  14389  14333  -1876    539   -421       C  
ATOM   2749  CD  GLU A 357      10.723   8.006  46.974  1.00115.59           C  
ANISOU 2749  CD  GLU A 357    15309  14364  14247  -1921    433   -560       C  
ATOM   2750  OE1 GLU A 357      10.935   9.129  46.451  1.00105.69           O  
ANISOU 2750  OE1 GLU A 357    14011  13175  12970  -1812    329   -586       O  
ATOM   2751  OE2 GLU A 357       9.928   7.164  46.490  1.00113.87           O  
ANISOU 2751  OE2 GLU A 357    15130  14111  14023  -2075    455   -638       O  
ATOM   2752  N   GLU A 358      10.148   8.172  52.102  1.00115.10           N  
ANISOU 2752  N   GLU A 358    15045  14233  14455  -2888   1308   1313       N  
ATOM   2753  CA  GLU A 358       9.748   7.220  53.154  1.00112.93           C  
ANISOU 2753  CA  GLU A 358    14776  13679  14452  -2841   1379   1633       C  
ATOM   2754  C   GLU A 358       8.373   7.558  53.748  1.00110.55           C  
ANISOU 2754  C   GLU A 358    14503  13388  14112  -2892   1553   1905       C  
ATOM   2755  O   GLU A 358       7.504   6.700  53.783  1.00114.36           O  
ANISOU 2755  O   GLU A 358    14859  13646  14947  -2952   1604   2028       O  
ATOM   2756  CB  GLU A 358      10.805   7.119  54.261  1.00109.14           C  
ANISOU 2756  CB  GLU A 358    14439  13197  13832  -2716   1344   1849       C  
ATOM   2757  N   CYS A 359       8.158   8.803  54.177  1.00109.27           N  
ANISOU 2757  N   CYS A 359    14468  13474  13575  -2874   1638   1964       N  
ATOM   2758  CA  CYS A 359       6.899   9.172  54.857  1.00109.44           C  
ANISOU 2758  CA  CYS A 359    14487  13540  13556  -2911   1815   2174       C  
ATOM   2759  C   CYS A 359       5.646   9.050  53.978  1.00112.75           C  
ANISOU 2759  C   CYS A 359    14751  13855  14235  -3030   1849   2080       C  
ATOM   2760  O   CYS A 359       4.552   8.795  54.494  1.00110.41           O  
ANISOU 2760  O   CYS A 359    14396  13488  14065  -3076   1992   2273       O  
ATOM   2761  CB  CYS A 359       6.961  10.595  55.425  1.00106.16           C  
ANISOU 2761  CB  CYS A 359    14176  13397  12763  -2857   1876   2146       C  
ATOM   2762  SG  CYS A 359       8.072  10.841  56.831  1.00105.71           S  
ANISOU 2762  SG  CYS A 359    14274  13544  12346  -2722   1896   2290       S  
ATOM   2763  N   CYS A 360       5.804   9.224  52.664  1.00116.07           N  
ANISOU 2763  N   CYS A 360    15082  14309  14708  -3094   1719   1791       N  
ATOM   2764  CA  CYS A 360       4.660   9.211  51.743  1.00116.98           C  
ANISOU 2764  CA  CYS A 360    15033  14392  15021  -3216   1724   1684       C  
ATOM   2765  C   CYS A 360       4.100   7.815  51.450  1.00115.75           C  
ANISOU 2765  C   CYS A 360    14709  13965  15305  -3272   1732   1659       C  
ATOM   2766  O   CYS A 360       3.013   7.702  50.892  1.00116.82           O  
ANISOU 2766  O   CYS A 360    14703  14052  15633  -3368   1761   1604       O  
ATOM   2767  CB  CYS A 360       5.013   9.930  50.438  1.00118.43           C  
ANISOU 2767  CB  CYS A 360    15140  14805  15051  -3294   1568   1425       C  
ATOM   2768  SG  CYS A 360       5.205  11.715  50.642  1.00121.03           S  
ANISOU 2768  SG  CYS A 360    15576  15369  15042  -3271   1541   1505       S  
ATOM   2769  N   ALA A 361       4.834   6.768  51.832  1.00118.50           N  
ANISOU 2769  N   ALA A 361    15047  14115  15864  -3213   1688   1702       N  
ATOM   2770  CA  ALA A 361       4.343   5.379  51.744  1.00120.12           C  
ANISOU 2770  CA  ALA A 361    15056  13975  16610  -3254   1679   1723       C  
ATOM   2771  C   ALA A 361       3.620   4.906  53.011  1.00121.21           C  
ANISOU 2771  C   ALA A 361    15220  13929  16905  -3254   1829   2194       C  
ATOM   2772  O   ALA A 361       3.050   3.823  53.016  1.00123.29           O  
ANISOU 2772  O   ALA A 361    15301  13881  17663  -3307   1829   2292       O  
ATOM   2773  CB  ALA A 361       5.487   4.424  51.423  1.00119.26           C  
ANISOU 2773  CB  ALA A 361    14843  13690  16780  -3201   1517   1512       C  
ATOM   2774  N   LYS A 362       3.647   5.704  54.078  1.00125.66           N  
ANISOU 2774  N   LYS A 362    15970  14714  17061  -3206   1952   2474       N  
ATOM   2775  CA  LYS A 362       3.009   5.322  55.352  1.00131.45           C  
ANISOU 2775  CA  LYS A 362    16702  15414  17828  -3230   2110   2939       C  
ATOM   2776  C   LYS A 362       1.500   5.602  55.361  1.00133.22           C  
ANISOU 2776  C   LYS A 362    16835  15671  18111  -3328   2279   2998       C  
ATOM   2777  O   LYS A 362       0.964   6.237  54.450  1.00132.26           O  
ANISOU 2777  O   LYS A 362    16677  15606  17970  -3363   2266   2699       O  
ATOM   2778  CB  LYS A 362       3.683   6.032  56.534  1.00128.53           C  
ANISOU 2778  CB  LYS A 362    16521  15360  16956  -3147   2177   3155       C  
ATOM   2779  N   ASP A 363       0.826   5.113  56.397  1.00137.26           N  
ANISOU 2779  N   ASP A 363    17286  16171  18695  -3385   2429   3413       N  
ATOM   2780  CA  ASP A 363      -0.628   5.247  56.517  1.00142.73           C  
ANISOU 2780  CA  ASP A 363    17861  16890  19481  -3487   2607   3495       C  
ATOM   2781  C   ASP A 363      -1.056   6.701  56.744  1.00145.20           C  
ANISOU 2781  C   ASP A 363    18262  17563  19345  -3458   2736   3320       C  
ATOM   2782  O   ASP A 363      -2.072   7.145  56.204  1.00148.64           O  
ANISOU 2782  O   ASP A 363    18605  17981  19891  -3512   2792   3145       O  
ATOM   2783  CB  ASP A 363      -1.161   4.356  57.648  1.00143.09           C  
ANISOU 2783  CB  ASP A 363    17792  16899  19678  -3578   2741   4030       C  
ATOM   2784  N   ASP A 364      -0.275   7.430  57.541  1.00148.68           N  
ANISOU 2784  N   ASP A 364    18848  18311  19332  -3371   2765   3350       N  
ATOM   2785  CA  ASP A 364      -0.538   8.840  57.861  1.00150.94           C  
ANISOU 2785  CA  ASP A 364    19176  18918  19255  -3325   2864   3137       C  
ATOM   2786  C   ASP A 364       0.735   9.658  57.610  1.00151.26           C  
ANISOU 2786  C   ASP A 364    19379  19070  19025  -3205   2709   2899       C  
ATOM   2787  O   ASP A 364       1.501   9.921  58.537  1.00153.55           O  
ANISOU 2787  O   ASP A 364    19761  19604  18976  -3133   2738   2983       O  
ATOM   2788  CB  ASP A 364      -0.999   8.974  59.321  1.00156.28           C  
ANISOU 2788  CB  ASP A 364    19797  19953  19631  -3354   3097   3385       C  
ATOM   2789  CG  ASP A 364      -1.457  10.390  59.685  1.00155.63           C  
ANISOU 2789  CG  ASP A 364    19671  20182  19280  -3309   3215   3078       C  
ATOM   2790  OD1 ASP A 364      -1.226  11.339  58.910  1.00147.71           O  
ANISOU 2790  OD1 ASP A 364    18708  19098  18316  -3242   3088   2739       O  
ATOM   2791  OD2 ASP A 364      -2.059  10.545  60.768  1.00161.21           O  
ANISOU 2791  OD2 ASP A 364    20262  21230  19759  -3354   3432   3180       O  
ATOM   2792  N   PRO A 365       0.974  10.042  56.343  1.00146.62           N  
ANISOU 2792  N   PRO A 365    18802  18337  18572  -3199   2539   2617       N  
ATOM   2793  CA  PRO A 365       2.158  10.813  55.964  1.00140.73           C  
ANISOU 2793  CA  PRO A 365    18177  17687  17606  -3113   2380   2411       C  
ATOM   2794  C   PRO A 365       2.430  12.085  56.785  1.00137.25           C  
ANISOU 2794  C   PRO A 365    17790  17524  16835  -3026   2440   2313       C  
ATOM   2795  O   PRO A 365       3.587  12.347  57.106  1.00134.53           O  
ANISOU 2795  O   PRO A 365    17566  17295  16255  -2938   2363   2276       O  
ATOM   2796  CB  PRO A 365       1.873  11.176  54.507  1.00139.56           C  
ANISOU 2796  CB  PRO A 365    17947  17431  17648  -3179   2232   2180       C  
ATOM   2797  CG  PRO A 365       1.070  10.033  53.995  1.00141.67           C  
ANISOU 2797  CG  PRO A 365    18085  17474  18268  -3276   2253   2240       C  
ATOM   2798  CD  PRO A 365       0.240   9.557  55.157  1.00146.27           C  
ANISOU 2798  CD  PRO A 365    18628  18045  18900  -3294   2467   2512       C  
ATOM   2799  N   HIS A 366       1.391  12.857  57.116  1.00132.68           N  
ANISOU 2799  N   HIS A 366    17093  17041  16278  -3047   2567   2231       N  
ATOM   2800  CA  HIS A 366       1.572  14.148  57.802  1.00127.82           C  
ANISOU 2800  CA  HIS A 366    16453  16659  15453  -2962   2605   2029       C  
ATOM   2801  C   HIS A 366       2.218  13.983  59.175  1.00130.15           C  
ANISOU 2801  C   HIS A 366    16818  17264  15371  -2891   2723   2124       C  
ATOM   2802  O   HIS A 366       3.174  14.681  59.492  1.00128.89           O  
ANISOU 2802  O   HIS A 366    16726  17250  14997  -2794   2648   1970       O  
ATOM   2803  CB  HIS A 366       0.250  14.916  57.928  1.00122.68           C  
ANISOU 2803  CB  HIS A 366    15601  16032  14981  -2998   2722   1877       C  
ATOM   2804  N   ALA A 367       1.715  13.039  59.971  1.00132.44           N  
ANISOU 2804  N   ALA A 367    17070  17672  15580  -2954   2893   2407       N  
ATOM   2805  CA  ALA A 367       2.319  12.699  61.267  1.00131.89           C  
ANISOU 2805  CA  ALA A 367    17040  17956  15117  -2925   2987   2605       C  
ATOM   2806  C   ALA A 367       3.833  12.464  61.142  1.00130.96           C  
ANISOU 2806  C   ALA A 367    17106  17783  14869  -2836   2795   2654       C  
ATOM   2807  O   ALA A 367       4.610  12.820  62.030  1.00130.53           O  
ANISOU 2807  O   ALA A 367    17094  18048  14451  -2762   2804   2628       O  
ATOM   2808  N   CYS A 368       4.235  11.875  60.019  1.00126.53           N  
ANISOU 2808  N   CYS A 368    16626  16844  14607  -2847   2621   2682       N  
ATOM   2809  CA  CYS A 368       5.627  11.554  59.741  1.00120.06           C  
ANISOU 2809  CA  CYS A 368    15949  15930  13739  -2773   2432   2693       C  
ATOM   2810  C   CYS A 368       6.433  12.790  59.320  1.00117.53           C  
ANISOU 2810  C   CYS A 368    15696  15674  13284  -2681   2309   2343       C  
ATOM   2811  O   CYS A 368       7.417  13.128  59.977  1.00119.04           O  
ANISOU 2811  O   CYS A 368    15968  16066  13194  -2589   2268   2305       O  
ATOM   2812  CB  CYS A 368       5.679  10.472  58.655  1.00117.47           C  
ANISOU 2812  CB  CYS A 368    15611  15211  13812  -2830   2303   2764       C  
ATOM   2813  SG  CYS A 368       7.290   9.718  58.349  1.00114.31           S  
ANISOU 2813  SG  CYS A 368    15315  14655  13464  -2755   2083   2784       S  
ATOM   2814  N   TYR A 369       6.015  13.466  58.243  1.00113.68           N  
ANISOU 2814  N   TYR A 369    15153  15030  13011  -2716   2236   2120       N  
ATOM   2815  CA  TYR A 369       6.780  14.609  57.698  1.00108.42           C  
ANISOU 2815  CA  TYR A 369    14513  14384  12297  -2661   2083   1861       C  
ATOM   2816  C   TYR A 369       6.645  15.931  58.471  1.00107.36           C  
ANISOU 2816  C   TYR A 369    14301  14455  12034  -2588   2144   1649       C  
ATOM   2817  O   TYR A 369       7.425  16.854  58.253  1.00101.98           O  
ANISOU 2817  O   TYR A 369    13629  13789  11328  -2530   2011   1466       O  
ATOM   2818  CB  TYR A 369       6.514  14.818  56.187  1.00106.23           C  
ANISOU 2818  CB  TYR A 369    14169  13907  12288  -2754   1938   1770       C  
ATOM   2819  CG  TYR A 369       5.110  15.241  55.756  1.00108.33           C  
ANISOU 2819  CG  TYR A 369    14274  14087  12800  -2842   1992   1742       C  
ATOM   2820  CD1 TYR A 369       4.623  16.522  56.014  1.00110.55           C  
ANISOU 2820  CD1 TYR A 369    14435  14417  13152  -2817   2003   1593       C  
ATOM   2821  CD2 TYR A 369       4.296  14.380  55.028  1.00110.85           C  
ANISOU 2821  CD2 TYR A 369    14526  14250  13340  -2949   2007   1832       C  
ATOM   2822  CE1 TYR A 369       3.352  16.911  55.592  1.00111.39           C  
ANISOU 2822  CE1 TYR A 369    14370  14415  13540  -2894   2028   1568       C  
ATOM   2823  CE2 TYR A 369       3.029  14.760  54.604  1.00110.77           C  
ANISOU 2823  CE2 TYR A 369    14361  14163  13564  -3030   2041   1809       C  
ATOM   2824  CZ  TYR A 369       2.556  16.023  54.883  1.00111.56           C  
ANISOU 2824  CZ  TYR A 369    14352  14307  13728  -3003   2048   1693       C  
ATOM   2825  OH  TYR A 369       1.287  16.385  54.458  1.00111.01           O  
ANISOU 2825  OH  TYR A 369    14105  14133  13941  -3080   2063   1674       O  
ATOM   2826  N   SER A 370       5.682  16.013  59.387  1.00113.85           N  
ANISOU 2826  N   SER A 370    15014  15447  12799  -2597   2341   1649       N  
ATOM   2827  CA  SER A 370       5.482  17.213  60.223  1.00117.03           C  
ANISOU 2827  CA  SER A 370    15275  16084  13109  -2525   2418   1354       C  
ATOM   2828  C   SER A 370       6.742  17.687  60.953  1.00117.37           C  
ANISOU 2828  C   SER A 370    15387  16359  12850  -2406   2358   1209       C  
ATOM   2829  O   SER A 370       6.975  18.887  61.078  1.00118.16           O  
ANISOU 2829  O   SER A 370    15375  16495  13026  -2334   2295    884       O  
ATOM   2830  CB  SER A 370       4.388  16.964  61.270  1.00120.19           C  
ANISOU 2830  CB  SER A 370    15531  16757  13379  -2564   2675   1380       C  
ATOM   2831  OG  SER A 370       3.110  16.876  60.671  1.00121.27           O  
ANISOU 2831  OG  SER A 370    15546  16687  13843  -2658   2735   1407       O  
ATOM   2832  N   THR A 371       7.544  16.742  61.434  1.00117.42           N  
ANISOU 2832  N   THR A 371    15551  16498  12567  -2387   2361   1450       N  
ATOM   2833  CA  THR A 371       8.657  17.047  62.330  1.00117.34           C  
ANISOU 2833  CA  THR A 371    15592  16782  12209  -2280   2328   1347       C  
ATOM   2834  C   THR A 371      10.003  17.155  61.616  1.00112.64           C  
ANISOU 2834  C   THR A 371    15150  15990  11660  -2219   2102   1316       C  
ATOM   2835  O   THR A 371      11.048  17.032  62.255  1.00109.99           O  
ANISOU 2835  O   THR A 371    14899  15847  11045  -2140   2052   1331       O  
ATOM   2836  CB  THR A 371       8.775  15.951  63.403  1.00118.21           C  
ANISOU 2836  CB  THR A 371    15749  17208  11958  -2306   2445   1689       C  
ATOM   2837  OG1 THR A 371       9.177  14.717  62.786  1.00114.98           O  
ANISOU 2837  OG1 THR A 371    15488  16503  11695  -2351   2340   2052       O  
ATOM   2838  CG2 THR A 371       7.441  15.766  64.111  1.00122.80           C  
ANISOU 2838  CG2 THR A 371    16156  18047  12455  -2398   2685   1765       C  
ATOM   2839  N   VAL A 372       9.986  17.398  60.309  1.00110.23           N  
ANISOU 2839  N   VAL A 372    14855  15349  11679  -2267   1963   1278       N  
ATOM   2840  CA  VAL A 372      11.204  17.240  59.504  1.00110.19           C  
ANISOU 2840  CA  VAL A 372    14976  15192  11698  -2250   1767   1298       C  
ATOM   2841  C   VAL A 372      12.295  18.280  59.782  1.00108.06           C  
ANISOU 2841  C   VAL A 372    14706  15028  11324  -2147   1651   1056       C  
ATOM   2842  O   VAL A 372      13.474  17.951  59.721  1.00108.65           O  
ANISOU 2842  O   VAL A 372    14902  15117  11264  -2099   1542   1090       O  
ATOM   2843  CB  VAL A 372      10.895  17.210  57.989  1.00109.16           C  
ANISOU 2843  CB  VAL A 372    14813  14787  11876  -2362   1652   1329       C  
ATOM   2844  CG1 VAL A 372      10.729  18.623  57.443  1.00109.91           C  
ANISOU 2844  CG1 VAL A 372    14765  14814  12181  -2382   1545   1140       C  
ATOM   2845  CG2 VAL A 372      11.985  16.458  57.241  1.00106.70           C  
ANISOU 2845  CG2 VAL A 372    14613  14393  11537  -2375   1511   1394       C  
ATOM   2846  N   PHE A 373      11.920  19.518  60.100  1.00110.27           N  
ANISOU 2846  N   PHE A 373    14822  15362  11714  -2111   1663    788       N  
ATOM   2847  CA  PHE A 373      12.918  20.583  60.308  1.00108.99           C  
ANISOU 2847  CA  PHE A 373    14612  15246  11554  -2017   1532    527       C  
ATOM   2848  C   PHE A 373      13.676  20.459  61.628  1.00108.93           C  
ANISOU 2848  C   PHE A 373    14654  15584  11151  -1897   1594    416       C  
ATOM   2849  O   PHE A 373      14.701  21.118  61.821  1.00107.34           O  
ANISOU 2849  O   PHE A 373    14444  15432  10909  -1812   1475    219       O  
ATOM   2850  CB  PHE A 373      12.273  21.964  60.184  1.00108.89           C  
ANISOU 2850  CB  PHE A 373    14346  15114  11913  -2016   1489    252       C  
ATOM   2851  CG  PHE A 373      11.777  22.262  58.803  1.00107.61           C  
ANISOU 2851  CG  PHE A 373    14111  14631  12144  -2144   1355    404       C  
ATOM   2852  CD1 PHE A 373      10.448  22.042  58.454  1.00106.47           C  
ANISOU 2852  CD1 PHE A 373    13880  14382  12193  -2234   1442    503       C  
ATOM   2853  CD2 PHE A 373      12.650  22.729  57.836  1.00105.98           C  
ANISOU 2853  CD2 PHE A 373    13908  14274  12086  -2193   1136    477       C  
ATOM   2854  CE1 PHE A 373       9.999  22.298  57.168  1.00103.29           C  
ANISOU 2854  CE1 PHE A 373    13392  13737  12116  -2366   1299    670       C  
ATOM   2855  CE2 PHE A 373      12.206  22.986  56.550  1.00103.38           C  
ANISOU 2855  CE2 PHE A 373    13481  13745  12054  -2343   1001    670       C  
ATOM   2856  CZ  PHE A 373      10.881  22.770  56.216  1.00102.21           C  
ANISOU 2856  CZ  PHE A 373    13247  13503  12086  -2427   1075    768       C  
ATOM   2857  N   ASP A 374      13.174  19.609  62.520  1.00110.33           N  
ANISOU 2857  N   ASP A 374    14862  16023  11037  -1904   1769    572       N  
ATOM   2858  CA  ASP A 374      13.941  19.185  63.681  1.00116.72           C  
ANISOU 2858  CA  ASP A 374    15734  17209  11407  -1827   1805    614       C  
ATOM   2859  C   ASP A 374      15.041  18.201  63.229  1.00117.96           C  
ANISOU 2859  C   ASP A 374    16107  17211  11503  -1820   1663    908       C  
ATOM   2860  O   ASP A 374      16.184  18.278  63.701  1.00123.45           O  
ANISOU 2860  O   ASP A 374    16862  18058  11984  -1730   1566    847       O  
ATOM   2861  CB  ASP A 374      13.027  18.551  64.740  1.00119.82           C  
ANISOU 2861  CB  ASP A 374    16050  17976  11500  -1877   2024    777       C  
ATOM   2862  N   LYS A 375      14.693  17.283  62.320  1.00114.55           N  
ANISOU 2862  N   LYS A 375    15757  16479  11287  -1911   1644   1181       N  
ATOM   2863  CA  LYS A 375      15.647  16.310  61.766  1.00111.44           C  
ANISOU 2863  CA  LYS A 375    15508  15894  10942  -1909   1505   1385       C  
ATOM   2864  C   LYS A 375      16.719  16.975  60.892  1.00109.37           C  
ANISOU 2864  C   LYS A 375    15280  15477  10799  -1874   1324   1162       C  
ATOM   2865  O   LYS A 375      17.808  16.430  60.729  1.00109.73           O  
ANISOU 2865  O   LYS A 375    15417  15473  10805  -1832   1203   1216       O  
ATOM   2866  CB  LYS A 375      14.911  15.229  60.960  1.00107.08           C  
ANISOU 2866  CB  LYS A 375    14967  15064  10657  -2020   1532   1631       C  
ATOM   2867  N   LEU A 376      16.416  18.145  60.329  1.00108.24           N  
ANISOU 2867  N   LEU A 376    15034  15257  10835  -1900   1295    933       N  
ATOM   2868  CA  LEU A 376      17.394  18.881  59.524  1.00106.04           C  
ANISOU 2868  CA  LEU A 376    14747  14871  10674  -1896   1120    775       C  
ATOM   2869  C   LEU A 376      18.318  19.737  60.396  1.00107.00           C  
ANISOU 2869  C   LEU A 376    14845  15173  10636  -1768   1063    542       C  
ATOM   2870  O   LEU A 376      19.513  19.828  60.122  1.00108.73           O  
ANISOU 2870  O   LEU A 376    15119  15373  10822  -1730    926    487       O  
ATOM   2871  CB  LEU A 376      16.696  19.742  58.464  1.00104.94           C  
ANISOU 2871  CB  LEU A 376    14467  14552  10853  -2008   1069    722       C  
ATOM   2872  CG  LEU A 376      15.932  18.972  57.381  1.00103.66           C  
ANISOU 2872  CG  LEU A 376    14302  14239  10844  -2149   1086    910       C  
ATOM   2873  CD1 LEU A 376      15.187  19.919  56.455  1.00106.78           C  
ANISOU 2873  CD1 LEU A 376    14528  14513  11530  -2267   1017    900       C  
ATOM   2874  CD2 LEU A 376      16.862  18.078  56.584  1.00104.36           C  
ANISOU 2874  CD2 LEU A 376    14475  14296  10882  -2188    988    972       C  
ATOM   2875  N   LYS A 377      17.780  20.340  61.453  1.00108.98           N  
ANISOU 2875  N   LYS A 377    14990  15630  10788  -1704   1169    368       N  
ATOM   2876  CA  LYS A 377      18.614  21.044  62.443  1.00111.51           C  
ANISOU 2876  CA  LYS A 377    15257  16195  10917  -1575   1129     94       C  
ATOM   2877  C   LYS A 377      19.931  20.291  62.752  1.00110.61           C  
ANISOU 2877  C   LYS A 377    15309  16191  10526  -1504   1037    216       C  
ATOM   2878  O   LYS A 377      21.009  20.886  62.785  1.00106.07           O  
ANISOU 2878  O   LYS A 377    14725  15629   9948  -1431    906     24       O  
ATOM   2879  CB  LYS A 377      17.826  21.259  63.740  1.00112.73           C  
ANISOU 2879  CB  LYS A 377    15279  16711  10844  -1528   1304    -72       C  
ATOM   2880  N   HIS A 378      19.827  18.981  62.967  1.00111.69           N  
ANISOU 2880  N   HIS A 378    15570  16376  10490  -1530   1090    546       N  
ATOM   2881  CA  HIS A 378      20.986  18.122  63.236  1.00113.00           C  
ANISOU 2881  CA  HIS A 378    15866  16592  10479  -1469    982    713       C  
ATOM   2882  C   HIS A 378      22.075  18.198  62.158  1.00112.90           C  
ANISOU 2882  C   HIS A 378    15909  16317  10670  -1468    809    630       C  
ATOM   2883  O   HIS A 378      23.273  18.211  62.475  1.00114.11           O  
ANISOU 2883  O   HIS A 378    16107  16550  10700  -1378    690    557       O  
ATOM   2884  CB  HIS A 378      20.530  16.668  63.396  1.00112.52           C  
ANISOU 2884  CB  HIS A 378    15874  16492  10386  -1526   1037   1126       C  
ATOM   2885  N   LEU A 379      21.664  18.253  60.890  1.00110.96           N  
ANISOU 2885  N   LEU A 379    15639  15809  10712  -1578    794    638       N  
ATOM   2886  CA  LEU A 379      22.622  18.291  59.778  1.00104.91           C  
ANISOU 2886  CA  LEU A 379    14883  14884  10096  -1617    649    563       C  
ATOM   2887  C   LEU A 379      23.401  19.602  59.698  1.00104.59           C  
ANISOU 2887  C   LEU A 379    14766  14884  10091  -1581    543    315       C  
ATOM   2888  O   LEU A 379      24.388  19.693  58.971  1.00108.57           O  
ANISOU 2888  O   LEU A 379    15264  15333  10654  -1607    421    253       O  
ATOM   2889  CB  LEU A 379      21.937  18.006  58.434  1.00103.47           C  
ANISOU 2889  CB  LEU A 379    14649  14516  10150  -1773    660    640       C  
ATOM   2890  CG  LEU A 379      21.702  16.520  58.090  1.00103.18           C  
ANISOU 2890  CG  LEU A 379    14657  14360  10188  -1814    687    812       C  
ATOM   2891  CD1 LEU A 379      21.450  16.370  56.602  1.00100.33           C  
ANISOU 2891  CD1 LEU A 379    14202  13898  10019  -1966    652    764       C  
ATOM   2892  CD2 LEU A 379      22.841  15.592  58.495  1.00103.70           C  
ANISOU 2892  CD2 LEU A 379    14790  14413  10197  -1716    594    844       C  
ATOM   2893  N   VAL A 380      22.953  20.625  60.412  1.00104.99           N  
ANISOU 2893  N   VAL A 380    14719  15029  10142  -1532    587    150       N  
ATOM   2894  CA  VAL A 380      23.693  21.876  60.476  1.00105.44           C  
ANISOU 2894  CA  VAL A 380    14662  15089  10311  -1484    471   -107       C  
ATOM   2895  C   VAL A 380      24.731  21.820  61.605  1.00108.38           C  
ANISOU 2895  C   VAL A 380    15087  15688  10404  -1327    429   -259       C  
ATOM   2896  O   VAL A 380      25.844  22.322  61.459  1.00108.59           O  
ANISOU 2896  O   VAL A 380    15087  15694  10478  -1286    295   -404       O  
ATOM   2897  CB  VAL A 380      22.738  23.061  60.672  1.00106.71           C  
ANISOU 2897  CB  VAL A 380    14625  15200  10721  -1498    509   -287       C  
ATOM   2898  CG1 VAL A 380      23.507  24.370  60.597  1.00112.42           C  
ANISOU 2898  CG1 VAL A 380    15179  15838  11699  -1465    352   -537       C  
ATOM   2899  CG2 VAL A 380      21.635  23.039  59.624  1.00101.24           C  
ANISOU 2899  CG2 VAL A 380    13876  14303  10289  -1654    540    -92       C  
ATOM   2900  N   ASP A 381      24.373  21.177  62.713  1.00110.20           N  
ANISOU 2900  N   ASP A 381    15375  16166  10331  -1256    537   -193       N  
ATOM   2901  CA  ASP A 381      25.251  21.079  63.883  1.00112.38           C  
ANISOU 2901  CA  ASP A 381    15674  16745  10279  -1123    494   -295       C  
ATOM   2902  C   ASP A 381      26.425  20.116  63.691  1.00113.05           C  
ANISOU 2902  C   ASP A 381    15906  16778  10270  -1087    369   -109       C  
ATOM   2903  O   ASP A 381      27.518  20.362  64.198  1.00114.89           O  
ANISOU 2903  O   ASP A 381    16137  17145  10369   -986    257   -258       O  
ATOM   2904  CB  ASP A 381      24.441  20.660  65.115  1.00115.50           C  
ANISOU 2904  CB  ASP A 381    16043  17509  10332  -1097    644   -214       C  
ATOM   2905  CG  ASP A 381      23.400  21.695  65.507  1.00117.81           C  
ANISOU 2905  CG  ASP A 381    16135  17927  10702  -1105    768   -521       C  
ATOM   2906  OD1 ASP A 381      23.753  22.889  65.625  1.00118.48           O  
ANISOU 2906  OD1 ASP A 381    16058  18009  10950  -1042    699   -924       O  
ATOM   2907  OD2 ASP A 381      22.225  21.316  65.698  1.00118.17           O  
ANISOU 2907  OD2 ASP A 381    16153  18055  10691  -1174    927   -378       O  
ATOM   2908  N   GLU A 382      26.205  19.016  62.978  1.00117.45           N  
ANISOU 2908  N   GLU A 382    16559  17132  10935  -1165    379    180       N  
ATOM   2909  CA  GLU A 382      27.266  18.023  62.779  1.00124.83           C  
ANISOU 2909  CA  GLU A 382    17582  17975  11872  -1128    251    318       C  
ATOM   2910  C   GLU A 382      28.553  18.671  62.204  1.00129.25           C  
ANISOU 2910  C   GLU A 382    18115  18459  12534  -1094    105     63       C  
ATOM   2911  O   GLU A 382      29.625  18.542  62.807  1.00135.10           O  
ANISOU 2911  O   GLU A 382    18882  19313  13137   -986     -8     10       O  
ATOM   2912  CB  GLU A 382      26.754  16.826  61.943  1.00123.88           C  
ANISOU 2912  CB  GLU A 382    17499  17600  11969  -1225    279    568       C  
ATOM   2913  CG  GLU A 382      27.792  15.756  61.636  1.00125.42           C  
ANISOU 2913  CG  GLU A 382    17723  17641  12290  -1188    135    647       C  
ATOM   2914  N   PRO A 383      28.449  19.400  61.069  1.00127.58           N  
ANISOU 2914  N   PRO A 383    17830  18087  12557  -1199     97    -66       N  
ATOM   2915  CA  PRO A 383      29.599  20.154  60.539  1.00126.23           C  
ANISOU 2915  CA  PRO A 383    17594  17883  12484  -1198    -33   -275       C  
ATOM   2916  C   PRO A 383      30.301  21.090  61.548  1.00126.15           C  
ANISOU 2916  C   PRO A 383    17536  18036  12361  -1065   -103   -513       C  
ATOM   2917  O   PRO A 383      31.532  21.162  61.557  1.00125.03           O  
ANISOU 2917  O   PRO A 383    17391  17914  12199  -1004   -227   -632       O  
ATOM   2918  CB  PRO A 383      28.975  20.980  59.402  1.00126.72           C  
ANISOU 2918  CB  PRO A 383    17538  17819  12793  -1361    -13   -284       C  
ATOM   2919  CG  PRO A 383      27.831  20.157  58.932  1.00125.85           C  
ANISOU 2919  CG  PRO A 383    17466  17630  12719  -1457    100    -78       C  
ATOM   2920  CD  PRO A 383      27.289  19.481  60.158  1.00128.11           C  
ANISOU 2920  CD  PRO A 383    17852  18013  12814  -1346    192     27       C  
ATOM   2921  N   GLN A 384      29.527  21.798  62.373  1.00122.14           N  
ANISOU 2921  N   GLN A 384    16958  17657  11794  -1022    -25   -626       N  
ATOM   2922  CA  GLN A 384      30.079  22.803  63.295  1.00119.60           C  
ANISOU 2922  CA  GLN A 384    16524  17509  11411   -902    -88   -950       C  
ATOM   2923  C   GLN A 384      31.063  22.250  64.338  1.00115.80           C  
ANISOU 2923  C   GLN A 384    16116  17292  10589   -760   -162   -980       C  
ATOM   2924  O   GLN A 384      31.897  22.997  64.841  1.00114.24           O  
ANISOU 2924  O   GLN A 384    15827  17207  10370   -666   -261  -1268       O  
ATOM   2925  CB  GLN A 384      28.955  23.568  64.004  1.00119.72           C  
ANISOU 2925  CB  GLN A 384    16397  17654  11439   -885     25  -1136       C  
ATOM   2926  N   ASN A 385      30.983  20.954  64.644  1.00112.22           N  
ANISOU 2926  N   ASN A 385    15801  16920   9917   -750   -137   -668       N  
ATOM   2927  CA  ASN A 385      31.953  20.307  65.544  1.00110.52           C  
ANISOU 2927  CA  ASN A 385    15642  16929   9421   -634   -248   -596       C  
ATOM   2928  C   ASN A 385      33.355  20.184  64.926  1.00106.22           C  
ANISOU 2928  C   ASN A 385    15124  16196   9037   -597   -418   -674       C  
ATOM   2929  O   ASN A 385      34.341  20.680  65.485  1.00104.96           O  
ANISOU 2929  O   ASN A 385    14916  16189   8777   -493   -533   -895       O  
ATOM   2930  CB  ASN A 385      31.446  18.922  65.962  1.00110.16           C  
ANISOU 2930  CB  ASN A 385    15693  16955   9209   -656   -208   -161       C  
ATOM   2931  N   LEU A 386      33.429  19.546  63.761  1.00102.74           N  
ANISOU 2931  N   LEU A 386    14732  15457   8847   -688   -427   -536       N  
ATOM   2932  CA  LEU A 386      34.706  19.366  63.049  1.00103.19           C  
ANISOU 2932  CA  LEU A 386    14776  15363   9068   -677   -565   -642       C  
ATOM   2933  C   LEU A 386      35.482  20.678  62.923  1.00101.11           C  
ANISOU 2933  C   LEU A 386    14408  15131   8877   -658   -636   -968       C  
ATOM   2934  O   LEU A 386      36.654  20.765  63.307  1.00 97.91           O  
ANISOU 2934  O   LEU A 386    13984  14798   8420   -557   -769  -1112       O  
ATOM   2935  CB  LEU A 386      34.474  18.786  61.643  1.00104.73           C  
ANISOU 2935  CB  LEU A 386    14962  15309   9523   -819   -526   -563       C  
ATOM   2936  N   ILE A 387      34.813  21.697  62.384  1.00 97.69           N  
ANISOU 2936  N   ILE A 387    13882  14621   8614   -759   -565  -1064       N  
ATOM   2937  CA  ILE A 387      35.438  22.990  62.174  1.00 97.19           C  
ANISOU 2937  CA  ILE A 387    13670  14521   8736   -767   -648  -1324       C  
ATOM   2938  C   ILE A 387      36.156  23.431  63.432  1.00 98.98           C  
ANISOU 2938  C   ILE A 387    13859  14956   8794   -594   -736  -1576       C  
ATOM   2939  O   ILE A 387      37.362  23.673  63.395  1.00102.22           O  
ANISOU 2939  O   ILE A 387    14224  15361   9253   -543   -865  -1731       O  
ATOM   2940  CB  ILE A 387      34.416  24.070  61.775  1.00 94.77           C  
ANISOU 2940  CB  ILE A 387    13227  14101   8680   -875   -582  -1360       C  
ATOM   2941  N   LYS A 388      35.421  23.510  64.544  1.00102.67           N  
ANISOU 2941  N   LYS A 388    14322  15653   9036   -512   -663  -1631       N  
ATOM   2942  CA  LYS A 388      35.987  24.005  65.809  1.00107.64           C  
ANISOU 2942  CA  LYS A 388    14865  16586   9449   -358   -738  -1928       C  
ATOM   2943  C   LYS A 388      37.254  23.234  66.182  1.00107.69           C  
ANISOU 2943  C   LYS A 388    14962  16704   9251   -259   -880  -1861       C  
ATOM   2944  O   LYS A 388      38.291  23.841  66.459  1.00103.63           O  
ANISOU 2944  O   LYS A 388    14355  16243   8777   -175  -1010  -2139       O  
ATOM   2945  CB  LYS A 388      34.961  23.926  66.951  1.00109.36           C  
ANISOU 2945  CB  LYS A 388    15052  17159   9342   -313   -616  -1954       C  
ATOM   2946  N   GLN A 389      37.162  21.903  66.164  1.00108.80           N  
ANISOU 2946  N   GLN A 389    15257  16845   9237   -269   -871  -1494       N  
ATOM   2947  CA  GLN A 389      38.299  21.036  66.495  1.00113.95           C  
ANISOU 2947  CA  GLN A 389    15972  17551   9773   -177  -1031  -1378       C  
ATOM   2948  C   GLN A 389      39.481  21.235  65.546  1.00109.23           C  
ANISOU 2948  C   GLN A 389    15341  16693   9470   -188  -1144  -1541       C  
ATOM   2949  O   GLN A 389      40.629  21.400  65.980  1.00104.78           O  
ANISOU 2949  O   GLN A 389    14732  16222   8858    -83  -1294  -1712       O  
ATOM   2950  CB  GLN A 389      37.883  19.555  66.488  1.00118.52           C  
ANISOU 2950  CB  GLN A 389    16671  18066  10296   -207  -1018   -929       C  
ATOM   2951  CG  GLN A 389      37.451  19.013  67.851  1.00123.57           C  
ANISOU 2951  CG  GLN A 389    17323  19098  10531   -151  -1024   -672       C  
ATOM   2952  CD  GLN A 389      37.100  17.532  67.808  1.00127.09           C  
ANISOU 2952  CD  GLN A 389    17846  19408  11034   -194  -1049   -169       C  
ATOM   2953  OE1 GLN A 389      37.077  16.911  66.736  1.00126.30           O  
ANISOU 2953  OE1 GLN A 389    17785  18907  11298   -256  -1044    -83       O  
ATOM   2954  NE2 GLN A 389      36.821  16.958  68.975  1.00126.10           N  
ANISOU 2954  NE2 GLN A 389    17707  19641  10567   -172  -1086    164       N  
ATOM   2955  N   ASN A 390      39.193  21.215  64.251  1.00104.49           N  
ANISOU 2955  N   ASN A 390    14739  15813   9149   -329  -1071  -1489       N  
ATOM   2956  CA  ASN A 390      40.233  21.418  63.255  1.00100.42           C  
ANISOU 2956  CA  ASN A 390    14152  15129   8876   -382  -1151  -1635       C  
ATOM   2957  C   ASN A 390      40.820  22.832  63.245  1.00 98.27           C  
ANISOU 2957  C   ASN A 390    13730  14872   8734   -381  -1211  -1939       C  
ATOM   2958  O   ASN A 390      42.003  23.012  62.960  1.00 97.72           O  
ANISOU 2958  O   ASN A 390    13589  14769   8770   -362  -1324  -2093       O  
ATOM   2959  CB  ASN A 390      39.727  21.005  61.878  1.00100.18           C  
ANISOU 2959  CB  ASN A 390    14115  14906   9043   -560  -1054  -1498       C  
ATOM   2960  CG  ASN A 390      39.783  19.499  61.692  1.00100.67           C  
ANISOU 2960  CG  ASN A 390    14250  14879   9119   -542  -1071  -1317       C  
ATOM   2961  OD1 ASN A 390      40.832  18.899  61.878  1.00 99.65           O  
ANISOU 2961  OD1 ASN A 390    14105  14731   9025   -449  -1204  -1377       O  
ATOM   2962  ND2 ASN A 390      38.655  18.883  61.366  1.00100.85           N  
ANISOU 2962  ND2 ASN A 390    14326  14823   9169   -624   -954  -1106       N  
ATOM   2963  N   CYS A 391      40.013  23.827  63.586  1.00 96.99           N  
ANISOU 2963  N   CYS A 391    13491  14746   8614   -396  -1146  -2044       N  
ATOM   2964  CA  CYS A 391      40.524  25.192  63.694  1.00 95.53           C  
ANISOU 2964  CA  CYS A 391    13115  14529   8651   -382  -1229  -2353       C  
ATOM   2965  C   CYS A 391      41.394  25.374  64.926  1.00 93.45           C  
ANISOU 2965  C   CYS A 391    12815  14496   8195   -191  -1351  -2630       C  
ATOM   2966  O   CYS A 391      42.403  26.080  64.874  1.00 89.58           O  
ANISOU 2966  O   CYS A 391    12191  13956   7888   -161  -1474  -2871       O  
ATOM   2967  CB  CYS A 391      39.387  26.202  63.661  1.00 96.00           C  
ANISOU 2967  CB  CYS A 391    13045  14506   8925   -451  -1148  -2423       C  
ATOM   2968  SG  CYS A 391      38.770  26.460  61.971  1.00 96.17           S  
ANISOU 2968  SG  CYS A 391    13004  14239   9298   -713  -1086  -2131       S  
ATOM   2969  N   ASP A 392      41.036  24.706  66.016  1.00 96.18           N  
ANISOU 2969  N   ASP A 392    13259  15126   8159    -78  -1328  -2570       N  
ATOM   2970  CA  ASP A 392      41.903  24.674  67.204  1.00100.19           C  
ANISOU 2970  CA  ASP A 392    13733  15945   8391     91  -1462  -2770       C  
ATOM   2971  C   ASP A 392      43.231  24.026  66.839  1.00 98.06           C  
ANISOU 2971  C   ASP A 392    13520  15568   8170    129  -1609  -2698       C  
ATOM   2972  O   ASP A 392      44.297  24.573  67.113  1.00 93.19           O  
ANISOU 2972  O   ASP A 392    12794  14996   7617    211  -1746  -2977       O  
ATOM   2973  CB  ASP A 392      41.254  23.899  68.357  1.00104.04           C  
ANISOU 2973  CB  ASP A 392    14303  16823   8406    160  -1417  -2588       C  
ATOM   2974  CG  ASP A 392      40.005  24.578  68.901  1.00108.55           C  
ANISOU 2974  CG  ASP A 392    14768  17597   8877    138  -1268  -2752       C  
ATOM   2975  OD1 ASP A 392      39.589  25.627  68.362  1.00109.43           O  
ANISOU 2975  OD1 ASP A 392    14743  17480   9353     78  -1213  -2997       O  
ATOM   2976  OD2 ASP A 392      39.426  24.049  69.872  1.00115.03           O  
ANISOU 2976  OD2 ASP A 392    15613  18820   9272    169  -1213  -2620       O  
ATOM   2977  N   GLN A 393      43.154  22.862  66.197  1.00 98.58           N  
ANISOU 2977  N   GLN A 393    13726  15478   8252     70  -1583  -2359       N  
ATOM   2978  CA  GLN A 393      44.351  22.145  65.759  1.00 99.37           C  
ANISOU 2978  CA  GLN A 393    13844  15448   8463    100  -1716  -2323       C  
ATOM   2979  C   GLN A 393      45.198  23.002  64.804  1.00 97.15           C  
ANISOU 2979  C   GLN A 393    13428  14984   8501     24  -1750  -2578       C  
ATOM   2980  O   GLN A 393      46.434  22.934  64.838  1.00 95.14           O  
ANISOU 2980  O   GLN A 393    13115  14726   8308     94  -1891  -2729       O  
ATOM   2981  CB  GLN A 393      43.973  20.815  65.111  1.00101.67           C  
ANISOU 2981  CB  GLN A 393    14243  15561   8824     34  -1669  -1991       C  
ATOM   2982  CG  GLN A 393      45.104  19.793  65.041  1.00104.68           C  
ANISOU 2982  CG  GLN A 393    14618  15847   9307    112  -1837  -1944       C  
ATOM   2983  CD  GLN A 393      44.649  18.467  64.438  1.00110.28           C  
ANISOU 2983  CD  GLN A 393    15377  16343  10181     53  -1803  -1670       C  
ATOM   2984  OE1 GLN A 393      43.443  18.192  64.338  1.00112.74           O  
ANISOU 2984  OE1 GLN A 393    15762  16630  10446    -25  -1666  -1451       O  
ATOM   2985  NE2 GLN A 393      45.613  17.637  64.021  1.00110.28           N  
ANISOU 2985  NE2 GLN A 393    15306  16172  10423     92  -1935  -1720       N  
ATOM   2986  N   PHE A 394      44.539  23.831  63.990  1.00 93.25           N  
ANISOU 2986  N   PHE A 394    12860  14354   8217   -129  -1635  -2599       N  
ATOM   2987  CA  PHE A 394      45.254  24.768  63.121  1.00 93.11           C  
ANISOU 2987  CA  PHE A 394    12669  14200   8508   -238  -1676  -2764       C  
ATOM   2988  C   PHE A 394      45.904  25.887  63.925  1.00 93.76           C  
ANISOU 2988  C   PHE A 394    12601  14348   8677   -128  -1797  -3099       C  
ATOM   2989  O   PHE A 394      47.095  26.173  63.746  1.00 92.90           O  
ANISOU 2989  O   PHE A 394    12385  14207   8705   -111  -1913  -3268       O  
ATOM   2990  CB  PHE A 394      44.338  25.376  62.048  1.00 92.85           C  
ANISOU 2990  CB  PHE A 394    12559  14018   8701   -453  -1554  -2615       C  
ATOM   2991  CG  PHE A 394      44.933  26.584  61.367  1.00 92.36           C  
ANISOU 2991  CG  PHE A 394    12265  13845   8983   -580  -1621  -2722       C  
ATOM   2992  CD1 PHE A 394      45.986  26.444  60.477  1.00 92.03           C  
ANISOU 2992  CD1 PHE A 394    12130  13805   9033   -687  -1669  -2721       C  
ATOM   2993  CD2 PHE A 394      44.469  27.867  61.652  1.00 92.43           C  
ANISOU 2993  CD2 PHE A 394    12107  13748   9264   -597  -1650  -2836       C  
ATOM   2994  CE1 PHE A 394      46.557  27.556  59.873  1.00 92.40           C  
ANISOU 2994  CE1 PHE A 394    11936  13775   9398   -828  -1739  -2757       C  
ATOM   2995  CE2 PHE A 394      45.034  28.979  61.047  1.00 92.15           C  
ANISOU 2995  CE2 PHE A 394    11819  13565   9628   -725  -1744  -2879       C  
ATOM   2996  CZ  PHE A 394      46.076  28.825  60.151  1.00 90.86           C  
ANISOU 2996  CZ  PHE A 394    11579  13429   9516   -851  -1787  -2802       C  
ATOM   2997  N   GLU A 395      45.113  26.524  64.794  1.00 94.71           N  
ANISOU 2997  N   GLU A 395    12679  14569   8736    -58  -1766  -3234       N  
ATOM   2998  CA  GLU A 395      45.610  27.597  65.663  1.00 95.98           C  
ANISOU 2998  CA  GLU A 395    12649  14821   8997     60  -1881  -3642       C  
ATOM   2999  C   GLU A 395      46.855  27.121  66.416  1.00 97.59           C  
ANISOU 2999  C   GLU A 395    12883  15226   8970    224  -2034  -3794       C  
ATOM   3000  O   GLU A 395      47.834  27.850  66.520  1.00 98.57           O  
ANISOU 3000  O   GLU A 395    12840  15311   9299    269  -2163  -4084       O  
ATOM   3001  CB  GLU A 395      44.519  28.069  66.636  1.00 94.96           C  
ANISOU 3001  CB  GLU A 395    12460  14878   8741    132  -1810  -3821       C  
ATOM   3002  N   LYS A 396      46.816  25.881  66.898  1.00 99.81           N  
ANISOU 3002  N   LYS A 396    13356  15695   8871    302  -2036  -3563       N  
ATOM   3003  CA  LYS A 396      47.901  25.288  67.697  1.00103.74           C  
ANISOU 3003  CA  LYS A 396    13881  16403   9133    460  -2208  -3625       C  
ATOM   3004  C   LYS A 396      49.194  25.064  66.915  1.00103.06           C  
ANISOU 3004  C   LYS A 396    13760  16105   9294    441  -2316  -3657       C  
ATOM   3005  O   LYS A 396      50.275  25.387  67.400  1.00107.32           O  
ANISOU 3005  O   LYS A 396    14195  16732   9849    550  -2475  -3915       O  
ATOM   3006  CB  LYS A 396      47.437  23.943  68.287  1.00105.13           C  
ANISOU 3006  CB  LYS A 396    14240  16775   8931    512  -2202  -3251       C  
ATOM   3007  CG  LYS A 396      48.366  23.342  69.334  1.00107.06           C  
ANISOU 3007  CG  LYS A 396    14484  17305   8891    672  -2407  -3237       C  
ATOM   3008  CD  LYS A 396      47.665  22.277  70.167  1.00108.26           C  
ANISOU 3008  CD  LYS A 396    14750  17735   8647    701  -2409  -2828       C  
ATOM   3009  CE  LYS A 396      48.511  21.855  71.357  1.00112.41           C  
ANISOU 3009  CE  LYS A 396    15225  18643   8843    843  -2637  -2785       C  
ATOM   3010  NZ  LYS A 396      47.681  21.316  72.476  1.00115.63           N  
ANISOU 3010  NZ  LYS A 396    15655  19530   8750    848  -2627  -2464       N  
ATOM   3011  N   LEU A 397      49.072  24.508  65.710  1.00101.91           N  
ANISOU 3011  N   LEU A 397    13675  15717   9328    299  -2227  -3429       N  
ATOM   3012  CA  LEU A 397      50.224  24.029  64.939  1.00 96.60           C  
ANISOU 3012  CA  LEU A 397    12956  14907   8839    270  -2306  -3457       C  
ATOM   3013  C   LEU A 397      50.681  24.984  63.846  1.00 96.41           C  
ANISOU 3013  C   LEU A 397    12753  14730   9149    104  -2268  -3600       C  
ATOM   3014  O   LEU A 397      51.836  24.922  63.426  1.00 94.70           O  
ANISOU 3014  O   LEU A 397    12432  14477   9073     95  -2354  -3736       O  
ATOM   3015  CB  LEU A 397      49.882  22.688  64.296  1.00 92.74           C  
ANISOU 3015  CB  LEU A 397    12586  14314   8339    212  -2241  -3171       C  
ATOM   3016  CG  LEU A 397      49.649  21.554  65.286  1.00 94.09           C  
ANISOU 3016  CG  LEU A 397    12892  14587   8269    359  -2327  -2942       C  
ATOM   3017  CD1 LEU A 397      48.841  20.450  64.631  1.00 90.78           C  
ANISOU 3017  CD1 LEU A 397    12565  14011   7915    270  -2221  -2647       C  
ATOM   3018  CD2 LEU A 397      50.979  21.032  65.806  1.00 94.53           C  
ANISOU 3018  CD2 LEU A 397    12893  14676   8347    512  -2552  -3038       C  
ATOM   3019  N   GLY A 398      49.782  25.852  63.375  1.00 97.22           N  
ANISOU 3019  N   GLY A 398    12795  14750   9395    -41  -2152  -3540       N  
ATOM   3020  CA  GLY A 398      50.045  26.672  62.187  1.00 96.00           C  
ANISOU 3020  CA  GLY A 398    12449  14463   9565   -257  -2117  -3526       C  
ATOM   3021  C   GLY A 398      49.981  25.821  60.927  1.00 95.20           C  
ANISOU 3021  C   GLY A 398    12372  14361   9440   -435  -2010  -3311       C  
ATOM   3022  O   GLY A 398      49.937  24.591  61.006  1.00 94.38           O  
ANISOU 3022  O   GLY A 398    12411  14295   9153   -360  -1991  -3245       O  
ATOM   3023  N   GLU A 399      50.000  26.469  59.762  1.00 94.53           N  
ANISOU 3023  N   GLU A 399    12106  14252   9560   -681  -1954  -3204       N  
ATOM   3024  CA  GLU A 399      49.788  25.780  58.478  1.00 90.98           C  
ANISOU 3024  CA  GLU A 399    11625  13898   9047   -892  -1832  -3026       C  
ATOM   3025  C   GLU A 399      50.628  24.507  58.316  1.00 90.29           C  
ANISOU 3025  C   GLU A 399    11570  13899   8838   -814  -1851  -3183       C  
ATOM   3026  O   GLU A 399      50.073  23.411  58.197  1.00 88.76           O  
ANISOU 3026  O   GLU A 399    11499  13704   8521   -784  -1783  -3112       O  
ATOM   3027  CB  GLU A 399      50.042  26.732  57.294  1.00 91.82           C  
ANISOU 3027  CB  GLU A 399    11458  14073   9355  -1186  -1812  -2894       C  
ATOM   3028  CG  GLU A 399      49.783  26.107  55.927  1.00 91.75           C  
ANISOU 3028  CG  GLU A 399    11364  14284   9214  -1439  -1680  -2731       C  
ATOM   3029  CD  GLU A 399      49.533  27.132  54.831  1.00 92.74           C  
ANISOU 3029  CD  GLU A 399    11231  14523   9484  -1770  -1655  -2435       C  
ATOM   3030  OE1 GLU A 399      48.632  27.974  54.998  1.00 93.13           O  
ANISOU 3030  OE1 GLU A 399    11275  14400   9712  -1816  -1673  -2212       O  
ATOM   3031  OE2 GLU A 399      50.206  27.077  53.782  1.00 92.16           O  
ANISOU 3031  OE2 GLU A 399    10931  14735   9350  -1999  -1621  -2410       O  
ATOM   3032  N   TYR A 400      51.954  24.648  58.318  1.00 81.15           N  
ANISOU 3032  N   TYR A 400    10636  11319   8877   -197  -1597  -2132       N  
ATOM   3033  CA  TYR A 400      52.836  23.526  57.978  1.00 78.55           C  
ANISOU 3033  CA  TYR A 400    10291  11009   8546   -208  -1632  -1977       C  
ATOM   3034  C   TYR A 400      52.603  22.342  58.893  1.00 79.37           C  
ANISOU 3034  C   TYR A 400    10545  11341   8273    -91  -1676  -1888       C  
ATOM   3035  O   TYR A 400      52.272  21.256  58.427  1.00 78.72           O  
ANISOU 3035  O   TYR A 400    10540  11291   8079   -107  -1560  -1644       O  
ATOM   3036  CB  TYR A 400      54.298  23.928  58.033  1.00 79.33           C  
ANISOU 3036  CB  TYR A 400    10217  11011   8915   -224  -1812  -2137       C  
ATOM   3037  CG  TYR A 400      55.219  22.782  57.737  1.00 79.12           C  
ANISOU 3037  CG  TYR A 400    10169  11007   8886   -222  -1843  -1978       C  
ATOM   3038  CD1 TYR A 400      55.151  22.111  56.529  1.00 81.28           C  
ANISOU 3038  CD1 TYR A 400    10457  11190   9236   -295  -1662  -1724       C  
ATOM   3039  CD2 TYR A 400      56.153  22.362  58.662  1.00 81.74           C  
ANISOU 3039  CD2 TYR A 400    10474  11451   9133   -134  -2059  -2087       C  
ATOM   3040  CE1 TYR A 400      55.994  21.051  56.251  1.00 83.09           C  
ANISOU 3040  CE1 TYR A 400    10674  11433   9465   -283  -1682  -1581       C  
ATOM   3041  CE2 TYR A 400      57.002  21.311  58.401  1.00 83.45           C  
ANISOU 3041  CE2 TYR A 400    10665  11685   9358   -127  -2083  -1935       C  
ATOM   3042  CZ  TYR A 400      56.924  20.657  57.198  1.00 85.00           C  
ANISOU 3042  CZ  TYR A 400    10875  11782   9638   -203  -1887  -1683       C  
ATOM   3043  OH  TYR A 400      57.776  19.602  56.946  1.00 86.42           O  
ANISOU 3043  OH  TYR A 400    11035  11972   9827   -185  -1904  -1537       O  
ATOM   3044  N   GLY A 401      52.756  22.559  60.194  1.00 80.29           N  
ANISOU 3044  N   GLY A 401    10704  11609   8193     39  -1843  -2084       N  
ATOM   3045  CA  GLY A 401      52.491  21.515  61.179  1.00 81.18           C  
ANISOU 3045  CA  GLY A 401    10967  11955   7925    182  -1874  -1994       C  
ATOM   3046  C   GLY A 401      51.107  20.897  61.045  1.00 83.98           C  
ANISOU 3046  C   GLY A 401    11458  12379   8073    191  -1652  -1758       C  
ATOM   3047  O   GLY A 401      50.944  19.693  61.251  1.00 86.84           O  
ANISOU 3047  O   GLY A 401    11908  12853   8235    244  -1602  -1553       O  
ATOM   3048  N   PHE A 402      50.110  21.720  60.704  1.00 83.52           N  
ANISOU 3048  N   PHE A 402    11405  12242   8085    139  -1520  -1781       N  
ATOM   3049  CA  PHE A 402      48.723  21.258  60.531  1.00 80.71           C  
ANISOU 3049  CA  PHE A 402    11150  11927   7587    138  -1311  -1564       C  
ATOM   3050  C   PHE A 402      48.615  20.316  59.331  1.00 81.54           C  
ANISOU 3050  C   PHE A 402    11243  11926   7813     16  -1192  -1299       C  
ATOM   3051  O   PHE A 402      47.946  19.280  59.407  1.00 86.90           O  
ANISOU 3051  O   PHE A 402    12008  12679   8333     43  -1093  -1081       O  
ATOM   3052  CB  PHE A 402      47.753  22.461  60.398  1.00 78.24           C  
ANISOU 3052  CB  PHE A 402    10826  11541   7361    109  -1212  -1666       C  
ATOM   3053  CG  PHE A 402      46.294  22.086  60.243  1.00 75.46           C  
ANISOU 3053  CG  PHE A 402    10554  11221   6899    108  -1005  -1450       C  
ATOM   3054  CD1 PHE A 402      45.709  21.118  61.040  1.00 76.48           C  
ANISOU 3054  CD1 PHE A 402    10794  11523   6742    225   -940  -1288       C  
ATOM   3055  CD2 PHE A 402      45.493  22.731  59.304  1.00 73.58           C  
ANISOU 3055  CD2 PHE A 402    10266  10830   6860     -5   -872  -1400       C  
ATOM   3056  CE1 PHE A 402      44.365  20.782  60.891  1.00 76.09           C  
ANISOU 3056  CE1 PHE A 402    10789  11481   6641    219   -748  -1079       C  
ATOM   3057  CE2 PHE A 402      44.151  22.400  59.156  1.00 70.44           C  
ANISOU 3057  CE2 PHE A 402     9920  10451   6392     -9   -699  -1205       C  
ATOM   3058  CZ  PHE A 402      43.583  21.426  59.952  1.00 71.63           C  
ANISOU 3058  CZ  PHE A 402    10166  10762   6288     98   -637  -1045       C  
ATOM   3059  N   GLN A 403      49.265  20.658  58.226  1.00 79.71           N  
ANISOU 3059  N   GLN A 403    10906  11514   7867   -107  -1199  -1315       N  
ATOM   3060  CA  GLN A 403      49.281  19.755  57.064  1.00 77.46           C  
ANISOU 3060  CA  GLN A 403    10625  11129   7678   -198  -1105  -1087       C  
ATOM   3061  C   GLN A 403      49.870  18.398  57.439  1.00 78.83           C  
ANISOU 3061  C   GLN A 403    10850  11404   7697   -138  -1163   -961       C  
ATOM   3062  O   GLN A 403      49.403  17.369  56.977  1.00 79.42           O  
ANISOU 3062  O   GLN A 403    10989  11468   7720   -162  -1073   -749       O  
ATOM   3063  CB  GLN A 403      50.115  20.322  55.939  1.00 73.81           C  
ANISOU 3063  CB  GLN A 403    10045  10477   7521   -298  -1109  -1130       C  
ATOM   3064  CG  GLN A 403      49.605  21.622  55.367  1.00 74.66           C  
ANISOU 3064  CG  GLN A 403    10088  10453   7824   -365  -1033  -1218       C  
ATOM   3065  CD  GLN A 403      50.572  22.189  54.359  1.00 75.72           C  
ANISOU 3065  CD  GLN A 403    10095  10407   8270   -439  -1030  -1248       C  
ATOM   3066  OE1 GLN A 403      51.762  21.874  54.389  1.00 74.95           O  
ANISOU 3066  OE1 GLN A 403     9928  10292   8255   -428  -1123  -1275       O  
ATOM   3067  NE2 GLN A 403      50.060  22.989  53.419  1.00 74.33           N  
ANISOU 3067  NE2 GLN A 403     9879  10089   8273   -506   -909  -1217       N  
ATOM   3068  N   ASN A 404      50.895  18.409  58.283  1.00 80.98           N  
ANISOU 3068  N   ASN A 404    11091  11768   7911    -56  -1326  -1098       N  
ATOM   3069  CA  ASN A 404      51.573  17.178  58.685  1.00 83.98           C  
ANISOU 3069  CA  ASN A 404    11508  12246   8156     13  -1394   -985       C  
ATOM   3070  C   ASN A 404      50.706  16.284  59.587  1.00 83.82           C  
ANISOU 3070  C   ASN A 404    11619  12401   7829    124  -1334   -837       C  
ATOM   3071  O   ASN A 404      50.910  15.069  59.654  1.00 82.02           O  
ANISOU 3071  O   ASN A 404    11435  12221   7509    159  -1321   -658       O  
ATOM   3072  CB  ASN A 404      52.917  17.500  59.370  1.00 86.60           C  
ANISOU 3072  CB  ASN A 404    11756  12629   8521     79  -1606  -1182       C  
ATOM   3073  CG  ASN A 404      53.906  18.183  58.435  1.00 87.43           C  
ANISOU 3073  CG  ASN A 404    11704  12541   8975    -28  -1650  -1277       C  
ATOM   3074  OD1 ASN A 404      53.808  18.053  57.219  1.00 92.47           O  
ANISOU 3074  OD1 ASN A 404    12317  13027   9789   -131  -1517  -1145       O  
ATOM   3075  ND2 ASN A 404      54.855  18.920  58.998  1.00 87.75           N  
ANISOU 3075  ND2 ASN A 404    11636  12583   9123      6  -1836  -1504       N  
ATOM   3076  N   ALA A 405      49.753  16.892  60.288  1.00 83.51           N  
ANISOU 3076  N   ALA A 405    11634  12451   7644    188  -1285   -901       N  
ATOM   3077  CA  ALA A 405      48.785  16.132  61.064  1.00 80.58           C  
ANISOU 3077  CA  ALA A 405    11376  12228   7013    296  -1180   -728       C  
ATOM   3078  C   ALA A 405      47.799  15.487  60.082  1.00 75.89           C  
ANISOU 3078  C   ALA A 405    10794  11510   6529    182  -1002   -486       C  
ATOM   3079  O   ALA A 405      47.435  14.319  60.229  1.00 79.18           O  
ANISOU 3079  O   ALA A 405    11263  11969   6851    216   -929   -263       O  
ATOM   3080  CB  ALA A 405      48.062  17.030  62.067  1.00 76.33           C  
ANISOU 3080  CB  ALA A 405    10893  11814   6297    413  -1163   -868       C  
ATOM   3081  N   LEU A 406      47.369  16.255  59.085  1.00 71.27           N  
ANISOU 3081  N   LEU A 406    10157  10768   6157     53   -941   -531       N  
ATOM   3082  CA  LEU A 406      46.423  15.746  58.104  1.00 70.56           C  
ANISOU 3082  CA  LEU A 406    10076  10554   6180    -51   -805   -333       C  
ATOM   3083  C   LEU A 406      47.029  14.585  57.302  1.00 68.89           C  
ANISOU 3083  C   LEU A 406     9867  10254   6054   -109   -825   -187       C  
ATOM   3084  O   LEU A 406      46.348  13.594  57.057  1.00 70.80           O  
ANISOU 3084  O   LEU A 406    10149  10466   6286   -127   -746     15       O  
ATOM   3085  CB  LEU A 406      45.942  16.861  57.181  1.00 66.96           C  
ANISOU 3085  CB  LEU A 406     9565   9953   5923   -159   -754   -422       C  
ATOM   3086  CG  LEU A 406      45.058  17.923  57.817  1.00 66.70           C  
ANISOU 3086  CG  LEU A 406     9533   9977   5831   -114   -697   -527       C  
ATOM   3087  CD1 LEU A 406      44.964  19.158  56.927  1.00 65.44           C  
ANISOU 3087  CD1 LEU A 406     9300   9667   5897   -213   -679   -654       C  
ATOM   3088  CD2 LEU A 406      43.687  17.328  58.028  1.00 65.60           C  
ANISOU 3088  CD2 LEU A 406     9442   9876   5608    -92   -555   -321       C  
ATOM   3089  N   ILE A 407      48.308  14.694  56.949  1.00 69.95           N  
ANISOU 3089  N   ILE A 407     9953  10342   6284   -128   -930   -289       N  
ATOM   3090  CA  ILE A 407      49.046  13.603  56.313  1.00 69.42           C  
ANISOU 3090  CA  ILE A 407     9893  10206   6279   -154   -953   -167       C  
ATOM   3091  C   ILE A 407      48.918  12.329  57.128  1.00 71.48           C  
ANISOU 3091  C   ILE A 407    10218  10582   6358    -64   -946      0       C  
ATOM   3092  O   ILE A 407      48.580  11.271  56.611  1.00 73.90           O  
ANISOU 3092  O   ILE A 407    10562  10816   6700    -97   -888    182       O  
ATOM   3093  CB  ILE A 407      50.546  13.931  56.189  1.00 72.74           C  
ANISOU 3093  CB  ILE A 407    10236  10601   6801   -148  -1072   -304       C  
ATOM   3094  CG1 ILE A 407      50.784  14.944  55.066  1.00 72.67           C  
ANISOU 3094  CG1 ILE A 407    10153  10427   7032   -247  -1044   -402       C  
ATOM   3095  CG2 ILE A 407      51.363  12.671  55.913  1.00 75.13           C  
ANISOU 3095  CG2 ILE A 407    10555  10882   7110   -130  -1099   -171       C  
ATOM   3096  CD1 ILE A 407      52.210  14.992  54.567  1.00 72.83           C  
ANISOU 3096  CD1 ILE A 407    10086  10367   7220   -258  -1112   -456       C  
ATOM   3097  N   VAL A 408      49.204  12.448  58.413  1.00 75.38           N  
ANISOU 3097  N   VAL A 408    10726  11254   6659     62  -1012    -66       N  
ATOM   3098  CA  VAL A 408      49.082  11.342  59.347  1.00 77.85           C  
ANISOU 3098  CA  VAL A 408    11102  11703   6773    181   -995    100       C  
ATOM   3099  C   VAL A 408      47.668  10.779  59.348  1.00 77.66           C  
ANISOU 3099  C   VAL A 408    11124  11661   6721    170   -835    308       C  
ATOM   3100  O   VAL A 408      47.467   9.577  59.146  1.00 75.50           O  
ANISOU 3100  O   VAL A 408    10873  11339   6473    162   -780    516       O  
ATOM   3101  CB  VAL A 408      49.505  11.780  60.781  1.00 79.65           C  
ANISOU 3101  CB  VAL A 408    11354  12147   6763    347  -1095    -32       C  
ATOM   3102  CG1 VAL A 408      48.728  11.027  61.865  1.00 79.21           C  
ANISOU 3102  CG1 VAL A 408    11384  12253   6458    494   -999    155       C  
ATOM   3103  CG2 VAL A 408      51.013  11.634  60.939  1.00 79.60           C  
ANISOU 3103  CG2 VAL A 408    11300  12171   6772    386  -1269   -138       C  
ATOM   3104  N   ARG A 409      46.691  11.650  59.566  1.00 79.15           N  
ANISOU 3104  N   ARG A 409    11315  11873   6884    168   -760    253       N  
ATOM   3105  CA  ARG A 409      45.303  11.214  59.651  1.00 79.55           C  
ANISOU 3105  CA  ARG A 409    11386  11908   6931    165   -604    453       C  
ATOM   3106  C   ARG A 409      44.871  10.507  58.367  1.00 78.72           C  
ANISOU 3106  C   ARG A 409    11258  11597   7056     18   -562    592       C  
ATOM   3107  O   ARG A 409      44.315   9.417  58.414  1.00 83.85           O  
ANISOU 3107  O   ARG A 409    11918  12213   7730     23   -489    810       O  
ATOM   3108  CB  ARG A 409      44.395  12.406  59.914  1.00 82.01           C  
ANISOU 3108  CB  ARG A 409    11690  12252   7219    174   -535    348       C  
ATOM   3109  CG  ARG A 409      42.979  12.019  60.311  1.00 84.61           C  
ANISOU 3109  CG  ARG A 409    12029  12603   7517    212   -362    561       C  
ATOM   3110  CD  ARG A 409      42.012  13.180  60.164  1.00 86.43           C  
ANISOU 3110  CD  ARG A 409    12231  12801   7808    176   -284    472       C  
ATOM   3111  NE  ARG A 409      42.485  14.388  60.836  1.00 87.81           N  
ANISOU 3111  NE  ARG A 409    12428  13091   7844    263   -352    218       N  
ATOM   3112  CZ  ARG A 409      41.850  15.553  60.805  1.00 92.74           C  
ANISOU 3112  CZ  ARG A 409    13033  13696   8509    249   -304     92       C  
ATOM   3113  NH1 ARG A 409      40.705  15.693  60.133  1.00 94.40           N  
ANISOU 3113  NH1 ARG A 409    13195  13787   8886    153   -185    205       N  
ATOM   3114  NH2 ARG A 409      42.362  16.588  61.451  1.00 97.29           N  
ANISOU 3114  NH2 ARG A 409    13632  14365   8969    334   -385   -155       N  
ATOM   3115  N   TYR A 410      45.133  11.128  57.224  1.00 73.58           N  
ANISOU 3115  N   TYR A 410    10575  10805   6577   -103   -610    466       N  
ATOM   3116  CA  TYR A 410      44.651  10.596  55.954  1.00 73.54           C  
ANISOU 3116  CA  TYR A 410    10566  10610   6767   -224   -585    567       C  
ATOM   3117  C   TYR A 410      45.464   9.377  55.455  1.00 72.85           C  
ANISOU 3117  C   TYR A 410    10504  10445   6729   -236   -640    657       C  
ATOM   3118  O   TYR A 410      44.893   8.479  54.841  1.00 70.30           O  
ANISOU 3118  O   TYR A 410    10197   9998   6516   -290   -614    800       O  
ATOM   3119  CB  TYR A 410      44.509  11.719  54.889  1.00 70.91           C  
ANISOU 3119  CB  TYR A 410    10203  10161   6580   -324   -596    423       C  
ATOM   3120  CG  TYR A 410      43.154  12.439  54.967  1.00 71.64           C  
ANISOU 3120  CG  TYR A 410    10270  10247   6704   -351   -507    438       C  
ATOM   3121  CD1 TYR A 410      42.918  13.441  55.910  1.00 74.70           C  
ANISOU 3121  CD1 TYR A 410    10641  10760   6980   -281   -472    331       C  
ATOM   3122  CD2 TYR A 410      42.103  12.089  54.118  1.00 70.92           C  
ANISOU 3122  CD2 TYR A 410    10169  10019   6758   -435   -466    557       C  
ATOM   3123  CE1 TYR A 410      41.681  14.077  55.994  1.00 75.79           C  
ANISOU 3123  CE1 TYR A 410    10753  10891   7154   -296   -376    357       C  
ATOM   3124  CE2 TYR A 410      40.863  12.719  54.191  1.00 70.94           C  
ANISOU 3124  CE2 TYR A 410    10132  10011   6810   -458   -385    585       C  
ATOM   3125  CZ  TYR A 410      40.657  13.712  55.127  1.00 74.76           C  
ANISOU 3125  CZ  TYR A 410    10599  10623   7184   -387   -329    492       C  
ATOM   3126  OH  TYR A 410      39.430  14.339  55.201  1.00 77.91           O  
ANISOU 3126  OH  TYR A 410    10955  11008   7639   -401   -235    527       O  
ATOM   3127  N   THR A 411      46.765   9.323  55.741  1.00 71.34           N  
ANISOU 3127  N   THR A 411    10314  10320   6472   -180   -723    574       N  
ATOM   3128  CA  THR A 411      47.561   8.153  55.382  1.00 70.79           C  
ANISOU 3128  CA  THR A 411    10268  10188   6441   -172   -764    667       C  
ATOM   3129  C   THR A 411      47.127   6.918  56.169  1.00 75.51           C  
ANISOU 3129  C   THR A 411    10891  10838   6959   -103   -714    880       C  
ATOM   3130  O   THR A 411      47.139   5.799  55.637  1.00 74.40           O  
ANISOU 3130  O   THR A 411    10773  10580   6917   -132   -708   1011       O  
ATOM   3131  CB  THR A 411      49.054   8.389  55.604  1.00 72.06           C  
ANISOU 3131  CB  THR A 411    10404  10414   6564   -120   -862    543       C  
ATOM   3132  OG1 THR A 411      49.418   9.612  54.970  1.00 72.03           O  
ANISOU 3132  OG1 THR A 411    10354  10354   6659   -178   -891    360       O  
ATOM   3133  CG2 THR A 411      49.898   7.266  54.988  1.00 72.19           C  
ANISOU 3133  CG2 THR A 411    10441  10333   6656   -121   -892    632       C  
ATOM   3134  N   ARG A 412      46.731   7.117  57.423  1.00 77.79           N  
ANISOU 3134  N   ARG A 412    11180  11298   7077     -1   -670    918       N  
ATOM   3135  CA  ARG A 412      46.104   6.045  58.210  1.00 81.09           C  
ANISOU 3135  CA  ARG A 412    11613  11766   7430     77   -580   1156       C  
ATOM   3136  C   ARG A 412      44.727   5.659  57.671  1.00 79.25           C  
ANISOU 3136  C   ARG A 412    11357  11385   7367    -13   -479   1307       C  
ATOM   3137  O   ARG A 412      44.378   4.482  57.639  1.00 81.76           O  
ANISOU 3137  O   ARG A 412    11669  11618   7777    -15   -433   1508       O  
ATOM   3138  CB  ARG A 412      45.936   6.477  59.657  1.00 85.82           C  
ANISOU 3138  CB  ARG A 412    12230  12593   7784    233   -538   1160       C  
ATOM   3139  CG  ARG A 412      47.223   6.459  60.451  1.00 88.26           C  
ANISOU 3139  CG  ARG A 412    12564  13066   7907    360   -649   1073       C  
ATOM   3140  CD  ARG A 412      47.007   6.907  61.888  1.00 89.02           C  
ANISOU 3140  CD  ARG A 412    12701  13398   7725    541   -621   1060       C  
ATOM   3141  NE  ARG A 412      48.246   6.752  62.656  1.00 94.02           N  
ANISOU 3141  NE  ARG A 412    13359  14186   8177    676   -755    987       N  
ATOM   3142  CZ  ARG A 412      48.653   7.547  63.649  1.00 98.33           C  
ANISOU 3142  CZ  ARG A 412    13938  14927   8494    817   -845    817       C  
ATOM   3143  NH1 ARG A 412      47.941   8.605  64.027  1.00 99.32           N  
ANISOU 3143  NH1 ARG A 412    14086  15121   8532    849   -805    691       N  
ATOM   3144  NH2 ARG A 412      49.800   7.286  64.267  1.00101.23           N  
ANISOU 3144  NH2 ARG A 412    14319  15421   8724    935   -990    760       N  
ATOM   3145  N   LYS A 413      43.945   6.661  57.285  1.00 77.45           N  
ANISOU 3145  N   LYS A 413    11107  11123   7199    -82   -451   1211       N  
ATOM   3146  CA  LYS A 413      42.599   6.451  56.738  1.00 78.65           C  
ANISOU 3146  CA  LYS A 413    11219  11131   7532   -173   -376   1332       C  
ATOM   3147  C   LYS A 413      42.648   5.670  55.428  1.00 74.35           C  
ANISOU 3147  C   LYS A 413    10681  10367   7202   -289   -448   1358       C  
ATOM   3148  O   LYS A 413      41.914   4.705  55.247  1.00 73.12           O  
ANISOU 3148  O   LYS A 413    10498  10088   7196   -324   -416   1531       O  
ATOM   3149  CB  LYS A 413      41.913   7.791  56.452  1.00 81.69           C  
ANISOU 3149  CB  LYS A 413    11578  11519   7943   -225   -354   1195       C  
ATOM   3150  CG  LYS A 413      41.240   8.492  57.622  1.00 84.69           C  
ANISOU 3150  CG  LYS A 413    11943  12063   8172   -123   -243   1214       C  
ATOM   3151  CD  LYS A 413      40.715   9.856  57.164  1.00 84.05           C  
ANISOU 3151  CD  LYS A 413    11836  11956   8144   -187   -237   1051       C  
ATOM   3152  CE  LYS A 413      39.774  10.503  58.172  1.00 85.30           C  
ANISOU 3152  CE  LYS A 413    11976  12240   8196    -94   -104   1091       C  
ATOM   3153  NZ  LYS A 413      39.447  11.893  57.760  1.00 83.81           N  
ANISOU 3153  NZ  LYS A 413    11764  12027   8052   -146   -109    908       N  
ATOM   3154  N   VAL A 414      43.520   6.101  54.522  1.00 69.56           N  
ANISOU 3154  N   VAL A 414    10110   9704   6615   -337   -546   1183       N  
ATOM   3155  CA  VAL A 414      43.579   5.546  53.180  1.00 66.53           C  
ANISOU 3155  CA  VAL A 414     9757   9120   6400   -425   -617   1171       C  
ATOM   3156  C   VAL A 414      45.029   5.325  52.715  1.00 66.15           C  
ANISOU 3156  C   VAL A 414     9760   9060   6315   -398   -692   1076       C  
ATOM   3157  O   VAL A 414      45.527   6.020  51.821  1.00 67.34           O  
ANISOU 3157  O   VAL A 414     9933   9160   6493   -433   -734    931       O  
ATOM   3158  CB  VAL A 414      42.800   6.435  52.191  1.00 66.33           C  
ANISOU 3158  CB  VAL A 414     9724   8997   6484   -516   -633   1073       C  
ATOM   3159  CG1 VAL A 414      41.307   6.243  52.419  1.00 67.73           C  
ANISOU 3159  CG1 VAL A 414     9840   9123   6773   -556   -573   1211       C  
ATOM   3160  CG2 VAL A 414      43.180   7.908  52.328  1.00 62.41           C  
ANISOU 3160  CG2 VAL A 414     9213   8610   5889   -503   -622    899       C  
ATOM   3161  N   PRO A 415      45.705   4.327  53.304  1.00 66.49           N  
ANISOU 3161  N   PRO A 415     9815   9143   6307   -329   -696   1177       N  
ATOM   3162  CA  PRO A 415      47.105   4.030  53.013  1.00 66.42           C  
ANISOU 3162  CA  PRO A 415     9839   9131   6267   -289   -757   1113       C  
ATOM   3163  C   PRO A 415      47.396   3.484  51.630  1.00 66.30           C  
ANISOU 3163  C   PRO A 415     9883   8922   6387   -338   -805   1083       C  
ATOM   3164  O   PRO A 415      48.543   3.531  51.187  1.00 67.62           O  
ANISOU 3164  O   PRO A 415    10073   9077   6542   -307   -837   1005       O  
ATOM   3165  CB  PRO A 415      47.441   2.958  54.035  1.00 67.01           C  
ANISOU 3165  CB  PRO A 415     9907   9283   6271   -199   -736   1273       C  
ATOM   3166  CG  PRO A 415      46.143   2.270  54.251  1.00 68.83           C  
ANISOU 3166  CG  PRO A 415    10119   9442   6594   -227   -669   1450       C  
ATOM   3167  CD  PRO A 415      45.169   3.396  54.310  1.00 68.56           C  
ANISOU 3167  CD  PRO A 415    10051   9451   6547   -273   -629   1382       C  
ATOM   3168  N  AGLN A 416      46.385   2.943  50.959  0.50 66.08           N  
ANISOU 3168  N  AGLN A 416     9879   8738   6491   -403   -812   1146       N  
ATOM   3169  N  BGLN A 416      46.382   2.945  50.964  0.50 65.72           N  
ANISOU 3169  N  BGLN A 416     9833   8693   6445   -402   -812   1146       N  
ATOM   3170  CA AGLN A 416      46.565   2.425  49.610  0.50 65.11           C  
ANISOU 3170  CA AGLN A 416     9835   8429   6476   -431   -874   1099       C  
ATOM   3171  CA BGLN A 416      46.544   2.418  49.623  0.50 64.56           C  
ANISOU 3171  CA BGLN A 416     9764   8358   6407   -431   -874   1101       C  
ATOM   3172  C  AGLN A 416      46.796   3.535  48.594  0.50 63.74           C  
ANISOU 3172  C  AGLN A 416     9697   8233   6290   -452   -890    937       C  
ATOM   3173  C  BGLN A 416      46.779   3.528  48.596  0.50 63.43           C  
ANISOU 3173  C  BGLN A 416     9657   8192   6251   -453   -891    938       C  
ATOM   3174  O  AGLN A 416      47.325   3.282  47.514  0.50 65.43           O  
ANISOU 3174  O  AGLN A 416     9991   8334   6535   -433   -925    878       O  
ATOM   3175  O  BGLN A 416      47.313   3.274  47.520  0.50 65.11           O  
ANISOU 3175  O  BGLN A 416     9951   8294   6496   -434   -925    879       O  
ATOM   3176  CB AGLN A 416      45.320   1.670  49.174  0.50 67.80           C  
ANISOU 3176  CB AGLN A 416    10182   8605   6976   -495   -908   1183       C  
ATOM   3177  CB BGLN A 416      45.284   1.651  49.233  0.50 66.72           C  
ANISOU 3177  CB BGLN A 416    10041   8471   6839   -495   -905   1191       C  
ATOM   3178  CG AGLN A 416      44.776   0.658  50.155  0.50 67.69           C  
ANISOU 3178  CG AGLN A 416    10106   8585   7027   -486   -867   1376       C  
ATOM   3179  CG BGLN A 416      44.587   0.882  50.359  0.50 66.18           C  
ANISOU 3179  CG BGLN A 416     9896   8429   6823   -490   -850   1383       C  
ATOM   3180  CD AGLN A 416      45.171  -0.736  49.741  0.50 66.50           C  
ANISOU 3180  CD AGLN A 416    10005   8274   6988   -467   -917   1442       C  
ATOM   3181  CD BGLN A 416      43.524   1.730  51.045  0.50 63.82           C  
ANISOU 3181  CD BGLN A 416     9514   8230   6505   -519   -781   1421       C  
ATOM   3182  OE1AGLN A 416      46.340  -0.999  49.449  0.50 63.58           O  
ANISOU 3182  OE1AGLN A 416     9697   7908   6553   -409   -936   1388       O  
ATOM   3183  OE1BGLN A 416      43.839   2.727  51.662  0.50 60.98           O  
ANISOU 3183  OE1BGLN A 416     9135   8045   5991   -482   -733   1354       O  
ATOM   3184  NE2AGLN A 416      44.194  -1.629  49.671  0.50 67.08           N  
ANISOU 3184  NE2AGLN A 416    10044   8189   7256   -516   -940   1558       N  
ATOM   3185  NE2BGLN A 416      42.260   1.344  50.914  0.50 63.99           N  
ANISOU 3185  NE2BGLN A 416     9482   8129   6702   -583   -780   1521       N  
ATOM   3186  N   VAL A 417      46.370   4.754  48.918  1.00 62.53           N  
ANISOU 3186  N   VAL A 417     9488   8179   6092   -480   -856    872       N  
ATOM   3187  CA  VAL A 417      46.405   5.868  47.950  1.00 59.96           C  
ANISOU 3187  CA  VAL A 417     9184   7820   5780   -502   -856    742       C  
ATOM   3188  C   VAL A 417      47.829   6.246  47.604  1.00 60.66           C  
ANISOU 3188  C   VAL A 417     9285   7932   5831   -446   -843    658       C  
ATOM   3189  O   VAL A 417      48.718   6.150  48.448  1.00 66.59           O  
ANISOU 3189  O   VAL A 417     9988   8785   6527   -401   -835    665       O  
ATOM   3190  CB  VAL A 417      45.674   7.124  48.494  1.00 59.28           C  
ANISOU 3190  CB  VAL A 417     9022   7835   5669   -539   -812    694       C  
ATOM   3191  CG1 VAL A 417      45.993   8.351  47.669  1.00 55.02           C  
ANISOU 3191  CG1 VAL A 417     8485   7277   5144   -546   -796    567       C  
ATOM   3192  CG2 VAL A 417      44.165   6.898  48.530  1.00 59.00           C  
ANISOU 3192  CG2 VAL A 417     8965   7743   5709   -599   -816    777       C  
ATOM   3193  N   SER A 418      48.052   6.681  46.374  1.00 60.06           N  
ANISOU 3193  N   SER A 418     9267   7763   5791   -437   -838    588       N  
ATOM   3194  CA  SER A 418      49.388   7.033  45.950  1.00 62.66           C  
ANISOU 3194  CA  SER A 418     9596   8094   6120   -376   -801    534       C  
ATOM   3195  C   SER A 418      49.954   8.176  46.815  1.00 62.16           C  
ANISOU 3195  C   SER A 418     9409   8161   6046   -381   -769    463       C  
ATOM   3196  O   SER A 418      49.227   9.044  47.289  1.00 62.64           O  
ANISOU 3196  O   SER A 418     9415   8286   6101   -428   -761    421       O  
ATOM   3197  CB  SER A 418      49.395   7.413  44.469  1.00 67.28           C  
ANISOU 3197  CB  SER A 418    10267   8561   6733   -347   -777    490       C  
ATOM   3198  OG  SER A 418      49.137   8.797  44.287  1.00 74.90           O  
ANISOU 3198  OG  SER A 418    11176   9560   7724   -374   -729    425       O  
ATOM   3199  N   THR A 419      51.263   8.164  47.014  1.00 61.48           N  
ANISOU 3199  N   THR A 419     9277   8105   5976   -329   -760    444       N  
ATOM   3200  CA  THR A 419      51.900   9.129  47.890  1.00 60.68           C  
ANISOU 3200  CA  THR A 419     9051   8116   5889   -328   -765    362       C  
ATOM   3201  C   THR A 419      51.790  10.561  47.368  1.00 61.86           C  
ANISOU 3201  C   THR A 419     9146   8235   6124   -359   -715    268       C  
ATOM   3202  O   THR A 419      51.447  11.463  48.143  1.00 59.32           O  
ANISOU 3202  O   THR A 419     8747   7995   5796   -392   -731    189       O  
ATOM   3203  CB  THR A 419      53.367   8.776  48.139  1.00 58.69           C  
ANISOU 3203  CB  THR A 419     8743   7883   5673   -265   -782    365       C  
ATOM   3204  OG1 THR A 419      53.442   7.462  48.696  1.00 57.31           O  
ANISOU 3204  OG1 THR A 419     8614   7741   5420   -231   -825    462       O  
ATOM   3205  CG2 THR A 419      53.975   9.742  49.109  1.00 59.69           C  
ANISOU 3205  CG2 THR A 419     8734   8119   5828   -265   -826    259       C  
ATOM   3206  N   PRO A 420      52.072  10.780  46.067  1.00 60.53           N  
ANISOU 3206  N   PRO A 420     9023   7947   6030   -335   -648    280       N  
ATOM   3207  CA  PRO A 420      51.939  12.163  45.576  1.00 59.78           C  
ANISOU 3207  CA  PRO A 420     8868   7816   6029   -357   -584    213       C  
ATOM   3208  C   PRO A 420      50.531  12.692  45.774  1.00 58.73           C  
ANISOU 3208  C   PRO A 420     8750   7711   5853   -421   -597    188       C  
ATOM   3209  O   PRO A 420      50.369  13.874  46.113  1.00 64.78           O  
ANISOU 3209  O   PRO A 420     9425   8507   6682   -454   -576    109       O  
ATOM   3210  CB  PRO A 420      52.307  12.073  44.085  1.00 58.60           C  
ANISOU 3210  CB  PRO A 420     8801   7539   5924   -292   -498    268       C  
ATOM   3211  CG  PRO A 420      53.064  10.780  43.932  1.00 59.40           C  
ANISOU 3211  CG  PRO A 420     8971   7614   5984   -228   -514    335       C  
ATOM   3212  CD  PRO A 420      52.531   9.857  45.010  1.00 60.14           C  
ANISOU 3212  CD  PRO A 420     9080   7790   5978   -270   -616    353       C  
ATOM   3213  N   THR A 421      49.528  11.827  45.623  1.00 56.04           N  
ANISOU 3213  N   THR A 421     8509   7354   5428   -439   -635    255       N  
ATOM   3214  CA  THR A 421      48.134  12.238  45.845  1.00 55.57           C  
ANISOU 3214  CA  THR A 421     8451   7316   5349   -500   -646    251       C  
ATOM   3215  C   THR A 421      47.918  12.634  47.297  1.00 57.63           C  
ANISOU 3215  C   THR A 421     8619   7709   5567   -526   -665    206       C  
ATOM   3216  O   THR A 421      47.430  13.721  47.558  1.00 59.75           O  
ANISOU 3216  O   THR A 421     8827   8008   5867   -555   -636    139       O  
ATOM   3217  CB  THR A 421      47.127  11.140  45.460  1.00 57.37           C  
ANISOU 3217  CB  THR A 421     8779   7484   5536   -517   -698    337       C  
ATOM   3218  OG1 THR A 421      47.182  10.901  44.031  1.00 59.66           O  
ANISOU 3218  OG1 THR A 421     9175   7651   5843   -476   -698    351       O  
ATOM   3219  CG2 THR A 421      45.706  11.574  45.860  1.00 55.77           C  
ANISOU 3219  CG2 THR A 421     8541   7309   5341   -580   -705    347       C  
ATOM   3220  N   LEU A 422      48.327  11.769  48.237  1.00 57.10           N  
ANISOU 3220  N   LEU A 422     8548   7723   5424   -499   -708    242       N  
ATOM   3221  CA  LEU A 422      48.237  12.069  49.657  1.00 56.69           C  
ANISOU 3221  CA  LEU A 422     8431   7817   5293   -487   -730    200       C  
ATOM   3222  C   LEU A 422      48.935  13.371  50.032  1.00 59.87           C  
ANISOU 3222  C   LEU A 422     8735   8264   5747   -479   -734     51       C  
ATOM   3223  O   LEU A 422      48.391  14.173  50.808  1.00 58.94           O  
ANISOU 3223  O   LEU A 422     8575   8225   5594   -485   -732    -25       O  
ATOM   3224  CB  LEU A 422      48.815  10.945  50.504  1.00 58.20           C  
ANISOU 3224  CB  LEU A 422     8637   8088   5391   -433   -777    269       C  
ATOM   3225  CG  LEU A 422      48.021   9.642  50.663  1.00 59.27           C  
ANISOU 3225  CG  LEU A 422     8838   8207   5475   -434   -775    424       C  
ATOM   3226  CD1 LEU A 422      48.878   8.593  51.354  1.00 56.13           C  
ANISOU 3226  CD1 LEU A 422     8447   7872   5007   -367   -813    493       C  
ATOM   3227  CD2 LEU A 422      46.719   9.865  51.430  1.00 55.66           C  
ANISOU 3227  CD2 LEU A 422     8364   7820   4964   -451   -738    468       C  
ATOM   3228  N   VAL A 423      50.134  13.583  49.503  1.00 61.53           N  
ANISOU 3228  N   VAL A 423     8905   8416   6059   -461   -737      8       N  
ATOM   3229  CA  VAL A 423      50.881  14.805  49.816  1.00 63.99           C  
ANISOU 3229  CA  VAL A 423     9097   8738   6476   -460   -752   -135       C  
ATOM   3230  C   VAL A 423      50.127  16.045  49.312  1.00 67.02           C  
ANISOU 3230  C   VAL A 423     9452   9058   6955   -508   -685   -193       C  
ATOM   3231  O   VAL A 423      49.950  16.998  50.067  1.00 63.75           O  
ANISOU 3231  O   VAL A 423     8967   8698   6558   -516   -708   -314       O  
ATOM   3232  CB  VAL A 423      52.315  14.767  49.241  1.00 64.69           C  
ANISOU 3232  CB  VAL A 423     9125   8749   6704   -432   -750   -139       C  
ATOM   3233  CG1 VAL A 423      52.956  16.146  49.277  1.00 64.22           C  
ANISOU 3233  CG1 VAL A 423     8924   8646   6833   -447   -747   -273       C  
ATOM   3234  CG2 VAL A 423      53.169  13.751  50.001  1.00 63.60           C  
ANISOU 3234  CG2 VAL A 423     8983   8693   6487   -378   -834   -110       C  
ATOM   3235  N   GLU A 424      49.665  16.020  48.055  1.00 66.93           N  
ANISOU 3235  N   GLU A 424     9500   8934   6995   -527   -610   -111       N  
ATOM   3236  CA  GLU A 424      48.998  17.186  47.448  1.00 64.95           C  
ANISOU 3236  CA  GLU A 424     9221   8614   6843   -560   -539   -145       C  
ATOM   3237  C   GLU A 424      47.706  17.523  48.186  1.00 66.05           C  
ANISOU 3237  C   GLU A 424     9367   8827   6901   -593   -548   -173       C  
ATOM   3238  O   GLU A 424      47.506  18.661  48.640  1.00 68.02           O  
ANISOU 3238  O   GLU A 424     9538   9091   7214   -608   -532   -280       O  
ATOM   3239  CB  GLU A 424      48.685  16.922  45.974  1.00 65.46           C  
ANISOU 3239  CB  GLU A 424     9376   8564   6932   -548   -474    -39       C  
ATOM   3240  CG  GLU A 424      48.233  18.142  45.179  1.00 67.19           C  
ANISOU 3240  CG  GLU A 424     9562   8700   7267   -560   -390    -53       C  
ATOM   3241  CD  GLU A 424      47.696  17.789  43.792  1.00 70.39           C  
ANISOU 3241  CD  GLU A 424    10086   9018   7639   -528   -350     53       C  
ATOM   3242  OE1 GLU A 424      48.441  17.198  42.974  1.00 69.81           O  
ANISOU 3242  OE1 GLU A 424    10079   8889   7557   -464   -324    115       O  
ATOM   3243  OE2 GLU A 424      46.521  18.121  43.509  1.00 73.79           O  
ANISOU 3243  OE2 GLU A 424    10548   9438   8050   -554   -348     72       O  
ATOM   3244  N   VAL A 425      46.840  16.522  48.299  1.00 62.46           N  
ANISOU 3244  N   VAL A 425     8998   8407   6326   -599   -567    -71       N  
ATOM   3245  CA  VAL A 425      45.570  16.660  48.996  1.00 63.96           C  
ANISOU 3245  CA  VAL A 425     9191   8665   6447   -620   -557    -58       C  
ATOM   3246  C   VAL A 425      45.713  17.117  50.452  1.00 68.03           C  
ANISOU 3246  C   VAL A 425     9651   9315   6884   -587   -581   -161       C  
ATOM   3247  O   VAL A 425      44.977  17.982  50.900  1.00 69.00           O  
ANISOU 3247  O   VAL A 425     9738   9469   7010   -593   -545   -222       O  
ATOM   3248  CB  VAL A 425      44.798  15.335  49.033  1.00 62.73           C  
ANISOU 3248  CB  VAL A 425     9113   8517   6206   -626   -579     84       C  
ATOM   3249  CG1 VAL A 425      43.511  15.510  49.825  1.00 60.79           C  
ANISOU 3249  CG1 VAL A 425     8845   8338   5913   -639   -545    119       C  
ATOM   3250  CG2 VAL A 425      44.504  14.866  47.625  1.00 64.57           C  
ANISOU 3250  CG2 VAL A 425     9416   8616   6501   -648   -584    162       C  
ATOM   3251  N   SER A 426      46.637  16.521  51.204  1.00 72.63           N  
ANISOU 3251  N   SER A 426    10232   9981   7385   -539   -646   -183       N  
ATOM   3252  CA  SER A 426      46.800  16.897  52.618  1.00 71.29           C  
ANISOU 3252  CA  SER A 426    10029   9954   7105   -480   -691   -292       C  
ATOM   3253  C   SER A 426      47.287  18.324  52.706  1.00 71.88           C  
ANISOU 3253  C   SER A 426    10013   9999   7300   -487   -709   -481       C  
ATOM   3254  O   SER A 426      46.870  19.068  53.570  1.00 75.03           O  
ANISOU 3254  O   SER A 426    10392  10473   7644   -455   -716   -591       O  
ATOM   3255  CB  SER A 426      47.769  15.977  53.352  1.00 71.60           C  
ANISOU 3255  CB  SER A 426    10083  10088   7033   -414   -775   -278       C  
ATOM   3256  OG  SER A 426      47.210  14.691  53.548  1.00 73.71           O  
ANISOU 3256  OG  SER A 426    10426  10396   7184   -395   -752   -103       O  
ATOM   3257  N   ARG A 427      48.159  18.700  51.790  1.00 72.90           N  
ANISOU 3257  N   ARG A 427    10085  10007   7607   -522   -709   -511       N  
ATOM   3258  CA  ARG A 427      48.649  20.053  51.702  1.00 76.70           C  
ANISOU 3258  CA  ARG A 427    10457  10416   8269   -540   -713   -668       C  
ATOM   3259  C   ARG A 427      47.487  21.031  51.519  1.00 77.35           C  
ANISOU 3259  C   ARG A 427    10534  10459   8397   -572   -630   -695       C  
ATOM   3260  O   ARG A 427      47.356  22.017  52.257  1.00 78.79           O  
ANISOU 3260  O   ARG A 427    10661  10670   8606   -556   -654   -851       O  
ATOM   3261  CB  ARG A 427      49.587  20.136  50.496  1.00 78.39           C  
ANISOU 3261  CB  ARG A 427    10619  10484   8681   -567   -674   -620       C  
ATOM   3262  CG  ARG A 427      50.476  21.343  50.488  1.00 88.52           C  
ANISOU 3262  CG  ARG A 427    11755  11678  10199   -578   -692   -766       C  
ATOM   3263  CD  ARG A 427      51.586  21.150  51.484  1.00 97.41           C  
ANISOU 3263  CD  ARG A 427    12813  12878  11319   -539   -835   -886       C  
ATOM   3264  NE  ARG A 427      52.781  20.663  50.855  1.00100.25           N  
ANISOU 3264  NE  ARG A 427    13118  13162  11809   -532   -835   -814       N  
ATOM   3265  CZ  ARG A 427      53.646  21.436  50.223  1.00102.48           C  
ANISOU 3265  CZ  ARG A 427    13264  13299  12374   -553   -796   -844       C  
ATOM   3266  NH1 ARG A 427      54.708  20.871  49.720  1.00111.73           N  
ANISOU 3266  NH1 ARG A 427    14391  14415  13645   -531   -784   -758       N  
ATOM   3267  NH2 ARG A 427      53.470  22.747  50.082  1.00 96.31           N  
ANISOU 3267  NH2 ARG A 427    12382  12418  11794   -588   -758   -943       N  
ATOM   3268  N   SER A 428      46.628  20.750  50.549  1.00 73.08           N  
ANISOU 3268  N   SER A 428    10050   9851   7865   -609   -544   -550       N  
ATOM   3269  CA  SER A 428      45.499  21.624  50.280  1.00 70.62           C  
ANISOU 3269  CA  SER A 428     9727   9496   7609   -637   -466   -553       C  
ATOM   3270  C   SER A 428      44.486  21.640  51.405  1.00 69.17           C  
ANISOU 3270  C   SER A 428     9572   9435   7275   -608   -462   -578       C  
ATOM   3271  O   SER A 428      43.897  22.678  51.690  1.00 69.83           O  
ANISOU 3271  O   SER A 428     9613   9509   7410   -607   -419   -665       O  
ATOM   3272  CB  SER A 428      44.834  21.219  48.979  1.00 71.95           C  
ANISOU 3272  CB  SER A 428     9955   9572   7809   -671   -403   -392       C  
ATOM   3273  OG  SER A 428      45.696  21.555  47.901  1.00 74.37           O  
ANISOU 3273  OG  SER A 428    10232   9760   8265   -674   -370   -379       O  
ATOM   3274  N   LEU A 429      44.260  20.487  52.026  1.00 66.93           N  
ANISOU 3274  N   LEU A 429     9358   9258   6813   -574   -491   -487       N  
ATOM   3275  CA  LEU A 429      43.371  20.411  53.179  1.00 66.87           C  
ANISOU 3275  CA  LEU A 429     9379   9379   6647   -519   -465   -484       C  
ATOM   3276  C   LEU A 429      43.870  21.314  54.299  1.00 68.05           C  
ANISOU 3276  C   LEU A 429     9494   9615   6746   -450   -516   -693       C  
ATOM   3277  O   LEU A 429      43.088  21.985  54.955  1.00 67.55           O  
ANISOU 3277  O   LEU A 429     9431   9604   6630   -408   -467   -756       O  
ATOM   3278  CB  LEU A 429      43.256  18.979  53.694  1.00 66.35           C  
ANISOU 3278  CB  LEU A 429     9384   9410   6416   -479   -483   -337       C  
ATOM   3279  CG  LEU A 429      42.351  18.087  52.862  1.00 66.32           C  
ANISOU 3279  CG  LEU A 429     9415   9328   6455   -537   -434   -136       C  
ATOM   3280  CD1 LEU A 429      42.449  16.640  53.309  1.00 65.44           C  
ANISOU 3280  CD1 LEU A 429     9358   9280   6227   -502   -458      5       C  
ATOM   3281  CD2 LEU A 429      40.927  18.608  52.963  1.00 68.74           C  
ANISOU 3281  CD2 LEU A 429     9700   9628   6790   -549   -342    -86       C  
ATOM   3282  N   GLY A 430      45.180  21.334  54.492  1.00 67.87           N  
ANISOU 3282  N   GLY A 430     9438   9599   6750   -432   -622   -808       N  
ATOM   3283  CA  GLY A 430      45.791  22.173  55.495  1.00 68.72           C  
ANISOU 3283  CA  GLY A 430     9505   9771   6835   -366   -715  -1035       C  
ATOM   3284  C   GLY A 430      45.591  23.658  55.236  1.00 69.37           C  
ANISOU 3284  C   GLY A 430     9507   9742   7110   -401   -684  -1190       C  
ATOM   3285  O   GLY A 430      45.282  24.401  56.168  1.00 71.65           O  
ANISOU 3285  O   GLY A 430     9798  10096   7328   -334   -706  -1350       O  
ATOM   3286  N   LYS A 431      45.778  24.083  53.981  1.00 66.37           N  
ANISOU 3286  N   LYS A 431     9058   9193   6966   -493   -628  -1140       N  
ATOM   3287  CA  LYS A 431      45.577  25.480  53.569  1.00 67.07           C  
ANISOU 3287  CA  LYS A 431     9058   9149   7276   -532   -576  -1250       C  
ATOM   3288  C   LYS A 431      44.193  25.979  53.973  1.00 67.35           C  
ANISOU 3288  C   LYS A 431     9134   9228   7229   -506   -485  -1249       C  
ATOM   3289  O   LYS A 431      43.979  27.191  54.098  1.00 70.27           O  
ANISOU 3289  O   LYS A 431     9441   9527   7733   -505   -461  -1390       O  
ATOM   3290  CB  LYS A 431      45.700  25.655  52.036  1.00 66.94           C  
ANISOU 3290  CB  LYS A 431     8994   8964   7478   -612   -485  -1116       C  
ATOM   3291  CG  LYS A 431      47.014  26.233  51.514  1.00 69.22           C  
ANISOU 3291  CG  LYS A 431     9162   9116   8023   -641   -519  -1193       C  
ATOM   3292  CD  LYS A 431      46.855  26.913  50.149  1.00 66.65           C  
ANISOU 3292  CD  LYS A 431     8779   8618   7926   -689   -387  -1088       C  
ATOM   3293  N   VAL A 432      43.249  25.062  54.137  1.00 62.34           N  
ANISOU 3293  N   VAL A 432     8590   8692   6405   -485   -427  -1083       N  
ATOM   3294  CA  VAL A 432      41.882  25.459  54.420  1.00 67.23           C  
ANISOU 3294  CA  VAL A 432     9233   9340   6972   -462   -320  -1042       C  
ATOM   3295  C   VAL A 432      41.812  26.162  55.763  1.00 72.00           C  
ANISOU 3295  C   VAL A 432     9850  10047   7459   -357   -349  -1244       C  
ATOM   3296  O   VAL A 432      40.999  27.068  55.961  1.00 74.45           O  
ANISOU 3296  O   VAL A 432    10142  10331   7813   -335   -269  -1305       O  
ATOM   3297  CB  VAL A 432      40.920  24.264  54.407  1.00 68.78           C  
ANISOU 3297  CB  VAL A 432     9502   9612   7018   -457   -256   -813       C  
ATOM   3298  CG1 VAL A 432      39.554  24.693  54.894  1.00 69.36           C  
ANISOU 3298  CG1 VAL A 432     9583   9727   7045   -415   -141   -774       C  
ATOM   3299  CG2 VAL A 432      40.837  23.673  53.002  1.00 63.15           C  
ANISOU 3299  CG2 VAL A 432     8785   8781   6427   -552   -240   -639       C  
ATOM   3300  N   GLY A 433      42.696  25.764  56.670  1.00 74.74           N  
ANISOU 3300  N   GLY A 433    10232  10507   7657   -281   -471  -1356       N  
ATOM   3301  CA  GLY A 433      42.842  26.445  57.940  1.00 77.51           C  
ANISOU 3301  CA  GLY A 433    10609  10958   7884   -161   -540  -1588       C  
ATOM   3302  C   GLY A 433      43.182  27.915  57.799  1.00 81.45           C  
ANISOU 3302  C   GLY A 433    11012  11315   8619   -190   -580  -1824       C  
ATOM   3303  O   GLY A 433      42.615  28.772  58.500  1.00 86.57           O  
ANISOU 3303  O   GLY A 433    11680  11990   9224   -111   -554  -1975       O  
ATOM   3304  N   THR A 434      44.108  28.209  56.895  1.00 80.71           N  
ANISOU 3304  N   THR A 434    10812  11065   8789   -293   -634  -1851       N  
ATOM   3305  CA  THR A 434      44.512  29.583  56.647  1.00 83.32           C  
ANISOU 3305  CA  THR A 434    11023  11227   9408   -334   -663  -2048       C  
ATOM   3306  C   THR A 434      43.406  30.381  55.992  1.00 82.53           C  
ANISOU 3306  C   THR A 434    10894  11017   9448   -378   -497  -1973       C  
ATOM   3307  O   THR A 434      43.182  31.548  56.338  1.00 87.46           O  
ANISOU 3307  O   THR A 434    11472  11569  10192   -352   -491  -2157       O  
ATOM   3308  CB  THR A 434      45.725  29.643  55.718  1.00 83.44           C  
ANISOU 3308  CB  THR A 434    10916  11087   9700   -430   -719  -2035       C  
ATOM   3309  OG1 THR A 434      46.644  28.599  56.066  1.00 87.91           O  
ANISOU 3309  OG1 THR A 434    11514  11758  10131   -403   -843  -2015       O  
ATOM   3310  CG2 THR A 434      46.405  30.988  55.822  1.00 84.21           C  
ANISOU 3310  CG2 THR A 434    10874  11024  10099   -449   -797  -2282       C  
ATOM   3311  N   ARG A 435      42.709  29.752  55.055  1.00 79.63           N  
ANISOU 3311  N   ARG A 435    10553  10633   9069   -440   -373  -1711       N  
ATOM   3312  CA  ARG A 435      41.710  30.461  54.261  1.00 81.75           C  
ANISOU 3312  CA  ARG A 435    10783  10788   9491   -487   -227  -1614       C  
ATOM   3313  C   ARG A 435      40.416  30.684  55.049  1.00 84.92           C  
ANISOU 3313  C   ARG A 435    11247  11286   9732   -409   -139  -1620       C  
ATOM   3314  O   ARG A 435      39.660  31.599  54.721  1.00 91.11           O  
ANISOU 3314  O   ARG A 435    11982  11974  10660   -423    -37  -1622       O  
ATOM   3315  CB  ARG A 435      41.438  29.748  52.928  1.00 75.67           C  
ANISOU 3315  CB  ARG A 435    10021   9959   8773   -568   -152  -1350       C  
ATOM   3316  N   CYS A 436      40.169  29.889  56.095  1.00 84.91           N  
ANISOU 3316  N   CYS A 436    11348  11470   9443   -315   -164  -1613       N  
ATOM   3317  CA  CYS A 436      38.875  29.954  56.801  1.00 86.62           C  
ANISOU 3317  CA  CYS A 436    11625  11786   9499   -227    -45  -1563       C  
ATOM   3318  C   CYS A 436      38.889  30.309  58.298  1.00 89.46           C  
ANISOU 3318  C   CYS A 436    12062  12286   9644    -66    -85  -1776       C  
ATOM   3319  O   CYS A 436      38.092  31.143  58.728  1.00 96.40           O  
ANISOU 3319  O   CYS A 436    12946  13158  10524      3      7  -1855       O  
ATOM   3320  CB  CYS A 436      38.115  28.638  56.619  1.00 86.22           C  
ANISOU 3320  CB  CYS A 436    11633  11828   9298   -236     29  -1281       C  
ATOM   3321  SG  CYS A 436      37.789  28.182  54.898  1.00 84.38           S  
ANISOU 3321  SG  CYS A 436    11340  11445   9273   -392     73  -1032       S  
ATOM   3322  N   CYS A 437      39.751  29.687  59.099  1.00 88.77           N  
ANISOU 3322  N   CYS A 437    12040  12329   9359     10   -218  -1867       N  
ATOM   3323  CA  CYS A 437      39.627  29.808  60.566  1.00 92.36           C  
ANISOU 3323  CA  CYS A 437    12603  12958   9532    200   -248  -2031       C  
ATOM   3324  C   CYS A 437      39.808  31.264  61.066  1.00 92.75           C  
ANISOU 3324  C   CYS A 437    12627  12931   9681    262   -310  -2357       C  
ATOM   3325  O   CYS A 437      39.109  31.721  61.972  1.00 90.45           O  
ANISOU 3325  O   CYS A 437    12417  12730   9221    412   -242  -2455       O  
ATOM   3326  CB  CYS A 437      40.588  28.850  61.289  1.00 92.62           C  
ANISOU 3326  CB  CYS A 437    12712  13147   9331    279   -400  -2064       C  
ATOM   3327  SG  CYS A 437      40.389  27.084  60.898  1.00 88.07           S  
ANISOU 3327  SG  CYS A 437    12177  12664   8624    233   -331  -1698       S  
ATOM   3328  N   THR A 438      40.748  31.971  60.450  1.00 93.74           N  
ANISOU 3328  N   THR A 438    12637  12881  10098    153   -430  -2515       N  
ATOM   3329  CA  THR A 438      40.914  33.418  60.617  1.00 94.19           C  
ANISOU 3329  CA  THR A 438    12626  12795  10366    166   -480  -2800       C  
ATOM   3330  C   THR A 438      39.634  34.247  60.418  1.00 92.44           C  
ANISOU 3330  C   THR A 438    12392  12498  10232    177   -284  -2753       C  
ATOM   3331  O   THR A 438      39.523  35.336  60.953  1.00 92.25           O  
ANISOU 3331  O   THR A 438    12364  12413  10273    253   -306  -3000       O  
ATOM   3332  CB  THR A 438      41.977  33.952  59.626  1.00 95.36           C  
ANISOU 3332  CB  THR A 438    12609  12719  10904      7   -576  -2866       C  
ATOM   3333  OG1 THR A 438      41.967  35.381  59.628  1.00 98.48           O  
ANISOU 3333  OG1 THR A 438    12915  12936  11566      0   -586  -3095       O  
ATOM   3334  CG2 THR A 438      41.699  33.458  58.195  1.00 94.57           C  
ANISOU 3334  CG2 THR A 438    12441  12522  10969   -147   -437  -2547       C  
ATOM   3335  N   LYS A 439      38.680  33.753  59.640  1.00 92.07           N  
ANISOU 3335  N   LYS A 439    12333  12444  10205    105   -105  -2447       N  
ATOM   3336  CA  LYS A 439      37.467  34.516  59.357  1.00 93.62           C  
ANISOU 3336  CA  LYS A 439    12497  12560  10514    108     77  -2378       C  
ATOM   3337  C   LYS A 439      36.572  34.618  60.584  1.00 96.17           C  
ANISOU 3337  C   LYS A 439    12940  13042  10560    299    170  -2439       C  
ATOM   3338  O   LYS A 439      36.780  33.907  61.561  1.00 99.16           O  
ANISOU 3338  O   LYS A 439    13438  13612  10629    428    115  -2472       O  
ATOM   3339  CB  LYS A 439      36.709  33.893  58.188  1.00 92.41           C  
ANISOU 3339  CB  LYS A 439    12294  12360  10457    -15    213  -2037       C  
ATOM   3340  CG  LYS A 439      37.426  34.086  56.855  1.00 91.53           C  
ANISOU 3340  CG  LYS A 439    12068  12066  10644   -177    165  -1980       C  
ATOM   3341  CD  LYS A 439      36.543  33.760  55.653  1.00 88.88           C  
ANISOU 3341  CD  LYS A 439    11688  11663  10421   -275    294  -1684       C  
ATOM   3342  CE  LYS A 439      37.033  34.472  54.399  1.00 86.64           C  
ANISOU 3342  CE  LYS A 439    11289  11173  10458   -388    294  -1666       C  
ATOM   3343  NZ  LYS A 439      38.521  34.415  54.280  1.00 89.81           N  
ANISOU 3343  NZ  LYS A 439    11654  11522  10946   -429    151  -1795       N  
ATOM   3344  N   PRO A 440      35.593  35.533  60.557  1.00 99.38           N  
ANISOU 3344  N   PRO A 440    13317  13369  11073    333    319  -2454       N  
ATOM   3345  CA  PRO A 440      34.602  35.638  61.637  1.00102.16           C  
ANISOU 3345  CA  PRO A 440    13779  13865  11174    527    454  -2470       C  
ATOM   3346  C   PRO A 440      33.983  34.296  62.025  1.00 98.43           C  
ANISOU 3346  C   PRO A 440    13391  13592  10414    596    558  -2189       C  
ATOM   3347  O   PRO A 440      33.449  33.603  61.168  1.00 94.42           O  
ANISOU 3347  O   PRO A 440    12817  13051  10006    474    646  -1893       O  
ATOM   3348  CB  PRO A 440      33.539  36.561  61.031  1.00102.46           C  
ANISOU 3348  CB  PRO A 440    13723  13750  11456    484    632  -2393       C  
ATOM   3349  CG  PRO A 440      34.314  37.461  60.127  1.00101.23           C  
ANISOU 3349  CG  PRO A 440    13439  13366  11657    335    528  -2532       C  
ATOM   3350  CD  PRO A 440      35.499  36.671  59.622  1.00 99.69           C  
ANISOU 3350  CD  PRO A 440    13220  13173  11485    218    359  -2498       C  
ATOM   3351  N   GLU A 441      34.052  33.954  63.308  1.00101.15           N  
ANISOU 3351  N   GLU A 441    13880  14136  10415    800    545  -2284       N  
ATOM   3352  CA  GLU A 441      33.615  32.642  63.826  1.00107.37           C  
ANISOU 3352  CA  GLU A 441    14753  15122  10919    892    641  -2023       C  
ATOM   3353  C   GLU A 441      32.415  32.013  63.105  1.00109.93           C  
ANISOU 3353  C   GLU A 441    14994  15411  11364    799    846  -1642       C  
ATOM   3354  O   GLU A 441      32.423  30.812  62.810  1.00108.70           O  
ANISOU 3354  O   GLU A 441    14829  15309  11164    734    849  -1398       O  
ATOM   3355  CB  GLU A 441      33.302  32.732  65.324  1.00105.27           C  
ANISOU 3355  CB  GLU A 441    14652  15059  10285   1178    709  -2139       C  
ATOM   3356  N   SER A 442      31.390  32.820  62.832  1.00111.46           N  
ANISOU 3356  N   SER A 442    15121  15506  11725    797   1007  -1599       N  
ATOM   3357  CA  SER A 442      30.163  32.324  62.194  1.00109.29           C  
ANISOU 3357  CA  SER A 442    14750  15187  11589    721   1192  -1253       C  
ATOM   3358  C   SER A 442      30.391  31.867  60.738  1.00103.48           C  
ANISOU 3358  C   SER A 442    13893  14302  11121    475   1099  -1094       C  
ATOM   3359  O   SER A 442      29.819  30.872  60.301  1.00 99.69           O  
ANISOU 3359  O   SER A 442    13367  13833  10676    407   1158   -808       O  
ATOM   3360  CB  SER A 442      29.052  33.387  62.261  1.00110.15           C  
ANISOU 3360  CB  SER A 442    14808  15220  11825    787   1376  -1262       C  
ATOM   3361  OG  SER A 442      29.271  34.423  61.312  1.00108.70           O  
ANISOU 3361  OG  SER A 442    14522  14833  11944    644   1306  -1394       O  
ATOM   3362  N   GLU A 443      31.225  32.596  59.999  1.00100.16           N  
ANISOU 3362  N   GLU A 443    13423  13740  10894    355    957  -1279       N  
ATOM   3363  CA  GLU A 443      31.528  32.271  58.595  1.00 93.68           C  
ANISOU 3363  CA  GLU A 443    12507  12780  10307    152    874  -1149       C  
ATOM   3364  C   GLU A 443      32.428  31.032  58.391  1.00 86.71           C  
ANISOU 3364  C   GLU A 443    11666  11962   9318     87    736  -1072       C  
ATOM   3365  O   GLU A 443      32.564  30.548  57.269  1.00 83.20           O  
ANISOU 3365  O   GLU A 443    11164  11425   9023    -58    683   -929       O  
ATOM   3366  CB  GLU A 443      32.201  33.473  57.915  1.00 95.39           C  
ANISOU 3366  CB  GLU A 443    12654  12822  10767     68    791  -1356       C  
ATOM   3367  CG  GLU A 443      31.405  34.779  57.928  1.00 97.24           C  
ANISOU 3367  CG  GLU A 443    12830  12952  11165    110    916  -1437       C  
ATOM   3368  CD  GLU A 443      32.178  35.957  57.328  1.00 98.60           C  
ANISOU 3368  CD  GLU A 443    12927  12939  11598     35    834  -1644       C  
ATOM   3369  OE1 GLU A 443      33.432  35.936  57.320  1.00 98.25           O  
ANISOU 3369  OE1 GLU A 443    12892  12872  11566     -3    675  -1807       O  
ATOM   3370  OE2 GLU A 443      31.533  36.924  56.866  1.00 98.72           O  
ANISOU 3370  OE2 GLU A 443    12860  12822  11828     16    934  -1635       O  
ATOM   3371  N   ARG A 444      33.019  30.522  59.468  1.00 87.00           N  
ANISOU 3371  N   ARG A 444    11809  12159   9088    207    679  -1166       N  
ATOM   3372  CA  ARG A 444      34.006  29.434  59.407  1.00 88.76           C  
ANISOU 3372  CA  ARG A 444    12075  12447   9202    166    540  -1127       C  
ATOM   3373  C   ARG A 444      33.559  28.165  58.654  1.00 88.14           C  
ANISOU 3373  C   ARG A 444    11963  12355   9170     62    571   -816       C  
ATOM   3374  O   ARG A 444      34.279  27.695  57.762  1.00 81.54           O  
ANISOU 3374  O   ARG A 444    11102  11443   8436    -64    456   -782       O  
ATOM   3375  CB  ARG A 444      34.475  29.043  60.827  1.00 90.76           C  
ANISOU 3375  CB  ARG A 444    12455  12901   9126    350    500  -1240       C  
ATOM   3376  CG  ARG A 444      35.426  30.037  61.490  1.00 93.38           C  
ANISOU 3376  CG  ARG A 444    12831  13243   9405    434    359  -1601       C  
ATOM   3377  CD  ARG A 444      36.082  29.458  62.737  1.00 93.70           C  
ANISOU 3377  CD  ARG A 444    13004  13489   9109    608    266  -1704       C  
ATOM   3378  N   MET A 445      32.398  27.616  59.014  1.00 90.63           N  
ANISOU 3378  N   MET A 445    12276  12734   9424    121    726   -595       N  
ATOM   3379  CA  MET A 445      31.919  26.360  58.429  1.00 92.89           C  
ANISOU 3379  CA  MET A 445    12525  13000   9770     34    746   -308       C  
ATOM   3380  C   MET A 445      31.609  26.486  56.920  1.00 86.84           C  
ANISOU 3380  C   MET A 445    11659  12050   9287   -144    703   -216       C  
ATOM   3381  O   MET A 445      32.123  25.706  56.120  1.00 86.94           O  
ANISOU 3381  O   MET A 445    11670  12009   9355   -248    592   -144       O  
ATOM   3382  CB  MET A 445      30.712  25.805  59.209  1.00 99.39           C  
ANISOU 3382  CB  MET A 445    13342  13916  10507    145    934    -82       C  
ATOM   3383  CG  MET A 445      30.030  24.609  58.547  1.00105.34           C  
ANISOU 3383  CG  MET A 445    14020  14605  11401     42    957    218       C  
ATOM   3384  SD  MET A 445      28.239  24.534  58.774  1.00117.75           S  
ANISOU 3384  SD  MET A 445    15479  16152  13107     89   1188    493       S  
ATOM   3385  CE  MET A 445      27.638  25.545  57.408  1.00110.97           C  
ANISOU 3385  CE  MET A 445    14501  15096  12566    -63   1149    458       C  
ATOM   3386  N   PRO A 446      30.774  27.456  56.525  1.00 80.75           N  
ANISOU 3386  N   PRO A 446    10812  11185   8684   -163    790   -218       N  
ATOM   3387  CA  PRO A 446      30.550  27.692  55.102  1.00 80.47           C  
ANISOU 3387  CA  PRO A 446    10696  10987   8893   -306    737   -150       C  
ATOM   3388  C   PRO A 446      31.837  27.805  54.291  1.00 78.85           C  
ANISOU 3388  C   PRO A 446    10514  10709   8735   -391    583   -281       C  
ATOM   3389  O   PRO A 446      31.922  27.288  53.168  1.00 84.68           O  
ANISOU 3389  O   PRO A 446    11234  11361   9580   -493    507   -172       O  
ATOM   3390  CB  PRO A 446      29.815  29.028  55.094  1.00 81.91           C  
ANISOU 3390  CB  PRO A 446    10814  11102   9206   -273    847   -220       C  
ATOM   3391  CG  PRO A 446      29.059  29.020  56.368  1.00 80.70           C  
ANISOU 3391  CG  PRO A 446    10683  11071   8909   -128   1000   -185       C  
ATOM   3392  CD  PRO A 446      29.884  28.272  57.359  1.00 81.77           C  
ANISOU 3392  CD  PRO A 446    10929  11359   8780    -39    953   -249       C  
ATOM   3393  N   CYS A 447      32.823  28.492  54.844  1.00 76.31           N  
ANISOU 3393  N   CYS A 447    10232  10417   8345   -341    538   -515       N  
ATOM   3394  CA  CYS A 447      34.096  28.628  54.165  1.00 76.73           C  
ANISOU 3394  CA  CYS A 447    10289  10398   8468   -412    409   -632       C  
ATOM   3395  C   CYS A 447      34.750  27.274  53.970  1.00 72.61           C  
ANISOU 3395  C   CYS A 447     9821   9926   7840   -448    311   -532       C  
ATOM   3396  O   CYS A 447      35.114  26.918  52.851  1.00 79.74           O  
ANISOU 3396  O   CYS A 447    10712  10738   8846   -538    247   -458       O  
ATOM   3397  CB  CYS A 447      35.036  29.530  54.945  1.00 78.83           C  
ANISOU 3397  CB  CYS A 447    10569  10684   8698   -346    359   -907       C  
ATOM   3398  SG  CYS A 447      36.650  29.721  54.159  1.00 85.18           S  
ANISOU 3398  SG  CYS A 447    11344  11382   9639   -431    214  -1035       S  
ATOM   3399  N   THR A 448      34.890  26.522  55.050  1.00 70.63           N  
ANISOU 3399  N   THR A 448     9636   9822   7377   -365    306   -525       N  
ATOM   3400  CA  THR A 448      35.636  25.268  55.013  1.00 72.30           C  
ANISOU 3400  CA  THR A 448     9901  10087   7482   -384    212   -450       C  
ATOM   3401  C   THR A 448      34.882  24.192  54.254  1.00 73.03           C  
ANISOU 3401  C   THR A 448     9980  10131   7638   -457    227   -201       C  
ATOM   3402  O   THR A 448      35.489  23.377  53.567  1.00 73.23           O  
ANISOU 3402  O   THR A 448    10030  10115   7681   -520    136   -142       O  
ATOM   3403  CB  THR A 448      35.902  24.700  56.417  1.00 71.71           C  
ANISOU 3403  CB  THR A 448     9902  10191   7153   -256    212   -482       C  
ATOM   3404  OG1 THR A 448      34.655  24.448  57.035  1.00 74.49           O  
ANISOU 3404  OG1 THR A 448    10254  10611   7436   -183    356   -328       O  
ATOM   3405  CG2 THR A 448      36.688  25.646  57.284  1.00 72.99           C  
ANISOU 3405  CG2 THR A 448    10093  10415   7225   -164    158   -753       C  
ATOM   3406  N   GLU A 449      33.560  24.201  54.361  1.00 76.30           N  
ANISOU 3406  N   GLU A 449    10350  10538   8102   -446    338    -59       N  
ATOM   3407  CA  GLU A 449      32.754  23.226  53.647  1.00 77.99           C  
ANISOU 3407  CA  GLU A 449    10529  10685   8419   -519    334    167       C  
ATOM   3408  C   GLU A 449      32.875  23.386  52.137  1.00 76.43           C  
ANISOU 3408  C   GLU A 449    10308  10338   8394   -629    243    176       C  
ATOM   3409  O   GLU A 449      32.916  22.397  51.408  1.00 78.58           O  
ANISOU 3409  O   GLU A 449    10598  10554   8704   -689    158    287       O  
ATOM   3410  CB  GLU A 449      31.281  23.273  54.083  1.00 79.55           C  
ANISOU 3410  CB  GLU A 449    10656  10893   8677   -482    475    323       C  
ATOM   3411  CG  GLU A 449      30.981  22.549  55.396  1.00 83.09           C  
ANISOU 3411  CG  GLU A 449    11131  11480   8959   -370    577    427       C  
ATOM   3412  CD  GLU A 449      31.037  21.031  55.288  1.00 84.51           C  
ANISOU 3412  CD  GLU A 449    11319  11655   9135   -407    526    611       C  
ATOM   3413  OE1 GLU A 449      30.076  20.362  55.739  1.00 85.78           O  
ANISOU 3413  OE1 GLU A 449    11424  11828   9339   -374    632    821       O  
ATOM   3414  OE2 GLU A 449      32.034  20.497  54.756  1.00 82.70           O  
ANISOU 3414  OE2 GLU A 449    11145  11399   8878   -464    389    555       O  
ATOM   3415  N   ASP A 450      32.939  24.620  51.661  1.00 78.04           N  
ANISOU 3415  N   ASP A 450    10479  10474   8699   -641    261     62       N  
ATOM   3416  CA  ASP A 450      33.083  24.832  50.230  1.00 78.44           C  
ANISOU 3416  CA  ASP A 450    10518  10394   8891   -717    191     82       C  
ATOM   3417  C   ASP A 450      34.437  24.354  49.745  1.00 73.14           C  
ANISOU 3417  C   ASP A 450     9914   9709   8165   -738     88     18       C  
ATOM   3418  O   ASP A 450      34.505  23.622  48.750  1.00 71.22           O  
ANISOU 3418  O   ASP A 450     9705   9401   7955   -783      9    110       O  
ATOM   3419  CB  ASP A 450      32.905  26.296  49.832  1.00 85.17           C  
ANISOU 3419  CB  ASP A 450    11313  11171   9876   -714    253     -9       C  
ATOM   3420  CG  ASP A 450      32.732  26.465  48.315  1.00 90.25           C  
ANISOU 3420  CG  ASP A 450    11944  11688  10658   -768    202     69       C  
ATOM   3421  OD1 ASP A 450      31.794  25.822  47.753  1.00 92.44           O  
ANISOU 3421  OD1 ASP A 450    12209  11931  10985   -799    163    222       O  
ATOM   3422  OD2 ASP A 450      33.540  27.215  47.695  1.00 91.02           O  
ANISOU 3422  OD2 ASP A 450    12043  11719  10820   -770    197    -19       O  
ATOM   3423  N   TYR A 451      35.510  24.777  50.420  1.00 67.98           N  
ANISOU 3423  N   TYR A 451     9279   9111   7440   -699     82   -144       N  
ATOM   3424  CA  TYR A 451      36.861  24.413  49.970  1.00 66.23           C  
ANISOU 3424  CA  TYR A 451     9100   8868   7198   -715     -5   -203       C  
ATOM   3425  C   TYR A 451      37.077  22.929  50.066  1.00 63.81           C  
ANISOU 3425  C   TYR A 451     8858   8611   6774   -721    -73    -96       C  
ATOM   3426  O   TYR A 451      37.585  22.326  49.147  1.00 61.78           O  
ANISOU 3426  O   TYR A 451     8641   8291   6539   -753   -138    -46       O  
ATOM   3427  CB  TYR A 451      37.953  25.157  50.725  1.00 68.47           C  
ANISOU 3427  CB  TYR A 451     9366   9189   7461   -675    -18   -403       C  
ATOM   3428  CG  TYR A 451      38.195  26.528  50.143  1.00 72.08           C  
ANISOU 3428  CG  TYR A 451     9753   9531   8104   -692     22   -505       C  
ATOM   3429  CD1 TYR A 451      37.651  27.674  50.750  1.00 74.56           C  
ANISOU 3429  CD1 TYR A 451    10012   9840   8476   -660     93   -613       C  
ATOM   3430  CD2 TYR A 451      38.914  26.687  48.957  1.00 72.61           C  
ANISOU 3430  CD2 TYR A 451     9808   9485   8297   -728      5   -478       C  
ATOM   3431  CE1 TYR A 451      37.841  28.946  50.211  1.00 74.23           C  
ANISOU 3431  CE1 TYR A 451     9894   9674   8636   -676    138   -696       C  
ATOM   3432  CE2 TYR A 451      39.106  27.957  48.405  1.00 76.20           C  
ANISOU 3432  CE2 TYR A 451    10186   9822   8945   -735     64   -541       C  
ATOM   3433  CZ  TYR A 451      38.570  29.092  49.039  1.00 75.96           C  
ANISOU 3433  CZ  TYR A 451    10090   9777   8993   -716    127   -652       C  
ATOM   3434  OH  TYR A 451      38.759  30.365  48.505  1.00 73.71           O  
ANISOU 3434  OH  TYR A 451     9719   9358   8930   -723    191   -709       O  
ATOM   3435  N   LEU A 452      36.634  22.322  51.151  1.00 63.83           N  
ANISOU 3435  N   LEU A 452     8874   8723   6656   -679    -47    -48       N  
ATOM   3436  CA  LEU A 452      36.815  20.898  51.279  1.00 63.14           C  
ANISOU 3436  CA  LEU A 452     8838   8673   6480   -681   -101     68       C  
ATOM   3437  C   LEU A 452      36.177  20.207  50.090  1.00 62.61           C  
ANISOU 3437  C   LEU A 452     8776   8489   6523   -751   -147    213       C  
ATOM   3438  O   LEU A 452      36.707  19.240  49.536  1.00 61.50           O  
ANISOU 3438  O   LEU A 452     8690   8310   6368   -773   -229    262       O  
ATOM   3439  CB  LEU A 452      36.208  20.381  52.576  1.00 64.01           C  
ANISOU 3439  CB  LEU A 452     8948   8906   6465   -613    -33    145       C  
ATOM   3440  CG  LEU A 452      37.189  20.126  53.706  1.00 62.90           C  
ANISOU 3440  CG  LEU A 452     8858   8904   6138   -527    -57     54       C  
ATOM   3441  CD1 LEU A 452      38.324  21.121  53.666  1.00 60.12           C  
ANISOU 3441  CD1 LEU A 452     8502   8546   5794   -519   -115   -166       C  
ATOM   3442  CD2 LEU A 452      36.416  20.154  55.011  1.00 62.49           C  
ANISOU 3442  CD2 LEU A 452     8806   8981   5956   -424     52    101       C  
ATOM   3443  N   SER A 453      35.018  20.705  49.707  1.00 62.75           N  
ANISOU 3443  N   SER A 453     8738   8449   6656   -777   -103    275       N  
ATOM   3444  CA  SER A 453      34.320  20.140  48.585  1.00 61.51           C  
ANISOU 3444  CA  SER A 453     8581   8179   6612   -834   -172    394       C  
ATOM   3445  C   SER A 453      35.229  20.169  47.350  1.00 60.63           C  
ANISOU 3445  C   SER A 453     8537   7987   6513   -849   -258    336       C  
ATOM   3446  O   SER A 453      35.281  19.220  46.577  1.00 59.58           O  
ANISOU 3446  O   SER A 453     8461   7790   6388   -869   -355    400       O  
ATOM   3447  CB  SER A 453      33.068  20.955  48.328  1.00 64.83           C  
ANISOU 3447  CB  SER A 453     8919   8551   7164   -849   -117    441       C  
ATOM   3448  OG  SER A 453      32.412  20.485  47.181  1.00 72.69           O  
ANISOU 3448  OG  SER A 453     9912   9434   8272   -897   -214    535       O  
ATOM   3449  N   LEU A 454      35.949  21.269  47.174  1.00 58.23           N  
ANISOU 3449  N   LEU A 454     8226   7679   6220   -828   -215    216       N  
ATOM   3450  CA  LEU A 454      36.824  21.421  46.027  1.00 55.28           C  
ANISOU 3450  CA  LEU A 454     7906   7230   5869   -822   -257    182       C  
ATOM   3451  C   LEU A 454      38.016  20.476  46.080  1.00 53.37           C  
ANISOU 3451  C   LEU A 454     7734   7011   5532   -806   -315    163       C  
ATOM   3452  O   LEU A 454      38.433  19.943  45.079  1.00 49.60           O  
ANISOU 3452  O   LEU A 454     7329   6468   5048   -797   -372    197       O  
ATOM   3453  CB  LEU A 454      37.332  22.862  45.959  1.00 57.73           C  
ANISOU 3453  CB  LEU A 454     8163   7518   6255   -802   -176     72       C  
ATOM   3454  CG  LEU A 454      36.223  23.899  45.863  1.00 60.66           C  
ANISOU 3454  CG  LEU A 454     8461   7855   6731   -808   -108     88       C  
ATOM   3455  CD1 LEU A 454      36.828  25.276  45.705  1.00 61.18           C  
ANISOU 3455  CD1 LEU A 454     8472   7873   6902   -789    -29    -17       C  
ATOM   3456  CD2 LEU A 454      35.297  23.582  44.701  1.00 62.07           C  
ANISOU 3456  CD2 LEU A 454     8666   7957   6962   -821   -164    212       C  
ATOM   3457  N   ILE A 455      38.597  20.314  47.256  1.00 54.24           N  
ANISOU 3457  N   ILE A 455     7828   7219   5562   -789   -298    102       N  
ATOM   3458  CA  ILE A 455      39.802  19.531  47.410  1.00 53.18           C  
ANISOU 3458  CA  ILE A 455     7744   7114   5349   -769   -348     78       C  
ATOM   3459  C   ILE A 455      39.497  18.035  47.416  1.00 52.68           C  
ANISOU 3459  C   ILE A 455     7740   7052   5223   -779   -414    197       C  
ATOM   3460  O   ILE A 455      40.193  17.245  46.766  1.00 51.95           O  
ANISOU 3460  O   ILE A 455     7717   6913   5110   -770   -473    221       O  
ATOM   3461  CB  ILE A 455      40.478  19.897  48.723  1.00 57.17           C  
ANISOU 3461  CB  ILE A 455     8207   7730   5784   -734   -329    -34       C  
ATOM   3462  CG1 ILE A 455      40.978  21.348  48.675  1.00 59.69           C  
ANISOU 3462  CG1 ILE A 455     8458   8017   6203   -728   -284   -175       C  
ATOM   3463  CG2 ILE A 455      41.622  18.939  49.023  1.00 57.14           C  
ANISOU 3463  CG2 ILE A 455     8247   7771   5692   -708   -392    -38       C  
ATOM   3464  CD1 ILE A 455      41.358  21.834  50.069  1.00 62.11           C  
ANISOU 3464  CD1 ILE A 455     8723   8433   6443   -686   -287   -313       C  
ATOM   3465  N   LEU A 456      38.460  17.639  48.146  1.00 49.83           N  
ANISOU 3465  N   LEU A 456     7348   6735   4849   -791   -396    278       N  
ATOM   3466  CA  LEU A 456      38.066  16.251  48.137  1.00 48.62           C  
ANISOU 3466  CA  LEU A 456     7228   6556   4688   -807   -452    405       C  
ATOM   3467  C   LEU A 456      37.721  15.840  46.722  1.00 50.37           C  
ANISOU 3467  C   LEU A 456     7500   6640   4997   -840   -540    449       C  
ATOM   3468  O   LEU A 456      37.969  14.670  46.348  1.00 50.77           O  
ANISOU 3468  O   LEU A 456     7614   6637   5040   -843   -620    501       O  
ATOM   3469  CB  LEU A 456      36.907  15.978  49.075  1.00 49.24           C  
ANISOU 3469  CB  LEU A 456     7243   6683   4783   -810   -394    513       C  
ATOM   3470  CG  LEU A 456      37.216  15.972  50.593  1.00 49.87           C  
ANISOU 3470  CG  LEU A 456     7306   6916   4726   -743   -316    503       C  
ATOM   3471  CD1 LEU A 456      36.063  15.394  51.400  1.00 48.50           C  
ANISOU 3471  CD1 LEU A 456     7079   6775   4575   -729   -242    665       C  
ATOM   3472  CD2 LEU A 456      38.507  15.238  50.894  1.00 48.75           C  
ANISOU 3472  CD2 LEU A 456     7225   6827   4472   -706   -369    471       C  
ATOM   3473  N   ASN A 457      37.222  16.785  45.908  1.00 48.86           N  
ANISOU 3473  N   ASN A 457     7293   6392   4881   -851   -532    419       N  
ATOM   3474  CA  ASN A 457      36.929  16.446  44.525  1.00 47.68           C  
ANISOU 3474  CA  ASN A 457     7210   6124   4782   -855   -630    447       C  
ATOM   3475  C   ASN A 457      38.186  16.167  43.806  1.00 47.64           C  
ANISOU 3475  C   ASN A 457     7305   6092   4704   -808   -659    395       C  
ATOM   3476  O   ASN A 457      38.245  15.244  42.998  1.00 53.64           O  
ANISOU 3476  O   ASN A 457     8155   6775   5451   -793   -758    422       O  
ATOM   3477  CB  ASN A 457      36.213  17.528  43.750  1.00 48.26           C  
ANISOU 3477  CB  ASN A 457     7255   6150   4933   -855   -616    437       C  
ATOM   3478  CG  ASN A 457      35.809  17.050  42.360  1.00 49.12           C  
ANISOU 3478  CG  ASN A 457     7447   6148   5069   -839   -746    467       C  
ATOM   3479  OD1 ASN A 457      35.072  16.080  42.253  1.00 50.15           O  
ANISOU 3479  OD1 ASN A 457     7580   6221   5254   -872   -855    528       O  
ATOM   3480  ND2 ASN A 457      36.330  17.689  41.297  1.00 47.30           N  
ANISOU 3480  ND2 ASN A 457     7287   5884   4802   -777   -738    426       N  
ATOM   3481  N   ARG A 458      39.198  16.966  44.057  1.00 46.24           N  
ANISOU 3481  N   ARG A 458     7110   5966   4492   -778   -575    317       N  
ATOM   3482  CA  ARG A 458      40.493  16.688  43.441  1.00 47.66           C  
ANISOU 3482  CA  ARG A 458     7367   6120   4622   -725   -580    284       C  
ATOM   3483  C   ARG A 458      40.983  15.287  43.821  1.00 48.82           C  
ANISOU 3483  C   ARG A 458     7568   6279   4703   -721   -644    318       C  
ATOM   3484  O   ARG A 458      41.558  14.600  42.995  1.00 50.58           O  
ANISOU 3484  O   ARG A 458     7887   6438   4891   -678   -690    329       O  
ATOM   3485  CB  ARG A 458      41.527  17.712  43.853  1.00 46.95           C  
ANISOU 3485  CB  ARG A 458     7212   6076   4552   -704   -486    199       C  
ATOM   3486  CG  ARG A 458      42.947  17.347  43.507  1.00 47.56           C  
ANISOU 3486  CG  ARG A 458     7334   6136   4602   -652   -477    180       C  
ATOM   3487  CD  ARG A 458      43.288  17.795  42.136  1.00 50.41           C  
ANISOU 3487  CD  ARG A 458     7751   6408   4995   -591   -435    201       C  
ATOM   3488  NE  ARG A 458      44.673  17.517  41.800  1.00 52.29           N  
ANISOU 3488  NE  ARG A 458     8017   6623   5227   -530   -397    198       N  
ATOM   3489  CZ  ARG A 458      45.132  17.374  40.548  1.00 56.03           C  
ANISOU 3489  CZ  ARG A 458     8587   7022   5680   -442   -364    246       C  
ATOM   3490  NH1 ARG A 458      44.319  17.431  39.473  1.00 51.38           N  
ANISOU 3490  NH1 ARG A 458     8093   6378   5051   -398   -388    291       N  
ATOM   3491  NH2 ARG A 458      46.427  17.136  40.362  1.00 58.40           N  
ANISOU 3491  NH2 ARG A 458     8892   7305   5993   -383   -310    254       N  
ATOM   3492  N   LEU A 459      40.752  14.858  45.056  1.00 49.03           N  
ANISOU 3492  N   LEU A 459     7537   6384   4706   -752   -638    343       N  
ATOM   3493  CA  LEU A 459      41.208  13.521  45.474  1.00 50.18           C  
ANISOU 3493  CA  LEU A 459     7726   6541   4801   -742   -688    395       C  
ATOM   3494  C   LEU A 459      40.509  12.425  44.663  1.00 52.87           C  
ANISOU 3494  C   LEU A 459     8137   6763   5187   -759   -790    468       C  
ATOM   3495  O   LEU A 459      41.142  11.454  44.242  1.00 50.67           O  
ANISOU 3495  O   LEU A 459     7940   6431   4880   -728   -846    479       O  
ATOM   3496  CB  LEU A 459      40.960  13.292  46.968  1.00 50.21           C  
ANISOU 3496  CB  LEU A 459     7658   6658   4763   -752   -648    433       C  
ATOM   3497  CG  LEU A 459      41.100  11.863  47.512  1.00 53.28           C  
ANISOU 3497  CG  LEU A 459     8073   7053   5119   -743   -687    530       C  
ATOM   3498  CD1 LEU A 459      42.513  11.348  47.253  1.00 55.95           C  
ANISOU 3498  CD1 LEU A 459     8473   7386   5398   -696   -716    491       C  
ATOM   3499  CD2 LEU A 459      40.747  11.741  48.988  1.00 52.37           C  
ANISOU 3499  CD2 LEU A 459     7891   7062   4945   -726   -624    591       C  
ATOM   3500  N   CYS A 460      39.204  12.597  44.440  1.00 52.49           N  
ANISOU 3500  N   CYS A 460     8051   6667   5225   -803   -822    510       N  
ATOM   3501  CA  CYS A 460      38.441  11.627  43.692  1.00 52.78           C  
ANISOU 3501  CA  CYS A 460     8135   6578   5341   -825   -948    562       C  
ATOM   3502  C   CYS A 460      38.868  11.545  42.243  1.00 53.84           C  
ANISOU 3502  C   CYS A 460     8401   6621   5437   -767  -1030    498       C  
ATOM   3503  O   CYS A 460      38.917  10.489  41.658  1.00 53.96           O  
ANISOU 3503  O   CYS A 460     8502   6540   5461   -749  -1140    502       O  
ATOM   3504  CB  CYS A 460      36.981  11.985  43.724  1.00 54.26           C  
ANISOU 3504  CB  CYS A 460     8233   6731   5652   -881   -970    615       C  
ATOM   3505  SG  CYS A 460      36.355  11.948  45.396  1.00 60.69           S  
ANISOU 3505  SG  CYS A 460     8906   7646   6508   -920   -855    718       S  
ATOM   3506  N   VAL A 461      39.158  12.681  41.650  1.00 54.40           N  
ANISOU 3506  N   VAL A 461     8488   6714   5466   -726   -972    442       N  
ATOM   3507  CA  VAL A 461      39.525  12.678  40.261  1.00 53.23           C  
ANISOU 3507  CA  VAL A 461     8473   6492   5260   -643  -1026    401       C  
ATOM   3508  C   VAL A 461      40.876  12.032  40.045  1.00 54.99           C  
ANISOU 3508  C   VAL A 461     8791   6710   5392   -572  -1002    378       C  
ATOM   3509  O   VAL A 461      41.061  11.323  39.063  1.00 56.74           O  
ANISOU 3509  O   VAL A 461     9148   6848   5563   -502  -1088    359       O  
ATOM   3510  CB  VAL A 461      39.624  14.087  39.736  1.00 51.70           C  
ANISOU 3510  CB  VAL A 461     8264   6327   5052   -601   -933    374       C  
ATOM   3511  CG1 VAL A 461      40.711  14.135  38.660  1.00 52.42           C  
ANISOU 3511  CG1 VAL A 461     8485   6386   5046   -482   -898    348       C  
ATOM   3512  CG2 VAL A 461      38.260  14.538  39.275  1.00 48.67           C  
ANISOU 3512  CG2 VAL A 461     7851   5902   4740   -628  -1006    394       C  
ATOM   3513  N   LEU A 462      41.824  12.320  40.932  1.00 54.98           N  
ANISOU 3513  N   LEU A 462     8722   6797   5372   -579   -890    372       N  
ATOM   3514  CA  LEU A 462      43.147  11.719  40.858  1.00 55.89           C  
ANISOU 3514  CA  LEU A 462     8898   6912   5425   -516   -860    362       C  
ATOM   3515  C   LEU A 462      43.043  10.210  41.132  1.00 58.39           C  
ANISOU 3515  C   LEU A 462     9263   7180   5742   -532   -960    399       C  
ATOM   3516  O   LEU A 462      43.760   9.407  40.528  1.00 58.39           O  
ANISOU 3516  O   LEU A 462     9373   7119   5694   -462   -989    391       O  
ATOM   3517  CB  LEU A 462      44.094  12.383  41.861  1.00 56.24           C  
ANISOU 3517  CB  LEU A 462     8832   7061   5475   -529   -748    341       C  
ATOM   3518  CG  LEU A 462      44.459  13.876  41.645  1.00 56.56           C  
ANISOU 3518  CG  LEU A 462     8806   7127   5556   -511   -638    298       C  
ATOM   3519  CD1 LEU A 462      45.039  14.457  42.913  1.00 55.40           C  
ANISOU 3519  CD1 LEU A 462     8528   7080   5443   -549   -580    254       C  
ATOM   3520  CD2 LEU A 462      45.432  14.101  40.502  1.00 53.61           C  
ANISOU 3520  CD2 LEU A 462     8507   6693   5167   -407   -572    302       C  
ATOM   3521  N   HIS A 463      42.134   9.823  42.023  1.00 57.24           N  
ANISOU 3521  N   HIS A 463     9034   7051   5662   -617  -1000    449       N  
ATOM   3522  CA  HIS A 463      42.047   8.442  42.432  1.00 57.32           C  
ANISOU 3522  CA  HIS A 463     9061   7011   5708   -637  -1071    506       C  
ATOM   3523  C   HIS A 463      41.300   7.607  41.410  1.00 60.61           C  
ANISOU 3523  C   HIS A 463     9571   7272   6184   -631  -1222    496       C  
ATOM   3524  O   HIS A 463      41.605   6.428  41.206  1.00 58.63           O  
ANISOU 3524  O   HIS A 463     9394   6935   5949   -606  -1295    505       O  
ATOM   3525  CB  HIS A 463      41.374   8.336  43.800  1.00 58.29           C  
ANISOU 3525  CB  HIS A 463     9052   7207   5888   -710  -1034    588       C  
ATOM   3526  CG  HIS A 463      41.263   6.936  44.300  1.00 58.79           C  
ANISOU 3526  CG  HIS A 463     9112   7215   6010   -727  -1083    677       C  
ATOM   3527  ND1 HIS A 463      40.118   6.191  44.162  1.00 59.57           N  
ANISOU 3527  ND1 HIS A 463     9184   7195   6254   -781  -1175    743       N  
ATOM   3528  CD2 HIS A 463      42.164   6.130  44.906  1.00 62.98           C  
ANISOU 3528  CD2 HIS A 463     9655   7778   6496   -692  -1056    719       C  
ATOM   3529  CE1 HIS A 463      40.311   4.983  44.660  1.00 62.89           C  
ANISOU 3529  CE1 HIS A 463     9599   7568   6727   -782  -1193    826       C  
ATOM   3530  NE2 HIS A 463      41.546   4.920  45.121  1.00 65.83           N  
ANISOU 3530  NE2 HIS A 463    10001   8038   6974   -725  -1119    816       N  
ATOM   3531  N   GLU A 464      40.321   8.218  40.759  1.00 63.65           N  
ANISOU 3531  N   GLU A 464     9956   7618   6612   -649  -1281    471       N  
ATOM   3532  CA  GLU A 464      39.534   7.531  39.736  1.00 68.10           C  
ANISOU 3532  CA  GLU A 464    10606   8032   7238   -638  -1460    438       C  
ATOM   3533  C   GLU A 464      40.367   6.913  38.585  1.00 70.60           C  
ANISOU 3533  C   GLU A 464    11113   8267   7444   -518  -1528    359       C  
ATOM   3534  O   GLU A 464      39.937   5.925  37.994  1.00 71.88           O  
ANISOU 3534  O   GLU A 464    11356   8294   7662   -504  -1693    323       O  
ATOM   3535  CB  GLU A 464      38.449   8.468  39.194  1.00 71.06           C  
ANISOU 3535  CB  GLU A 464    10945   8397   7656   -658  -1509    420       C  
ATOM   3536  CG  GLU A 464      37.442   7.833  38.244  1.00 78.80           C  
ANISOU 3536  CG  GLU A 464    11986   9226   8728   -656  -1728    380       C  
ATOM   3537  CD  GLU A 464      37.605   8.299  36.804  1.00 89.73           C  
ANISOU 3537  CD  GLU A 464    13535  10583   9974   -531  -1802    285       C  
ATOM   3538  OE1 GLU A 464      37.929   9.505  36.609  1.00101.06           O  
ANISOU 3538  OE1 GLU A 464    14970  12118  11311   -485  -1671    287       O  
ATOM   3539  OE2 GLU A 464      37.395   7.481  35.870  1.00 92.42           O  
ANISOU 3539  OE2 GLU A 464    14008  10801  10306   -469  -1989    210       O  
ATOM   3540  N   LYS A 465      41.551   7.452  38.286  1.00 69.54           N  
ANISOU 3540  N   LYS A 465    11046   8206   7172   -426  -1402    333       N  
ATOM   3541  CA  LYS A 465      42.335   6.947  37.154  1.00 74.03           C  
ANISOU 3541  CA  LYS A 465    11801   8704   7622   -287  -1437    271       C  
ATOM   3542  C   LYS A 465      43.019   5.619  37.516  1.00 77.76           C  
ANISOU 3542  C   LYS A 465    12313   9118   8113   -276  -1462    284       C  
ATOM   3543  O   LYS A 465      42.844   4.601  36.821  1.00 84.19           O  
ANISOU 3543  O   LYS A 465    13254   9801   8933   -225  -1604    230       O  
ATOM   3544  CB  LYS A 465      43.342   7.999  36.644  1.00 70.62           C  
ANISOU 3544  CB  LYS A 465    11413   8353   7066   -181  -1272    266       C  
ATOM   3545  N   THR A 466      43.784   5.631  38.605  1.00 76.47           N  
ANISOU 3545  N   THR A 466    12044   9048   7964   -318  -1334    348       N  
ATOM   3546  CA  THR A 466      44.446   4.433  39.155  1.00 74.16           C  
ANISOU 3546  CA  THR A 466    11758   8719   7699   -314  -1338    386       C  
ATOM   3547  C   THR A 466      43.694   4.066  40.413  1.00 71.43           C  
ANISOU 3547  C   THR A 466    11260   8398   7483   -441  -1356    472       C  
ATOM   3548  O   THR A 466      44.109   4.530  41.504  1.00 73.61           O  
ANISOU 3548  O   THR A 466    11419   8808   7741   -477  -1239    529       O  
ATOM   3549  CB  THR A 466      45.908   4.731  39.600  1.00 71.20           C  
ANISOU 3549  CB  THR A 466    11354   8449   7250   -258  -1179    413       C  
ATOM   3550  OG1 THR A 466      46.496   3.537  40.124  1.00 69.52           O  
ANISOU 3550  OG1 THR A 466    11147   8200   7069   -249  -1191    458       O  
ATOM   3551  CG2 THR A 466      45.973   5.797  40.697  1.00 62.94           C  
ANISOU 3551  CG2 THR A 466    10140   7555   6218   -334  -1071    449       C  
ATOM   3552  N   PRO A 467      42.578   3.295  40.289  1.00 66.13           N  
ANISOU 3552  N   PRO A 467    10582   7598   6945   -500  -1499    484       N  
ATOM   3553  CA  PRO A 467      41.752   3.032  41.487  1.00 64.93           C  
ANISOU 3553  CA  PRO A 467    10268   7468   6936   -613  -1486    598       C  
ATOM   3554  C   PRO A 467      42.347   1.912  42.314  1.00 66.88           C  
ANISOU 3554  C   PRO A 467    10486   7700   7225   -610  -1451    689       C  
ATOM   3555  O   PRO A 467      42.480   0.783  41.822  1.00 68.10           O  
ANISOU 3555  O   PRO A 467    10722   7704   7447   -581  -1548    671       O  
ATOM   3556  CB  PRO A 467      40.354   2.674  40.929  1.00 62.06           C  
ANISOU 3556  CB  PRO A 467     9890   6950   6740   -673  -1654    583       C  
ATOM   3557  CG  PRO A 467      40.480   2.696  39.443  1.00 62.87           C  
ANISOU 3557  CG  PRO A 467    10168   6958   6761   -583  -1779    442       C  
ATOM   3558  CD  PRO A 467      41.945   2.755  39.076  1.00 65.60           C  
ANISOU 3558  CD  PRO A 467    10640   7365   6919   -464  -1680    395       C  
ATOM   3559  N   VAL A 468      42.739   2.251  43.547  1.00 65.55           N  
ANISOU 3559  N   VAL A 468    10211   7689   7008   -627  -1316    776       N  
ATOM   3560  CA  VAL A 468      43.442   1.325  44.440  1.00 64.77           C  
ANISOU 3560  CA  VAL A 468    10082   7616   6914   -604  -1263    876       C  
ATOM   3561  C   VAL A 468      42.880   1.224  45.870  1.00 65.12           C  
ANISOU 3561  C   VAL A 468     9979   7753   7010   -653  -1181   1028       C  
ATOM   3562  O   VAL A 468      43.272   0.325  46.614  1.00 71.76           O  
ANISOU 3562  O   VAL A 468    10792   8599   7875   -628  -1145   1138       O  
ATOM   3563  CB  VAL A 468      44.933   1.705  44.550  1.00 62.79           C  
ANISOU 3563  CB  VAL A 468     9872   7486   6501   -521  -1175    831       C  
ATOM   3564  CG1 VAL A 468      45.618   1.529  43.207  1.00 58.24           C  
ANISOU 3564  CG1 VAL A 468     9446   6805   5876   -442  -1223    722       C  
ATOM   3565  CG2 VAL A 468      45.090   3.119  45.121  1.00 58.25           C  
ANISOU 3565  CG2 VAL A 468     9217   7091   5823   -532  -1079    799       C  
ATOM   3566  N   SER A 469      41.980   2.127  46.241  1.00 63.60           N  
ANISOU 3566  N   SER A 469     9700   7635   6831   -705  -1142   1043       N  
ATOM   3567  CA  SER A 469      41.390   2.155  47.560  1.00 65.80           C  
ANISOU 3567  CA  SER A 469     9852   8014   7135   -727  -1044   1188       C  
ATOM   3568  C   SER A 469      39.862   2.114  47.529  1.00 67.89           C  
ANISOU 3568  C   SER A 469    10024   8179   7593   -806  -1072   1266       C  
ATOM   3569  O   SER A 469      39.224   3.109  47.211  1.00 69.05           O  
ANISOU 3569  O   SER A 469    10145   8353   7738   -841  -1075   1202       O  
ATOM   3570  CB  SER A 469      41.807   3.414  48.295  1.00 64.57           C  
ANISOU 3570  CB  SER A 469     9661   8072   6800   -695   -938   1141       C  
ATOM   3571  OG  SER A 469      40.908   3.651  49.364  1.00 66.00           O  
ANISOU 3571  OG  SER A 469     9734   8339   7004   -709   -848   1260       O  
ATOM   3572  N   GLU A 470      39.291   0.977  47.917  1.00 69.25           N  
ANISOU 3572  N   GLU A 470    10128   8233   7950   -832  -1081   1418       N  
ATOM   3573  CA  GLU A 470      37.841   0.789  47.969  1.00 70.96           C  
ANISOU 3573  CA  GLU A 470    10223   8330   8407   -910  -1103   1524       C  
ATOM   3574  C   GLU A 470      37.090   1.853  48.777  1.00 70.73           C  
ANISOU 3574  C   GLU A 470    10087   8451   8334   -918   -971   1590       C  
ATOM   3575  O   GLU A 470      35.909   2.119  48.513  1.00 74.09           O  
ANISOU 3575  O   GLU A 470    10424   8791   8936   -984  -1003   1621       O  
ATOM   3576  CB  GLU A 470      37.501  -0.598  48.549  1.00 73.79           C  
ANISOU 3576  CB  GLU A 470    10497   8558   8982   -921  -1084   1721       C  
ATOM   3577  CG  GLU A 470      38.023  -1.787  47.736  1.00 76.26           C  
ANISOU 3577  CG  GLU A 470    10899   8672   9404   -920  -1227   1665       C  
ATOM   3578  N   LYS A 471      37.757   2.449  49.759  1.00 67.60           N  
ANISOU 3578  N   LYS A 471     9700   8274   7712   -845   -833   1604       N  
ATOM   3579  CA  LYS A 471      37.116   3.417  50.645  1.00 67.63           C  
ANISOU 3579  CA  LYS A 471     9617   8429   7648   -828   -696   1660       C  
ATOM   3580  C   LYS A 471      36.996   4.786  49.983  1.00 65.11           C  
ANISOU 3580  C   LYS A 471     9329   8159   7251   -855   -730   1482       C  
ATOM   3581  O   LYS A 471      35.968   5.464  50.101  1.00 64.30           O  
ANISOU 3581  O   LYS A 471     9142   8063   7225   -887   -683   1515       O  
ATOM   3582  CB  LYS A 471      37.909   3.542  51.947  1.00 70.00           C  
ANISOU 3582  CB  LYS A 471     9931   8946   7718   -720   -561   1717       C  
ATOM   3583  CG  LYS A 471      37.862   2.288  52.789  1.00 74.50           C  
ANISOU 3583  CG  LYS A 471    10454   9494   8360   -673   -487   1939       C  
ATOM   3584  CD  LYS A 471      38.652   2.453  54.073  1.00 78.82           C  
ANISOU 3584  CD  LYS A 471    11028  10274   8644   -542   -369   1988       C  
ATOM   3585  CE  LYS A 471      40.158   2.437  53.839  1.00 79.79           C  
ANISOU 3585  CE  LYS A 471    11261  10466   8592   -500   -454   1837       C  
ATOM   3586  NZ  LYS A 471      40.886   2.139  55.115  1.00 77.06           N  
ANISOU 3586  NZ  LYS A 471    10928  10307   8044   -366   -368   1933       N  
ATOM   3587  N   VAL A 472      38.053   5.194  49.292  1.00 60.59           N  
ANISOU 3587  N   VAL A 472     8868   7614   6538   -835   -797   1310       N  
ATOM   3588  CA  VAL A 472      38.007   6.413  48.504  1.00 59.15           C  
ANISOU 3588  CA  VAL A 472     8719   7449   6308   -855   -831   1153       C  
ATOM   3589  C   VAL A 472      36.944   6.242  47.437  1.00 60.03           C  
ANISOU 3589  C   VAL A 472     8813   7380   6616   -927   -949   1149       C  
ATOM   3590  O   VAL A 472      36.021   7.054  47.323  1.00 61.15           O  
ANISOU 3590  O   VAL A 472     8888   7524   6823   -962   -933   1146       O  
ATOM   3591  CB  VAL A 472      39.364   6.715  47.846  1.00 57.44           C  
ANISOU 3591  CB  VAL A 472     8618   7261   5945   -812   -874   1000       C  
ATOM   3592  CG1 VAL A 472      39.213   7.693  46.708  1.00 56.05           C  
ANISOU 3592  CG1 VAL A 472     8485   7040   5772   -830   -925    869       C  
ATOM   3593  CG2 VAL A 472      40.327   7.239  48.889  1.00 57.47           C  
ANISOU 3593  CG2 VAL A 472     8613   7452   5770   -747   -775    970       C  
ATOM   3594  N   THR A 473      37.043   5.149  46.691  1.00 60.21           N  
ANISOU 3594  N   THR A 473     8893   7241   6744   -943  -1078   1148       N  
ATOM   3595  CA  THR A 473      36.031   4.835  45.685  1.00 62.38           C  
ANISOU 3595  CA  THR A 473     9154   7329   7220  -1004  -1232   1131       C  
ATOM   3596  C   THR A 473      34.598   4.892  46.235  1.00 64.27           C  
ANISOU 3596  C   THR A 473     9224   7525   7670  -1069  -1195   1273       C  
ATOM   3597  O   THR A 473      33.710   5.452  45.592  1.00 62.21           O  
ANISOU 3597  O   THR A 473     8923   7201   7514  -1111  -1272   1234       O  
ATOM   3598  CB  THR A 473      36.270   3.453  45.052  1.00 61.33           C  
ANISOU 3598  CB  THR A 473     9091   7013   7200  -1006  -1378   1124       C  
ATOM   3599  OG1 THR A 473      37.623   3.374  44.602  1.00 59.95           O  
ANISOU 3599  OG1 THR A 473     9067   6881   6830   -931  -1385   1012       O  
ATOM   3600  CG2 THR A 473      35.329   3.247  43.861  1.00 58.88           C  
ANISOU 3600  CG2 THR A 473     8791   6510   7069  -1052  -1581   1051       C  
ATOM   3601  N   LYS A 474      34.380   4.310  47.410  1.00 66.60           N  
ANISOU 3601  N   LYS A 474     9417   7855   8032  -1066  -1072   1450       N  
ATOM   3602  CA  LYS A 474      33.051   4.343  48.041  1.00 72.60           C  
ANISOU 3602  CA  LYS A 474    10002   8580   9004  -1110   -994   1620       C  
ATOM   3603  C   LYS A 474      32.682   5.793  48.362  1.00 71.36           C  
ANISOU 3603  C   LYS A 474     9809   8578   8728  -1094   -881   1582       C  
ATOM   3604  O   LYS A 474      31.601   6.256  48.008  1.00 74.72           O  
ANISOU 3604  O   LYS A 474    10141   8934   9317  -1145   -914   1601       O  
ATOM   3605  CB  LYS A 474      33.032   3.465  49.312  1.00 77.25           C  
ANISOU 3605  CB  LYS A 474    10505   9201   9647  -1075   -843   1840       C  
ATOM   3606  CG  LYS A 474      31.706   3.380  50.068  1.00 79.18           C  
ANISOU 3606  CG  LYS A 474    10557   9406  10124  -1100   -720   2062       C  
ATOM   3607  CD  LYS A 474      30.968   2.064  49.864  1.00 84.76           C  
ANISOU 3607  CD  LYS A 474    11142   9862  11199  -1169   -803   2215       C  
ATOM   3608  CE  LYS A 474      30.030   1.756  51.030  1.00 88.19           C  
ANISOU 3608  CE  LYS A 474    11386  10299  11824  -1149   -596   2507       C  
ATOM   3609  NZ  LYS A 474      28.930   0.803  50.676  1.00 89.45           N  
ANISOU 3609  NZ  LYS A 474    11366  10178  12444  -1245   -688   2653       N  
ATOM   3610  N   CYS A 475      33.589   6.524  48.995  1.00 66.83           N  
ANISOU 3610  N   CYS A 475     9305   8203   7885  -1020   -761   1516       N  
ATOM   3611  CA  CYS A 475      33.280   7.888  49.376  1.00 68.46           C  
ANISOU 3611  CA  CYS A 475     9477   8546   7987   -997   -651   1469       C  
ATOM   3612  C   CYS A 475      33.126   8.805  48.182  1.00 66.64           C  
ANISOU 3612  C   CYS A 475     9290   8265   7766  -1035   -760   1310       C  
ATOM   3613  O   CYS A 475      32.377   9.780  48.251  1.00 71.26           O  
ANISOU 3613  O   CYS A 475     9805   8885   8386  -1045   -701   1307       O  
ATOM   3614  CB  CYS A 475      34.337   8.447  50.326  1.00 70.04           C  
ANISOU 3614  CB  CYS A 475     9742   8958   7913   -906   -528   1409       C  
ATOM   3615  SG  CYS A 475      34.158   7.856  52.018  1.00 77.45           S  
ANISOU 3615  SG  CYS A 475    10611  10024   8793   -819   -341   1619       S  
ATOM   3616  N   CYS A 476      33.846   8.533  47.101  1.00 64.27           N  
ANISOU 3616  N   CYS A 476     9109   7887   7423  -1040   -904   1185       N  
ATOM   3617  CA  CYS A 476      33.807   9.428  45.929  1.00 62.73           C  
ANISOU 3617  CA  CYS A 476     8976   7658   7203  -1047   -994   1044       C  
ATOM   3618  C   CYS A 476      32.576   9.190  45.085  1.00 62.90           C  
ANISOU 3618  C   CYS A 476     8937   7515   7448  -1107  -1138   1075       C  
ATOM   3619  O   CYS A 476      31.975  10.124  44.578  1.00 66.77           O  
ANISOU 3619  O   CYS A 476     9400   8003   7968  -1117  -1156   1032       O  
ATOM   3620  CB  CYS A 476      35.070   9.281  45.081  1.00 60.26           C  
ANISOU 3620  CB  CYS A 476     8822   7335   6741  -1000  -1070    910       C  
ATOM   3621  SG  CYS A 476      36.548   9.984  45.878  1.00 59.03           S  
ANISOU 3621  SG  CYS A 476     8715   7370   6345   -930   -921    835       S  
ATOM   3622  N   THR A 477      32.156   7.944  44.987  1.00 64.88           N  
ANISOU 3622  N   THR A 477     9152   7620   7878  -1147  -1243   1155       N  
ATOM   3623  CA  THR A 477      31.062   7.602  44.101  1.00 67.92           C  
ANISOU 3623  CA  THR A 477     9482   7826   8500  -1205  -1429   1159       C  
ATOM   3624  C   THR A 477      29.679   7.533  44.762  1.00 70.56           C  
ANISOU 3624  C   THR A 477     9604   8100   9104  -1270  -1377   1331       C  
ATOM   3625  O   THR A 477      28.672   7.480  44.060  1.00 70.43           O  
ANISOU 3625  O   THR A 477     9512   7944   9305  -1321  -1531   1333       O  
ATOM   3626  CB  THR A 477      31.347   6.261  43.409  1.00 66.24           C  
ANISOU 3626  CB  THR A 477     9349   7441   8376  -1213  -1619   1118       C  
ATOM   3627  OG1 THR A 477      31.449   5.251  44.399  1.00 66.53           O  
ANISOU 3627  OG1 THR A 477     9310   7454   8513  -1232  -1533   1263       O  
ATOM   3628  CG2 THR A 477      32.665   6.329  42.654  1.00 65.06           C  
ANISOU 3628  CG2 THR A 477     9410   7340   7970  -1133  -1662    957       C  
ATOM   3629  N   GLU A 478      29.614   7.519  46.086  1.00 75.00           N  
ANISOU 3629  N   GLU A 478    10070   8767   9658  -1257  -1166   1480       N  
ATOM   3630  CA  GLU A 478      28.340   7.221  46.749  1.00 82.98           C  
ANISOU 3630  CA  GLU A 478    10874   9701  10953  -1304  -1094   1683       C  
ATOM   3631  C   GLU A 478      27.411   8.393  46.687  1.00 82.52           C  
ANISOU 3631  C   GLU A 478    10718   9683  10953  -1316  -1042   1691       C  
ATOM   3632  O   GLU A 478      26.235   8.231  46.394  1.00 92.54           O  
ANISOU 3632  O   GLU A 478    11836  10811  12516  -1377  -1122   1778       O  
ATOM   3633  CB  GLU A 478      28.513   6.781  48.202  1.00 85.92           C  
ANISOU 3633  CB  GLU A 478    11181  10175  11289  -1258   -865   1867       C  
ATOM   3634  CG  GLU A 478      28.618   5.271  48.345  1.00 93.22           C  
ANISOU 3634  CG  GLU A 478    12074  10955  12393  -1283   -922   1982       C  
ATOM   3635  CD  GLU A 478      28.280   4.784  49.738  1.00 99.95           C  
ANISOU 3635  CD  GLU A 478    12796  11859  13320  -1240   -689   2239       C  
ATOM   3636  OE1 GLU A 478      28.427   5.568  50.700  1.00106.56           O  
ANISOU 3636  OE1 GLU A 478    13641  12903  13944  -1157   -479   2283       O  
ATOM   3637  OE2 GLU A 478      27.866   3.613  49.868  1.00103.47           O  
ANISOU 3637  OE2 GLU A 478    13136  12135  14043  -1280   -717   2398       O  
ATOM   3638  N   SER A 479      27.939   9.568  46.972  1.00 79.10           N  
ANISOU 3638  N   SER A 479    10360   9432  10262  -1256   -911   1602       N  
ATOM   3639  CA  SER A 479      27.166  10.788  46.870  1.00 77.93           C  
ANISOU 3639  CA  SER A 479    10136   9327  10148  -1256   -854   1591       C  
ATOM   3640  C   SER A 479      28.101  11.967  46.736  1.00 70.52           C  
ANISOU 3640  C   SER A 479     9334   8542   8917  -1196   -792   1420       C  
ATOM   3641  O   SER A 479      29.177  11.971  47.302  1.00 69.79           O  
ANISOU 3641  O   SER A 479     9340   8570   8606  -1144   -704   1366       O  
ATOM   3642  CB  SER A 479      26.295  10.960  48.111  1.00 80.38           C  
ANISOU 3642  CB  SER A 479    10278   9693  10569  -1237   -632   1787       C  
ATOM   3643  OG  SER A 479      25.668  12.230  48.137  1.00 87.73           O  
ANISOU 3643  OG  SER A 479    11149  10686  11499  -1220   -545   1768       O  
ATOM   3644  N   LEU A 480      27.680  12.964  45.983  1.00 66.68           N  
ANISOU 3644  N   LEU A 480     8843   8042   8452  -1203   -843   1342       N  
ATOM   3645  CA  LEU A 480      28.470  14.162  45.822  1.00 67.81           C  
ANISOU 3645  CA  LEU A 480     9087   8304   8372  -1149   -773   1197       C  
ATOM   3646  C   LEU A 480      28.415  15.052  47.059  1.00 66.87           C  
ANISOU 3646  C   LEU A 480     8908   8334   8164  -1102   -542   1225       C  
ATOM   3647  O   LEU A 480      29.415  15.636  47.438  1.00 67.70           O  
ANISOU 3647  O   LEU A 480     9102   8557   8064  -1050   -459   1115       O  
ATOM   3648  CB  LEU A 480      27.985  14.944  44.604  1.00 67.23           C  
ANISOU 3648  CB  LEU A 480     9022   8160   8361  -1159   -893   1125       C  
ATOM   3649  CG  LEU A 480      28.852  16.140  44.227  1.00 63.33           C  
ANISOU 3649  CG  LEU A 480     8633   7757   7673  -1102   -832    984       C  
ATOM   3650  CD1 LEU A 480      30.303  15.716  44.078  1.00 59.80           C  
ANISOU 3650  CD1 LEU A 480     8339   7352   7030  -1066   -852    885       C  
ATOM   3651  CD2 LEU A 480      28.308  16.729  42.933  1.00 63.74           C  
ANISOU 3651  CD2 LEU A 480     8698   7727   7793  -1097   -963    945       C  
ATOM   3652  N   VAL A 481      27.241  15.133  47.674  1.00 70.88           N  
ANISOU 3652  N   VAL A 481     9265   8827   8841  -1112   -444   1371       N  
ATOM   3653  CA  VAL A 481      26.994  16.018  48.824  1.00 72.66           C  
ANISOU 3653  CA  VAL A 481     9433   9185   8990  -1047   -219   1402       C  
ATOM   3654  C   VAL A 481      27.595  15.487  50.132  1.00 75.50           C  
ANISOU 3654  C   VAL A 481     9828   9672   9187   -978    -77   1454       C  
ATOM   3655  O   VAL A 481      28.124  16.257  50.928  1.00 77.37           O  
ANISOU 3655  O   VAL A 481    10117  10053   9226   -899     54   1370       O  
ATOM   3656  CB  VAL A 481      25.477  16.204  49.064  1.00 73.32           C  
ANISOU 3656  CB  VAL A 481     9333   9205   9321  -1065   -141   1570       C  
ATOM   3657  CG1 VAL A 481      24.738  16.381  47.752  1.00 74.97           C  
ANISOU 3657  CG1 VAL A 481     9486   9265   9736  -1137   -326   1556       C  
ATOM   3658  CG2 VAL A 481      24.886  15.006  49.789  1.00 78.63           C  
ANISOU 3658  CG2 VAL A 481     9896   9829  10150  -1073    -81   1783       C  
ATOM   3659  N   ASN A 482      27.502  14.173  50.344  1.00 77.49           N  
ANISOU 3659  N   ASN A 482    10051   9862   9529  -1000   -111   1591       N  
ATOM   3660  CA  ASN A 482      27.982  13.540  51.566  1.00 78.72           C  
ANISOU 3660  CA  ASN A 482    10233  10132   9545   -923     24   1679       C  
ATOM   3661  C   ASN A 482      29.463  13.126  51.501  1.00 78.49           C  
ANISOU 3661  C   ASN A 482    10361  10166   9295   -902    -59   1546       C  
ATOM   3662  O   ASN A 482      29.925  12.386  52.369  1.00 80.60           O  
ANISOU 3662  O   ASN A 482    10656  10509   9460   -842     11   1627       O  
ATOM   3663  CB  ASN A 482      27.136  12.294  51.902  1.00 81.91           C  
ANISOU 3663  CB  ASN A 482    10508  10428  10187   -949     54   1927       C  
ATOM   3664  CG  ASN A 482      25.655  12.604  52.129  1.00 83.34           C  
ANISOU 3664  CG  ASN A 482    10503  10545  10618   -959    165   2099       C  
ATOM   3665  OD1 ASN A 482      25.282  13.570  52.802  1.00 80.38           O  
ANISOU 3665  OD1 ASN A 482    10100  10283  10159   -882    340   2106       O  
ATOM   3666  ND2 ASN A 482      24.800  11.749  51.584  1.00 85.66           N  
ANISOU 3666  ND2 ASN A 482    10661  10645  11240  -1049     62   2239       N  
ATOM   3667  N   ARG A 483      30.208  13.580  50.490  1.00 74.72           N  
ANISOU 3667  N   ARG A 483     9982   9659   8751   -939   -198   1360       N  
ATOM   3668  CA  ARG A 483      31.634  13.232  50.386  1.00 71.49           C  
ANISOU 3668  CA  ARG A 483     9707   9301   8155   -915   -267   1241       C  
ATOM   3669  C   ARG A 483      32.431  13.640  51.593  1.00 69.60           C  
ANISOU 3669  C   ARG A 483     9516   9247   7681   -816   -141   1187       C  
ATOM   3670  O   ARG A 483      33.265  12.880  52.058  1.00 68.63           O  
ANISOU 3670  O   ARG A 483     9453   9180   7443   -777   -151   1201       O  
ATOM   3671  CB  ARG A 483      32.294  13.904  49.187  1.00 70.46           C  
ANISOU 3671  CB  ARG A 483     9663   9125   7984   -945   -387   1061       C  
ATOM   3672  CG  ARG A 483      32.331  13.076  47.929  1.00 70.30           C  
ANISOU 3672  CG  ARG A 483     9691   8948   8071  -1003   -568   1056       C  
ATOM   3673  CD  ARG A 483      32.754  13.925  46.747  1.00 68.49           C  
ANISOU 3673  CD  ARG A 483     9538   8684   7800  -1005   -648    909       C  
ATOM   3674  NE  ARG A 483      32.789  13.122  45.538  1.00 66.24           N  
ANISOU 3674  NE  ARG A 483     9324   8260   7583  -1031   -826    893       N  
ATOM   3675  CZ  ARG A 483      33.271  13.531  44.379  1.00 63.40           C  
ANISOU 3675  CZ  ARG A 483     9064   7859   7167  -1009   -911    786       C  
ATOM   3676  NH1 ARG A 483      33.749  14.765  44.249  1.00 61.46           N  
ANISOU 3676  NH1 ARG A 483     8838   7686   6830   -972   -826    698       N  
ATOM   3677  NH2 ARG A 483      33.259  12.694  43.341  1.00 63.89           N  
ANISOU 3677  NH2 ARG A 483     9206   7798   7271  -1011  -1079    769       N  
ATOM   3678  N   ARG A 484      32.228  14.863  52.070  1.00 70.86           N  
ANISOU 3678  N   ARG A 484     9656   9500   7767   -770    -38   1108       N  
ATOM   3679  CA  ARG A 484      33.032  15.349  53.195  1.00 72.90           C  
ANISOU 3679  CA  ARG A 484     9971   9934   7792   -664     49   1012       C  
ATOM   3680  C   ARG A 484      32.773  14.527  54.468  1.00 73.58           C  
ANISOU 3680  C   ARG A 484    10043  10123   7793   -571    168   1182       C  
ATOM   3681  O   ARG A 484      33.730  14.073  55.110  1.00 76.03           O  
ANISOU 3681  O   ARG A 484    10427  10536   7923   -501    157   1154       O  
ATOM   3682  CB  ARG A 484      32.834  16.848  53.439  1.00 73.60           C  
ANISOU 3682  CB  ARG A 484    10045  10085   7837   -626    125    875       C  
ATOM   3683  CG  ARG A 484      34.023  17.512  54.118  1.00 79.65           C  
ANISOU 3683  CG  ARG A 484    10889  10983   8391   -546    123    681       C  
ATOM   3684  CD  ARG A 484      34.012  17.425  55.646  1.00 78.86           C  
ANISOU 3684  CD  ARG A 484    10815  11057   8093   -405    238    711       C  
ATOM   3685  NE  ARG A 484      32.823  18.061  56.206  1.00 78.43           N  
ANISOU 3685  NE  ARG A 484    10698  11033   8067   -348    392    777       N  
ATOM   3686  CZ  ARG A 484      31.908  17.460  56.970  1.00 82.49           C  
ANISOU 3686  CZ  ARG A 484    11170  11594   8580   -277    533    988       C  
ATOM   3687  NH1 ARG A 484      32.034  16.186  57.337  1.00 82.45           N  
ANISOU 3687  NH1 ARG A 484    11175  11610   8542   -252    542   1159       N  
ATOM   3688  NH2 ARG A 484      30.855  18.149  57.394  1.00 82.53           N  
ANISOU 3688  NH2 ARG A 484    11115  11618   8627   -221    683   1041       N  
ATOM   3689  N   PRO A 485      31.490  14.310  54.825  1.00 71.76           N  
ANISOU 3689  N   PRO A 485     9708   9859   7698   -561    287   1374       N  
ATOM   3690  CA  PRO A 485      31.181  13.417  55.959  1.00 72.64           C  
ANISOU 3690  CA  PRO A 485     9794  10049   7757   -464    424   1584       C  
ATOM   3691  C   PRO A 485      31.690  11.979  55.791  1.00 70.58           C  
ANISOU 3691  C   PRO A 485     9553   9722   7542   -497    341   1697       C  
ATOM   3692  O   PRO A 485      32.274  11.434  56.718  1.00 70.41           O  
ANISOU 3692  O   PRO A 485     9586   9823   7343   -391    402   1757       O  
ATOM   3693  CB  PRO A 485      29.657  13.454  56.024  1.00 74.44           C  
ANISOU 3693  CB  PRO A 485     9876  10194   8212   -480    549   1780       C  
ATOM   3694  CG  PRO A 485      29.274  14.753  55.380  1.00 73.15           C  
ANISOU 3694  CG  PRO A 485     9690   9994   8108   -530    522   1626       C  
ATOM   3695  CD  PRO A 485      30.279  14.969  54.300  1.00 70.75           C  
ANISOU 3695  CD  PRO A 485     9475   9633   7774   -619    322   1416       C  
ATOM   3696  N   CYS A 486      31.484  11.390  54.615  1.00 69.79           N  
ANISOU 3696  N   CYS A 486     9417   9432   7669   -630    197   1715       N  
ATOM   3697  CA  CYS A 486      32.024  10.079  54.309  1.00 69.44           C  
ANISOU 3697  CA  CYS A 486     9401   9300   7683   -667     97   1786       C  
ATOM   3698  C   CYS A 486      33.498   9.991  54.639  1.00 68.70           C  
ANISOU 3698  C   CYS A 486     9440   9334   7330   -601     51   1654       C  
ATOM   3699  O   CYS A 486      33.934   9.045  55.278  1.00 77.87           O  
ANISOU 3699  O   CYS A 486    10622  10538   8425   -540     84   1769       O  
ATOM   3700  CB  CYS A 486      31.833   9.742  52.847  1.00 70.89           C  
ANISOU 3700  CB  CYS A 486     9573   9277   8085   -803    -93   1729       C  
ATOM   3701  SG  CYS A 486      32.147   8.007  52.427  1.00 79.45           S  
ANISOU 3701  SG  CYS A 486    10665  10199   9322   -854   -214   1842       S  
ATOM   3702  N   PHE A 487      34.274  10.973  54.221  1.00 68.14           N  
ANISOU 3702  N   PHE A 487     9445   9317   7130   -608    -23   1425       N  
ATOM   3703  CA  PHE A 487      35.719  10.949  54.472  1.00 69.58           C  
ANISOU 3703  CA  PHE A 487     9731   9604   7103   -553    -82   1290       C  
ATOM   3704  C   PHE A 487      36.052  11.184  55.937  1.00 71.67           C  
ANISOU 3704  C   PHE A 487    10025  10078   7129   -405     32   1301       C  
ATOM   3705  O   PHE A 487      36.938  10.539  56.487  1.00 73.49           O  
ANISOU 3705  O   PHE A 487    10311  10392   7219   -335     10   1318       O  
ATOM   3706  CB  PHE A 487      36.452  11.963  53.587  1.00 67.55           C  
ANISOU 3706  CB  PHE A 487     9524   9325   6817   -601   -183   1056       C  
ATOM   3707  CG  PHE A 487      36.779  11.427  52.225  1.00 68.68           C  
ANISOU 3707  CG  PHE A 487     9703   9304   7090   -694   -321   1025       C  
ATOM   3708  CD1 PHE A 487      37.780  10.472  52.070  1.00 68.45           C  
ANISOU 3708  CD1 PHE A 487     9737   9255   7014   -682   -396   1029       C  
ATOM   3709  CD2 PHE A 487      36.075  11.837  51.110  1.00 68.95           C  
ANISOU 3709  CD2 PHE A 487     9710   9205   7281   -776   -377    996       C  
ATOM   3710  CE1 PHE A 487      38.080   9.944  50.836  1.00 65.39           C  
ANISOU 3710  CE1 PHE A 487     9399   8719   6727   -744   -514    997       C  
ATOM   3711  CE2 PHE A 487      36.378  11.319  49.863  1.00 69.93           C  
ANISOU 3711  CE2 PHE A 487     9890   9189   7491   -832   -509    960       C  
ATOM   3712  CZ  PHE A 487      37.380  10.369  49.731  1.00 68.77           C  
ANISOU 3712  CZ  PHE A 487     9817   9024   7288   -813   -573    958       C  
ATOM   3713  N   SER A 488      35.341  12.111  56.562  1.00 72.82           N  
ANISOU 3713  N   SER A 488    10138  10310   7221   -346    148   1287       N  
ATOM   3714  CA  SER A 488      35.551  12.410  57.969  1.00 76.32           C  
ANISOU 3714  CA  SER A 488    10625  10959   7413   -179    257   1283       C  
ATOM   3715  C   SER A 488      35.385  11.151  58.819  1.00 81.15           C  
ANISOU 3715  C   SER A 488    11233  11627   7975    -84    353   1533       C  
ATOM   3716  O   SER A 488      36.159  10.915  59.739  1.00 82.19           O  
ANISOU 3716  O   SER A 488    11440  11918   7871     49    361   1520       O  
ATOM   3717  CB  SER A 488      34.552  13.465  58.435  1.00 76.35           C  
ANISOU 3717  CB  SER A 488    10587  11016   7404   -124    392   1269       C  
ATOM   3718  OG  SER A 488      34.809  14.709  57.835  1.00 75.96           O  
ANISOU 3718  OG  SER A 488    10547  10937   7377   -184    317   1033       O  
ATOM   3719  N   ALA A 489      34.373  10.348  58.484  1.00 85.69           N  
ANISOU 3719  N   ALA A 489    11712  12059   8789   -151    418   1762       N  
ATOM   3720  CA  ALA A 489      33.989   9.176  59.277  1.00 85.32           C  
ANISOU 3720  CA  ALA A 489    11626  12031   8760    -65    547   2046       C  
ATOM   3721  C   ALA A 489      34.921   7.977  59.101  1.00 83.58           C  
ANISOU 3721  C   ALA A 489    11449  11769   8540    -82    445   2099       C  
ATOM   3722  O   ALA A 489      34.847   7.026  59.870  1.00 87.55           O  
ANISOU 3722  O   ALA A 489    11937  12312   9015     14    550   2322       O  
ATOM   3723  CB  ALA A 489      32.555   8.774  58.958  1.00 84.92           C  
ANISOU 3723  CB  ALA A 489    11427  11814   9025   -141    647   2274       C  
ATOM   3724  N   LEU A 490      35.789   8.001  58.096  1.00 83.96           N  
ANISOU 3724  N   LEU A 490    11547  11729   8624   -192    256   1910       N  
ATOM   3725  CA  LEU A 490      36.739   6.899  57.910  1.00 85.80           C  
ANISOU 3725  CA  LEU A 490    11826  11920   8853   -199    162   1946       C  
ATOM   3726  C   LEU A 490      37.692   6.801  59.090  1.00 86.57           C  
ANISOU 3726  C   LEU A 490    12006  12238   8648    -30    197   1941       C  
ATOM   3727  O   LEU A 490      38.062   7.817  59.687  1.00 89.87           O  
ANISOU 3727  O   LEU A 490    12478  12827   8840     61    203   1779       O  
ATOM   3728  CB  LEU A 490      37.555   7.078  56.622  1.00 84.28           C  
ANISOU 3728  CB  LEU A 490    11684  11612   8728   -323    -29   1732       C  
ATOM   3729  CG  LEU A 490      36.843   7.017  55.269  1.00 84.07           C  
ANISOU 3729  CG  LEU A 490    11608  11359   8974   -479   -117   1712       C  
ATOM   3730  CD1 LEU A 490      37.921   6.951  54.203  1.00 84.29           C  
ANISOU 3730  CD1 LEU A 490    11719  11311   8998   -541   -280   1534       C  
ATOM   3731  CD2 LEU A 490      35.895   5.836  55.131  1.00 85.44           C  
ANISOU 3731  CD2 LEU A 490    11690  11365   9407   -530    -87   1947       C  
ATOM   3732  N   THR A 491      38.077   5.578  59.433  1.00 86.98           N  
ANISOU 3732  N   THR A 491    12065  12280   8703     21    212   2115       N  
ATOM   3733  CA  THR A 491      39.072   5.344  60.489  1.00 90.70           C  
ANISOU 3733  CA  THR A 491    12617  12955   8889    189    219   2121       C  
ATOM   3734  C   THR A 491      40.139   4.408  59.941  1.00 91.44           C  
ANISOU 3734  C   THR A 491    12744  12963   9038    141     86   2107       C  
ATOM   3735  O   THR A 491      39.910   3.753  58.919  1.00 87.97           O  
ANISOU 3735  O   THR A 491    12263  12305   8857      3     29   2150       O  
ATOM   3736  CB  THR A 491      38.429   4.702  61.723  1.00 91.06           C  
ANISOU 3736  CB  THR A 491    12640  13109   8848    356    421   2413       C  
ATOM   3737  OG1 THR A 491      37.773   3.497  61.315  1.00 92.26           O  
ANISOU 3737  OG1 THR A 491    12697  13057   9300    275    480   2668       O  
ATOM   3738  CG2 THR A 491      37.423   5.652  62.363  1.00 88.80           C  
ANISOU 3738  CG2 THR A 491    12335  12930   8477    438    575   2430       C  
ATOM   3739  N   PRO A 492      41.303   4.327  60.617  1.00 93.24           N  
ANISOU 3739  N   PRO A 492    13044  13356   9025    264     29   2043       N  
ATOM   3740  CA  PRO A 492      42.357   3.440  60.098  1.00 93.56           C  
ANISOU 3740  CA  PRO A 492    13109  13312   9126    226    -89   2035       C  
ATOM   3741  C   PRO A 492      41.880   1.996  60.026  1.00 98.37           C  
ANISOU 3741  C   PRO A 492    13669  13773   9934    209    -12   2317       C  
ATOM   3742  O   PRO A 492      41.053   1.588  60.837  1.00 99.34           O  
ANISOU 3742  O   PRO A 492    13749  13938  10056    297    149   2553       O  
ATOM   3743  CB  PRO A 492      43.491   3.577  61.122  1.00 90.91           C  
ANISOU 3743  CB  PRO A 492    12841  13209   8492    395   -138   1969       C  
ATOM   3744  CG  PRO A 492      43.152   4.777  61.952  1.00 92.69           C  
ANISOU 3744  CG  PRO A 492    13094  13626   8499    497    -94   1852       C  
ATOM   3745  CD  PRO A 492      41.661   4.919  61.918  1.00 91.97           C  
ANISOU 3745  CD  PRO A 492    12946  13461   8537    458     68   1995       C  
ATOM   3746  N   ASP A 493      42.387   1.231  59.063  1.00104.16           N  
ANISOU 3746  N   ASP A 493    14406  14324  10848    107   -116   2297       N  
ATOM   3747  CA  ASP A 493      41.955  -0.155  58.902  1.00109.76           C  
ANISOU 3747  CA  ASP A 493    15062  14854  11787     79    -65   2540       C  
ATOM   3748  C   ASP A 493      43.017  -1.170  59.316  1.00106.84           C  
ANISOU 3748  C   ASP A 493    14730  14522  11343    175    -87   2639       C  
ATOM   3749  O   ASP A 493      44.102  -1.203  58.749  1.00106.10           O  
ANISOU 3749  O   ASP A 493    14691  14408  11216    149   -218   2480       O  
ATOM   3750  CB  ASP A 493      41.488  -0.397  57.465  1.00116.82           C  
ANISOU 3750  CB  ASP A 493    15928  15474  12984   -105   -163   2465       C  
ATOM   3751  CG  ASP A 493      39.969  -0.326  57.330  1.00125.46           C  
ANISOU 3751  CG  ASP A 493    16922  16447  14300   -181    -79   2587       C  
ATOM   3752  OD1 ASP A 493      39.266  -0.999  58.120  1.00137.92           O  
ANISOU 3752  OD1 ASP A 493    18421  18016  15965   -118     68   2854       O  
ATOM   3753  OD2 ASP A 493      39.470   0.404  56.448  1.00126.80           O  
ANISOU 3753  OD2 ASP A 493    17082  16528  14567   -295   -152   2431       O  
ATOM   3754  N   GLU A 494      42.682  -1.999  60.303  1.00105.65           N  
ANISOU 3754  N   GLU A 494    14543  14422  11178    296     55   2920       N  
ATOM   3755  CA  GLU A 494      43.606  -3.014  60.838  1.00108.59           C  
ANISOU 3755  CA  GLU A 494    14943  14843  11475    412     57   3059       C  
ATOM   3756  C   GLU A 494      43.858  -4.132  59.824  1.00107.51           C  
ANISOU 3756  C   GLU A 494    14786  14433  11631    296    -22   3093       C  
ATOM   3757  O   GLU A 494      44.791  -4.928  59.980  1.00101.45           O  
ANISOU 3757  O   GLU A 494    14047  13668  10830    364    -55   3154       O  
ATOM   3758  CB  GLU A 494      43.081  -3.603  62.163  1.00112.11           C  
ANISOU 3758  CB  GLU A 494    15353  15410  11833    590    256   3384       C  
ATOM   3759  N   THR A 495      42.999  -4.199  58.809  1.00108.79           N  
ANISOU 3759  N   THR A 495    14899  14358  12078    132    -55   3054       N  
ATOM   3760  CA  THR A 495      43.212  -5.069  57.648  1.00111.78           C  
ANISOU 3760  CA  THR A 495    15282  14464  12723     14   -170   3007       C  
ATOM   3761  C   THR A 495      44.542  -4.774  56.926  1.00109.01           C  
ANISOU 3761  C   THR A 495    15034  14140  12244      1   -322   2755       C  
ATOM   3762  O   THR A 495      45.276  -5.693  56.547  1.00113.04           O  
ANISOU 3762  O   THR A 495    15575  14536  12840     10   -376   2776       O  
ATOM   3763  CB  THR A 495      42.046  -4.951  56.634  1.00109.88           C  
ANISOU 3763  CB  THR A 495    14985  13990  12772   -151   -219   2951       C  
ATOM   3764  OG1 THR A 495      42.388  -5.631  55.420  1.00112.75           O  
ANISOU 3764  OG1 THR A 495    15391  14113  13336   -246   -366   2837       O  
ATOM   3765  CG2 THR A 495      41.760  -3.502  56.288  1.00110.17           C  
ANISOU 3765  CG2 THR A 495    15050  14134  12676   -205   -261   2730       C  
ATOM   3766  N   TYR A 496      44.856  -3.491  56.779  1.00100.35           N  
ANISOU 3766  N   TYR A 496    13982  13191  10957    -10   -376   2532       N  
ATOM   3767  CA  TYR A 496      46.004  -3.046  55.995  1.00 92.52           C  
ANISOU 3767  CA  TYR A 496    13064  12205   9882    -34   -503   2294       C  
ATOM   3768  C   TYR A 496      47.339  -3.655  56.436  1.00 91.67           C  
ANISOU 3768  C   TYR A 496    12988  12183   9659     77   -529   2331       C  
ATOM   3769  O   TYR A 496      47.807  -3.434  57.559  1.00 92.32           O  
ANISOU 3769  O   TYR A 496    13065  12487   9527    202   -493   2385       O  
ATOM   3770  CB  TYR A 496      46.073  -1.520  56.026  1.00 87.31           C  
ANISOU 3770  CB  TYR A 496    12419  11707   9048    -46   -529   2087       C  
ATOM   3771  CG  TYR A 496      47.325  -0.952  55.443  1.00 85.38           C  
ANISOU 3771  CG  TYR A 496    12225  11499   8715    -47   -633   1872       C  
ATOM   3772  CD1 TYR A 496      47.614  -1.088  54.083  1.00 84.59           C  
ANISOU 3772  CD1 TYR A 496    12171  11212   8756   -132   -709   1752       C  
ATOM   3773  CD2 TYR A 496      48.227  -0.260  56.241  1.00 85.65           C  
ANISOU 3773  CD2 TYR A 496    12259  11750   8532     48   -656   1786       C  
ATOM   3774  CE1 TYR A 496      48.776  -0.562  53.540  1.00 81.50           C  
ANISOU 3774  CE1 TYR A 496    11816  10849   8303   -120   -775   1582       C  
ATOM   3775  CE2 TYR A 496      49.389   0.270  55.709  1.00 86.11           C  
ANISOU 3775  CE2 TYR A 496    12337  11825   8558     43   -746   1603       C  
ATOM   3776  CZ  TYR A 496      49.658   0.115  54.361  1.00 80.96           C  
ANISOU 3776  CZ  TYR A 496    11720  10983   8059    -40   -790   1515       C  
ATOM   3777  OH  TYR A 496      50.810   0.646  53.866  1.00 73.73           O  
ANISOU 3777  OH  TYR A 496    10810  10082   7124    -30   -849   1362       O  
ATOM   3778  N   VAL A 497      47.939  -4.429  55.537  1.00 88.71           N  
ANISOU 3778  N   VAL A 497    12651  11629   9426     40   -597   2297       N  
ATOM   3779  CA  VAL A 497      49.268  -4.969  55.756  1.00 87.82           C  
ANISOU 3779  CA  VAL A 497    12564  11570   9233    135   -631   2311       C  
ATOM   3780  C   VAL A 497      50.255  -3.856  55.434  1.00 86.87           C  
ANISOU 3780  C   VAL A 497    12472  11569   8965    139   -711   2075       C  
ATOM   3781  O   VAL A 497      50.283  -3.368  54.301  1.00 86.91           O  
ANISOU 3781  O   VAL A 497    12514  11459   9047     51   -763   1906       O  
ATOM   3782  CB  VAL A 497      49.565  -6.156  54.830  1.00 87.13           C  
ANISOU 3782  CB  VAL A 497    12513  11232   9361    101   -668   2345       C  
ATOM   3783  CG1 VAL A 497      50.919  -6.757  55.178  1.00 85.60           C  
ANISOU 3783  CG1 VAL A 497    12332  11103   9091    213   -684   2391       C  
ATOM   3784  CG2 VAL A 497      48.460  -7.199  54.915  1.00 88.32           C  
ANISOU 3784  CG2 VAL A 497    12619  11200   9739     63   -607   2548       C  
ATOM   3785  N   PRO A 498      51.061  -3.444  56.422  1.00 87.18           N  
ANISOU 3785  N   PRO A 498    12491  11835   8800    249   -726   2066       N  
ATOM   3786  CA  PRO A 498      51.984  -2.321  56.226  1.00 85.96           C  
ANISOU 3786  CA  PRO A 498    12333  11789   8540    250   -809   1844       C  
ATOM   3787  C   PRO A 498      53.016  -2.576  55.138  1.00 83.42           C  
ANISOU 3787  C   PRO A 498    12035  11327   8333    224   -864   1748       C  
ATOM   3788  O   PRO A 498      53.488  -3.695  54.993  1.00 80.28           O  
ANISOU 3788  O   PRO A 498    11654  10835   8015    266   -857   1861       O  
ATOM   3789  CB  PRO A 498      52.666  -2.176  57.584  1.00 87.68           C  
ANISOU 3789  CB  PRO A 498    12519  12251   8544    394   -835   1886       C  
ATOM   3790  CG  PRO A 498      52.474  -3.486  58.263  1.00 90.20           C  
ANISOU 3790  CG  PRO A 498    12840  12564   8868    483   -765   2147       C  
ATOM   3791  CD  PRO A 498      51.153  -4.000  57.780  1.00 89.85           C  
ANISOU 3791  CD  PRO A 498    12802  12335   9000    388   -673   2264       C  
ATOM   3792  N   LYS A 499      53.339  -1.530  54.383  1.00 80.77           N  
ANISOU 3792  N   LYS A 499    11700  10976   8012    165   -903   1550       N  
ATOM   3793  CA  LYS A 499      54.328  -1.603  53.317  1.00 78.78           C  
ANISOU 3793  CA  LYS A 499    11469  10603   7859    157   -930   1459       C  
ATOM   3794  C   LYS A 499      55.685  -2.079  53.852  1.00 80.73           C  
ANISOU 3794  C   LYS A 499    11672  10930   8072    263   -967   1505       C  
ATOM   3795  O   LYS A 499      56.093  -1.724  54.978  1.00 77.18           O  
ANISOU 3795  O   LYS A 499    11160  10675   7489    335  -1014   1509       O  
ATOM   3796  CB  LYS A 499      54.468  -0.220  52.682  1.00 78.28           C  
ANISOU 3796  CB  LYS A 499    11388  10552   7801     98   -947   1263       C  
ATOM   3797  CG  LYS A 499      55.143  -0.173  51.320  1.00 79.74           C  
ANISOU 3797  CG  LYS A 499    11614  10581   8103     83   -935   1180       C  
ATOM   3798  CD  LYS A 499      54.888   1.164  50.613  1.00 77.85           C  
ANISOU 3798  CD  LYS A 499    11366  10327   7884     16   -924   1024       C  
ATOM   3799  CE  LYS A 499      55.714   1.305  49.333  1.00 79.41           C  
ANISOU 3799  CE  LYS A 499    11598  10395   8178     36   -889    959       C  
ATOM   3800  NZ  LYS A 499      55.502   2.565  48.564  1.00 78.64           N  
ANISOU 3800  NZ  LYS A 499    11494  10271   8113    -13   -858    835       N  
ATOM   3801  N   ALA A 500      56.388  -2.881  53.054  1.00 80.68           N  
ANISOU 3801  N   ALA A 500    11699  10775   8180    286   -955   1536       N  
ATOM   3802  CA  ALA A 500      57.738  -3.341  53.435  1.00 83.22           C  
ANISOU 3802  CA  ALA A 500    11968  11152   8500    387   -987   1583       C  
ATOM   3803  C   ALA A 500      58.737  -2.173  53.461  1.00 81.13           C  
ANISOU 3803  C   ALA A 500    11613  10990   8221    399  -1044   1428       C  
ATOM   3804  O   ALA A 500      58.617  -1.215  52.689  1.00 80.83           O  
ANISOU 3804  O   ALA A 500    11576  10901   8233    330  -1029   1289       O  
ATOM   3805  CB  ALA A 500      58.221  -4.427  52.479  1.00 81.28           C  
ANISOU 3805  CB  ALA A 500    11784  10704   8393    412   -946   1643       C  
ATOM   3806  N   PHE A 501      59.720  -2.243  54.343  1.00 80.59           N  
ANISOU 3806  N   PHE A 501    11460  11060   8102    490  -1115   1455       N  
ATOM   3807  CA  PHE A 501      60.707  -1.175  54.409  1.00 80.90           C  
ANISOU 3807  CA  PHE A 501    11387  11176   8173    500  -1190   1307       C  
ATOM   3808  C   PHE A 501      61.456  -1.022  53.099  1.00 79.57           C  
ANISOU 3808  C   PHE A 501    11207  10837   8188    476  -1129   1251       C  
ATOM   3809  O   PHE A 501      61.816  -2.009  52.479  1.00 77.05           O  
ANISOU 3809  O   PHE A 501    10939  10388   7948    515  -1067   1348       O  
ATOM   3810  CB  PHE A 501      61.734  -1.421  55.496  1.00 79.58           C  
ANISOU 3810  CB  PHE A 501    11125  11164   7949    613  -1299   1349       C  
ATOM   3811  CG  PHE A 501      62.721  -0.305  55.636  1.00 79.41           C  
ANISOU 3811  CG  PHE A 501    10966  11211   7996    617  -1404   1186       C  
ATOM   3812  CD1 PHE A 501      63.993  -0.410  55.092  1.00 79.57           C  
ANISOU 3812  CD1 PHE A 501    10890  11146   8198    648  -1410   1183       C  
ATOM   3813  CD2 PHE A 501      62.374   0.863  56.309  1.00 81.20           C  
ANISOU 3813  CD2 PHE A 501    11149  11574   8129    592  -1494   1034       C  
ATOM   3814  CE1 PHE A 501      64.911   0.621  55.228  1.00 80.27           C  
ANISOU 3814  CE1 PHE A 501    10822  11275   8400    646  -1511   1041       C  
ATOM   3815  CE2 PHE A 501      63.285   1.900  56.450  1.00 82.77           C  
ANISOU 3815  CE2 PHE A 501    11205  11813   8431    590  -1608    870       C  
ATOM   3816  CZ  PHE A 501      64.558   1.779  55.908  1.00 81.56           C  
ANISOU 3816  CZ  PHE A 501    10938  11565   8487    612  -1619    878       C  
ATOM   3817  N   ASP A 502      61.714   0.227  52.720  1.00 80.95           N  
ANISOU 3817  N   ASP A 502    11311  11014   8432    425  -1141   1101       N  
ATOM   3818  CA  ASP A 502      62.457   0.541  51.512  1.00 79.91           C  
ANISOU 3818  CA  ASP A 502    11153  10734   8475    420  -1062   1059       C  
ATOM   3819  C   ASP A 502      63.369   1.757  51.732  1.00 79.58           C  
ANISOU 3819  C   ASP A 502    10939  10750   8548    414  -1126    935       C  
ATOM   3820  O   ASP A 502      62.920   2.899  51.705  1.00 73.83           O  
ANISOU 3820  O   ASP A 502    10178  10047   7826    344  -1140    811       O  
ATOM   3821  CB  ASP A 502      61.487   0.792  50.366  1.00 79.84           C  
ANISOU 3821  CB  ASP A 502    11270  10592   8475    349   -959   1022       C  
ATOM   3822  CG  ASP A 502      62.192   1.160  49.057  1.00 81.68           C  
ANISOU 3822  CG  ASP A 502    11497  10679   8860    369   -852    992       C  
ATOM   3823  OD1 ASP A 502      63.440   1.177  49.017  1.00 79.45           O  
ANISOU 3823  OD1 ASP A 502    11102  10383   8701    433   -843   1013       O  
ATOM   3824  OD2 ASP A 502      61.479   1.426  48.060  1.00 82.40           O  
ANISOU 3824  OD2 ASP A 502    11696  10667   8945    333   -774    957       O  
ATOM   3825  N   GLU A 503      64.659   1.471  51.901  1.00 83.58           N  
ANISOU 3825  N   GLU A 503    11327  11257   9171    489  -1163    974       N  
ATOM   3826  CA  GLU A 503      65.695   2.479  52.141  1.00 86.54           C  
ANISOU 3826  CA  GLU A 503    11504  11663   9713    491  -1243    871       C  
ATOM   3827  C   GLU A 503      65.632   3.685  51.201  1.00 84.75           C  
ANISOU 3827  C   GLU A 503    11230  11327   9642    419  -1153    771       C  
ATOM   3828  O   GLU A 503      65.855   4.809  51.629  1.00 90.43           O  
ANISOU 3828  O   GLU A 503    11813  12096  10449    378  -1243    640       O  
ATOM   3829  CB  GLU A 503      67.093   1.835  52.036  1.00 91.00           C  
ANISOU 3829  CB  GLU A 503    11956  12179  10441    583  -1243    966       C  
ATOM   3830  CG  GLU A 503      68.255   2.773  52.367  1.00 94.70           C  
ANISOU 3830  CG  GLU A 503    12184  12667  11129    589  -1349    872       C  
ATOM   3831  N   LYS A 504      65.332   3.454  49.927  1.00 80.49           N  
ANISOU 3831  N   LYS A 504    10806  10637   9137    415   -980    831       N  
ATOM   3832  CA  LYS A 504      65.362   4.514  48.928  1.00 77.42           C  
ANISOU 3832  CA  LYS A 504    10380  10138   8899    376   -866    773       C  
ATOM   3833  C   LYS A 504      64.367   5.636  49.258  1.00 79.17           C  
ANISOU 3833  C   LYS A 504    10605  10425   9053    277   -919    638       C  
ATOM   3834  O   LYS A 504      64.577   6.796  48.876  1.00 80.09           O  
ANISOU 3834  O   LYS A 504    10614  10487   9331    238   -881    561       O  
ATOM   3835  CB  LYS A 504      65.102   3.936  47.529  1.00 75.22           C  
ANISOU 3835  CB  LYS A 504    10269   9707   8605    420   -681    864       C  
ATOM   3836  CG  LYS A 504      65.997   2.735  47.163  1.00 76.46           C  
ANISOU 3836  CG  LYS A 504    10452   9789   8810    531   -614    995       C  
ATOM   3837  CD  LYS A 504      65.887   2.293  45.701  1.00 71.72           C  
ANISOU 3837  CD  LYS A 504    10018   9029   8204    603   -429   1061       C  
ATOM   3838  N   LEU A 505      63.310   5.302  49.997  1.00 77.93           N  
ANISOU 3838  N   LEU A 505    10556  10377   8676    244   -998    620       N  
ATOM   3839  CA  LEU A 505      62.274   6.272  50.348  1.00 77.94           C  
ANISOU 3839  CA  LEU A 505    10574  10444   8595    162  -1038    504       C  
ATOM   3840  C   LEU A 505      62.724   7.251  51.426  1.00 80.65           C  
ANISOU 3840  C   LEU A 505    10752  10901   8992    147  -1190    363       C  
ATOM   3841  O   LEU A 505      62.184   8.348  51.532  1.00 82.73           O  
ANISOU 3841  O   LEU A 505    10983  11179   9271     84  -1207    241       O  
ATOM   3842  CB  LEU A 505      60.997   5.556  50.815  1.00 78.41           C  
ANISOU 3842  CB  LEU A 505    10792  10578   8421    144  -1057    552       C  
ATOM   3843  CG  LEU A 505      60.331   4.585  49.819  1.00 77.60           C  
ANISOU 3843  CG  LEU A 505    10863  10354   8269    146   -944    664       C  
ATOM   3844  CD1 LEU A 505      58.974   4.126  50.344  1.00 70.28           C  
ANISOU 3844  CD1 LEU A 505    10047   9487   7169    108   -970    699       C  
ATOM   3845  CD2 LEU A 505      60.200   5.201  48.427  1.00 70.38           C  
ANISOU 3845  CD2 LEU A 505     9990   9294   7456    123   -821    636       C  
ATOM   3846  N   PHE A 506      63.716   6.862  52.219  1.00 81.01           N  
ANISOU 3846  N   PHE A 506    10691  11022   9068    212  -1311    369       N  
ATOM   3847  CA  PHE A 506      64.157   7.662  53.359  1.00 82.80           C  
ANISOU 3847  CA  PHE A 506    10772  11370   9319    219  -1501    217       C  
ATOM   3848  C   PHE A 506      65.545   8.272  53.184  1.00 83.08           C  
ANISOU 3848  C   PHE A 506    10582  11321   9661    228  -1555    160       C  
ATOM   3849  O   PHE A 506      66.009   9.011  54.053  1.00 83.86           O  
ANISOU 3849  O   PHE A 506    10539  11494   9831    231  -1736      8       O  
ATOM   3850  CB  PHE A 506      64.083   6.804  54.629  1.00 83.38           C  
ANISOU 3850  CB  PHE A 506    10898  11626   9154    301  -1640    254       C  
ATOM   3851  CG  PHE A 506      62.757   6.122  54.793  1.00 80.22           C  
ANISOU 3851  CG  PHE A 506    10695  11287   8498    297  -1566    346       C  
ATOM   3852  CD1 PHE A 506      61.690   6.797  55.362  1.00 80.51           C  
ANISOU 3852  CD1 PHE A 506    10791  11419   8379    264  -1594    250       C  
ATOM   3853  CD2 PHE A 506      62.558   4.839  54.320  1.00 77.15           C  
ANISOU 3853  CD2 PHE A 506    10422  10838   8052    325  -1459    528       C  
ATOM   3854  CE1 PHE A 506      60.455   6.194  55.487  1.00 77.84           C  
ANISOU 3854  CE1 PHE A 506    10609  11120   7846    258  -1512    352       C  
ATOM   3855  CE2 PHE A 506      61.323   4.234  54.427  1.00 77.14           C  
ANISOU 3855  CE2 PHE A 506    10576  10863   7871    310  -1392    616       C  
ATOM   3856  CZ  PHE A 506      60.269   4.914  55.013  1.00 76.49           C  
ANISOU 3856  CZ  PHE A 506    10536  10879   7648    275  -1415    536       C  
ATOM   3857  N   THR A 507      66.191   7.969  52.062  1.00 85.03           N  
ANISOU 3857  N   THR A 507    10797  11410  10099    242  -1398    278       N  
ATOM   3858  CA  THR A 507      67.462   8.582  51.700  1.00 87.88           C  
ANISOU 3858  CA  THR A 507    10931  11657  10804    249  -1396    259       C  
ATOM   3859  C   THR A 507      67.206   9.995  51.211  1.00 85.98           C  
ANISOU 3859  C   THR A 507    10602  11318  10747    166  -1339    148       C  
ATOM   3860  O   THR A 507      66.318  10.211  50.405  1.00 82.38           O  
ANISOU 3860  O   THR A 507    10282  10803  10217    127  -1183    180       O  
ATOM   3861  CB  THR A 507      68.181   7.818  50.560  1.00 86.94           C  
ANISOU 3861  CB  THR A 507    10819  11392  10823    311  -1201    446       C  
ATOM   3862  OG1 THR A 507      68.147   6.403  50.804  1.00 86.61           O  
ANISOU 3862  OG1 THR A 507    10911  11414  10581    383  -1208    568       O  
ATOM   3863  CG2 THR A 507      69.637   8.292  50.437  1.00 88.05           C  
ANISOU 3863  CG2 THR A 507    10688  11432  11334    338  -1219    453       C  
ATOM   3864  N   PHE A 508      67.981  10.950  51.708  1.00 94.12           N  
ANISOU 3864  N   PHE A 508    11401  12326  12033    141  -1478     15       N  
ATOM   3865  CA  PHE A 508      67.918  12.319  51.211  1.00101.80           C  
ANISOU 3865  CA  PHE A 508    12251  13172  13258     66  -1415    -78       C  
ATOM   3866  C   PHE A 508      69.266  12.708  50.638  1.00103.37           C  
ANISOU 3866  C   PHE A 508    12193  13198  13883     82  -1352    -17       C  
ATOM   3867  O   PHE A 508      70.298  12.376  51.211  1.00103.43           O  
ANISOU 3867  O   PHE A 508    12043  13226  14029    125  -1496    -22       O  
ATOM   3868  CB  PHE A 508      67.522  13.278  52.329  1.00107.10           C  
ANISOU 3868  CB  PHE A 508    12860  13940  13894     14  -1639   -316       C  
ATOM   3869  CG  PHE A 508      66.150  13.027  52.880  1.00109.40           C  
ANISOU 3869  CG  PHE A 508    13386  14391  13789      5  -1671   -365       C  
ATOM   3870  CD1 PHE A 508      65.968  12.618  54.193  1.00113.45           C  
ANISOU 3870  CD1 PHE A 508    13957  15100  14047     57  -1882   -456       C  
ATOM   3871  CD2 PHE A 508      65.036  13.190  52.077  1.00111.90           C  
ANISOU 3871  CD2 PHE A 508    13864  14661  13991    -41  -1483   -307       C  
ATOM   3872  CE1 PHE A 508      64.702  12.386  54.701  1.00115.06           C  
ANISOU 3872  CE1 PHE A 508    14365  15445  13906     61  -1883   -475       C  
ATOM   3873  CE2 PHE A 508      63.766  12.960  52.576  1.00114.41           C  
ANISOU 3873  CE2 PHE A 508    14376  15113  13983    -51  -1504   -337       C  
ATOM   3874  CZ  PHE A 508      63.598  12.557  53.890  1.00114.96           C  
ANISOU 3874  CZ  PHE A 508    14492  15371  13817      0  -1692   -413       C  
ATOM   3875  N   HIS A 509      69.246  13.402  49.504  1.00107.06           N  
ANISOU 3875  N   HIS A 509    12618  13498  14564     58  -1131     56       N  
ATOM   3876  CA  HIS A 509      70.469  13.805  48.815  1.00116.46           C  
ANISOU 3876  CA  HIS A 509    13562  14501  16185     84  -1011    157       C  
ATOM   3877  C   HIS A 509      70.719  15.306  48.956  1.00118.33           C  
ANISOU 3877  C   HIS A 509    13554  14619  16786      1  -1070     17       C  
ATOM   3878  O   HIS A 509      69.793  16.088  49.160  1.00118.56           O  
ANISOU 3878  O   HIS A 509    13651  14676  16721    -69  -1110   -118       O  
ATOM   3879  CB  HIS A 509      70.402  13.418  47.327  1.00120.65           C  
ANISOU 3879  CB  HIS A 509    14218  14913  16711    153   -679    384       C  
ATOM   3880  CG  HIS A 509      71.040  12.100  47.003  1.00125.24           C  
ANISOU 3880  CG  HIS A 509    14868  15502  17216    262   -597    555       C  
ATOM   3881  ND1 HIS A 509      72.236  11.999  46.321  1.00128.23           N  
ANISOU 3881  ND1 HIS A 509    15074  15736  17913    342   -436    716       N  
ATOM   3882  CD2 HIS A 509      70.643  10.829  47.250  1.00124.20           C  
ANISOU 3882  CD2 HIS A 509    14954  15492  16743    310   -639    598       C  
ATOM   3883  CE1 HIS A 509      72.549  10.726  46.167  1.00127.58           C  
ANISOU 3883  CE1 HIS A 509    15110  15691  17674    438   -389    840       C  
ATOM   3884  NE2 HIS A 509      71.600   9.995  46.723  1.00129.76           N  
ANISOU 3884  NE2 HIS A 509    15621  16124  17557    416   -515    769       N  
ATOM   3885  N   ALA A 510      71.978  15.705  48.810  1.00118.91           N  
ANISOU 3885  N   ALA A 510    13332  14542  17306     12  -1066     60       N  
ATOM   3886  CA  ALA A 510      72.365  17.117  48.915  1.00118.18           C  
ANISOU 3886  CA  ALA A 510    12962  14295  17646    -67  -1124    -62       C  
ATOM   3887  C   ALA A 510      71.544  18.041  48.013  1.00116.28           C  
ANISOU 3887  C   ALA A 510    12788  13945  17447   -108   -894    -24       C  
ATOM   3888  O   ALA A 510      71.445  19.237  48.278  1.00109.85           O  
ANISOU 3888  O   ALA A 510    11816  13041  16883   -189   -973   -173       O  
ATOM   3889  CB  ALA A 510      73.844  17.285  48.615  1.00121.54           C  
ANISOU 3889  CB  ALA A 510    13055  14538  18587    -36  -1079     50       C  
ATOM   3890  N   ASP A 511      70.975  17.482  46.945  1.00116.16           N  
ANISOU 3890  N   ASP A 511    13007  13934  17194    -44   -620    170       N  
ATOM   3891  CA  ASP A 511      70.043  18.196  46.073  1.00115.32           C  
ANISOU 3891  CA  ASP A 511    13022  13761  17034    -63   -410    217       C  
ATOM   3892  C   ASP A 511      68.932  18.894  46.855  1.00114.85           C  
ANISOU 3892  C   ASP A 511    13046  13799  16794   -163   -590    -14       C  
ATOM   3893  O   ASP A 511      68.398  19.906  46.404  1.00111.66           O  
ANISOU 3893  O   ASP A 511    12620  13300  16507   -207   -481    -31       O  
ATOM   3894  CB  ASP A 511      69.419  17.220  45.065  1.00113.63           C  
ANISOU 3894  CB  ASP A 511    13115  13600  16459     32   -182    406       C  
ATOM   3895  CG  ASP A 511      68.248  17.826  44.302  1.00111.14           C  
ANISOU 3895  CG  ASP A 511    12973  13264  15990     17    -21    427       C  
ATOM   3896  N   ILE A 512      68.583  18.332  48.012  1.00114.23           N  
ANISOU 3896  N   ILE A 512    13069  13909  16424   -185   -850   -175       N  
ATOM   3897  CA  ILE A 512      67.556  18.893  48.893  1.00111.75           C  
ANISOU 3897  CA  ILE A 512    12844  13709  15905   -257  -1030   -397       C  
ATOM   3898  C   ILE A 512      67.772  20.368  49.271  1.00113.75           C  
ANISOU 3898  C   ILE A 512    12856  13836  16528   -337  -1133   -582       C  
ATOM   3899  O   ILE A 512      66.819  21.149  49.249  1.00114.68           O  
ANISOU 3899  O   ILE A 512    13047  13948  16578   -388  -1106   -673       O  
ATOM   3900  CB  ILE A 512      67.399  18.038  50.180  1.00111.50           C  
ANISOU 3900  CB  ILE A 512    12923  13901  15543   -236  -1295   -524       C  
ATOM   3901  CG1 ILE A 512      66.120  18.416  50.927  1.00111.03           C  
ANISOU 3901  CG1 ILE A 512    13026  13980  15179   -279  -1410   -699       C  
ATOM   3902  CG2 ILE A 512      68.612  18.169  51.097  1.00114.12           C  
ANISOU 3902  CG2 ILE A 512    13003  14223  16133   -229  -1546   -651       C  
ATOM   3903  CD1 ILE A 512      65.727  17.408  51.984  1.00109.95           C  
ANISOU 3903  CD1 ILE A 512    13062  14073  14640   -230  -1587   -750       C  
ATOM   3904  N   CYS A 513      69.005  20.757  49.596  1.00113.82           N  
ANISOU 3904  N   CYS A 513    12570  13728  16950   -347  -1254   -638       N  
ATOM   3905  CA  CYS A 513      69.280  22.134  50.023  1.00114.88           C  
ANISOU 3905  CA  CYS A 513    12452  13718  17479   -425  -1388   -837       C  
ATOM   3906  C   CYS A 513      69.050  23.164  48.909  1.00116.00           C  
ANISOU 3906  C   CYS A 513    12508  13646  17921   -461  -1111   -720       C  
ATOM   3907  O   CYS A 513      68.871  24.345  49.193  1.00115.39           O  
ANISOU 3907  O   CYS A 513    12292  13460  18092   -532  -1188   -887       O  
ATOM   3908  CB  CYS A 513      70.704  22.272  50.564  1.00116.12           C  
ANISOU 3908  CB  CYS A 513    12288  13775  18058   -428  -1590   -913       C  
ATOM   3909  SG  CYS A 513      71.258  20.920  51.634  1.00115.61           S  
ANISOU 3909  SG  CYS A 513    12291  13938  17696   -353  -1866   -966       S  
ATOM   3910  N   THR A 514      69.064  22.715  47.655  1.00118.95           N  
ANISOU 3910  N   THR A 514    12968  13959  18268   -397   -792   -435       N  
ATOM   3911  CA  THR A 514      68.759  23.568  46.491  1.00122.72           C  
ANISOU 3911  CA  THR A 514    13413  14260  18955   -396   -493   -280       C  
ATOM   3912  C   THR A 514      67.255  23.847  46.314  1.00118.13           C  
ANISOU 3912  C   THR A 514    13094  13775  18014   -421   -431   -327       C  
ATOM   3913  O   THR A 514      66.876  24.883  45.755  1.00117.76           O  
ANISOU 3913  O   THR A 514    12984  13591  18167   -449   -282   -298       O  
ATOM   3914  CB  THR A 514      69.313  22.941  45.181  1.00126.63           C  
ANISOU 3914  CB  THR A 514    13935  14673  19505   -283   -167     48       C  
ATOM   3915  OG1 THR A 514      70.742  23.052  45.162  1.00126.92           O  
ANISOU 3915  OG1 THR A 514    13654  14549  20019   -265   -161    125       O  
ATOM   3916  CG2 THR A 514      68.742  23.621  43.929  1.00126.65           C  
ANISOU 3916  CG2 THR A 514    14003  14555  19562   -244    156    231       C  
ATOM   3917  N   LEU A 515      66.404  22.935  46.779  1.00114.57           N  
ANISOU 3917  N   LEU A 515    12922  13548  17060   -408   -536   -385       N  
ATOM   3918  CA  LEU A 515      64.959  23.057  46.556  1.00108.71           C  
ANISOU 3918  CA  LEU A 515    12431  12900  15975   -424   -468   -401       C  
ATOM   3919  C   LEU A 515      64.342  24.239  47.324  1.00104.66           C  
ANISOU 3919  C   LEU A 515    11844  12370  15553   -513   -615   -642       C  
ATOM   3920  O   LEU A 515      64.704  24.497  48.479  1.00103.27           O  
ANISOU 3920  O   LEU A 515    11548  12232  15457   -553   -877   -869       O  
ATOM   3921  CB  LEU A 515      64.253  21.752  46.937  1.00103.99           C  
ANISOU 3921  CB  LEU A 515    12117  12529  14866   -390   -552   -398       C  
ATOM   3922  N   PRO A 516      63.430  24.981  46.675  1.00103.74           N  
ANISOU 3922  N   PRO A 516    11799  12192  15426   -531   -451   -597       N  
ATOM   3923  CA  PRO A 516      62.619  26.008  47.361  1.00105.87           C  
ANISOU 3923  CA  PRO A 516    12052  12464  15710   -604   -569   -816       C  
ATOM   3924  C   PRO A 516      61.723  25.459  48.478  1.00106.20           C  
ANISOU 3924  C   PRO A 516    12297  12740  15312   -614   -780   -994       C  
ATOM   3925  O   PRO A 516      61.319  24.293  48.427  1.00105.44           O  
ANISOU 3925  O   PRO A 516    12413  12803  14846   -570   -766   -894       O  
ATOM   3926  CB  PRO A 516      61.757  26.585  46.234  1.00103.58           C  
ANISOU 3926  CB  PRO A 516    11851  12089  15417   -594   -308   -659       C  
ATOM   3927  CG  PRO A 516      62.557  26.363  44.995  1.00104.74           C  
ANISOU 3927  CG  PRO A 516    11930  12102  15766   -521    -60   -389       C  
ATOM   3928  CD  PRO A 516      63.337  25.095  45.208  1.00103.08           C  
ANISOU 3928  CD  PRO A 516    11759  11990  15418   -471   -135   -334       C  
ATOM   3929  N   ASP A 517      61.397  26.311  49.453  1.00105.69           N  
ANISOU 3929  N   ASP A 517    12170  12688  15301   -661   -960  -1248       N  
ATOM   3930  CA  ASP A 517      60.633  25.915  50.653  1.00106.29           C  
ANISOU 3930  CA  ASP A 517    12416  12984  14985   -649  -1163  -1430       C  
ATOM   3931  C   ASP A 517      59.464  24.950  50.406  1.00105.52           C  
ANISOU 3931  C   ASP A 517    12607  13061  14426   -617  -1058  -1289       C  
ATOM   3932  O   ASP A 517      59.234  24.025  51.197  1.00101.87           O  
ANISOU 3932  O   ASP A 517    12283  12790  13634   -578  -1186  -1324       O  
ATOM   3933  CB  ASP A 517      60.076  27.151  51.361  1.00108.96           C  
ANISOU 3933  CB  ASP A 517    12696  13284  15420   -689  -1272  -1680       C  
ATOM   3934  CG  ASP A 517      61.153  28.022  51.948  1.00113.99           C  
ANISOU 3934  CG  ASP A 517    13062  13775  16474   -719  -1463  -1894       C  
ATOM   3935  OD1 ASP A 517      62.281  27.996  51.413  1.00123.51           O  
ANISOU 3935  OD1 ASP A 517    14072  14832  18025   -729  -1421  -1790       O  
ATOM   3936  OD2 ASP A 517      60.868  28.735  52.934  1.00111.72           O  
ANISOU 3936  OD2 ASP A 517    12754  13513  16182   -724  -1655  -2167       O  
ATOM   3937  N   THR A 518      58.711  25.181  49.333  1.00 99.75           N  
ANISOU 3937  N   THR A 518    11958  12259  13683   -629   -835  -1128       N  
ATOM   3938  CA  THR A 518      57.554  24.353  49.050  1.00 96.10           C  
ANISOU 3938  CA  THR A 518    11747  11934  12833   -607   -753  -1006       C  
ATOM   3939  C   THR A 518      57.998  22.936  48.654  1.00 92.08           C  
ANISOU 3939  C   THR A 518    11343  11494  12150   -555   -720   -832       C  
ATOM   3940  O   THR A 518      57.499  21.960  49.213  1.00 90.35           O  
ANISOU 3940  O   THR A 518    11281  11439  11609   -532   -800   -826       O  
ATOM   3941  CB  THR A 518      56.610  25.012  48.010  1.00 96.36           C  
ANISOU 3941  CB  THR A 518    11837  11873  12902   -624   -550   -895       C  
ATOM   3942  OG1 THR A 518      57.305  25.249  46.785  1.00100.59           O  
ANISOU 3942  OG1 THR A 518    12280  12240  13698   -601   -366   -722       O  
ATOM   3943  CG2 THR A 518      56.078  26.353  48.555  1.00 91.56           C  
ANISOU 3943  CG2 THR A 518    11139  11210  12441   -672   -595  -1082       C  
ATOM   3944  N   GLU A 519      58.948  22.818  47.732  1.00 88.95           N  
ANISOU 3944  N   GLU A 519    10853  10967  11976   -527   -597   -686       N  
ATOM   3945  CA  GLU A 519      59.450  21.499  47.332  1.00 87.79           C  
ANISOU 3945  CA  GLU A 519    10801  10870  11686   -466   -560   -528       C  
ATOM   3946  C   GLU A 519      60.255  20.847  48.450  1.00 86.99           C  
ANISOU 3946  C   GLU A 519    10637  10872  11542   -452   -767   -628       C  
ATOM   3947  O   GLU A 519      60.378  19.625  48.501  1.00 89.90           O  
ANISOU 3947  O   GLU A 519    11124  11335  11699   -405   -787   -535       O  
ATOM   3948  CB  GLU A 519      60.293  21.594  46.060  1.00 93.71           C  
ANISOU 3948  CB  GLU A 519    11466  11452  12688   -416   -355   -341       C  
ATOM   3949  CG  GLU A 519      59.508  22.020  44.822  1.00 99.44           C  
ANISOU 3949  CG  GLU A 519    12295  12097  13391   -393   -137   -202       C  
ATOM   3950  CD  GLU A 519      60.363  22.769  43.797  1.00105.99           C  
ANISOU 3950  CD  GLU A 519    12960  12730  14582   -348     67    -64       C  
ATOM   3951  OE1 GLU A 519      61.347  22.186  43.272  1.00101.24           O  
ANISOU 3951  OE1 GLU A 519    12318  12075  14073   -274    159     74       O  
ATOM   3952  OE2 GLU A 519      60.037  23.945  43.510  1.00109.16           O  
ANISOU 3952  OE2 GLU A 519    13269  13026  15182   -378    152    -81       O  
ATOM   3953  N   LYS A 520      60.826  21.656  49.337  1.00 86.77           N  
ANISOU 3953  N   LYS A 520    10423  10820  11725   -484   -931   -820       N  
ATOM   3954  CA  LYS A 520      61.510  21.126  50.525  1.00 86.91           C  
ANISOU 3954  CA  LYS A 520    10388  10957  11676   -458  -1167   -945       C  
ATOM   3955  C   LYS A 520      60.506  20.381  51.402  1.00 83.42           C  
ANISOU 3955  C   LYS A 520    10165  10735  10798   -432  -1268   -993       C  
ATOM   3956  O   LYS A 520      60.714  19.223  51.766  1.00 84.36           O  
ANISOU 3956  O   LYS A 520    10373  10974  10705   -380  -1328   -922       O  
ATOM   3957  CB  LYS A 520      62.163  22.249  51.350  1.00 89.52           C  
ANISOU 3957  CB  LYS A 520    10491  11219  12305   -492  -1357  -1184       C  
ATOM   3958  CG  LYS A 520      63.682  22.307  51.322  1.00 90.13           C  
ANISOU 3958  CG  LYS A 520    10318  11174  12752   -485  -1430  -1183       C  
ATOM   3959  CD  LYS A 520      64.179  23.432  52.224  1.00 92.53           C  
ANISOU 3959  CD  LYS A 520    10406  11409  13343   -523  -1661  -1457       C  
ATOM   3960  CE  LYS A 520      65.564  23.940  51.836  1.00 93.81           C  
ANISOU 3960  CE  LYS A 520    10255  11352  14037   -547  -1666  -1435       C  
ATOM   3961  NZ  LYS A 520      65.664  25.423  51.992  1.00 92.55           N  
ANISOU 3961  NZ  LYS A 520     9884  11009  14273   -616  -1733  -1625       N  
ATOM   3962  N   GLN A 521      59.421  21.071  51.737  1.00 79.03           N  
ANISOU 3962  N   GLN A 521     9682  10220  10128   -462  -1272  -1101       N  
ATOM   3963  CA  GLN A 521      58.337  20.487  52.521  1.00 77.01           C  
ANISOU 3963  CA  GLN A 521     9622  10156   9482   -433  -1329  -1124       C  
ATOM   3964  C   GLN A 521      57.719  19.277  51.803  1.00 73.38           C  
ANISOU 3964  C   GLN A 521     9349   9740   8793   -417  -1184   -895       C  
ATOM   3965  O   GLN A 521      57.429  18.264  52.430  1.00 70.66           O  
ANISOU 3965  O   GLN A 521     9126   9544   8179   -371  -1246   -849       O  
ATOM   3966  CB  GLN A 521      57.268  21.539  52.812  1.00 76.06           C  
ANISOU 3966  CB  GLN A 521     9531  10039   9329   -466  -1315  -1256       C  
ATOM   3967  CG  GLN A 521      57.722  22.627  53.768  1.00 78.07           C  
ANISOU 3967  CG  GLN A 521     9639  10279   9746   -466  -1499  -1525       C  
ATOM   3968  CD  GLN A 521      56.858  23.873  53.724  1.00 80.62           C  
ANISOU 3968  CD  GLN A 521     9947  10529  10156   -509  -1443  -1643       C  
ATOM   3969  OE1 GLN A 521      55.878  23.948  52.973  1.00 77.63           O  
ANISOU 3969  OE1 GLN A 521     9665  10119   9714   -540  -1263  -1513       O  
ATOM   3970  NE2 GLN A 521      57.232  24.879  54.529  1.00 83.37           N  
ANISOU 3970  NE2 GLN A 521    10168  10841  10666   -506  -1611  -1900       N  
ATOM   3971  N   ILE A 522      57.548  19.372  50.492  1.00 71.36           N  
ANISOU 3971  N   ILE A 522     9112   9349   8652   -443   -997   -751       N  
ATOM   3972  CA  ILE A 522      57.048  18.241  49.742  1.00 73.34           C  
ANISOU 3972  CA  ILE A 522     9535   9618   8712   -421   -886   -558       C  
ATOM   3973  C   ILE A 522      57.902  17.015  50.050  1.00 74.79           C  
ANISOU 3973  C   ILE A 522     9735   9865   8817   -364   -956   -486       C  
ATOM   3974  O   ILE A 522      57.363  15.965  50.392  1.00 72.33           O  
ANISOU 3974  O   ILE A 522     9566   9661   8254   -338   -982   -414       O  
ATOM   3975  CB  ILE A 522      56.996  18.491  48.212  1.00 75.66           C  
ANISOU 3975  CB  ILE A 522     9846   9753   9147   -425   -688   -419       C  
ATOM   3976  CG1 ILE A 522      55.826  19.426  47.872  1.00 78.60           C  
ANISOU 3976  CG1 ILE A 522    10259  10092   9515   -470   -612   -449       C  
ATOM   3977  CG2 ILE A 522      56.854  17.169  47.463  1.00 71.33           C  
ANISOU 3977  CG2 ILE A 522     9463   9212   8427   -377   -613   -244       C  
ATOM   3978  CD1 ILE A 522      55.794  19.996  46.456  1.00 80.69           C  
ANISOU 3978  CD1 ILE A 522    10515  10201   9941   -460   -426   -334       C  
ATOM   3979  N   LYS A 523      59.224  17.139  49.934  1.00 79.14           N  
ANISOU 3979  N   LYS A 523    10129  10339   9601   -344   -981   -492       N  
ATOM   3980  CA  LYS A 523      60.101  15.977  50.121  1.00 82.73           C  
ANISOU 3980  CA  LYS A 523    10588  10839  10008   -284  -1033   -406       C  
ATOM   3981  C   LYS A 523      59.978  15.406  51.528  1.00 81.93           C  
ANISOU 3981  C   LYS A 523    10528  10924   9677   -251  -1222   -488       C  
ATOM   3982  O   LYS A 523      59.925  14.180  51.701  1.00 79.81           O  
ANISOU 3982  O   LYS A 523    10373  10735   9217   -203  -1230   -376       O  
ATOM   3983  CB  LYS A 523      61.561  16.308  49.814  1.00 88.67           C  
ANISOU 3983  CB  LYS A 523    11131  11469  11089   -266  -1030   -400       C  
ATOM   3984  CG  LYS A 523      61.873  16.506  48.335  1.00 96.71           C  
ANISOU 3984  CG  LYS A 523    12130  12311  12303   -253   -804   -247       C  
ATOM   3985  CD  LYS A 523      61.908  15.189  47.559  1.00100.83           C  
ANISOU 3985  CD  LYS A 523    12815  12831  12664   -183   -689    -60       C  
ATOM   3986  CE  LYS A 523      61.998  15.416  46.048  1.00102.33           C  
ANISOU 3986  CE  LYS A 523    13038  12867  12976   -142   -453     86       C  
ATOM   3987  NZ  LYS A 523      61.490  14.270  45.238  1.00101.11           N  
ANISOU 3987  NZ  LYS A 523    13116  12720  12582    -79   -354    223       N  
ATOM   3988  N   LYS A 524      59.919  16.294  52.521  1.00 79.82           N  
ANISOU 3988  N   LYS A 524    10178  10723   9428   -263  -1368   -683       N  
ATOM   3989  CA  LYS A 524      59.746  15.878  53.914  1.00 79.25           C  
ANISOU 3989  CA  LYS A 524    10160  10845   9105   -204  -1546   -772       C  
ATOM   3990  C   LYS A 524      58.372  15.245  54.094  1.00 75.47           C  
ANISOU 3990  C   LYS A 524     9887  10475   8312   -195  -1471   -681       C  
ATOM   3991  O   LYS A 524      58.223  14.209  54.746  1.00 75.39           O  
ANISOU 3991  O   LYS A 524     9974  10598   8072   -130  -1518   -601       O  
ATOM   3992  CB  LYS A 524      59.871  17.063  54.887  1.00 81.52           C  
ANISOU 3992  CB  LYS A 524    10337  11174   9462   -204  -1719  -1025       C  
ATOM   3993  CG  LYS A 524      61.210  17.794  54.865  1.00 84.11           C  
ANISOU 3993  CG  LYS A 524    10428  11382  10147   -220  -1833  -1147       C  
ATOM   3994  N   GLN A 525      57.365  15.881  53.519  1.00 71.95           N  
ANISOU 3994  N   GLN A 525     9494   9966   7878   -256  -1350   -681       N  
ATOM   3995  CA  GLN A 525      56.011  15.385  53.636  1.00 71.55           C  
ANISOU 3995  CA  GLN A 525     9609   9995   7582   -257  -1276   -593       C  
ATOM   3996  C   GLN A 525      55.831  14.066  52.862  1.00 70.61           C  
ANISOU 3996  C   GLN A 525     9604   9836   7387   -252  -1174   -379       C  
ATOM   3997  O   GLN A 525      55.066  13.185  53.272  1.00 71.10           O  
ANISOU 3997  O   GLN A 525     9784   9988   7243   -226  -1163   -281       O  
ATOM   3998  CB  GLN A 525      55.030  16.469  53.204  1.00 71.85           C  
ANISOU 3998  CB  GLN A 525     9653   9964   7682   -322  -1186   -655       C  
ATOM   3999  CG  GLN A 525      54.999  17.619  54.198  1.00 74.37           C  
ANISOU 3999  CG  GLN A 525     9894  10345   8017   -309  -1299   -875       C  
ATOM   4000  CD  GLN A 525      54.119  18.779  53.772  1.00 78.71           C  
ANISOU 4000  CD  GLN A 525    10431  10812   8665   -371  -1207   -943       C  
ATOM   4001  OE1 GLN A 525      54.112  19.190  52.609  1.00 80.45           O  
ANISOU 4001  OE1 GLN A 525    10614  10878   9076   -431  -1088   -879       O  
ATOM   4002  NE2 GLN A 525      53.369  19.322  54.721  1.00 80.93           N  
ANISOU 4002  NE2 GLN A 525    10747  11196   8805   -341  -1256  -1067       N  
ATOM   4003  N   THR A 526      56.566  13.906  51.772  1.00 70.22           N  
ANISOU 4003  N   THR A 526     9516   9648   7516   -266  -1099   -305       N  
ATOM   4004  CA  THR A 526      56.607  12.622  51.087  1.00 70.98           C  
ANISOU 4004  CA  THR A 526     9718   9701   7550   -241  -1028   -130       C  
ATOM   4005  C   THR A 526      57.163  11.551  52.052  1.00 70.89           C  
ANISOU 4005  C   THR A 526     9716   9809   7408   -171  -1133    -84       C  
ATOM   4006  O   THR A 526      56.612  10.441  52.149  1.00 71.49           O  
ANISOU 4006  O   THR A 526     9912   9923   7328   -148  -1110     42       O  
ATOM   4007  CB  THR A 526      57.436  12.689  49.767  1.00 71.16           C  
ANISOU 4007  CB  THR A 526     9700   9559   7780   -237   -919    -65       C  
ATOM   4008  OG1 THR A 526      56.832  13.610  48.837  1.00 70.24           O  
ANISOU 4008  OG1 THR A 526     9593   9339   7756   -284   -808    -79       O  
ATOM   4009  CG2 THR A 526      57.521  11.316  49.111  1.00 69.00           C  
ANISOU 4009  CG2 THR A 526     9549   9241   7426   -192   -859     94       C  
ATOM   4010  N   ALA A 527      58.242  11.882  52.761  1.00 69.82           N  
ANISOU 4010  N   ALA A 527     9450   9726   7353   -133  -1254   -181       N  
ATOM   4011  CA  ALA A 527      58.889  10.914  53.656  1.00 71.67           C  
ANISOU 4011  CA  ALA A 527     9683  10077   7473    -51  -1365   -135       C  
ATOM   4012  C   ALA A 527      57.954  10.513  54.785  1.00 72.46           C  
ANISOU 4012  C   ALA A 527     9887  10349   7296     -6  -1418   -123       C  
ATOM   4013  O   ALA A 527      57.927   9.352  55.198  1.00 69.95           O  
ANISOU 4013  O   ALA A 527     9642  10102   6833     55  -1426     10       O  
ATOM   4014  CB  ALA A 527      60.186  11.469  54.214  1.00 72.83           C  
ANISOU 4014  CB  ALA A 527     9653  10244   7774    -17  -1512   -263       C  
ATOM   4015  N   LEU A 528      57.170  11.479  55.257  1.00 73.45           N  
ANISOU 4015  N   LEU A 528    10017  10532   7358    -30  -1437   -248       N  
ATOM   4016  CA  LEU A 528      56.215  11.242  56.320  1.00 73.43           C  
ANISOU 4016  CA  LEU A 528    10112  10693   7096     27  -1459   -233       C  
ATOM   4017  C   LEU A 528      55.128  10.272  55.886  1.00 72.47           C  
ANISOU 4017  C   LEU A 528    10119  10538   6876      4  -1320    -35       C  
ATOM   4018  O   LEU A 528      54.738   9.378  56.639  1.00 70.44           O  
ANISOU 4018  O   LEU A 528     9936  10392   6436     75  -1319     84       O  
ATOM   4019  CB  LEU A 528      55.596  12.570  56.762  1.00 74.25           C  
ANISOU 4019  CB  LEU A 528    10193  10838   7183      8  -1486   -415       C  
ATOM   4020  CG  LEU A 528      54.592  12.452  57.903  1.00 75.63           C  
ANISOU 4020  CG  LEU A 528    10468  11188   7081     89  -1489   -405       C  
ATOM   4021  CD1 LEU A 528      55.183  11.649  59.052  1.00 77.32           C  
ANISOU 4021  CD1 LEU A 528    10707  11576   7094    228  -1606   -368       C  
ATOM   4022  CD2 LEU A 528      54.153  13.834  58.353  1.00 76.61           C  
ANISOU 4022  CD2 LEU A 528    10562  11345   7201     86  -1528   -614       C  
ATOM   4023  N   VAL A 529      54.624  10.465  54.674  1.00 71.44           N  
ANISOU 4023  N   VAL A 529    10012  10252   6879    -90  -1206      2       N  
ATOM   4024  CA  VAL A 529      53.594   9.582  54.154  1.00 71.14           C  
ANISOU 4024  CA  VAL A 529    10084  10155   6790   -121  -1101    167       C  
ATOM   4025  C   VAL A 529      54.115   8.159  54.137  1.00 74.59           C  
ANISOU 4025  C   VAL A 529    10564  10581   7198    -70  -1107    321       C  
ATOM   4026  O   VAL A 529      53.460   7.244  54.632  1.00 77.32           O  
ANISOU 4026  O   VAL A 529    10977  10976   7426    -38  -1080    457       O  
ATOM   4027  CB  VAL A 529      53.177   9.970  52.723  1.00 66.79           C  
ANISOU 4027  CB  VAL A 529     9555   9430   6393   -211  -1008    170       C  
ATOM   4028  CG1 VAL A 529      52.252   8.915  52.127  1.00 60.47           C  
ANISOU 4028  CG1 VAL A 529     8863   8549   5563   -237   -939    327       C  
ATOM   4029  CG2 VAL A 529      52.528  11.349  52.725  1.00 66.57           C  
ANISOU 4029  CG2 VAL A 529     9487   9404   6401   -261   -987     40       C  
ATOM   4030  N   GLU A 530      55.296   7.989  53.553  1.00 79.49           N  
ANISOU 4030  N   GLU A 530    11134  11122   7945    -60  -1128    310       N  
ATOM   4031  CA  GLU A 530      55.918   6.676  53.421  1.00 82.58           C  
ANISOU 4031  CA  GLU A 530    11559  11481   8336     -8  -1127    448       C  
ATOM   4032  C   GLU A 530      56.202   6.022  54.781  1.00 84.05           C  
ANISOU 4032  C   GLU A 530    11736  11835   8362     90  -1211    506       C  
ATOM   4033  O   GLU A 530      56.194   4.797  54.920  1.00 90.69           O  
ANISOU 4033  O   GLU A 530    12633  12671   9154    136  -1189    663       O  
ATOM   4034  CB  GLU A 530      57.207   6.792  52.600  1.00 84.16           C  
ANISOU 4034  CB  GLU A 530    11688  11574   8714      0  -1125    416       C  
ATOM   4035  CG  GLU A 530      56.983   7.030  51.111  1.00 87.82           C  
ANISOU 4035  CG  GLU A 530    12200  11862   9307    -56  -1013    422       C  
ATOM   4036  CD  GLU A 530      56.196   5.912  50.420  1.00 90.40           C  
ANISOU 4036  CD  GLU A 530    12669  12091   9586    -64   -947    550       C  
ATOM   4037  OE1 GLU A 530      56.133   4.783  50.959  1.00 95.08           O  
ANISOU 4037  OE1 GLU A 530    13306  12719  10100    -24   -972    659       O  
ATOM   4038  OE2 GLU A 530      55.641   6.164  49.327  1.00 85.35           O  
ANISOU 4038  OE2 GLU A 530    12098  11334   8998   -105   -877    540       O  
ATOM   4039  N   LEU A 531      56.451   6.847  55.781  1.00 80.13           N  
ANISOU 4039  N   LEU A 531    11175  11485   7784    134  -1310    378       N  
ATOM   4040  CA  LEU A 531      56.669   6.364  57.131  1.00 82.09           C  
ANISOU 4040  CA  LEU A 531    11430  11920   7842    253  -1399    418       C  
ATOM   4041  C   LEU A 531      55.426   5.683  57.696  1.00 81.14           C  
ANISOU 4041  C   LEU A 531    11414  11870   7546    287  -1314    573       C  
ATOM   4042  O   LEU A 531      55.488   4.577  58.241  1.00 84.08           O  
ANISOU 4042  O   LEU A 531    11826  12302   7820    370  -1304    739       O  
ATOM   4043  CB  LEU A 531      57.046   7.547  58.008  1.00 82.85           C  
ANISOU 4043  CB  LEU A 531    11451  12149   7880    296  -1535    209       C  
ATOM   4044  CG  LEU A 531      57.757   7.331  59.321  1.00 83.78           C  
ANISOU 4044  CG  LEU A 531    11544  12459   7828    441  -1691    177       C  
ATOM   4045  CD1 LEU A 531      58.913   6.360  59.188  1.00 82.23           C  
ANISOU 4045  CD1 LEU A 531    11300  12235   7709    489  -1742    282       C  
ATOM   4046  CD2 LEU A 531      58.235   8.720  59.745  1.00 85.32           C  
ANISOU 4046  CD2 LEU A 531    11643  12704   8069    443  -1842    -88       C  
ATOM   4047  N   LEU A 532      54.297   6.363  57.565  1.00 75.06           N  
ANISOU 4047  N   LEU A 532    10677  11086   6757    225  -1243    530       N  
ATOM   4048  CA  LEU A 532      53.043   5.851  58.065  1.00 72.04           C  
ANISOU 4048  CA  LEU A 532    10368  10754   6248    250  -1145    680       C  
ATOM   4049  C   LEU A 532      52.548   4.670  57.242  1.00 72.71           C  
ANISOU 4049  C   LEU A 532    10502  10677   6448    191  -1047    873       C  
ATOM   4050  O   LEU A 532      51.849   3.812  57.767  1.00 74.71           O  
ANISOU 4050  O   LEU A 532    10796  10962   6630    237   -978   1054       O  
ATOM   4051  CB  LEU A 532      51.998   6.958  58.082  1.00 73.48           C  
ANISOU 4051  CB  LEU A 532    10558  10951   6412    198  -1096    577       C  
ATOM   4052  CG  LEU A 532      52.026   7.922  59.281  1.00 77.24           C  
ANISOU 4052  CG  LEU A 532    11022  11620   6704    297  -1168    427       C  
ATOM   4053  CD1 LEU A 532      51.519   7.226  60.535  1.00 76.98           C  
ANISOU 4053  CD1 LEU A 532    11055  11764   6429    445  -1127    582       C  
ATOM   4054  CD2 LEU A 532      53.406   8.541  59.526  1.00 76.17           C  
ANISOU 4054  CD2 LEU A 532    10812  11536   6593    335  -1336    231       C  
ATOM   4055  N   LYS A 533      52.907   4.602  55.958  1.00 90.36           N  
ANISOU 4055  N   LYS A 533    12900  14719   6716   1013  -1978   1150       N  
ATOM   4056  CA  LYS A 533      52.562   3.424  55.141  1.00 89.74           C  
ANISOU 4056  CA  LYS A 533    13151  14389   6557    761  -2038   1353       C  
ATOM   4057  C   LYS A 533      53.302   2.155  55.614  1.00 93.40           C  
ANISOU 4057  C   LYS A 533    14001  14586   6902    774  -2122   1498       C  
ATOM   4058  O   LYS A 533      52.793   1.043  55.502  1.00 95.82           O  
ANISOU 4058  O   LYS A 533    14578  14725   7105    500  -2137   1700       O  
ATOM   4059  CB  LYS A 533      52.868   3.681  53.666  1.00 86.86           C  
ANISOU 4059  CB  LYS A 533    12811  13792   6399    838  -2028   1267       C  
ATOM   4060  CG  LYS A 533      51.845   4.558  52.955  1.00 84.02           C  
ANISOU 4060  CG  LYS A 533    12147  13692   6084    783  -1931   1256       C  
ATOM   4061  CD  LYS A 533      52.027   4.513  51.451  1.00 81.35           C  
ANISOU 4061  CD  LYS A 533    11859  13204   5846    843  -1929   1246       C  
ATOM   4062  CE  LYS A 533      51.247   5.625  50.769  1.00 80.78           C  
ANISOU 4062  CE  LYS A 533    11439  13426   5830    948  -1794   1266       C  
ATOM   4063  NZ  LYS A 533      51.517   5.767  49.314  1.00 76.62           N  
ANISOU 4063  NZ  LYS A 533    10891  12843   5376   1108  -1761   1286       N  
ATOM   4064  N   HIS A 534      54.496   2.346  56.169  1.00 93.79           N  
ANISOU 4064  N   HIS A 534    14054  14605   6975   1102  -2156   1384       N  
ATOM   4065  CA  HIS A 534      55.340   1.252  56.631  1.00 95.37           C  
ANISOU 4065  CA  HIS A 534    14595  14597   7045   1237  -2224   1531       C  
ATOM   4066  C   HIS A 534      55.173   1.026  58.147  1.00 99.29           C  
ANISOU 4066  C   HIS A 534    15022  15452   7253   1300  -2207   1694       C  
ATOM   4067  O   HIS A 534      55.140  -0.120  58.613  1.00100.65           O  
ANISOU 4067  O   HIS A 534    15504  15488   7250   1254  -2202   2011       O  
ATOM   4068  CB  HIS A 534      56.802   1.548  56.256  1.00 93.92           C  
ANISOU 4068  CB  HIS A 534    14426  14253   7006   1599  -2277   1303       C  
ATOM   4069  CG  HIS A 534      57.810   0.720  56.998  1.00 95.27           C  
ANISOU 4069  CG  HIS A 534    14825  14381   6991   1877  -2343   1403       C  
ATOM   4070  ND1 HIS A 534      58.160  -0.557  56.610  1.00 96.50           N  
ANISOU 4070  ND1 HIS A 534    15431  14126   7108   1894  -2387   1617       N  
ATOM   4071  CD2 HIS A 534      58.549   0.996  58.098  1.00 93.57           C  
ANISOU 4071  CD2 HIS A 534    14428  14521   6603   2185  -2363   1303       C  
ATOM   4072  CE1 HIS A 534      59.057  -1.036  57.452  1.00 95.96           C  
ANISOU 4072  CE1 HIS A 534    15470  14149   6841   2232  -2422   1705       C  
ATOM   4073  NE2 HIS A 534      59.312  -0.113  58.360  1.00 94.58           N  
ANISOU 4073  NE2 HIS A 534    14897  14483   6555   2415  -2418   1511       N  
ATOM   4074  N   LYS A 535      55.061   2.106  58.919  1.00 99.16           N  
ANISOU 4074  N   LYS A 535    14590  15896   7189   1422  -2178   1486       N  
ATOM   4075  CA  LYS A 535      54.840   1.993  60.373  1.00102.73           C  
ANISOU 4075  CA  LYS A 535    14892  16825   7315   1510  -2164   1606       C  
ATOM   4076  C   LYS A 535      53.523   2.692  60.741  1.00102.41           C  
ANISOU 4076  C   LYS A 535    14521  17177   7211   1274  -2094   1582       C  
ATOM   4077  O   LYS A 535      53.536   3.751  61.378  1.00100.31           O  
ANISOU 4077  O   LYS A 535    13851  17326   6937   1434  -2076   1282       O  
ATOM   4078  CB  LYS A 535      56.034   2.565  61.165  1.00100.41           C  
ANISOU 4078  CB  LYS A 535    14351  16856   6945   1934  -2210   1301       C  
ATOM   4079  N   PRO A 536      52.376   2.089  60.337  1.00101.47           N  
ANISOU 4079  N   PRO A 536    14556  16944   7054    888  -2049   1862       N  
ATOM   4080  CA  PRO A 536      51.050   2.714  60.455  1.00100.52           C  
ANISOU 4080  CA  PRO A 536    14127  17192   6875    645  -1985   1840       C  
ATOM   4081  C   PRO A 536      50.507   2.879  61.871  1.00103.20           C  
ANISOU 4081  C   PRO A 536    14191  18138   6883    681  -1950   1925       C  
ATOM   4082  O   PRO A 536      49.612   3.699  62.078  1.00102.31           O  
ANISOU 4082  O   PRO A 536    13729  18415   6729    602  -1908   1790       O  
ATOM   4083  CB  PRO A 536      50.147   1.766  59.660  1.00101.23           C  
ANISOU 4083  CB  PRO A 536    14482  17003   6978    214  -1953   2107       C  
ATOM   4084  CG  PRO A 536      50.818   0.445  59.755  1.00103.02           C  
ANISOU 4084  CG  PRO A 536    15161  16814   7169    211  -1966   2378       C  
ATOM   4085  CD  PRO A 536      52.287   0.740  59.743  1.00101.35           C  
ANISOU 4085  CD  PRO A 536    15005  16447   7057    654  -2046   2178       C  
ATOM   4086  N   LYS A 537      51.022   2.112  62.828  1.00106.67           N  
ANISOU 4086  N   LYS A 537    14770  18700   7061    835  -1958   2162       N  
ATOM   4087  CA  LYS A 537      50.575   2.236  64.219  1.00110.65           C  
ANISOU 4087  CA  LYS A 537    14981  19874   7186    925  -1921   2266       C  
ATOM   4088  C   LYS A 537      51.462   3.184  65.030  1.00111.20           C  
ANISOU 4088  C   LYS A 537    14680  20394   7176   1372  -1982   1846       C  
ATOM   4089  O   LYS A 537      51.250   3.346  66.228  1.00115.15           O  
ANISOU 4089  O   LYS A 537    14885  21540   7326   1526  -1971   1855       O  
ATOM   4090  CB  LYS A 537      50.491   0.856  64.888  1.00115.48           C  
ANISOU 4090  CB  LYS A 537    15909  20461   7508    854  -1851   2833       C  
ATOM   4091  CG  LYS A 537      49.129   0.184  64.728  1.00117.33           C  
ANISOU 4091  CG  LYS A 537    16251  20636   7692    342  -1733   3204       C  
ATOM   4092  N   ALA A 538      52.448   3.803  64.380  1.00107.96           N  
ANISOU 4092  N   ALA A 538    14254  19681   7083   1567  -2036   1455       N  
ATOM   4093  CA  ALA A 538      53.394   4.706  65.052  1.00108.28           C  
ANISOU 4093  CA  ALA A 538    13926  20097   7120   1946  -2079    963       C  
ATOM   4094  C   ALA A 538      52.679   5.839  65.785  1.00109.40           C  
ANISOU 4094  C   ALA A 538    13547  20817   7204   1970  -2038    609       C  
ATOM   4095  O   ALA A 538      51.751   6.425  65.238  1.00109.09           O  
ANISOU 4095  O   ALA A 538    13415  20668   7369   1748  -1975    554       O  
ATOM   4096  CB  ALA A 538      54.374   5.284  64.043  1.00102.97           C  
ANISOU 4096  CB  ALA A 538    13302  18933   6890   2044  -2096    601       C  
ATOM   4097  N   THR A 539      53.127   6.159  67.003  1.00111.88           N  
ANISOU 4097  N   THR A 539    13500  21783   7225   2273  -2073    341       N  
ATOM   4098  CA  THR A 539      52.404   7.101  67.874  1.00115.26           C  
ANISOU 4098  CA  THR A 539    13416  22858   7519   2321  -2041      2       C  
ATOM   4099  C   THR A 539      52.767   8.567  67.644  1.00115.39           C  
ANISOU 4099  C   THR A 539    13059  22799   7983   2424  -1995   -721       C  
ATOM   4100  O   THR A 539      53.908   8.896  67.297  1.00112.40           O  
ANISOU 4100  O   THR A 539    12675  22139   7891   2570  -2006  -1069       O  
ATOM   4101  CB  THR A 539      52.618   6.796  69.379  1.00118.63           C  
ANISOU 4101  CB  THR A 539    13549  24158   7367   2620  -2091     10       C  
ATOM   4102  OG1 THR A 539      53.983   7.045  69.736  1.00119.52           O  
ANISOU 4102  OG1 THR A 539    13485  24454   7473   2972  -2160   -426       O  
ATOM   4103  CG2 THR A 539      52.253   5.354  69.715  1.00118.11           C  
ANISOU 4103  CG2 THR A 539    13844  24161   6870   2547  -2077    791       C  
ATOM   4104  N   GLU A 540      51.779   9.440  67.869  1.00118.00           N  
ANISOU 4104  N   GLU A 540    13068  23387   8381   2351  -1924   -943       N  
ATOM   4105  CA  GLU A 540      51.935  10.887  67.682  1.00118.90           C  
ANISOU 4105  CA  GLU A 540    12828  23373   8976   2438  -1824  -1605       C  
ATOM   4106  C   GLU A 540      53.237  11.384  68.315  1.00122.91           C  
ANISOU 4106  C   GLU A 540    13024  24114   9562   2712  -1853  -2233       C  
ATOM   4107  O   GLU A 540      54.016  12.105  67.684  1.00125.64           O  
ANISOU 4107  O   GLU A 540    13332  23973  10431   2733  -1770  -2635       O  
ATOM   4108  CB  GLU A 540      50.733  11.635  68.275  1.00115.80           C  
ANISOU 4108  CB  GLU A 540    12057  23461   8480   2427  -1762  -1785       C  
ATOM   4109  N   GLU A 541      53.484  10.956  69.547  1.00125.26           N  
ANISOU 4109  N   GLU A 541    13083  25192   9316   2924  -1960  -2297       N  
ATOM   4110  CA  GLU A 541      54.690  11.348  70.268  1.00129.90           C  
ANISOU 4110  CA  GLU A 541    13300  26195   9861   3208  -2008  -2930       C  
ATOM   4111  C   GLU A 541      55.965  10.902  69.544  1.00127.63           C  
ANISOU 4111  C   GLU A 541    13313  25399   9782   3251  -2043  -2883       C  
ATOM   4112  O   GLU A 541      56.937  11.660  69.487  1.00133.84           O  
ANISOU 4112  O   GLU A 541    13831  26108  10914   3342  -2003  -3528       O  
ATOM   4113  CB  GLU A 541      54.681  10.784  71.701  1.00131.68           C  
ANISOU 4113  CB  GLU A 541    13233  27464   9337   3483  -2126  -2876       C  
ATOM   4114  N   GLN A 542      55.964   9.680  69.005  1.00121.92           N  
ANISOU 4114  N   GLN A 542    13124  24338   8863   3179  -2104  -2155       N  
ATOM   4115  CA  GLN A 542      57.136   9.147  68.293  1.00117.59           C  
ANISOU 4115  CA  GLN A 542    12891  23324   8464   3248  -2148  -2061       C  
ATOM   4116  C   GLN A 542      57.494   9.975  67.063  1.00114.70           C  
ANISOU 4116  C   GLN A 542    12598  22179   8805   3072  -2033  -2355       C  
ATOM   4117  O   GLN A 542      58.659  10.276  66.835  1.00118.33           O  
ANISOU 4117  O   GLN A 542    12956  22506   9497   3184  -2026  -2748       O  
ATOM   4118  CB  GLN A 542      56.904   7.706  67.843  1.00115.05           C  
ANISOU 4118  CB  GLN A 542    13159  22674   7878   3170  -2204  -1231       C  
ATOM   4119  CG  GLN A 542      56.986   6.673  68.945  1.00117.07           C  
ANISOU 4119  CG  GLN A 542    13441  23577   7464   3427  -2285   -838       C  
ATOM   4120  CD  GLN A 542      56.658   5.277  68.453  1.00115.85           C  
ANISOU 4120  CD  GLN A 542    13899  22957   7160   3297  -2283    -18       C  
ATOM   4121  OE1 GLN A 542      55.643   5.052  67.788  1.00113.13           O  
ANISOU 4121  OE1 GLN A 542    13825  22165   6993   2937  -2222    333       O  
ATOM   4122  NE2 GLN A 542      57.510   4.326  68.793  1.00117.21           N  
ANISOU 4122  NE2 GLN A 542    14275  23253   7006   3602  -2338    272       N  
ATOM   4123  N   LEU A 543      56.486  10.338  66.278  1.00109.57           N  
ANISOU 4123  N   LEU A 543    12100  21063   8469   2813  -1928  -2144       N  
ATOM   4124  CA  LEU A 543      56.695  11.147  65.083  1.00105.86           C  
ANISOU 4124  CA  LEU A 543    11696  19879   8646   2681  -1779  -2321       C  
ATOM   4125  C   LEU A 543      57.267  12.535  65.421  1.00107.12           C  
ANISOU 4125  C   LEU A 543    11354  20100   9246   2767  -1639  -3124       C  
ATOM   4126  O   LEU A 543      58.023  13.101  64.637  1.00104.47           O  
ANISOU 4126  O   LEU A 543    11023  19249   9421   2734  -1513  -3363       O  
ATOM   4127  CB  LEU A 543      55.379  11.304  64.298  1.00104.25           C  
ANISOU 4127  CB  LEU A 543    11680  19328   8604   2453  -1687  -1933       C  
ATOM   4128  CG  LEU A 543      54.556  10.065  63.893  1.00102.38           C  
ANISOU 4128  CG  LEU A 543    11880  19006   8014   2272  -1783  -1215       C  
ATOM   4129  CD1 LEU A 543      53.194  10.469  63.357  1.00100.22           C  
ANISOU 4129  CD1 LEU A 543    11603  18621   7855   2079  -1684  -1008       C  
ATOM   4130  CD2 LEU A 543      55.261   9.197  62.871  1.00 97.88           C  
ANISOU 4130  CD2 LEU A 543    11760  17904   7524   2228  -1839   -888       C  
ATOM   4131  N   LYS A 544      56.899  13.091  66.576  1.00111.17           N  
ANISOU 4131  N   LYS A 544    11419  21237   9582   2865  -1639  -3558       N  
ATOM   4132  CA  LYS A 544      57.446  14.382  66.999  1.00114.36           C  
ANISOU 4132  CA  LYS A 544    11311  21721  10419   2929  -1497  -4418       C  
ATOM   4133  C   LYS A 544      58.965  14.319  66.924  1.00115.87           C  
ANISOU 4133  C   LYS A 544    11415  21875  10736   3018  -1522  -4792       C  
ATOM   4134  O   LYS A 544      59.606  15.143  66.261  1.00114.76           O  
ANISOU 4134  O   LYS A 544    11183  21193  11227   2924  -1334  -5166       O  
ATOM   4135  CB  LYS A 544      56.984  14.750  68.420  1.00116.88           C  
ANISOU 4135  CB  LYS A 544    11129  22906  10375   3075  -1553  -4876       C  
ATOM   4136  N   THR A 545      59.529  13.314  67.583  1.00119.39           N  
ANISOU 4136  N   THR A 545    11892  22901  10571   3212  -1735  -4644       N  
ATOM   4137  CA  THR A 545      60.973  13.125  67.598  1.00126.10           C  
ANISOU 4137  CA  THR A 545    12637  23865  11412   3352  -1791  -4973       C  
ATOM   4138  C   THR A 545      61.544  12.749  66.220  1.00121.51           C  
ANISOU 4138  C   THR A 545    12522  22474  11172   3236  -1746  -4576       C  
ATOM   4139  O   THR A 545      62.630  13.204  65.861  1.00123.44           O  
ANISOU 4139  O   THR A 545    12604  22522  11775   3230  -1665  -5014       O  
ATOM   4140  CB  THR A 545      61.398  12.070  68.645  1.00132.70           C  
ANISOU 4140  CB  THR A 545    13408  25574  11439   3673  -2023  -4818       C  
ATOM   4141  OG1 THR A 545      60.594  10.891  68.497  1.00132.07           O  
ANISOU 4141  OG1 THR A 545    13838  25409  10931   3672  -2124  -3915       O  
ATOM   4142  CG2 THR A 545      61.249  12.628  70.074  1.00136.62           C  
ANISOU 4142  CG2 THR A 545    13264  27041  11604   3856  -2061  -5455       C  
ATOM   4143  N   VAL A 546      60.820  11.939  65.451  1.00117.28           N  
ANISOU 4143  N   VAL A 546    12527  21509  10527   3133  -1790  -3794       N  
ATOM   4144  CA  VAL A 546      61.282  11.562  64.115  1.00112.28           C  
ANISOU 4144  CA  VAL A 546    12318  20164  10180   3040  -1756  -3429       C  
ATOM   4145  C   VAL A 546      61.320  12.788  63.215  1.00113.85           C  
ANISOU 4145  C   VAL A 546    12391  19739  11127   2856  -1497  -3721       C  
ATOM   4146  O   VAL A 546      62.319  13.041  62.548  1.00114.56           O  
ANISOU 4146  O   VAL A 546    12473  19491  11564   2846  -1410  -3908       O  
ATOM   4147  CB  VAL A 546      60.399  10.490  63.453  1.00106.96           C  
ANISOU 4147  CB  VAL A 546    12203  19175   9262   2935  -1842  -2611       C  
ATOM   4148  CG1 VAL A 546      60.893  10.219  62.037  1.00103.28           C  
ANISOU 4148  CG1 VAL A 546    12105  18025   9111   2856  -1801  -2336       C  
ATOM   4149  CG2 VAL A 546      60.396   9.209  64.272  1.00104.52           C  
ANISOU 4149  CG2 VAL A 546    12078  19355   8278   3112  -2043  -2233       C  
ATOM   4150  N   MET A 547      60.230  13.545  63.200  1.00118.34           N  
ANISOU 4150  N   MET A 547    12857  20167  11938   2733  -1353  -3731       N  
ATOM   4151  CA  MET A 547      60.197  14.819  62.482  1.00122.60           C  
ANISOU 4151  CA  MET A 547    13241  20130  13213   2614  -1053  -4003       C  
ATOM   4152  C   MET A 547      61.305  15.735  63.002  1.00128.05           C  
ANISOU 4152  C   MET A 547    13448  20921  14286   2634   -917  -4838       C  
ATOM   4153  O   MET A 547      62.089  16.276  62.215  1.00131.47           O  
ANISOU 4153  O   MET A 547    13856  20842  15254   2555   -718  -4999       O  
ATOM   4154  CB  MET A 547      58.844  15.527  62.653  1.00124.08           C  
ANISOU 4154  CB  MET A 547    13318  20290  13535   2558   -923  -3963       C  
ATOM   4155  CG  MET A 547      57.699  14.970  61.825  1.00119.51           C  
ANISOU 4155  CG  MET A 547    13150  19475  12784   2482   -958  -3212       C  
ATOM   4156  SD  MET A 547      56.192  15.843  62.285  1.00123.70           S  
ANISOU 4156  SD  MET A 547    13440  20174  13388   2478   -825  -3284       S  
ATOM   4157  CE  MET A 547      54.962  14.963  61.329  1.00114.87           C  
ANISOU 4157  CE  MET A 547    12771  18933  11941   2372   -914  -2422       C  
ATOM   4158  N   GLU A 548      61.363  15.906  64.324  1.00130.17           N  
ANISOU 4158  N   GLU A 548    13301  21886  14272   2733  -1014  -5383       N  
ATOM   4159  CA  GLU A 548      62.395  16.746  64.937  1.00134.40           C  
ANISOU 4159  CA  GLU A 548    13299  22644  15123   2736   -902  -6295       C  
ATOM   4160  C   GLU A 548      63.780  16.355  64.414  1.00136.36           C  
ANISOU 4160  C   GLU A 548    13609  22775  15428   2750   -934  -6359       C  
ATOM   4161  O   GLU A 548      64.612  17.218  64.113  1.00139.59           O  
ANISOU 4161  O   GLU A 548    13739  22863  16434   2620   -702  -6901       O  
ATOM   4162  CB  GLU A 548      62.358  16.643  66.467  1.00133.95           C  
ANISOU 4162  CB  GLU A 548    12797  23576  14523   2911  -1089  -6808       C  
ATOM   4163  N   ASN A 549      64.013  15.048  64.290  1.00133.22           N  
ANISOU 4163  N   ASN A 549    13577  22612  14428   2905  -1199  -5797       N  
ATOM   4164  CA  ASN A 549      65.313  14.545  63.867  1.00132.14           C  
ANISOU 4164  CA  ASN A 549    13506  22470  14232   2984  -1268  -5831       C  
ATOM   4165  C   ASN A 549      65.572  14.662  62.361  1.00130.35           C  
ANISOU 4165  C   ASN A 549    13626  21390  14512   2829  -1094  -5446       C  
ATOM   4166  O   ASN A 549      66.729  14.734  61.963  1.00131.30           O  
ANISOU 4166  O   ASN A 549    13642  21425  14822   2828  -1042  -5694       O  
ATOM   4167  CB  ASN A 549      65.519  13.109  64.366  1.00129.49           C  
ANISOU 4167  CB  ASN A 549    13418  22712  13069   3268  -1594  -5399       C  
ATOM   4168  CG  ASN A 549      65.662  13.044  65.886  1.00132.45           C  
ANISOU 4168  CG  ASN A 549    13330  24084  12911   3499  -1744  -5876       C  
ATOM   4169  OD1 ASN A 549      66.251  13.932  66.507  1.00131.84           O  
ANISOU 4169  OD1 ASN A 549    12672  24379  13041   3484  -1655  -6722       O  
ATOM   4170  ND2 ASN A 549      65.096  12.006  66.491  1.00131.43           N  
ANISOU 4170  ND2 ASN A 549    13433  24405  12101   3709  -1951  -5345       N  
ATOM   4171  N   PHE A 550      64.520  14.683  61.535  1.00126.57           N  
ANISOU 4171  N   PHE A 550    13516  20361  14213   2718  -1004  -4856       N  
ATOM   4172  CA  PHE A 550      64.689  14.965  60.098  1.00125.01           C  
ANISOU 4172  CA  PHE A 550    13570  19414  14514   2599   -798  -4517       C  
ATOM   4173  C   PHE A 550      65.187  16.405  59.938  1.00128.33           C  
ANISOU 4173  C   PHE A 550    13578  19458  15721   2440   -427  -5109       C  
ATOM   4174  O   PHE A 550      66.133  16.656  59.194  1.00127.62           O  
ANISOU 4174  O   PHE A 550    13457  19037  15997   2377   -269  -5189       O  
ATOM   4175  CB  PHE A 550      63.382  14.805  59.276  1.00124.51           C  
ANISOU 4175  CB  PHE A 550    13902  18941  14466   2541   -756  -3819       C  
ATOM   4176  CG  PHE A 550      63.069  13.386  58.798  1.00122.70           C  
ANISOU 4176  CG  PHE A 550    14177  18761  13681   2613  -1027  -3142       C  
ATOM   4177  CD1 PHE A 550      64.068  12.437  58.555  1.00120.40           C  
ANISOU 4177  CD1 PHE A 550    14082  18563  13102   2732  -1207  -3035       C  
ATOM   4178  CD2 PHE A 550      61.737  13.023  58.528  1.00122.46           C  
ANISOU 4178  CD2 PHE A 550    14420  18657  13453   2553  -1077  -2625       C  
ATOM   4179  CE1 PHE A 550      63.743  11.157  58.108  1.00117.51           C  
ANISOU 4179  CE1 PHE A 550    14189  18161  12301   2788  -1422  -2453       C  
ATOM   4180  CE2 PHE A 550      61.411  11.744  58.074  1.00117.82           C  
ANISOU 4180  CE2 PHE A 550    14274  18065  12426   2565  -1291  -2068       C  
ATOM   4181  CZ  PHE A 550      62.416  10.810  57.866  1.00115.52           C  
ANISOU 4181  CZ  PHE A 550    14194  17803  11896   2680  -1457  -1988       C  
ATOM   4182  N   VAL A 551      64.547  17.342  60.643  1.00131.40           N  
ANISOU 4182  N   VAL A 551    13649  19890  16389   2370   -270  -5529       N  
ATOM   4183  CA  VAL A 551      64.911  18.765  60.564  1.00134.62           C  
ANISOU 4183  CA  VAL A 551    13666  19856  17629   2200    133  -6126       C  
ATOM   4184  C   VAL A 551      66.281  19.029  61.177  1.00140.58           C  
ANISOU 4184  C   VAL A 551    13956  20955  18506   2137    149  -6950       C  
ATOM   4185  O   VAL A 551      67.067  19.812  60.636  1.00143.67           O  
ANISOU 4185  O   VAL A 551    14154  20874  19561   1962    468  -7262       O  
ATOM   4186  CB  VAL A 551      63.877  19.665  61.275  1.00134.96           C  
ANISOU 4186  CB  VAL A 551    13464  19899  17915   2174    283  -6449       C  
ATOM   4187  CG1 VAL A 551      64.391  21.099  61.385  1.00138.01           C  
ANISOU 4187  CG1 VAL A 551    13400  19848  19188   1994    707  -7212       C  
ATOM   4188  CG2 VAL A 551      62.539  19.618  60.552  1.00129.61           C  
ANISOU 4188  CG2 VAL A 551    13180  18842  17224   2229    340  -5682       C  
ATOM   4189  N   ALA A 552      66.554  18.384  62.311  1.00142.54           N  
ANISOU 4189  N   ALA A 552    13995  22062  18101   2288   -175  -7294       N  
ATOM   4190  CA  ALA A 552      67.872  18.449  62.940  1.00145.85           C  
ANISOU 4190  CA  ALA A 552    13947  23011  18460   2290   -226  -8062       C  
ATOM   4191  C   ALA A 552      68.938  17.929  61.978  1.00143.05           C  
ANISOU 4191  C   ALA A 552    13800  22431  18123   2292   -235  -7776       C  
ATOM   4192  O   ALA A 552      70.031  18.482  61.887  1.00148.84           O  
ANISOU 4192  O   ALA A 552    14163  23133  19256   2148    -56  -8363       O  
ATOM   4193  CB  ALA A 552      67.887  17.645  64.231  1.00146.17           C  
ANISOU 4193  CB  ALA A 552    13800  24098  17638   2557   -603  -8272       C  
ATOM   4194  N   PHE A 553      68.594  16.865  61.260  1.00136.45           N  
ANISOU 4194  N   PHE A 553    13537  21449  16860   2445   -438  -6901       N  
ATOM   4195  CA  PHE A 553      69.476  16.244  60.268  1.00131.72           C  
ANISOU 4195  CA  PHE A 553    13201  20640  16206   2495   -479  -6536       C  
ATOM   4196  C   PHE A 553      69.641  17.133  59.039  1.00131.63           C  
ANISOU 4196  C   PHE A 553    13233  19784  16998   2260    -81  -6405       C  
ATOM   4197  O   PHE A 553      70.765  17.414  58.631  1.00132.32           O  
ANISOU 4197  O   PHE A 553    13108  19783  17386   2168     68  -6702       O  
ATOM   4198  CB  PHE A 553      68.913  14.864  59.893  1.00126.18           C  
ANISOU 4198  CB  PHE A 553    13100  19995  14848   2716   -794  -5680       C  
ATOM   4199  CG  PHE A 553      69.452  14.287  58.617  1.00122.06           C  
ANISOU 4199  CG  PHE A 553    12950  19076  14351   2757   -800  -5171       C  
ATOM   4200  CD1 PHE A 553      70.814  14.156  58.406  1.00124.13           C  
ANISOU 4200  CD1 PHE A 553    13029  19518  14615   2815   -808  -5473       C  
ATOM   4201  CD2 PHE A 553      68.583  13.820  57.645  1.00118.36           C  
ANISOU 4201  CD2 PHE A 553    12988  18140  13843   2755   -817  -4414       C  
ATOM   4202  CE1 PHE A 553      71.297  13.603  57.233  1.00121.91           C  
ANISOU 4202  CE1 PHE A 553    13078  18921  14321   2880   -824  -5012       C  
ATOM   4203  CE2 PHE A 553      69.063  13.269  56.473  1.00116.43           C  
ANISOU 4203  CE2 PHE A 553    13056  17597  13584   2815   -836  -3988       C  
ATOM   4204  CZ  PHE A 553      70.420  13.161  56.266  1.00117.15           C  
ANISOU 4204  CZ  PHE A 553    12976  17844  13691   2885   -839  -4276       C  
ATOM   4205  N   VAL A 554      68.526  17.587  58.464  1.00132.20           N  
ANISOU 4205  N   VAL A 554    13550  19280  17398   2183    109  -5947       N  
ATOM   4206  CA  VAL A 554      68.567  18.423  57.257  1.00132.83           C  
ANISOU 4206  CA  VAL A 554    13698  18564  18207   2028    520  -5687       C  
ATOM   4207  C   VAL A 554      69.295  19.739  57.529  1.00138.97           C  
ANISOU 4207  C   VAL A 554    13943  19081  19777   1776    926  -6469       C  
ATOM   4208  O   VAL A 554      70.184  20.129  56.771  1.00139.98           O  
ANISOU 4208  O   VAL A 554    13973  18853  20362   1646   1190  -6509       O  
ATOM   4209  CB  VAL A 554      67.155  18.723  56.702  1.00131.08           C  
ANISOU 4209  CB  VAL A 554    13783  17875  18146   2054    657  -5076       C  
ATOM   4210  CG1 VAL A 554      67.229  19.708  55.543  1.00131.51           C  
ANISOU 4210  CG1 VAL A 554    13845  17152  18973   1952   1138  -4818       C  
ATOM   4211  CG2 VAL A 554      66.473  17.442  56.258  1.00127.26           C  
ANISOU 4211  CG2 VAL A 554    13808  17583  16962   2237    304  -4324       C  
ATOM   4212  N   ASP A 555      68.921  20.412  58.617  1.00143.08           N  
ANISOU 4212  N   ASP A 555    14104  19793  20468   1697    986  -7112       N  
ATOM   4213  CA  ASP A 555      69.600  21.643  59.028  1.00148.61           C  
ANISOU 4213  CA  ASP A 555    14248  20283  21935   1426   1365  -8003       C  
ATOM   4214  C   ASP A 555      71.084  21.381  59.310  1.00150.91           C  
ANISOU 4214  C   ASP A 555    14174  21069  22097   1347   1270  -8609       C  
ATOM   4215  O   ASP A 555      71.917  22.261  59.096  1.00156.67           O  
ANISOU 4215  O   ASP A 555    14537  21455  23537   1069   1645  -9136       O  
ATOM   4216  CB  ASP A 555      68.917  22.267  60.256  1.00149.20           C  
ANISOU 4216  CB  ASP A 555    13978  20622  22089   1397   1374  -8663       C  
ATOM   4217  N   LYS A 556      71.407  20.168  59.766  1.00148.03           N  
ANISOU 4217  N   LYS A 556    13908  21502  20837   1599    792  -8509       N  
ATOM   4218  CA  LYS A 556      72.791  19.784  60.111  1.00148.13           C  
ANISOU 4218  CA  LYS A 556    13567  22148  20567   1619    642  -9056       C  
ATOM   4219  C   LYS A 556      73.754  19.624  58.936  1.00145.31           C  
ANISOU 4219  C   LYS A 556    13337  21444  20429   1551    783  -8744       C  
ATOM   4220  O   LYS A 556      74.969  19.715  59.127  1.00146.94           O  
ANISOU 4220  O   LYS A 556    13124  22031  20677   1462    811  -9348       O  
ATOM   4221  CB  LYS A 556      72.805  18.471  60.903  1.00144.51           C  
ANISOU 4221  CB  LYS A 556    13231  22626  19052   1997    109  -8912       C  
ATOM   4222  N   CYS A 557      73.230  19.364  57.740  1.00140.40           N  
ANISOU 4222  N   CYS A 557    13252  20195  19897   1609    860  -7833       N  
ATOM   4223  CA  CYS A 557      74.088  19.088  56.579  1.00139.47           C  
ANISOU 4223  CA  CYS A 557    13283  19832  19876   1605    955  -7455       C  
ATOM   4224  C   CYS A 557      74.127  20.208  55.545  1.00142.94           C  
ANISOU 4224  C   CYS A 557    13679  19382  21251   1327   1515  -7277       C  
ATOM   4225  O   CYS A 557      75.153  20.413  54.892  1.00145.79           O  
ANISOU 4225  O   CYS A 557    13869  19613  21911   1197   1726  -7356       O  
ATOM   4226  CB  CYS A 557      73.669  17.785  55.906  1.00132.02           C  
ANISOU 4226  CB  CYS A 557    12955  18970  18235   1929    597  -6558       C  
ATOM   4227  SG  CYS A 557      74.137  16.292  56.809  1.00128.26           S  
ANISOU 4227  SG  CYS A 557    12560  19482  16691   2301      6  -6654       S  
ATOM   4228  N   CYS A 558      73.027  20.939  55.391  1.00145.09           N  
ANISOU 4228  N   CYS A 558    14090  19058  21981   1259   1779  -7013       N  
ATOM   4229  CA  CYS A 558      73.005  22.047  54.440  1.00149.39           C  
ANISOU 4229  CA  CYS A 558    14601  18724  23435   1051   2363  -6776       C  
ATOM   4230  C   CYS A 558      73.943  23.190  54.862  1.00156.97           C  
ANISOU 4230  C   CYS A 558    14956  19470  25216    661   2798  -7690       C  
ATOM   4231  O   CYS A 558      74.298  24.025  54.036  1.00162.18           O  
ANISOU 4231  O   CYS A 558    15532  19440  26648    455   3316  -7537       O  
ATOM   4232  CB  CYS A 558      71.570  22.544  54.194  1.00148.89           C  
ANISOU 4232  CB  CYS A 558    14829  18112  23628   1140   2546  -6250       C  
ATOM   4233  SG  CYS A 558      70.445  21.326  53.448  1.00140.91           S  
ANISOU 4233  SG  CYS A 558    14491  17261  21786   1525   2138  -5156       S  
ATOM   4234  N   ALA A 559      74.366  23.211  56.128  1.00159.68           N  
ANISOU 4234  N   ALA A 559    14854  20433  25385    561   2603  -8640       N  
ATOM   4235  CA  ALA A 559      75.367  24.182  56.603  1.00164.89           C  
ANISOU 4235  CA  ALA A 559    14863  21039  26750    161   2966  -9659       C  
ATOM   4236  C   ALA A 559      76.812  23.652  56.585  1.00164.58           C  
ANISOU 4236  C   ALA A 559    14509  21636  26387    104   2804 -10060       C  
ATOM   4237  O   ALA A 559      77.751  24.440  56.701  1.00171.72           O  
ANISOU 4237  O   ALA A 559    14880  22438  27927   -272   3161 -10810       O  
ATOM   4238  CB  ALA A 559      75.009  24.663  58.004  1.00168.30           C  
ANISOU 4238  CB  ALA A 559    14879  21829  27238     69   2897 -10599       C  
ATOM   4239  N   ALA A 560      76.991  22.339  56.433  1.00157.02           N  
ANISOU 4239  N   ALA A 560    13867  21317  24478    469   2293  -9582       N  
ATOM   4240  CA  ALA A 560      78.314  21.704  56.573  1.00157.24           C  
ANISOU 4240  CA  ALA A 560    13596  22109  24039    520   2058  -9984       C  
ATOM   4241  C   ALA A 560      79.264  21.967  55.399  1.00156.71           C  
ANISOU 4241  C   ALA A 560    13471  21646  24428    328   2403  -9747       C  
ATOM   4242  O   ALA A 560      78.824  22.196  54.272  1.00154.64           O  
ANISOU 4242  O   ALA A 560    13593  20625  24540    320   2681  -8941       O  
ATOM   4243  CB  ALA A 560      78.157  20.207  56.783  1.00152.49           C  
ANISOU 4243  CB  ALA A 560    13391  22240  22308   1016   1434  -9504       C  
ATOM   4244  N   ASP A 561      80.567  21.898  55.681  1.00158.07           N  
ANISOU 4244  N   ASP A 561    13132  22426  24500    205   2371 -10444       N  
ATOM   4245  CA  ASP A 561      81.625  22.244  54.714  1.00158.92           C  
ANISOU 4245  CA  ASP A 561    13036  22273  25073    -41   2733 -10400       C  
ATOM   4246  C   ASP A 561      81.502  21.512  53.372  1.00151.30           C  
ANISOU 4246  C   ASP A 561    12665  21027  23797    253   2652  -9267       C  
ATOM   4247  O   ASP A 561      81.495  22.152  52.319  1.00151.40           O  
ANISOU 4247  O   ASP A 561    12772  20284  24469     61   3123  -8783       O  
ATOM   4248  CB  ASP A 561      83.009  21.987  55.322  1.00161.70           C  
ANISOU 4248  CB  ASP A 561    12768  23584  25086   -105   2563 -11302       C  
ATOM   4249  N   ASP A 562      81.426  20.182  53.415  1.00143.95           N  
ANISOU 4249  N   ASP A 562    12108  20714  21874    730   2081  -8862       N  
ATOM   4250  CA  ASP A 562      81.141  19.373  52.229  1.00136.80           C  
ANISOU 4250  CA  ASP A 562    11798  19588  20591   1051   1936  -7833       C  
ATOM   4251  C   ASP A 562      79.799  18.679  52.429  1.00128.38           C  
ANISOU 4251  C   ASP A 562    11312  18442  19024   1373   1584  -7248       C  
ATOM   4252  O   ASP A 562      79.749  17.542  52.892  1.00124.52           O  
ANISOU 4252  O   ASP A 562    11053  18554  17707   1732   1078  -7166       O  
ATOM   4253  CB  ASP A 562      82.249  18.340  51.982  1.00134.98           C  
ANISOU 4253  CB  ASP A 562    11534  20092  19662   1336   1594  -7845       C  
ATOM   4254  N   LYS A 563      78.719  19.384  52.084  1.00126.28           N  
ANISOU 4254  N   LYS A 563    11265  17431  19283   1245   1882  -6840       N  
ATOM   4255  CA  LYS A 563      77.338  18.884  52.253  1.00121.91           C  
ANISOU 4255  CA  LYS A 563    11210  16761  18348   1486   1615  -6309       C  
ATOM   4256  C   LYS A 563      77.161  17.465  51.693  1.00117.21           C  
ANISOU 4256  C   LYS A 563    11144  16473  16916   1895   1155  -5628       C  
ATOM   4257  O   LYS A 563      76.507  16.620  52.311  1.00115.78           O  
ANISOU 4257  O   LYS A 563    11248  16619  16126   2128    749  -5507       O  
ATOM   4258  CB  LYS A 563      76.330  19.841  51.598  1.00119.62           C  
ANISOU 4258  CB  LYS A 563    11089  15613  18748   1343   2058  -5821       C  
ATOM   4259  N   GLU A 564      77.763  17.206  50.531  1.00115.70           N  
ANISOU 4259  N   GLU A 564    11068  16178  16716   1975   1240  -5205       N  
ATOM   4260  CA  GLU A 564      77.766  15.877  49.930  1.00110.69           C  
ANISOU 4260  CA  GLU A 564    10885  15829  15343   2352    833  -4663       C  
ATOM   4261  C   GLU A 564      78.309  14.870  50.941  1.00111.38           C  
ANISOU 4261  C   GLU A 564    10938  16663  14717   2589    360  -5086       C  
ATOM   4262  O   GLU A 564      77.640  13.897  51.279  1.00105.33           O  
ANISOU 4262  O   GLU A 564    10571  16078  13372   2851    -17  -4801       O  
ATOM   4263  CB  GLU A 564      78.612  15.867  48.651  1.00111.93           C  
ANISOU 4263  CB  GLU A 564    11012  15895  15620   2388   1022  -4346       C  
ATOM   4264  N   ALA A 565      79.517  15.134  51.440  1.00118.72           N  
ANISOU 4264  N   ALA A 565    11365  18038  15704   2498    410  -5768       N  
ATOM   4265  CA  ALA A 565      80.141  14.302  52.482  1.00120.29           C  
ANISOU 4265  CA  ALA A 565    11427  19052  15227   2764      4  -6231       C  
ATOM   4266  C   ALA A 565      79.246  14.130  53.731  1.00119.02           C  
ANISOU 4266  C   ALA A 565    11328  19109  14783   2834   -220  -6407       C  
ATOM   4267  O   ALA A 565      79.242  13.066  54.352  1.00116.70           O  
ANISOU 4267  O   ALA A 565    11235  19338  13770   3196   -621  -6339       O  
ATOM   4268  CB  ALA A 565      81.504  14.871  52.873  1.00124.14           C  
ANISOU 4268  CB  ALA A 565    11236  20015  15915   2588    164  -7045       C  
ATOM   4269  N   CYS A 566      78.479  15.158  54.082  1.00119.06           N  
ANISOU 4269  N   CYS A 566    11173  18713  15352   2517     56  -6595       N  
ATOM   4270  CA  CYS A 566      77.610  15.077  55.254  1.00121.49           C  
ANISOU 4270  CA  CYS A 566    11493  19261  15407   2573   -131  -6780       C  
ATOM   4271  C   CYS A 566      76.527  14.017  55.094  1.00116.69           C  
ANISOU 4271  C   CYS A 566    11535  18541  14261   2856   -445  -6009       C  
ATOM   4272  O   CYS A 566      76.462  13.062  55.875  1.00116.86           O  
ANISOU 4272  O   CYS A 566    11694  19102  13604   3158   -808  -5987       O  
ATOM   4273  CB  CYS A 566      76.949  16.423  55.548  1.00125.44           C  
ANISOU 4273  CB  CYS A 566    11716  19281  16665   2190    254  -7111       C  
ATOM   4274  SG  CYS A 566      76.138  16.477  57.167  1.00129.30           S  
ANISOU 4274  SG  CYS A 566    12019  20265  16845   2247     43  -7587       S  
ATOM   4275  N   PHE A 567      75.689  14.189  54.077  1.00113.39           N  
ANISOU 4275  N   PHE A 567    11492  17442  14147   2762   -282  -5377       N  
ATOM   4276  CA  PHE A 567      74.561  13.289  53.843  1.00110.69           C  
ANISOU 4276  CA  PHE A 567    11727  16946  13384   2950   -530  -4689       C  
ATOM   4277  C   PHE A 567      75.007  11.827  53.726  1.00106.18           C  
ANISOU 4277  C   PHE A 567    11509  16744  12092   3316   -921  -4398       C  
ATOM   4278  O   PHE A 567      74.335  10.923  54.236  1.00103.86           O  
ANISOU 4278  O   PHE A 567    11549  16616  11298   3504  -1205  -4123       O  
ATOM   4279  CB  PHE A 567      73.784  13.706  52.586  1.00111.08           C  
ANISOU 4279  CB  PHE A 567    12052  16307  13847   2824   -278  -4090       C  
ATOM   4280  CG  PHE A 567      72.978  14.958  52.765  1.00114.51           C  
ANISOU 4280  CG  PHE A 567    12287  16321  14902   2557     72  -4202       C  
ATOM   4281  CD1 PHE A 567      71.866  14.966  53.588  1.00113.86           C  
ANISOU 4281  CD1 PHE A 567    12287  16298  14676   2546    -38  -4200       C  
ATOM   4282  CD2 PHE A 567      73.338  16.133  52.125  1.00119.55           C  
ANISOU 4282  CD2 PHE A 567    12648  16497  16280   2329    535  -4299       C  
ATOM   4283  CE1 PHE A 567      71.123  16.122  53.771  1.00115.83           C  
ANISOU 4283  CE1 PHE A 567    12349  16169  15491   2341    285  -4326       C  
ATOM   4284  CE2 PHE A 567      72.597  17.292  52.307  1.00121.14           C  
ANISOU 4284  CE2 PHE A 567    12684  16252  17091   2121    889  -4397       C  
ATOM   4285  CZ  PHE A 567      71.486  17.286  53.126  1.00117.88           C  
ANISOU 4285  CZ  PHE A 567    12360  15917  16511   2141    752  -4424       C  
ATOM   4286  N   ALA A 568      76.149  11.609  53.080  1.00102.79           N  
ANISOU 4286  N   ALA A 568    10992  16434  11629   3419   -912  -4466       N  
ATOM   4287  CA  ALA A 568      76.711  10.269  52.937  1.00100.99           C  
ANISOU 4287  CA  ALA A 568    11070  16543  10760   3806  -1254  -4245       C  
ATOM   4288  C   ALA A 568      76.705   9.510  54.259  1.00102.95           C  
ANISOU 4288  C   ALA A 568    11331  17369  10416   4075  -1562  -4431       C  
ATOM   4289  O   ALA A 568      76.197   8.389  54.323  1.00101.04           O  
ANISOU 4289  O   ALA A 568    11568  17118   9706   4327  -1819  -3978       O  
ATOM   4290  CB  ALA A 568      78.126  10.337  52.387  1.00101.45           C  
ANISOU 4290  CB  ALA A 568    10848  16837  10862   3882  -1185  -4512       C  
ATOM   4291  N   VAL A 569      77.256  10.128  55.308  1.00105.38           N  
ANISOU 4291  N   VAL A 569    11095  18190  10755   4022  -1513  -5101       N  
ATOM   4292  CA  VAL A 569      77.415   9.459  56.602  1.00106.63           C  
ANISOU 4292  CA  VAL A 569    11163  19062  10290   4345  -1788  -5314       C  
ATOM   4293  C   VAL A 569      76.226   9.685  57.523  1.00104.12           C  
ANISOU 4293  C   VAL A 569    10869  18750   9943   4236  -1806  -5286       C  
ATOM   4294  O   VAL A 569      75.758   8.764  58.191  1.00100.22           O  
ANISOU 4294  O   VAL A 569    10654  18526   8899   4518  -2047  -4979       O  
ATOM   4295  CB  VAL A 569      78.699   9.922  57.313  1.00112.74           C  
ANISOU 4295  CB  VAL A 569    11263  20583  10989   4406  -1764  -6119       C  
ATOM   4296  CG1 VAL A 569      78.954   9.087  58.564  1.00113.09           C  
ANISOU 4296  CG1 VAL A 569    11223  21482  10265   4864  -2068  -6253       C  
ATOM   4297  CG2 VAL A 569      79.881   9.818  56.354  1.00114.62           C  
ANISOU 4297  CG2 VAL A 569    11419  20827  11306   4467  -1709  -6176       C  
ATOM   4298  N   GLU A 570      75.731  10.913  57.539  1.00106.07           N  
ANISOU 4298  N   GLU A 570    10826  18679  10798   3837  -1526  -5582       N  
ATOM   4299  CA  GLU A 570      74.674  11.303  58.464  1.00107.48           C  
ANISOU 4299  CA  GLU A 570    10919  18929  10989   3724  -1516  -5681       C  
ATOM   4300  C   GLU A 570      73.315  10.726  58.090  1.00105.56           C  
ANISOU 4300  C   GLU A 570    11268  18207  10633   3716  -1597  -4923       C  
ATOM   4301  O   GLU A 570      72.484  10.460  58.963  1.00106.25           O  
ANISOU 4301  O   GLU A 570    11421  18536  10413   3781  -1720  -4825       O  
ATOM   4302  CB  GLU A 570      74.588  12.828  58.523  1.00109.60           C  
ANISOU 4302  CB  GLU A 570    10703  18930  12009   3312  -1157  -6254       C  
ATOM   4303  CG  GLU A 570      75.827  13.495  59.097  1.00114.04           C  
ANISOU 4303  CG  GLU A 570    10582  20026  12722   3242  -1054  -7153       C  
ATOM   4304  CD  GLU A 570      76.109  13.053  60.515  1.00117.43           C  
ANISOU 4304  CD  GLU A 570    10685  21440  12493   3538  -1325  -7604       C  
ATOM   4305  OE1 GLU A 570      75.128  12.870  61.271  1.00116.10           O  
ANISOU 4305  OE1 GLU A 570    10629  21430  12053   3620  -1444  -7449       O  
ATOM   4306  OE2 GLU A 570      77.303  12.880  60.861  1.00119.66           O  
ANISOU 4306  OE2 GLU A 570    10580  22387  12497   3712  -1414  -8092       O  
ATOM   4307  N   GLY A 571      73.089  10.536  56.790  1.00106.15           N  
ANISOU 4307  N   GLY A 571    11734  17660  10936   3634  -1521  -4408       N  
ATOM   4308  CA  GLY A 571      71.834   9.949  56.289  1.00102.08           C  
ANISOU 4308  CA  GLY A 571    11756  16716  10313   3606  -1595  -3722       C  
ATOM   4309  C   GLY A 571      71.530   8.594  56.916  1.00100.26           C  
ANISOU 4309  C   GLY A 571    11894  16797   9404   3895  -1912  -3372       C  
ATOM   4310  O   GLY A 571      70.585   8.466  57.702  1.00100.55           O  
ANISOU 4310  O   GLY A 571    11988  16969   9248   3866  -1975  -3254       O  
ATOM   4311  N   PRO A 572      72.356   7.584  56.605  1.00 97.35           N  
ANISOU 4311  N   PRO A 572    11760  16551   8676   4192  -2090  -3205       N  
ATOM   4312  CA  PRO A 572      72.273   6.273  57.246  1.00 97.69           C  
ANISOU 4312  CA  PRO A 572    12141  16875   8100   4527  -2348  -2882       C  
ATOM   4313  C   PRO A 572      72.093   6.353  58.772  1.00101.57           C  
ANISOU 4313  C   PRO A 572    12336  18008   8249   4654  -2420  -3134       C  
ATOM   4314  O   PRO A 572      71.405   5.510  59.347  1.00104.63           O  
ANISOU 4314  O   PRO A 572    13026  18483   8245   4793  -2547  -2729       O  
ATOM   4315  CB  PRO A 572      73.617   5.643  56.914  1.00 98.50           C  
ANISOU 4315  CB  PRO A 572    12268  17197   7959   4868  -2461  -2968       C  
ATOM   4316  CG  PRO A 572      74.050   6.310  55.663  1.00 96.12           C  
ANISOU 4316  CG  PRO A 572    11876  16500   8147   4656  -2288  -3070       C  
ATOM   4317  CD  PRO A 572      73.518   7.698  55.709  1.00 95.23           C  
ANISOU 4317  CD  PRO A 572    11393  16210   8581   4254  -2028  -3359       C  
ATOM   4318  N   LYS A 573      72.706   7.347  59.418  1.00102.44           N  
ANISOU 4318  N   LYS A 573    11836  18582   8504   4605  -2325  -3808       N  
ATOM   4319  CA  LYS A 573      72.407   7.635  60.821  1.00105.93           C  
ANISOU 4319  CA  LYS A 573    11907  19666   8674   4679  -2366  -4133       C  
ATOM   4320  C   LYS A 573      70.890   7.738  61.029  1.00105.30           C  
ANISOU 4320  C   LYS A 573    12045  19290   8676   4446  -2323  -3777       C  
ATOM   4321  O   LYS A 573      70.317   6.983  61.806  1.00105.45           O  
ANISOU 4321  O   LYS A 573    12244  19605   8217   4632  -2459  -3443       O  
ATOM   4322  CB  LYS A 573      73.097   8.924  61.282  1.00107.77           C  
ANISOU 4322  CB  LYS A 573    11421  20287   9242   4519  -2209  -5007       C  
ATOM   4323  N   LEU A 574      70.243   8.641  60.294  1.00105.53           N  
ANISOU 4323  N   LEU A 574    12063  18737   9297   4061  -2119  -3801       N  
ATOM   4324  CA  LEU A 574      68.788   8.846  60.401  1.00106.62           C  
ANISOU 4324  CA  LEU A 574    12363  18610   9538   3835  -2061  -3498       C  
ATOM   4325  C   LEU A 574      67.990   7.544  60.247  1.00106.15           C  
ANISOU 4325  C   LEU A 574    12892  18372   9071   3925  -2226  -2755       C  
ATOM   4326  O   LEU A 574      67.165   7.211  61.113  1.00109.61           O  
ANISOU 4326  O   LEU A 574    13369  19096   9183   3955  -2296  -2565       O  
ATOM   4327  CB  LEU A 574      68.303   9.873  59.363  1.00104.65           C  
ANISOU 4327  CB  LEU A 574    12095  17696   9970   3488  -1805  -3508       C  
ATOM   4328  N   VAL A 575      68.259   6.816  59.160  1.00101.42           N  
ANISOU 4328  N   VAL A 575    12720  17317   8499   3961  -2272  -2370       N  
ATOM   4329  CA  VAL A 575      67.586   5.542  58.861  1.00100.05           C  
ANISOU 4329  CA  VAL A 575    13120  16868   8026   4006  -2400  -1722       C  
ATOM   4330  C   VAL A 575      67.667   4.579  60.049  1.00104.77           C  
ANISOU 4330  C   VAL A 575    13808  17963   8035   4321  -2555  -1538       C  
ATOM   4331  O   VAL A 575      66.648   4.142  60.578  1.00106.51           O  
ANISOU 4331  O   VAL A 575    14203  18219   8048   4244  -2574  -1189       O  
ATOM   4332  CB  VAL A 575      68.177   4.869  57.590  1.00 98.67           C  
ANISOU 4332  CB  VAL A 575    13321  16236   7934   4079  -2444  -1483       C  
ATOM   4333  CG1 VAL A 575      67.600   3.470  57.380  1.00 96.62           C  
ANISOU 4333  CG1 VAL A 575    13638  15695   7379   4139  -2569   -908       C  
ATOM   4334  CG2 VAL A 575      67.925   5.725  56.349  1.00 91.86           C  
ANISOU 4334  CG2 VAL A 575    12406  14901   7597   3793  -2273  -1525       C  
ATOM   4335  N   VAL A 576      68.885   4.282  60.481  1.00108.86           N  
ANISOU 4335  N   VAL A 576    14174  18915   8273   4692  -2645  -1762       N  
ATOM   4336  CA  VAL A 576      69.120   3.437  61.654  1.00114.17           C  
ANISOU 4336  CA  VAL A 576    14865  20170   8343   5094  -2768  -1589       C  
ATOM   4337  C   VAL A 576      68.429   3.941  62.931  1.00115.45           C  
ANISOU 4337  C   VAL A 576    14652  20920   8294   5064  -2744  -1749       C  
ATOM   4338  O   VAL A 576      67.866   3.159  63.702  1.00114.56           O  
ANISOU 4338  O   VAL A 576    14727  21040   7760   5225  -2791  -1313       O  
ATOM   4339  CB  VAL A 576      70.626   3.329  61.918  1.00118.41           C  
ANISOU 4339  CB  VAL A 576    15138  21226   8626   5519  -2852  -1949       C  
ATOM   4340  CG1 VAL A 576      70.885   2.600  63.228  1.00123.23           C  
ANISOU 4340  CG1 VAL A 576    15669  22587   8566   6006  -2958  -1795       C  
ATOM   4341  CG2 VAL A 576      71.315   2.632  60.745  1.00117.95           C  
ANISOU 4341  CG2 VAL A 576    15488  20655   8671   5633  -2898  -1727       C  
ATOM   4342  N   SER A 577      68.470   5.253  63.138  1.00117.11           N  
ANISOU 4342  N   SER A 577    14324  21353   8817   4857  -2649  -2374       N  
ATOM   4343  CA  SER A 577      67.848   5.882  64.295  1.00117.91           C  
ANISOU 4343  CA  SER A 577    14000  22033   8768   4818  -2621  -2654       C  
ATOM   4344  C   SER A 577      66.325   5.739  64.259  1.00114.48           C  
ANISOU 4344  C   SER A 577    13853  21254   8391   4529  -2570  -2174       C  
ATOM   4345  O   SER A 577      65.699   5.217  65.177  1.00111.71           O  
ANISOU 4345  O   SER A 577    13533  21308   7602   4654  -2619  -1870       O  
ATOM   4346  CB  SER A 577      68.223   7.360  64.325  1.00119.36           C  
ANISOU 4346  CB  SER A 577    13586  22349   9416   4606  -2491  -3474       C  
ATOM   4347  OG  SER A 577      67.653   7.992  65.459  1.00126.99           O  
ANISOU 4347  OG  SER A 577    14106  23904  10241   4589  -2469  -3830       O  
ATOM   4348  N   THR A 578      65.738   6.198  63.169  1.00112.67           N  
ANISOU 4348  N   THR A 578    13812  20313   8683   4155  -2460  -2090       N  
ATOM   4349  CA  THR A 578      64.300   6.120  62.995  1.00112.75           C  
ANISOU 4349  CA  THR A 578    14060  20010   8770   3862  -2407  -1680       C  
ATOM   4350  C   THR A 578      63.758   4.698  63.087  1.00111.82           C  
ANISOU 4350  C   THR A 578    14460  19772   8252   3930  -2496   -965       C  
ATOM   4351  O   THR A 578      62.730   4.469  63.719  1.00118.09           O  
ANISOU 4351  O   THR A 578    15283  20760   8825   3832  -2483   -685       O  
ATOM   4352  CB  THR A 578      63.900   6.759  61.664  1.00111.93           C  
ANISOU 4352  CB  THR A 578    14083  19198   9249   3527  -2275  -1672       C  
ATOM   4353  OG1 THR A 578      63.984   8.180  61.820  1.00114.29           O  
ANISOU 4353  OG1 THR A 578    13883  19594   9949   3411  -2126  -2266       O  
ATOM   4354  CG2 THR A 578      62.484   6.352  61.236  1.00112.06           C  
ANISOU 4354  CG2 THR A 578    14443  18865   9270   3256  -2252  -1148       C  
ATOM   4355  N   GLN A 579      64.440   3.744  62.473  1.00107.27           N  
ANISOU 4355  N   GLN A 579    14285  18870   7603   4092  -2565   -679       N  
ATOM   4356  CA  GLN A 579      63.980   2.365  62.537  1.00108.32           C  
ANISOU 4356  CA  GLN A 579    14936  18787   7435   4150  -2608    -20       C  
ATOM   4357  C   GLN A 579      63.842   1.879  63.973  1.00112.52           C  
ANISOU 4357  C   GLN A 579    15349  19982   7421   4434  -2634    189       C  
ATOM   4358  O   GLN A 579      62.820   1.294  64.331  1.00109.99           O  
ANISOU 4358  O   GLN A 579    15247  19607   6936   4288  -2587    662       O  
ATOM   4359  CB  GLN A 579      64.912   1.450  61.752  1.00109.36           C  
ANISOU 4359  CB  GLN A 579    15473  18511   7567   4366  -2674    167       C  
ATOM   4360  CG  GLN A 579      64.665   1.478  60.252  1.00106.37           C  
ANISOU 4360  CG  GLN A 579    15380  17403   7632   4053  -2644    216       C  
ATOM   4361  CD  GLN A 579      65.468   0.428  59.526  1.00106.69           C  
ANISOU 4361  CD  GLN A 579    15854  17053   7630   4278  -2716    427       C  
ATOM   4362  OE1 GLN A 579      66.687   0.371  59.658  1.00107.09           O  
ANISOU 4362  OE1 GLN A 579    15795  17351   7545   4647  -2781    216       O  
ATOM   4363  NE2 GLN A 579      64.788  -0.412  58.758  1.00107.78           N  
ANISOU 4363  NE2 GLN A 579    16461  16608   7881   4059  -2702    803       N  
ATOM   4364  N   THR A 580      64.876   2.124  64.779  1.00117.78           N  
ANISOU 4364  N   THR A 580    15638  21322   7792   4844  -2697   -165       N  
ATOM   4365  CA  THR A 580      64.875   1.773  66.204  1.00125.80           C  
ANISOU 4365  CA  THR A 580    16431  23150   8217   5207  -2723    -22       C  
ATOM   4366  C   THR A 580      63.742   2.472  66.943  1.00129.26           C  
ANISOU 4366  C   THR A 580    16530  23973   8609   4963  -2663   -127       C  
ATOM   4367  O   THR A 580      63.028   1.849  67.741  1.00127.88           O  
ANISOU 4367  O   THR A 580    16449  24093   8048   5037  -2630    354       O  
ATOM   4368  CB  THR A 580      66.192   2.192  66.885  1.00130.18           C  
ANISOU 4368  CB  THR A 580    16481  24500   8484   5663  -2808   -577       C  
ATOM   4369  OG1 THR A 580      67.294   1.738  66.095  1.00131.58           O  
ANISOU 4369  OG1 THR A 580    16899  24341   8753   5866  -2864   -591       O  
ATOM   4370  CG2 THR A 580      66.301   1.629  68.322  1.00134.81           C  
ANISOU 4370  CG2 THR A 580    16865  26012   8344   6162  -2842   -336       C  
ATOM   4371  N   ALA A 581      63.582   3.765  66.651  1.00129.21           N  
ANISOU 4371  N   ALA A 581    16137  23939   9019   4680  -2628   -739       N  
ATOM   4372  CA  ALA A 581      62.564   4.599  67.290  1.00129.24           C  
ANISOU 4372  CA  ALA A 581    15767  24301   9038   4467  -2568   -959       C  
ATOM   4373  C   ALA A 581      61.159   4.047  67.071  1.00127.63           C  
ANISOU 4373  C   ALA A 581    15944  23712   8839   4143  -2504   -331       C  
ATOM   4374  O   ALA A 581      60.369   3.983  68.006  1.00129.30           O  
ANISOU 4374  O   ALA A 581    15985  24434   8711   4157  -2481   -159       O  
ATOM   4375  CB  ALA A 581      62.650   6.026  66.766  1.00125.26           C  
ANISOU 4375  CB  ALA A 581    14893  23594   9107   4208  -2495  -1662       C  
ATOM   4376  N   LEU A 582      60.871   3.630  65.838  1.00125.87           N  
ANISOU 4376  N   LEU A 582    16203  22649   8975   3858  -2472    -13       N  
ATOM   4377  CA  LEU A 582      59.544   3.119  65.465  1.00124.39           C  
ANISOU 4377  CA  LEU A 582    16355  22063   8844   3488  -2405    507       C  
ATOM   4378  C   LEU A 582      59.341   1.638  65.827  1.00126.74           C  
ANISOU 4378  C   LEU A 582    17102  22284   8771   3585  -2393   1220       C  
ATOM   4379  O   LEU A 582      58.262   1.091  65.613  1.00124.48           O  
ANISOU 4379  O   LEU A 582    17089  21697   8511   3257  -2319   1658       O  
ATOM   4380  CB  LEU A 582      59.304   3.335  63.960  1.00118.20           C  
ANISOU 4380  CB  LEU A 582    15835  20488   8586   3148  -2371    486       C  
ATOM   4381  N   ALA A 583      60.378   0.993  66.363  1.00131.59           N  
ANISOU 4381  N   ALA A 583    17782  23162   9054   4039  -2444   1336       N  
ATOM   4382  CA  ALA A 583      60.294  -0.404  66.797  1.00136.03           C  
ANISOU 4382  CA  ALA A 583    18771  23642   9273   4219  -2388   2050       C  
ATOM   4383  C   ALA A 583      59.691  -1.279  65.700  1.00135.06           C  
ANISOU 4383  C   ALA A 583    19247  22579   9489   3828  -2318   2481       C  
ATOM   4384  O   ALA A 583      59.807  -2.499  65.737  1.00139.54           O  
ANISOU 4384  O   ALA A 583    20271  22809   9937   3950  -2250   3024       O  
ATOM   4385  CB  ALA A 583      59.487  -0.520  68.091  1.00137.42           C  
ANISOU 4385  CB  ALA A 583    18713  24506   8994   4281  -2312   2357       C  
TER    4386      ALA A 583                                                      
HETATM 4387 CA    CA A 584      27.509  22.775  19.913  1.00 80.51          CA  
HETATM 4388 CA    CA A 585      50.397  12.182  36.252  1.00 77.52          CA  
HETATM 4389 CA    CA A 586      24.896  34.744  21.155  1.00 76.78          CA  
HETATM 4390  O   HOH A 587      48.708  20.775  36.231  1.00 49.18           O  
HETATM 4391  O   HOH A 588      35.576  40.436  41.967  1.00 65.45           O  
HETATM 4392  O   HOH A 589      28.260  21.102  18.284  1.00 69.04           O  
HETATM 4393  O   HOH A 590      24.414  23.924  20.091  1.00 52.55           O  
HETATM 4394  O   HOH A 591      27.361  21.717  21.931  1.00 61.23           O  
HETATM 4395  O   HOH A 592      50.883  10.100  37.194  1.00 91.48           O  
HETATM 4396  O   HOH A 593      48.287  11.492  35.346  1.00 62.24           O  
HETATM 4397  O   HOH A 594      20.958  13.990  35.847  1.00 74.00           O  
HETATM 4398  O   HOH A 595      45.988   7.164  44.264  1.00 42.11           O  
HETATM 4399  O   HOH A 596      44.506  12.135  34.779  1.00 52.73           O  
HETATM 4400  O   HOH A 597      56.795  21.807  28.687  1.00 55.61           O  
HETATM 4401  O   HOH A 598      40.410  32.010  46.013  1.00 51.81           O  
HETATM 4402  O   HOH A 599      35.497  29.627  38.263  1.00 57.83           O  
HETATM 4403  O   HOH A 600      27.915  46.098  29.235  1.00 73.82           O  
HETATM 4404  O   HOH A 601      45.919  22.551   6.060  1.00 79.37           O  
HETATM 4405  O   HOH A 602      43.001  23.320   6.748  1.00 73.22           O  
HETATM 4406  O   HOH A 603      21.076  33.036  28.563  1.00 53.80           O  
HETATM 4407  O   HOH A 604      50.216  11.978  33.912  1.00 66.60           O  
HETATM 4408  O   HOH A 605      23.879  32.402  20.794  1.00 57.05           O  
HETATM 4409  O   HOH A 606      45.797  35.259   6.145  1.00 76.47           O  
HETATM 4410  O   HOH A 607      25.636  36.919  21.578  1.00 73.86           O  
HETATM 4411  O   HOH A 608      48.128  26.963   5.658  1.00 55.63           O  
HETATM 4412  O   HOH A 609      39.944  18.403  57.298  1.00 53.71           O  
ENDMDL                                                                          
MASTER        0    0    0   63    0    0   13    6 8810    2    0   90          
END                                                                             



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