CNRS Nantes University UFIP UFIP
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***  3qh3  ***

elNémo ID: 191121123327129296

Job options:

ID        	=	 191121123327129296
JOBID     	=	 3qh3
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 3qh3

HEADER    IMMUNE SYSTEM                           25-JAN-11   XXXX              
TITLE     THE CRYSTAL STRUCTURE OF TCR A6                                       
KEYWDS    TAX PEPTIDE, TEL1P PEPTIDE, NONAPEPTIDE, MHC CLASS I, HLA-A2, TCR A6, 
KEYWDS   2 CROSS-REACTIVITY, IMMUNE SYSTEM                                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    O.Y.BORBULEVYCH, B.M.BAKER                                            
JRNL        AUTH   D.R.SCOTT, O.Y.BORBULEVYCH, K.H.PIEPENBRINK, S.A.CORCELLI,   
JRNL        AUTH 2 B.M.BAKER                                                    
JRNL        TITL   DISPARATE DEGREES OF HYPERVARIABLE LOOP FLEXIBILITY CONTROL  
JRNL        TITL 2 T-CELL RECEPTOR CROSS-REACTIVITY, SPECIFICITY, AND BINDING   
JRNL        TITL 3 MECHANISM.                                                   
JRNL        REF    J.MOL.BIOL.                   V. 414   385 2011              
JRNL        REFN   ASTM JMOBAK  UK ISSN 0022-2836                               
JRNL        PMID   22019736                                                     
JRNL        DOI    10.1016/J.JMB.2011.10.006                                    
SEQRES   1 A  194  LYS GLU VAL GLU GLN ASN SER GLY PRO LEU SER VAL PRO          
SEQRES   2 A  194  GLU GLY ALA ILE ALA SER LEU ASN CYS THR TYR SER ASP          
SEQRES   3 A  194  ARG GLY SER GLN SER PHE PHE TRP TYR ARG GLN TYR SER          
SEQRES   4 A  194  GLY LYS SER PRO GLU LEU ILE MET SER ILE TYR SER ASN          
SEQRES   5 A  194  GLY ASP LYS GLU ASP GLY ARG PHE THR ALA GLN LEU ASN          
SEQRES   6 A  194  LYS ALA SER GLN TYR VAL SER LEU LEU ILE ARG ASP SER          
SEQRES   7 A  194  GLN PRO SER ASP SER ALA THR TYR LEU CYS ALA VAL THR          
SEQRES   8 A  194  THR ASP SER TRP GLY LYS LEU GLN PHE GLY ALA GLY THR          
SEQRES   9 A  194  GLN VAL VAL VAL THR PRO ASP ILE GLN ASN PRO ASP PRO          
SEQRES  10 A  194  ALA VAL TYR GLN LEU ARG ASP SER LYS SER SER ASP LYS          
SEQRES  11 A  194  SER VAL CYS LEU PHE THR ASP PHE ASP SER GLN THR ASN          
SEQRES  12 A  194  VAL SER GLN SER LYS ASP SER ASP VAL TYR ILE THR ASP          
SEQRES  13 A  194  LYS CYS VAL LEU ASP MET ARG SER MET ASP PHE LYS SER          
SEQRES  14 A  194  ASN SER ALA VAL ALA TRP SER ASN LYS SER ASP PHE ALA          
SEQRES  15 A  194  CYS ALA ASN ALA PHE ASN ASN SER ILE ILE PRO GLU              
SEQRES   1 B  245  ASN ALA GLY VAL THR GLN THR PRO LYS PHE GLN VAL LEU          
SEQRES   2 B  245  LYS THR GLY GLN SER MET THR LEU GLN CYS ALA GLN ASP          
SEQRES   3 B  245  MET ASN HIS GLU TYR MET SER TRP TYR ARG GLN ASP PRO          
SEQRES   4 B  245  GLY MET GLY LEU ARG LEU ILE HIS TYR SER VAL GLY ALA          
SEQRES   5 B  245  GLY ILE THR ASP GLN GLY GLU VAL PRO ASN GLY TYR ASN          
SEQRES   6 B  245  VAL SER ARG SER THR THR GLU ASP PHE PRO LEU ARG LEU          
SEQRES   7 B  245  LEU SER ALA ALA PRO SER GLN THR SER VAL TYR PHE CYS          
SEQRES   8 B  245  ALA SER ARG PRO GLY LEU ALA GLY GLY ARG PRO GLU GLN          
SEQRES   9 B  245  TYR PHE GLY PRO GLY THR ARG LEU THR VAL THR GLU ASP          
SEQRES  10 B  245  LEU LYS ASN VAL PHE PRO PRO GLU VAL ALA VAL PHE GLU          
SEQRES  11 B  245  PRO SER GLU ALA GLU ILE SER HIS THR GLN LYS ALA THR          
SEQRES  12 B  245  LEU VAL CYS LEU ALA THR GLY PHE TYR PRO ASP HIS VAL          
SEQRES  13 B  245  GLU LEU SER TRP TRP VAL ASN GLY LYS GLU VAL HIS SER          
SEQRES  14 B  245  GLY VAL CYS THR ASP PRO GLN PRO LEU LYS GLU GLN PRO          
SEQRES  15 B  245  ALA LEU ASN ASP SER ARG TYR ALA LEU SER SER ARG LEU          
SEQRES  16 B  245  ARG VAL SER ALA THR PHE TRP GLN ASP PRO ARG ASN HIS          
SEQRES  17 B  245  PHE ARG CYS GLN VAL GLN PHE TYR GLY LEU SER GLU ASN          
SEQRES  18 B  245  ASP GLU TRP THR GLN ASP ARG ALA LYS PRO VAL THR GLN          
SEQRES  19 B  245  ILE VAL SER ALA GLU ALA TRP GLY ARG ALA ASP                  
SEQRES   1 C  194  LYS GLU VAL GLU GLN ASN SER GLY PRO LEU SER VAL PRO          
SEQRES   2 C  194  GLU GLY ALA ILE ALA SER LEU ASN CYS THR TYR SER ASP          
SEQRES   3 C  194  ARG GLY SER GLN SER PHE PHE TRP TYR ARG GLN TYR SER          
SEQRES   4 C  194  GLY LYS SER PRO GLU LEU ILE MET SER ILE TYR SER ASN          
SEQRES   5 C  194  GLY ASP LYS GLU ASP GLY ARG PHE THR ALA GLN LEU ASN          
SEQRES   6 C  194  LYS ALA SER GLN TYR VAL SER LEU LEU ILE ARG ASP SER          
SEQRES   7 C  194  GLN PRO SER ASP SER ALA THR TYR LEU CYS ALA VAL THR          
SEQRES   8 C  194  THR ASP SER TRP GLY LYS LEU GLN PHE GLY ALA GLY THR          
SEQRES   9 C  194  GLN VAL VAL VAL THR PRO ASP ILE GLN ASN PRO ASP PRO          
SEQRES  10 C  194  ALA VAL TYR GLN LEU ARG ASP SER LYS SER SER ASP LYS          
SEQRES  11 C  194  SER VAL CYS LEU PHE THR ASP PHE ASP SER GLN THR ASN          
SEQRES  12 C  194  VAL SER GLN SER LYS ASP SER ASP VAL TYR ILE THR ASP          
SEQRES  13 C  194  LYS CYS VAL LEU ASP MET ARG SER MET ASP PHE LYS SER          
SEQRES  14 C  194  ASN SER ALA VAL ALA TRP SER ASN LYS SER ASP PHE ALA          
SEQRES  15 C  194  CYS ALA ASN ALA PHE ASN ASN SER ILE ILE PRO GLU              
SEQRES   1 D  245  ASN ALA GLY VAL THR GLN THR PRO LYS PHE GLN VAL LEU          
SEQRES   2 D  245  LYS THR GLY GLN SER MET THR LEU GLN CYS ALA GLN ASP          
SEQRES   3 D  245  MET ASN HIS GLU TYR MET SER TRP TYR ARG GLN ASP PRO          
SEQRES   4 D  245  GLY MET GLY LEU ARG LEU ILE HIS TYR SER VAL GLY ALA          
SEQRES   5 D  245  GLY ILE THR ASP GLN GLY GLU VAL PRO ASN GLY TYR ASN          
SEQRES   6 D  245  VAL SER ARG SER THR THR GLU ASP PHE PRO LEU ARG LEU          
SEQRES   7 D  245  LEU SER ALA ALA PRO SER GLN THR SER VAL TYR PHE CYS          
SEQRES   8 D  245  ALA SER ARG PRO GLY LEU ALA GLY GLY ARG PRO GLU GLN          
SEQRES   9 D  245  TYR PHE GLY PRO GLY THR ARG LEU THR VAL THR GLU ASP          
SEQRES  10 D  245  LEU LYS ASN VAL PHE PRO PRO GLU VAL ALA VAL PHE GLU          
SEQRES  11 D  245  PRO SER GLU ALA GLU ILE SER HIS THR GLN LYS ALA THR          
SEQRES  12 D  245  LEU VAL CYS LEU ALA THR GLY PHE TYR PRO ASP HIS VAL          
SEQRES  13 D  245  GLU LEU SER TRP TRP VAL ASN GLY LYS GLU VAL HIS SER          
SEQRES  14 D  245  GLY VAL CYS THR ASP PRO GLN PRO LEU LYS GLU GLN PRO          
SEQRES  15 D  245  ALA LEU ASN ASP SER ARG TYR ALA LEU SER SER ARG LEU          
SEQRES  16 D  245  ARG VAL SER ALA THR PHE TRP GLN ASP PRO ARG ASN HIS          
SEQRES  17 D  245  PHE ARG CYS GLN VAL GLN PHE TYR GLY LEU SER GLU ASN          
SEQRES  18 D  245  ASP GLU TRP THR GLN ASP ARG ALA LYS PRO VAL THR GLN          
SEQRES  19 D  245  ILE VAL SER ALA GLU ALA TRP GLY ARG ALA ASP                  
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETNAM     GOL GLYCEROL                                                         
HETSYN     EDO ETHYLENE GLYCOL                                                  
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   5  EDO    10(C2 H6 O2)                                                 
FORMUL   8  GOL    5(C3 H8 O3)                                                  
FORMUL  20  HOH   *256(H2 O)                                                    
HELIX    1   1 GLN A   79  SER A   83  5                                   5    
HELIX    2   2 ARG A  163  ASP A  166  5                                   4    
HELIX    3   3 ALA A  182  ASN A  188  1                                   7    
HELIX    4   4 ALA B   82  THR B   86  5                                   5    
HELIX    5   5 ASP B  117  VAL B  121  5                                   5    
HELIX    6   6 SER B  132  GLN B  140  1                                   9    
HELIX    7   7 ALA B  199  GLN B  203  1                                   5    
HELIX    8   8 GLN C   79  SER C   83  5                                   5    
HELIX    9   9 ALA C  182  PHE C  187  1                                   6    
HELIX   10  10 ALA D   82  THR D   86  5                                   5    
HELIX   11  11 ASP D  117  VAL D  121  5                                   5    
HELIX   12  12 SER D  132  GLN D  140  1                                   9    
HELIX   13  13 ALA D  199  ASP D  204  1                                   6    
SHEET    1   A 5 VAL A   3  GLN A   5  0                                        
SHEET    2   A 5 ALA A  18  TYR A  24 -1  O  THR A  23   N  GLU A   4           
SHEET    3   A 5 TYR A  70  ILE A  75 -1  O  ILE A  75   N  ALA A  18           
SHEET    4   A 5 PHE A  60  ASN A  65 -1  N  ASN A  65   O  TYR A  70           
SHEET    5   A 5 GLY A  53  ASP A  57 -1  N  ASP A  57   O  PHE A  60           
SHEET    1   B 5 LEU A  10  PRO A  13  0                                        
SHEET    2   B 5 THR A 104  THR A 109  1  O  VAL A 107   N  LEU A  10           
SHEET    3   B 5 ALA A  84  THR A  91 -1  N  ALA A  84   O  VAL A 106           
SHEET    4   B 5 PHE A  32  GLN A  37 -1  N  GLN A  37   O  THR A  85           
SHEET    5   B 5 GLU A  44  ILE A  49 -1  O  ILE A  46   N  TRP A  34           
SHEET    1   C 4 LEU A  10  PRO A  13  0                                        
SHEET    2   C 4 THR A 104  THR A 109  1  O  VAL A 107   N  LEU A  10           
SHEET    3   C 4 ALA A  84  THR A  91 -1  N  ALA A  84   O  VAL A 106           
SHEET    4   C 4 LEU A  98  PHE A 100 -1  O  GLN A  99   N  VAL A  90           
SHEET    1   D 8 TYR A 153  ILE A 154  0                                        
SHEET    2   D 8 PHE A 167  TRP A 175 -1  O  TRP A 175   N  TYR A 153           
SHEET    3   D 8 SER A 131  THR A 136 -1  N  CYS A 133   O  ALA A 174           
SHEET    4   D 8 ALA A 118  ASP A 124 -1  N  TYR A 120   O  LEU A 134           
SHEET    5   D 8 GLU B 125  GLU B 130 -1  O  GLU B 130   N  ARG A 123           
SHEET    6   D 8 LYS B 141  PHE B 151 -1  O  LEU B 147   N  ALA B 127           
SHEET    7   D 8 TYR B 189  SER B 198 -1  O  SER B 193   N  CYS B 146           
SHEET    8   D 8 VAL B 171  THR B 173 -1  N  CYS B 172   O  ARG B 194           
SHEET    1   E 8 CYS A 158  MET A 162  0                                        
SHEET    2   E 8 PHE A 167  TRP A 175 -1  O  PHE A 167   N  MET A 162           
SHEET    3   E 8 SER A 131  THR A 136 -1  N  CYS A 133   O  ALA A 174           
SHEET    4   E 8 ALA A 118  ASP A 124 -1  N  TYR A 120   O  LEU A 134           
SHEET    5   E 8 GLU B 125  GLU B 130 -1  O  GLU B 130   N  ARG A 123           
SHEET    6   E 8 LYS B 141  PHE B 151 -1  O  LEU B 147   N  ALA B 127           
SHEET    7   E 8 TYR B 189  SER B 198 -1  O  SER B 193   N  CYS B 146           
SHEET    8   E 8 LEU B 178  LYS B 179 -1  N  LEU B 178   O  ALA B 190           
SHEET    1   F 4 VAL B   4  THR B   7  0                                        
SHEET    2   F 4 MET B  19  GLN B  25 -1  O  GLN B  22   N  THR B   7           
SHEET    3   F 4 LEU B  76  LEU B  78 -1  O  LEU B  76   N  LEU B  21           
SHEET    4   F 4 ASN B  65  VAL B  66 -1  N  ASN B  65   O  ARG B  77           
SHEET    1   G 6 PHE B  10  LYS B  14  0                                        
SHEET    2   G 6 THR B 110  THR B 115  1  O  THR B 115   N  LEU B  13           
SHEET    3   G 6 SER B  87  ARG B  94 -1  N  SER B  87   O  LEU B 112           
SHEET    4   G 6 TYR B  31  GLN B  37 -1  N  TYR B  35   O  PHE B  90           
SHEET    5   G 6 LEU B  43  GLY B  51 -1  O  ILE B  46   N  TRP B  34           
SHEET    6   G 6 ILE B  54  GLN B  57 -1  O  ASP B  56   N  TYR B  48           
SHEET    1   H 4 PHE B  10  LYS B  14  0                                        
SHEET    2   H 4 THR B 110  THR B 115  1  O  THR B 115   N  LEU B  13           
SHEET    3   H 4 SER B  87  ARG B  94 -1  N  SER B  87   O  LEU B 112           
SHEET    4   H 4 TYR B 105  PHE B 106 -1  O  TYR B 105   N  SER B  93           
SHEET    1   I 4 LYS B 165  VAL B 167  0                                        
SHEET    2   I 4 VAL B 156  VAL B 162 -1  N  VAL B 162   O  LYS B 165           
SHEET    3   I 4 HIS B 208  PHE B 215 -1  O  ARG B 210   N  TRP B 161           
SHEET    4   I 4 GLN B 234  TRP B 241 -1  O  GLN B 234   N  PHE B 215           
SHEET    1   J 5 VAL C   3  GLN C   5  0                                        
SHEET    2   J 5 ALA C  18  TYR C  24 -1  O  THR C  23   N  GLU C   4           
SHEET    3   J 5 TYR C  70  ILE C  75 -1  O  VAL C  71   N  CYS C  22           
SHEET    4   J 5 PHE C  60  ASN C  65 -1  N  THR C  61   O  LEU C  74           
SHEET    5   J 5 GLY C  53  ASP C  57 -1  N  LYS C  55   O  ALA C  62           
SHEET    1   K 5 LEU C  10  PRO C  13  0                                        
SHEET    2   K 5 THR C 104  THR C 109  1  O  VAL C 107   N  LEU C  10           
SHEET    3   K 5 ALA C  84  THR C  92 -1  N  ALA C  84   O  VAL C 106           
SHEET    4   K 5 SER C  29  GLN C  37 -1  N  GLN C  30   O  THR C  91           
SHEET    5   K 5 GLU C  44  ILE C  49 -1  O  GLU C  44   N  ARG C  36           
SHEET    1   L 4 LEU C  10  PRO C  13  0                                        
SHEET    2   L 4 THR C 104  THR C 109  1  O  VAL C 107   N  LEU C  10           
SHEET    3   L 4 ALA C  84  THR C  92 -1  N  ALA C  84   O  VAL C 106           
SHEET    4   L 4 GLN C  99  PHE C 100 -1  O  GLN C  99   N  VAL C  90           
SHEET    1   M 4 ALA C 118  ARG C 123  0                                        
SHEET    2   M 4 SER C 131  THR C 136 -1  O  LEU C 134   N  TYR C 120           
SHEET    3   M 4 PHE C 167  SER C 176 -1  O  ALA C 174   N  CYS C 133           
SHEET    4   M 4 VAL C 152  ILE C 154 -1  N  TYR C 153   O  TRP C 175           
SHEET    1   N 4 ALA C 118  ARG C 123  0                                        
SHEET    2   N 4 SER C 131  THR C 136 -1  O  LEU C 134   N  TYR C 120           
SHEET    3   N 4 PHE C 167  SER C 176 -1  O  ALA C 174   N  CYS C 133           
SHEET    4   N 4 CYS C 158  MET C 162 -1  N  MET C 162   O  PHE C 167           
SHEET    1   O 4 VAL D   4  THR D   7  0                                        
SHEET    2   O 4 MET D  19  GLN D  25 -1  O  GLN D  22   N  THR D   7           
SHEET    3   O 4 LEU D  76  LEU D  78 -1  O  LEU D  76   N  LEU D  21           
SHEET    4   O 4 TYR D  64  VAL D  66 -1  N  ASN D  65   O  ARG D  77           
SHEET    1   P 6 PHE D  10  LYS D  14  0                                        
SHEET    2   P 6 THR D 110  THR D 115  1  O  THR D 115   N  LEU D  13           
SHEET    3   P 6 SER D  87  ARG D  94 -1  N  SER D  87   O  LEU D 112           
SHEET    4   P 6 TYR D  31  ASP D  38 -1  N  GLN D  37   O  VAL D  88           
SHEET    5   P 6 GLY D  42  GLY D  51 -1  O  ILE D  46   N  TRP D  34           
SHEET    6   P 6 ILE D  54  GLN D  57 -1  O  ASP D  56   N  TYR D  48           
SHEET    1   Q 4 PHE D  10  LYS D  14  0                                        
SHEET    2   Q 4 THR D 110  THR D 115  1  O  THR D 115   N  LEU D  13           
SHEET    3   Q 4 SER D  87  ARG D  94 -1  N  SER D  87   O  LEU D 112           
SHEET    4   Q 4 TYR D 105  PHE D 106 -1  O  TYR D 105   N  SER D  93           
SHEET    1   R 4 GLU D 125  PHE D 129  0                                        
SHEET    2   R 4 LYS D 141  PHE D 151 -1  O  VAL D 145   N  PHE D 129           
SHEET    3   R 4 TYR D 189  SER D 198 -1  O  VAL D 197   N  ALA D 142           
SHEET    4   R 4 VAL D 171  THR D 173 -1  N  CYS D 172   O  ARG D 194           
SHEET    1   S 4 GLU D 125  PHE D 129  0                                        
SHEET    2   S 4 LYS D 141  PHE D 151 -1  O  VAL D 145   N  PHE D 129           
SHEET    3   S 4 TYR D 189  SER D 198 -1  O  VAL D 197   N  ALA D 142           
SHEET    4   S 4 LEU D 178  LYS D 179 -1  N  LEU D 178   O  ALA D 190           
SHEET    1   T 4 LYS D 165  VAL D 167  0                                        
SHEET    2   T 4 VAL D 156  VAL D 162 -1  N  VAL D 162   O  LYS D 165           
SHEET    3   T 4 HIS D 208  PHE D 215 -1  O  GLN D 212   N  SER D 159           
SHEET    4   T 4 GLN D 234  TRP D 241 -1  O  GLN D 234   N  PHE D 215           
SSBOND   1 CYS A   22    CYS A   88                          1555   1555  2.00  
SSBOND   2 CYS A  133    CYS A  183                          1555   1555  2.04  
SSBOND   3 CYS A  158    CYS B  172                          1555   1555  2.06  
SSBOND   4 CYS B   23    CYS B   91                          1555   1555  2.00  
SSBOND   5 CYS B  146    CYS B  211                          1555   1555  2.00  
SSBOND   6 CYS C   22    CYS C   88                          1555   1555  2.07  
SSBOND   7 CYS C  133    CYS C  183                          1555   1555  2.07  
SSBOND   8 CYS C  158    CYS D  172                          1555   1555  2.13  
SSBOND   9 CYS D   23    CYS D   91                          1555   1555  1.98  
SSBOND  10 CYS D  146    CYS D  211                          1555   1555  1.91  
CISPEP   1 GLY A    8    PRO A    9          1         0.90                     
CISPEP   2 THR B    7    PRO B    8          1       -10.43                     
CISPEP   3 TYR B  152    PRO B  153          1         2.44                     
CISPEP   4 GLY C    8    PRO C    9          1         4.64                     
CISPEP   5 THR D    7    PRO D    8          1        -7.39                     
CISPEP   6 TYR D  152    PRO D  153          1        -2.75                     
SITE     1 AC1  2 ARG A  59  PHE A  60                                          
SITE     1 AC2  6 PRO A  43  GLU A  44  LEU A  45  GLU B 103                    
SITE     2 AC2  6 GLN B 104  PHE B 106                                          
SITE     1 AC3  3 TYR A  50  SER A  51  LYS A  55                               
SITE     1 AC4  5 SER A   7  LEU A  10  SER D 237  ALA D 238                    
SITE     2 AC4  5 HOH D 306                                                     
SITE     1 AC5  3 VAL B 167  HIS B 168  SER B 169                               
SITE     1 AC6  4 SER A 125  ALA B 238  GLU B 239  EDO B 248                    
SITE     1 AC7  7 ASP A 124  SER A 125  VAL B 126  ALA B 127                    
SITE     2 AC7  7 VAL B 128  ALA B 238  EDO B 247                               
SITE     1 AC8  3 PRO B 124  GLU B 125  HOH B 311                               
SITE     1 AC9  2 GLY C  40  HOH C 223                                          
SITE     1 BC1  1 ARG C  59                                                     
SITE     1 BC2  6 LEU C 122  ARG C 123  HOH C 250  GLU D 130                    
SITE     2 BC2  6 PRO D 131  ARG D 243                                          
SITE     1 BC3  4 ASP D 117  LEU D 118  GLU D 223  THR D 225                    
SITE     1 BC4  5 GLY C  40  LYS D   9  PRO D 108  GLY D 109                    
SITE     2 BC4  5 ARG D 111                                                     
SITE     1 BC5  2 THR D  20  GLN D  22                                          
SITE     1 BC6  1 ARG D 228                                                     
CRYST1   91.247   51.735   96.336  90.00 105.05  90.00 P 1 21 1      4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.010959  0.000000  0.002947        0.00000                         
SCALE2      0.000000  0.019329  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010749        0.00000                         
MODEL        1                                                                  
ATOM      1  N   LYS A   1      73.171  47.395  55.704  1.00 66.58           N  
ANISOU    1  N   LYS A   1     8351  10958   5988   -281   2371    845       N  
ATOM      2  CA  LYS A   1      73.090  47.946  57.081  1.00 64.19           C  
ANISOU    2  CA  LYS A   1     7936  10403   6048   -271   2155    935       C  
ATOM      3  C   LYS A   1      72.436  47.007  58.106  1.00 61.50           C  
ANISOU    3  C   LYS A   1     7671   9841   5852   -179   2058    681       C  
ATOM      4  O   LYS A   1      71.520  46.224  57.805  1.00 61.69           O  
ANISOU    4  O   LYS A   1     7870   9866   5701   -175   2036    464       O  
ATOM      5  CB  LYS A   1      72.357  49.282  57.109  1.00 64.01           C  
ANISOU    5  CB  LYS A   1     7925  10344   6051   -397   1907   1169       C  
ATOM      6  CG  LYS A   1      73.258  50.487  56.960  1.00 67.60           C  
ANISOU    6  CG  LYS A   1     8225  10843   6615   -487   1931   1485       C  
ATOM      7  CD  LYS A   1      72.421  51.727  56.660  1.00 70.19           C  
ANISOU    7  CD  LYS A   1     8615  11146   6905   -599   1728   1718       C  
ATOM      8  CE  LYS A   1      73.131  52.595  55.638  1.00 73.45           C  
ANISOU    8  CE  LYS A   1     8958  11754   7193   -707   1842   2016       C  
ATOM      9  NZ  LYS A   1      72.130  53.353  54.834  1.00 75.26           N  
ANISOU    9  NZ  LYS A   1     9300  12068   7225   -781   1704   2203       N  
ATOM     10  N   GLU A   2      72.925  47.123  59.325  1.00 57.83           N  
ANISOU   10  N   GLU A   2     7070   9199   5703   -126   1991    723       N  
ATOM     11  CA  GLU A   2      72.595  46.208  60.370  1.00 55.06           C  
ANISOU   11  CA  GLU A   2     6751   8654   5513    -26   1938    525       C  
ATOM     12  C   GLU A   2      72.044  47.072  61.521  1.00 50.19           C  
ANISOU   12  C   GLU A   2     6097   7861   5111    -84   1667    622       C  
ATOM     13  O   GLU A   2      72.654  48.066  61.944  1.00 49.98           O  
ANISOU   13  O   GLU A   2     5937   7809   5244   -148   1600    821       O  
ATOM     14  CB  GLU A   2      73.871  45.409  60.748  1.00 56.70           C  
ANISOU   14  CB  GLU A   2     6811   8852   5880    116   2155    493       C  
ATOM     15  CG  GLU A   2      73.849  44.574  62.066  1.00 57.23           C  
ANISOU   15  CG  GLU A   2     6846   8710   6186    233   2098    373       C  
ATOM     16  CD  GLU A   2      75.130  44.757  62.938  1.00 60.98           C  
ANISOU   16  CD  GLU A   2     7058   9181   6928    291   2128    543       C  
ATOM     17  OE1 GLU A   2      74.964  45.072  64.143  1.00 60.05           O  
ANISOU   17  OE1 GLU A   2     6881   8934   6998    259   1925    588       O  
ATOM     18  OE2 GLU A   2      76.289  44.618  62.429  1.00 62.62           O  
ANISOU   18  OE2 GLU A   2     7109   9534   7146    358   2350    639       O  
ATOM     19  N   VAL A   3      70.844  46.739  61.960  1.00 45.84           N  
ANISOU   19  N   VAL A   3     5674   7195   4545    -79   1517    480       N  
ATOM     20  CA  VAL A   3      70.414  47.114  63.270  1.00 40.53           C  
ANISOU   20  CA  VAL A   3     4973   6333   4092    -80   1322    491       C  
ATOM     21  C   VAL A   3      70.095  45.734  63.795  1.00 40.09           C  
ANISOU   21  C   VAL A   3     4984   6186   4062     19   1369    262       C  
ATOM     22  O   VAL A   3      69.331  44.976  63.168  1.00 41.24           O  
ANISOU   22  O   VAL A   3     5271   6368   4026     18   1406    101       O  
ATOM     23  CB  VAL A   3      69.122  47.999  63.286  1.00 40.07           C  
ANISOU   23  CB  VAL A   3     5004   6226   3992   -154   1112    552       C  
ATOM     24  CG1 VAL A   3      68.581  48.132  64.715  1.00 33.81           C  
ANISOU   24  CG1 VAL A   3     4206   5232   3406   -128    950    500       C  
ATOM     25  CG2 VAL A   3      69.347  49.380  62.669  1.00 39.59           C  
ANISOU   25  CG2 VAL A   3     4904   6228   3910   -247   1073    801       C  
ATOM     26  N   GLU A   4      70.627  45.419  64.964  1.00 38.44           N  
ANISOU   26  N   GLU A   4     4678   5856   4070     86   1352    254       N  
ATOM     27  CA  GLU A   4      70.558  44.079  65.486  1.00 38.31           C  
ANISOU   27  CA  GLU A   4     4704   5741   4110    197   1427     81       C  
ATOM     28  C   GLU A   4      70.195  44.145  66.963  1.00 35.81           C  
ANISOU   28  C   GLU A   4     4352   5272   3980    206   1253     83       C  
ATOM     29  O   GLU A   4      70.917  44.764  67.744  1.00 34.83           O  
ANISOU   29  O   GLU A   4     4088   5135   4007    190   1187    214       O  
ATOM     30  CB  GLU A   4      71.956  43.481  65.279  1.00 40.46           C  
ANISOU   30  CB  GLU A   4     4848   6072   4451    309   1653    116       C  
ATOM     31  CG  GLU A   4      72.017  42.023  65.090  1.00 43.92           C  
ANISOU   31  CG  GLU A   4     5374   6442   4871    442   1841    -67       C  
ATOM     32  CD  GLU A   4      71.141  41.549  63.959  1.00 47.99           C  
ANISOU   32  CD  GLU A   4     6108   6995   5128    388   1910   -255       C  
ATOM     33  OE1 GLU A   4      71.528  41.789  62.766  1.00 50.13           O  
ANISOU   33  OE1 GLU A   4     6399   7434   5214    358   2053   -239       O  
ATOM     34  OE2 GLU A   4      70.077  40.952  64.295  1.00 44.03           O  
ANISOU   34  OE2 GLU A   4     5750   6372   4604    358   1815   -409       O  
ATOM     35  N   GLN A   5      69.094  43.495  67.343  1.00 34.79           N  
ANISOU   35  N   GLN A   5     4347   5045   3825    215   1181    -63       N  
ATOM     36  CA  GLN A   5      68.684  43.323  68.758  1.00 33.38           C  
ANISOU   36  CA  GLN A   5     4151   4733   3797    236   1048    -82       C  
ATOM     37  C   GLN A   5      68.942  41.919  69.303  1.00 34.94           C  
ANISOU   37  C   GLN A   5     4358   4833   4082    350   1152   -177       C  
ATOM     38  O   GLN A   5      69.133  40.963  68.525  1.00 34.04           O  
ANISOU   38  O   GLN A   5     4316   4714   3903    411   1329   -283       O  
ATOM     39  CB  GLN A   5      67.174  43.566  68.916  1.00 32.00           C  
ANISOU   39  CB  GLN A   5     4090   4517   3551    169    897   -153       C  
ATOM     40  CG  GLN A   5      66.792  44.937  68.530  1.00 33.36           C  
ANISOU   40  CG  GLN A   5     4256   4746   3673     88    788    -40       C  
ATOM     41  CD  GLN A   5      65.340  45.243  68.782  1.00 28.07           C  
ANISOU   41  CD  GLN A   5     3656   4043   2964     53    646    -76       C  
ATOM     42  OE1 GLN A   5      64.678  45.811  67.923  1.00 30.55           O  
ANISOU   42  OE1 GLN A   5     4007   4441   3158      5    600    -27       O  
ATOM     43  NE2 GLN A   5      64.857  44.929  69.961  1.00 26.55           N  
ANISOU   43  NE2 GLN A   5     3466   3749   2873     82    576   -134       N  
ATOM     44  N   ASN A   6      68.938  41.826  70.649  1.00 34.43           N  
ANISOU   44  N   ASN A   6     4233   4685   4160    375   1048   -137       N  
ATOM     45  CA AASN A   6      68.875  40.553  71.388  0.50 36.11           C  
ANISOU   45  CA AASN A   6     4472   4779   4467    472   1100   -200       C  
ATOM     46  CA BASN A   6      68.949  40.541  71.349  0.50 36.02           C  
ANISOU   46  CA BASN A   6     4455   4772   4457    476   1109   -197       C  
ATOM     47  C   ASN A   6      67.694  39.724  70.963  1.00 36.22           C  
ANISOU   47  C   ASN A   6     4667   4710   4384    443   1126   -376       C  
ATOM     48  O   ASN A   6      66.630  40.292  70.677  1.00 36.51           O  
ANISOU   48  O   ASN A   6     4777   4786   4309    335   1012   -422       O  
ATOM     49  CB AASN A   6      68.640  40.816  72.872  0.50 34.99           C  
ANISOU   49  CB AASN A   6     4273   4594   4425    452    934   -133       C  
ATOM     50  CB BASN A   6      68.991  40.760  72.877  0.50 34.93           C  
ANISOU   50  CB BASN A   6     4231   4598   4443    474    959   -105       C  
ATOM     51  CG AASN A   6      69.883  41.093  73.583  0.50 34.63           C  
ANISOU   51  CG AASN A   6     4047   4609   4499    490    915     24       C  
ATOM     52  CG BASN A   6      69.151  42.227  73.250  0.50 32.96           C  
ANISOU   52  CG BASN A   6     3905   4427   4192    367    806     -6       C  
ATOM     53  OD1AASN A   6      69.903  41.885  74.520  0.50 34.94           O  
ANISOU   53  OD1AASN A   6     4029   4678   4568    414    759     93       O  
ATOM     54  OD1BASN A   6      68.178  42.964  73.372  0.50 27.42           O  
ANISOU   54  OD1BASN A   6     3284   3705   3430    283    689    -48       O  
ATOM     55  ND2AASN A   6      70.964  40.460  73.138  0.50 34.42           N  
ANISOU   55  ND2AASN A   6     3923   4614   4538    603   1079     83       N  
ATOM     56  ND2BASN A   6      70.384  42.656  73.401  0.50 35.83           N  
ANISOU   56  ND2BASN A   6     4109   4872   4629    367    817    129       N  
ATOM     57  N   SER A   7      67.839  38.403  70.958  1.00 37.37           N  
ANISOU   57  N   SER A   7     4878   4735   4582    532   1270   -462       N  
ATOM     58  CA  SER A   7      66.699  37.551  70.649  1.00 39.05           C  
ANISOU   58  CA  SER A   7     5272   4850   4714    467   1285   -638       C  
ATOM     59  C   SER A   7      65.935  37.224  71.949  1.00 38.53           C  
ANISOU   59  C   SER A   7     5207   4684   4745    448   1157   -615       C  
ATOM     60  O   SER A   7      66.504  37.249  73.062  1.00 38.92           O  
ANISOU   60  O   SER A   7     5143   4710   4935    526   1116   -482       O  
ATOM     61  CB  SER A   7      67.109  36.330  69.880  1.00 40.47           C  
ANISOU   61  CB  SER A   7     5570   4919   4888    542   1516   -773       C  
ATOM     62  OG  SER A   7      67.728  36.768  68.667  1.00 45.23           O  
ANISOU   62  OG  SER A   7     6169   5654   5360    545   1631   -793       O  
ATOM     63  N   GLY A   8      64.630  37.012  71.814  1.00 38.18           N  
ANISOU   63  N   GLY A   8     5275   4620   4610    327   1081   -725       N  
ATOM     64  CA  GLY A   8      63.767  36.780  72.978  1.00 36.52           C  
ANISOU   64  CA  GLY A   8     5060   4346   4467    290    966   -699       C  
ATOM     65  C   GLY A   8      63.078  35.482  72.657  1.00 36.96           C  
ANISOU   65  C   GLY A   8     5271   4261   4509    229   1050   -848       C  
ATOM     66  O   GLY A   8      63.510  34.779  71.754  1.00 39.12           O  
ANISOU   66  O   GLY A   8     5649   4461   4753    249   1207   -961       O  
ATOM     67  N   PRO A   9      61.989  35.170  73.367  1.00 35.78           N  
ANISOU   67  N   PRO A   9     5145   4074   4376    141    956   -858       N  
ATOM     68  CA  PRO A   9      61.359  35.987  74.448  1.00 33.22           C  
ANISOU   68  CA  PRO A   9     4710   3842   4068    121    794   -745       C  
ATOM     69  C   PRO A   9      62.247  36.028  75.700  1.00 32.88           C  
ANISOU   69  C   PRO A   9     4570   3760   4160    247    791   -597       C  
ATOM     70  O   PRO A   9      62.929  35.040  76.014  1.00 33.16           O  
ANISOU   70  O   PRO A   9     4628   3662   4310    336    899   -563       O  
ATOM     71  CB  PRO A   9      60.047  35.224  74.774  1.00 33.47           C  
ANISOU   71  CB  PRO A   9     4807   3820   4091     -4    756   -808       C  
ATOM     72  CG  PRO A   9      59.898  34.136  73.621  1.00 35.24           C  
ANISOU   72  CG  PRO A   9     5195   3933   4260    -96    873   -983       C  
ATOM     73  CD  PRO A   9      61.290  33.900  73.104  1.00 36.23           C  
ANISOU   73  CD  PRO A   9     5354   3979   4431     44   1028   -997       C  
ATOM     74  N   LEU A  10      62.229  37.150  76.417  1.00 31.35           N  
ANISOU   74  N   LEU A  10     4275   3682   3952    252    669   -506       N  
ATOM     75  CA  LEU A  10      63.063  37.311  77.610  1.00 30.38           C  
ANISOU   75  CA  LEU A  10     4059   3569   3915    334    637   -370       C  
ATOM     76  C   LEU A  10      62.118  37.286  78.785  1.00 30.13           C  
ANISOU   76  C   LEU A  10     4024   3552   3871    287    552   -341       C  
ATOM     77  O   LEU A  10      61.122  38.028  78.769  1.00 28.41           O  
ANISOU   77  O   LEU A  10     3811   3409   3575    218    477   -389       O  
ATOM     78  CB  LEU A  10      63.777  38.656  77.554  1.00 30.24           C  
ANISOU   78  CB  LEU A  10     3951   3667   3869    341    566   -313       C  
ATOM     79  CG  LEU A  10      65.243  38.726  77.135  1.00 32.17           C  
ANISOU   79  CG  LEU A  10     4115   3935   4173    418    635   -238       C  
ATOM     80  CD1 LEU A  10      65.681  37.667  76.143  1.00 35.98           C  
ANISOU   80  CD1 LEU A  10     4650   4330   4691    488    806   -292       C  
ATOM     81  CD2 LEU A  10      65.612  40.133  76.662  1.00 27.76           C  
ANISOU   81  CD2 LEU A  10     3503   3481   3563    367    571   -215       C  
ATOM     82  N   SER A  11      62.408  36.433  79.780  1.00 29.77           N  
ANISOU   82  N   SER A  11     3964   3445   3902    335    575   -247       N  
ATOM     83  CA  SER A  11      61.575  36.316  80.978  1.00 30.44           C  
ANISOU   83  CA  SER A  11     4044   3560   3960    291    514   -200       C  
ATOM     84  C   SER A  11      62.255  37.116  82.070  1.00 28.19           C  
ANISOU   84  C   SER A  11     3671   3392   3645    321    423    -96       C  
ATOM     85  O   SER A  11      63.449  36.919  82.262  1.00 27.18           O  
ANISOU   85  O   SER A  11     3478   3268   3578    393    432      6       O  
ATOM     86  CB  SER A  11      61.487  34.852  81.404  1.00 32.69           C  
ANISOU   86  CB  SER A  11     4378   3704   4337    311    596   -137       C  
ATOM     87  OG  SER A  11      60.137  34.501  81.645  1.00 38.61           O  
ANISOU   87  OG  SER A  11     5177   4443   5049    204    586   -183       O  
ATOM     88  N   VAL A  12      61.516  38.022  82.758  1.00 25.64           N  
ANISOU   88  N   VAL A  12     3344   3169   3226    264    341   -127       N  
ATOM     89  CA  VAL A  12      62.089  38.901  83.791  1.00 22.57           C  
ANISOU   89  CA  VAL A  12     2906   2892   2775    256    250    -73       C  
ATOM     90  C   VAL A  12      61.228  38.878  85.058  1.00 22.08           C  
ANISOU   90  C   VAL A  12     2865   2901   2623    218    223    -57       C  
ATOM     91  O   VAL A  12      60.058  39.194  84.988  1.00 22.26           O  
ANISOU   91  O   VAL A  12     2923   2933   2602    188    240   -141       O  
ATOM     92  CB  VAL A  12      62.156  40.376  83.272  1.00 21.44           C  
ANISOU   92  CB  VAL A  12     2769   2788   2589    224    199   -162       C  
ATOM     93  CG1 VAL A  12      62.679  41.372  84.418  1.00 18.31           C  
ANISOU   93  CG1 VAL A  12     2356   2488   2112    176    102   -146       C  
ATOM     94  CG2 VAL A  12      63.077  40.493  82.016  1.00 19.79           C  
ANISOU   94  CG2 VAL A  12     2529   2541   2449    251    232   -159       C  
ATOM     95  N   PRO A  13      61.775  38.503  86.214  1.00 22.13           N  
ANISOU   95  N   PRO A  13     2837   2978   2592    221    183     64       N  
ATOM     96  CA  PRO A  13      60.948  38.629  87.500  1.00 22.11           C  
ANISOU   96  CA  PRO A  13     2861   3079   2457    174    164     72       C  
ATOM     97  C   PRO A  13      60.490  40.083  87.800  1.00 20.10           C  
ANISOU   97  C   PRO A  13     2651   2899   2087    131    126    -70       C  
ATOM     98  O   PRO A  13      61.293  40.998  87.740  1.00 19.73           O  
ANISOU   98  O   PRO A  13     2601   2874   2018    107     60   -108       O  
ATOM     99  CB  PRO A  13      61.946  38.249  88.608  1.00 21.48           C  
ANISOU   99  CB  PRO A  13     2729   3106   2326    173     95    237       C  
ATOM    100  CG  PRO A  13      63.050  37.485  87.863  1.00 23.93           C  
ANISOU  100  CG  PRO A  13     2971   3325   2796    253    116    349       C  
ATOM    101  CD  PRO A  13      63.148  38.079  86.490  1.00 22.37           C  
ANISOU  101  CD  PRO A  13     2787   3036   2673    266    149    212       C  
ATOM    102  N   GLU A  14      59.225  40.266  88.129  1.00 19.58           N  
ANISOU  102  N   GLU A  14     2619   2859   1959    123    179   -138       N  
ATOM    103  CA  GLU A  14      58.732  41.528  88.632  1.00 20.87           C  
ANISOU  103  CA  GLU A  14     2835   3078   2016    111    178   -263       C  
ATOM    104  C   GLU A  14      59.735  42.166  89.634  1.00 22.32           C  
ANISOU  104  C   GLU A  14     3053   3352   2073     50     92   -269       C  
ATOM    105  O   GLU A  14      60.257  41.497  90.530  1.00 22.70           O  
ANISOU  105  O   GLU A  14     3076   3505   2043     14     47   -151       O  
ATOM    106  CB  GLU A  14      57.344  41.277  89.282  1.00 22.61           C  
ANISOU  106  CB  GLU A  14     3059   3366   2165    120    266   -277       C  
ATOM    107  CG  GLU A  14      56.758  42.463  90.022  1.00 27.78           C  
ANISOU  107  CG  GLU A  14     3776   4081   2696    134    307   -406       C  
ATOM    108  CD  GLU A  14      55.354  42.224  90.511  1.00 32.53           C  
ANISOU  108  CD  GLU A  14     4348   4762   3249    165    420   -408       C  
ATOM    109  OE1 GLU A  14      54.796  41.137  90.272  1.00 34.75           O  
ANISOU  109  OE1 GLU A  14     4556   5053   3591    149    452   -304       O  
ATOM    110  OE2 GLU A  14      54.782  43.159  91.115  1.00 39.79           O  
ANISOU  110  OE2 GLU A  14     5318   5726   4074    204    489   -520       O  
ATOM    111  N   GLY A  15      60.030  43.452  89.464  1.00 23.41           N  
ANISOU  111  N   GLY A  15     3249   3453   2192     23     59   -393       N  
ATOM    112  CA  GLY A  15      60.918  44.152  90.406  1.00 25.87           C  
ANISOU  112  CA  GLY A  15     3610   3851   2369    -78    -32   -430       C  
ATOM    113  C   GLY A  15      62.363  44.237  89.924  1.00 27.76           C  
ANISOU  113  C   GLY A  15     3780   4087   2681   -135   -141   -352       C  
ATOM    114  O   GLY A  15      63.137  45.090  90.395  1.00 29.79           O  
ANISOU  114  O   GLY A  15     4073   4390   2855   -250   -231   -406       O  
ATOM    115  N   ALA A  16      62.736  43.366  88.979  1.00 27.01           N  
ANISOU  115  N   ALA A  16     3585   3940   2738    -66   -125   -231       N  
ATOM    116  CA  ALA A  16      64.077  43.368  88.442  1.00 26.33           C  
ANISOU  116  CA  ALA A  16     3404   3863   2737    -93   -196   -138       C  
ATOM    117  C   ALA A  16      64.162  44.255  87.203  1.00 26.18           C  
ANISOU  117  C   ALA A  16     3405   3717   2824    -88   -171   -225       C  
ATOM    118  O   ALA A  16      63.176  44.842  86.785  1.00 25.64           O  
ANISOU  118  O   ALA A  16     3422   3553   2766    -55   -108   -342       O  
ATOM    119  CB  ALA A  16      64.532  41.974  88.110  1.00 26.13           C  
ANISOU  119  CB  ALA A  16     3267   3840   2817     -3   -165     36       C  
ATOM    120  N   ILE A  17      65.360  44.369  86.646  1.00 25.70           N  
ANISOU  120  N   ILE A  17     3251   3672   2840   -120   -218   -143       N  
ATOM    121  CA  ILE A  17      65.570  45.222  85.500  1.00 26.46           C  
ANISOU  121  CA  ILE A  17     3359   3669   3024   -133   -197   -194       C  
ATOM    122  C   ILE A  17      65.434  44.359  84.250  1.00 25.80           C  
ANISOU  122  C   ILE A  17     3224   3524   3054    -15    -97   -140       C  
ATOM    123  O   ILE A  17      66.127  43.348  84.137  1.00 27.08           O  
ANISOU  123  O   ILE A  17     3286   3730   3272     39    -76    -21       O  
ATOM    124  CB  ILE A  17      66.967  45.930  85.546  1.00 26.98           C  
ANISOU  124  CB  ILE A  17     3345   3801   3103   -261   -297   -135       C  
ATOM    125  CG1 ILE A  17      66.985  46.900  86.736  1.00 28.81           C  
ANISOU  125  CG1 ILE A  17     3674   4072   3200   -416   -396   -239       C  
ATOM    126  CG2 ILE A  17      67.230  46.683  84.182  1.00 28.73           C  
ANISOU  126  CG2 ILE A  17     3563   3919   3434   -267   -252   -147       C  
ATOM    127  CD1 ILE A  17      68.366  47.279  87.343  1.00 32.62           C  
ANISOU  127  CD1 ILE A  17     4058   4700   3633   -595   -543   -162       C  
ATOM    128  N   ALA A  18      64.560  44.748  83.333  1.00 24.32           N  
ANISOU  128  N   ALA A  18     3106   3239   2894     23    -34   -223       N  
ATOM    129  CA  ALA A  18      64.494  44.118  81.997  1.00 24.86           C  
ANISOU  129  CA  ALA A  18     3146   3264   3036     97     51   -198       C  
ATOM    130  C   ALA A  18      65.469  44.888  81.115  1.00 26.50           C  
ANISOU  130  C   ALA A  18     3306   3469   3291     56     43   -158       C  
ATOM    131  O   ALA A  18      65.466  46.130  81.102  1.00 27.60           O  
ANISOU  131  O   ALA A  18     3491   3571   3421    -15     -2   -195       O  
ATOM    132  CB  ALA A  18      63.114  44.260  81.410  1.00 22.42           C  
ANISOU  132  CB  ALA A  18     2913   2897   2708    133     97   -283       C  
ATOM    133  N   SER A  19      66.302  44.188  80.371  1.00 26.39           N  
ANISOU  133  N   SER A  19     3207   3484   3336    101    104    -80       N  
ATOM    134  CA  SER A  19      67.190  44.952  79.525  1.00 27.32           C  
ANISOU  134  CA  SER A  19     3269   3620   3490     55    111    -29       C  
ATOM    135  C   SER A  19      67.281  44.428  78.123  1.00 27.44           C  
ANISOU  135  C   SER A  19     3272   3627   3524    125    230    -20       C  
ATOM    136  O   SER A  19      67.283  43.227  77.899  1.00 27.61           O  
ANISOU  136  O   SER A  19     3283   3641   3565    214    317    -21       O  
ATOM    137  CB  SER A  19      68.566  45.113  80.155  1.00 26.36           C  
ANISOU  137  CB  SER A  19     3012   3596   3405     -9     46     82       C  
ATOM    138  OG  SER A  19      69.057  43.857  80.339  1.00 25.36           O  
ANISOU  138  OG  SER A  19     2792   3519   3322     91     99    164       O  
ATOM    139  N   LEU A  20      67.340  45.379  77.202  1.00 28.18           N  
ANISOU  139  N   LEU A  20     3384   3715   3607     76    238    -12       N  
ATOM    140  CA  LEU A  20      67.475  45.117  75.772  1.00 29.43           C  
ANISOU  140  CA  LEU A  20     3540   3898   3742    115    348     -1       C  
ATOM    141  C   LEU A  20      68.642  45.903  75.239  1.00 29.61           C  
ANISOU  141  C   LEU A  20     3468   3982   3800     53    363    107       C  
ATOM    142  O   LEU A  20      68.918  47.020  75.688  1.00 28.29           O  
ANISOU  142  O   LEU A  20     3290   3796   3662    -51    269    148       O  
ATOM    143  CB  LEU A  20      66.232  45.589  75.030  1.00 28.93           C  
ANISOU  143  CB  LEU A  20     3589   3798   3604    105    339    -65       C  
ATOM    144  CG  LEU A  20      64.939  45.014  75.561  1.00 30.94           C  
ANISOU  144  CG  LEU A  20     3919   4011   3826    139    311   -160       C  
ATOM    145  CD1 LEU A  20      64.401  46.136  76.457  1.00 36.83           C  
ANISOU  145  CD1 LEU A  20     4700   4703   4589    101    211   -168       C  
ATOM    146  CD2 LEU A  20      63.985  44.794  74.512  1.00 28.60           C  
ANISOU  146  CD2 LEU A  20     3682   3735   3446    146    342   -206       C  
ATOM    147  N   ASN A  21      69.365  45.317  74.303  1.00 30.58           N  
ANISOU  147  N   ASN A  21     3523   4172   3922    108    491    152       N  
ATOM    148  CA  ASN A  21      70.232  46.170  73.517  1.00 31.74           C  
ANISOU  148  CA  ASN A  21     3591   4389   4077     39    524    260       C  
ATOM    149  C   ASN A  21      70.203  45.952  72.036  1.00 30.04           C  
ANISOU  149  C   ASN A  21     3408   4231   3772     78    664    257       C  
ATOM    150  O   ASN A  21      69.646  44.966  71.537  1.00 28.60           O  
ANISOU  150  O   ASN A  21     3306   4038   3519    162    753    153       O  
ATOM    151  CB  ASN A  21      71.645  46.416  74.102  1.00 35.22           C  
ANISOU  151  CB  ASN A  21     3847   4916   4618    -15    498    395       C  
ATOM    152  CG  ASN A  21      72.589  45.334  73.802  1.00 40.47           C  
ANISOU  152  CG  ASN A  21     4371   5675   5329    106    641    458       C  
ATOM    153  OD1 ASN A  21      72.288  44.191  74.103  1.00 50.71           O  
ANISOU  153  OD1 ASN A  21     5700   6929   6638    231    695    394       O  
ATOM    154  ND2 ASN A  21      73.751  45.659  73.185  1.00 41.98           N  
ANISOU  154  ND2 ASN A  21     4402   5988   5559     78    722    593       N  
ATOM    155  N   CYS A  22      70.779  46.920  71.357  1.00 28.57           N  
ANISOU  155  N   CYS A  22     3170   4104   3578     -6    677    369       N  
ATOM    156  CA  CYS A  22      70.635  47.072  69.955  1.00 28.34           C  
ANISOU  156  CA  CYS A  22     3189   4147   3430     -7    779    390       C  
ATOM    157  C   CYS A  22      71.972  47.612  69.428  1.00 29.72           C  
ANISOU  157  C   CYS A  22     3212   4436   3642    -66    861    553       C  
ATOM    158  O   CYS A  22      72.502  48.600  69.928  1.00 28.69           O  
ANISOU  158  O   CYS A  22     3007   4286   3607   -184    767    665       O  
ATOM    159  CB  CYS A  22      69.532  48.062  69.772  1.00 28.16           C  
ANISOU  159  CB  CYS A  22     3289   4053   3356    -75    663    392       C  
ATOM    160  SG  CYS A  22      69.332  48.473  68.136  1.00 34.85           S  
ANISOU  160  SG  CYS A  22     4185   5013   4042   -104    745    468       S  
ATOM    161  N   THR A  23      72.542  46.915  68.467  1.00 29.83           N  
ANISOU  161  N   THR A  23     3180   4569   3585      9   1048    560       N  
ATOM    162  CA  THR A  23      73.757  47.364  67.888  1.00 33.66           C  
ANISOU  162  CA  THR A  23     3505   5189   4093    -36   1153    723       C  
ATOM    163  C   THR A  23      73.412  47.824  66.474  1.00 35.50           C  
ANISOU  163  C   THR A  23     3832   5509   4148    -80   1236    758       C  
ATOM    164  O   THR A  23      72.437  47.349  65.856  1.00 34.90           O  
ANISOU  164  O   THR A  23     3918   5427   3915    -34   1261    629       O  
ATOM    165  CB  THR A  23      74.881  46.284  67.909  1.00 34.75           C  
ANISOU  165  CB  THR A  23     3477   5427   4300    101   1335    742       C  
ATOM    166  OG1 THR A  23      74.460  45.149  67.169  1.00 35.94           O  
ANISOU  166  OG1 THR A  23     3749   5574   4330    242   1505    584       O  
ATOM    167  CG2 THR A  23      75.174  45.827  69.323  1.00 33.84           C  
ANISOU  167  CG2 THR A  23     3261   5248   4348    145   1231    743       C  
ATOM    168  N   TYR A  24      74.182  48.781  65.988  1.00 36.85           N  
ANISOU  168  N   TYR A  24     3898   5770   4334   -190   1263    947       N  
ATOM    169  CA  TYR A  24      73.898  49.403  64.697  1.00 39.45           C  
ANISOU  169  CA  TYR A  24     4304   6192   4491   -255   1322   1035       C  
ATOM    170  C   TYR A  24      75.224  49.504  63.951  1.00 42.53           C  
ANISOU  170  C   TYR A  24     4518   6774   4866   -279   1513   1195       C  
ATOM    171  O   TYR A  24      76.271  49.728  64.577  1.00 43.50           O  
ANISOU  171  O   TYR A  24     4445   6921   5161   -324   1511   1309       O  
ATOM    172  CB  TYR A  24      73.185  50.756  64.886  1.00 37.06           C  
ANISOU  172  CB  TYR A  24     4091   5759   4230   -386   1131   1138       C  
ATOM    173  CG  TYR A  24      73.964  51.778  65.667  1.00 37.63           C  
ANISOU  173  CG  TYR A  24     4049   5745   4501   -529   1035   1283       C  
ATOM    174  CD1 TYR A  24      73.853  51.872  67.062  1.00 35.03           C  
ANISOU  174  CD1 TYR A  24     3718   5258   4332   -553    882   1199       C  
ATOM    175  CD2 TYR A  24      74.825  52.667  65.011  1.00 40.17           C  
ANISOU  175  CD2 TYR A  24     4270   6153   4839   -664   1096   1504       C  
ATOM    176  CE1 TYR A  24      74.591  52.856  67.804  1.00 32.65           C  
ANISOU  176  CE1 TYR A  24     3329   4879   4195   -727    780   1311       C  
ATOM    177  CE2 TYR A  24      75.552  53.648  65.728  1.00 38.77           C  
ANISOU  177  CE2 TYR A  24     3996   5885   4850   -840    996   1633       C  
ATOM    178  CZ  TYR A  24      75.417  53.744  67.114  1.00 35.97           C  
ANISOU  178  CZ  TYR A  24     3657   5366   4641   -877    833   1523       C  
ATOM    179  OH  TYR A  24      76.161  54.701  67.793  1.00 35.91           O  
ANISOU  179  OH  TYR A  24     3570   5280   4794  -1086    731   1628       O  
ATOM    180  N   SER A  25      75.195  49.286  62.637  1.00 45.66           N  
ANISOU  180  N   SER A  25     4970   7331   5046   -253   1681   1204       N  
ATOM    181  CA  SER A  25      76.438  49.178  61.854  1.00 50.00           C  
ANISOU  181  CA  SER A  25     5352   8093   5553   -242   1916   1332       C  
ATOM    182  C   SER A  25      76.953  50.514  61.309  1.00 52.51           C  
ANISOU  182  C   SER A  25     5580   8499   5870   -423   1902   1607       C  
ATOM    183  O   SER A  25      78.179  50.684  61.062  1.00 55.37           O  
ANISOU  183  O   SER A  25     5729   9017   6293   -460   2048   1774       O  
ATOM    184  CB  SER A  25      76.275  48.171  60.713  1.00 51.78           C  
ANISOU  184  CB  SER A  25     5687   8462   5522   -120   2149   1181       C  
ATOM    185  OG  SER A  25      75.302  48.634  59.766  1.00 54.51           O  
ANISOU  185  OG  SER A  25     6222   8865   5621   -207   2092   1185       O  
ATOM    186  N   ASP A  26      76.052  51.463  61.113  1.00 52.74           N  
ANISOU  186  N   ASP A  26     5758   8432   5848   -535   1737   1678       N  
ATOM    187  CA  ASP A  26      76.458  52.737  60.502  1.00 56.10           C  
ANISOU  187  CA  ASP A  26     6130   8914   6271   -708   1732   1958       C  
ATOM    188  C   ASP A  26      76.842  53.802  61.515  1.00 56.24           C  
ANISOU  188  C   ASP A  26     6064   8744   6561   -868   1558   2093       C  
ATOM    189  O   ASP A  26      75.967  54.431  62.121  1.00 55.02           O  
ANISOU  189  O   ASP A  26     6050   8361   6493   -911   1360   2061       O  
ATOM    190  CB  ASP A  26      75.407  53.298  59.542  1.00 56.47           C  
ANISOU  190  CB  ASP A  26     6366   8982   6106   -746   1677   2031       C  
ATOM    191  CG  ASP A  26      76.005  54.356  58.619  1.00 62.54           C  
ANISOU  191  CG  ASP A  26     7067   9876   6818   -898   1753   2344       C  
ATOM    192  OD1 ASP A  26      75.906  54.163  57.375  1.00 66.70           O  
ANISOU  192  OD1 ASP A  26     7644  10634   7064   -883   1894   2401       O  
ATOM    193  OD2 ASP A  26      76.637  55.335  59.141  1.00 62.47           O  
ANISOU  193  OD2 ASP A  26     6953   9746   7035  -1048   1681   2529       O  
ATOM    194  N   ARG A  27      78.149  54.023  61.650  1.00 58.69           N  
ANISOU  194  N   ARG A  27     6143   9159   6995   -964   1643   2246       N  
ATOM    195  CA  ARG A  27      78.733  54.981  62.598  1.00 59.73           C  
ANISOU  195  CA  ARG A  27     6170   9148   7376  -1163   1488   2370       C  
ATOM    196  C   ARG A  27      78.220  56.428  62.496  1.00 59.93           C  
ANISOU  196  C   ARG A  27     6340   8965   7462  -1349   1345   2526       C  
ATOM    197  O   ARG A  27      78.293  57.175  63.485  1.00 60.58           O  
ANISOU  197  O   ARG A  27     6439   8831   7746  -1498   1175   2531       O  
ATOM    198  CB  ARG A  27      80.269  54.953  62.498  1.00 62.69           C  
ANISOU  198  CB  ARG A  27     6236   9742   7838  -1253   1628   2549       C  
ATOM    199  CG  ARG A  27      81.002  56.181  63.079  1.00 68.22           C  
ANISOU  199  CG  ARG A  27     6817  10349   8752  -1545   1493   2750       C  
ATOM    200  CD  ARG A  27      81.334  56.072  64.597  1.00 74.38           C  
ANISOU  200  CD  ARG A  27     7503  11021   9735  -1613   1305   2641       C  
ATOM    201  NE  ARG A  27      82.382  57.044  64.987  1.00 81.06           N  
ANISOU  201  NE  ARG A  27     8160  11880  10757  -1918   1226   2848       N  
ATOM    202  CZ  ARG A  27      82.205  58.118  65.774  1.00 82.88           C  
ANISOU  202  CZ  ARG A  27     8505  11853  11129  -2163   1013   2849       C  
ATOM    203  NH1 ARG A  27      81.016  58.412  66.307  1.00 79.93           N  
ANISOU  203  NH1 ARG A  27     8428  11183  10756  -2118    865   2661       N  
ATOM    204  NH2 ARG A  27      83.237  58.915  66.033  1.00 86.48           N  
ANISOU  204  NH2 ARG A  27     8777  12349  11730  -2465    956   3036       N  
ATOM    205  N   GLY A  28      77.715  56.832  61.330  1.00 59.45           N  
ANISOU  205  N   GLY A  28     6394   8962   7231  -1344   1414   2657       N  
ATOM    206  CA  GLY A  28      77.141  58.170  61.194  1.00 59.78           C  
ANISOU  206  CA  GLY A  28     6586   8782   7345  -1481   1288   2829       C  
ATOM    207  C   GLY A  28      75.793  58.426  61.877  1.00 57.17           C  
ANISOU  207  C   GLY A  28     6480   8165   7075  -1398   1100   2675       C  
ATOM    208  O   GLY A  28      75.445  59.593  62.094  1.00 57.72           O  
ANISOU  208  O   GLY A  28     6662   7980   7286  -1509    991   2798       O  
ATOM    209  N   SER A  29      75.065  57.353  62.248  1.00 53.58           N  
ANISOU  209  N   SER A  29     6087   7737   6531  -1206   1074   2414       N  
ATOM    210  CA  SER A  29      73.653  57.426  62.701  1.00 50.81           C  
ANISOU  210  CA  SER A  29     5931   7185   6188  -1092    927   2275       C  
ATOM    211  C   SER A  29      73.449  58.495  63.772  1.00 49.61           C  
ANISOU  211  C   SER A  29     5865   6697   6286  -1197    773   2279       C  
ATOM    212  O   SER A  29      74.238  58.621  64.704  1.00 49.03           O  
ANISOU  212  O   SER A  29     5711   6543   6372  -1315    731   2223       O  
ATOM    213  CB  SER A  29      73.163  56.058  63.209  1.00 48.58           C  
ANISOU  213  CB  SER A  29     5661   6970   5825   -917    924   1985       C  
ATOM    214  OG  SER A  29      73.274  55.045  62.201  1.00 51.08           O  
ANISOU  214  OG  SER A  29     5941   7560   5904   -821   1081   1944       O  
ATOM    215  N   GLN A  30      72.384  59.263  63.646  1.00 49.21           N  
ANISOU  215  N   GLN A  30     5979   6454   6265  -1153    690   2344       N  
ATOM    216  CA  GLN A  30      72.207  60.450  64.496  1.00 49.70           C  
ANISOU  216  CA  GLN A  30     6156   6159   6568  -1254    582   2370       C  
ATOM    217  C   GLN A  30      71.172  60.248  65.603  1.00 46.73           C  
ANISOU  217  C   GLN A  30     5904   5587   6263  -1121    474   2124       C  
ATOM    218  O   GLN A  30      71.310  60.779  66.710  1.00 46.77           O  
ANISOU  218  O   GLN A  30     5976   5347   6445  -1210    400   2016       O  
ATOM    219  CB  GLN A  30      71.882  61.688  63.633  1.00 52.44           C  
ANISOU  219  CB  GLN A  30     6598   6366   6957  -1305    591   2668       C  
ATOM    220  CG  GLN A  30      73.132  62.530  63.257  1.00 58.74           C  
ANISOU  220  CG  GLN A  30     7316   7146   7857  -1556    653   2909       C  
ATOM    221  CD  GLN A  30      72.805  63.728  62.349  1.00 67.35           C  
ANISOU  221  CD  GLN A  30     8507   8092   8991  -1602    672   3240       C  
ATOM    222  OE1 GLN A  30      72.107  63.582  61.332  1.00 70.61           O  
ANISOU  222  OE1 GLN A  30     8940   8668   9220  -1465    703   3385       O  
ATOM    223  NE2 GLN A  30      73.321  64.917  62.703  1.00 69.73           N  
ANISOU  223  NE2 GLN A  30     8874   8089   9531  -1811    650   3372       N  
ATOM    224  N   SER A  31      70.156  59.445  65.311  1.00 43.88           N  
ANISOU  224  N   SER A  31     5571   5352   5748   -924    469   2027       N  
ATOM    225  CA  SER A  31      68.995  59.327  66.197  1.00 41.21           C  
ANISOU  225  CA  SER A  31     5343   4847   5466   -782    381   1841       C  
ATOM    226  C   SER A  31      68.571  57.897  66.455  1.00 37.83           C  
ANISOU  226  C   SER A  31     4866   4614   4893   -650    382   1618       C  
ATOM    227  O   SER A  31      68.509  57.090  65.523  1.00 36.50           O  
ANISOU  227  O   SER A  31     4639   4699   4530   -595    444   1639       O  
ATOM    228  CB  SER A  31      67.812  60.080  65.608  1.00 42.09           C  
ANISOU  228  CB  SER A  31     5559   4848   5584   -666    350   2001       C  
ATOM    229  OG  SER A  31      68.154  61.433  65.482  1.00 47.67           O  
ANISOU  229  OG  SER A  31     6339   5311   6462   -778    355   2206       O  
ATOM    230  N   PHE A  32      68.224  57.610  67.720  1.00 35.54           N  
ANISOU  230  N   PHE A  32     4618   4193   4690   -606    318   1403       N  
ATOM    231  CA  PHE A  32      68.003  56.235  68.193  1.00 31.95           C  
ANISOU  231  CA  PHE A  32     4113   3886   4137   -511    320   1190       C  
ATOM    232  C   PHE A  32      66.734  56.223  69.047  1.00 31.61           C  
ANISOU  232  C   PHE A  32     4168   3701   4139   -389    247   1048       C  
ATOM    233  O   PHE A  32      66.523  57.156  69.837  1.00 32.72           O  
ANISOU  233  O   PHE A  32     4401   3600   4428   -414    201   1028       O  
ATOM    234  CB  PHE A  32      69.239  55.785  68.997  1.00 31.04           C  
ANISOU  234  CB  PHE A  32     3899   3810   4082   -614    331   1102       C  
ATOM    235  CG  PHE A  32      70.538  56.033  68.267  1.00 32.85           C  
ANISOU  235  CG  PHE A  32     4008   4161   4311   -748    408   1272       C  
ATOM    236  CD1 PHE A  32      71.100  55.027  67.473  1.00 30.18           C  
ANISOU  236  CD1 PHE A  32     3551   4078   3836   -700    524   1288       C  
ATOM    237  CD2 PHE A  32      71.149  57.297  68.299  1.00 31.09           C  
ANISOU  237  CD2 PHE A  32     3799   3789   4222   -921    383   1422       C  
ATOM    238  CE1 PHE A  32      72.266  55.249  66.744  1.00 28.91           C  
ANISOU  238  CE1 PHE A  32     3263   4056   3665   -806    623   1457       C  
ATOM    239  CE2 PHE A  32      72.352  57.570  67.550  1.00 31.22           C  
ANISOU  239  CE2 PHE A  32     3683   3940   4238  -1062    464   1613       C  
ATOM    240  CZ  PHE A  32      72.904  56.550  66.778  1.00 33.87           C  
ANISOU  240  CZ  PHE A  32     3877   4560   4429   -996    587   1636       C  
ATOM    241  N   PHE A  33      65.904  55.175  68.902  1.00 30.00           N  
ANISOU  241  N   PHE A  33     3949   3640   3808   -268    247    943       N  
ATOM    242  CA  PHE A  33      64.542  55.150  69.424  1.00 28.97           C  
ANISOU  242  CA  PHE A  33     3880   3431   3696   -143    191    859       C  
ATOM    243  C   PHE A  33      64.165  53.759  69.932  1.00 28.30           C  
ANISOU  243  C   PHE A  33     3760   3467   3522    -82    190    665       C  
ATOM    244  O   PHE A  33      64.676  52.766  69.421  1.00 27.39           O  
ANISOU  244  O   PHE A  33     3588   3522   3294   -103    242    628       O  
ATOM    245  CB  PHE A  33      63.542  55.509  68.319  1.00 29.54           C  
ANISOU  245  CB  PHE A  33     3959   3577   3686    -62    175   1022       C  
ATOM    246  CG  PHE A  33      63.799  56.814  67.680  1.00 31.14           C  
ANISOU  246  CG  PHE A  33     4197   3667   3968   -103    182   1255       C  
ATOM    247  CD1 PHE A  33      63.371  57.982  68.287  1.00 33.37           C  
ANISOU  247  CD1 PHE A  33     4568   3669   4440    -59    160   1306       C  
ATOM    248  CD2 PHE A  33      64.471  56.881  66.457  1.00 30.69           C  
ANISOU  248  CD2 PHE A  33     4095   3772   3794   -184    227   1428       C  
ATOM    249  CE1 PHE A  33      63.610  59.200  67.696  1.00 36.27           C  
ANISOU  249  CE1 PHE A  33     4984   3891   4905    -97    175   1537       C  
ATOM    250  CE2 PHE A  33      64.704  58.072  65.860  1.00 33.98           C  
ANISOU  250  CE2 PHE A  33     4542   4081   4284   -230    236   1671       C  
ATOM    251  CZ  PHE A  33      64.302  59.251  66.488  1.00 36.69           C  
ANISOU  251  CZ  PHE A  33     4981   4114   4846   -192    207   1733       C  
ATOM    252  N   TRP A  34      63.267  53.711  70.926  1.00 26.50           N  
ANISOU  252  N   TRP A  34     3574   3141   3353     -5    148    549       N  
ATOM    253  CA  TRP A  34      62.712  52.481  71.411  1.00 25.46           C  
ANISOU  253  CA  TRP A  34     3416   3106   3150     49    144    396       C  
ATOM    254  C   TRP A  34      61.222  52.675  71.304  1.00 25.94           C  
ANISOU  254  C   TRP A  34     3487   3171   3198    155    106    420       C  
ATOM    255  O   TRP A  34      60.696  53.718  71.736  1.00 26.58           O  
ANISOU  255  O   TRP A  34     3614   3093   3393    217     91    467       O  
ATOM    256  CB  TRP A  34      63.113  52.191  72.852  1.00 23.58           C  
ANISOU  256  CB  TRP A  34     3193   2778   2986     28    133    250       C  
ATOM    257  CG  TRP A  34      64.542  51.728  72.989  1.00 26.35           C  
ANISOU  257  CG  TRP A  34     3487   3184   3341    -64    160    239       C  
ATOM    258  CD1 TRP A  34      65.592  52.467  73.451  1.00 26.70           C  
ANISOU  258  CD1 TRP A  34     3525   3146   3472   -171    141    275       C  
ATOM    259  CD2 TRP A  34      65.091  50.420  72.656  1.00 22.58           C  
ANISOU  259  CD2 TRP A  34     2936   2856   2786    -55    216    201       C  
ATOM    260  NE1 TRP A  34      66.757  51.725  73.398  1.00 25.88           N  
ANISOU  260  NE1 TRP A  34     3317   3165   3352   -222    175    288       N  
ATOM    261  CE2 TRP A  34      66.482  50.472  72.921  1.00 22.72           C  
ANISOU  261  CE2 TRP A  34     2881   2891   2859   -134    234    242       C  
ATOM    262  CE3 TRP A  34      64.543  49.232  72.182  1.00 21.14           C  
ANISOU  262  CE3 TRP A  34     2748   2780   2503      5    258    133       C  
ATOM    263  CZ2 TRP A  34      67.338  49.358  72.748  1.00 21.77           C  
ANISOU  263  CZ2 TRP A  34     2668   2890   2712   -114    308    232       C  
ATOM    264  CZ3 TRP A  34      65.390  48.123  71.995  1.00 22.18           C  
ANISOU  264  CZ3 TRP A  34     2826   2995   2604     11    339     96       C  
ATOM    265  CH2 TRP A  34      66.769  48.207  72.261  1.00 24.40           C  
ANISOU  265  CH2 TRP A  34     3023   3291   2957    -28    372    155       C  
ATOM    266  N   TYR A  35      60.573  51.703  70.653  1.00 25.62           N  
ANISOU  266  N   TYR A  35     3399   3313   3020    172     99    397       N  
ATOM    267  CA  TYR A  35      59.156  51.651  70.485  1.00 25.69           C  
ANISOU  267  CA  TYR A  35     3373   3394   2994    250     50    428       C  
ATOM    268  C   TYR A  35      58.649  50.462  71.249  1.00 25.72           C  
ANISOU  268  C   TYR A  35     3357   3448   2966    253     51    259       C  
ATOM    269  O   TYR A  35      59.324  49.412  71.283  1.00 26.24           O  
ANISOU  269  O   TYR A  35     3434   3562   2972    188     88    150       O  
ATOM    270  CB  TYR A  35      58.833  51.418  69.023  1.00 27.58           C  
ANISOU  270  CB  TYR A  35     3572   3839   3065    213     23    541       C  
ATOM    271  CG  TYR A  35      58.905  52.670  68.215  1.00 26.30           C  
ANISOU  271  CG  TYR A  35     3411   3653   2927    235      6    766       C  
ATOM    272  CD1 TYR A  35      60.137  53.206  67.823  1.00 23.01           C  
ANISOU  272  CD1 TYR A  35     3034   3175   2530    165     57    842       C  
ATOM    273  CD2 TYR A  35      57.747  53.334  67.872  1.00 26.04           C  
ANISOU  273  CD2 TYR A  35     3326   3656   2911    329    -56    928       C  
ATOM    274  CE1 TYR A  35      60.167  54.409  67.049  1.00 29.69           C  
ANISOU  274  CE1 TYR A  35     3888   3984   3408    177     44   1084       C  
ATOM    275  CE2 TYR A  35      57.763  54.528  67.094  1.00 28.63           C  
ANISOU  275  CE2 TYR A  35     3654   3947   3275    366    -72   1181       C  
ATOM    276  CZ  TYR A  35      58.970  55.066  66.708  1.00 30.63           C  
ANISOU  276  CZ  TYR A  35     3970   4120   3548    285    -20   1254       C  
ATOM    277  OH  TYR A  35      58.971  56.259  65.982  1.00 33.03           O  
ANISOU  277  OH  TYR A  35     4281   4364   3903    316    -30   1523       O  
ATOM    278  N   ARG A  36      57.490  50.599  71.881  1.00 25.15           N  
ANISOU  278  N   ARG A  36     3251   3358   2944    336     24    248       N  
ATOM    279  CA  ARG A  36      56.931  49.465  72.637  1.00 24.69           C  
ANISOU  279  CA  ARG A  36     3167   3355   2859    326     29    109       C  
ATOM    280  C   ARG A  36      55.699  49.018  71.876  1.00 25.75           C  
ANISOU  280  C   ARG A  36     3213   3675   2894    319    -27    164       C  
ATOM    281  O   ARG A  36      54.915  49.867  71.444  1.00 28.40           O  
ANISOU  281  O   ARG A  36     3486   4053   3252    395    -68    312       O  
ATOM    282  CB  ARG A  36      56.581  49.877  74.082  1.00 24.41           C  
ANISOU  282  CB  ARG A  36     3150   3182   2940    408     56     42       C  
ATOM    283  CG  ARG A  36      55.839  48.827  74.942  1.00 20.72           C  
ANISOU  283  CG  ARG A  36     2644   2780   2449    405     66    -64       C  
ATOM    284  CD  ARG A  36      55.304  49.371  76.291  1.00 21.49           C  
ANISOU  284  CD  ARG A  36     2755   2777   2632    501    109   -114       C  
ATOM    285  NE  ARG A  36      54.516  50.604  76.143  1.00 26.62           N  
ANISOU  285  NE  ARG A  36     3379   3370   3365    631    122    -13       N  
ATOM    286  CZ  ARG A  36      54.371  51.543  77.091  1.00 31.88           C  
ANISOU  286  CZ  ARG A  36     4109   3877   4125    730    186    -55       C  
ATOM    287  NH1 ARG A  36      54.901  51.366  78.301  1.00 27.64           N  
ANISOU  287  NH1 ARG A  36     3660   3261   3580    690    224   -200       N  
ATOM    288  NH2 ARG A  36      53.652  52.642  76.857  1.00 31.77           N  
ANISOU  288  NH2 ARG A  36     4076   3786   4209    874    218     50       N  
ATOM    289  N   GLN A  37      55.513  47.716  71.710  1.00 24.30           N  
ANISOU  289  N   GLN A  37     3021   3601   2609    223    -31     60       N  
ATOM    290  CA  GLN A  37      54.336  47.260  70.993  1.00 25.30           C  
ANISOU  290  CA  GLN A  37     3061   3924   2627    170   -103    102       C  
ATOM    291  C   GLN A  37      53.674  46.152  71.807  1.00 25.92           C  
ANISOU  291  C   GLN A  37     3111   4022   2715    121    -94    -18       C  
ATOM    292  O   GLN A  37      54.306  45.107  72.054  1.00 24.39           O  
ANISOU  292  O   GLN A  37     2998   3769   2500     43    -43   -155       O  
ATOM    293  CB  GLN A  37      54.741  46.733  69.603  1.00 25.92           C  
ANISOU  293  CB  GLN A  37     3181   4143   2523     42   -123     95       C  
ATOM    294  CG  GLN A  37      53.565  46.339  68.700  1.00 26.06           C  
ANISOU  294  CG  GLN A  37     3111   4403   2384    -55   -227    146       C  
ATOM    295  CD  GLN A  37      54.014  45.787  67.365  1.00 30.08           C  
ANISOU  295  CD  GLN A  37     3697   5054   2676   -201   -234    101       C  
ATOM    296  OE1 GLN A  37      55.190  45.428  67.158  1.00 28.62           O  
ANISOU  296  OE1 GLN A  37     3630   4779   2462   -226   -135      0       O  
ATOM    297  NE2 GLN A  37      53.103  45.754  66.441  1.00 27.11           N  
ANISOU  297  NE2 GLN A  37     3245   4917   2136   -295   -347    185       N  
ATOM    298  N   TYR A  38      52.463  46.414  72.309  1.00 26.95           N  
ANISOU  298  N   TYR A  38     3123   4216   2898    182   -127     46       N  
ATOM    299  CA  TYR A  38      51.687  45.390  72.976  1.00 27.90           C  
ANISOU  299  CA  TYR A  38     3190   4390   3017    114   -123    -33       C  
ATOM    300  C   TYR A  38      51.113  44.458  71.923  1.00 30.00           C  
ANISOU  300  C   TYR A  38     3420   4845   3132    -65   -202    -51       C  
ATOM    301  O   TYR A  38      50.988  44.839  70.735  1.00 30.50           O  
ANISOU  301  O   TYR A  38     3454   5049   3084   -106   -277     36       O  
ATOM    302  CB  TYR A  38      50.552  46.013  73.806  1.00 29.66           C  
ANISOU  302  CB  TYR A  38     3276   4650   3342    243   -115     55       C  
ATOM    303  CG  TYR A  38      51.085  46.629  75.085  1.00 29.79           C  
ANISOU  303  CG  TYR A  38     3369   4469   3480    377    -17      3       C  
ATOM    304  CD1 TYR A  38      51.612  45.827  76.094  1.00 30.39           C  
ANISOU  304  CD1 TYR A  38     3528   4451   3566    329     41   -127       C  
ATOM    305  CD2 TYR A  38      51.138  48.002  75.243  1.00 31.46           C  
ANISOU  305  CD2 TYR A  38     3588   4578   3785    538     12     84       C  
ATOM    306  CE1 TYR A  38      52.149  46.387  77.214  1.00 31.12           C  
ANISOU  306  CE1 TYR A  38     3696   4396   3729    421    110   -178       C  
ATOM    307  CE2 TYR A  38      51.630  48.563  76.373  1.00 31.65           C  
ANISOU  307  CE2 TYR A  38     3707   4424   3894    626     95      7       C  
ATOM    308  CZ  TYR A  38      52.148  47.754  77.347  1.00 30.67           C  
ANISOU  308  CZ  TYR A  38     3656   4249   3747    557    136   -126       C  
ATOM    309  OH  TYR A  38      52.674  48.332  78.481  1.00 32.31           O  
ANISOU  309  OH  TYR A  38     3963   4308   4004    619    203   -206       O  
ATOM    310  N   SER A  39      50.730  43.262  72.342  1.00 29.78           N  
ANISOU  310  N   SER A  39     3397   4827   3088   -189   -189   -159       N  
ATOM    311  CA  SER A  39      50.366  42.245  71.374  1.00 31.53           C  
ANISOU  311  CA  SER A  39     3638   5181   3160   -404   -252   -229       C  
ATOM    312  C   SER A  39      49.087  42.693  70.714  1.00 32.67           C  
ANISOU  312  C   SER A  39     3593   5589   3229   -448   -382    -78       C  
ATOM    313  O   SER A  39      48.202  43.168  71.409  1.00 32.20           O  
ANISOU  313  O   SER A  39     3372   5590   3273   -347   -393     35       O  
ATOM    314  CB  SER A  39      50.166  40.892  72.053  1.00 32.26           C  
ANISOU  314  CB  SER A  39     3781   5193   3283   -534   -204   -363       C  
ATOM    315  OG  SER A  39      49.729  39.931  71.086  1.00 36.79           O  
ANISOU  315  OG  SER A  39     4389   5878   3707   -771   -267   -451       O  
ATOM    316  N   GLY A  40      49.043  42.635  69.373  1.00 33.92           N  
ANISOU  316  N   GLY A  40     3765   5917   3205   -579   -473    -61       N  
ATOM    317  CA  GLY A  40      47.899  43.125  68.603  1.00 35.69           C  
ANISOU  317  CA  GLY A  40     3791   6436   3331   -626   -624    120       C  
ATOM    318  C   GLY A  40      47.760  44.641  68.575  1.00 36.02           C  
ANISOU  318  C   GLY A  40     3711   6508   3466   -385   -643    357       C  
ATOM    319  O   GLY A  40      46.783  45.147  68.098  1.00 37.58           O  
ANISOU  319  O   GLY A  40     3712   6937   3627   -369   -757    554       O  
ATOM    320  N   LYS A  41      48.736  45.379  69.091  1.00 34.72           N  
ANISOU  320  N   LYS A  41     3657   6102   3430   -199   -531    349       N  
ATOM    321  CA  LYS A  41      48.654  46.849  69.050  1.00 35.25           C  
ANISOU  321  CA  LYS A  41     3644   6142   3604     21   -533    564       C  
ATOM    322  C   LYS A  41      49.745  47.421  68.140  1.00 35.96           C  
ANISOU  322  C   LYS A  41     3867   6179   3614     27   -525    604       C  
ATOM    323  O   LYS A  41      50.504  46.661  67.560  1.00 35.73           O  
ANISOU  323  O   LYS A  41     3975   6159   3440   -127   -510    460       O  
ATOM    324  CB  LYS A  41      48.775  47.425  70.457  1.00 33.13           C  
ANISOU  324  CB  LYS A  41     3390   5635   3560    223   -409    538       C  
ATOM    325  CG  LYS A  41      47.821  46.782  71.471  1.00 32.51           C  
ANISOU  325  CG  LYS A  41     3196   5602   3551    214   -383    484       C  
ATOM    326  CD  LYS A  41      46.371  47.060  71.138  1.00 37.32           C  
ANISOU  326  CD  LYS A  41     3545   6474   4161    247   -476    687       C  
ATOM    327  CE  LYS A  41      45.471  46.657  72.353  1.00 38.83           C  
ANISOU  327  CE  LYS A  41     3606   6685   4460    289   -405    656       C  
ATOM    328  NZ  LYS A  41      44.092  47.067  72.054  1.00 38.21           N  
ANISOU  328  NZ  LYS A  41     3237   6870   4409    358   -481    887       N  
ATOM    329  N   SER A  42      49.825  48.747  68.028  1.00 36.62           N  
ANISOU  329  N   SER A  42     3916   6196   3802    208   -518    800       N  
ATOM    330  CA  SER A  42      50.853  49.368  67.231  1.00 36.42           C  
ANISOU  330  CA  SER A  42     4005   6112   3719    211   -500    867       C  
ATOM    331  C   SER A  42      52.077  49.727  68.054  1.00 33.43           C  
ANISOU  331  C   SER A  42     3784   5425   3492    288   -367    751       C  
ATOM    332  O   SER A  42      51.992  49.878  69.273  1.00 32.16           O  
ANISOU  332  O   SER A  42     3631   5086   3500    390   -298    673       O  
ATOM    333  CB  SER A  42      50.297  50.580  66.455  1.00 40.30           C  
ANISOU  333  CB  SER A  42     4376   6714   4220    330   -580   1181       C  
ATOM    334  OG  SER A  42      49.202  51.208  67.098  1.00 41.34           O  
ANISOU  334  OG  SER A  42     4343   6836   4528    514   -589   1326       O  
ATOM    335  N   PRO A  43      53.237  49.849  67.392  1.00 32.72           N  
ANISOU  335  N   PRO A  43     3813   5293   3326    224   -331    740       N  
ATOM    336  CA  PRO A  43      54.428  50.365  68.055  1.00 30.80           C  
ANISOU  336  CA  PRO A  43     3688   4789   3226    282   -227    680       C  
ATOM    337  C   PRO A  43      54.205  51.780  68.567  1.00 31.38           C  
ANISOU  337  C   PRO A  43     3742   4679   3500    454   -209    835       C  
ATOM    338  O   PRO A  43      53.598  52.579  67.878  1.00 32.03           O  
ANISOU  338  O   PRO A  43     3748   4836   3583    527   -265   1059       O  
ATOM    339  CB  PRO A  43      55.472  50.370  66.935  1.00 30.94           C  
ANISOU  339  CB  PRO A  43     3780   4874   3100    181   -206    717       C  
ATOM    340  CG  PRO A  43      54.911  49.454  65.904  1.00 31.82           C  
ANISOU  340  CG  PRO A  43     3859   5262   2967     47   -275    692       C  
ATOM    341  CD  PRO A  43      53.476  49.641  65.946  1.00 34.02           C  
ANISOU  341  CD  PRO A  43     3994   5674   3254     94   -385    811       C  
ATOM    342  N   GLU A  44      54.630  52.053  69.797  1.00 30.82           N  
ANISOU  342  N   GLU A  44     3743   4371   3593    517   -131    716       N  
ATOM    343  CA AGLU A  44      54.447  53.379  70.426  0.50 32.55           C  
ANISOU  343  CA AGLU A  44     3988   4365   4013    673    -87    808       C  
ATOM    344  CA BGLU A  44      54.479  53.415  70.343  0.50 32.76           C  
ANISOU  344  CA BGLU A  44     4015   4395   4035    670    -89    820       C  
ATOM    345  C   GLU A  44      55.827  53.879  70.829  1.00 31.51           C  
ANISOU  345  C   GLU A  44     3999   4010   3962    617    -24    736       C  
ATOM    346  O   GLU A  44      56.489  53.194  71.584  1.00 29.82           O  
ANISOU  346  O   GLU A  44     3837   3755   3735    541      6    549       O  
ATOM    347  CB AGLU A  44      53.550  53.235  71.686  0.50 32.18           C  
ANISOU  347  CB AGLU A  44     3900   4257   4067    782    -45    700       C  
ATOM    348  CB BGLU A  44      53.416  53.488  71.466  0.50 33.13           C  
ANISOU  348  CB BGLU A  44     4006   4383   4199    808    -54    761       C  
ATOM    349  CG AGLU A  44      53.298  54.517  72.446  0.50 34.12           C  
ANISOU  349  CG AGLU A  44     4198   4250   4513    954     32    743       C  
ATOM    350  CG BGLU A  44      52.013  53.206  70.954  0.50 35.83           C  
ANISOU  350  CG BGLU A  44     4164   4965   4484    867   -125    896       C  
ATOM    351  CD AGLU A  44      52.794  54.299  73.872  0.50 34.55           C  
ANISOU  351  CD AGLU A  44     4265   4224   4637   1030    110    569       C  
ATOM    352  CD BGLU A  44      50.911  53.639  71.893  0.50 38.25           C  
ANISOU  352  CD BGLU A  44     4383   5209   4938   1054    -66    916       C  
ATOM    353  OE1AGLU A  44      52.061  53.315  74.138  0.50 33.26           O  
ANISOU  353  OE1AGLU A  44     3993   4247   4397   1010     91    511       O  
ATOM    354  OE1BGLU A  44      51.103  53.599  73.125  0.50 37.02           O  
ANISOU  354  OE1BGLU A  44     4312   4890   4864   1088     26    736       O  
ATOM    355  OE2AGLU A  44      53.153  55.124  74.737  0.50 35.25           O  
ANISOU  355  OE2AGLU A  44     4483   4062   4849   1094    196    487       O  
ATOM    356  OE2BGLU A  44      49.839  54.019  71.376  0.50 41.46           O  
ANISOU  356  OE2BGLU A  44     4626   5757   5370   1169   -111   1124       O  
ATOM    357  N   LEU A  45      56.257  55.029  70.329  1.00 32.68           N  
ANISOU  357  N   LEU A  45     4198   4027   4191    643    -12    899       N  
ATOM    358  CA  LEU A  45      57.557  55.589  70.733  1.00 32.78           C  
ANISOU  358  CA  LEU A  45     4334   3827   4292    559     37    843       C  
ATOM    359  C   LEU A  45      57.605  55.774  72.274  1.00 32.10           C  
ANISOU  359  C   LEU A  45     4331   3530   4332    593     89    647       C  
ATOM    360  O   LEU A  45      56.725  56.443  72.868  1.00 31.72           O  
ANISOU  360  O   LEU A  45     4302   3345   4404    739    126    654       O  
ATOM    361  CB  LEU A  45      57.808  56.935  70.044  1.00 34.37           C  
ANISOU  361  CB  LEU A  45     4582   3878   4596    587     48   1071       C  
ATOM    362  CG  LEU A  45      59.103  57.688  70.427  1.00 37.26           C  
ANISOU  362  CG  LEU A  45     5073   4006   5077    473     94   1039       C  
ATOM    363  CD1 LEU A  45      60.367  56.934  70.038  1.00 36.22           C  
ANISOU  363  CD1 LEU A  45     4919   4022   4819    295     92    983       C  
ATOM    364  CD2 LEU A  45      59.139  59.068  69.817  1.00 38.70           C  
ANISOU  364  CD2 LEU A  45     5314   3997   5392    512    113   1279       C  
ATOM    365  N   ILE A  46      58.608  55.194  72.919  1.00 30.75           N  
ANISOU  365  N   ILE A  46     4205   3348   4129    469     98    481       N  
ATOM    366  CA  ILE A  46      58.799  55.460  74.357  1.00 31.08           C  
ANISOU  366  CA  ILE A  46     4340   3209   4257    466    134    306       C  
ATOM    367  C   ILE A  46      60.081  56.193  74.728  1.00 33.31           C  
ANISOU  367  C   ILE A  46     4728   3312   4613    329    140    272       C  
ATOM    368  O   ILE A  46      60.070  57.007  75.661  1.00 35.25           O  
ANISOU  368  O   ILE A  46     5092   3339   4958    334    172    178       O  
ATOM    369  CB  ILE A  46      58.598  54.209  75.235  1.00 29.39           C  
ANISOU  369  CB  ILE A  46     4085   3129   3953    452    130    132       C  
ATOM    370  CG1 ILE A  46      59.458  53.030  74.768  1.00 27.15           C  
ANISOU  370  CG1 ILE A  46     3740   3022   3554    335    101    110       C  
ATOM    371  CG2 ILE A  46      57.054  53.820  75.285  1.00 24.89           C  
ANISOU  371  CG2 ILE A  46     3428   2666   3361    596    139    147       C  
ATOM    372  CD1 ILE A  46      59.794  52.023  75.940  1.00 22.76           C  
ANISOU  372  CD1 ILE A  46     3184   2508   2956    289    104    -54       C  
ATOM    373  N   MET A  47      61.176  55.980  74.001  1.00 33.23           N  
ANISOU  373  N   MET A  47     4680   3389   4558    197    117    346       N  
ATOM    374  CA  MET A  47      62.399  56.745  74.333  1.00 35.04           C  
ANISOU  374  CA  MET A  47     4983   3462   4868     41    113    339       C  
ATOM    375  C   MET A  47      63.088  57.205  73.067  1.00 35.72           C  
ANISOU  375  C   MET A  47     5033   3577   4961    -35    118    543       C  
ATOM    376  O   MET A  47      63.129  56.484  72.080  1.00 34.41           O  
ANISOU  376  O   MET A  47     4767   3626   4678    -21    120    630       O  
ATOM    377  CB  MET A  47      63.383  55.967  75.223  1.00 34.00           C  
ANISOU  377  CB  MET A  47     4819   3416   4680    -86     83    193       C  
ATOM    378  CG  MET A  47      62.836  55.579  76.606  1.00 37.74           C  
ANISOU  378  CG  MET A  47     5342   3865   5129    -40     77      0       C  
ATOM    379  SD  MET A  47      62.656  57.062  77.670  1.00 45.17           S  
ANISOU  379  SD  MET A  47     6484   4486   6190    -72    100   -114       S  
ATOM    380  CE  MET A  47      64.382  57.624  77.683  1.00 48.79           C  
ANISOU  380  CE  MET A  47     6957   4891   6690   -345     38    -82       C  
ATOM    381  N   SER A  48      63.588  58.432  73.125  1.00 37.14           N  
ANISOU  381  N   SER A  48     5309   3528   5273   -123    127    612       N  
ATOM    382  CA  SER A  48      64.428  59.003  72.090  1.00 38.55           C  
ANISOU  382  CA  SER A  48     5462   3707   5477   -237    137    815       C  
ATOM    383  C   SER A  48      65.769  59.355  72.695  1.00 38.83           C  
ANISOU  383  C   SER A  48     5518   3658   5576   -461    118    759       C  
ATOM    384  O   SER A  48      65.812  59.909  73.796  1.00 40.54           O  
ANISOU  384  O   SER A  48     5854   3668   5882   -524     99    611       O  
ATOM    385  CB  SER A  48      63.798  60.277  71.558  1.00 39.88           C  
ANISOU  385  CB  SER A  48     5728   3648   5776   -160    165    995       C  
ATOM    386  OG  SER A  48      62.523  59.959  71.084  1.00 40.28           O  
ANISOU  386  OG  SER A  48     5731   3805   5768     44    166   1060       O  
ATOM    387  N   ILE A  49      66.852  59.035  71.998  1.00 37.35           N  
ANISOU  387  N   ILE A  49     5211   3646   5334   -587    125    871       N  
ATOM    388  CA  ILE A  49      68.155  59.463  72.454  1.00 38.29           C  
ANISOU  388  CA  ILE A  49     5311   3710   5525   -820     98    867       C  
ATOM    389  C   ILE A  49      69.003  59.886  71.267  1.00 39.63           C  
ANISOU  389  C   ILE A  49     5397   3953   5705   -936    142   1111       C  
ATOM    390  O   ILE A  49      68.866  59.327  70.171  1.00 37.11           O  
ANISOU  390  O   ILE A  49     4986   3843   5269   -842    195   1234       O  
ATOM    391  CB  ILE A  49      68.856  58.442  73.391  1.00 38.17           C  
ANISOU  391  CB  ILE A  49     5189   3872   5439   -885     52    704       C  
ATOM    392  CG1 ILE A  49      70.087  59.103  74.054  1.00 39.02           C  
ANISOU  392  CG1 ILE A  49     5286   3903   5634  -1153     -7    697       C  
ATOM    393  CG2 ILE A  49      69.152  57.090  72.659  1.00 34.89           C  
ANISOU  393  CG2 ILE A  49     4595   3772   4887   -793    101    751       C  
ATOM    394  CD1 ILE A  49      70.650  58.258  75.227  1.00 40.05           C  
ANISOU  394  CD1 ILE A  49     5328   4186   5701  -1217    -81    541       C  
ATOM    395  N   TYR A  50      69.796  60.940  71.483  1.00 41.39           N  
ANISOU  395  N   TYR A  50     5673   3988   6063  -1151    123   1177       N  
ATOM    396  CA  TYR A  50      70.625  61.483  70.444  1.00 44.99           C  
ANISOU  396  CA  TYR A  50     6055   4489   6550  -1292    169   1427       C  
ATOM    397  C   TYR A  50      72.069  61.656  70.859  1.00 47.11           C  
ANISOU  397  C   TYR A  50     6213   4809   6876  -1568    135   1443       C  
ATOM    398  O   TYR A  50      72.966  61.643  69.994  1.00 48.44           O  
ANISOU  398  O   TYR A  50     6230   5152   7022  -1675    190   1643       O  
ATOM    399  CB  TYR A  50      70.098  62.826  69.962  1.00 47.75           C  
ANISOU  399  CB  TYR A  50     6572   4533   7038  -1296    194   1593       C  
ATOM    400  CG  TYR A  50      68.613  62.873  69.876  1.00 48.96           C  
ANISOU  400  CG  TYR A  50     6840   4578   7183  -1032    205   1566       C  
ATOM    401  CD1 TYR A  50      67.951  62.390  68.751  1.00 51.22           C  
ANISOU  401  CD1 TYR A  50     7050   5078   7333   -854    240   1719       C  
ATOM    402  CD2 TYR A  50      67.861  63.395  70.925  1.00 51.25           C  
ANISOU  402  CD2 TYR A  50     7306   4574   7591   -964    185   1385       C  
ATOM    403  CE1 TYR A  50      66.562  62.426  68.664  1.00 52.20           C  
ANISOU  403  CE1 TYR A  50     7241   5140   7450   -620    235   1720       C  
ATOM    404  CE2 TYR A  50      66.477  63.447  70.855  1.00 53.63           C  
ANISOU  404  CE2 TYR A  50     7680   4796   7901   -704    208   1382       C  
ATOM    405  CZ  TYR A  50      65.828  62.963  69.716  1.00 53.69           C  
ANISOU  405  CZ  TYR A  50     7579   5035   7784   -535    223   1564       C  
ATOM    406  OH  TYR A  50      64.447  63.017  69.634  1.00 56.27           O  
ANISOU  406  OH  TYR A  50     7940   5318   8121   -288    230   1588       O  
ATOM    407  N   SER A  51      72.323  61.863  72.149  1.00 47.05           N  
ANISOU  407  N   SER A  51     6272   4670   6934  -1702     46   1250       N  
ATOM    408  CA  SER A  51      73.717  61.955  72.527  1.00 49.70           C  
ANISOU  408  CA  SER A  51     6463   5112   7307  -1983     -8   1285       C  
ATOM    409  C   SER A  51      74.227  60.846  73.439  1.00 48.44           C  
ANISOU  409  C   SER A  51     6144   5205   7053  -1985    -77   1134       C  
ATOM    410  O   SER A  51      73.458  60.195  74.165  1.00 45.61           O  
ANISOU  410  O   SER A  51     5854   4852   6622  -1818   -106    941       O  
ATOM    411  CB  SER A  51      74.112  63.370  73.005  1.00 52.70           C  
ANISOU  411  CB  SER A  51     7004   5163   7854  -2273    -65   1286       C  
ATOM    412  OG  SER A  51      73.049  64.029  73.670  1.00 54.52           O  
ANISOU  412  OG  SER A  51     7515   5046   8151  -2191    -76   1108       O  
ATOM    413  N   ASN A  52      75.538  60.627  73.340  1.00 50.07           N  
ANISOU  413  N   ASN A  52     6118   5636   7267  -2168    -94   1258       N  
ATOM    414  CA  ASN A  52      76.253  59.680  74.189  1.00 51.08           C  
ANISOU  414  CA  ASN A  52     6052   6021   7335  -2201   -169   1181       C  
ATOM    415  C   ASN A  52      75.868  59.817  75.675  1.00 51.38           C  
ANISOU  415  C   ASN A  52     6244   5921   7354  -2275   -306    934       C  
ATOM    416  O   ASN A  52      75.733  60.936  76.200  1.00 52.67           O  
ANISOU  416  O   ASN A  52     6610   5809   7592  -2472   -372    844       O  
ATOM    417  CB  ASN A  52      77.771  59.859  73.995  1.00 53.60           C  
ANISOU  417  CB  ASN A  52     6109   6544   7713  -2461   -190   1375       C  
ATOM    418  CG  ASN A  52      78.534  58.538  74.061  1.00 54.47           C  
ANISOU  418  CG  ASN A  52     5914   7026   7754  -2347   -164   1436       C  
ATOM    419  OD1 ASN A  52      78.419  57.691  73.169  1.00 51.72           O  
ANISOU  419  OD1 ASN A  52     5467   6837   7344  -2107    -18   1510       O  
ATOM    420  ND2 ASN A  52      79.315  58.359  75.126  1.00 56.08           N  
ANISOU  420  ND2 ASN A  52     5972   7367   7966  -2519   -305   1405       N  
ATOM    421  N   GLY A  53      75.665  58.683  76.336  1.00 49.79           N  
ANISOU  421  N   GLY A  53     5967   5899   7049  -2116   -336    822       N  
ATOM    422  CA  GLY A  53      75.403  58.667  77.767  1.00 50.68           C  
ANISOU  422  CA  GLY A  53     6193   5956   7105  -2189   -463    608       C  
ATOM    423  C   GLY A  53      74.012  58.142  78.025  1.00 48.63           C  
ANISOU  423  C   GLY A  53     6104   5600   6772  -1907   -411    442       C  
ATOM    424  O   GLY A  53      73.496  57.418  77.196  1.00 46.56           O  
ANISOU  424  O   GLY A  53     5791   5416   6483  -1664   -304    505       O  
ATOM    425  N   ASP A  54      73.424  58.538  79.160  1.00 49.77           N  
ANISOU  425  N   ASP A  54     6451   5583   6876  -1959   -481    229       N  
ATOM    426  CA  ASP A  54      72.121  58.053  79.655  1.00 48.66           C  
ANISOU  426  CA  ASP A  54     6457   5373   6657  -1718   -439     60       C  
ATOM    427  C   ASP A  54      71.000  59.085  79.533  1.00 48.79           C  
ANISOU  427  C   ASP A  54     6745   5048   6743  -1643   -366    -41       C  
ATOM    428  O   ASP A  54      71.216  60.252  79.797  1.00 50.69           O  
ANISOU  428  O   ASP A  54     7144   5053   7061  -1839   -391    -97       O  
ATOM    429  CB  ASP A  54      72.187  57.733  81.160  1.00 49.35           C  
ANISOU  429  CB  ASP A  54     6583   5544   6623  -1810   -551   -115       C  
ATOM    430  CG  ASP A  54      73.220  56.690  81.506  1.00 53.06           C  
ANISOU  430  CG  ASP A  54     6784   6352   7023  -1863   -639     -7       C  
ATOM    431  OD1 ASP A  54      73.477  55.785  80.678  1.00 55.41           O  
ANISOU  431  OD1 ASP A  54     6884   6821   7346  -1701   -568    153       O  
ATOM    432  OD2 ASP A  54      73.767  56.767  82.637  1.00 57.38           O  
ANISOU  432  OD2 ASP A  54     7320   6997   7484  -2065   -776    -82       O  
ATOM    433  N   LYS A  55      69.794  58.619  79.207  1.00 46.52           N  
ANISOU  433  N   LYS A  55     6508   4736   6432  -1363   -276    -68       N  
ATOM    434  CA  LYS A  55      68.568  59.406  79.285  1.00 46.82           C  
ANISOU  434  CA  LYS A  55     6772   4490   6527  -1230   -200   -167       C  
ATOM    435  C   LYS A  55      67.488  58.599  79.996  1.00 45.17           C  
ANISOU  435  C   LYS A  55     6594   4355   6213  -1021   -172   -313       C  
ATOM    436  O   LYS A  55      67.355  57.386  79.791  1.00 42.64           O  
ANISOU  436  O   LYS A  55     6118   4274   5809   -894   -170   -265       O  
ATOM    437  CB  LYS A  55      68.094  59.795  77.896  1.00 47.04           C  
ANISOU  437  CB  LYS A  55     6793   4427   6652  -1091   -111     21       C  
ATOM    438  CG  LYS A  55      67.075  60.924  77.869  1.00 50.31           C  
ANISOU  438  CG  LYS A  55     7427   4503   7183   -987    -35    -15       C  
ATOM    439  CD  LYS A  55      67.112  61.575  76.500  1.00 54.51           C  
ANISOU  439  CD  LYS A  55     7940   4943   7826   -961     15    232       C  
ATOM    440  CE  LYS A  55      65.734  62.092  76.060  1.00 57.55           C  
ANISOU  440  CE  LYS A  55     8432   5140   8293   -703    105    289       C  
ATOM    441  NZ  LYS A  55      65.781  62.643  74.664  1.00 59.02           N  
ANISOU  441  NZ  LYS A  55     8577   5286   8558   -675    141    574       N  
ATOM    442  N   GLU A  56      66.681  59.304  80.768  1.00 46.33           N  
ANISOU  442  N   GLU A  56     6950   4277   6375   -980   -130   -485       N  
ATOM    443  CA  GLU A  56      65.857  58.743  81.790  1.00 46.80           C  
ANISOU  443  CA  GLU A  56     7063   4398   6321   -860   -109   -659       C  
ATOM    444  C   GLU A  56      64.411  59.234  81.672  1.00 46.77           C  
ANISOU  444  C   GLU A  56     7190   4194   6387   -616     20   -706       C  
ATOM    445  O   GLU A  56      64.152  60.396  81.431  1.00 48.77           O  
ANISOU  445  O   GLU A  56     7597   4158   6773   -606     85   -709       O  
ATOM    446  CB  GLU A  56      66.480  59.172  83.099  1.00 49.91           C  
ANISOU  446  CB  GLU A  56     7584   4747   6630  -1095   -184   -852       C  
ATOM    447  CG  GLU A  56      65.805  58.704  84.356  1.00 53.88           C  
ANISOU  447  CG  GLU A  56     8166   5326   6977  -1028   -167  -1048       C  
ATOM    448  CD  GLU A  56      66.789  58.705  85.524  1.00 59.47           C  
ANISOU  448  CD  GLU A  56     8907   6150   7536  -1310   -299  -1175       C  
ATOM    449  OE1 GLU A  56      67.557  59.694  85.676  1.00 62.60           O  
ANISOU  449  OE1 GLU A  56     9417   6391   7974  -1563   -357  -1236       O  
ATOM    450  OE2 GLU A  56      66.815  57.692  86.257  1.00 60.32           O  
ANISOU  450  OE2 GLU A  56     8916   6517   7484  -1292   -354  -1194       O  
ATOM    451  N   ASP A  57      63.457  58.326  81.823  1.00 45.53           N  
ANISOU  451  N   ASP A  57     6955   4191   6152   -414     63   -723       N  
ATOM    452  CA  ASP A  57      62.045  58.706  81.772  1.00 44.49           C  
ANISOU  452  CA  ASP A  57     6900   3920   6084   -172    185   -749       C  
ATOM    453  C   ASP A  57      61.230  57.731  82.583  1.00 41.25           C  
ANISOU  453  C   ASP A  57     6436   3693   5542    -50    215   -852       C  
ATOM    454  O   ASP A  57      60.889  56.616  82.132  1.00 38.39           O  
ANISOU  454  O   ASP A  57     5903   3558   5126     40    195   -752       O  
ATOM    455  CB  ASP A  57      61.521  58.807  80.345  1.00 44.67           C  
ANISOU  455  CB  ASP A  57     6821   3936   6215    -16    218   -525       C  
ATOM    456  CG  ASP A  57      60.004  59.093  80.287  1.00 48.61           C  
ANISOU  456  CG  ASP A  57     7341   4347   6779    252    332   -512       C  
ATOM    457  OD1 ASP A  57      59.482  59.873  81.112  1.00 50.57           O  
ANISOU  457  OD1 ASP A  57     7754   4378   7080    321    428   -658       O  
ATOM    458  OD2 ASP A  57      59.321  58.490  79.421  1.00 53.17           O  
ANISOU  458  OD2 ASP A  57     7762   5093   7348    393    329   -358       O  
ATOM    459  N   GLY A  58      60.931  58.158  83.798  1.00 40.38           N  
ANISOU  459  N   GLY A  58     6488   3480   5374    -65    270  -1058       N  
ATOM    460  CA  GLY A  58      60.245  57.318  84.738  1.00 37.71           C  
ANISOU  460  CA  GLY A  58     6117   3317   4891     18    306  -1162       C  
ATOM    461  C   GLY A  58      61.091  56.085  84.988  1.00 35.09           C  
ANISOU  461  C   GLY A  58     5641   3267   4422   -120    178  -1117       C  
ATOM    462  O   GLY A  58      62.217  56.190  85.469  1.00 34.54           O  
ANISOU  462  O   GLY A  58     5605   3229   4287   -336     78  -1164       O  
ATOM    463  N   ARG A  59      60.552  54.920  84.650  1.00 32.33           N  
ANISOU  463  N   ARG A  59     5126   3119   4038      0    181  -1013       N  
ATOM    464  CA  ARG A  59      61.259  53.701  84.926  1.00 31.17           C  
ANISOU  464  CA  ARG A  59     4852   3205   3783    -93     87   -961       C  
ATOM    465  C   ARG A  59      62.167  53.291  83.783  1.00 30.22           C  
ANISOU  465  C   ARG A  59     4597   3151   3734   -150     15   -795       C  
ATOM    466  O   ARG A  59      62.841  52.295  83.902  1.00 29.65           O  
ANISOU  466  O   ARG A  59     4411   3250   3603   -206    -47   -733       O  
ATOM    467  CB  ARG A  59      60.278  52.573  85.306  1.00 30.07           C  
ANISOU  467  CB  ARG A  59     4627   3231   3565     36    138   -951       C  
ATOM    468  CG  ARG A  59      59.638  52.768  86.690  1.00 29.79           C  
ANISOU  468  CG  ARG A  59     4708   3204   3406     54    207  -1113       C  
ATOM    469  CD  ARG A  59      58.822  51.543  87.117  1.00 31.42           C  
ANISOU  469  CD  ARG A  59     4809   3601   3527    144    248  -1072       C  
ATOM    470  NE  ARG A  59      57.667  51.245  86.245  1.00 29.00           N  
ANISOU  470  NE  ARG A  59     4396   3300   3319    313    323   -981       N  
ATOM    471  CZ  ARG A  59      57.626  50.345  85.270  1.00 31.42           C  
ANISOU  471  CZ  ARG A  59     4563   3694   3681    333    281   -844       C  
ATOM    472  NH1 ARG A  59      58.662  49.566  84.979  1.00 29.30           N  
ANISOU  472  NH1 ARG A  59     4234   3498   3397    231    191   -772       N  
ATOM    473  NH2 ARG A  59      56.517  50.191  84.577  1.00 29.71           N  
ANISOU  473  NH2 ARG A  59     4260   3499   3528    457    337   -779       N  
ATOM    474  N   PHE A  60      62.160  54.054  82.680  1.00 30.75           N  
ANISOU  474  N   PHE A  60     4675   3083   3926   -120     38   -713       N  
ATOM    475  CA  PHE A  60      62.953  53.756  81.486  1.00 29.51           C  
ANISOU  475  CA  PHE A  60     4396   2992   3821   -164     -2   -555       C  
ATOM    476  C   PHE A  60      64.261  54.511  81.551  1.00 30.58           C  
ANISOU  476  C   PHE A  60     4562   3061   3993   -364    -69   -541       C  
ATOM    477  O   PHE A  60      64.278  55.727  81.812  1.00 31.71           O  
ANISOU  477  O   PHE A  60     4853   2997   4195   -436    -59   -611       O  
ATOM    478  CB  PHE A  60      62.237  54.192  80.167  1.00 29.54           C  
ANISOU  478  CB  PHE A  60     4386   2920   3918    -38     54   -438       C  
ATOM    479  CG  PHE A  60      60.953  53.425  79.875  1.00 30.19           C  
ANISOU  479  CG  PHE A  60     4400   3104   3967    133    102   -418       C  
ATOM    480  CD1 PHE A  60      60.940  52.017  79.894  1.00 26.90           C  
ANISOU  480  CD1 PHE A  60     3875   2879   3465    142     86   -412       C  
ATOM    481  CD2 PHE A  60      59.771  54.112  79.550  1.00 28.26           C  
ANISOU  481  CD2 PHE A  60     4188   2759   3787    280    163   -388       C  
ATOM    482  CE1 PHE A  60      59.740  51.291  79.651  1.00 28.17           C  
ANISOU  482  CE1 PHE A  60     3974   3134   3595    259    121   -399       C  
ATOM    483  CE2 PHE A  60      58.562  53.415  79.289  1.00 30.04           C  
ANISOU  483  CE2 PHE A  60     4320   3112   3980    414    192   -354       C  
ATOM    484  CZ  PHE A  60      58.538  51.987  79.335  1.00 26.06           C  
ANISOU  484  CZ  PHE A  60     3718   2805   3379    386    166   -367       C  
ATOM    485  N   THR A  61      65.332  53.797  81.242  1.00 29.18           N  
ANISOU  485  N   THR A  61     4241   3049   3797   -450   -127   -442       N  
ATOM    486  CA  THR A  61      66.613  54.396  80.973  1.00 32.12           C  
ANISOU  486  CA  THR A  61     4574   3407   4221   -636   -186   -369       C  
ATOM    487  C   THR A  61      67.088  53.910  79.616  1.00 30.79           C  
ANISOU  487  C   THR A  61     4257   3343   4097   -591   -151   -194       C  
ATOM    488  O   THR A  61      67.059  52.725  79.373  1.00 29.13           O  
ANISOU  488  O   THR A  61     3934   3293   3840   -491   -126   -154       O  
ATOM    489  CB  THR A  61      67.655  53.982  82.046  1.00 33.72           C  
ANISOU  489  CB  THR A  61     4705   3763   4343   -801   -292   -398       C  
ATOM    490  OG1 THR A  61      67.164  54.378  83.345  1.00 39.54           O  
ANISOU  490  OG1 THR A  61     5600   4431   4993   -852   -320   -580       O  
ATOM    491  CG2 THR A  61      69.017  54.668  81.793  1.00 36.37           C  
ANISOU  491  CG2 THR A  61     4973   4105   4739  -1028   -366   -309       C  
ATOM    492  N   ALA A  62      67.477  54.847  78.740  1.00 32.12           N  
ANISOU  492  N   ALA A  62     4444   3407   4353   -664   -134    -95       N  
ATOM    493  CA  ALA A  62      68.139  54.581  77.456  1.00 31.67           C  
ANISOU  493  CA  ALA A  62     4250   3460   4320   -664    -93     76       C  
ATOM    494  C   ALA A  62      69.609  54.915  77.649  1.00 33.48           C  
ANISOU  494  C   ALA A  62     4379   3751   4589   -879   -153    150       C  
ATOM    495  O   ALA A  62      69.935  55.907  78.320  1.00 36.42           O  
ANISOU  495  O   ALA A  62     4846   3986   5005  -1055   -220     95       O  
ATOM    496  CB  ALA A  62      67.566  55.463  76.387  1.00 32.32           C  
ANISOU  496  CB  ALA A  62     4412   3402   4463   -615    -37    169       C  
ATOM    497  N   GLN A  63      70.509  54.097  77.117  1.00 32.42           N  
ANISOU  497  N   GLN A  63     4053   3824   4441   -875   -127    269       N  
ATOM    498  CA  GLN A  63      71.909  54.498  77.059  1.00 35.10           C  
ANISOU  498  CA  GLN A  63     4252   4247   4834  -1074   -169    389       C  
ATOM    499  C   GLN A  63      72.441  54.325  75.645  1.00 34.76           C  
ANISOU  499  C   GLN A  63     4081   4314   4812  -1034    -59    565       C  
ATOM    500  O   GLN A  63      72.278  53.259  75.020  1.00 32.90           O  
ANISOU  500  O   GLN A  63     3770   4211   4520   -858     34    586       O  
ATOM    501  CB  GLN A  63      72.795  53.676  77.998  1.00 36.23           C  
ANISOU  501  CB  GLN A  63     4228   4591   4945  -1129   -245    395       C  
ATOM    502  CG  GLN A  63      72.078  53.099  79.226  1.00 39.92           C  
ANISOU  502  CG  GLN A  63     4783   5054   5330  -1055   -307    237       C  
ATOM    503  CD  GLN A  63      73.037  52.304  80.114  1.00 45.24           C  
ANISOU  503  CD  GLN A  63     5269   5949   5969  -1112   -394    296       C  
ATOM    504  OE1 GLN A  63      72.915  51.070  80.242  1.00 45.15           O  
ANISOU  504  OE1 GLN A  63     5171   6056   5927   -939   -352    321       O  
ATOM    505  NE2 GLN A  63      74.000  53.006  80.722  1.00 47.07           N  
ANISOU  505  NE2 GLN A  63     5435   6238   6211  -1362   -519    331       N  
ATOM    506  N   LEU A  64      73.107  55.365  75.167  1.00 35.21           N  
ANISOU  506  N   LEU A  64     4121   4313   4943  -1211    -65    685       N  
ATOM    507  CA  LEU A  64      73.734  55.363  73.869  1.00 34.81           C  
ANISOU  507  CA  LEU A  64     3942   4381   4901  -1211     43    871       C  
ATOM    508  C   LEU A  64      75.234  55.340  74.056  1.00 36.03           C  
ANISOU  508  C   LEU A  64     3864   4714   5110  -1387     17   1000       C  
ATOM    509  O   LEU A  64      75.804  56.150  74.784  1.00 37.25           O  
ANISOU  509  O   LEU A  64     4016   4805   5332  -1624    -99   1004       O  
ATOM    510  CB  LEU A  64      73.304  56.612  73.080  1.00 35.21           C  
ANISOU  510  CB  LEU A  64     4139   4235   5002  -1279     69    958       C  
ATOM    511  CG  LEU A  64      73.964  56.904  71.724  1.00 38.04           C  
ANISOU  511  CG  LEU A  64     4390   4701   5362  -1328    176   1182       C  
ATOM    512  CD1 LEU A  64      73.979  55.702  70.760  1.00 37.73           C  
ANISOU  512  CD1 LEU A  64     4233   4905   5197  -1134    313   1220       C  
ATOM    513  CD2 LEU A  64      73.223  58.043  71.121  1.00 38.98           C  
ANISOU  513  CD2 LEU A  64     4691   4594   5523  -1348    185   1258       C  
ATOM    514  N   ASN A  65      75.870  54.404  73.388  1.00 35.68           N  
ANISOU  514  N   ASN A  65     3621   4899   5035  -1275    131   1104       N  
ATOM    515  CA  ASN A  65      77.318  54.342  73.353  1.00 38.47           C  
ANISOU  515  CA  ASN A  65     3704   5461   5450  -1406    142   1274       C  
ATOM    516  C   ASN A  65      77.773  54.435  71.891  1.00 39.44           C  
ANISOU  516  C   ASN A  65     3730   5696   5560  -1378    317   1449       C  
ATOM    517  O   ASN A  65      77.729  53.450  71.162  1.00 39.32           O  
ANISOU  517  O   ASN A  65     3653   5815   5471  -1166    472   1455       O  
ATOM    518  CB  ASN A  65      77.798  53.042  74.007  1.00 37.15           C  
ANISOU  518  CB  ASN A  65     3351   5491   5272  -1269    144   1259       C  
ATOM    519  CG  ASN A  65      79.292  53.003  74.170  1.00 40.44           C  
ANISOU  519  CG  ASN A  65     3451   6144   5767  -1403    128   1452       C  
ATOM    520  OD1 ASN A  65      80.043  53.399  73.265  1.00 38.81           O  
ANISOU  520  OD1 ASN A  65     3103   6040   5600  -1483    229   1623       O  
ATOM    521  ND2 ASN A  65      79.742  52.546  75.341  1.00 39.62           N  
ANISOU  521  ND2 ASN A  65     3219   6151   5682  -1439     -1   1447       N  
ATOM    522  N   LYS A  66      78.121  55.631  71.444  1.00 41.29           N  
ANISOU  522  N   LYS A  66     3981   5854   5852  -1591    302   1580       N  
ATOM    523  CA  LYS A  66      78.539  55.834  70.055  1.00 43.16           C  
ANISOU  523  CA  LYS A  66     4134   6206   6058  -1588    468   1770       C  
ATOM    524  C   LYS A  66      79.854  55.132  69.683  1.00 44.19           C  
ANISOU  524  C   LYS A  66     3938   6649   6203  -1568    597   1928       C  
ATOM    525  O   LYS A  66      79.983  54.605  68.600  1.00 45.01           O  
ANISOU  525  O   LYS A  66     3980   6902   6219  -1420    790   1998       O  
ATOM    526  CB  LYS A  66      78.535  57.314  69.685  1.00 45.03           C  
ANISOU  526  CB  LYS A  66     4482   6258   6366  -1823    424   1896       C  
ATOM    527  CG  LYS A  66      77.091  57.859  69.638  1.00 45.24           C  
ANISOU  527  CG  LYS A  66     4824   5997   6365  -1738    375   1777       C  
ATOM    528  CD  LYS A  66      77.030  59.304  69.165  1.00 51.61           C  
ANISOU  528  CD  LYS A  66     5759   6588   7262  -1930    359   1929       C  
ATOM    529  CE  LYS A  66      76.486  59.385  67.760  1.00 53.95           C  
ANISOU  529  CE  LYS A  66     6117   6928   7452  -1797    491   2074       C  
ATOM    530  NZ  LYS A  66      76.865  60.698  67.144  1.00 60.31           N  
ANISOU  530  NZ  LYS A  66     6958   7601   8353  -2014    508   2314       N  
ATOM    531  N   ALA A  67      80.811  55.087  70.593  1.00 46.30           N  
ANISOU  531  N   ALA A  67     3993   7030   6569  -1706    495   1982       N  
ATOM    532  CA  ALA A  67      82.080  54.421  70.328  1.00 48.26           C  
ANISOU  532  CA  ALA A  67     3890   7588   6856  -1668    616   2157       C  
ATOM    533  C   ALA A  67      81.859  52.934  70.056  1.00 46.34           C  
ANISOU  533  C   ALA A  67     3608   7459   6539  -1317    782   2069       C  
ATOM    534  O   ALA A  67      82.384  52.398  69.086  1.00 47.93           O  
ANISOU  534  O   ALA A  67     3665   7842   6705  -1178   1006   2171       O  
ATOM    535  CB  ALA A  67      83.068  54.627  71.502  1.00 50.72           C  
ANISOU  535  CB  ALA A  67     3968   8018   7285  -1889    433   2238       C  
ATOM    536  N   SER A  68      81.063  52.271  70.880  1.00 43.23           N  
ANISOU  536  N   SER A  68     3360   6946   6118  -1176    690   1874       N  
ATOM    537  CA  SER A  68      80.786  50.847  70.636  1.00 41.67           C  
ANISOU  537  CA  SER A  68     3161   6808   5864   -858    849   1779       C  
ATOM    538  C   SER A  68      79.572  50.597  69.713  1.00 38.97           C  
ANISOU  538  C   SER A  68     3102   6327   5375   -705    961   1620       C  
ATOM    539  O   SER A  68      79.213  49.439  69.399  1.00 37.28           O  
ANISOU  539  O   SER A  68     2939   6128   5097   -467   1100   1508       O  
ATOM    540  CB  SER A  68      80.621  50.129  71.965  1.00 40.30           C  
ANISOU  540  CB  SER A  68     2971   6604   5736   -783    708   1683       C  
ATOM    541  OG  SER A  68      81.827  50.278  72.675  1.00 43.67           O  
ANISOU  541  OG  SER A  68     3098   7219   6274   -919    614   1861       O  
ATOM    542  N   GLN A  69      78.914  51.687  69.323  1.00 37.07           N  
ANISOU  542  N   GLN A  69     3050   5945   5087   -852    889   1614       N  
ATOM    543  CA  GLN A  69      77.755  51.587  68.462  1.00 35.95           C  
ANISOU  543  CA  GLN A  69     3151   5706   4801   -740    958   1503       C  
ATOM    544  C   GLN A  69      76.631  50.646  68.997  1.00 33.05           C  
ANISOU  544  C   GLN A  69     2957   5219   4378   -560    914   1274       C  
ATOM    545  O   GLN A  69      76.210  49.680  68.314  1.00 31.85           O  
ANISOU  545  O   GLN A  69     2874   5112   4115   -382   1057   1176       O  
ATOM    546  CB  GLN A  69      78.221  51.195  67.055  1.00 36.75           C  
ANISOU  546  CB  GLN A  69     3175   5996   4789   -648   1202   1592       C  
ATOM    547  CG  GLN A  69      79.251  52.222  66.509  1.00 43.96           C  
ANISOU  547  CG  GLN A  69     3919   7030   5753   -849   1246   1843       C  
ATOM    548  CD  GLN A  69      79.649  51.990  65.065  1.00 48.07           C  
ANISOU  548  CD  GLN A  69     4383   7751   6130   -779   1498   1944       C  
ATOM    549  OE1 GLN A  69      80.742  52.390  64.643  1.00 53.36           O  
ANISOU  549  OE1 GLN A  69     4835   8592   6844   -883   1601   2153       O  
ATOM    550  NE2 GLN A  69      78.761  51.356  64.296  1.00 47.68           N  
ANISOU  550  NE2 GLN A  69     4526   7696   5892   -620   1598   1798       N  
ATOM    551  N   TYR A  70      76.162  50.920  70.214  1.00 31.07           N  
ANISOU  551  N   TYR A  70     2783   4822   4198   -621    724   1185       N  
ATOM    552  CA  TYR A  70      74.927  50.302  70.705  1.00 29.23           C  
ANISOU  552  CA  TYR A  70     2735   4459   3911   -492    667    990       C  
ATOM    553  C   TYR A  70      74.083  51.322  71.449  1.00 30.35           C  
ANISOU  553  C   TYR A  70     3043   4404   4083   -609    489    924       C  
ATOM    554  O   TYR A  70      74.618  52.345  71.960  1.00 32.36           O  
ANISOU  554  O   TYR A  70     3263   4606   4426   -799    385    999       O  
ATOM    555  CB  TYR A  70      75.210  49.039  71.588  1.00 28.06           C  
ANISOU  555  CB  TYR A  70     2491   4362   3808   -357    676    922       C  
ATOM    556  CG  TYR A  70      75.867  49.321  72.933  1.00 27.68           C  
ANISOU  556  CG  TYR A  70     2318   4332   3866   -476    516    972       C  
ATOM    557  CD1 TYR A  70      75.144  49.847  74.006  1.00 26.82           C  
ANISOU  557  CD1 TYR A  70     2349   4081   3758   -569    338    866       C  
ATOM    558  CD2 TYR A  70      77.211  49.075  73.121  1.00 30.61           C  
ANISOU  558  CD2 TYR A  70     2422   4883   4323   -502    546   1131       C  
ATOM    559  CE1 TYR A  70      75.762  50.103  75.249  1.00 29.43           C  
ANISOU  559  CE1 TYR A  70     2580   4454   4146   -705    183    898       C  
ATOM    560  CE2 TYR A  70      77.835  49.337  74.334  1.00 32.72           C  
ANISOU  560  CE2 TYR A  70     2559   5210   4663   -639    377   1192       C  
ATOM    561  CZ  TYR A  70      77.108  49.840  75.400  1.00 30.66           C  
ANISOU  561  CZ  TYR A  70     2464   4811   4374   -750    190   1066       C  
ATOM    562  OH  TYR A  70      77.760  50.073  76.586  1.00 30.43           O  
ANISOU  562  OH  TYR A  70     2314   4869   4380   -908     19   1117       O  
ATOM    563  N   VAL A  71      72.781  51.028  71.510  1.00 29.96           N  
ANISOU  563  N   VAL A  71     3172   4245   3963   -501    464    781       N  
ATOM    564  CA  VAL A  71      71.788  51.731  72.316  1.00 30.10           C  
ANISOU  564  CA  VAL A  71     3353   4075   4006   -542    328    685       C  
ATOM    565  C   VAL A  71      71.180  50.600  73.187  1.00 28.37           C  
ANISOU  565  C   VAL A  71     3164   3855   3759   -413    304    532       C  
ATOM    566  O   VAL A  71      70.945  49.501  72.684  1.00 27.20           O  
ANISOU  566  O   VAL A  71     3005   3782   3544   -279    401    488       O  
ATOM    567  CB  VAL A  71      70.560  52.234  71.490  1.00 29.60           C  
ANISOU  567  CB  VAL A  71     3451   3919   3874   -487    341    676       C  
ATOM    568  CG1 VAL A  71      70.043  53.566  71.991  1.00 30.59           C  
ANISOU  568  CG1 VAL A  71     3704   3836   4082   -577    239    680       C  
ATOM    569  CG2 VAL A  71      70.833  52.246  70.058  1.00 34.87           C  
ANISOU  569  CG2 VAL A  71     4081   4708   4459   -476    455    798       C  
ATOM    570  N   SER A  72      70.924  50.893  74.458  1.00 27.32           N  
ANISOU  570  N   SER A  72     3083   3630   3666   -468    183    452       N  
ATOM    571  CA  SER A  72      70.240  49.988  75.372  1.00 28.11           C  
ANISOU  571  CA  SER A  72     3228   3718   3733   -366    151    325       C  
ATOM    572  C   SER A  72      68.926  50.573  75.875  1.00 26.41           C  
ANISOU  572  C   SER A  72     3187   3349   3497   -352     89    210       C  
ATOM    573  O   SER A  72      68.707  51.775  75.786  1.00 26.96           O  
ANISOU  573  O   SER A  72     3344   3296   3603   -431     53    224       O  
ATOM    574  CB  SER A  72      71.071  49.675  76.604  1.00 28.25           C  
ANISOU  574  CB  SER A  72     3139   3807   3787   -430     69    336       C  
ATOM    575  OG  SER A  72      72.278  49.032  76.293  1.00 33.34           O  
ANISOU  575  OG  SER A  72     3587   4608   4471   -412    130    461       O  
ATOM    576  N   LEU A  73      68.069  49.699  76.395  1.00 25.39           N  
ANISOU  576  N   LEU A  73     3103   3222   3321   -244     91    109       N  
ATOM    577  CA  LEU A  73      66.919  50.138  77.146  1.00 25.89           C  
ANISOU  577  CA  LEU A  73     3296   3171   3368   -222     41      2       C  
ATOM    578  C   LEU A  73      66.908  49.292  78.408  1.00 25.69           C  
ANISOU  578  C   LEU A  73     3250   3197   3312   -204      2    -67       C  
ATOM    579  O   LEU A  73      66.996  48.063  78.320  1.00 25.56           O  
ANISOU  579  O   LEU A  73     3167   3267   3278   -123     48    -53       O  
ATOM    580  CB  LEU A  73      65.603  49.947  76.365  1.00 25.04           C  
ANISOU  580  CB  LEU A  73     3255   3040   3218   -106     90    -25       C  
ATOM    581  CG  LEU A  73      64.275  50.387  77.076  1.00 25.61           C  
ANISOU  581  CG  LEU A  73     3432   3012   3286    -50     63   -116       C  
ATOM    582  CD1 LEU A  73      64.179  51.881  77.355  1.00 24.88           C  
ANISOU  582  CD1 LEU A  73     3436   2756   3261   -101     34   -118       C  
ATOM    583  CD2 LEU A  73      63.072  49.952  76.264  1.00 22.90           C  
ANISOU  583  CD2 LEU A  73     3095   2711   2895     52     99   -112       C  
ATOM    584  N   LEU A  74      66.805  49.963  79.555  1.00 25.23           N  
ANISOU  584  N   LEU A  74     3263   3078   3243   -282    -74   -140       N  
ATOM    585  CA  LEU A  74      66.642  49.326  80.856  1.00 24.84           C  
ANISOU  585  CA  LEU A  74     3219   3088   3132   -278   -118   -204       C  
ATOM    586  C   LEU A  74      65.257  49.691  81.372  1.00 25.81           C  
ANISOU  586  C   LEU A  74     3481   3112   3213   -215    -99   -327       C  
ATOM    587  O   LEU A  74      64.849  50.876  81.358  1.00 27.10           O  
ANISOU  587  O   LEU A  74     3755   3138   3404   -244    -97   -385       O  
ATOM    588  CB  LEU A  74      67.706  49.811  81.826  1.00 24.91           C  
ANISOU  588  CB  LEU A  74     3194   3147   3121   -443   -224   -195       C  
ATOM    589  CG  LEU A  74      69.102  49.173  81.770  1.00 27.22           C  
ANISOU  589  CG  LEU A  74     3295   3604   3444   -492   -259    -50       C  
ATOM    590  CD1 LEU A  74      69.705  49.330  80.382  1.00 24.36           C  
ANISOU  590  CD1 LEU A  74     2845   3243   3168   -479   -187     55       C  
ATOM    591  CD2 LEU A  74      70.049  49.782  82.776  1.00 26.09           C  
ANISOU  591  CD2 LEU A  74     3111   3537   3262   -693   -395    -40       C  
ATOM    592  N   ILE A  75      64.527  48.679  81.820  1.00 24.99           N  
ANISOU  592  N   ILE A  75     3367   3069   3057   -124    -70   -356       N  
ATOM    593  CA  ILE A  75      63.224  48.905  82.419  1.00 25.51           C  
ANISOU  593  CA  ILE A  75     3530   3081   3079    -60    -38   -458       C  
ATOM    594  C   ILE A  75      63.366  48.572  83.891  1.00 25.96           C  
ANISOU  594  C   ILE A  75     3608   3214   3039   -112    -82   -509       C  
ATOM    595  O   ILE A  75      63.358  47.392  84.281  1.00 25.69           O  
ANISOU  595  O   ILE A  75     3507   3285   2966    -77    -79   -459       O  
ATOM    596  CB  ILE A  75      62.129  48.023  81.768  1.00 25.06           C  
ANISOU  596  CB  ILE A  75     3440   3054   3026     60     28   -440       C  
ATOM    597  CG1 ILE A  75      62.130  48.242  80.251  1.00 24.83           C  
ANISOU  597  CG1 ILE A  75     3381   2999   3053     88     55   -374       C  
ATOM    598  CG2 ILE A  75      60.764  48.368  82.399  1.00 24.94           C  
ANISOU  598  CG2 ILE A  75     3492   3006   2978    130     69   -523       C  
ATOM    599  CD1 ILE A  75      60.922  47.660  79.501  1.00 24.52           C  
ANISOU  599  CD1 ILE A  75     3322   2995   2999    172    100   -369       C  
ATOM    600  N   ARG A  76      63.494  49.612  84.706  1.00 26.53           N  
ANISOU  600  N   ARG A  76     3786   3229   3064   -203   -118   -608       N  
ATOM    601  CA  ARG A  76      63.714  49.441  86.117  1.00 27.76           C  
ANISOU  601  CA  ARG A  76     3977   3481   3087   -286   -171   -666       C  
ATOM    602  C   ARG A  76      62.398  48.995  86.836  1.00 28.31           C  
ANISOU  602  C   ARG A  76     4100   3580   3072   -179    -90   -737       C  
ATOM    603  O   ARG A  76      61.289  49.276  86.351  1.00 26.07           O  
ANISOU  603  O   ARG A  76     3854   3207   2845    -61      2   -778       O  
ATOM    604  CB  ARG A  76      64.259  50.746  86.648  1.00 29.21           C  
ANISOU  604  CB  ARG A  76     4282   3580   3235   -444   -228   -778       C  
ATOM    605  CG  ARG A  76      65.680  51.115  86.096  1.00 31.36           C  
ANISOU  605  CG  ARG A  76     4469   3865   3579   -593   -323   -683       C  
ATOM    606  CD  ARG A  76      66.147  52.526  86.610  1.00 39.38           C  
ANISOU  606  CD  ARG A  76     5635   4758   4568   -792   -381   -815       C  
ATOM    607  NE  ARG A  76      65.571  53.546  85.734  1.00 43.27           N  
ANISOU  607  NE  ARG A  76     6239   5007   5194   -729   -290   -858       N  
ATOM    608  CZ  ARG A  76      65.389  54.849  85.998  1.00 46.57           C  
ANISOU  608  CZ  ARG A  76     6850   5206   5636   -811   -264  -1001       C  
ATOM    609  NH1 ARG A  76      65.781  55.419  87.140  1.00 50.47           N  
ANISOU  609  NH1 ARG A  76     7479   5686   6011  -1001   -327  -1160       N  
ATOM    610  NH2 ARG A  76      64.834  55.617  85.055  1.00 45.06           N  
ANISOU  610  NH2 ARG A  76     6726   4799   5594   -708   -174   -978       N  
ATOM    611  N   ASP A  77      62.531  48.330  87.987  1.00 29.39           N  
ANISOU  611  N   ASP A  77     4227   3863   3074   -224   -126   -729       N  
ATOM    612  CA  ASP A  77      61.360  47.879  88.789  1.00 29.85           C  
ANISOU  612  CA  ASP A  77     4327   3980   3034   -145    -43   -779       C  
ATOM    613  C   ASP A  77      60.219  47.347  87.886  1.00 27.96           C  
ANISOU  613  C   ASP A  77     4027   3691   2903      6     57   -735       C  
ATOM    614  O   ASP A  77      59.102  47.895  87.820  1.00 26.55           O  
ANISOU  614  O   ASP A  77     3898   3447   2740     95    151   -814       O  
ATOM    615  CB  ASP A  77      60.885  49.000  89.701  1.00 32.12           C  
ANISOU  615  CB  ASP A  77     4781   4214   3207   -182      2   -966       C  
ATOM    616  CG  ASP A  77      59.756  48.556  90.645  1.00 35.79           C  
ANISOU  616  CG  ASP A  77     5277   4775   3543   -106    104  -1012       C  
ATOM    617  OD1 ASP A  77      59.730  47.391  91.059  1.00 33.99           O  
ANISOU  617  OD1 ASP A  77     4960   4700   3253   -104     85   -893       O  
ATOM    618  OD2 ASP A  77      58.875  49.380  90.957  1.00 42.55           O  
ANISOU  618  OD2 ASP A  77     6245   5547   4372    -39    218  -1157       O  
ATOM    619  N   SER A  78      60.551  46.301  87.137  1.00 26.67           N  
ANISOU  619  N   SER A  78     3751   3559   2820     30     37   -605       N  
ATOM    620  CA  SER A  78      59.697  45.801  86.065  1.00 26.15           C  
ANISOU  620  CA  SER A  78     3630   3451   2853    124    103   -567       C  
ATOM    621  C   SER A  78      58.364  45.391  86.610  1.00 25.34           C  
ANISOU  621  C   SER A  78     3525   3401   2701    182    182   -589       C  
ATOM    622  O   SER A  78      58.291  44.833  87.718  1.00 24.59           O  
ANISOU  622  O   SER A  78     3436   3401   2503    154    188   -571       O  
ATOM    623  CB  SER A  78      60.338  44.576  85.418  1.00 26.37           C  
ANISOU  623  CB  SER A  78     3570   3504   2945    122     84   -451       C  
ATOM    624  OG  SER A  78      61.450  45.000  84.649  1.00 31.08           O  
ANISOU  624  OG  SER A  78     4142   4060   3606     90     39   -421       O  
ATOM    625  N   GLN A  79      57.342  45.645  85.796  1.00 23.56           N  
ANISOU  625  N   GLN A  79     3272   3135   2544    257    237   -602       N  
ATOM    626  CA  GLN A  79      55.963  45.359  86.095  1.00 23.44           C  
ANISOU  626  CA  GLN A  79     3214   3183   2508    316    318   -604       C  
ATOM    627  C   GLN A  79      55.415  44.406  85.052  1.00 22.50           C  
ANISOU  627  C   GLN A  79     3000   3087   2460    313    317   -527       C  
ATOM    628  O   GLN A  79      55.816  44.452  83.884  1.00 20.98           O  
ANISOU  628  O   GLN A  79     2795   2844   2333    304    276   -505       O  
ATOM    629  CB  GLN A  79      55.124  46.644  86.111  1.00 23.74           C  
ANISOU  629  CB  GLN A  79     3285   3169   2566    414    387   -681       C  
ATOM    630  CG  GLN A  79      55.638  47.749  87.105  1.00 26.06           C  
ANISOU  630  CG  GLN A  79     3719   3395   2786    402    405   -805       C  
ATOM    631  CD  GLN A  79      55.536  47.318  88.540  1.00 27.63           C  
ANISOU  631  CD  GLN A  79     3958   3709   2828    361    442   -848       C  
ATOM    632  OE1 GLN A  79      54.472  46.996  89.000  1.00 30.32           O  
ANISOU  632  OE1 GLN A  79     4251   4137   3130    424    537   -841       O  
ATOM    633  NE2 GLN A  79      56.652  47.308  89.254  1.00 30.36           N  
ANISOU  633  NE2 GLN A  79     4378   4081   3073    247    363   -877       N  
ATOM    634  N   PRO A  80      54.487  43.512  85.452  1.00 23.14           N  
ANISOU  634  N   PRO A  80     3020   3255   2517    300    365   -487       N  
ATOM    635  CA  PRO A  80      53.896  42.651  84.374  1.00 22.47           C  
ANISOU  635  CA  PRO A  80     2857   3186   2495    260    355   -435       C  
ATOM    636  C   PRO A  80      53.213  43.422  83.251  1.00 22.07           C  
ANISOU  636  C   PRO A  80     2749   3144   2493    308    341   -437       C  
ATOM    637  O   PRO A  80      53.206  42.960  82.114  1.00 20.23           O  
ANISOU  637  O   PRO A  80     2489   2910   2287    255    299   -415       O  
ATOM    638  CB  PRO A  80      52.878  41.836  85.153  1.00 23.84           C  
ANISOU  638  CB  PRO A  80     2968   3456   2634    227    415   -391       C  
ATOM    639  CG  PRO A  80      53.623  41.613  86.494  1.00 23.29           C  
ANISOU  639  CG  PRO A  80     2970   3394   2483    215    428   -383       C  
ATOM    640  CD  PRO A  80      54.140  43.007  86.792  1.00 23.52           C  
ANISOU  640  CD  PRO A  80     3071   3390   2473    282    417   -471       C  
ATOM    641  N   SER A  81      52.676  44.614  83.557  1.00 22.74           N  
ANISOU  641  N   SER A  81     2825   3231   2582    413    381   -461       N  
ATOM    642  CA  SER A  81      52.090  45.497  82.518  1.00 24.67           C  
ANISOU  642  CA  SER A  81     3009   3476   2888    489    366   -424       C  
ATOM    643  C   SER A  81      53.117  45.999  81.491  1.00 25.21           C  
ANISOU  643  C   SER A  81     3143   3446   2987    472    297   -420       C  
ATOM    644  O   SER A  81      52.714  46.509  80.429  1.00 26.71           O  
ANISOU  644  O   SER A  81     3279   3656   3212    508    266   -357       O  
ATOM    645  CB  SER A  81      51.328  46.679  83.120  1.00 25.05           C  
ANISOU  645  CB  SER A  81     3044   3511   2963    638    452   -441       C  
ATOM    646  OG  SER A  81      52.230  47.533  83.831  1.00 29.29           O  
ANISOU  646  OG  SER A  81     3731   3911   3484    665    476   -537       O  
ATOM    647  N   ASP A  82      54.413  45.881  81.811  1.00 24.17           N  
ANISOU  647  N   ASP A  82     3110   3234   2838    416    274   -464       N  
ATOM    648  CA  ASP A  82      55.505  46.096  80.832  1.00 25.42           C  
ANISOU  648  CA  ASP A  82     3309   3327   3020    376    220   -446       C  
ATOM    649  C   ASP A  82      55.691  44.973  79.781  1.00 25.32           C  
ANISOU  649  C   ASP A  82     3263   3366   2991    299    193   -417       C  
ATOM    650  O   ASP A  82      56.496  45.145  78.820  1.00 25.98           O  
ANISOU  650  O   ASP A  82     3369   3421   3079    274    170   -397       O  
ATOM    651  CB  ASP A  82      56.868  46.284  81.522  1.00 22.77           C  
ANISOU  651  CB  ASP A  82     3055   2920   2676    332    202   -484       C  
ATOM    652  CG  ASP A  82      56.895  47.450  82.466  1.00 25.12           C  
ANISOU  652  CG  ASP A  82     3429   3146   2970    368    222   -547       C  
ATOM    653  OD1 ASP A  82      56.265  48.517  82.153  1.00 25.64           O  
ANISOU  653  OD1 ASP A  82     3509   3145   3085    448    252   -548       O  
ATOM    654  OD2 ASP A  82      57.550  47.306  83.538  1.00 21.47           O  
ANISOU  654  OD2 ASP A  82     3016   2689   2450    314    210   -594       O  
ATOM    655  N   SER A  83      55.022  43.827  79.973  1.00 24.94           N  
ANISOU  655  N   SER A  83     3174   3382   2920    250    210   -421       N  
ATOM    656  CA  SER A  83      55.185  42.666  79.020  1.00 24.49           C  
ANISOU  656  CA  SER A  83     3122   3338   2843    158    202   -429       C  
ATOM    657  C   SER A  83      54.740  43.107  77.652  1.00 24.99           C  
ANISOU  657  C   SER A  83     3150   3469   2874    142    160   -403       C  
ATOM    658  O   SER A  83      53.568  43.448  77.472  1.00 25.17           O  
ANISOU  658  O   SER A  83     3086   3589   2885    154    133   -361       O  
ATOM    659  CB  SER A  83      54.376  41.447  79.466  1.00 24.53           C  
ANISOU  659  CB  SER A  83     3099   3380   2841     85    226   -436       C  
ATOM    660  OG  SER A  83      54.870  41.003  80.749  1.00 25.76           O  
ANISOU  660  OG  SER A  83     3288   3484   3013    102    263   -429       O  
ATOM    661  N   ALA A  84      55.678  43.165  76.703  1.00 23.87           N  
ANISOU  661  N   ALA A  84     3059   3297   2711    121    155   -410       N  
ATOM    662  CA  ALA A  84      55.370  43.670  75.382  1.00 24.43           C  
ANISOU  662  CA  ALA A  84     3106   3453   2723    101    112   -367       C  
ATOM    663  C   ALA A  84      56.512  43.305  74.453  1.00 24.55           C  
ANISOU  663  C   ALA A  84     3193   3440   2693     57    143   -398       C  
ATOM    664  O   ALA A  84      57.460  42.634  74.879  1.00 23.62           O  
ANISOU  664  O   ALA A  84     3126   3233   2614     58    202   -446       O  
ATOM    665  CB  ALA A  84      55.186  45.221  75.432  1.00 24.38           C  
ANISOU  665  CB  ALA A  84     3064   3435   2762    206     84   -277       C  
ATOM    666  N   THR A  85      56.437  43.729  73.190  1.00 24.23           N  
ANISOU  666  N   THR A  85     3147   3489   2566     26    112   -356       N  
ATOM    667  CA  THR A  85      57.654  43.691  72.397  1.00 24.91           C  
ANISOU  667  CA  THR A  85     3295   3555   2614     12    165   -367       C  
ATOM    668  C   THR A  85      58.318  45.080  72.201  1.00 24.60           C  
ANISOU  668  C   THR A  85     3240   3492   2615     75    152   -255       C  
ATOM    669  O   THR A  85      57.638  46.117  72.040  1.00 25.16           O  
ANISOU  669  O   THR A  85     3267   3595   2695    114     91   -155       O  
ATOM    670  CB  THR A  85      57.676  42.634  71.205  1.00 25.81           C  
ANISOU  670  CB  THR A  85     3473   3743   2587    -95    204   -459       C  
ATOM    671  OG1 THR A  85      58.088  43.206  69.947  1.00 32.88           O  
ANISOU  671  OG1 THR A  85     4385   4739   3368   -117    206   -405       O  
ATOM    672  CG2 THR A  85      56.495  41.807  71.113  1.00 24.80           C  
ANISOU  672  CG2 THR A  85     3342   3683   2398   -196    159   -525       C  
ATOM    673  N   TYR A  86      59.642  45.107  72.303  1.00 23.56           N  
ANISOU  673  N   TYR A  86     3134   3290   2527     88    213   -258       N  
ATOM    674  CA  TYR A  86      60.354  46.394  72.263  1.00 23.13           C  
ANISOU  674  CA  TYR A  86     3066   3191   2530    115    200   -153       C  
ATOM    675  C   TYR A  86      61.252  46.420  71.033  1.00 24.42           C  
ANISOU  675  C   TYR A  86     3238   3424   2613     75    258   -107       C  
ATOM    676  O   TYR A  86      61.943  45.440  70.760  1.00 24.67           O  
ANISOU  676  O   TYR A  86     3287   3476   2610     61    342   -179       O  
ATOM    677  CB  TYR A  86      61.161  46.641  73.527  1.00 20.95           C  
ANISOU  677  CB  TYR A  86     2786   2800   2373    137    206   -169       C  
ATOM    678  CG  TYR A  86      60.291  46.848  74.763  1.00 20.75           C  
ANISOU  678  CG  TYR A  86     2765   2715   2403    177    162   -209       C  
ATOM    679  CD1 TYR A  86      59.718  45.752  75.430  1.00 18.81           C  
ANISOU  679  CD1 TYR A  86     2515   2487   2144    181    173   -288       C  
ATOM    680  CD2 TYR A  86      59.968  48.139  75.195  1.00 21.37           C  
ANISOU  680  CD2 TYR A  86     2861   2714   2543    211    127   -168       C  
ATOM    681  CE1 TYR A  86      58.902  45.912  76.515  1.00 21.58           C  
ANISOU  681  CE1 TYR A  86     2862   2812   2524    216    152   -317       C  
ATOM    682  CE2 TYR A  86      59.127  48.336  76.323  1.00 23.98           C  
ANISOU  682  CE2 TYR A  86     3203   2997   2909    263    117   -221       C  
ATOM    683  CZ  TYR A  86      58.606  47.196  76.969  1.00 21.61           C  
ANISOU  683  CZ  TYR A  86     2881   2753   2576    263    130   -292       C  
ATOM    684  OH  TYR A  86      57.807  47.334  78.050  1.00 22.71           O  
ANISOU  684  OH  TYR A  86     3023   2874   2730    309    138   -335       O  
ATOM    685  N   LEU A  87      61.220  47.527  70.297  1.00 24.46           N  
ANISOU  685  N   LEU A  87     3234   3464   2594     68    226     21       N  
ATOM    686  CA  LEU A  87      61.780  47.572  68.977  1.00 26.87           C  
ANISOU  686  CA  LEU A  87     3547   3884   2778     22    278     83       C  
ATOM    687  C   LEU A  87      62.762  48.729  68.977  1.00 27.57           C  
ANISOU  687  C   LEU A  87     3612   3905   2957     14    291    217       C  
ATOM    688  O   LEU A  87      62.375  49.845  69.317  1.00 26.36           O  
ANISOU  688  O   LEU A  87     3461   3659   2894     36    225    312       O  
ATOM    689  CB  LEU A  87      60.696  47.856  67.913  1.00 28.68           C  
ANISOU  689  CB  LEU A  87     3777   4258   2859     -4    211    162       C  
ATOM    690  CG  LEU A  87      59.455  47.018  67.476  1.00 30.38           C  
ANISOU  690  CG  LEU A  87     3998   4611   2934    -49    155     85       C  
ATOM    691  CD1 LEU A  87      59.811  45.598  67.098  1.00 33.43           C  
ANISOU  691  CD1 LEU A  87     4452   5043   3205   -119    243    -94       C  
ATOM    692  CD2 LEU A  87      58.372  46.981  68.454  1.00 32.94           C  
ANISOU  692  CD2 LEU A  87     4279   4879   3355     -4     81     58       C  
ATOM    693  N   CYS A  88      64.004  48.414  68.594  1.00 26.97           N  
ANISOU  693  N   CYS A  88     3513   3869   2863    -15    389    222       N  
ATOM    694  CA  CYS A  88      65.066  49.350  68.341  1.00 30.55           C  
ANISOU  694  CA  CYS A  88     3925   4306   3375    -59    419    362       C  
ATOM    695  C   CYS A  88      64.811  49.988  66.960  1.00 32.04           C  
ANISOU  695  C   CYS A  88     4132   4615   3426    -95    426    508       C  
ATOM    696  O   CYS A  88      64.471  49.245  66.020  1.00 31.52           O  
ANISOU  696  O   CYS A  88     4094   4705   3175   -103    469    459       O  
ATOM    697  CB  CYS A  88      66.382  48.541  68.187  1.00 30.51           C  
ANISOU  697  CB  CYS A  88     3860   4367   3364    -63    548    325       C  
ATOM    698  SG  CYS A  88      67.696  49.626  68.179  1.00 41.52           S  
ANISOU  698  SG  CYS A  88     5166   5744   4865   -140    570    496       S  
ATOM    699  N   ALA A  89      65.056  51.303  66.815  1.00 31.33           N  
ANISOU  699  N   ALA A  89     4033   4454   3415   -130    391    686       N  
ATOM    700  CA  ALA A  89      65.059  51.952  65.509  1.00 33.10           C  
ANISOU  700  CA  ALA A  89     4261   4799   3515   -172    410    873       C  
ATOM    701  C   ALA A  89      66.115  53.040  65.478  1.00 35.21           C  
ANISOU  701  C   ALA A  89     4494   4979   3902   -247    441   1043       C  
ATOM    702  O   ALA A  89      66.367  53.714  66.479  1.00 34.67           O  
ANISOU  702  O   ALA A  89     4431   4712   4028   -268    394   1043       O  
ATOM    703  CB  ALA A  89      63.682  52.538  65.104  1.00 32.79           C  
ANISOU  703  CB  ALA A  89     4256   4777   3426   -127    303    980       C  
ATOM    704  N   VAL A  90      66.719  53.195  64.304  1.00 36.13           N  
ANISOU  704  N   VAL A  90     4583   5256   3886   -306    526   1184       N  
ATOM    705  CA  VAL A  90      67.882  53.993  64.105  1.00 37.58           C  
ANISOU  705  CA  VAL A  90     4711   5413   4154   -404    586   1350       C  
ATOM    706  C   VAL A  90      67.644  54.758  62.800  1.00 41.57           C  
ANISOU  706  C   VAL A  90     5238   6033   4522   -444    598   1594       C  
ATOM    707  O   VAL A  90      67.138  54.229  61.779  1.00 41.40           O  
ANISOU  707  O   VAL A  90     5240   6231   4258   -421    624   1601       O  
ATOM    708  CB  VAL A  90      69.138  53.082  63.979  1.00 37.59           C  
ANISOU  708  CB  VAL A  90     4612   5558   4109   -427    732   1272       C  
ATOM    709  CG1 VAL A  90      70.339  53.819  63.430  1.00 39.95           C  
ANISOU  709  CG1 VAL A  90     4821   5918   4440   -541    821   1480       C  
ATOM    710  CG2 VAL A  90      69.491  52.369  65.360  1.00 35.24           C  
ANISOU  710  CG2 VAL A  90     4270   5150   3969   -386    709   1079       C  
ATOM    711  N   THR A  91      68.047  56.002  62.813  1.00 44.63           N  
ANISOU  711  N   THR A  91     5624   6278   5054   -522    579   1802       N  
ATOM    712  CA  THR A  91      67.802  56.817  61.677  1.00 50.54           C  
ANISOU  712  CA  THR A  91     6394   7106   5699   -554    581   2073       C  
ATOM    713  C   THR A  91      68.967  56.679  60.669  1.00 53.64           C  
ANISOU  713  C   THR A  91     6709   7729   5942   -658    733   2198       C  
ATOM    714  O   THR A  91      70.146  56.617  61.053  1.00 54.22           O  
ANISOU  714  O   THR A  91     6694   7782   6122   -737    816   2173       O  
ATOM    715  CB  THR A  91      67.485  58.227  62.150  1.00 51.87           C  
ANISOU  715  CB  THR A  91     6625   6973   6107   -569    495   2246       C  
ATOM    716  OG1 THR A  91      66.315  58.676  61.470  1.00 54.94           O  
ANISOU  716  OG1 THR A  91     7064   7397   6414   -479    422   2418       O  
ATOM    717  CG2 THR A  91      68.685  59.170  61.971  1.00 55.50           C  
ANISOU  717  CG2 THR A  91     7053   7342   6692   -733    561   2449       C  
ATOM    718  N   THR A  92      68.611  56.601  59.385  1.00 56.10           N  
ANISOU  718  N   THR A  92     7040   8286   5990   -658    768   2334       N  
ATOM    719  CA  THR A  92      69.527  56.150  58.334  1.00 58.82           C  
ANISOU  719  CA  THR A  92     7325   8916   6107   -726    940   2388       C  
ATOM    720  C   THR A  92      69.614  57.140  57.165  1.00 62.38           C  
ANISOU  720  C   THR A  92     7779   9491   6430   -813    965   2741       C  
ATOM    721  O   THR A  92      70.285  56.878  56.162  1.00 63.93           O  
ANISOU  721  O   THR A  92     7934   9956   6398   -874   1116   2823       O  
ATOM    722  CB  THR A  92      69.109  54.739  57.806  1.00 58.22           C  
ANISOU  722  CB  THR A  92     7289   9088   5741   -658   1002   2142       C  
ATOM    723  OG1 THR A  92      67.780  54.812  57.280  1.00 59.75           O  
ANISOU  723  OG1 THR A  92     7567   9370   5764   -626    867   2189       O  
ATOM    724  CG2 THR A  92      69.155  53.657  58.937  1.00 54.56           C  
ANISOU  724  CG2 THR A  92     6819   8500   5411   -573   1006   1812       C  
ATOM    725  N   ASP A  93      68.894  58.258  57.303  1.00 63.88           N  
ANISOU  725  N   ASP A  93     8022   9481   6766   -804    827   2955       N  
ATOM    726  CA  ASP A  93      68.834  59.330  56.309  1.00 66.94           C  
ANISOU  726  CA  ASP A  93     8423   9929   7082   -870    824   3339       C  
ATOM    727  C   ASP A  93      69.059  60.702  56.918  1.00 67.42           C  
ANISOU  727  C   ASP A  93     8506   9622   7488   -926    771   3552       C  
ATOM    728  O   ASP A  93      68.835  60.913  58.117  1.00 64.82           O  
ANISOU  728  O   ASP A  93     8216   8980   7432   -882    692   3395       O  
ATOM    729  CB  ASP A  93      67.436  59.371  55.671  1.00 68.54           C  
ANISOU  729  CB  ASP A  93     8685  10262   7093   -775    690   3446       C  
ATOM    730  CG  ASP A  93      67.345  58.563  54.404  1.00 71.10           C  
ANISOU  730  CG  ASP A  93     9008  11023   6984   -810    755   3440       C  
ATOM    731  OD1 ASP A  93      68.265  57.743  54.152  1.00 73.36           O  
ANISOU  731  OD1 ASP A  93     9264  11485   7124   -867    921   3265       O  
ATOM    732  OD2 ASP A  93      66.341  58.748  53.674  1.00 73.26           O  
ANISOU  732  OD2 ASP A  93     9308  11466   7059   -779    641   3608       O  
ATOM    733  N   SER A  94      69.467  61.643  56.071  1.00 69.99           N  
ANISOU  733  N   SER A  94     8823   9980   7788  -1030    821   3912       N  
ATOM    734  CA  SER A  94      69.322  63.052  56.397  1.00 71.96           C  
ANISOU  734  CA  SER A  94     9139   9864   8337  -1064    755   4173       C  
ATOM    735  C   SER A  94      67.929  63.535  55.933  1.00 73.25           C  
ANISOU  735  C   SER A  94     9374  10007   8449   -911    628   4381       C  
ATOM    736  O   SER A  94      67.804  64.580  55.274  1.00 76.60           O  
ANISOU  736  O   SER A  94     9829  10360   8914   -937    620   4767       O  
ATOM    737  CB  SER A  94      70.427  63.877  55.731  1.00 75.36           C  
ANISOU  737  CB  SER A  94     9523  10312   8796  -1259    870   4496       C  
ATOM    738  OG  SER A  94      70.219  63.892  54.339  1.00 76.23           O  
ANISOU  738  OG  SER A  94     9615  10762   8587  -1262    914   4774       O  
ATOM    739  N   TRP A  95      66.917  62.716  56.221  1.00 70.93           N  
ANISOU  739  N   TRP A  95     9088   9810   8052   -758    535   4147       N  
ATOM    740  CA  TRP A  95      65.505  63.077  56.170  1.00 71.55           C  
ANISOU  740  CA  TRP A  95     9201   9828   8156   -586    395   4274       C  
ATOM    741  C   TRP A  95      64.882  62.489  57.421  1.00 68.20           C  
ANISOU  741  C   TRP A  95     8797   9227   7888   -463    328   3910       C  
ATOM    742  O   TRP A  95      63.963  63.067  58.017  1.00 68.27           O  
ANISOU  742  O   TRP A  95     8847   8980   8111   -318    244   3951       O  
ATOM    743  CB  TRP A  95      64.817  62.463  54.962  1.00 72.81           C  
ANISOU  743  CB  TRP A  95     9311  10440   7911   -556    343   4383       C  
ATOM    744  CG  TRP A  95      63.922  63.459  54.236  1.00 78.44           C  
ANISOU  744  CG  TRP A  95    10023  11160   8619   -468    241   4822       C  
ATOM    745  CD1 TRP A  95      62.538  63.520  54.259  1.00 79.49           C  
ANISOU  745  CD1 TRP A  95    10125  11324   8752   -294     90   4905       C  
ATOM    746  CD2 TRP A  95      64.354  64.538  53.385  1.00 81.51           C  
ANISOU  746  CD2 TRP A  95    10422  11532   9013   -543    285   5270       C  
ATOM    747  NE1 TRP A  95      62.099  64.564  53.463  1.00 83.50           N  
ANISOU  747  NE1 TRP A  95    10618  11841   9266   -240     35   5386       N  
ATOM    748  CE2 TRP A  95      63.186  65.205  52.922  1.00 84.50           C  
ANISOU  748  CE2 TRP A  95    10782  11926   9397   -392    152   5618       C  
ATOM    749  CE3 TRP A  95      65.613  65.012  52.981  1.00 83.57           C  
ANISOU  749  CE3 TRP A  95    10694  11771   9287   -724    426   5433       C  
ATOM    750  CZ2 TRP A  95      63.243  66.321  52.072  1.00 88.92           C  
ANISOU  750  CZ2 TRP A  95    11349  12460   9974   -409    156   6129       C  
ATOM    751  CZ3 TRP A  95      65.670  66.127  52.118  1.00 88.31           C  
ANISOU  751  CZ3 TRP A  95    11305  12351   9895   -763    434   5934       C  
ATOM    752  CH2 TRP A  95      64.489  66.762  51.678  1.00 89.88           C  
ANISOU  752  CH2 TRP A  95    11502  12548  10100   -601    299   6277       C  
ATOM    753  N   GLY A  96      65.414  61.326  57.806  1.00 65.19           N  
ANISOU  753  N   GLY A  96     8383   8987   7398   -515    382   3564       N  
ATOM    754  CA  GLY A  96      64.945  60.568  58.967  1.00 61.12           C  
ANISOU  754  CA  GLY A  96     7878   8357   6986   -422    333   3205       C  
ATOM    755  C   GLY A  96      64.431  59.161  58.673  1.00 58.68           C  
ANISOU  755  C   GLY A  96     7531   8373   6391   -385    312   2968       C  
ATOM    756  O   GLY A  96      63.672  58.617  59.473  1.00 56.85           O  
ANISOU  756  O   GLY A  96     7304   8072   6224   -289    243   2745       O  
ATOM    757  N   LYS A  97      64.829  58.560  57.547  1.00 58.45           N  
ANISOU  757  N   LYS A  97     7474   8690   6043   -472    380   3003       N  
ATOM    758  CA  LYS A  97      64.473  57.164  57.296  1.00 55.34           C  
ANISOU  758  CA  LYS A  97     7077   8567   5383   -467    384   2731       C  
ATOM    759  C   LYS A  97      64.899  56.254  58.458  1.00 51.78           C  
ANISOU  759  C   LYS A  97     6628   7967   5079   -444    436   2368       C  
ATOM    760  O   LYS A  97      66.060  56.239  58.880  1.00 51.13           O  
ANISOU  760  O   LYS A  97     6521   7783   5121   -498    547   2303       O  
ATOM    761  CB  LYS A  97      65.038  56.670  55.977  1.00 57.04           C  
ANISOU  761  CB  LYS A  97     7291   9142   5238   -575    494   2782       C  
ATOM    762  CG  LYS A  97      64.330  55.439  55.453  1.00 56.80           C  
ANISOU  762  CG  LYS A  97     7292   9402   4886   -585    464   2560       C  
ATOM    763  CD  LYS A  97      64.121  55.504  53.953  1.00 61.40           C  
ANISOU  763  CD  LYS A  97     7891  10361   5074   -675    461   2762       C  
ATOM    764  CE  LYS A  97      65.092  54.603  53.226  1.00 64.98           C  
ANISOU  764  CE  LYS A  97     8387  11054   5247   -770    665   2583       C  
ATOM    765  NZ  LYS A  97      66.295  55.353  52.762  1.00 69.60           N  
ANISOU  765  NZ  LYS A  97     8932  11655   5855   -829    821   2821       N  
ATOM    766  N   LEU A  98      63.924  55.504  58.955  1.00 48.85           N  
ANISOU  766  N   LEU A  98     6269   7602   4688   -368    348   2160       N  
ATOM    767  CA  LEU A  98      64.031  54.656  60.104  1.00 45.36           C  
ANISOU  767  CA  LEU A  98     5833   7017   4383   -327    366   1850       C  
ATOM    768  C   LEU A  98      64.282  53.220  59.708  1.00 44.25           C  
ANISOU  768  C   LEU A  98     5712   7089   4011   -366    456   1600       C  
ATOM    769  O   LEU A  98      63.596  52.674  58.848  1.00 47.09           O  
ANISOU  769  O   LEU A  98     6101   7687   4103   -399    422   1574       O  
ATOM    770  CB  LEU A  98      62.691  54.724  60.873  1.00 45.42           C  
ANISOU  770  CB  LEU A  98     5842   6903   4511   -220    222   1797       C  
ATOM    771  CG  LEU A  98      62.552  55.416  62.243  1.00 44.77           C  
ANISOU  771  CG  LEU A  98     5770   6481   4759   -138    183   1766       C  
ATOM    772  CD1 LEU A  98      63.243  56.781  62.263  1.00 45.76           C  
ANISOU  772  CD1 LEU A  98     5916   6399   5070   -169    212   1994       C  
ATOM    773  CD2 LEU A  98      61.082  55.519  62.723  1.00 42.98           C  
ANISOU  773  CD2 LEU A  98     5527   6204   4599    -14     64   1762       C  
ATOM    774  N   GLN A  99      65.267  52.599  60.320  1.00 41.53           N  
ANISOU  774  N   GLN A  99     5353   6658   3766   -368    573   1419       N  
ATOM    775  CA  GLN A  99      65.416  51.162  60.202  1.00 40.48           C  
ANISOU  775  CA  GLN A  99     5255   6642   3484   -366    668   1149       C  
ATOM    776  C   GLN A  99      65.238  50.542  61.563  1.00 36.30           C  
ANISOU  776  C   GLN A  99     4722   5906   3164   -295    632    938       C  
ATOM    777  O   GLN A  99      65.841  50.980  62.568  1.00 34.14           O  
ANISOU  777  O   GLN A  99     4398   5438   3136   -270    630    955       O  
ATOM    778  CB  GLN A  99      66.745  50.722  59.562  1.00 42.49           C  
ANISOU  778  CB  GLN A  99     5489   7024   3631   -402    877   1123       C  
ATOM    779  CG  GLN A  99      66.793  49.193  59.244  1.00 46.72           C  
ANISOU  779  CG  GLN A  99     6097   7672   3983   -386   1004    836       C  
ATOM    780  CD  GLN A  99      68.173  48.674  58.700  1.00 50.77           C  
ANISOU  780  CD  GLN A  99     6578   8290   4420   -377   1256    790       C  
ATOM    781  OE1 GLN A  99      69.018  49.446  58.244  1.00 48.63           O  
ANISOU  781  OE1 GLN A  99     6228   8097   4150   -414   1336    997       O  
ATOM    782  NE2 GLN A  99      68.383  47.353  58.789  1.00 51.50           N  
ANISOU  782  NE2 GLN A  99     6729   8372   4466   -320   1392    525       N  
ATOM    783  N   PHE A 100      64.408  49.505  61.569  1.00 34.19           N  
ANISOU  783  N   PHE A 100     4511   5699   2781   -286    601    742       N  
ATOM    784  CA  PHE A 100      63.980  48.836  62.765  1.00 31.73           C  
ANISOU  784  CA  PHE A 100     4203   5222   2628   -228    554    557       C  
ATOM    785  C   PHE A 100      64.766  47.569  62.932  1.00 31.64           C  
ANISOU  785  C   PHE A 100     4219   5197   2605   -209    707    346       C  
ATOM    786  O   PHE A 100      65.128  46.938  61.936  1.00 31.68           O  
ANISOU  786  O   PHE A 100     4276   5354   2405   -246    832    275       O  
ATOM    787  CB  PHE A 100      62.503  48.488  62.664  1.00 30.61           C  
ANISOU  787  CB  PHE A 100     4095   5153   2381   -244    422    499       C  
ATOM    788  CG  PHE A 100      61.625  49.585  63.073  1.00 31.60           C  
ANISOU  788  CG  PHE A 100     4167   5206   2630   -197    274    674       C  
ATOM    789  CD1 PHE A 100      61.200  50.519  62.153  1.00 32.55           C  
ANISOU  789  CD1 PHE A 100     4265   5456   2645   -216    203    911       C  
ATOM    790  CD2 PHE A 100      61.240  49.724  64.421  1.00 29.34           C  
ANISOU  790  CD2 PHE A 100     3857   4714   2575   -119    218    616       C  
ATOM    791  CE1 PHE A 100      60.399  51.573  62.546  1.00 32.32           C  
ANISOU  791  CE1 PHE A 100     4186   5328   2765   -138     88   1091       C  
ATOM    792  CE2 PHE A 100      60.423  50.770  64.809  1.00 29.37           C  
ANISOU  792  CE2 PHE A 100     3822   4632   2705    -50    113    767       C  
ATOM    793  CZ  PHE A 100      60.007  51.701  63.864  1.00 28.99           C  
ANISOU  793  CZ  PHE A 100     3748   4688   2578    -49     53   1008       C  
ATOM    794  N   GLY A 101      65.015  47.212  64.198  1.00 29.45           N  
ANISOU  794  N   GLY A 101     3910   4737   2543   -145    703    253       N  
ATOM    795  CA  GLY A 101      65.443  45.887  64.551  1.00 30.38           C  
ANISOU  795  CA  GLY A 101     4055   4804   2682   -101    820     57       C  
ATOM    796  C   GLY A 101      64.271  44.912  64.521  1.00 31.60           C  
ANISOU  796  C   GLY A 101     4306   4965   2734   -129    770   -119       C  
ATOM    797  O   GLY A 101      63.146  45.270  64.162  1.00 31.67           O  
ANISOU  797  O   GLY A 101     4337   5059   2637   -189    639    -80       O  
ATOM    798  N   ALA A 102      64.546  43.666  64.883  1.00 31.69           N  
ANISOU  798  N   ALA A 102     4367   4888   2785    -90    876   -297       N  
ATOM    799  CA  ALA A 102      63.556  42.606  64.759  1.00 32.60           C  
ANISOU  799  CA  ALA A 102     4592   4995   2799   -148    856   -482       C  
ATOM    800  C   ALA A 102      62.639  42.556  65.981  1.00 31.00           C  
ANISOU  800  C   ALA A 102     4355   4671   2751   -136    713   -490       C  
ATOM    801  O   ALA A 102      61.678  41.814  65.993  1.00 31.98           O  
ANISOU  801  O   ALA A 102     4544   4793   2813   -206    666   -609       O  
ATOM    802  CB  ALA A 102      64.255  41.231  64.508  1.00 32.62           C  
ANISOU  802  CB  ALA A 102     4693   4921   2779   -111   1065   -677       C  
ATOM    803  N   GLY A 103      62.954  43.323  67.016  1.00 29.52           N  
ANISOU  803  N   GLY A 103     4070   4390   2755    -63    653   -370       N  
ATOM    804  CA  GLY A 103      62.120  43.372  68.218  1.00 28.00           C  
ANISOU  804  CA  GLY A 103     3845   4098   2692    -44    536   -373       C  
ATOM    805  C   GLY A 103      62.494  42.261  69.193  1.00 28.06           C  
ANISOU  805  C   GLY A 103     3870   3963   2827      8    608   -477       C  
ATOM    806  O   GLY A 103      62.997  41.215  68.769  1.00 28.12           O  
ANISOU  806  O   GLY A 103     3943   3938   2800     17    741   -585       O  
ATOM    807  N   THR A 104      62.260  42.488  70.485  1.00 26.35           N  
ANISOU  807  N   THR A 104     3602   3657   2752     49    532   -440       N  
ATOM    808  CA  THR A 104      62.462  41.447  71.530  1.00 26.21           C  
ANISOU  808  CA  THR A 104     3593   3517   2848     95    576   -502       C  
ATOM    809  C   THR A 104      61.226  41.410  72.406  1.00 25.63           C  
ANISOU  809  C   THR A 104     3515   3420   2802     67    472   -518       C  
ATOM    810  O   THR A 104      60.832  42.433  72.931  1.00 24.02           O  
ANISOU  810  O   THR A 104     3259   3237   2628     80    380   -444       O  
ATOM    811  CB  THR A 104      63.680  41.772  72.474  1.00 26.28           C  
ANISOU  811  CB  THR A 104     3514   3472   3000    174    592   -408       C  
ATOM    812  OG1 THR A 104      64.787  42.207  71.688  1.00 30.40           O  
ANISOU  812  OG1 THR A 104     3992   4052   3504    191    667   -346       O  
ATOM    813  CG2 THR A 104      64.110  40.534  73.311  1.00 22.77           C  
ANISOU  813  CG2 THR A 104     3070   2923   2658    240    664   -438       C  
ATOM    814  N   GLN A 105      60.594  40.236  72.515  1.00 26.17           N  
ANISOU  814  N   GLN A 105     3644   3439   2858     24    502   -617       N  
ATOM    815  CA  GLN A 105      59.495  40.061  73.433  1.00 25.60           C  
ANISOU  815  CA  GLN A 105     3551   3354   2823     -5    425   -618       C  
ATOM    816  C   GLN A 105      60.023  39.980  74.874  1.00 23.93           C  
ANISOU  816  C   GLN A 105     3298   3053   2739     74    430   -561       C  
ATOM    817  O   GLN A 105      60.927  39.199  75.191  1.00 22.59           O  
ANISOU  817  O   GLN A 105     3145   2794   2642    125    511   -559       O  
ATOM    818  CB  GLN A 105      58.672  38.813  73.075  1.00 27.65           C  
ANISOU  818  CB  GLN A 105     3887   3586   3031   -111    453   -732       C  
ATOM    819  CG  GLN A 105      57.499  38.617  74.056  1.00 29.83           C  
ANISOU  819  CG  GLN A 105     4115   3868   3348   -154    382   -710       C  
ATOM    820  CD  GLN A 105      56.651  37.378  73.787  1.00 34.50           C  
ANISOU  820  CD  GLN A 105     4775   4425   3906   -296    400   -810       C  
ATOM    821  OE1 GLN A 105      55.610  37.193  74.416  1.00 36.22           O  
ANISOU  821  OE1 GLN A 105     4939   4679   4143   -359    345   -785       O  
ATOM    822  NE2 GLN A 105      57.082  36.528  72.866  1.00 39.33           N  
ANISOU  822  NE2 GLN A 105     5510   4966   4465   -357    487   -930       N  
ATOM    823  N   VAL A 106      59.521  40.877  75.720  1.00 22.63           N  
ANISOU  823  N   VAL A 106     3077   2925   2596     93    346   -504       N  
ATOM    824  CA  VAL A 106      59.794  40.820  77.137  1.00 21.24           C  
ANISOU  824  CA  VAL A 106     2873   2702   2492    138    333   -462       C  
ATOM    825  C   VAL A 106      58.558  40.271  77.872  1.00 21.22           C  
ANISOU  825  C   VAL A 106     2868   2708   2484    101    316   -480       C  
ATOM    826  O   VAL A 106      57.440  40.740  77.639  1.00 20.08           O  
ANISOU  826  O   VAL A 106     2695   2638   2295     70    272   -489       O  
ATOM    827  CB  VAL A 106      60.182  42.250  77.699  1.00 21.17           C  
ANISOU  827  CB  VAL A 106     2827   2718   2499    172    270   -408       C  
ATOM    828  CG1 VAL A 106      60.473  42.168  79.174  1.00 19.23           C  
ANISOU  828  CG1 VAL A 106     2566   2456   2285    191    249   -380       C  
ATOM    829  CG2 VAL A 106      61.467  42.860  76.895  1.00 21.50           C  
ANISOU  829  CG2 VAL A 106     2852   2761   2553    181    287   -365       C  
ATOM    830  N   VAL A 107      58.766  39.276  78.738  1.00 21.00           N  
ANISOU  830  N   VAL A 107     2855   2616   2507    107    355   -461       N  
ATOM    831  CA  VAL A 107      57.732  38.727  79.610  1.00 21.01           C  
ANISOU  831  CA  VAL A 107     2846   2628   2507     66    350   -450       C  
ATOM    832  C   VAL A 107      58.118  39.082  81.093  1.00 21.25           C  
ANISOU  832  C   VAL A 107     2846   2681   2544    120    328   -378       C  
ATOM    833  O   VAL A 107      59.109  38.556  81.587  1.00 19.99           O  
ANISOU  833  O   VAL A 107     2693   2474   2429    157    347   -318       O  
ATOM    834  CB  VAL A 107      57.613  37.181  79.458  1.00 22.53           C  
ANISOU  834  CB  VAL A 107     3100   2713   2746      8    421   -469       C  
ATOM    835  CG1 VAL A 107      56.414  36.610  80.307  1.00 23.34           C  
ANISOU  835  CG1 VAL A 107     3180   2839   2848    -66    417   -440       C  
ATOM    836  CG2 VAL A 107      57.448  36.798  77.982  1.00 26.13           C  
ANISOU  836  CG2 VAL A 107     3617   3143   3166    -64    450   -572       C  
ATOM    837  N   VAL A 108      57.382  40.001  81.753  1.00 19.43           N  
ANISOU  837  N   VAL A 108     2584   2532   2264    130    292   -383       N  
ATOM    838  CA  VAL A 108      57.608  40.238  83.170  1.00 19.48           C  
ANISOU  838  CA  VAL A 108     2587   2578   2236    154    279   -342       C  
ATOM    839  C   VAL A 108      56.650  39.367  83.977  1.00 20.37           C  
ANISOU  839  C   VAL A 108     2684   2724   2328    117    318   -304       C  
ATOM    840  O   VAL A 108      55.450  39.503  83.888  1.00 19.79           O  
ANISOU  840  O   VAL A 108     2574   2708   2235     95    336   -328       O  
ATOM    841  CB  VAL A 108      57.551  41.738  83.581  1.00 19.70           C  
ANISOU  841  CB  VAL A 108     2621   2649   2214    189    245   -388       C  
ATOM    842  CG1 VAL A 108      57.840  41.876  85.092  1.00 15.08           C  
ANISOU  842  CG1 VAL A 108     2057   2120   1554    184    233   -369       C  
ATOM    843  CG2 VAL A 108      58.560  42.541  82.746  1.00 19.61           C  
ANISOU  843  CG2 VAL A 108     2623   2590   2237    199    207   -401       C  
ATOM    844  N   THR A 109      57.198  38.411  84.696  1.00 21.06           N  
ANISOU  844  N   THR A 109     2786   2781   2433    110    335   -219       N  
ATOM    845  CA  THR A 109      56.377  37.449  85.364  1.00 22.50           C  
ANISOU  845  CA  THR A 109     2960   2976   2611     60    381   -156       C  
ATOM    846  C   THR A 109      56.044  38.007  86.739  1.00 23.71           C  
ANISOU  846  C   THR A 109     3095   3260   2650     73    377   -125       C  
ATOM    847  O   THR A 109      56.902  38.623  87.409  1.00 25.81           O  
ANISOU  847  O   THR A 109     3380   3575   2852    106    332   -116       O  
ATOM    848  CB  THR A 109      57.065  36.083  85.518  1.00 23.29           C  
ANISOU  848  CB  THR A 109     3094   2960   2795     55    416    -51       C  
ATOM    849  OG1 THR A 109      58.200  36.247  86.352  1.00 23.66           O  
ANISOU  849  OG1 THR A 109     3128   3045   2816    117    377     41       O  
ATOM    850  CG2 THR A 109      57.497  35.454  84.153  1.00 22.71           C  
ANISOU  850  CG2 THR A 109     3068   2732   2829     53    453   -109       C  
ATOM    851  N   PRO A 110      54.793  37.825  87.154  1.00 23.63           N  
ANISOU  851  N   PRO A 110     3048   3325   2603     33    428   -116       N  
ATOM    852  CA  PRO A 110      54.348  38.373  88.441  1.00 24.17           C  
ANISOU  852  CA  PRO A 110     3106   3534   2542     52    457   -105       C  
ATOM    853  C   PRO A 110      54.979  37.642  89.631  1.00 26.37           C  
ANISOU  853  C   PRO A 110     3411   3854   2751     29    452     25       C  
ATOM    854  O   PRO A 110      55.251  36.423  89.593  1.00 25.91           O  
ANISOU  854  O   PRO A 110     3357   3714   2773     -5    462    147       O  
ATOM    855  CB  PRO A 110      52.811  38.139  88.440  1.00 23.66           C  
ANISOU  855  CB  PRO A 110     2961   3548   2479     12    532    -97       C  
ATOM    856  CG  PRO A 110      52.589  36.939  87.503  1.00 22.35           C  
ANISOU  856  CG  PRO A 110     2781   3272   2436    -80    528    -54       C  
ATOM    857  CD  PRO A 110      53.745  37.016  86.460  1.00 23.64           C  
ANISOU  857  CD  PRO A 110     3011   3296   2675    -47    466   -111       C  
ATOM    858  N   ASP A 111      55.180  38.383  90.710  1.00 27.71           N  
ANISOU  858  N   ASP A 111     3609   4152   2767     46    443      5       N  
ATOM    859  CA  ASP A 111      55.572  37.761  91.953  1.00 29.95           C  
ANISOU  859  CA  ASP A 111     3906   4535   2937     12    435    146       C  
ATOM    860  C   ASP A 111      54.329  37.225  92.703  1.00 29.75           C  
ANISOU  860  C   ASP A 111     3846   4617   2840    -28    539    218       C  
ATOM    861  O   ASP A 111      53.584  37.982  93.330  1.00 30.21           O  
ANISOU  861  O   ASP A 111     3904   4808   2763    -14    606    134       O  
ATOM    862  CB  ASP A 111      56.345  38.798  92.770  1.00 32.42           C  
ANISOU  862  CB  ASP A 111     4275   4963   3081     14    369     77       C  
ATOM    863  CG  ASP A 111      56.726  38.308  94.134  1.00 36.81           C  
ANISOU  863  CG  ASP A 111     4842   5679   3463    -34    343    222       C  
ATOM    864  OD1 ASP A 111      56.791  37.074  94.346  1.00 40.41           O  
ANISOU  864  OD1 ASP A 111     5258   6119   3974    -48    352    422       O  
ATOM    865  OD2 ASP A 111      56.953  39.187  94.992  1.00 43.78           O  
ANISOU  865  OD2 ASP A 111     5785   6701   4147    -65    315    134       O  
ATOM    866  N   ILE A 112      54.103  35.920  92.638  1.00 29.75           N  
ANISOU  866  N   ILE A 112     3818   4548   2937    -80    569    374       N  
ATOM    867  CA  ILE A 112      52.945  35.317  93.315  1.00 30.11           C  
ANISOU  867  CA  ILE A 112     3817   4694   2930   -146    670    473       C  
ATOM    868  C   ILE A 112      53.205  35.155  94.815  1.00 33.71           C  
ANISOU  868  C   ILE A 112     4297   5328   3184   -164    682    610       C  
ATOM    869  O   ILE A 112      53.998  34.291  95.216  1.00 34.10           O  
ANISOU  869  O   ILE A 112     4366   5339   3248   -180    634    796       O  
ATOM    870  CB  ILE A 112      52.567  33.990  92.686  1.00 28.72           C  
ANISOU  870  CB  ILE A 112     3618   4356   2937   -227    701    585       C  
ATOM    871  CG1 ILE A 112      52.375  34.142  91.181  1.00 29.08           C  
ANISOU  871  CG1 ILE A 112     3654   4253   3141   -231    676    439       C  
ATOM    872  CG2 ILE A 112      51.272  33.427  93.338  1.00 29.90           C  
ANISOU  872  CG2 ILE A 112     3697   4619   3041   -325    808    694       C  
ATOM    873  CD1 ILE A 112      51.317  35.262  90.713  1.00 23.57           C  
ANISOU  873  CD1 ILE A 112     2876   3673   2405   -209    701    280       C  
ATOM    874  N   GLN A 113      52.529  35.974  95.633  1.00 35.60           N  
ANISOU  874  N   GLN A 113     4533   5763   3228   -154    755    528       N  
ATOM    875  CA  GLN A 113      52.798  36.059  97.066  1.00 39.64           C  
ANISOU  875  CA  GLN A 113     5090   6486   3484   -179    764    610       C  
ATOM    876  C   GLN A 113      52.347  34.811  97.809  1.00 40.90           C  
ANISOU  876  C   GLN A 113     5209   6718   3612   -258    829    868       C  
ATOM    877  O   GLN A 113      53.067  34.304  98.639  1.00 42.59           O  
ANISOU  877  O   GLN A 113     5454   7014   3712   -287    772   1049       O  
ATOM    878  CB  GLN A 113      52.133  37.305  97.716  1.00 41.71           C  
ANISOU  878  CB  GLN A 113     5385   6925   3535   -141    862    416       C  
ATOM    879  CG  GLN A 113      52.493  38.697  97.074  1.00 47.51           C  
ANISOU  879  CG  GLN A 113     6183   7570   4298    -62    819    155       C  
ATOM    880  CD  GLN A 113      54.007  38.956  96.942  1.00 51.42           C  
ANISOU  880  CD  GLN A 113     6752   7999   4787    -82    648    138       C  
ATOM    881  OE1 GLN A 113      54.506  39.155  95.844  1.00 55.79           O  
ANISOU  881  OE1 GLN A 113     7293   8376   5526    -48    574     81       O  
ATOM    882  NE2 GLN A 113      54.727  38.939  98.049  1.00 57.16           N  
ANISOU  882  NE2 GLN A 113     7539   8889   5290   -146    584    203       N  
ATOM    883  N   ASN A 114      51.139  34.347  97.515  1.00 40.94           N  
ANISOU  883  N   ASN A 114     5133   6705   3717   -302    943    902       N  
ATOM    884  CA  ASN A 114      50.544  33.209  98.171  1.00 43.11           C  
ANISOU  884  CA  ASN A 114     5361   7038   3978   -400   1024   1145       C  
ATOM    885  C   ASN A 114      50.153  32.162  97.134  1.00 41.77           C  
ANISOU  885  C   ASN A 114     5146   6628   4094   -476   1029   1221       C  
ATOM    886  O   ASN A 114      48.997  32.083  96.747  1.00 42.22           O  
ANISOU  886  O   ASN A 114     5111   6706   4225   -540   1114   1186       O  
ATOM    887  CB  ASN A 114      49.310  33.664  98.978  1.00 45.74           C  
ANISOU  887  CB  ASN A 114     5626   7627   4124   -418   1186   1118       C  
ATOM    888  CG  ASN A 114      49.661  34.709 100.042  1.00 48.90           C  
ANISOU  888  CG  ASN A 114     6108   8257   4212   -356   1205   1004       C  
ATOM    889  OD1 ASN A 114      50.013  34.361 101.174  1.00 53.12           O  
ANISOU  889  OD1 ASN A 114     6690   8964   4528   -405   1205   1162       O  
ATOM    890  ND2 ASN A 114      49.602  35.988  99.663  1.00 47.63           N  
ANISOU  890  ND2 ASN A 114     5978   8091   4025   -258   1216    732       N  
ATOM    891  N   PRO A 115      51.125  31.389  96.643  1.00 41.04           N  
ANISOU  891  N   PRO A 115     5117   6308   4165   -471    940   1314       N  
ATOM    892  CA  PRO A 115      50.863  30.306  95.695  1.00 40.47           C  
ANISOU  892  CA  PRO A 115     5048   5971   4356   -555    955   1369       C  
ATOM    893  C   PRO A 115      49.876  29.306  96.226  1.00 42.16           C  
ANISOU  893  C   PRO A 115     5215   6207   4596   -704   1060   1571       C  
ATOM    894  O   PRO A 115      49.975  28.918  97.376  1.00 43.41           O  
ANISOU  894  O   PRO A 115     5378   6492   4620   -721   1096   1787       O  
ATOM    895  CB  PRO A 115      52.232  29.645  95.561  1.00 41.22           C  
ANISOU  895  CB  PRO A 115     5231   5865   4564   -486    876   1488       C  
ATOM    896  CG  PRO A 115      53.186  30.842  95.657  1.00 40.31           C  
ANISOU  896  CG  PRO A 115     5131   5875   4310   -357    776   1348       C  
ATOM    897  CD  PRO A 115      52.576  31.603  96.834  1.00 41.02           C  
ANISOU  897  CD  PRO A 115     5186   6279   4119   -376    821   1339       C  
ATOM    898  N   ASP A 116      48.889  28.947  95.403  1.00 38.04           N  
ANISOU  898  N   ASP A 116     5876   4549   4026    674   -653   1407       N  
ATOM    899  CA  ASP A 116      47.911  27.906  95.742  1.00 39.49           C  
ANISOU  899  CA  ASP A 116     6372   4488   4141    568   -534   1615       C  
ATOM    900  C   ASP A 116      47.615  27.046  94.516  1.00 37.94           C  
ANISOU  900  C   ASP A 116     6104   4043   4267    623   -455   1561       C  
ATOM    901  O   ASP A 116      46.462  26.876  94.130  1.00 37.72           O  
ANISOU  901  O   ASP A 116     6110   3919   4303    423   -228   1545       O  
ATOM    902  CB  ASP A 116      46.617  28.511  96.295  1.00 39.31           C  
ANISOU  902  CB  ASP A 116     6454   4566   3913    280   -231   1612       C  
ATOM    903  CG  ASP A 116      45.777  27.494  97.061  1.00 43.91           C  
ANISOU  903  CG  ASP A 116     7392   4959   4332    114   -108   1880       C  
ATOM    904  OD1 ASP A 116      46.266  26.387  97.392  1.00 46.39           O  
ANISOU  904  OD1 ASP A 116     7961   5041   4622    222   -314   2116       O  
ATOM    905  OD2 ASP A 116      44.596  27.792  97.320  1.00 48.72           O  
ANISOU  905  OD2 ASP A 116     8017   5634   4858   -131    208   1862       O  
ATOM    906  N   PRO A 117      48.657  26.462  93.913  1.00 38.02           N  
ANISOU  906  N   PRO A 117     6006   3951   4489    898   -651   1509       N  
ATOM    907  CA  PRO A 117      48.429  25.804  92.634  1.00 36.00           C  
ANISOU  907  CA  PRO A 117     5679   3492   4505    954   -555   1371       C  
ATOM    908  C   PRO A 117      47.336  24.731  92.700  1.00 36.60           C  
ANISOU  908  C   PRO A 117     6056   3227   4620    784   -461   1514       C  
ATOM    909  O   PRO A 117      47.337  23.868  93.570  1.00 40.02           O  
ANISOU  909  O   PRO A 117     6801   3426   4978    796   -573   1769       O  
ATOM    910  CB  PRO A 117      49.800  25.173  92.330  1.00 37.97           C  
ANISOU  910  CB  PRO A 117     5819   3661   4946   1323   -785   1318       C  
ATOM    911  CG  PRO A 117      50.396  24.915  93.696  1.00 40.69           C  
ANISOU  911  CG  PRO A 117     6341   3992   5127   1442  -1065   1571       C  
ATOM    912  CD  PRO A 117      49.965  26.091  94.515  1.00 40.38           C  
ANISOU  912  CD  PRO A 117     6308   4254   4781   1183   -986   1606       C  
ATOM    913  N   ALA A 118      46.381  24.818  91.797  1.00 34.47           N  
ANISOU  913  N   ALA A 118     5703   2931   4463    597   -269   1364       N  
ATOM    914  CA  ALA A 118      45.293  23.857  91.760  1.00 36.23           C  
ANISOU  914  CA  ALA A 118     6145   2846   4774    373   -176   1458       C  
ATOM    915  C   ALA A 118      44.790  23.731  90.326  1.00 34.78           C  
ANISOU  915  C   ALA A 118     5818   2601   4795    316   -111   1194       C  
ATOM    916  O   ALA A 118      44.972  24.647  89.489  1.00 33.01           O  
ANISOU  916  O   ALA A 118     5336   2639   4565    374    -73    984       O  
ATOM    917  CB  ALA A 118      44.152  24.269  92.756  1.00 34.63           C  
ANISOU  917  CB  ALA A 118     6013   2764   4381     38     27   1628       C  
ATOM    918  N   VAL A 119      44.176  22.596  90.049  1.00 36.90           N  
ANISOU  918  N   VAL A 119     6288   2507   5223    185   -116   1213       N  
ATOM    919  CA  VAL A 119      43.499  22.319  88.772  1.00 36.35           C  
ANISOU  919  CA  VAL A 119     6145   2342   5321     63    -92    961       C  
ATOM    920  C   VAL A 119      41.986  22.159  89.014  1.00 37.35           C  
ANISOU  920  C   VAL A 119     6266   2412   5513   -357     36   1038       C  
ATOM    921  O   VAL A 119      41.593  21.422  89.875  1.00 39.11           O  
ANISOU  921  O   VAL A 119     6710   2392   5755   -540     85   1271       O  
ATOM    922  CB  VAL A 119      44.048  21.023  88.081  1.00 39.93           C  
ANISOU  922  CB  VAL A 119     6830   2373   5967    248   -229    829       C  
ATOM    923  CG1 VAL A 119      43.178  20.668  86.883  1.00 40.26           C  
ANISOU  923  CG1 VAL A 119     6860   2299   6137     45   -225    563       C  
ATOM    924  CG2 VAL A 119      45.561  21.172  87.657  1.00 37.91           C  
ANISOU  924  CG2 VAL A 119     6479   2218   5705    696   -315    678       C  
ATOM    925  N   TYR A 120      41.157  22.883  88.246  1.00 36.66           N  
ANISOU  925  N   TYR A 120     5906   2560   5461   -507     86    852       N  
ATOM    926  CA  TYR A 120      39.704  22.876  88.405  1.00 37.98           C  
ANISOU  926  CA  TYR A 120     5935   2752   5744   -886    203    880       C  
ATOM    927  C   TYR A 120      38.971  22.480  87.144  1.00 39.17           C  
ANISOU  927  C   TYR A 120     5994   2803   6084  -1040     77    628       C  
ATOM    928  O   TYR A 120      39.371  22.871  86.065  1.00 38.13           O  
ANISOU  928  O   TYR A 120     5800   2789   5898   -855    -51    408       O  
ATOM    929  CB  TYR A 120      39.278  24.280  88.780  1.00 34.99           C  
ANISOU  929  CB  TYR A 120     5249   2791   5253   -897    337    888       C  
ATOM    930  CG  TYR A 120      39.819  24.746  90.105  1.00 33.80           C  
ANISOU  930  CG  TYR A 120     5192   2769   4879   -808    465   1100       C  
ATOM    931  CD1 TYR A 120      39.359  24.202  91.302  1.00 34.29           C  
ANISOU  931  CD1 TYR A 120     5425   2727   4875  -1032    637   1343       C  
ATOM    932  CD2 TYR A 120      40.778  25.768  90.159  1.00 32.15           C  
ANISOU  932  CD2 TYR A 120     4915   2797   4500   -536    413   1054       C  
ATOM    933  CE1 TYR A 120      39.871  24.653  92.546  1.00 35.34           C  
ANISOU  933  CE1 TYR A 120     5699   3006   4722   -953    728   1527       C  
ATOM    934  CE2 TYR A 120      41.293  26.224  91.380  1.00 29.52           C  
ANISOU  934  CE2 TYR A 120     4681   2593   3940   -469    480   1211       C  
ATOM    935  CZ  TYR A 120      40.816  25.682  92.564  1.00 32.81           C  
ANISOU  935  CZ  TYR A 120     5296   2926   4243   -667    628   1437       C  
ATOM    936  OH  TYR A 120      41.330  26.175  93.749  1.00 32.44           O  
ANISOU  936  OH  TYR A 120     5386   3036   3902   -602    668   1570       O  
ATOM    937  N   GLN A 121      37.893  21.723  87.282  1.00 43.91           N  
ANISOU  937  N   GLN A 121     6593   3201   6887  -1408    116    661       N  
ATOM    938  CA  GLN A 121      37.012  21.379  86.156  1.00 46.85           C  
ANISOU  938  CA  GLN A 121     6835   3508   7456  -1626    -43    406       C  
ATOM    939  C   GLN A 121      35.922  22.445  86.067  1.00 46.85           C  
ANISOU  939  C   GLN A 121     6376   3907   7517  -1770      2    356       C  
ATOM    940  O   GLN A 121      35.273  22.751  87.072  1.00 46.67           O  
ANISOU  940  O   GLN A 121     6168   4020   7545  -1949    236    530       O  
ATOM    941  CB  GLN A 121      36.369  19.990  86.334  1.00 52.21           C  
ANISOU  941  CB  GLN A 121     7712   3737   8386  -2001    -50    448       C  
ATOM    942  CG  GLN A 121      35.984  19.314  84.963  1.00 56.46           C  
ANISOU  942  CG  GLN A 121     8297   4067   9087  -2129   -323    101       C  
ATOM    943  CD  GLN A 121      35.032  18.143  85.048  1.00 64.62           C  
ANISOU  943  CD  GLN A 121     9412   4704  10433  -2615   -349     95       C  
ATOM    944  OE1 GLN A 121      35.199  17.145  84.341  1.00 67.63           O  
ANISOU  944  OE1 GLN A 121    10094   4675  10926  -2667   -540   -112       O  
ATOM    945  NE2 GLN A 121      34.002  18.261  85.890  1.00 69.66           N  
ANISOU  945  NE2 GLN A 121     9778   5460  11229  -2998   -138    296       N  
ATOM    946  N   LEU A 122      35.739  23.009  84.870  1.00 46.81           N  
ANISOU  946  N   LEU A 122     6204   4087   7492  -1670   -218    118       N  
ATOM    947  CA  LEU A 122      34.709  24.029  84.614  1.00 48.53           C  
ANISOU  947  CA  LEU A 122     5982   4652   7805  -1739   -265     53       C  
ATOM    948  C   LEU A 122      33.618  23.452  83.742  1.00 53.55           C  
ANISOU  948  C   LEU A 122     6443   5218   8683  -2039   -509   -150       C  
ATOM    949  O   LEU A 122      33.928  22.804  82.739  1.00 55.89           O  
ANISOU  949  O   LEU A 122     6986   5328   8920  -2030   -751   -347       O  
ATOM    950  CB  LEU A 122      35.295  25.217  83.830  1.00 44.67           C  
ANISOU  950  CB  LEU A 122     5456   4427   7086  -1395   -405    -28       C  
ATOM    951  CG  LEU A 122      36.474  26.141  84.186  1.00 40.19           C  
ANISOU  951  CG  LEU A 122     5007   4004   6258  -1060   -280     82       C  
ATOM    952  CD1 LEU A 122      35.969  27.518  84.421  1.00 35.14           C  
ANISOU  952  CD1 LEU A 122     4061   3655   5633   -970   -239    128       C  
ATOM    953  CD2 LEU A 122      37.338  25.677  85.339  1.00 37.65           C  
ANISOU  953  CD2 LEU A 122     4911   3535   5857  -1003    -61    263       C  
ATOM    954  N   ARG A 123      32.351  23.718  84.039  1.00 57.02           N  
ANISOU  954  N   ARG A 123     6439   5831   9394  -2290   -468   -147       N  
ATOM    955  CA  ARG A 123      31.316  23.219  83.127  1.00 62.58           C  
ANISOU  955  CA  ARG A 123     6920   6505  10351  -2582   -776   -370       C  
ATOM    956  C   ARG A 123      30.728  24.249  82.154  1.00 63.61           C  
ANISOU  956  C   ARG A 123     6706   6971  10488  -2422  -1110   -526       C  
ATOM    957  O   ARG A 123      30.621  25.437  82.465  1.00 61.31           O  
ANISOU  957  O   ARG A 123     6161   6963  10170  -2181  -1024   -434       O  
ATOM    958  CB  ARG A 123      30.193  22.495  83.885  1.00 67.25           C  
ANISOU  958  CB  ARG A 123     7217   7006  11326  -3068   -587   -311       C  
ATOM    959  CG  ARG A 123      30.497  21.043  84.253  1.00 70.84           C  
ANISOU  959  CG  ARG A 123     8092   6978  11844  -3368   -478   -239       C  
ATOM    960  CD  ARG A 123      30.950  20.195  83.059  1.00 72.99           C  
ANISOU  960  CD  ARG A 123     8752   6929  12052  -3360   -848   -497       C  
ATOM    961  NE  ARG A 123      30.861  18.760  83.338  1.00 78.22           N  
ANISOU  961  NE  ARG A 123     9725   7076  12916  -3739   -798   -476       N  
ATOM    962  CZ  ARG A 123      31.143  17.785  82.462  1.00 81.90           C  
ANISOU  962  CZ  ARG A 123    10568   7151  13399  -3811  -1074   -726       C  
ATOM    963  NH1 ARG A 123      31.011  16.504  82.825  1.00 83.08           N  
ANISOU  963  NH1 ARG A 123    11013   6771  13780  -4173  -1012   -679       N  
ATOM    964  NH2 ARG A 123      31.560  18.076  81.223  1.00 79.51           N  
ANISOU  964  NH2 ARG A 123    10385   6958  12864  -3531  -1399  -1025       N  
ATOM    965  N   ASP A 124      30.307  23.772  80.981  1.00 68.57           N  
ANISOU  965  N   ASP A 124     7352   7544  11157  -2563  -1520   -767       N  
ATOM    966  CA  ASP A 124      29.571  24.620  80.038  1.00 71.47           C  
ANISOU  966  CA  ASP A 124     7386   8214  11553  -2460  -1923   -898       C  
ATOM    967  C   ASP A 124      28.279  25.164  80.656  1.00 74.67           C  
ANISOU  967  C   ASP A 124     7106   8874  12390  -2594  -1859   -852       C  
ATOM    968  O   ASP A 124      27.511  24.405  81.263  1.00 77.34           O  
ANISOU  968  O   ASP A 124     7169   9129  13085  -2993  -1693   -866       O  
ATOM    969  CB  ASP A 124      29.261  23.890  78.726  1.00 75.18           C  
ANISOU  969  CB  ASP A 124     8009   8582  11973  -2646  -2408  -1187       C  
ATOM    970  CG  ASP A 124      28.837  24.852  77.605  1.00 77.92           C  
ANISOU  970  CG  ASP A 124     8197   9238  12171  -2435  -2891  -1279       C  
ATOM    971  OD1 ASP A 124      29.477  24.854  76.530  1.00 79.25           O  
ANISOU  971  OD1 ASP A 124     8802   9390  11919  -2281  -3149  -1400       O  
ATOM    972  OD2 ASP A 124      27.859  25.610  77.787  1.00 81.63           O  
ANISOU  972  OD2 ASP A 124     8113   9967  12934  -2410  -3013  -1229       O  
ATOM    973  N   SER A 125      28.066  26.481  80.500  1.00 74.51           N  
ANISOU  973  N   SER A 125     6817   9146  12345  -2256  -1970   -800       N  
ATOM    974  CA  SER A 125      26.871  27.163  81.031  1.00 78.49           C  
ANISOU  974  CA  SER A 125     6625   9918  13278  -2270  -1913   -794       C  
ATOM    975  C   SER A 125      25.553  26.608  80.485  1.00 85.71           C  
ANISOU  975  C   SER A 125     7026  10922  14617  -2617  -2275  -1000       C  
ATOM    976  O   SER A 125      24.570  26.524  81.222  1.00 89.58           O  
ANISOU  976  O   SER A 125     6932  11547  15557  -2848  -2050  -1017       O  
ATOM    977  CB  SER A 125      26.940  28.692  80.875  1.00 76.50           C  
ANISOU  977  CB  SER A 125     6240   9886  12937  -1788  -2021   -713       C  
ATOM    978  OG  SER A 125      27.454  29.100  79.622  1.00 76.05           O  
ANISOU  978  OG  SER A 125     6543   9824  12527  -1551  -2477   -735       O  
ATOM    979  N   LYS A 126      25.530  26.201  79.218  1.00 88.64           N  
ANISOU  979  N   LYS A 126     7601  11235  14841  -2684  -2818  -1175       N  
ATOM    980  CA  LYS A 126      24.307  25.617  78.686  1.00 96.55           C  
ANISOU  980  CA  LYS A 126     8121  12316  16246  -3055  -3221  -1399       C  
ATOM    981  C   LYS A 126      24.509  24.320  77.905  1.00 99.42           C  
ANISOU  981  C   LYS A 126     8910  12391  16473  -3423  -3502  -1611       C  
ATOM    982  O   LYS A 126      23.584  23.509  77.827  1.00105.07           O  
ANISOU  982  O   LYS A 126     9271  13064  17586  -3889  -3668  -1789       O  
ATOM    983  CB  LYS A 126      23.522  26.648  77.854  1.00 99.55           C  
ANISOU  983  CB  LYS A 126     8057  13022  16743  -2770  -3787  -1470       C  
ATOM    984  CG  LYS A 126      22.006  26.398  77.818  1.00108.02           C  
ANISOU  984  CG  LYS A 126     8285  14307  18450  -3092  -4062  -1655       C  
ATOM    985  CD  LYS A 126      21.230  27.710  77.842  1.00110.87           C  
ANISOU  985  CD  LYS A 126     7999  15012  19115  -2681  -4258  -1610       C  
ATOM    986  CE  LYS A 126      19.766  27.495  77.540  1.00119.21           C  
ANISOU  986  CE  LYS A 126     8187  16317  20789  -2944  -4682  -1831       C  
ATOM    987  NZ  LYS A 126      19.544  27.297  76.080  1.00123.73           N  
ANISOU  987  NZ  LYS A 126     8922  16924  21166  -2972  -5549  -2002       N  
ATOM    988  N   SER A 127      25.711  24.110  77.365  1.00 96.41           N  
ANISOU  988  N   SER A 127     9269  11803  15560  -3230  -3525  -1616       N  
ATOM    989  CA  SER A 127      25.866  23.205  76.205  1.00100.07           C  
ANISOU  989  CA  SER A 127    10156  12072  15793  -3429  -3965  -1902       C  
ATOM    990  C   SER A 127      25.920  21.691  76.453  1.00102.96           C  
ANISOU  990  C   SER A 127    10776  12012  16330  -3901  -3816  -2054       C  
ATOM    991  O   SER A 127      26.533  20.979  75.663  1.00104.17           O  
ANISOU  991  O   SER A 127    11499  11913  16167  -3931  -4005  -2270       O  
ATOM    992  CB  SER A 127      27.037  23.646  75.300  1.00 96.67           C  
ANISOU  992  CB  SER A 127    10381  11645  14703  -3020  -4097  -1908       C  
ATOM    993  OG  SER A 127      26.755  23.394  73.928  1.00 99.34           O  
ANISOU  993  OG  SER A 127    10917  12036  14790  -3100  -4707  -2191       O  
ATOM    994  N   SER A 128      25.252  21.201  77.503  1.00105.17           N  
ANISOU  994  N   SER A 128    10654  12199  17106  -4279  -3481  -1956       N  
ATOM    995  CA  SER A 128      25.148  19.744  77.797  1.00108.65           C  
ANISOU  995  CA  SER A 128    11312  12181  17788  -4803  -3352  -2061       C  
ATOM    996  C   SER A 128      26.495  19.054  78.063  1.00104.82           C  
ANISOU  996  C   SER A 128    11608  11250  16966  -4651  -3032  -1982       C  
ATOM    997  O   SER A 128      27.061  18.392  77.180  1.00105.99           O  
ANISOU  997  O   SER A 128    12292  11123  16854  -4627  -3290  -2239       O  
ATOM    998  CB  SER A 128      24.360  18.985  76.710  1.00115.22           C  
ANISOU  998  CB  SER A 128    12069  12920  18789  -5216  -3954  -2454       C  
ATOM    999  OG  SER A 128      23.085  18.594  77.180  1.00121.24           O  
ANISOU  999  OG  SER A 128    12159  13735  20171  -5763  -3952  -2489       O  
ATOM   1000  N   ASP A 129      26.980  19.203  79.292  1.00100.89           N  
ANISOU 1000  N   ASP A 129    11158  10692  16481  -4540  -2481  -1646       N  
ATOM   1001  CA  ASP A 129      28.273  18.646  79.731  1.00 97.56           C  
ANISOU 1001  CA  ASP A 129    11398   9883  15787  -4337  -2171  -1511       C  
ATOM   1002  C   ASP A 129      29.464  18.762  78.737  1.00 94.17           C  
ANISOU 1002  C   ASP A 129    11523   9395  14860  -3885  -2370  -1689       C  
ATOM   1003  O   ASP A 129      29.925  17.746  78.184  1.00 97.00           O  
ANISOU 1003  O   ASP A 129    12366   9347  15143  -3960  -2501  -1920       O  
ATOM   1004  CB  ASP A 129      28.106  17.203  80.249  1.00101.81           C  
ANISOU 1004  CB  ASP A 129    12192   9864  16626  -4825  -2020  -1497       C  
ATOM   1005  CG  ASP A 129      27.629  17.146  81.703  1.00103.06           C  
ANISOU 1005  CG  ASP A 129    12068  10023  17066  -5109  -1526  -1131       C  
ATOM   1006  OD1 ASP A 129      27.985  18.051  82.498  1.00 99.09           O  
ANISOU 1006  OD1 ASP A 129    11441   9817  16389  -4789  -1199   -863       O  
ATOM   1007  OD2 ASP A 129      26.904  16.188  82.055  1.00108.40           O  
ANISOU 1007  OD2 ASP A 129    12674  10395  18117  -5678  -1451  -1118       O  
ATOM   1008  N   LYS A 130      29.939  19.992  78.512  1.00 88.32           N  
ANISOU 1008  N   LYS A 130    10709   9048  13799  -3434  -2369  -1595       N  
ATOM   1009  CA  LYS A 130      31.203  20.205  77.797  1.00 84.23           C  
ANISOU 1009  CA  LYS A 130    10688   8517  12798  -3005  -2401  -1686       C  
ATOM   1010  C   LYS A 130      32.278  20.550  78.808  1.00 78.56           C  
ANISOU 1010  C   LYS A 130    10126   7770  11951  -2687  -1951  -1383       C  
ATOM   1011  O   LYS A 130      31.994  21.195  79.833  1.00 76.56           O  
ANISOU 1011  O   LYS A 130     9545   7701  11842  -2678  -1695  -1105       O  
ATOM   1012  CB  LYS A 130      31.103  21.264  76.695  1.00 83.25           C  
ANISOU 1012  CB  LYS A 130    10475   8803  12353  -2762  -2743  -1794       C  
ATOM   1013  CG  LYS A 130      30.349  20.777  75.449  1.00 90.10           C  
ANISOU 1013  CG  LYS A 130    11378   9665  13189  -3015  -3278  -2159       C  
ATOM   1014  CD  LYS A 130      31.102  21.119  74.187  1.00 90.47           C  
ANISOU 1014  CD  LYS A 130    11865   9849  12660  -2716  -3499  -2347       C  
ATOM   1015  CE  LYS A 130      30.828  20.097  73.116  1.00 96.72           C  
ANISOU 1015  CE  LYS A 130    12979  10429  13339  -2973  -3889  -2784       C  
ATOM   1016  NZ  LYS A 130      31.795  20.234  72.002  1.00 97.80           N  
ANISOU 1016  NZ  LYS A 130    13663  10645  12848  -2676  -3951  -2989       N  
ATOM   1017  N   SER A 131      33.508  20.123  78.508  1.00 76.01           N  
ANISOU 1017  N   SER A 131    10291   7232  11358  -2419  -1864  -1467       N  
ATOM   1018  CA  SER A 131      34.565  20.019  79.518  1.00 71.06           C  
ANISOU 1018  CA  SER A 131     9860   6448  10689  -2180  -1493  -1220       C  
ATOM   1019  C   SER A 131      35.795  20.850  79.204  1.00 65.10           C  
ANISOU 1019  C   SER A 131     9251   5929   9555  -1716  -1388  -1192       C  
ATOM   1020  O   SER A 131      36.420  20.698  78.153  1.00 65.88           O  
ANISOU 1020  O   SER A 131     9623   6018   9388  -1540  -1502  -1447       O  
ATOM   1021  CB  SER A 131      34.963  18.535  79.715  1.00 75.05           C  
ANISOU 1021  CB  SER A 131    10782   6380  11353  -2294  -1446  -1310       C  
ATOM   1022  OG  SER A 131      35.582  18.315  80.979  1.00 73.97           O  
ANISOU 1022  OG  SER A 131    10753   6057  11292  -2186  -1139   -986       O  
ATOM   1023  N   VAL A 132      36.142  21.694  80.168  1.00 58.45           N  
ANISOU 1023  N   VAL A 132     8227   5290   8690  -1550  -1143   -893       N  
ATOM   1024  CA  VAL A 132      37.318  22.536  80.146  1.00 52.17           C  
ANISOU 1024  CA  VAL A 132     7506   4709   7608  -1168   -997   -809       C  
ATOM   1025  C   VAL A 132      37.977  22.383  81.521  1.00 48.36           C  
ANISOU 1025  C   VAL A 132     7062   4099   7213  -1066   -721   -539       C  
ATOM   1026  O   VAL A 132      37.266  22.264  82.519  1.00 46.63           O  
ANISOU 1026  O   VAL A 132     6692   3827   7197  -1287   -617   -345       O  
ATOM   1027  CB  VAL A 132      36.878  24.008  79.846  1.00 50.35           C  
ANISOU 1027  CB  VAL A 132     6975   4907   7247  -1101  -1075   -728       C  
ATOM   1028  CG1 VAL A 132      37.654  25.016  80.602  1.00 45.13           C  
ANISOU 1028  CG1 VAL A 132     6232   4438   6476   -860   -842   -498       C  
ATOM   1029  CG2 VAL A 132      36.901  24.300  78.333  1.00 52.03           C  
ANISOU 1029  CG2 VAL A 132     7321   5273   7173  -1033  -1337   -958       C  
ATOM   1030  N   CYS A 133      39.317  22.370  81.546  1.00 45.69           N  
ANISOU 1030  N   CYS A 133     6917   3732   6710   -743   -610   -536       N  
ATOM   1031  CA  CYS A 133      40.135  22.337  82.787  1.00 43.88           C  
ANISOU 1031  CA  CYS A 133     6731   3432   6507   -580   -420   -282       C  
ATOM   1032  C   CYS A 133      41.031  23.576  82.986  1.00 38.85           C  
ANISOU 1032  C   CYS A 133     5947   3148   5663   -317   -310   -181       C  
ATOM   1033  O   CYS A 133      41.703  24.050  82.092  1.00 37.40           O  
ANISOU 1033  O   CYS A 133     5771   3138   5300   -136   -319   -329       O  
ATOM   1034  CB  CYS A 133      41.030  21.080  82.842  1.00 46.76           C  
ANISOU 1034  CB  CYS A 133     7423   3388   6953   -408   -423   -353       C  
ATOM   1035  SG  CYS A 133      40.187  19.520  82.479  1.00 55.48           S  
ANISOU 1035  SG  CYS A 133     8801   3961   8318   -708   -570   -522       S  
ATOM   1036  N   LEU A 134      41.083  24.065  84.205  1.00 36.65           N  
ANISOU 1036  N   LEU A 134     5563   2962   5399   -319   -189     69       N  
ATOM   1037  CA  LEU A 134      41.844  25.256  84.487  1.00 32.55           C  
ANISOU 1037  CA  LEU A 134     4905   2743   4716   -129   -107    152       C  
ATOM   1038  C   LEU A 134      42.946  24.974  85.513  1.00 31.80           C  
ANISOU 1038  C   LEU A 134     4908   2571   4603     61    -47    306       C  
ATOM   1039  O   LEU A 134      42.664  24.563  86.637  1.00 33.98           O  
ANISOU 1039  O   LEU A 134     5266   2715   4928    -35     -8    505       O  
ATOM   1040  CB  LEU A 134      40.902  26.377  84.959  1.00 30.45           C  
ANISOU 1040  CB  LEU A 134     4399   2717   4451   -278    -54    260       C  
ATOM   1041  CG  LEU A 134      41.525  27.715  85.395  1.00 28.50           C  
ANISOU 1041  CG  LEU A 134     4028   2734   4065   -133     25    344       C  
ATOM   1042  CD1 LEU A 134      41.764  28.617  84.197  1.00 24.88           C  
ANISOU 1042  CD1 LEU A 134     3508   2456   3490    -47    -44    228       C  
ATOM   1043  CD2 LEU A 134      40.613  28.414  86.427  1.00 27.57           C  
ANISOU 1043  CD2 LEU A 134     3748   2729   3997   -265    134    465       C  
ATOM   1044  N   PHE A 135      44.197  25.181  85.129  1.00 30.35           N  
ANISOU 1044  N   PHE A 135     4710   2483   4339    323    -44    221       N  
ATOM   1045  CA  PHE A 135      45.339  25.137  86.080  1.00 30.54           C  
ANISOU 1045  CA  PHE A 135     4736   2514   4354    536    -45    357       C  
ATOM   1046  C   PHE A 135      45.539  26.605  86.503  1.00 28.28           C  
ANISOU 1046  C   PHE A 135     4240   2573   3931    509     15    435       C  
ATOM   1047  O   PHE A 135      45.761  27.465  85.662  1.00 24.56           O  
ANISOU 1047  O   PHE A 135     3636   2310   3384    522     60    319       O  
ATOM   1048  CB  PHE A 135      46.601  24.576  85.370  1.00 31.32           C  
ANISOU 1048  CB  PHE A 135     4844   2551   4502    840    -62    174       C  
ATOM   1049  CG  PHE A 135      47.858  24.405  86.271  1.00 31.58           C  
ANISOU 1049  CG  PHE A 135     4822   2586   4590   1110   -131    288       C  
ATOM   1050  CD1 PHE A 135      49.149  24.470  85.691  1.00 32.65           C  
ANISOU 1050  CD1 PHE A 135     4774   2858   4773   1391    -95    112       C  
ATOM   1051  CD2 PHE A 135      47.765  24.083  87.642  1.00 32.44           C  
ANISOU 1051  CD2 PHE A 135     5061   2559   4703   1091   -240    559       C  
ATOM   1052  CE1 PHE A 135      50.310  24.299  86.459  1.00 36.81           C  
ANISOU 1052  CE1 PHE A 135     5175   3409   5400   1659   -208    192       C  
ATOM   1053  CE2 PHE A 135      48.919  23.886  88.434  1.00 31.46           C  
ANISOU 1053  CE2 PHE A 135     4897   2438   4616   1360   -386    668       C  
ATOM   1054  CZ  PHE A 135      50.201  23.999  87.857  1.00 34.65           C  
ANISOU 1054  CZ  PHE A 135     5049   2992   5123   1657   -396    480       C  
ATOM   1055  N   THR A 136      45.448  26.888  87.800  1.00 28.60           N  
ANISOU 1055  N   THR A 136     4295   2652   3919    455     17    629       N  
ATOM   1056  CA  THR A 136      45.561  28.249  88.210  1.00 28.61           C  
ANISOU 1056  CA  THR A 136     4138   2927   3804    415     66    656       C  
ATOM   1057  C   THR A 136      46.270  28.376  89.543  1.00 29.00           C  
ANISOU 1057  C   THR A 136     4231   3031   3755    487      4    803       C  
ATOM   1058  O   THR A 136      46.351  27.404  90.286  1.00 32.05           O  
ANISOU 1058  O   THR A 136     4805   3234   4137    526    -68    947       O  
ATOM   1059  CB  THR A 136      44.143  28.910  88.260  1.00 28.51           C  
ANISOU 1059  CB  THR A 136     4066   2978   3787    193    161    665       C  
ATOM   1060  OG1 THR A 136      44.273  30.310  88.476  1.00 28.06           O  
ANISOU 1060  OG1 THR A 136     3876   3135   3649    189    202    646       O  
ATOM   1061  CG2 THR A 136      43.286  28.291  89.387  1.00 32.61           C  
ANISOU 1061  CG2 THR A 136     4707   3378   4305     33    231    820       C  
ATOM   1062  N   ASP A 137      46.790  29.577  89.815  1.00 26.64           N  
ANISOU 1062  N   ASP A 137     3788   2965   3367    492      6    771       N  
ATOM   1063  CA  ASP A 137      47.369  29.984  91.099  1.00 27.19           C  
ANISOU 1063  CA  ASP A 137     3892   3144   3294    513    -82    866       C  
ATOM   1064  C   ASP A 137      48.711  29.408  91.424  1.00 28.70           C  
ANISOU 1064  C   ASP A 137     4056   3331   3515    730   -282    906       C  
ATOM   1065  O   ASP A 137      49.087  29.351  92.584  1.00 31.57           O  
ANISOU 1065  O   ASP A 137     4527   3730   3738    761   -429   1030       O  
ATOM   1066  CB  ASP A 137      46.371  29.876  92.305  1.00 26.66           C  
ANISOU 1066  CB  ASP A 137     4031   3036   3060    354     -5   1009       C  
ATOM   1067  CG  ASP A 137      45.109  30.605  92.031  1.00 26.44           C  
ANISOU 1067  CG  ASP A 137     3925   3060   3058    181    192    929       C  
ATOM   1068  OD1 ASP A 137      45.122  31.407  91.056  1.00 32.41           O  
ANISOU 1068  OD1 ASP A 137     4505   3890   3917    196    211    791       O  
ATOM   1069  OD2 ASP A 137      44.068  30.365  92.694  1.00 30.09           O  
ANISOU 1069  OD2 ASP A 137     4486   3487   3457     31    337   1006       O  
ATOM   1070  N   PHE A 138      49.442  28.983  90.399  1.00 28.51           N  
ANISOU 1070  N   PHE A 138     3884   3280   3665    896   -296    789       N  
ATOM   1071  CA  PHE A 138      50.782  28.476  90.605  1.00 29.38           C  
ANISOU 1071  CA  PHE A 138     3870   3412   3880   1154   -481    784       C  
ATOM   1072  C   PHE A 138      51.797  29.643  90.523  1.00 30.26           C  
ANISOU 1072  C   PHE A 138     3658   3830   4009   1136   -502    668       C  
ATOM   1073  O   PHE A 138      51.499  30.708  89.937  1.00 28.78           O  
ANISOU 1073  O   PHE A 138     3376   3773   3783    945   -334    577       O  
ATOM   1074  CB  PHE A 138      51.075  27.387  89.556  1.00 29.13           C  
ANISOU 1074  CB  PHE A 138     3821   3194   4051   1362   -441    667       C  
ATOM   1075  CG  PHE A 138      50.761  27.793  88.093  1.00 28.58           C  
ANISOU 1075  CG  PHE A 138     3648   3203   4005   1267   -205    462       C  
ATOM   1076  CD1 PHE A 138      51.749  28.357  87.275  1.00 25.80           C  
ANISOU 1076  CD1 PHE A 138     3004   3084   3712   1337    -99    292       C  
ATOM   1077  CD2 PHE A 138      49.515  27.553  87.527  1.00 24.83           C  
ANISOU 1077  CD2 PHE A 138     3369   2577   3486   1099   -101    444       C  
ATOM   1078  CE1 PHE A 138      51.500  28.690  85.958  1.00 22.20           C  
ANISOU 1078  CE1 PHE A 138     2526   2705   3203   1243    112    140       C  
ATOM   1079  CE2 PHE A 138      49.272  27.887  86.208  1.00 24.03           C  
ANISOU 1079  CE2 PHE A 138     3217   2556   3356   1030     46    273       C  
ATOM   1080  CZ  PHE A 138      50.268  28.472  85.424  1.00 22.52           C  
ANISOU 1080  CZ  PHE A 138     2804   2594   3156   1102    159    134       C  
ATOM   1081  N   ASP A 139      52.971  29.450  91.115  1.00 33.15           N  
ANISOU 1081  N   ASP A 139     3856   4290   4449   1322   -731    684       N  
ATOM   1082  CA  ASP A 139      54.109  30.400  91.021  1.00 35.63           C  
ANISOU 1082  CA  ASP A 139     3789   4895   4852   1295   -776    555       C  
ATOM   1083  C   ASP A 139      54.665  30.558  89.603  1.00 35.66           C  
ANISOU 1083  C   ASP A 139     3495   5010   5042   1324   -530    364       C  
ATOM   1084  O   ASP A 139      54.323  29.798  88.699  1.00 34.58           O  
ANISOU 1084  O   ASP A 139     3449   4729   4961   1433   -370    301       O  
ATOM   1085  CB  ASP A 139      55.259  30.117  92.053  1.00 39.38           C  
ANISOU 1085  CB  ASP A 139     4097   5475   5388   1493  -1147    609       C  
ATOM   1086  CG  ASP A 139      56.048  28.851  91.767  1.00 43.73           C  
ANISOU 1086  CG  ASP A 139     4503   5915   6196   1884  -1277    594       C  
ATOM   1087  OD1 ASP A 139      56.247  28.477  90.605  1.00 48.14           O  
ANISOU 1087  OD1 ASP A 139     4898   6444   6946   2001  -1045    434       O  
ATOM   1088  OD2 ASP A 139      56.508  28.216  92.735  1.00 48.70           O  
ANISOU 1088  OD2 ASP A 139     5198   6478   6826   2102  -1634    737       O  
ATOM   1089  N   SER A 140      55.482  31.588  89.422  1.00 36.96           N  
ANISOU 1089  N   SER A 140     3337   5431   5273   1183   -486    265       N  
ATOM   1090  CA  SER A 140      55.856  32.023  88.079  1.00 37.72           C  
ANISOU 1090  CA  SER A 140     3212   5664   5454   1094   -173    119       C  
ATOM   1091  C   SER A 140      57.061  31.224  87.594  1.00 42.25           C  
ANISOU 1091  C   SER A 140     3412   6357   6284   1383   -139    -29       C  
ATOM   1092  O   SER A 140      57.423  31.303  86.412  1.00 42.15           O  
ANISOU 1092  O   SER A 140     3228   6465   6322   1362    173   -176       O  
ATOM   1093  CB  SER A 140      56.085  33.544  88.045  1.00 37.09           C  
ANISOU 1093  CB  SER A 140     2999   5758   5334    749    -92    104       C  
ATOM   1094  OG  SER A 140      54.829  34.229  88.117  1.00 32.32           O  
ANISOU 1094  OG  SER A 140     2753   5000   4525    541    -39    197       O  
ATOM   1095  N   GLN A 141      57.638  30.428  88.505  1.00 45.69           N  
ANISOU 1095  N   GLN A 141     3746   6750   6864   1671   -457      9       N  
ATOM   1096  CA  GLN A 141      58.734  29.500  88.183  1.00 52.75           C  
ANISOU 1096  CA  GLN A 141     4277   7701   8062   2052   -485   -137       C  
ATOM   1097  C   GLN A 141      58.174  28.236  87.573  1.00 53.39           C  
ANISOU 1097  C   GLN A 141     4653   7472   8159   2319   -379   -182       C  
ATOM   1098  O   GLN A 141      58.910  27.415  87.077  1.00 57.00           O  
ANISOU 1098  O   GLN A 141     4879   7915   8861   2659   -321   -355       O  
ATOM   1099  CB  GLN A 141      59.541  29.098  89.428  1.00 56.37           C  
ANISOU 1099  CB  GLN A 141     4544   8191   8682   2306   -953    -51       C  
ATOM   1100  CG  GLN A 141      60.876  29.758  89.614  1.00 62.94           C  
ANISOU 1100  CG  GLN A 141     4758   9394   9760   2281  -1060   -177       C  
ATOM   1101  CD  GLN A 141      61.894  28.883  90.378  1.00 74.46           C  
ANISOU 1101  CD  GLN A 141     5903  10874  11511   2732  -1503   -172       C  
ATOM   1102  OE1 GLN A 141      61.969  27.651  90.182  1.00 79.13           O  
ANISOU 1102  OE1 GLN A 141     6566  11230  12269   3164  -1556   -187       O  
ATOM   1103  NE2 GLN A 141      62.723  29.528  91.219  1.00 78.52           N  
ANISOU 1103  NE2 GLN A 141     6053  11660  12118   2643  -1850   -168       N  
ATOM   1104  N   THR A 142      56.861  28.085  87.615  1.00 51.68           N  
ANISOU 1104  N   THR A 142     4930   6999   7705   2162   -355    -51       N  
ATOM   1105  CA  THR A 142      56.215  26.869  87.146  1.00 53.52           C  
ANISOU 1105  CA  THR A 142     5491   6888   7956   2351   -306    -86       C  
ATOM   1106  C   THR A 142      56.092  26.828  85.627  1.00 54.46           C  
ANISOU 1106  C   THR A 142     5594   7056   8040   2313     70   -333       C  
ATOM   1107  O   THR A 142      55.535  27.752  85.008  1.00 52.50           O  
ANISOU 1107  O   THR A 142     5415   6954   7577   1990    278   -336       O  
ATOM   1108  CB  THR A 142      54.845  26.696  87.815  1.00 50.66           C  
ANISOU 1108  CB  THR A 142     5613   6254   7380   2154   -425    144       C  
ATOM   1109  OG1 THR A 142      55.040  26.281  89.174  1.00 53.44           O  
ANISOU 1109  OG1 THR A 142     6071   6489   7745   2284   -772    366       O  
ATOM   1110  CG2 THR A 142      53.996  25.659  87.094  1.00 51.38           C  
ANISOU 1110  CG2 THR A 142     6037   6006   7477   2205   -317     75       C  
ATOM   1111  N   ASN A 143      56.624  25.747  85.051  1.00 58.74           N  
ANISOU 1111  N   ASN A 143     6075   7460   8780   2667    137   -542       N  
ATOM   1112  CA  ASN A 143      56.520  25.440  83.627  1.00 60.59           C  
ANISOU 1112  CA  ASN A 143     6374   7700   8946   2692    482   -825       C  
ATOM   1113  C   ASN A 143      55.240  24.681  83.279  1.00 59.33           C  
ANISOU 1113  C   ASN A 143     6735   7160   8645   2616    449   -824       C  
ATOM   1114  O   ASN A 143      54.881  23.730  83.976  1.00 60.24           O  
ANISOU 1114  O   ASN A 143     7096   6900   8891   2769    199   -714       O  
ATOM   1115  CB  ASN A 143      57.732  24.606  83.186  1.00 66.40           C  
ANISOU 1115  CB  ASN A 143     6782   8461   9985   3142    592  -1117       C  
ATOM   1116  CG  ASN A 143      58.957  25.462  82.932  1.00 69.95           C  
ANISOU 1116  CG  ASN A 143     6642   9392  10544   3124    809  -1235       C  
ATOM   1117  OD1 ASN A 143      58.852  26.539  82.347  1.00 72.80           O  
ANISOU 1117  OD1 ASN A 143     6941  10047  10671   2755   1073  -1225       O  
ATOM   1118  ND2 ASN A 143      60.111  25.010  83.391  1.00 72.29           N  
ANISOU 1118  ND2 ASN A 143     6494   9760  11213   3506    681  -1328       N  
ATOM   1119  N   VAL A 144      54.556  25.099  82.211  1.00 57.44           N  
ANISOU 1119  N   VAL A 144     6671   7011   8140   2360    678   -933       N  
ATOM   1120  CA  VAL A 144      53.359  24.387  81.780  1.00 57.31           C  
ANISOU 1120  CA  VAL A 144     7096   6668   8010   2262    623   -979       C  
ATOM   1121  C   VAL A 144      53.670  23.593  80.517  1.00 61.80           C  
ANISOU 1121  C   VAL A 144     7756   7169   8556   2460    845  -1366       C  
ATOM   1122  O   VAL A 144      54.028  24.159  79.480  1.00 62.51           O  
ANISOU 1122  O   VAL A 144     7743   7572   8432   2383   1138  -1548       O  
ATOM   1123  CB  VAL A 144      52.124  25.326  81.564  1.00 52.88           C  
ANISOU 1123  CB  VAL A 144     6723   6204   7164   1839    616   -819       C  
ATOM   1124  CG1 VAL A 144      50.873  24.519  81.270  1.00 52.47           C  
ANISOU 1124  CG1 VAL A 144     7053   5816   7065   1725    497   -862       C  
ATOM   1125  CG2 VAL A 144      51.872  26.200  82.781  1.00 49.78           C  
ANISOU 1125  CG2 VAL A 144     6230   5900   6781   1666    456   -500       C  
ATOM   1126  N   SER A 145      53.538  22.278  80.603  1.00 65.50           N  
ANISOU 1126  N   SER A 145     8455   7209   9222   2704    717  -1496       N  
ATOM   1127  CA  SER A 145      53.802  21.448  79.419  1.00 71.29           C  
ANISOU 1127  CA  SER A 145     9327   7827   9933   2914    924  -1927       C  
ATOM   1128  C   SER A 145      52.568  21.058  78.618  1.00 71.31           C  
ANISOU 1128  C   SER A 145     9785   7609   9699   2657    885  -2064       C  
ATOM   1129  O   SER A 145      51.579  20.541  79.168  1.00 69.86           O  
ANISOU 1129  O   SER A 145     9881   7058   9604   2502    619  -1901       O  
ATOM   1130  CB  SER A 145      54.639  20.192  79.733  1.00 76.02           C  
ANISOU 1130  CB  SER A 145     9882   8071  10930   3423    852  -2112       C  
ATOM   1131  OG  SER A 145      55.957  20.533  80.132  1.00 78.35           O  
ANISOU 1131  OG  SER A 145     9666   8657  11445   3715    931  -2107       O  
ATOM   1132  N   GLN A 146      52.680  21.311  77.311  1.00 73.95           N  
ANISOU 1132  N   GLN A 146    10180   8195   9722   2599   1159  -2369       N  
ATOM   1133  CA  GLN A 146      51.895  20.641  76.270  1.00 76.73           C  
ANISOU 1133  CA  GLN A 146    10961   8338   9855   2495   1150  -2682       C  
ATOM   1134  C   GLN A 146      51.992  19.136  76.397  1.00 81.08           C  
ANISOU 1134  C   GLN A 146    11743   8334  10729   2804   1037  -2944       C  
ATOM   1135  O   GLN A 146      52.966  18.535  75.907  1.00 86.98           O  
ANISOU 1135  O   GLN A 146    12420   9045  11581   3192   1266  -3312       O  
ATOM   1136  CB  GLN A 146      52.415  21.032  74.886  1.00 79.40           C  
ANISOU 1136  CB  GLN A 146    11309   9065   9794   2502   1524  -3019       C  
ATOM   1137  CG  GLN A 146      51.370  20.941  73.803  1.00 80.61           C  
ANISOU 1137  CG  GLN A 146    11904   9191   9530   2218   1449  -3210       C  
ATOM   1138  CD  GLN A 146      50.524  22.199  73.705  1.00 77.71           C  
ANISOU 1138  CD  GLN A 146    11549   9127   8847   1801   1320  -2860       C  
ATOM   1139  OE1 GLN A 146      50.963  23.298  74.076  1.00 74.91           O  
ANISOU 1139  OE1 GLN A 146    10895   9101   8466   1725   1438  -2566       O  
ATOM   1140  NE2 GLN A 146      49.299  22.047  73.200  1.00 77.69           N  
ANISOU 1140  NE2 GLN A 146    11887   8996   8634   1533   1053  -2903       N  
ATOM   1141  N   SER A 147      51.005  18.519  77.052  1.00 79.98           N  
ANISOU 1141  N   SER A 147    11872   7745  10771   2637    709  -2764       N  
ATOM   1142  CA  SER A 147      50.910  17.039  77.121  1.00 84.65           C  
ANISOU 1142  CA  SER A 147    12793   7699  11669   2852    564  -2994       C  
ATOM   1143  C   SER A 147      50.593  16.489  75.725  1.00 88.27           C  
ANISOU 1143  C   SER A 147    13599   8060  11877   2809    670  -3520       C  
ATOM   1144  O   SER A 147      49.427  16.262  75.385  1.00 88.05           O  
ANISOU 1144  O   SER A 147    13887   7848  11718   2443    469  -3561       O  
ATOM   1145  CB  SER A 147      49.849  16.586  78.136  1.00 83.04           C  
ANISOU 1145  CB  SER A 147    12810   7058  11683   2578    223  -2636       C  
ATOM   1146  OG  SER A 147      50.104  17.116  79.432  1.00 80.29           O  
ANISOU 1146  OG  SER A 147    12199   6827  11479   2597    130  -2163       O  
ATOM   1147  N   LYS A 148      51.649  16.314  74.931  1.00 91.98           N  
ANISOU 1147  N   LYS A 148    13981   8693  12273   3176    993  -3934       N  
ATOM   1148  CA  LYS A 148      51.558  16.033  73.490  1.00 96.02           C  
ANISOU 1148  CA  LYS A 148    14794   9284  12406   3154   1193  -4474       C  
ATOM   1149  C   LYS A 148      50.725  14.805  73.125  1.00 99.26           C  
ANISOU 1149  C   LYS A 148    15735   9072  12905   3069    947  -4801       C  
ATOM   1150  O   LYS A 148      51.236  13.697  72.912  1.00104.45           O  
ANISOU 1150  O   LYS A 148    16589   9282  13815   3445   1009  -5209       O  
ATOM   1151  CB  LYS A 148      52.951  16.036  72.825  1.00100.76           C  
ANISOU 1151  CB  LYS A 148    15150  10187  12944   3598   1662  -4868       C  
ATOM   1152  CG  LYS A 148      53.580  17.451  72.786  1.00 98.55           C  
ANISOU 1152  CG  LYS A 148    14406  10628  12410   3490   1951  -4603       C  
ATOM   1153  CD  LYS A 148      55.100  17.437  72.594  1.00103.56           C  
ANISOU 1153  CD  LYS A 148    14604  11541  13201   3953   2395  -4868       C  
ATOM   1154  CE  LYS A 148      55.698  18.842  72.753  1.00 99.91           C  
ANISOU 1154  CE  LYS A 148    13651  11728  12580   3773   2632  -4535       C  
ATOM   1155  NZ  LYS A 148      57.065  18.942  72.148  1.00104.52           N  
ANISOU 1155  NZ  LYS A 148    13831  12715  13166   4093   3178  -4886       N  
ATOM   1156  N   ASP A 149      49.420  15.062  73.094  1.00 95.51           N  
ANISOU 1156  N   ASP A 149    15460   8572  12256   2561    651  -4608       N  
ATOM   1157  CA  ASP A 149      48.370  14.167  72.626  1.00 98.04           C  
ANISOU 1157  CA  ASP A 149    16253   8425  12572   2290    369  -4886       C  
ATOM   1158  C   ASP A 149      47.815  14.855  71.364  1.00 97.38           C  
ANISOU 1158  C   ASP A 149    16322   8818  11860   1976    390  -5108       C  
ATOM   1159  O   ASP A 149      47.946  16.081  71.214  1.00 93.53           O  
ANISOU 1159  O   ASP A 149    15569   8927  11041   1871    525  -4846       O  
ATOM   1160  CB  ASP A 149      47.306  14.066  73.735  1.00 94.81           C  
ANISOU 1160  CB  ASP A 149    15829   7701  12493   1924      5  -4402       C  
ATOM   1161  CG  ASP A 149      46.147  13.118  73.407  1.00 99.00           C  
ANISOU 1161  CG  ASP A 149    16784   7711  13120   1562   -315  -4635       C  
ATOM   1162  OD1 ASP A 149      45.716  13.027  72.233  1.00101.91           O  
ANISOU 1162  OD1 ASP A 149    17415   8178  13127   1387   -371  -5063       O  
ATOM   1163  OD2 ASP A 149      45.632  12.487  74.365  1.00 99.81           O  
ANISOU 1163  OD2 ASP A 149    16961   7312  13649   1407   -526  -4362       O  
ATOM   1164  N   SER A 150      47.214  14.078  70.462  1.00100.96           N  
ANISOU 1164  N   SER A 150    17229   8991  12138   1823    231  -5583       N  
ATOM   1165  CA  SER A 150      46.648  14.613  69.213  1.00101.11           C  
ANISOU 1165  CA  SER A 150    17475   9430  11512   1529    173  -5823       C  
ATOM   1166  C   SER A 150      45.563  15.660  69.465  1.00 94.43           C  
ANISOU 1166  C   SER A 150    16430   8924  10524   1073   -134  -5330       C  
ATOM   1167  O   SER A 150      45.648  16.784  68.946  1.00 92.40           O  
ANISOU 1167  O   SER A 150    16061   9245   9800    995    -27  -5173       O  
ATOM   1168  CB  SER A 150      46.105  13.490  68.322  1.00108.05           C  
ANISOU 1168  CB  SER A 150    18900   9877  12274   1414    -33  -6436       C  
ATOM   1169  OG  SER A 150      47.152  12.792  67.662  1.00115.02           O  
ANISOU 1169  OG  SER A 150    20014  10632  13058   1856    332  -7014       O  
ATOM   1170  N   ASP A 151      44.567  15.296  70.278  1.00 90.84           N  
ANISOU 1170  N   ASP A 151    15925   8099  10491    784   -494  -5078       N  
ATOM   1171  CA  ASP A 151      43.436  16.184  70.551  1.00 84.70           C  
ANISOU 1171  CA  ASP A 151    14919   7601   9662    371   -796  -4664       C  
ATOM   1172  C   ASP A 151      43.261  16.588  72.019  1.00 77.59           C  
ANISOU 1172  C   ASP A 151    13610   6648   9220    324   -803  -4083       C  
ATOM   1173  O   ASP A 151      42.129  16.781  72.492  1.00 75.66           O  
ANISOU 1173  O   ASP A 151    13217   6370   9158    -37  -1085  -3823       O  
ATOM   1174  CB  ASP A 151      42.148  15.606  69.958  1.00 88.56           C  
ANISOU 1174  CB  ASP A 151    15673   7863  10110    -49  -1244  -4929       C  
ATOM   1175  CG  ASP A 151      42.196  15.524  68.431  1.00 94.56           C  
ANISOU 1175  CG  ASP A 151    16843   8834  10249    -61  -1294  -5457       C  
ATOM   1176  OD1 ASP A 151      42.331  14.401  67.888  1.00 99.18           O  
ANISOU 1176  OD1 ASP A 151    17835   9009  10838     -7  -1319  -5994       O  
ATOM   1177  OD2 ASP A 151      42.109  16.587  67.774  1.00 93.78           O  
ANISOU 1177  OD2 ASP A 151    16700   9294   9636   -122  -1310  -5336       O  
ATOM   1178  N   VAL A 152      44.373  16.734  72.739  1.00 73.28           N  
ANISOU 1178  N   VAL A 152    12866   6125   8850    686   -493  -3896       N  
ATOM   1179  CA  VAL A 152      44.324  17.466  74.013  1.00 65.71           C  
ANISOU 1179  CA  VAL A 152    11519   5299   8146    652   -471  -3337       C  
ATOM   1180  C   VAL A 152      44.988  18.823  73.837  1.00 60.92           C  
ANISOU 1180  C   VAL A 152    10640   5290   7217    778   -240  -3140       C  
ATOM   1181  O   VAL A 152      46.185  18.896  73.551  1.00 61.41           O  
ANISOU 1181  O   VAL A 152    10661   5505   7167   1108     65  -3288       O  
ATOM   1182  CB  VAL A 152      44.956  16.726  75.228  1.00 65.75           C  
ANISOU 1182  CB  VAL A 152    11474   4880   8628    900   -389  -3154       C  
ATOM   1183  CG1 VAL A 152      44.933  17.642  76.478  1.00 59.00           C  
ANISOU 1183  CG1 VAL A 152    10246   4264   7908    849   -360  -2601       C  
ATOM   1184  CG2 VAL A 152      44.222  15.435  75.519  1.00 67.48           C  
ANISOU 1184  CG2 VAL A 152    11990   4448   9197    709   -621  -3257       C  
ATOM   1185  N   TYR A 153      44.206  19.887  74.025  1.00 55.73           N  
ANISOU 1185  N   TYR A 153     9779   4947   6449    512   -381  -2813       N  
ATOM   1186  CA  TYR A 153      44.682  21.258  73.780  1.00 51.22           C  
ANISOU 1186  CA  TYR A 153     9005   4895   5561    564   -208  -2608       C  
ATOM   1187  C   TYR A 153      45.101  21.947  75.065  1.00 46.08           C  
ANISOU 1187  C   TYR A 153     7998   4337   5173    649    -92  -2189       C  
ATOM   1188  O   TYR A 153      44.405  21.856  76.068  1.00 43.93           O  
ANISOU 1188  O   TYR A 153     7604   3884   5202    506   -248  -1940       O  
ATOM   1189  CB  TYR A 153      43.638  22.065  72.979  1.00 50.97           C  
ANISOU 1189  CB  TYR A 153     9034   5142   5188    272   -462  -2556       C  
ATOM   1190  CG  TYR A 153      43.323  21.483  71.599  1.00 55.46           C  
ANISOU 1190  CG  TYR A 153     9997   5694   5380    187   -603  -2993       C  
ATOM   1191  CD1 TYR A 153      42.174  20.728  71.389  1.00 57.37           C  
ANISOU 1191  CD1 TYR A 153    10390   5665   5741    -71   -979  -3173       C  
ATOM   1192  CD2 TYR A 153      44.195  21.666  70.525  1.00 58.05           C  
ANISOU 1192  CD2 TYR A 153    10548   6283   5223    343   -344  -3244       C  
ATOM   1193  CE1 TYR A 153      41.883  20.177  70.148  1.00 63.00           C  
ANISOU 1193  CE1 TYR A 153    11490   6356   6091   -166  -1153  -3609       C  
ATOM   1194  CE2 TYR A 153      43.921  21.130  69.273  1.00 63.91           C  
ANISOU 1194  CE2 TYR A 153    11704   7027   5550    264   -465  -3671       C  
ATOM   1195  CZ  TYR A 153      42.760  20.385  69.083  1.00 67.06           C  
ANISOU 1195  CZ  TYR A 153    12276   7142   6062     14   -899  -3865       C  
ATOM   1196  OH  TYR A 153      42.482  19.844  67.832  1.00 72.73           O  
ANISOU 1196  OH  TYR A 153    13435   7860   6337    -81  -1065  -4329       O  
ATOM   1197  N   ILE A 154      46.256  22.613  75.045  1.00 45.03           N  
ANISOU 1197  N   ILE A 154     7699   4491   4919    861    195  -2131       N  
ATOM   1198  CA  ILE A 154      46.782  23.309  76.237  1.00 41.54           C  
ANISOU 1198  CA  ILE A 154     6925   4160   4698    941    287  -1776       C  
ATOM   1199  C   ILE A 154      47.453  24.648  75.871  1.00 40.19           C  
ANISOU 1199  C   ILE A 154     6576   4438   4255    937    498  -1645       C  
ATOM   1200  O   ILE A 154      48.379  24.720  75.063  1.00 42.34           O  
ANISOU 1200  O   ILE A 154     6866   4912   4308   1070    764  -1846       O  
ATOM   1201  CB  ILE A 154      47.774  22.420  77.079  1.00 43.47           C  
ANISOU 1201  CB  ILE A 154     7079   4146   5292   1258    388  -1814       C  
ATOM   1202  CG1 ILE A 154      47.323  20.943  77.137  1.00 46.92           C  
ANISOU 1202  CG1 ILE A 154     7799   4064   5961   1297    227  -2017       C  
ATOM   1203  CG2 ILE A 154      48.044  23.049  78.468  1.00 38.36           C  
ANISOU 1203  CG2 ILE A 154     6142   3571   4860   1277    364  -1426       C  
ATOM   1204  CD1 ILE A 154      48.375  19.932  77.548  1.00 47.39           C  
ANISOU 1204  CD1 ILE A 154     7869   3819   6316   1688    313  -2153       C  
ATOM   1205  N   THR A 155      46.922  25.714  76.431  1.00 37.42           N  
ANISOU 1205  N   THR A 155     6071   4229   3916    761    393  -1317       N  
ATOM   1206  CA  THR A 155      47.424  27.066  76.184  1.00 37.31           C  
ANISOU 1206  CA  THR A 155     5924   4564   3688    701    550  -1141       C  
ATOM   1207  C   THR A 155      48.706  27.327  76.978  1.00 36.92           C  
ANISOU 1207  C   THR A 155     5575   4616   3834    871    770  -1057       C  
ATOM   1208  O   THR A 155      48.962  26.670  77.988  1.00 36.10           O  
ANISOU 1208  O   THR A 155     5353   4316   4046   1019    711  -1028       O  
ATOM   1209  CB  THR A 155      46.382  28.115  76.653  1.00 34.48           C  
ANISOU 1209  CB  THR A 155     5497   4250   3353    491    334   -835       C  
ATOM   1210  OG1 THR A 155      46.399  28.171  78.076  1.00 33.46           O  
ANISOU 1210  OG1 THR A 155     5149   4009   3554    526    299   -645       O  
ATOM   1211  CG2 THR A 155      44.990  27.739  76.235  1.00 35.79           C  
ANISOU 1211  CG2 THR A 155     5832   4281   3484    337     35   -893       C  
ATOM   1212  N   ASP A 156      49.493  28.300  76.542  1.00 38.36           N  
ANISOU 1212  N   ASP A 156     5641   5101   3831    825   1000   -997       N  
ATOM   1213  CA  ASP A 156      50.591  28.833  77.347  1.00 38.86           C  
ANISOU 1213  CA  ASP A 156     5361   5305   4097    900   1152   -877       C  
ATOM   1214  C   ASP A 156      49.984  29.449  78.618  1.00 35.15           C  
ANISOU 1214  C   ASP A 156     4788   4735   3830    794    916   -586       C  
ATOM   1215  O   ASP A 156      48.787  29.712  78.685  1.00 33.59           O  
ANISOU 1215  O   ASP A 156     4746   4433   3584    648    715   -469       O  
ATOM   1216  CB  ASP A 156      51.398  29.898  76.557  1.00 40.34           C  
ANISOU 1216  CB  ASP A 156     5463   5831   4033    763   1450   -839       C  
ATOM   1217  CG  ASP A 156      52.217  29.312  75.415  1.00 51.08           C  
ANISOU 1217  CG  ASP A 156     6865   7357   5184    882   1787  -1151       C  
ATOM   1218  OD1 ASP A 156      52.636  28.115  75.460  1.00 58.17           O  
ANISOU 1218  OD1 ASP A 156     7714   8129   6258   1161   1840  -1430       O  
ATOM   1219  OD2 ASP A 156      52.481  30.052  74.422  1.00 60.18           O  
ANISOU 1219  OD2 ASP A 156     8124   8765   5976    700   2032  -1128       O  
ATOM   1220  N   LYS A 157      50.785  29.668  79.645  1.00 34.42           N  
ANISOU 1220  N   LYS A 157     4423   4688   3966    876    932   -493       N  
ATOM   1221  CA  LYS A 157      50.264  30.369  80.793  1.00 32.20           C  
ANISOU 1221  CA  LYS A 157     4084   4351   3798    759    751   -254       C  
ATOM   1222  C   LYS A 157      49.905  31.821  80.431  1.00 30.67           C  
ANISOU 1222  C   LYS A 157     3925   4293   3433    519    780    -98       C  
ATOM   1223  O   LYS A 157      50.546  32.423  79.596  1.00 32.27           O  
ANISOU 1223  O   LYS A 157     4101   4680   3478    435    974   -116       O  
ATOM   1224  CB  LYS A 157      51.273  30.351  81.931  1.00 31.56           C  
ANISOU 1224  CB  LYS A 157     3731   4316   3941    884    724   -205       C  
ATOM   1225  CG  LYS A 157      52.595  30.984  81.610  1.00 36.33           C  
ANISOU 1225  CG  LYS A 157     4046   5193   4562    877    929   -262       C  
ATOM   1226  CD  LYS A 157      53.427  30.980  82.898  1.00 36.05           C  
ANISOU 1226  CD  LYS A 157     3732   5194   4770    988    787   -202       C  
ATOM   1227  CE  LYS A 157      54.765  31.667  82.756  1.00 40.51           C  
ANISOU 1227  CE  LYS A 157     3914   6049   5427    938    952   -259       C  
ATOM   1228  NZ  LYS A 157      55.438  31.809  84.107  1.00 36.16           N  
ANISOU 1228  NZ  LYS A 157     3107   5542   5090   1002    713   -187       N  
ATOM   1229  N   CYS A 158      48.856  32.366  81.037  1.00 29.49           N  
ANISOU 1229  N   CYS A 158     3849   4034   3320    411    602     55       N  
ATOM   1230  CA  CYS A 158      48.654  33.815  80.985  1.00 29.68           C  
ANISOU 1230  CA  CYS A 158     3882   4123   3271    238    600    214       C  
ATOM   1231  C   CYS A 158      48.302  34.460  82.334  1.00 26.53           C  
ANISOU 1231  C   CYS A 158     3397   3645   3038    200    482    331       C  
ATOM   1232  O   CYS A 158      47.887  33.765  83.289  1.00 24.38           O  
ANISOU 1232  O   CYS A 158     3105   3273   2886    279    386    323       O  
ATOM   1233  CB  CYS A 158      47.967  34.318  79.680  1.00 32.86           C  
ANISOU 1233  CB  CYS A 158     4513   4545   3425    130    579    257       C  
ATOM   1234  SG  CYS A 158      46.256  34.871  79.385  1.00 38.93           S  
ANISOU 1234  SG  CYS A 158     5460   5178   4152     68    304    377       S  
ATOM   1235  N   VAL A 159      48.612  35.746  82.433  1.00 24.48           N  
ANISOU 1235  N   VAL A 159     3104   3428   2769     68    517    427       N  
ATOM   1236  CA  VAL A 159      48.618  36.461  83.729  1.00 23.20           C  
ANISOU 1236  CA  VAL A 159     2860   3215   2739     27    442    476       C  
ATOM   1237  C   VAL A 159      47.417  37.379  83.722  1.00 22.24           C  
ANISOU 1237  C   VAL A 159     2875   2953   2621    -24    348    559       C  
ATOM   1238  O   VAL A 159      47.308  38.228  82.853  1.00 19.49           O  
ANISOU 1238  O   VAL A 159     2638   2572   2194   -111    357    643       O  
ATOM   1239  CB  VAL A 159      49.880  37.349  83.899  1.00 25.20           C  
ANISOU 1239  CB  VAL A 159     2968   3575   3032   -106    530    486       C  
ATOM   1240  CG1 VAL A 159      49.807  38.176  85.215  1.00 25.35           C  
ANISOU 1240  CG1 VAL A 159     2961   3518   3152   -170    417    494       C  
ATOM   1241  CG2 VAL A 159      51.163  36.488  83.870  1.00 28.20           C  
ANISOU 1241  CG2 VAL A 159     3116   4132   3466    -21    621    382       C  
ATOM   1242  N   LEU A 160      46.526  37.190  84.684  1.00 21.48           N  
ANISOU 1242  N   LEU A 160     2772   2773   2616     38    267    541       N  
ATOM   1243  CA  LEU A 160      45.448  38.138  84.851  1.00 23.32           C  
ANISOU 1243  CA  LEU A 160     3062   2883   2916     33    198    578       C  
ATOM   1244  C   LEU A 160      45.684  38.937  86.136  1.00 23.46           C  
ANISOU 1244  C   LEU A 160     3051   2860   3004      2    216    534       C  
ATOM   1245  O   LEU A 160      46.246  38.422  87.151  1.00 20.81           O  
ANISOU 1245  O   LEU A 160     2658   2602   2647      6    235    481       O  
ATOM   1246  CB  LEU A 160      44.073  37.421  84.874  1.00 22.35           C  
ANISOU 1246  CB  LEU A 160     2915   2716   2859    110    130    552       C  
ATOM   1247  CG  LEU A 160      43.582  36.590  86.045  1.00 25.14           C  
ANISOU 1247  CG  LEU A 160     3196   3075   3279    134    176    502       C  
ATOM   1248  CD1 LEU A 160      43.007  37.464  87.154  1.00 21.50           C  
ANISOU 1248  CD1 LEU A 160     2698   2575   2893    146    227    464       C  
ATOM   1249  CD2 LEU A 160      42.450  35.547  85.576  1.00 25.77           C  
ANISOU 1249  CD2 LEU A 160     3238   3127   3426    135    121    483       C  
ATOM   1250  N   ASP A 161      45.190  40.171  86.112  1.00 23.51           N  
ANISOU 1250  N   ASP A 161     3127   2722   3083    -11    181    550       N  
ATOM   1251  CA  ASP A 161      45.474  41.130  87.197  1.00 23.72           C  
ANISOU 1251  CA  ASP A 161     3179   2668   3163    -58    194    464       C  
ATOM   1252  C   ASP A 161      44.126  41.674  87.726  1.00 24.73           C  
ANISOU 1252  C   ASP A 161     3325   2659   3411     69    189    388       C  
ATOM   1253  O   ASP A 161      43.484  42.471  87.022  1.00 25.34           O  
ANISOU 1253  O   ASP A 161     3460   2569   3598    134    115    442       O  
ATOM   1254  CB  ASP A 161      46.340  42.287  86.633  1.00 23.43           C  
ANISOU 1254  CB  ASP A 161     3232   2522   3149   -215    182    527       C  
ATOM   1255  CG  ASP A 161      46.629  43.380  87.692  1.00 26.37           C  
ANISOU 1255  CG  ASP A 161     3667   2754   3599   -295    163    401       C  
ATOM   1256  OD1 ASP A 161      46.124  43.309  88.812  1.00 28.62           O  
ANISOU 1256  OD1 ASP A 161     3948   3043   3881   -207    172    256       O  
ATOM   1257  OD2 ASP A 161      47.363  44.325  87.414  1.00 30.24           O  
ANISOU 1257  OD2 ASP A 161     4230   3121   4138   -472    152    435       O  
ATOM   1258  N   MET A 162      43.667  41.233  88.901  1.00 23.85           N  
ANISOU 1258  N   MET A 162     3161   2621   3276    119    270    272       N  
ATOM   1259  CA  MET A 162      42.489  41.848  89.503  1.00 26.13           C  
ANISOU 1259  CA  MET A 162     3426   2812   3688    241    335    148       C  
ATOM   1260  C   MET A 162      42.879  43.087  90.278  1.00 27.50           C  
ANISOU 1260  C   MET A 162     3732   2840   3875    219    350      0       C  
ATOM   1261  O   MET A 162      43.234  42.993  91.444  1.00 28.00           O  
ANISOU 1261  O   MET A 162     3851   2993   3792    164    422   -130       O  
ATOM   1262  CB  MET A 162      41.706  40.857  90.416  1.00 25.92           C  
ANISOU 1262  CB  MET A 162     3299   2942   3607    271    486     85       C  
ATOM   1263  CG  MET A 162      41.370  39.536  89.720  1.00 25.11           C  
ANISOU 1263  CG  MET A 162     3091   2938   3510    247    458    212       C  
ATOM   1264  SD  MET A 162      40.745  38.236  90.819  1.00 27.74           S  
ANISOU 1264  SD  MET A 162     3373   3413   3750    182    646    205       S  
ATOM   1265  CE  MET A 162      39.156  38.878  91.458  1.00 19.99           C  
ANISOU 1265  CE  MET A 162     2203   2442   2948    269    854     39       C  
ATOM   1266  N   ARG A 163      42.789  44.244  89.624  1.00 30.29           N  
ANISOU 1266  N   ARG A 163     4174   2945   4389    255    259     21       N  
ATOM   1267  CA  ARG A 163      43.077  45.570  90.222  1.00 33.04           C  
ANISOU 1267  CA  ARG A 163     4690   3050   4811    232    249   -137       C  
ATOM   1268  C   ARG A 163      42.322  45.853  91.512  1.00 35.10           C  
ANISOU 1268  C   ARG A 163     4955   3303   5078    365    397   -416       C  
ATOM   1269  O   ARG A 163      42.847  46.503  92.383  1.00 37.53           O  
ANISOU 1269  O   ARG A 163     5418   3529   5312    283    413   -608       O  
ATOM   1270  CB  ARG A 163      42.718  46.710  89.248  1.00 35.48           C  
ANISOU 1270  CB  ARG A 163     5118   3017   5345    315    121    -37       C  
ATOM   1271  CG  ARG A 163      43.487  46.717  87.898  1.00 38.55           C  
ANISOU 1271  CG  ARG A 163     5589   3374   5681    148      6    248       C  
ATOM   1272  CD  ARG A 163      43.162  47.986  87.037  1.00 43.73           C  
ANISOU 1272  CD  ARG A 163     6463   3631   6521    210   -140    390       C  
ATOM   1273  NE  ARG A 163      43.114  49.151  87.901  1.00 52.76           N  
ANISOU 1273  NE  ARG A 163     7758   4452   7837    246   -134    179       N  
ATOM   1274  CZ  ARG A 163      42.118  50.036  87.939  1.00 57.25           C  
ANISOU 1274  CZ  ARG A 163     8405   4686   8659    519   -213    102       C  
ATOM   1275  NH1 ARG A 163      41.086  49.950  87.089  1.00 58.35           N  
ANISOU 1275  NH1 ARG A 163     8467   4778   8923    776   -350    259       N  
ATOM   1276  NH2 ARG A 163      42.190  51.033  88.808  1.00 58.75           N  
ANISOU 1276  NH2 ARG A 163     8756   4575   8989    542   -181   -147       N  
ATOM   1277  N   SER A 164      41.082  45.400  91.638  1.00 35.00           N  
ANISOU 1277  N   SER A 164     4766   3381   5151    553    517   -463       N  
ATOM   1278  CA  SER A 164      40.265  45.748  92.794  1.00 37.66           C  
ANISOU 1278  CA  SER A 164     5081   3724   5503    694    729   -750       C  
ATOM   1279  C   SER A 164      40.721  45.004  94.049  1.00 37.28           C  
ANISOU 1279  C   SER A 164     5112   3947   5103    541    886   -848       C  
ATOM   1280  O   SER A 164      40.161  45.198  95.122  1.00 39.22           O  
ANISOU 1280  O   SER A 164     5393   4255   5252    609   1108  -1093       O  
ATOM   1281  CB  SER A 164      38.824  45.286  92.546  1.00 38.62           C  
ANISOU 1281  CB  SER A 164     4902   3942   5827    894    846   -753       C  
ATOM   1282  OG  SER A 164      38.776  43.839  92.711  1.00 39.19           O  
ANISOU 1282  OG  SER A 164     4851   4327   5712    749    945   -623       O  
ATOM   1283  N   MET A 165      41.632  44.052  93.887  1.00 35.24           N  
ANISOU 1283  N   MET A 165     4873   3866   4648    360    783   -648       N  
ATOM   1284  CA  MET A 165      42.157  43.301  95.024  1.00 36.73           C  
ANISOU 1284  CA  MET A 165     5175   4289   4489    231    850   -680       C  
ATOM   1285  C   MET A 165      43.697  43.323  95.062  1.00 34.91           C  
ANISOU 1285  C   MET A 165     5064   4083   4114     55    614   -617       C  
ATOM   1286  O   MET A 165      44.291  42.640  95.903  1.00 35.96           O  
ANISOU 1286  O   MET A 165     5288   4410   3965    -34    574   -599       O  
ATOM   1287  CB  MET A 165      41.686  41.824  94.945  1.00 36.07           C  
ANISOU 1287  CB  MET A 165     4960   4415   4328    210    946   -483       C  
ATOM   1288  CG  MET A 165      40.276  41.506  95.433  1.00 42.18           C  
ANISOU 1288  CG  MET A 165     5603   5283   5139    287   1243   -568       C  
ATOM   1289  SD  MET A 165      39.812  39.744  95.153  1.00 47.43           S  
ANISOU 1289  SD  MET A 165     6129   6115   5777    179   1313   -300       S  
ATOM   1290  CE  MET A 165      38.443  39.721  96.265  1.00 51.44           C  
ANISOU 1290  CE  MET A 165     6547   6771   6227    182   1739   -475       C  
ATOM   1291  N   ASP A 166      44.344  44.052  94.156  1.00 32.84           N  
ANISOU 1291  N   ASP A 166     4788   3641   4046     -1    453   -564       N  
ATOM   1292  CA  ASP A 166      45.805  43.940  93.993  1.00 33.60           C  
ANISOU 1292  CA  ASP A 166     4881   3809   4076   -187    258   -481       C  
ATOM   1293  C   ASP A 166      46.239  42.451  93.992  1.00 30.10           C  
ANISOU 1293  C   ASP A 166     4327   3627   3482   -188    220   -295       C  
ATOM   1294  O   ASP A 166      47.041  42.036  94.804  1.00 30.22           O  
ANISOU 1294  O   ASP A 166     4383   3798   3300   -257    104   -317       O  
ATOM   1295  CB  ASP A 166      46.572  44.723  95.077  1.00 36.81           C  
ANISOU 1295  CB  ASP A 166     5453   4193   4340   -329    150   -715       C  
ATOM   1296  CG  ASP A 166      48.083  44.861  94.767  1.00 41.87           C  
ANISOU 1296  CG  ASP A 166     6002   4881   5023   -550    -69   -655       C  
ATOM   1297  OD1 ASP A 166      48.471  45.612  93.820  1.00 45.96           O  
ANISOU 1297  OD1 ASP A 166     6476   5211   5775   -665    -99   -592       O  
ATOM   1298  OD2 ASP A 166      48.886  44.246  95.520  1.00 47.44           O  
ANISOU 1298  OD2 ASP A 166     6678   5818   5526   -617   -217   -670       O  
ATOM   1299  N   PHE A 167      45.673  41.672  93.086  1.00 27.22           N  
ANISOU 1299  N   PHE A 167     3842   3280   3220    -98    287   -125       N  
ATOM   1300  CA  PHE A 167      45.928  40.249  93.022  1.00 28.12           C  
ANISOU 1300  CA  PHE A 167     3887   3557   3238    -73    264     30       C  
ATOM   1301  C   PHE A 167      46.200  39.787  91.573  1.00 26.41           C  
ANISOU 1301  C   PHE A 167     3536   3324   3174    -56    229    179       C  
ATOM   1302  O   PHE A 167      45.330  39.926  90.706  1.00 27.08           O  
ANISOU 1302  O   PHE A 167     3589   3314   3385     -1    287    218       O  
ATOM   1303  CB  PHE A 167      44.716  39.509  93.584  1.00 28.60           C  
ANISOU 1303  CB  PHE A 167     3985   3662   3219     -2    431     46       C  
ATOM   1304  CG  PHE A 167      44.825  38.020  93.497  1.00 29.67           C  
ANISOU 1304  CG  PHE A 167     4102   3881   3289     10    410    221       C  
ATOM   1305  CD1 PHE A 167      45.530  37.297  94.470  1.00 34.48           C  
ANISOU 1305  CD1 PHE A 167     4837   4594   3670     -9    317    286       C  
ATOM   1306  CD2 PHE A 167      44.197  37.329  92.454  1.00 28.26           C  
ANISOU 1306  CD2 PHE A 167     3812   3649   3276     48    450    318       C  
ATOM   1307  CE1 PHE A 167      45.635  35.862  94.396  1.00 35.16           C  
ANISOU 1307  CE1 PHE A 167     4951   4682   3726     27    276    469       C  
ATOM   1308  CE2 PHE A 167      44.291  35.944  92.339  1.00 29.59           C  
ANISOU 1308  CE2 PHE A 167     3999   3827   3416     54    424    453       C  
ATOM   1309  CZ  PHE A 167      45.026  35.190  93.334  1.00 33.30           C  
ANISOU 1309  CZ  PHE A 167     4610   4353   3687     53    345    539       C  
ATOM   1310  N   LYS A 168      47.369  39.231  91.305  1.00 25.86           N  
ANISOU 1310  N   LYS A 168     3381   3359   3085    -87    131    242       N  
ATOM   1311  CA  LYS A 168      47.624  38.620  89.990  1.00 24.69           C  
ANISOU 1311  CA  LYS A 168     3128   3227   3024    -53    150    344       C  
ATOM   1312  C   LYS A 168      47.581  37.099  90.069  1.00 23.45           C  
ANISOU 1312  C   LYS A 168     2958   3127   2823     56    138    414       C  
ATOM   1313  O   LYS A 168      47.908  36.552  91.107  1.00 24.10           O  
ANISOU 1313  O   LYS A 168     3083   3266   2805     88     64    427       O  
ATOM   1314  CB  LYS A 168      48.960  39.085  89.458  1.00 25.20           C  
ANISOU 1314  CB  LYS A 168     3067   3361   3145   -157    111    337       C  
ATOM   1315  CG  LYS A 168      48.945  40.572  89.357  1.00 26.70           C  
ANISOU 1315  CG  LYS A 168     3324   3421   3399   -304    121    293       C  
ATOM   1316  CD  LYS A 168      50.210  41.141  88.763  1.00 30.50           C  
ANISOU 1316  CD  LYS A 168     3674   3957   3957   -486    127    305       C  
ATOM   1317  CE  LYS A 168      50.366  42.566  89.279  1.00 32.21           C  
ANISOU 1317  CE  LYS A 168     3988   4010   4239   -670     74    219       C  
ATOM   1318  NZ  LYS A 168      50.525  43.304  88.033  1.00 41.35           N  
ANISOU 1318  NZ  LYS A 168     5188   5048   5474   -817    174    341       N  
ATOM   1319  N   SER A 169      47.189  36.420  88.976  1.00 21.85           N  
ANISOU 1319  N   SER A 169     2736   2887   2679    108    185    460       N  
ATOM   1320  CA  SER A 169      47.290  34.950  88.958  1.00 23.20           C  
ANISOU 1320  CA  SER A 169     2920   3049   2844    208    161    505       C  
ATOM   1321  C   SER A 169      47.689  34.443  87.612  1.00 23.05           C  
ANISOU 1321  C   SER A 169     2845   3036   2875    259    191    481       C  
ATOM   1322  O   SER A 169      47.380  35.035  86.580  1.00 22.77           O  
ANISOU 1322  O   SER A 169     2816   2998   2835    202    242    467       O  
ATOM   1323  CB  SER A 169      46.027  34.259  89.471  1.00 22.76           C  
ANISOU 1323  CB  SER A 169     2973   2900   2775    199    204    552       C  
ATOM   1324  OG  SER A 169      44.892  34.842  88.872  1.00 25.53           O  
ANISOU 1324  OG  SER A 169     3298   3206   3196    148    266    520       O  
ATOM   1325  N   ASN A 170      48.469  33.370  87.633  1.00 23.94           N  
ANISOU 1325  N   ASN A 170     2920   3156   3017    384    152    470       N  
ATOM   1326  CA  ASN A 170      48.829  32.684  86.392  1.00 23.21           C  
ANISOU 1326  CA  ASN A 170     2800   3060   2956    467    215    393       C  
ATOM   1327  C   ASN A 170      47.788  31.655  86.160  1.00 22.80           C  
ANISOU 1327  C   ASN A 170     2908   2833   2919    489    195    394       C  
ATOM   1328  O   ASN A 170      47.286  31.057  87.117  1.00 22.98           O  
ANISOU 1328  O   ASN A 170     3024   2740   2966    490    135    476       O  
ATOM   1329  CB  ASN A 170      50.159  31.947  86.551  1.00 24.91           C  
ANISOU 1329  CB  ASN A 170     2871   3334   3257    644    181    341       C  
ATOM   1330  CG  ASN A 170      51.317  32.866  86.648  1.00 25.34           C  
ANISOU 1330  CG  ASN A 170     2688   3593   3345    595    201    309       C  
ATOM   1331  OD1 ASN A 170      51.504  33.733  85.796  1.00 26.87           O  
ANISOU 1331  OD1 ASN A 170     2819   3889   3501    458    341    277       O  
ATOM   1332  ND2 ASN A 170      52.141  32.677  87.672  1.00 29.23           N  
ANISOU 1332  ND2 ASN A 170     3050   4147   3909    689     43    329       N  
ATOM   1333  N   SER A 171      47.465  31.411  84.895  1.00 23.99           N  
ANISOU 1333  N   SER A 171     3113   2962   3038    478    242    305       N  
ATOM   1334  CA  SER A 171      46.634  30.247  84.565  1.00 24.66           C  
ANISOU 1334  CA  SER A 171     3343   2861   3165    486    194    256       C  
ATOM   1335  C   SER A 171      46.899  29.677  83.172  1.00 25.87           C  
ANISOU 1335  C   SER A 171     3570   3005   3253    548    237     81       C  
ATOM   1336  O   SER A 171      47.493  30.330  82.276  1.00 25.12           O  
ANISOU 1336  O   SER A 171     3432   3084   3027    546    338     19       O  
ATOM   1337  CB  SER A 171      45.149  30.567  84.727  1.00 24.46           C  
ANISOU 1337  CB  SER A 171     3352   2781   3160    323    145    316       C  
ATOM   1338  OG  SER A 171      44.745  31.368  83.618  1.00 28.00           O  
ANISOU 1338  OG  SER A 171     3795   3324   3517    261    127    273       O  
ATOM   1339  N   ALA A 172      46.458  28.440  82.995  1.00 25.75           N  
ANISOU 1339  N   ALA A 172     3697   2775   3312    580    176     -5       N  
ATOM   1340  CA  ALA A 172      46.566  27.777  81.705  1.00 27.66           C  
ANISOU 1340  CA  ALA A 172     4068   2972   3469    633    203   -226       C  
ATOM   1341  C   ALA A 172      45.323  26.925  81.526  1.00 28.43           C  
ANISOU 1341  C   ALA A 172     4330   2835   3637    498     62   -281       C  
ATOM   1342  O   ALA A 172      44.777  26.414  82.504  1.00 26.43           O  
ANISOU 1342  O   ALA A 172     4094   2396   3552    430      0   -159       O  
ATOM   1343  CB  ALA A 172      47.836  26.869  81.665  1.00 29.72           C  
ANISOU 1343  CB  ALA A 172     4314   3159   3819    896    291   -371       C  
ATOM   1344  N   VAL A 173      44.860  26.819  80.276  1.00 29.73           N  
ANISOU 1344  N   VAL A 173     4619   3024   3650    426      9   -458       N  
ATOM   1345  CA  VAL A 173      43.566  26.188  80.012  1.00 30.30           C  
ANISOU 1345  CA  VAL A 173     4797   2918   3797    237   -174   -528       C  
ATOM   1346  C   VAL A 173      43.813  24.963  79.163  1.00 33.09           C  
ANISOU 1346  C   VAL A 173     5389   3062   4121    303   -199   -820       C  
ATOM   1347  O   VAL A 173      44.658  24.973  78.255  1.00 34.33           O  
ANISOU 1347  O   VAL A 173     5638   3335   4068    452    -82  -1009       O  
ATOM   1348  CB  VAL A 173      42.534  27.242  79.399  1.00 29.91           C  
ANISOU 1348  CB  VAL A 173     4671   3073   3616     69   -320   -472       C  
ATOM   1349  CG1 VAL A 173      41.258  26.607  78.931  1.00 31.40           C  
ANISOU 1349  CG1 VAL A 173     4911   3133   3886   -128   -552   -592       C  
ATOM   1350  CG2 VAL A 173      42.178  28.342  80.439  1.00 25.05           C  
ANISOU 1350  CG2 VAL A 173     3825   2578   3115     30   -287   -216       C  
ATOM   1351  N   ALA A 174      43.107  23.885  79.479  1.00 35.54           N  
ANISOU 1351  N   ALA A 174     5810   3047   4644    182   -320   -871       N  
ATOM   1352  CA  ALA A 174      43.146  22.669  78.637  1.00 39.43           C  
ANISOU 1352  CA  ALA A 174     6579   3264   5138    206   -387  -1194       C  
ATOM   1353  C   ALA A 174      41.747  22.108  78.385  1.00 41.34           C  
ANISOU 1353  C   ALA A 174     6895   3315   5497   -118   -628  -1279       C  
ATOM   1354  O   ALA A 174      40.846  22.261  79.209  1.00 40.94           O  
ANISOU 1354  O   ALA A 174     6672   3234   5648   -336   -689  -1060       O  
ATOM   1355  CB  ALA A 174      44.094  21.590  79.219  1.00 40.43           C  
ANISOU 1355  CB  ALA A 174     6832   3053   5474    452   -288  -1241       C  
ATOM   1356  N   TRP A 175      41.579  21.494  77.226  1.00 44.84           N  
ANISOU 1356  N   TRP A 175     7575   3659   5800   -162   -752  -1621       N  
ATOM   1357  CA  TRP A 175      40.313  20.892  76.860  1.00 48.66           C  
ANISOU 1357  CA  TRP A 175     8127   3959   6403   -493  -1027  -1764       C  
ATOM   1358  C   TRP A 175      40.508  19.804  75.831  1.00 54.41           C  
ANISOU 1358  C   TRP A 175     9225   4414   7031   -473  -1119  -2201       C  
ATOM   1359  O   TRP A 175      41.565  19.732  75.196  1.00 55.33           O  
ANISOU 1359  O   TRP A 175     9524   4593   6904   -186   -950  -2413       O  
ATOM   1360  CB  TRP A 175      39.340  21.946  76.311  1.00 47.29           C  
ANISOU 1360  CB  TRP A 175     7749   4155   6063   -678  -1240  -1699       C  
ATOM   1361  CG  TRP A 175      39.723  22.527  75.004  1.00 47.14           C  
ANISOU 1361  CG  TRP A 175     7897   4428   5585   -559  -1295  -1882       C  
ATOM   1362  CD1 TRP A 175      39.292  22.125  73.773  1.00 50.55           C  
ANISOU 1362  CD1 TRP A 175     8579   4862   5765   -678  -1548  -2210       C  
ATOM   1363  CD2 TRP A 175      40.604  23.628  74.779  1.00 44.21           C  
ANISOU 1363  CD2 TRP A 175     7490   4394   4914   -337  -1094  -1740       C  
ATOM   1364  NE1 TRP A 175      39.845  22.909  72.799  1.00 50.23           N  
ANISOU 1364  NE1 TRP A 175     8689   5155   5239   -534  -1500  -2257       N  
ATOM   1365  CE2 TRP A 175      40.647  23.846  73.385  1.00 48.14           C  
ANISOU 1365  CE2 TRP A 175     8244   5091   4956   -340  -1209  -1960       C  
ATOM   1366  CE3 TRP A 175      41.327  24.481  75.619  1.00 41.69           C  
ANISOU 1366  CE3 TRP A 175     6959   4228   4652   -174   -843  -1445       C  
ATOM   1367  CZ2 TRP A 175      41.417  24.863  72.805  1.00 47.49           C  
ANISOU 1367  CZ2 TRP A 175     8222   5340   4479   -197  -1034  -1862       C  
ATOM   1368  CZ3 TRP A 175      42.095  25.496  75.039  1.00 40.04           C  
ANISOU 1368  CZ3 TRP A 175     6778   4333   4101    -40   -693  -1378       C  
ATOM   1369  CH2 TRP A 175      42.137  25.667  73.652  1.00 42.70           C  
ANISOU 1369  CH2 TRP A 175     7379   4848   3994    -61   -768  -1568       C  
ATOM   1370  N   SER A 176      39.466  18.982  75.681  1.00 59.06           N  
ANISOU 1370  N   SER A 176     9905   4712   7821   -799  -1372  -2353       N  
ATOM   1371  CA  SER A 176      39.364  17.949  74.667  1.00 65.70           C  
ANISOU 1371  CA  SER A 176    11118   5264   8582   -874  -1542  -2817       C  
ATOM   1372  C   SER A 176      37.911  17.545  74.483  1.00 70.28           C  
ANISOU 1372  C   SER A 176    11633   5708   9359  -1347  -1902  -2908       C  
ATOM   1373  O   SER A 176      37.131  17.515  75.443  1.00 69.84           O  
ANISOU 1373  O   SER A 176    11305   5557   9672  -1609  -1926  -2625       O  
ATOM   1374  CB  SER A 176      40.190  16.715  75.036  1.00 68.06           C  
ANISOU 1374  CB  SER A 176    11715   5025   9118   -670  -1380  -2968       C  
ATOM   1375  OG  SER A 176      39.997  15.682  74.096  1.00 72.57           O  
ANISOU 1375  OG  SER A 176    12670   5252   9649   -765  -1554  -3456       O  
ATOM   1376  N   ASN A 177      37.561  17.239  73.237  1.00 76.19           N  
ANISOU 1376  N   ASN A 177    12626   6474   9848  -1468  -2175  -3322       N  
ATOM   1377  CA  ASN A 177      36.273  16.641  72.899  1.00 82.11           C  
ANISOU 1377  CA  ASN A 177    13358   7041  10797  -1931  -2575  -3523       C  
ATOM   1378  C   ASN A 177      36.222  15.178  73.354  1.00 87.44           C  
ANISOU 1378  C   ASN A 177    14295   7032  11894  -2113  -2557  -3687       C  
ATOM   1379  O   ASN A 177      36.625  14.256  72.629  1.00 91.68           O  
ANISOU 1379  O   ASN A 177    15283   7219  12332  -2051  -2614  -4131       O  
ATOM   1380  CB  ASN A 177      35.980  16.765  71.388  1.00 86.16           C  
ANISOU 1380  CB  ASN A 177    14111   7791  10834  -1996  -2922  -3939       C  
ATOM   1381  CG  ASN A 177      34.986  17.883  71.063  1.00 85.67           C  
ANISOU 1381  CG  ASN A 177    13675   8236  10639  -2166  -3257  -3751       C  
ATOM   1382  OD1 ASN A 177      35.115  19.012  71.530  1.00 83.28           O  
ANISOU 1382  OD1 ASN A 177    13060   8288  10291  -1989  -3106  -3360       O  
ATOM   1383  ND2 ASN A 177      33.993  17.564  70.256  1.00 91.38           N  
ANISOU 1383  ND2 ASN A 177    14433   8971  11316  -2497  -3745  -4045       N  
ATOM   1384  N   LYS A 178      35.770  15.001  74.595  1.00 87.44           N  
ANISOU 1384  N   LYS A 178    14038   6834  12351  -2322  -2444  -3313       N  
ATOM   1385  CA  LYS A 178      35.371  13.703  75.172  1.00 92.39           C  
ANISOU 1385  CA  LYS A 178    14850   6804  13447  -2650  -2472  -3346       C  
ATOM   1386  C   LYS A 178      36.227  12.465  74.845  1.00 97.28           C  
ANISOU 1386  C   LYS A 178    16052   6799  14109  -2447  -2421  -3696       C  
ATOM   1387  O   LYS A 178      35.718  11.322  74.871  1.00103.03           O  
ANISOU 1387  O   LYS A 178    17032   6937  15175  -2795  -2578  -3881       O  
ATOM   1388  CB  LYS A 178      33.891  13.436  74.856  1.00 96.79           C  
ANISOU 1388  CB  LYS A 178    15189   7341  14246  -3253  -2843  -3490       C  
ATOM   1389  CG  LYS A 178      32.910  14.458  75.431  1.00 93.68           C  
ANISOU 1389  CG  LYS A 178    14154   7447  13991  -3480  -2864  -3123       C  
ATOM   1390  CD  LYS A 178      31.611  14.524  74.614  1.00 97.91           C  
ANISOU 1390  CD  LYS A 178    14410   8187  14603  -3919  -3337  -3390       C  
ATOM   1391  CE  LYS A 178      30.764  13.266  74.769  1.00104.82           C  
ANISOU 1391  CE  LYS A 178    15344   8522  15959  -4510  -3506  -3567       C  
ATOM   1392  NZ  LYS A 178      30.533  12.922  76.201  1.00104.17           N  
ANISOU 1392  NZ  LYS A 178    15081   8169  16330  -4750  -3138  -3130       N  
ATOM   1393  N   SER A 179      37.513  12.658  74.554  1.00 95.97           N  
ANISOU 1393  N   SER A 179    16088   6726  13647  -1895  -2195  -3800       N  
ATOM   1394  CA  SER A 179      38.393  11.491  74.303  1.00101.40           C  
ANISOU 1394  CA  SER A 179    17288   6809  14428  -1614  -2113  -4148       C  
ATOM   1395  C   SER A 179      39.074  10.994  75.608  1.00100.84           C  
ANISOU 1395  C   SER A 179    17277   6302  14733  -1384  -1872  -3753       C  
ATOM   1396  O   SER A 179      40.054  11.615  76.074  1.00 96.28           O  
ANISOU 1396  O   SER A 179    16541   6010  14030   -939  -1617  -3506       O  
ATOM   1397  CB  SER A 179      39.406  11.766  73.167  1.00101.87           C  
ANISOU 1397  CB  SER A 179    17555   7153  13996  -1148  -1992  -4575       C  
ATOM   1398  OG  SER A 179      40.049  13.025  73.304  1.00 95.68           O  
ANISOU 1398  OG  SER A 179    16437   7011  12903   -836  -1753  -4283       O  
ATOM   1399  N   ASP A 180      38.533   9.904  76.192  1.00104.89           N  
ANISOU 1399  N   ASP A 180    18024   6135  15694  -1718  -1979  -3678       N  
ATOM   1400  CA  ASP A 180      38.912   9.395  77.544  1.00104.87           C  
ANISOU 1400  CA  ASP A 180    18119   5678  16048  -1625  -1820  -3202       C  
ATOM   1401  C   ASP A 180      39.540  10.462  78.501  1.00 98.35           C  
ANISOU 1401  C   ASP A 180    16921   5375  15070  -1303  -1569  -2685       C  
ATOM   1402  O   ASP A 180      40.561  10.201  79.154  1.00 98.17           O  
ANISOU 1402  O   ASP A 180    17037   5127  15135   -868  -1435  -2491       O  
ATOM   1403  CB  ASP A 180      39.831   8.161  77.425  1.00110.17           C  
ANISOU 1403  CB  ASP A 180    19335   5586  16938  -1242  -1817  -3472       C  
ATOM   1404  CG  ASP A 180      39.296   7.093  76.439  1.00117.62           C  
ANISOU 1404  CG  ASP A 180    20710   5961  18019  -1532  -2066  -4058       C  
ATOM   1405  OD1 ASP A 180      38.780   7.476  75.364  1.00117.68           O  
ANISOU 1405  OD1 ASP A 180    20627   6355  17731  -1733  -2216  -4463       O  
ATOM   1406  OD2 ASP A 180      39.412   5.868  76.727  1.00121.96           O  
ANISOU 1406  OD2 ASP A 180    21724   5654  18958  -1551  -2139  -4122       O  
ATOM   1407  N   PHE A 181      38.901  11.636  78.595  1.00 93.53           N  
ANISOU 1407  N   PHE A 181    15845   5432  14260  -1520  -1542  -2478       N  
ATOM   1408  CA  PHE A 181      39.529  12.883  79.107  1.00 87.37           C  
ANISOU 1408  CA  PHE A 181    14703   5263  13227  -1192  -1334  -2154       C  
ATOM   1409  C   PHE A 181      38.911  13.424  80.391  1.00 84.34           C  
ANISOU 1409  C   PHE A 181    14018   5069  12956  -1464  -1222  -1614       C  
ATOM   1410  O   PHE A 181      37.707  13.717  80.446  1.00 84.49           O  
ANISOU 1410  O   PHE A 181    13778   5269  13053  -1931  -1290  -1543       O  
ATOM   1411  CB  PHE A 181      39.500  13.979  78.020  1.00 84.19           C  
ANISOU 1411  CB  PHE A 181    14052   5514  12420  -1105  -1370  -2406       C  
ATOM   1412  CG  PHE A 181      39.970  15.356  78.480  1.00 79.47           C  
ANISOU 1412  CG  PHE A 181    13075   5531  11587   -868  -1182  -2084       C  
ATOM   1413  CD1 PHE A 181      41.313  15.694  78.428  1.00 77.22           C  
ANISOU 1413  CD1 PHE A 181    12803   5409  11124   -367   -994  -2104       C  
ATOM   1414  CD2 PHE A 181      39.055  16.315  78.912  1.00 76.94           C  
ANISOU 1414  CD2 PHE A 181    12368   5616  11247  -1153  -1198  -1803       C  
ATOM   1415  CE1 PHE A 181      41.753  16.948  78.809  1.00 74.95           C  
ANISOU 1415  CE1 PHE A 181    12187   5649  10640   -197   -841  -1840       C  
ATOM   1416  CE2 PHE A 181      39.482  17.596  79.314  1.00 75.23           C  
ANISOU 1416  CE2 PHE A 181    11847   5908  10827   -939  -1039  -1544       C  
ATOM   1417  CZ  PHE A 181      40.838  17.918  79.259  1.00 72.61           C  
ANISOU 1417  CZ  PHE A 181    11566   5709  10310   -484   -869  -1557       C  
ATOM   1418  N   ALA A 182      39.759  13.582  81.405  1.00 81.88           N  
ANISOU 1418  N   ALA A 182    13720   4750  12640  -1150  -1053  -1261       N  
ATOM   1419  CA  ALA A 182      39.361  14.157  82.686  1.00 79.23           C  
ANISOU 1419  CA  ALA A 182    13151   4633  12318  -1335   -905   -762       C  
ATOM   1420  C   ALA A 182      40.470  15.097  83.115  1.00 74.31           C  
ANISOU 1420  C   ALA A 182    12357   4425  11450   -862   -772   -591       C  
ATOM   1421  O   ALA A 182      41.575  15.028  82.576  1.00 74.31           O  
ANISOU 1421  O   ALA A 182    12453   4415  11364   -415   -781   -808       O  
ATOM   1422  CB  ALA A 182      39.129  13.055  83.733  1.00 83.60           C  
ANISOU 1422  CB  ALA A 182    14038   4571  13152  -1568   -883   -437       C  
ATOM   1423  N   CYS A 183      40.192  15.974  84.075  1.00 70.89           N  
ANISOU 1423  N   CYS A 183    11656   4360  10915   -967   -635   -234       N  
ATOM   1424  CA  CYS A 183      41.182  16.983  84.457  1.00 66.11           C  
ANISOU 1424  CA  CYS A 183    10861   4179  10077   -577   -536   -104       C  
ATOM   1425  C   CYS A 183      42.457  16.441  85.119  1.00 67.61           C  
ANISOU 1425  C   CYS A 183    11287   4097  10303   -161   -555     51       C  
ATOM   1426  O   CYS A 183      43.505  17.073  85.028  1.00 64.91           O  
ANISOU 1426  O   CYS A 183    10791   4053   9820    224   -526      3       O  
ATOM   1427  CB  CYS A 183      40.530  18.119  85.253  1.00 62.59           C  
ANISOU 1427  CB  CYS A 183    10084   4194   9502   -787   -397    167       C  
ATOM   1428  SG  CYS A 183      39.282  19.026  84.240  1.00 60.39           S  
ANISOU 1428  SG  CYS A 183     9422   4336   9186  -1088   -440    -74       S  
ATOM   1429  N   ALA A 184      42.375  15.252  85.730  1.00 72.67           N  
ANISOU 1429  N   ALA A 184    12300   4154  11156   -242   -624    231       N  
ATOM   1430  CA  ALA A 184      43.548  14.588  86.302  1.00 75.53           C  
ANISOU 1430  CA  ALA A 184    12924   4170  11602    191   -720    378       C  
ATOM   1431  C   ALA A 184      44.710  14.439  85.309  1.00 76.78           C  
ANISOU 1431  C   ALA A 184    13049   4318  11803    712   -776    -23       C  
ATOM   1432  O   ALA A 184      45.857  14.696  85.658  1.00 76.25           O  
ANISOU 1432  O   ALA A 184    12873   4397  11701   1151   -800     45       O  
ATOM   1433  CB  ALA A 184      43.169  13.234  86.873  1.00 81.43           C  
ANISOU 1433  CB  ALA A 184    14149   4189  12600      0   -818    598       C  
ATOM   1434  N   ASN A 185      44.404  14.025  84.080  1.00 79.38           N  
ANISOU 1434  N   ASN A 185    13460   4500  12201    648   -790   -459       N  
ATOM   1435  CA  ASN A 185      45.412  13.750  83.042  1.00 82.06           C  
ANISOU 1435  CA  ASN A 185    13817   4796  12562   1110   -782   -906       C  
ATOM   1436  C   ASN A 185      46.021  15.019  82.486  1.00 78.27           C  
ANISOU 1436  C   ASN A 185    12921   5023  11795   1303   -627  -1054       C  
ATOM   1437  O   ASN A 185      47.244  15.115  82.277  1.00 78.81           O  
ANISOU 1437  O   ASN A 185    12856   5219  11869   1772   -559  -1200       O  
ATOM   1438  CB  ASN A 185      44.786  12.979  81.868  1.00 85.44           C  
ANISOU 1438  CB  ASN A 185    14505   4888  13070    918   -838  -1361       C  
ATOM   1439  CG  ASN A 185      44.157  11.650  82.292  1.00 91.38           C  
ANISOU 1439  CG  ASN A 185    15708   4859  14152    668   -994  -1263       C  
ATOM   1440  OD1 ASN A 185      43.596  11.529  83.386  1.00 90.94           O  
ANISOU 1440  OD1 ASN A 185    15723   4642  14185    370  -1021   -803       O  
ATOM   1441  ND2 ASN A 185      44.241  10.650  81.412  1.00 95.96           N  
ANISOU 1441  ND2 ASN A 185    16622   4938  14900    764  -1077  -1707       N  
ATOM   1442  N   ALA A 186      45.140  15.993  82.272  1.00 74.84           N  
ANISOU 1442  N   ALA A 186    12267   5028  11138    928   -573  -1000       N  
ATOM   1443  CA  ALA A 186      45.403  17.131  81.423  1.00 72.22           C  
ANISOU 1443  CA  ALA A 186    11641   5282  10514    988   -447  -1190       C  
ATOM   1444  C   ALA A 186      46.784  17.754  81.552  1.00 71.62           C  
ANISOU 1444  C   ALA A 186    11313   5537  10361   1413   -314  -1176       C  
ATOM   1445  O   ALA A 186      47.440  17.993  80.530  1.00 72.85           O  
ANISOU 1445  O   ALA A 186    11385   5921  10372   1617   -179  -1503       O  
ATOM   1446  CB  ALA A 186      44.297  18.183  81.589  1.00 68.27           C  
ANISOU 1446  CB  ALA A 186    10920   5168   9852    578   -449   -991       C  
ATOM   1447  N   PHE A 187      47.239  18.013  82.779  1.00 71.02           N  
ANISOU 1447  N   PHE A 187    11114   5506  10362   1524   -347   -816       N  
ATOM   1448  CA  PHE A 187      48.416  18.877  82.953  1.00 70.43           C  
ANISOU 1448  CA  PHE A 187    10702   5855  10203   1821   -247   -780       C  
ATOM   1449  C   PHE A 187      49.715  18.198  83.365  1.00 75.84           C  
ANISOU 1449  C   PHE A 187    11354   6338  11123   2312   -307   -801       C  
ATOM   1450  O   PHE A 187      50.787  18.594  82.894  1.00 76.56           O  
ANISOU 1450  O   PHE A 187    11156   6730  11203   2607   -174  -1000       O  
ATOM   1451  CB  PHE A 187      48.112  20.055  83.883  1.00 65.12           C  
ANISOU 1451  CB  PHE A 187     9810   5554   9377   1601   -246   -428       C  
ATOM   1452  CG  PHE A 187      47.228  21.102  83.257  1.00 58.92           C  
ANISOU 1452  CG  PHE A 187     8902   5123   8361   1267   -153   -474       C  
ATOM   1453  CD1 PHE A 187      45.858  21.118  83.505  1.00 54.13           C  
ANISOU 1453  CD1 PHE A 187     8392   4428   7746    889   -212   -342       C  
ATOM   1454  CD2 PHE A 187      47.766  22.060  82.391  1.00 53.55           C  
ANISOU 1454  CD2 PHE A 187     8000   4855   7488   1332     -7   -642       C  
ATOM   1455  CE1 PHE A 187      45.039  22.096  82.911  1.00 49.85           C  
ANISOU 1455  CE1 PHE A 187     7705   4203   7031    639   -176   -387       C  
ATOM   1456  CE2 PHE A 187      46.961  22.998  81.794  1.00 47.23           C  
ANISOU 1456  CE2 PHE A 187     7138   4327   6479   1060     27   -652       C  
ATOM   1457  CZ  PHE A 187      45.599  23.023  82.055  1.00 45.56           C  
ANISOU 1457  CZ  PHE A 187     7003   4022   6286    742    -81   -529       C  
ATOM   1458  N   ASN A 188      49.605  17.197  84.239  1.00 80.81           N  
ANISOU 1458  N   ASN A 188    12266   6464  11974   2388   -507   -584       N  
ATOM   1459  CA  ASN A 188      50.742  16.451  84.788  1.00 87.41           C  
ANISOU 1459  CA  ASN A 188    13113   7021  13076   2884   -659   -535       C  
ATOM   1460  C   ASN A 188      52.101  16.537  84.085  1.00 91.36           C  
ANISOU 1460  C   ASN A 188    13271   7749  13691   3375   -538   -887       C  
ATOM   1461  O   ASN A 188      53.139  16.507  84.762  1.00 94.01           O  
ANISOU 1461  O   ASN A 188    13386   8134  14198   3751   -674   -763       O  
ATOM   1462  CB  ASN A 188      50.366  14.976  84.958  1.00 92.50           C  
ANISOU 1462  CB  ASN A 188    14249   6909  13988   2944   -832   -511       C  
ATOM   1463  CG  ASN A 188      50.250  14.564  86.412  1.00 93.66           C  
ANISOU 1463  CG  ASN A 188    14640   6743  14204   2915  -1082      7       C  
ATOM   1464  OD1 ASN A 188      50.391  13.382  86.737  1.00 97.51           O  
ANISOU 1464  OD1 ASN A 188    15497   6598  14954   3119  -1273     98       O  
ATOM   1465  ND2 ASN A 188      50.006  15.539  87.300  1.00 89.36           N  
ANISOU 1465  ND2 ASN A 188    13928   6618  13403   2666  -1082    351       N  
ATOM   1466  N   ASN A 189      52.096  16.613  82.746  1.00 93.70           N  
ANISOU 1466  N   ASN A 189    13521   8192  13890   3369   -290  -1326       N  
ATOM   1467  CA  ASN A 189      53.331  16.734  81.946  1.00 97.95           C  
ANISOU 1467  CA  ASN A 189    13714   9007  14494   3783    -68  -1707       C  
ATOM   1468  C   ASN A 189      54.238  17.930  82.305  1.00 96.72           C  
ANISOU 1468  C   ASN A 189    13015   9466  14266   3846     22  -1572       C  
ATOM   1469  O   ASN A 189      55.468  17.848  82.105  1.00100.30           O  
ANISOU 1469  O   ASN A 189    13106  10082  14921   4269    125  -1783       O  
ATOM   1470  CB  ASN A 189      53.021  16.755  80.444  1.00 98.56           C  
ANISOU 1470  CB  ASN A 189    13898   9208  14342   3661    217  -2170       C  
ATOM   1471  CG  ASN A 189      52.701  15.379  79.888  1.00104.00           C  
ANISOU 1471  CG  ASN A 189    15033   9274  15205   3808    159  -2502       C  
ATOM   1472  OD1 ASN A 189      51.650  14.806  80.176  1.00104.10           O  
ANISOU 1472  OD1 ASN A 189    15443   8850  15258   3518    -48  -2361       O  
ATOM   1473  ND2 ASN A 189      53.599  14.854  79.064  1.00108.94           N  
ANISOU 1473  ND2 ASN A 189    15588   9858  15944   4242    367  -2975       N  
ATOM   1474  N   SER A 190      53.631  19.020  82.811  1.00 92.55           N  
ANISOU 1474  N   SER A 190    12417   9264  13483   3428     -7  -1255       N  
ATOM   1475  CA  SER A 190      54.342  20.240  83.277  1.00 91.11           C  
ANISOU 1475  CA  SER A 190    11780   9615  13223   3389     34  -1093       C  
ATOM   1476  C   SER A 190      55.330  19.912  84.416  1.00 94.82           C  
ANISOU 1476  C   SER A 190    12037  10007  13982   3762   -242   -902       C  
ATOM   1477  O   SER A 190      54.906  19.575  85.530  1.00 95.05           O  
ANISOU 1477  O   SER A 190    12317   9762  14036   3714   -542   -557       O  
ATOM   1478  CB  SER A 190      53.327  21.329  83.688  1.00 85.83           C  
ANISOU 1478  CB  SER A 190    11182   9172  12254   2886     13   -802       C  
ATOM   1479  OG  SER A 190      52.773  21.121  84.981  1.00 84.15           O  
ANISOU 1479  OG  SER A 190    11176   8728  12067   2778   -259   -433       O  
ATOM   1480  N   ILE A 191      56.634  20.026  84.135  1.00 98.85           N  
ANISOU 1480  N   ILE A 191    12076  10783  14696   4119   -142  -1120       N  
ATOM   1481  CA  ILE A 191      57.687  19.204  84.814  1.00104.74           C  
ANISOU 1481  CA  ILE A 191    12632  11318  15844   4667   -419  -1102       C  
ATOM   1482  C   ILE A 191      57.893  19.344  86.365  1.00105.17           C  
ANISOU 1482  C   ILE A 191    12669  11343  15947   4706   -875   -656       C  
ATOM   1483  O   ILE A 191      58.548  20.281  86.841  1.00104.28           O  
ANISOU 1483  O   ILE A 191    12132  11681  15808   4647   -942   -566       O  
ATOM   1484  CB  ILE A 191      59.053  19.180  83.980  1.00109.52           C  
ANISOU 1484  CB  ILE A 191    12660  12229  16721   5088   -150  -1532       C  
ATOM   1485  CG1 ILE A 191      58.816  18.608  82.568  1.00110.97           C  
ANISOU 1485  CG1 ILE A 191    13039  12272  16851   5157    240  -1986       C  
ATOM   1486  CG2 ILE A 191      60.157  18.365  84.689  1.00115.26           C  
ANISOU 1486  CG2 ILE A 191    13111  12755  17926   5710   -484  -1523       C  
ATOM   1487  CD1 ILE A 191      59.827  19.043  81.513  1.00112.69           C  
ANISOU 1487  CD1 ILE A 191    12731  12981  17103   5307    704  -2408       C  
ATOM   1488  N   ILE A 192      57.305  18.393  87.112  1.00107.19           N  
ANISOU 1488  N   ILE A 192    13429  11051  16247   4774  -1182   -385       N  
ATOM   1489  CA  ILE A 192      57.507  18.154  88.583  1.00109.45           C  
ANISOU 1489  CA  ILE A 192    13853  11171  16561   4899  -1660     51       C  
ATOM   1490  C   ILE A 192      56.874  19.205  89.545  1.00104.56           C  
ANISOU 1490  C   ILE A 192    13330  10858  15539   4407  -1748    408       C  
ATOM   1491  O   ILE A 192      57.521  20.215  89.858  1.00103.45           O  
ANISOU 1491  O   ILE A 192    12762  11211  15332   4352  -1790    407       O  
ATOM   1492  CB  ILE A 192      59.032  17.827  88.972  1.00115.63           C  
ANISOU 1492  CB  ILE A 192    14163  12029  17740   5521  -1971     -7       C  
ATOM   1493  CG1 ILE A 192      59.702  16.854  87.971  1.00120.80           C  
ANISOU 1493  CG1 ILE A 192    14659  12414  18824   6056  -1820   -434       C  
ATOM   1494  CG2 ILE A 192      59.155  17.329  90.434  1.00118.97           C  
ANISOU 1494  CG2 ILE A 192    14879  12162  18163   5698  -2541    468       C  
ATOM   1495  CD1 ILE A 192      59.704  15.376  88.364  1.00126.51           C  
ANISOU 1495  CD1 ILE A 192    15834  12381  19852   6510  -2164   -309       C  
ATOM   1496  N   PRO A 193      55.621  18.954  90.031  1.00102.44           N  
ANISOU 1496  N   PRO A 193    13610  10290  15022   4044  -1763    690       N  
ATOM   1497  CA  PRO A 193      54.819  19.937  90.840  1.00 98.10           C  
ANISOU 1497  CA  PRO A 193    13186  10015  14069   3553  -1745    965       C  
ATOM   1498  C   PRO A 193      55.195  20.096  92.350  1.00 99.97           C  
ANISOU 1498  C   PRO A 193    13522  10324  14135   3604  -2143   1347       C  
ATOM   1499  O   PRO A 193      56.363  19.938  92.703  1.00103.86           O  
ANISOU 1499  O   PRO A 193    13746  10893  14820   4007  -2454   1349       O  
ATOM   1500  CB  PRO A 193      53.370  19.436  90.667  1.00 96.43           C  
ANISOU 1500  CB  PRO A 193    13468   9441  13727   3186  -1567   1064       C  
ATOM   1501  CG  PRO A 193      53.504  17.942  90.367  1.00101.28           C  
ANISOU 1501  CG  PRO A 193    14385   9440  14654   3512  -1692   1028       C  
ATOM   1502  CD  PRO A 193      54.859  17.716  89.735  1.00104.42           C  
ANISOU 1502  CD  PRO A 193    14371   9915  15386   4055  -1746    709       C  
ATOM   1503  N   GLU A 194      54.230  20.509  93.188  1.00 97.34           N  
ANISOU 1503  N   GLU A 194    13523  10031  13428   3190  -2118   1628       N  
ATOM   1504  CA  GLU A 194      54.193  20.197  94.645  1.00100.15           C  
ANISOU 1504  CA  GLU A 194    14267  10253  13533   3185  -2465   2061       C  
ATOM   1505  C   GLU A 194      52.835  20.537  95.281  1.00 97.60           C  
ANISOU 1505  C   GLU A 194    14342   9937  12802   2660  -2247   2293       C  
ATOM   1506  O   GLU A 194      52.164  19.637  95.790  1.00100.13           O  
ANISOU 1506  O   GLU A 194    15165   9845  13035   2551  -2281   2593       O  
ATOM   1507  CB  GLU A 194      55.373  20.772  95.475  1.00102.48           C  
ANISOU 1507  CB  GLU A 194    14270  10907  13760   3420  -2859   2125       C  
ATOM   1508  CG  GLU A 194      55.469  20.139  96.907  1.00106.54           C  
ANISOU 1508  CG  GLU A 194    15272  11190  14016   3524  -3314   2595       C  
ATOM   1509  CD  GLU A 194      56.832  20.319  97.627  1.00110.38           C  
ANISOU 1509  CD  GLU A 194    15471  11919  14549   3909  -3861   2654       C  
ATOM   1510  OE1 GLU A 194      57.905  20.073  97.014  1.00111.35           O  
ANISOU 1510  OE1 GLU A 194    15107  12072  15126   4352  -4016   2416       O  
ATOM   1511  OE2 GLU A 194      56.828  20.668  98.837  1.00110.86           O  
ANISOU 1511  OE2 GLU A 194    15794  12144  14182   3773  -4150   2932       O  
ATOM   1512  OXT GLU A 194      52.369  21.685  95.298  1.00 93.03           O  
ANISOU 1512  OXT GLU A 194    13593   9753  11997   2336  -2017   2184       O  
TER    1513      GLU A 194                                                      
ATOM   1514  N   ASN B   1      40.904  64.864  65.288  1.00 83.26           N  
ANISOU 1514  N   ASN B   1    11656   7944  12033   2119   4109  -1110       N  
ATOM   1515  CA  ASN B   1      40.349  63.937  66.325  1.00 83.95           C  
ANISOU 1515  CA  ASN B   1    11811   8227  11857   2051   4404  -1280       C  
ATOM   1516  C   ASN B   1      40.474  62.454  65.929  1.00 79.39           C  
ANISOU 1516  C   ASN B   1    11008   8133  11024   1887   4034  -1076       C  
ATOM   1517  O   ASN B   1      39.895  61.566  66.586  1.00 80.19           O  
ANISOU 1517  O   ASN B   1    11072   8421  10975   1843   4240  -1124       O  
ATOM   1518  CB  ASN B   1      38.891  64.295  66.643  1.00 88.53           C  
ANISOU 1518  CB  ASN B   1    12112   8610  12914   2376   4954  -1277       C  
ATOM   1519  CG  ASN B   1      38.501  63.953  68.083  1.00 92.54           C  
ANISOU 1519  CG  ASN B   1    12940   9102  13117   2290   5473  -1612       C  
ATOM   1520  OD1 ASN B   1      37.915  64.776  68.799  1.00 95.46           O  
ANISOU 1520  OD1 ASN B   1    13464   9119  13688   2457   6038  -1850       O  
ATOM   1521  ND2 ASN B   1      38.830  62.731  68.515  1.00 90.12           N  
ANISOU 1521  ND2 ASN B   1    12759   9164  12318   2025   5304  -1630       N  
ATOM   1522  N   ALA B   2      41.245  62.193  64.872  1.00 74.46           N  
ANISOU 1522  N   ALA B   2    10257   7684  10349   1786   3524   -860       N  
ATOM   1523  CA  ALA B   2      41.339  60.855  64.288  1.00 69.40           C  
ANISOU 1523  CA  ALA B   2     9374   7450   9541   1659   3175   -655       C  
ATOM   1524  C   ALA B   2      42.762  60.276  64.306  1.00 64.64           C  
ANISOU 1524  C   ALA B   2     9051   7024   8482   1364   2797   -724       C  
ATOM   1525  O   ALA B   2      42.944  59.115  64.699  1.00 63.03           O  
ANISOU 1525  O   ALA B   2     8895   7073   7978   1205   2705   -742       O  
ATOM   1526  CB  ALA B   2      40.759  60.850  62.848  1.00 68.89           C  
ANISOU 1526  CB  ALA B   2     8816   7486   9870   1822   2920   -291       C  
ATOM   1527  N   GLY B   3      43.748  61.081  63.883  1.00 62.04           N  
ANISOU 1527  N   GLY B   3     8883   6546   8142   1296   2592   -743       N  
ATOM   1528  CA  GLY B   3      45.137  60.635  63.759  1.00 56.81           C  
ANISOU 1528  CA  GLY B   3     8399   6036   7147   1036   2227   -773       C  
ATOM   1529  C   GLY B   3      45.339  59.752  62.513  1.00 51.97           C  
ANISOU 1529  C   GLY B   3     7466   5713   6567   1008   1879   -501       C  
ATOM   1530  O   GLY B   3      44.706  59.971  61.473  1.00 51.75           O  
ANISOU 1530  O   GLY B   3     7138   5696   6828   1162   1828   -273       O  
ATOM   1531  N   VAL B   4      46.226  58.767  62.623  1.00 47.22           N  
ANISOU 1531  N   VAL B   4     6942   5331   5667    808   1641   -523       N  
ATOM   1532  CA  VAL B   4      46.408  57.781  61.570  1.00 42.73           C  
ANISOU 1532  CA  VAL B   4     6120   5023   5093    766   1375   -324       C  
ATOM   1533  C   VAL B   4      45.344  56.669  61.665  1.00 41.09           C  
ANISOU 1533  C   VAL B   4     5710   5003   4895    818   1461   -249       C  
ATOM   1534  O   VAL B   4      45.252  55.981  62.667  1.00 40.55           O  
ANISOU 1534  O   VAL B   4     5783   4993   4630    746   1571   -361       O  
ATOM   1535  CB  VAL B   4      47.849  57.203  61.558  1.00 40.80           C  
ANISOU 1535  CB  VAL B   4     6001   4895   4605    556   1105   -367       C  
ATOM   1536  CG1 VAL B   4      48.089  56.440  60.270  1.00 36.36           C  
ANISOU 1536  CG1 VAL B   4     5197   4533   4083    530    889   -182       C  
ATOM   1537  CG2 VAL B   4      48.910  58.317  61.721  1.00 41.66           C  
ANISOU 1537  CG2 VAL B   4     6319   4804   4706    458   1042   -474       C  
ATOM   1538  N   THR B   5      44.544  56.527  60.614  1.00 40.15           N  
ANISOU 1538  N   THR B   5     5273   4977   5004    921   1397    -45       N  
ATOM   1539  CA  THR B   5      43.510  55.494  60.499  1.00 41.03           C  
ANISOU 1539  CA  THR B   5     5137   5272   5180    940   1433     49       C  
ATOM   1540  C   THR B   5      43.788  54.537  59.308  1.00 38.67           C  
ANISOU 1540  C   THR B   5     4675   5199   4816    825   1124    192       C  
ATOM   1541  O   THR B   5      44.220  54.976  58.237  1.00 39.24           O  
ANISOU 1541  O   THR B   5     4700   5282   4925    820    931    304       O  
ATOM   1542  CB  THR B   5      42.125  56.134  60.254  1.00 44.09           C  
ANISOU 1542  CB  THR B   5     5231   5578   5941   1150   1609    179       C  
ATOM   1543  OG1 THR B   5      42.202  56.955  59.091  1.00 45.18           O  
ANISOU 1543  OG1 THR B   5     5238   5662   6263   1234   1416    362       O  
ATOM   1544  CG2 THR B   5      41.682  57.017  61.445  1.00 47.61           C  
ANISOU 1544  CG2 THR B   5     5825   5772   6490   1286   2008     10       C  
ATOM   1545  N   GLN B   6      43.573  53.241  59.479  1.00 36.43           N  
ANISOU 1545  N   GLN B   6     4341   5078   4422    718   1097    182       N  
ATOM   1546  CA  GLN B   6      43.729  52.300  58.354  1.00 35.63           C  
ANISOU 1546  CA  GLN B   6     4110   5160   4265    600    848    280       C  
ATOM   1547  C   GLN B   6      42.443  51.509  58.148  1.00 37.20           C  
ANISOU 1547  C   GLN B   6     4040   5488   4607    582    868    374       C  
ATOM   1548  O   GLN B   6      41.782  51.146  59.098  1.00 37.75           O  
ANISOU 1548  O   GLN B   6     4083   5538   4720    597   1083    327       O  
ATOM   1549  CB  GLN B   6      44.866  51.307  58.587  1.00 32.61           C  
ANISOU 1549  CB  GLN B   6     3922   4829   3639    451    753    176       C  
ATOM   1550  CG  GLN B   6      46.162  51.982  58.923  1.00 31.70           C  
ANISOU 1550  CG  GLN B   6     4031   4602   3410    438    716     85       C  
ATOM   1551  CD  GLN B   6      47.308  51.041  59.066  1.00 30.64           C  
ANISOU 1551  CD  GLN B   6     4016   4514   3109    318    596     24       C  
ATOM   1552  OE1 GLN B   6      48.182  51.285  59.861  1.00 32.23           O  
ANISOU 1552  OE1 GLN B   6     4394   4639   3211    287    582    -58       O  
ATOM   1553  NE2 GLN B   6      47.317  49.964  58.297  1.00 25.73           N  
ANISOU 1553  NE2 GLN B   6     3296   4004   2474    245    502     64       N  
ATOM   1554  N   THR B   7      42.105  51.256  56.903  1.00 37.28           N  
ANISOU 1554  N   THR B   7     3862   5629   4672    526    645    508       N  
ATOM   1555  CA  THR B   7      40.861  50.579  56.583  1.00 41.01           C  
ANISOU 1555  CA  THR B   7     4042   6232   5306    475    604    611       C  
ATOM   1556  C   THR B   7      41.331  49.618  55.515  1.00 39.16           C  
ANISOU 1556  C   THR B   7     3858   6142   4878    273    345    607       C  
ATOM   1557  O   THR B   7      42.131  50.010  54.669  1.00 37.99           O  
ANISOU 1557  O   THR B   7     3833   6006   4595    250    191    625       O  
ATOM   1558  CB  THR B   7      39.837  51.558  55.932  1.00 43.76           C  
ANISOU 1558  CB  THR B   7     4082   6588   5956    619    527    822       C  
ATOM   1559  OG1 THR B   7      39.753  52.771  56.696  1.00 47.50           O  
ANISOU 1559  OG1 THR B   7     4587   6857   6602    841    771    807       O  
ATOM   1560  CG2 THR B   7      38.450  50.925  55.822  1.00 49.17           C  
ANISOU 1560  CG2 THR B   7     4396   7402   6883    572    505    937       C  
ATOM   1561  N   PRO B   8      40.902  48.348  55.584  1.00 38.86           N  
ANISOU 1561  N   PRO B   8     3758   6189   4817    114    334    564       N  
ATOM   1562  CA  PRO B   8      40.192  47.692  56.677  1.00 38.44           C  
ANISOU 1562  CA  PRO B   8     3627   6106   4869     96    556    526       C  
ATOM   1563  C   PRO B   8      41.171  47.247  57.801  1.00 35.81           C  
ANISOU 1563  C   PRO B   8     3613   5657   4336     91    730    377       C  
ATOM   1564  O   PRO B   8      42.375  47.213  57.594  1.00 34.60           O  
ANISOU 1564  O   PRO B   8     3681   5465   3998     73    636    303       O  
ATOM   1565  CB  PRO B   8      39.600  46.480  55.980  1.00 39.50           C  
ANISOU 1565  CB  PRO B   8     3620   6368   5019   -125    395    546       C  
ATOM   1566  CG  PRO B   8      40.665  46.116  54.973  1.00 38.49           C  
ANISOU 1566  CG  PRO B   8     3713   6270   4640   -239    185    470       C  
ATOM   1567  CD  PRO B   8      41.151  47.421  54.462  1.00 38.05           C  
ANISOU 1567  CD  PRO B   8     3696   6205   4555    -93    103    540       C  
ATOM   1568  N   LYS B   9      40.671  46.952  58.986  1.00 36.00           N  
ANISOU 1568  N   LYS B   9     3652   5626   4398    103    981    352       N  
ATOM   1569  CA  LYS B   9      41.514  46.417  60.068  1.00 34.89           C  
ANISOU 1569  CA  LYS B   9     3824   5395   4038     67   1097    256       C  
ATOM   1570  C   LYS B   9      42.011  45.004  59.794  1.00 32.19           C  
ANISOU 1570  C   LYS B   9     3577   5062   3591    -99    970    234       C  
ATOM   1571  O   LYS B   9      43.057  44.617  60.281  1.00 29.70           O  
ANISOU 1571  O   LYS B   9     3507   4672   3106   -111    943    184       O  
ATOM   1572  CB  LYS B   9      40.690  46.349  61.366  1.00 36.88           C  
ANISOU 1572  CB  LYS B   9     4085   5600   4325     86   1422    257       C  
ATOM   1573  CG  LYS B   9      40.356  47.660  61.989  1.00 42.81           C  
ANISOU 1573  CG  LYS B   9     4844   6274   5145    260   1648    224       C  
ATOM   1574  CD  LYS B   9      39.179  47.469  62.995  1.00 52.10           C  
ANISOU 1574  CD  LYS B   9     5926   7434   6434    261   2027    239       C  
ATOM   1575  CE  LYS B   9      39.302  48.436  64.182  1.00 57.01           C  
ANISOU 1575  CE  LYS B   9     6807   7925   6929    377   2341    118       C  
ATOM   1576  NZ  LYS B   9      38.011  48.536  64.934  1.00 61.71           N  
ANISOU 1576  NZ  LYS B   9     7238   8494   7715    424   2776    128       N  
ATOM   1577  N   PHE B  10      41.201  44.227  59.071  1.00 32.97           N  
ANISOU 1577  N   PHE B  10     3471   5238   3819   -233    897    277       N  
ATOM   1578  CA  PHE B  10      41.443  42.810  58.773  1.00 33.46           C  
ANISOU 1578  CA  PHE B  10     3610   5269   3832   -413    817    241       C  
ATOM   1579  C   PHE B  10      40.970  42.466  57.347  1.00 33.73           C  
ANISOU 1579  C   PHE B  10     3464   5409   3942   -557    602    237       C  
ATOM   1580  O   PHE B  10      39.987  43.006  56.892  1.00 33.39           O  
ANISOU 1580  O   PHE B  10     3157   5480   4049   -559    544    319       O  
ATOM   1581  CB  PHE B  10      40.636  41.911  59.740  1.00 35.39           C  
ANISOU 1581  CB  PHE B  10     3832   5463   4148   -519   1025    289       C  
ATOM   1582  CG  PHE B  10      41.067  41.994  61.198  1.00 38.07           C  
ANISOU 1582  CG  PHE B  10     4421   5705   4338   -439   1233    302       C  
ATOM   1583  CD1 PHE B  10      42.016  41.117  61.705  1.00 37.95           C  
ANISOU 1583  CD1 PHE B  10     4677   5571   4168   -483   1198    300       C  
ATOM   1584  CD2 PHE B  10      40.541  42.951  62.039  1.00 38.66           C  
ANISOU 1584  CD2 PHE B  10     4472   5795   4421   -324   1456    319       C  
ATOM   1585  CE1 PHE B  10      42.412  41.174  63.030  1.00 38.63           C  
ANISOU 1585  CE1 PHE B  10     5017   5588   4071   -440   1330    340       C  
ATOM   1586  CE2 PHE B  10      40.941  43.022  63.382  1.00 43.08           C  
ANISOU 1586  CE2 PHE B  10     5324   6276   4769   -292   1639    313       C  
ATOM   1587  CZ  PHE B  10      41.875  42.120  63.876  1.00 40.68           C  
ANISOU 1587  CZ  PHE B  10     5300   5885   4271   -364   1549    337       C  
ATOM   1588  N   GLN B  11      41.633  41.537  56.658  1.00 33.81           N  
ANISOU 1588  N   GLN B  11     3619   5373   3854   -686    486    143       N  
ATOM   1589  CA  GLN B  11      41.129  41.101  55.333  1.00 35.81           C  
ANISOU 1589  CA  GLN B  11     3763   5725   4118   -880    287    107       C  
ATOM   1590  C   GLN B  11      41.619  39.706  55.019  1.00 36.28           C  
ANISOU 1590  C   GLN B  11     4013   5654   4116  -1054    285    -27       C  
ATOM   1591  O   GLN B  11      42.810  39.400  55.241  1.00 35.40           O  
ANISOU 1591  O   GLN B  11     4127   5405   3919   -969    353   -101       O  
ATOM   1592  CB  GLN B  11      41.596  42.098  54.234  1.00 36.56           C  
ANISOU 1592  CB  GLN B  11     3868   5929   4091   -815    107    111       C  
ATOM   1593  CG  GLN B  11      41.089  41.866  52.798  1.00 40.16           C  
ANISOU 1593  CG  GLN B  11     4257   6525   4476  -1026   -139     95       C  
ATOM   1594  CD  GLN B  11      39.599  42.120  52.674  1.00 47.12           C  
ANISOU 1594  CD  GLN B  11     4795   7552   5554  -1102   -267    247       C  
ATOM   1595  OE1 GLN B  11      39.164  43.262  52.806  1.00 51.39           O  
ANISOU 1595  OE1 GLN B  11     5142   8166   6217   -930   -290    404       O  
ATOM   1596  NE2 GLN B  11      38.799  41.048  52.457  1.00 47.65           N  
ANISOU 1596  NE2 GLN B  11     4764   7641   5698  -1359   -340    207       N  
ATOM   1597  N   VAL B  12      40.725  38.842  54.558  1.00 37.90           N  
ANISOU 1597  N   VAL B  12     4118   5879   4401  -1297    214    -55       N  
ATOM   1598  CA  VAL B  12      41.150  37.672  53.804  1.00 39.92           C  
ANISOU 1598  CA  VAL B  12     4571   6016   4580  -1497    169   -228       C  
ATOM   1599  C   VAL B  12      41.126  37.928  52.290  1.00 41.04           C  
ANISOU 1599  C   VAL B  12     4736   6305   4551  -1642    -59   -320       C  
ATOM   1600  O   VAL B  12      40.209  38.562  51.781  1.00 42.53           O  
ANISOU 1600  O   VAL B  12     4703   6699   4757  -1714   -252   -216       O  
ATOM   1601  CB  VAL B  12      40.223  36.414  53.983  1.00 42.86           C  
ANISOU 1601  CB  VAL B  12     4885   6291   5106  -1765    201   -255       C  
ATOM   1602  CG1 VAL B  12      40.892  35.356  54.775  1.00 42.77           C  
ANISOU 1602  CG1 VAL B  12     5100   6002   5147  -1743    401   -298       C  
ATOM   1603  CG2 VAL B  12      38.811  36.769  54.427  1.00 43.78           C  
ANISOU 1603  CG2 VAL B  12     4653   6558   5421  -1831    186    -89       C  
ATOM   1604  N   LEU B  13      42.090  37.363  51.577  1.00 41.86           N  
ANISOU 1604  N   LEU B  13     5109   6296   4497  -1699    -30   -508       N  
ATOM   1605  CA  LEU B  13      42.159  37.434  50.120  1.00 44.22           C  
ANISOU 1605  CA  LEU B  13     5526   6713   4560  -1882   -201   -633       C  
ATOM   1606  C   LEU B  13      42.463  36.043  49.631  1.00 46.27           C  
ANISOU 1606  C   LEU B  13     6039   6768   4773  -2104   -113   -884       C  
ATOM   1607  O   LEU B  13      43.217  35.326  50.285  1.00 46.08           O  
ANISOU 1607  O   LEU B  13     6145   6489   4873  -1992    112   -954       O  
ATOM   1608  CB  LEU B  13      43.312  38.344  49.727  1.00 43.42           C  
ANISOU 1608  CB  LEU B  13     5554   6650   4292  -1682   -151   -638       C  
ATOM   1609  CG  LEU B  13      43.117  39.855  49.883  1.00 43.40           C  
ANISOU 1609  CG  LEU B  13     5364   6833   4293  -1489   -256   -417       C  
ATOM   1610  CD1 LEU B  13      44.445  40.578  49.673  1.00 42.66           C  
ANISOU 1610  CD1 LEU B  13     5421   6706   4079  -1305   -146   -441       C  
ATOM   1611  CD2 LEU B  13      42.051  40.377  48.876  1.00 47.65           C  
ANISOU 1611  CD2 LEU B  13     5764   7615   4722  -1668   -559   -310       C  
ATOM   1612  N   LYS B  14      41.868  35.620  48.517  1.00 49.95           N  
ANISOU 1612  N   LYS B  14     6585   7322   5071  -2427   -296  -1017       N  
ATOM   1613  CA  LYS B  14      42.344  34.406  47.865  1.00 51.32           C  
ANISOU 1613  CA  LYS B  14     7081   7273   5144  -2638   -174  -1318       C  
ATOM   1614  C   LYS B  14      43.570  34.798  47.053  1.00 50.25           C  
ANISOU 1614  C   LYS B  14     7201   7133   4757  -2530    -48  -1457       C  
ATOM   1615  O   LYS B  14      43.663  35.911  46.599  1.00 49.42           O  
ANISOU 1615  O   LYS B  14     7042   7261   4473  -2452   -175  -1335       O  
ATOM   1616  CB  LYS B  14      41.257  33.670  47.056  1.00 55.80           C  
ANISOU 1616  CB  LYS B  14     7685   7900   5615  -3076   -403  -1451       C  
ATOM   1617  CG  LYS B  14      40.948  34.179  45.672  1.00 58.47           C  
ANISOU 1617  CG  LYS B  14     8127   8509   5578  -3318   -692  -1508       C  
ATOM   1618  CD  LYS B  14      40.030  33.199  44.916  1.00 65.78           C  
ANISOU 1618  CD  LYS B  14     9160   9434   6398  -3803   -909  -1702       C  
ATOM   1619  CE  LYS B  14      39.724  33.690  43.496  1.00 68.70           C  
ANISOU 1619  CE  LYS B  14     9683  10098   6322  -4086  -1250  -1747       C  
ATOM   1620  NZ  LYS B  14      39.125  32.626  42.647  1.00 75.12           N  
ANISOU 1620  NZ  LYS B  14    10733  10865   6942  -4595  -1426  -2026       N  
ATOM   1621  N   THR B  15      44.543  33.907  46.939  1.00 50.80           N  
ANISOU 1621  N   THR B  15     7528   6913   4858  -2500    234  -1690       N  
ATOM   1622  CA  THR B  15      45.725  34.163  46.116  1.00 51.45           C  
ANISOU 1622  CA  THR B  15     7844   6968   4734  -2419    422  -1851       C  
ATOM   1623  C   THR B  15      45.355  34.664  44.707  1.00 53.61           C  
ANISOU 1623  C   THR B  15     8288   7510   4571  -2693    225  -1936       C  
ATOM   1624  O   THR B  15      44.572  34.014  44.004  1.00 55.91           O  
ANISOU 1624  O   THR B  15     8728   7829   4684  -3051     69  -2097       O  
ATOM   1625  CB  THR B  15      46.553  32.871  45.950  1.00 54.64           C  
ANISOU 1625  CB  THR B  15     8518   6992   5250  -2438    759  -2151       C  
ATOM   1626  OG1 THR B  15      47.076  32.467  47.225  1.00 53.67           O  
ANISOU 1626  OG1 THR B  15     8252   6616   5522  -2151    924  -2026       O  
ATOM   1627  CG2 THR B  15      47.706  33.071  44.930  1.00 55.77           C  
ANISOU 1627  CG2 THR B  15     8911   7109   5169  -2399   1010  -2360       C  
ATOM   1628  N   GLY B  16      45.935  35.802  44.319  1.00 51.75           N  
ANISOU 1628  N   GLY B  16     8045   7460   4156  -2545    223  -1817       N  
ATOM   1629  CA  GLY B  16      45.691  36.409  43.021  1.00 55.19           C  
ANISOU 1629  CA  GLY B  16     8663   8158   4147  -2777     36  -1833       C  
ATOM   1630  C   GLY B  16      44.707  37.568  42.955  1.00 55.10           C  
ANISOU 1630  C   GLY B  16     8403   8477   4055  -2794   -370  -1502       C  
ATOM   1631  O   GLY B  16      44.547  38.184  41.889  1.00 56.93           O  
ANISOU 1631  O   GLY B  16     8784   8936   3909  -2964   -560  -1449       O  
ATOM   1632  N   GLN B  17      44.034  37.858  44.070  1.00 53.50           N  
ANISOU 1632  N   GLN B  17     7834   8290   4202  -2623   -492  -1269       N  
ATOM   1633  CA  GLN B  17      43.119  38.991  44.129  1.00 54.03           C  
ANISOU 1633  CA  GLN B  17     7612   8620   4295  -2574   -824   -942       C  
ATOM   1634  C   GLN B  17      43.891  40.248  44.436  1.00 51.48           C  
ANISOU 1634  C   GLN B  17     7215   8329   4014  -2251   -717   -753       C  
ATOM   1635  O   GLN B  17      44.909  40.209  45.109  1.00 48.82           O  
ANISOU 1635  O   GLN B  17     6907   7809   3833  -2021   -419   -819       O  
ATOM   1636  CB  GLN B  17      42.028  38.793  45.166  1.00 53.12           C  
ANISOU 1636  CB  GLN B  17     7135   8498   4547  -2536   -943   -792       C  
ATOM   1637  CG  GLN B  17      40.826  37.973  44.650  1.00 57.77           C  
ANISOU 1637  CG  GLN B  17     7681   9176   5093  -2922  -1224   -857       C  
ATOM   1638  CD  GLN B  17      39.817  37.663  45.771  1.00 59.23           C  
ANISOU 1638  CD  GLN B  17     7489   9319   5696  -2887  -1252   -721       C  
ATOM   1639  OE1 GLN B  17      40.159  37.712  46.974  1.00 52.59           O  
ANISOU 1639  OE1 GLN B  17     6533   8319   5129  -2607   -987   -661       O  
ATOM   1640  NE2 GLN B  17      38.571  37.348  45.383  1.00 60.31           N  
ANISOU 1640  NE2 GLN B  17     7433   9606   5873  -3190  -1573   -664       N  
ATOM   1641  N   SER B  18      43.418  41.367  43.917  1.00 53.03           N  
ANISOU 1641  N   SER B  18     7316   8750   4084  -2247   -979   -504       N  
ATOM   1642  CA  SER B  18      44.034  42.627  44.254  1.00 51.87           C  
ANISOU 1642  CA  SER B  18     7084   8607   4017  -1956   -893   -306       C  
ATOM   1643  C   SER B  18      43.297  43.220  45.462  1.00 49.98           C  
ANISOU 1643  C   SER B  18     6464   8353   4170  -1718   -957    -83       C  
ATOM   1644  O   SER B  18      42.153  42.867  45.751  1.00 50.43           O  
ANISOU 1644  O   SER B  18     6296   8471   4392  -1805  -1131    -15       O  
ATOM   1645  CB  SER B  18      43.982  43.576  43.064  1.00 54.21           C  
ANISOU 1645  CB  SER B  18     7509   9107   3979  -2058  -1109   -133       C  
ATOM   1646  OG  SER B  18      42.638  43.900  42.773  1.00 57.32           O  
ANISOU 1646  OG  SER B  18     7688   9697   4393  -2172  -1517    100       O  
ATOM   1647  N   MET B  19      43.972  44.120  46.163  1.00 48.05           N  
ANISOU 1647  N   MET B  19     6156   8020   4079  -1435   -791     15       N  
ATOM   1648  CA  MET B  19      43.327  44.859  47.227  1.00 47.39           C  
ANISOU 1648  CA  MET B  19     5772   7915   4319  -1209   -813    210       C  
ATOM   1649  C   MET B  19      44.018  46.175  47.506  1.00 45.58           C  
ANISOU 1649  C   MET B  19     5543   7629   4145   -969   -720    344       C  
ATOM   1650  O   MET B  19      45.209  46.356  47.225  1.00 44.73           O  
ANISOU 1650  O   MET B  19     5640   7455   3898   -944   -567    257       O  
ATOM   1651  CB  MET B  19      43.211  44.003  48.497  1.00 46.38           C  
ANISOU 1651  CB  MET B  19     5548   7637   4435  -1142   -625     93       C  
ATOM   1652  CG  MET B  19      44.200  44.281  49.543  1.00 46.12           C  
ANISOU 1652  CG  MET B  19     5567   7437   4521   -913   -376     49       C  
ATOM   1653  SD  MET B  19      43.284  44.341  51.070  1.00 59.43           S  
ANISOU 1653  SD  MET B  19     7002   9060   6516   -766   -291    144       S  
ATOM   1654  CE  MET B  19      41.677  44.932  50.446  1.00 54.10           C  
ANISOU 1654  CE  MET B  19     6022   8581   5949   -834   -559    364       C  
ATOM   1655  N   THR B  20      43.263  47.102  48.065  1.00 45.25           N  
ANISOU 1655  N   THR B  20     5258   7593   4339   -796   -792    552       N  
ATOM   1656  CA  THR B  20      43.835  48.368  48.397  1.00 45.29           C  
ANISOU 1656  CA  THR B  20     5273   7503   4428   -581   -699    666       C  
ATOM   1657  C   THR B  20      43.711  48.644  49.911  1.00 42.59           C  
ANISOU 1657  C   THR B  20     4793   7010   4377   -364   -504    644       C  
ATOM   1658  O   THR B  20      42.630  48.519  50.466  1.00 44.33           O  
ANISOU 1658  O   THR B  20     4790   7250   4804   -321   -523    708       O  
ATOM   1659  CB  THR B  20      43.278  49.456  47.459  1.00 47.26           C  
ANISOU 1659  CB  THR B  20     5457   7859   4641   -570   -942    944       C  
ATOM   1660  OG1 THR B  20      43.826  50.724  47.810  1.00 48.71           O  
ANISOU 1660  OG1 THR B  20     5662   7902   4941   -364   -831   1054       O  
ATOM   1661  CG2 THR B  20      41.763  49.508  47.534  1.00 53.46           C  
ANISOU 1661  CG2 THR B  20     5917   8743   5652   -555  -1158   1130       C  
ATOM   1662  N   LEU B  21      44.833  48.918  50.581  1.00 39.72           N  
ANISOU 1662  N   LEU B  21     4572   6503   4014   -259   -309    537       N  
ATOM   1663  CA  LEU B  21      44.812  49.242  52.026  1.00 38.59           C  
ANISOU 1663  CA  LEU B  21     4374   6220   4067    -87   -134    501       C  
ATOM   1664  C   LEU B  21      44.767  50.747  52.143  1.00 39.00           C  
ANISOU 1664  C   LEU B  21     4390   6184   4243     79   -120    640       C  
ATOM   1665  O   LEU B  21      45.653  51.410  51.626  1.00 37.95           O  
ANISOU 1665  O   LEU B  21     4389   6009   4019     77   -132    665       O  
ATOM   1666  CB  LEU B  21      46.076  48.738  52.717  1.00 36.74           C  
ANISOU 1666  CB  LEU B  21     4316   5877   3763    -86     13    325       C  
ATOM   1667  CG  LEU B  21      46.399  47.241  52.748  1.00 37.64           C  
ANISOU 1667  CG  LEU B  21     4503   5998   3800   -212     48    178       C  
ATOM   1668  CD1 LEU B  21      47.488  47.039  53.734  1.00 37.13           C  
ANISOU 1668  CD1 LEU B  21     4545   5803   3757   -143    167     83       C  
ATOM   1669  CD2 LEU B  21      45.153  46.404  53.150  1.00 41.61           C  
ANISOU 1669  CD2 LEU B  21     4873   6544   4391   -273     37    188       C  
ATOM   1670  N   GLN B  22      43.718  51.290  52.752  1.00 40.11           N  
ANISOU 1670  N   GLN B  22     4345   6281   4614    218    -76    736       N  
ATOM   1671  CA  GLN B  22      43.606  52.751  52.902  1.00 41.58           C  
ANISOU 1671  CA  GLN B  22     4501   6327   4971    400    -30    862       C  
ATOM   1672  C   GLN B  22      44.418  53.226  54.099  1.00 40.25           C  
ANISOU 1672  C   GLN B  22     4509   5968   4817    487    189    700       C  
ATOM   1673  O   GLN B  22      44.560  52.499  55.079  1.00 38.38           O  
ANISOU 1673  O   GLN B  22     4334   5718   4530    459    315    543       O  
ATOM   1674  CB  GLN B  22      42.163  53.178  53.091  1.00 44.85           C  
ANISOU 1674  CB  GLN B  22     4623   6734   5681    541    -28   1023       C  
ATOM   1675  CG  GLN B  22      41.184  52.716  51.999  1.00 49.08           C  
ANISOU 1675  CG  GLN B  22     4926   7477   6242    438   -304   1211       C  
ATOM   1676  CD  GLN B  22      41.570  53.128  50.582  1.00 53.16           C  
ANISOU 1676  CD  GLN B  22     5543   8086   6570    343   -571   1379       C  
ATOM   1677  OE1 GLN B  22      42.282  54.122  50.349  1.00 53.45           O  
ANISOU 1677  OE1 GLN B  22     5734   7998   6576    421   -543   1445       O  
ATOM   1678  NE2 GLN B  22      41.091  52.353  49.617  1.00 56.97           N  
ANISOU 1678  NE2 GLN B  22     5958   8783   6903    146   -830   1448       N  
ATOM   1679  N   CYS B  23      44.982  54.426  53.992  1.00 40.46           N  
ANISOU 1679  N   CYS B  23     4637   5844   4890    564    213    746       N  
ATOM   1680  CA  CYS B  23      45.687  55.047  55.089  1.00 39.40           C  
ANISOU 1680  CA  CYS B  23     4679   5516   4776    620    387    594       C  
ATOM   1681  C   CYS B  23      45.400  56.536  55.048  1.00 41.23           C  
ANISOU 1681  C   CYS B  23     4906   5537   5222    774    452    704       C  
ATOM   1682  O   CYS B  23      45.610  57.175  54.029  1.00 42.00           O  
ANISOU 1682  O   CYS B  23     4999   5616   5340    769    327    875       O  
ATOM   1683  CB  CYS B  23      47.210  54.799  55.023  1.00 37.76           C  
ANISOU 1683  CB  CYS B  23     4662   5309   4375    478    345    475       C  
ATOM   1684  SG  CYS B  23      47.974  55.772  56.395  1.00 38.43           S  
ANISOU 1684  SG  CYS B  23     4957   5146   4496    514    495    304       S  
ATOM   1685  N   ALA B  24      44.903  57.072  56.162  1.00 42.12           N  
ANISOU 1685  N   ALA B  24     5041   5473   5490    908    670    606       N  
ATOM   1686  CA  ALA B  24      44.471  58.453  56.257  1.00 44.44           C  
ANISOU 1686  CA  ALA B  24     5324   5510   6052   1089    792    685       C  
ATOM   1687  C   ALA B  24      45.020  59.110  57.532  1.00 45.95           C  
ANISOU 1687  C   ALA B  24     5781   5455   6221   1099   1025    435       C  
ATOM   1688  O   ALA B  24      45.117  58.508  58.636  1.00 44.41           O  
ANISOU 1688  O   ALA B  24     5711   5292   5868   1037   1156    225       O  
ATOM   1689  CB  ALA B  24      42.979  58.561  56.221  1.00 47.17           C  
ANISOU 1689  CB  ALA B  24     5374   5852   6694   1279    868    836       C  
ATOM   1690  N   GLN B  25      45.357  60.372  57.364  1.00 47.11           N  
ANISOU 1690  N   GLN B  25     6040   5344   6516   1160   1067    470       N  
ATOM   1691  CA  GLN B  25      46.235  61.037  58.274  1.00 47.83           C  
ANISOU 1691  CA  GLN B  25     6434   5210   6527   1079   1191    233       C  
ATOM   1692  C   GLN B  25      45.666  62.422  58.384  1.00 51.49           C  
ANISOU 1692  C   GLN B  25     6927   5317   7316   1273   1391    270       C  
ATOM   1693  O   GLN B  25      45.643  63.208  57.438  1.00 52.67           O  
ANISOU 1693  O   GLN B  25     7004   5342   7665   1347   1301    498       O  
ATOM   1694  CB  GLN B  25      47.656  60.984  57.687  1.00 46.92           C  
ANISOU 1694  CB  GLN B  25     6433   5164   6229    863    973    243       C  
ATOM   1695  CG  GLN B  25      48.711  61.735  58.419  1.00 46.38           C  
ANISOU 1695  CG  GLN B  25     6641   4876   6103    727   1019     38       C  
ATOM   1696  CD  GLN B  25      48.826  63.135  57.920  1.00 43.13           C  
ANISOU 1696  CD  GLN B  25     6297   4157   5933    780   1070    140       C  
ATOM   1697  OE1 GLN B  25      48.609  64.069  58.661  1.00 40.47           O  
ANISOU 1697  OE1 GLN B  25     6132   3509   5733    845   1266     -2       O  
ATOM   1698  NE2 GLN B  25      49.197  63.285  56.661  1.00 39.83           N  
ANISOU 1698  NE2 GLN B  25     5774   3804   5553    739    912    384       N  
ATOM   1699  N   ASP B  26      45.183  62.664  59.585  1.00 53.68           N  
ANISOU 1699  N   ASP B  26     7332   5425   7637   1353   1687     44       N  
ATOM   1700  CA  ASP B  26      44.442  63.821  59.985  1.00 58.82           C  
ANISOU 1700  CA  ASP B  26     8016   5709   8623   1574   1989      6       C  
ATOM   1701  C   ASP B  26      45.275  65.075  60.186  1.00 59.89           C  
ANISOU 1701  C   ASP B  26     8464   5475   8814   1508   2054   -124       C  
ATOM   1702  O   ASP B  26      44.768  66.183  60.130  1.00 63.73           O  
ANISOU 1702  O   ASP B  26     8957   5604   9651   1704   2253    -77       O  
ATOM   1703  CB  ASP B  26      43.815  63.469  61.349  1.00 60.91           C  
ANISOU 1703  CB  ASP B  26     8390   5947   8803   1615   2332   -267       C  
ATOM   1704  CG  ASP B  26      42.422  63.917  61.457  1.00 65.22           C  
ANISOU 1704  CG  ASP B  26     8694   6319   9766   1921   2647   -186       C  
ATOM   1705  OD1 ASP B  26      41.852  64.284  60.412  1.00 69.35           O  
ANISOU 1705  OD1 ASP B  26     8897   6812  10639   2105   2520    132       O  
ATOM   1706  OD2 ASP B  26      41.885  63.897  62.576  1.00 71.90           O  
ANISOU 1706  OD2 ASP B  26     9661   7061  10593   1976   3023   -424       O  
ATOM   1707  N   MET B  27      46.546  64.880  60.484  1.00 57.40           N  
ANISOU 1707  N   MET B  27     8399   5230   8179   1226   1894   -294       N  
ATOM   1708  CA  MET B  27      47.296  65.871  61.261  1.00 59.05           C  
ANISOU 1708  CA  MET B  27     8984   5101   8351   1090   2016   -566       C  
ATOM   1709  C   MET B  27      48.121  66.763  60.333  1.00 57.87           C  
ANISOU 1709  C   MET B  27     8862   4767   8357   1003   1847   -405       C  
ATOM   1710  O   MET B  27      48.943  67.546  60.790  1.00 58.54           O  
ANISOU 1710  O   MET B  27     9235   4593   8414    825   1873   -601       O  
ATOM   1711  CB  MET B  27      48.187  65.136  62.294  1.00 58.01           C  
ANISOU 1711  CB  MET B  27     9104   5155   7780    806   1917   -849       C  
ATOM   1712  CG  MET B  27      47.526  63.879  62.931  1.00 59.96           C  
ANISOU 1712  CG  MET B  27     9272   5705   7805    844   1985   -901       C  
ATOM   1713  SD  MET B  27      48.638  62.552  63.541  1.00 64.43           S  
ANISOU 1713  SD  MET B  27     9959   6634   7887    537   1683  -1007       S  
ATOM   1714  CE  MET B  27      49.113  63.262  65.130  1.00 65.33           C  
ANISOU 1714  CE  MET B  27    10597   6495   7728    336   1837  -1409       C  
ATOM   1715  N   ASN B  28      47.891  66.608  59.027  1.00 55.53           N  
ANISOU 1715  N   ASN B  28     8279   4616   8201   1102   1668    -43       N  
ATOM   1716  CA  ASN B  28      48.611  67.343  57.970  1.00 55.52           C  
ANISOU 1716  CA  ASN B  28     8285   4488   8320   1016   1511    181       C  
ATOM   1717  C   ASN B  28      50.087  67.046  57.904  1.00 51.96           C  
ANISOU 1717  C   ASN B  28     7950   4182   7609    683   1310     84       C  
ATOM   1718  O   ASN B  28      50.875  67.927  57.580  1.00 53.85           O  
ANISOU 1718  O   ASN B  28     8318   4190   7953    543   1285    119       O  
ATOM   1719  CB  ASN B  28      48.445  68.852  58.137  1.00 60.28           C  
ANISOU 1719  CB  ASN B  28     9074   4561   9267   1121   1726    160       C  
ATOM   1720  CG  ASN B  28      47.022  69.292  58.005  1.00 64.88           C  
ANISOU 1720  CG  ASN B  28     9479   4949  10222   1490   1924    330       C  
ATOM   1721  OD1 ASN B  28      46.414  69.720  58.983  1.00 68.80           O  
ANISOU 1721  OD1 ASN B  28    10094   5174  10870   1634   2240     91       O  
ATOM   1722  ND2 ASN B  28      46.470  69.191  56.788  1.00 66.73           N  
ANISOU 1722  ND2 ASN B  28     9421   5320  10611   1644   1743    750       N  
ATOM   1723  N   HIS B  29      50.454  65.823  58.244  1.00 47.44           N  
ANISOU 1723  N   HIS B  29     7318   3969   6738    559   1182    -28       N  
ATOM   1724  CA  HIS B  29      51.843  65.384  58.237  1.00 45.22           C  
ANISOU 1724  CA  HIS B  29     7076   3853   6250    269    986   -109       C  
ATOM   1725  C   HIS B  29      52.377  65.236  56.795  1.00 43.73           C  
ANISOU 1725  C   HIS B  29     6707   3821   6084    205    837    182       C  
ATOM   1726  O   HIS B  29      51.643  64.742  55.925  1.00 41.83           O  
ANISOU 1726  O   HIS B  29     6283   3768   5843    352    799    410       O  
ATOM   1727  CB  HIS B  29      51.946  64.075  59.012  1.00 41.63           C  
ANISOU 1727  CB  HIS B  29     6593   3710   5513    207    903   -272       C  
ATOM   1728  CG  HIS B  29      51.911  64.259  60.494  1.00 46.16           C  
ANISOU 1728  CG  HIS B  29     7434   4143   5959    143   1009   -586       C  
ATOM   1729  ND1 HIS B  29      52.182  63.235  61.378  1.00 46.02           N  
ANISOU 1729  ND1 HIS B  29     7470   4355   5657     37    914   -737       N  
ATOM   1730  CD2 HIS B  29      51.674  65.365  61.255  1.00 46.95           C  
ANISOU 1730  CD2 HIS B  29     7803   3881   6153    151   1208   -784       C  
ATOM   1731  CE1 HIS B  29      52.091  63.702  62.615  1.00 49.20           C  
ANISOU 1731  CE1 HIS B  29     8180   4572   5941    -31   1038  -1006       C  
ATOM   1732  NE2 HIS B  29      51.793  64.992  62.563  1.00 47.32           N  
ANISOU 1732  NE2 HIS B  29     8083   3968   5926     31   1232  -1063       N  
ATOM   1733  N   GLU B  30      53.625  65.648  56.542  1.00 43.84           N  
ANISOU 1733  N   GLU B  30     6777   3769   6111    -32    762    173       N  
ATOM   1734  CA  GLU B  30      54.140  65.627  55.147  1.00 44.74           C  
ANISOU 1734  CA  GLU B  30     6758   3999   6240   -108    693    450       C  
ATOM   1735  C   GLU B  30      54.619  64.258  54.715  1.00 41.22           C  
ANISOU 1735  C   GLU B  30     6130   3953   5578   -183    578    467       C  
ATOM   1736  O   GLU B  30      54.427  63.872  53.572  1.00 39.77           O  
ANISOU 1736  O   GLU B  30     5838   3947   5326   -148    556    685       O  
ATOM   1737  CB  GLU B  30      55.250  66.675  54.883  1.00 46.84           C  
ANISOU 1737  CB  GLU B  30     7125   4014   6655   -336    712    477       C  
ATOM   1738  CG  GLU B  30      54.855  68.166  55.041  1.00 53.09           C  
ANISOU 1738  CG  GLU B  30     8120   4337   7714   -276    848    509       C  
ATOM   1739  CD  GLU B  30      53.636  68.601  54.220  1.00 58.96           C  
ANISOU 1739  CD  GLU B  30     8826   4975   8599      3    914    816       C  
ATOM   1740  OE1 GLU B  30      52.777  69.310  54.793  1.00 62.77           O  
ANISOU 1740  OE1 GLU B  30     9414   5152   9283    198   1046    758       O  
ATOM   1741  OE2 GLU B  30      53.528  68.267  53.012  1.00 60.06           O  
ANISOU 1741  OE2 GLU B  30     8838   5324   8658     29    836   1117       O  
ATOM   1742  N   TYR B  31      55.237  63.543  55.658  1.00 40.97           N  
ANISOU 1742  N   TYR B  31     6088   4042   5434   -292    504    235       N  
ATOM   1743  CA  TYR B  31      55.870  62.244  55.446  1.00 40.17           C  
ANISOU 1743  CA  TYR B  31     5817   4258   5187   -366    406    218       C  
ATOM   1744  C   TYR B  31      54.988  61.048  55.864  1.00 38.59           C  
ANISOU 1744  C   TYR B  31     5560   4274   4827   -212    379    160       C  
ATOM   1745  O   TYR B  31      54.527  60.959  57.011  1.00 38.76           O  
ANISOU 1745  O   TYR B  31     5687   4243   4796   -159    385     -1       O  
ATOM   1746  CB  TYR B  31      57.176  62.233  56.232  1.00 41.33           C  
ANISOU 1746  CB  TYR B  31     5959   4381   5363   -588    301     47       C  
ATOM   1747  CG  TYR B  31      58.091  61.038  56.026  1.00 43.58           C  
ANISOU 1747  CG  TYR B  31     6030   4929   5597   -670    210     45       C  
ATOM   1748  CD1 TYR B  31      59.231  61.126  55.198  1.00 48.84           C  
ANISOU 1748  CD1 TYR B  31     6536   5631   6389   -827    239    138       C  
ATOM   1749  CD2 TYR B  31      57.863  59.848  56.705  1.00 43.53           C  
ANISOU 1749  CD2 TYR B  31     5979   5107   5453   -593    120    -45       C  
ATOM   1750  CE1 TYR B  31      60.099  60.026  55.044  1.00 51.18           C  
ANISOU 1750  CE1 TYR B  31     6606   6136   6703   -875    196    127       C  
ATOM   1751  CE2 TYR B  31      58.703  58.765  56.563  1.00 48.08           C  
ANISOU 1751  CE2 TYR B  31     6356   5874   6038   -642     47    -39       C  
ATOM   1752  CZ  TYR B  31      59.820  58.845  55.731  1.00 52.41           C  
ANISOU 1752  CZ  TYR B  31     6721   6449   6743   -769     91     39       C  
ATOM   1753  OH  TYR B  31      60.626  57.710  55.610  1.00 57.27           O  
ANISOU 1753  OH  TYR B  31     7110   7229   7419   -779     56     39       O  
ATOM   1754  N   MET B  32      54.757  60.114  54.944  1.00 37.05           N  
ANISOU 1754  N   MET B  32     5224   4314   4538   -163    366    282       N  
ATOM   1755  CA  MET B  32      54.001  58.905  55.279  1.00 35.69           C  
ANISOU 1755  CA  MET B  32     4989   4336   4236    -56    338    230       C  
ATOM   1756  C   MET B  32      54.764  57.709  54.788  1.00 34.05           C  
ANISOU 1756  C   MET B  32     4652   4342   3940   -139    291    223       C  
ATOM   1757  O   MET B  32      55.471  57.798  53.782  1.00 35.93           O  
ANISOU 1757  O   MET B  32     4833   4621   4196   -230    326    312       O  
ATOM   1758  CB  MET B  32      52.571  58.930  54.720  1.00 35.47           C  
ANISOU 1758  CB  MET B  32     4921   4345   4209    111    375    374       C  
ATOM   1759  CG  MET B  32      51.737  60.028  55.356  1.00 37.18           C  
ANISOU 1759  CG  MET B  32     5232   4318   4576    243    466    366       C  
ATOM   1760  SD  MET B  32      50.124  60.240  54.621  1.00 38.48           S  
ANISOU 1760  SD  MET B  32     5269   4499   4852    457    483    596       S  
ATOM   1761  CE  MET B  32      49.334  58.770  55.261  1.00 33.64           C  
ANISOU 1761  CE  MET B  32     4541   4122   4115    506    481    481       C  
ATOM   1762  N   SER B  33      54.670  56.621  55.530  1.00 32.65           N  
ANISOU 1762  N   SER B  33     4445   4276   3684   -111    241    116       N  
ATOM   1763  CA  SER B  33      55.354  55.355  55.188  1.00 32.57           C  
ANISOU 1763  CA  SER B  33     4310   4427   3634   -157    215     95       C  
ATOM   1764  C   SER B  33      54.421  54.183  55.323  1.00 30.28           C  
ANISOU 1764  C   SER B  33     4002   4263   3238    -67    212     76       C  
ATOM   1765  O   SER B  33      53.492  54.246  56.098  1.00 30.00           O  
ANISOU 1765  O   SER B  33     4035   4198   3165      9    213     48       O  
ATOM   1766  CB  SER B  33      56.443  55.065  56.188  1.00 32.58           C  
ANISOU 1766  CB  SER B  33     4280   4402   3696   -236    111     -5       C  
ATOM   1767  OG  SER B  33      57.494  55.930  56.027  1.00 39.91           O  
ANISOU 1767  OG  SER B  33     5169   5236   4756   -360     96      3       O  
ATOM   1768  N   TRP B  34      54.725  53.092  54.632  1.00 29.28           N  
ANISOU 1768  N   TRP B  34     3789   4256   3078    -90    236     75       N  
ATOM   1769  CA  TRP B  34      54.034  51.847  54.844  1.00 27.71           C  
ANISOU 1769  CA  TRP B  34     3575   4145   2806    -41    228     38       C  
ATOM   1770  C   TRP B  34      55.110  50.817  55.213  1.00 27.94           C  
ANISOU 1770  C   TRP B  34     3532   4176   2906    -65    205    -25       C  
ATOM   1771  O   TRP B  34      56.191  50.818  54.610  1.00 30.27           O  
ANISOU 1771  O   TRP B  34     3738   4466   3297   -117    254    -27       O  
ATOM   1772  CB  TRP B  34      53.339  51.423  53.583  1.00 27.87           C  
ANISOU 1772  CB  TRP B  34     3581   4276   2732    -58    275     89       C  
ATOM   1773  CG  TRP B  34      51.949  51.874  53.426  1.00 28.75           C  
ANISOU 1773  CG  TRP B  34     3706   4419   2799     -4    243    176       C  
ATOM   1774  CD1 TRP B  34      51.492  52.877  52.605  1.00 30.46           C  
ANISOU 1774  CD1 TRP B  34     3934   4635   3004      1    224    311       C  
ATOM   1775  CD2 TRP B  34      50.771  51.298  54.049  1.00 29.47           C  
ANISOU 1775  CD2 TRP B  34     3766   4545   2884     53    224    165       C  
ATOM   1776  NE1 TRP B  34      50.107  52.994  52.721  1.00 29.49           N  
ANISOU 1776  NE1 TRP B  34     3756   4541   2905     82    176    390       N  
ATOM   1777  CE2 TRP B  34      49.647  52.036  53.590  1.00 27.24           C  
ANISOU 1777  CE2 TRP B  34     3437   4285   2628    106    193    291       C  
ATOM   1778  CE3 TRP B  34      50.567  50.265  54.979  1.00 27.06           C  
ANISOU 1778  CE3 TRP B  34     3462   4243   2575     64    237     84       C  
ATOM   1779  CZ2 TRP B  34      48.348  51.757  54.017  1.00 29.69           C  
ANISOU 1779  CZ2 TRP B  34     3657   4631   2991    168    193    322       C  
ATOM   1780  CZ3 TRP B  34      49.265  49.987  55.402  1.00 27.59           C  
ANISOU 1780  CZ3 TRP B  34     3482   4343   2654    105    256    110       C  
ATOM   1781  CH2 TRP B  34      48.171  50.722  54.924  1.00 26.57           C  
ANISOU 1781  CH2 TRP B  34     3265   4248   2583    157    242    220       C  
ATOM   1782  N   TYR B  35      54.825  49.994  56.213  1.00 26.16           N  
ANISOU 1782  N   TYR B  35     3335   3946   2658    -24    144    -56       N  
ATOM   1783  CA  TYR B  35      55.706  48.908  56.671  1.00 27.43           C  
ANISOU 1783  CA  TYR B  35     3424   4085   2912    -16     91    -73       C  
ATOM   1784  C   TYR B  35      54.934  47.564  56.689  1.00 27.02           C  
ANISOU 1784  C   TYR B  35     3398   4055   2811     21    134    -84       C  
ATOM   1785  O   TYR B  35      53.699  47.561  56.860  1.00 26.43           O  
ANISOU 1785  O   TYR B  35     3402   4017   2622     29    159    -78       O  
ATOM   1786  CB  TYR B  35      56.144  49.151  58.115  1.00 27.36           C  
ANISOU 1786  CB  TYR B  35     3472   4023   2898    -28    -73    -63       C  
ATOM   1787  CG  TYR B  35      57.003  50.393  58.363  1.00 29.64           C  
ANISOU 1787  CG  TYR B  35     3749   4262   3250   -106   -161    -72       C  
ATOM   1788  CD1 TYR B  35      56.415  51.596  58.712  1.00 27.97           C  
ANISOU 1788  CD1 TYR B  35     3687   4001   2938   -134   -148   -107       C  
ATOM   1789  CD2 TYR B  35      58.408  50.353  58.237  1.00 25.37           C  
ANISOU 1789  CD2 TYR B  35     3028   3702   2908   -157   -241    -47       C  
ATOM   1790  CE1 TYR B  35      57.205  52.718  58.984  1.00 29.49           C  
ANISOU 1790  CE1 TYR B  35     3896   4112   3196   -236   -229   -135       C  
ATOM   1791  CE2 TYR B  35      59.180  51.459  58.462  1.00 24.66           C  
ANISOU 1791  CE2 TYR B  35     2911   3562   2896   -266   -333    -56       C  
ATOM   1792  CZ  TYR B  35      58.574  52.631  58.838  1.00 28.79           C  
ANISOU 1792  CZ  TYR B  35     3627   4023   3286   -317   -333   -107       C  
ATOM   1793  OH  TYR B  35      59.303  53.756  59.086  1.00 33.59           O  
ANISOU 1793  OH  TYR B  35     4242   4546   3973   -451   -420   -136       O  
ATOM   1794  N   ARG B  36      55.643  46.443  56.542  1.00 26.69           N  
ANISOU 1794  N   ARG B  36     3277   3969   2893     44    155    -96       N  
ATOM   1795  CA  ARG B  36      55.091  45.167  56.994  1.00 27.69           C  
ANISOU 1795  CA  ARG B  36     3455   4055   3010     73    157    -88       C  
ATOM   1796  C   ARG B  36      55.837  44.648  58.161  1.00 28.00           C  
ANISOU 1796  C   ARG B  36     3480   4014   3144    119     15     -9       C  
ATOM   1797  O   ARG B  36      56.997  44.916  58.333  1.00 29.23           O  
ANISOU 1797  O   ARG B  36     3520   4140   3445    135    -74     25       O  
ATOM   1798  CB  ARG B  36      55.051  44.074  55.917  1.00 29.13           C  
ANISOU 1798  CB  ARG B  36     3608   4203   3255     63    308   -164       C  
ATOM   1799  CG  ARG B  36      56.303  43.965  55.032  1.00 30.89           C  
ANISOU 1799  CG  ARG B  36     3708   4380   3649     80    425   -218       C  
ATOM   1800  CD  ARG B  36      56.102  42.821  54.000  1.00 32.25           C  
ANISOU 1800  CD  ARG B  36     3925   4494   3833     52    618   -341       C  
ATOM   1801  NE  ARG B  36      55.927  41.483  54.600  1.00 35.79           N  
ANISOU 1801  NE  ARG B  36     4403   4798   4397    104    613   -335       N  
ATOM   1802  CZ  ARG B  36      55.417  40.417  53.950  1.00 37.89           C  
ANISOU 1802  CZ  ARG B  36     4765   4982   4648     50    751   -452       C  
ATOM   1803  NH1 ARG B  36      55.013  40.543  52.692  1.00 36.62           N  
ANISOU 1803  NH1 ARG B  36     4693   4902   4317    -70    878   -589       N  
ATOM   1804  NH2 ARG B  36      55.299  39.224  54.547  1.00 30.21           N  
ANISOU 1804  NH2 ARG B  36     3826   3836   3813     95    752   -427       N  
ATOM   1805  N   GLN B  37      55.152  43.861  58.961  1.00 29.44           N  
ANISOU 1805  N   GLN B  37     3772   4162   3252    128    -15     41       N  
ATOM   1806  CA  GLN B  37      55.760  43.252  60.120  1.00 31.10           C  
ANISOU 1806  CA  GLN B  37     4010   4294   3511    163   -179    163       C  
ATOM   1807  C   GLN B  37      55.359  41.808  60.126  1.00 32.54           C  
ANISOU 1807  C   GLN B  37     4228   4368   3767    195   -105    203       C  
ATOM   1808  O   GLN B  37      54.189  41.481  60.091  1.00 31.83           O  
ANISOU 1808  O   GLN B  37     4244   4296   3554    144      2    174       O  
ATOM   1809  CB  GLN B  37      55.345  43.947  61.435  1.00 29.52           C  
ANISOU 1809  CB  GLN B  37     3996   4148   3072    108   -307    214       C  
ATOM   1810  CG  GLN B  37      55.742  43.147  62.692  1.00 32.09           C  
ANISOU 1810  CG  GLN B  37     4423   4409   3360    113   -495    375       C  
ATOM   1811  CD  GLN B  37      55.341  43.841  63.981  1.00 31.45           C  
ANISOU 1811  CD  GLN B  37     4590   4388   2969     24   -593    398       C  
ATOM   1812  OE1 GLN B  37      54.182  44.212  64.169  1.00 30.84           O  
ANISOU 1812  OE1 GLN B  37     4658   4355   2704    -12   -418    325       O  
ATOM   1813  NE2 GLN B  37      56.310  44.060  64.854  1.00 34.89           N  
ANISOU 1813  NE2 GLN B  37     5070   4827   3358    -19   -868    492       N  
ATOM   1814  N   ASP B  38      56.362  40.957  60.199  1.00 35.77           N  
ANISOU 1814  N   ASP B  38     4528   4645   4415    278   -166    283       N  
ATOM   1815  CA  ASP B  38      56.176  39.529  60.137  1.00 39.53           C  
ANISOU 1815  CA  ASP B  38     5032   4953   5033    325    -82    324       C  
ATOM   1816  C   ASP B  38      56.730  38.866  61.373  1.00 43.24           C  
ANISOU 1816  C   ASP B  38     5536   5311   5580    389   -295    552       C  
ATOM   1817  O   ASP B  38      57.800  39.279  61.874  1.00 44.46           O  
ANISOU 1817  O   ASP B  38     5573   5486   5832    436   -512    662       O  
ATOM   1818  CB  ASP B  38      56.888  38.999  58.885  1.00 39.98           C  
ANISOU 1818  CB  ASP B  38     4924   4897   5368    395    101    204       C  
ATOM   1819  CG  ASP B  38      56.288  39.559  57.664  1.00 39.14           C  
ANISOU 1819  CG  ASP B  38     4840   4908   5121    302    286      6       C  
ATOM   1820  OD1 ASP B  38      55.166  39.137  57.369  1.00 40.68           O  
ANISOU 1820  OD1 ASP B  38     5166   5111   5179    213    378    -65       O  
ATOM   1821  OD2 ASP B  38      56.874  40.463  57.043  1.00 37.22           O  
ANISOU 1821  OD2 ASP B  38     4491   4759   4890    296    319    -56       O  
ATOM   1822  N   PRO B  39      56.052  37.797  61.834  1.00 45.92           N  
ANISOU 1822  N   PRO B  39     6026   5525   5897    377   -252    643       N  
ATOM   1823  CA  PRO B  39      56.428  37.179  63.119  1.00 49.41           C  
ANISOU 1823  CA  PRO B  39     6563   5868   6342    416   -477    912       C  
ATOM   1824  C   PRO B  39      57.788  36.545  63.009  1.00 52.56           C  
ANISOU 1824  C   PRO B  39     6738   6092   7140    582   -598   1042       C  
ATOM   1825  O   PRO B  39      57.887  35.317  63.138  1.00 56.11           O  
ANISOU 1825  O   PRO B  39     7202   6304   7812    670   -569   1174       O  
ATOM   1826  CB  PRO B  39      55.350  36.088  63.344  1.00 49.70           C  
ANISOU 1826  CB  PRO B  39     6791   5769   6323    358   -325    962       C  
ATOM   1827  CG  PRO B  39      54.367  36.187  62.138  1.00 48.15           C  
ANISOU 1827  CG  PRO B  39     6573   5624   6098    270    -43    694       C  
ATOM   1828  CD  PRO B  39      55.131  36.938  61.056  1.00 46.25           C  
ANISOU 1828  CD  PRO B  39     6128   5463   5978    328     -5    519       C  
ATOM   1829  N   GLY B  40      58.819  37.368  62.779  1.00 52.82           N  
ANISOU 1829  N   GLY B  40     6548   6219   7299    627   -720   1017       N  
ATOM   1830  CA  GLY B  40      60.206  36.930  62.688  1.00 55.22           C  
ANISOU 1830  CA  GLY B  40     6556   6383   8041    792   -842   1152       C  
ATOM   1831  C   GLY B  40      61.180  38.073  62.430  1.00 55.99           C  
ANISOU 1831  C   GLY B  40     6403   6635   8232    777   -957   1098       C  
ATOM   1832  O   GLY B  40      62.344  38.023  62.839  1.00 58.06           O  
ANISOU 1832  O   GLY B  40     6416   6859   8785    863  -1206   1284       O  
ATOM   1833  N   MET B  41      60.733  39.120  61.748  1.00 53.27           N  
ANISOU 1833  N   MET B  41     6104   6459   7674    662   -793    867       N  
ATOM   1834  CA  MET B  41      61.705  40.100  61.275  1.00 54.12           C  
ANISOU 1834  CA  MET B  41     5955   6664   7943    646   -826    804       C  
ATOM   1835  C   MET B  41      61.514  41.563  61.638  1.00 51.76           C  
ANISOU 1835  C   MET B  41     5765   6571   7331    474   -968    737       C  
ATOM   1836  O   MET B  41      62.173  42.414  61.036  1.00 52.19           O  
ANISOU 1836  O   MET B  41     5628   6689   7511    435   -923    652       O  
ATOM   1837  CB  MET B  41      61.913  39.995  59.763  1.00 54.64           C  
ANISOU 1837  CB  MET B  41     5858   6673   8228    701   -442    597       C  
ATOM   1838  CG  MET B  41      60.739  39.481  58.923  1.00 55.09           C  
ANISOU 1838  CG  MET B  41     6141   6691   8098    670   -126    407       C  
ATOM   1839  SD  MET B  41      61.349  38.129  57.843  1.00 66.08           S  
ANISOU 1839  SD  MET B  41     7367   7812   9926    834    220    310       S  
ATOM   1840  CE  MET B  41      62.947  38.806  57.303  1.00 62.07           C  
ANISOU 1840  CE  MET B  41     6451   7330   9802    908    281    313       C  
ATOM   1841  N   GLY B  42      60.633  41.865  62.586  1.00 49.17           N  
ANISOU 1841  N   GLY B  42     5745   6323   6611    369  -1099    765       N  
ATOM   1842  CA  GLY B  42      60.302  43.270  62.868  1.00 46.49           C  
ANISOU 1842  CA  GLY B  42     5554   6133   5974    215  -1158    654       C  
ATOM   1843  C   GLY B  42      59.710  44.011  61.667  1.00 42.75           C  
ANISOU 1843  C   GLY B  42     5076   5713   5453    189   -851    442       C  
ATOM   1844  O   GLY B  42      59.166  43.381  60.743  1.00 41.99           O  
ANISOU 1844  O   GLY B  42     4965   5572   5414    252   -593    363       O  
ATOM   1845  N   LEU B  43      59.818  45.341  61.692  1.00 40.18           N  
ANISOU 1845  N   LEU B  43     4782   5470   5014     79   -898    359       N  
ATOM   1846  CA  LEU B  43      59.197  46.234  60.710  1.00 36.47           C  
ANISOU 1846  CA  LEU B  43     4350   5047   4461     43   -659    207       C  
ATOM   1847  C   LEU B  43      60.079  46.490  59.504  1.00 36.02           C  
ANISOU 1847  C   LEU B  43     4034   4978   4670     55   -522    165       C  
ATOM   1848  O   LEU B  43      61.229  46.848  59.648  1.00 36.73           O  
ANISOU 1848  O   LEU B  43     3928   5058   4967     18   -657    215       O  
ATOM   1849  CB  LEU B  43      58.897  47.581  61.345  1.00 36.65           C  
ANISOU 1849  CB  LEU B  43     4553   5111   4260    -75   -750    145       C  
ATOM   1850  CG  LEU B  43      57.784  47.578  62.376  1.00 35.57           C  
ANISOU 1850  CG  LEU B  43     4717   4990   3808    -99   -761    132       C  
ATOM   1851  CD1 LEU B  43      57.981  48.752  63.319  1.00 39.00           C  
ANISOU 1851  CD1 LEU B  43     5332   5423   4061   -232   -917     74       C  
ATOM   1852  CD2 LEU B  43      56.453  47.575  61.701  1.00 29.79           C  
ANISOU 1852  CD2 LEU B  43     4055   4276   2984    -45   -493     59       C  
ATOM   1853  N   ARG B  44      59.517  46.325  58.308  1.00 33.97           N  
ANISOU 1853  N   ARG B  44     3784   4731   4392     85   -252     76       N  
ATOM   1854  CA  ARG B  44      60.299  46.540  57.093  1.00 33.30           C  
ANISOU 1854  CA  ARG B  44     3508   4642   4503     78    -62     29       C  
ATOM   1855  C   ARG B  44      59.582  47.568  56.229  1.00 30.87           C  
ANISOU 1855  C   ARG B  44     3329   4403   3997      0     83    -40       C  
ATOM   1856  O   ARG B  44      58.408  47.386  55.873  1.00 28.96           O  
ANISOU 1856  O   ARG B  44     3251   4201   3551      7    167    -80       O  
ATOM   1857  CB  ARG B  44      60.534  45.196  56.364  1.00 32.90           C  
ANISOU 1857  CB  ARG B  44     3355   4514   4631    180    136     -4       C  
ATOM   1858  CG  ARG B  44      61.613  44.305  57.039  1.00 37.88           C  
ANISOU 1858  CG  ARG B  44     3760   5035   5597    288      7    106       C  
ATOM   1859  CD  ARG B  44      61.775  42.939  56.330  1.00 41.20           C  
ANISOU 1859  CD  ARG B  44     4107   5318   6227    412    254     52       C  
ATOM   1860  NE  ARG B  44      60.487  42.226  56.258  1.00 40.78           N  
ANISOU 1860  NE  ARG B  44     4321   5245   5928    404    325    -14       N  
ATOM   1861  CZ  ARG B  44      60.140  41.362  55.303  1.00 40.81           C  
ANISOU 1861  CZ  ARG B  44     4397   5166   5943    422    594   -150       C  
ATOM   1862  NH1 ARG B  44      60.984  41.063  54.323  1.00 42.59           N  
ANISOU 1862  NH1 ARG B  44     4476   5311   6395    467    866   -250       N  
ATOM   1863  NH2 ARG B  44      58.947  40.788  55.337  1.00 39.66           N  
ANISOU 1863  NH2 ARG B  44     4473   5011   5583    376    607   -198       N  
ATOM   1864  N   LEU B  45      60.285  48.655  55.909  1.00 30.55           N  
ANISOU 1864  N   LEU B  45     3199   4368   4038    -84     95    -31       N  
ATOM   1865  CA  LEU B  45      59.743  49.711  55.042  1.00 29.57           C  
ANISOU 1865  CA  LEU B  45     3190   4281   3760   -156    224    -50       C  
ATOM   1866  C   LEU B  45      59.402  49.172  53.637  1.00 29.01           C  
ANISOU 1866  C   LEU B  45     3153   4260   3609   -149    476    -94       C  
ATOM   1867  O   LEU B  45      60.232  48.484  53.036  1.00 30.48           O  
ANISOU 1867  O   LEU B  45     3199   4425   3957   -134    640   -132       O  
ATOM   1868  CB  LEU B  45      60.777  50.850  54.924  1.00 30.87           C  
ANISOU 1868  CB  LEU B  45     3234   4410   4085   -267    212    -16       C  
ATOM   1869  CG  LEU B  45      60.307  52.123  54.206  1.00 30.76           C  
ANISOU 1869  CG  LEU B  45     3357   4390   3940   -350    308      7       C  
ATOM   1870  CD1 LEU B  45      59.096  52.706  54.915  1.00 30.56           C  
ANISOU 1870  CD1 LEU B  45     3552   4340   3718   -317    187      2       C  
ATOM   1871  CD2 LEU B  45      61.474  53.172  54.143  1.00 33.80           C  
ANISOU 1871  CD2 LEU B  45     3603   4706   4533   -490    307     45       C  
ATOM   1872  N   ILE B  46      58.208  49.471  53.123  1.00 27.44           N  
ANISOU 1872  N   ILE B  46     3135   4122   3169   -166    505    -92       N  
ATOM   1873  CA  ILE B  46      57.783  49.001  51.765  1.00 28.16           C  
ANISOU 1873  CA  ILE B  46     3308   4283   3105   -206    691   -133       C  
ATOM   1874  C   ILE B  46      57.936  50.138  50.738  1.00 29.85           C  
ANISOU 1874  C   ILE B  46     3581   4536   3223   -307    792    -63       C  
ATOM   1875  O   ILE B  46      58.702  50.005  49.786  1.00 31.45           O  
ANISOU 1875  O   ILE B  46     3754   4751   3441   -374   1004    -93       O  
ATOM   1876  CB  ILE B  46      56.301  48.531  51.748  1.00 25.83           C  
ANISOU 1876  CB  ILE B  46     3156   4051   2604   -190    614   -143       C  
ATOM   1877  CG1 ILE B  46      56.092  47.405  52.756  1.00 26.18           C  
ANISOU 1877  CG1 ILE B  46     3172   4042   2732   -112    537   -189       C  
ATOM   1878  CG2 ILE B  46      55.861  48.101  50.340  1.00 27.28           C  
ANISOU 1878  CG2 ILE B  46     3453   4322   2587   -282    745   -189       C  
ATOM   1879  CD1 ILE B  46      54.622  46.948  52.892  1.00 26.70           C  
ANISOU 1879  CD1 ILE B  46     3339   4161   2643   -115    469   -190       C  
ATOM   1880  N   HIS B  47      57.194  51.227  50.974  1.00 29.06           N  
ANISOU 1880  N   HIS B  47     3570   4435   3037   -311    662     35       N  
ATOM   1881  CA  HIS B  47      57.270  52.503  50.245  1.00 30.45           C  
ANISOU 1881  CA  HIS B  47     3813   4599   3157   -391    708    155       C  
ATOM   1882  C   HIS B  47      57.126  53.644  51.224  1.00 30.91           C  
ANISOU 1882  C   HIS B  47     3878   4540   3325   -360    566    211       C  
ATOM   1883  O   HIS B  47      56.592  53.449  52.322  1.00 29.54           O  
ANISOU 1883  O   HIS B  47     3711   4335   3175   -276    437    160       O  
ATOM   1884  CB  HIS B  47      56.114  52.628  49.265  1.00 29.69           C  
ANISOU 1884  CB  HIS B  47     3873   4602   2804   -416    687    245       C  
ATOM   1885  CG  HIS B  47      56.210  51.718  48.081  1.00 30.55           C  
ANISOU 1885  CG  HIS B  47     4060   4824   2721   -507    837    181       C  
ATOM   1886  ND1 HIS B  47      56.932  52.044  46.953  1.00 33.11           N  
ANISOU 1886  ND1 HIS B  47     4459   5179   2940   -633   1035    218       N  
ATOM   1887  CD2 HIS B  47      55.665  50.502  47.839  1.00 31.16           C  
ANISOU 1887  CD2 HIS B  47     4185   4977   2675   -513    839     66       C  
ATOM   1888  CE1 HIS B  47      56.815  51.078  46.058  1.00 34.46           C  
ANISOU 1888  CE1 HIS B  47     4745   5446   2900   -712   1161    113       C  
ATOM   1889  NE2 HIS B  47      56.069  50.120  46.576  1.00 32.41           N  
ANISOU 1889  NE2 HIS B  47     4468   5206   2640   -643   1037     11       N  
ATOM   1890  N   TYR B  48      57.562  54.847  50.829  1.00 32.79           N  
ANISOU 1890  N   TYR B  48     4146   4697   3616   -440    613    310       N  
ATOM   1891  CA  TYR B  48      57.358  56.057  51.639  1.00 32.64           C  
ANISOU 1891  CA  TYR B  48     4182   4519   3698   -427    509    349       C  
ATOM   1892  C   TYR B  48      57.083  57.256  50.724  1.00 34.79           C  
ANISOU 1892  C   TYR B  48     4567   4715   3933   -475    568    527       C  
ATOM   1893  O   TYR B  48      57.248  57.165  49.501  1.00 36.08           O  
ANISOU 1893  O   TYR B  48     4766   4968   3973   -550    682    627       O  
ATOM   1894  CB  TYR B  48      58.555  56.306  52.573  1.00 33.79           C  
ANISOU 1894  CB  TYR B  48     4219   4566   4053   -507    458    259       C  
ATOM   1895  CG  TYR B  48      59.865  56.702  51.903  1.00 37.06           C  
ANISOU 1895  CG  TYR B  48     4510   4951   4620   -660    587    304       C  
ATOM   1896  CD1 TYR B  48      60.613  55.783  51.173  1.00 40.16           C  
ANISOU 1896  CD1 TYR B  48     4755   5456   5045   -688    746    282       C  
ATOM   1897  CD2 TYR B  48      60.349  57.999  52.026  1.00 38.68           C  
ANISOU 1897  CD2 TYR B  48     4744   4991   4962   -782    582    358       C  
ATOM   1898  CE1 TYR B  48      61.825  56.153  50.569  1.00 42.44           C  
ANISOU 1898  CE1 TYR B  48     4899   5717   5509   -830    919    324       C  
ATOM   1899  CE2 TYR B  48      61.542  58.399  51.432  1.00 43.07           C  
ANISOU 1899  CE2 TYR B  48     5164   5512   5686   -948    720    412       C  
ATOM   1900  CZ  TYR B  48      62.280  57.477  50.709  1.00 44.28           C  
ANISOU 1900  CZ  TYR B  48     5142   5801   5879   -969    897    400       C  
ATOM   1901  OH  TYR B  48      63.449  57.890  50.126  1.00 47.53           O  
ANISOU 1901  OH  TYR B  48     5394   6179   6487  -1134   1083    456       O  
ATOM   1902  N   SER B  49      56.636  58.360  51.316  1.00 34.11           N  
ANISOU 1902  N   SER B  49     4565   4450   3942   -432    501    571       N  
ATOM   1903  CA  SER B  49      56.269  59.522  50.554  1.00 35.08           C  
ANISOU 1903  CA  SER B  49     4801   4454   4074   -445    536    773       C  
ATOM   1904  C   SER B  49      56.566  60.774  51.370  1.00 35.78           C  
ANISOU 1904  C   SER B  49     4956   4264   4374   -474    527    745       C  
ATOM   1905  O   SER B  49      56.007  60.960  52.468  1.00 33.88           O  
ANISOU 1905  O   SER B  49     4761   3915   4196   -374    463    626       O  
ATOM   1906  CB  SER B  49      54.788  59.484  50.155  1.00 34.85           C  
ANISOU 1906  CB  SER B  49     4825   4484   3931   -294    455    909       C  
ATOM   1907  OG  SER B  49      54.400  60.769  49.676  1.00 37.35           O  
ANISOU 1907  OG  SER B  49     5242   4619   4329   -268    455   1129       O  
ATOM   1908  N   VAL B  50      57.439  61.624  50.819  1.00 36.97           N  
ANISOU 1908  N   VAL B  50     5132   4289   4625   -631    615    846       N  
ATOM   1909  CA  VAL B  50      57.822  62.890  51.474  1.00 39.41           C  
ANISOU 1909  CA  VAL B  50     5527   4295   5151   -711    617    817       C  
ATOM   1910  C   VAL B  50      56.821  64.041  51.258  1.00 41.15           C  
ANISOU 1910  C   VAL B  50     5915   4272   5448   -589    632    991       C  
ATOM   1911  O   VAL B  50      56.977  65.126  51.835  1.00 43.63           O  
ANISOU 1911  O   VAL B  50     6340   4280   5956   -633    655    948       O  
ATOM   1912  CB  VAL B  50      59.215  63.425  50.990  1.00 41.09           C  
ANISOU 1912  CB  VAL B  50     5680   4430   5500   -961    721    869       C  
ATOM   1913  CG1 VAL B  50      60.302  62.427  51.233  1.00 40.44           C  
ANISOU 1913  CG1 VAL B  50     5377   4540   5446  -1069    718    720       C  
ATOM   1914  CG2 VAL B  50      59.138  63.835  49.534  1.00 42.11           C  
ANISOU 1914  CG2 VAL B  50     5886   4575   5540  -1008    858   1149       C  
ATOM   1915  N   GLY B  51      55.843  63.834  50.388  1.00 41.07           N  
ANISOU 1915  N   GLY B  51     5920   4378   5306   -450    611   1198       N  
ATOM   1916  CA  GLY B  51      54.943  64.910  50.015  1.00 42.74           C  
ANISOU 1916  CA  GLY B  51     6244   4361   5631   -320    606   1435       C  
ATOM   1917  C   GLY B  51      53.994  64.404  48.962  1.00 43.11           C  
ANISOU 1917  C   GLY B  51     6261   4635   5484   -213    514   1675       C  
ATOM   1918  O   GLY B  51      54.250  63.367  48.321  1.00 41.25           O  
ANISOU 1918  O   GLY B  51     5972   4702   4999   -302    499   1659       O  
ATOM   1919  N   ALA B  52      52.885  65.131  48.816  1.00 44.40           N  
ANISOU 1919  N   ALA B  52     6452   4635   5781    -21    449   1890       N  
ATOM   1920  CA  ALA B  52      51.893  64.889  47.787  1.00 45.71           C  
ANISOU 1920  CA  ALA B  52     6582   4979   5804     72    297   2186       C  
ATOM   1921  C   ALA B  52      52.510  65.012  46.389  1.00 47.83           C  
ANISOU 1921  C   ALA B  52     6981   5364   5827   -129    295   2442       C  
ATOM   1922  O   ALA B  52      53.073  66.067  46.040  1.00 51.20           O  
ANISOU 1922  O   ALA B  52     7543   5547   6363   -217    383   2617       O  
ATOM   1923  CB  ALA B  52      50.726  65.904  47.932  1.00 48.54           C  
ANISOU 1923  CB  ALA B  52     6919   5062   6463    327    235   2416       C  
ATOM   1924  N   GLY B  53      52.341  63.961  45.584  1.00 46.64           N  
ANISOU 1924  N   GLY B  53     6817   5565   5339   -212    207   2470       N  
ATOM   1925  CA  GLY B  53      52.878  63.919  44.247  1.00 48.44           C  
ANISOU 1925  CA  GLY B  53     7209   5945   5250   -424    237   2674       C  
ATOM   1926  C   GLY B  53      54.181  63.138  44.165  1.00 46.79           C  
ANISOU 1926  C   GLY B  53     7008   5886   4882   -639    459   2409       C  
ATOM   1927  O   GLY B  53      54.693  62.942  43.083  1.00 47.81           O  
ANISOU 1927  O   GLY B  53     7278   6164   4721   -829    556   2517       O  
ATOM   1928  N   ILE B  54      54.674  62.653  45.305  1.00 43.53           N  
ANISOU 1928  N   ILE B  54     6444   5440   4654   -604    541   2073       N  
ATOM   1929  CA  ILE B  54      55.988  62.051  45.410  1.00 42.72           C  
ANISOU 1929  CA  ILE B  54     6282   5416   4532   -771    744   1841       C  
ATOM   1930  C   ILE B  54      55.938  60.713  46.178  1.00 40.35           C  
ANISOU 1930  C   ILE B  54     5824   5290   4217   -698    711   1529       C  
ATOM   1931  O   ILE B  54      55.499  60.678  47.347  1.00 37.55           O  
ANISOU 1931  O   ILE B  54     5375   4844   4045   -553    610   1388       O  
ATOM   1932  CB  ILE B  54      56.927  63.004  46.193  1.00 43.73           C  
ANISOU 1932  CB  ILE B  54     6367   5258   4989   -838    851   1770       C  
ATOM   1933  CG1 ILE B  54      56.999  64.396  45.538  1.00 48.99           C  
ANISOU 1933  CG1 ILE B  54     7199   5684   5729   -915    900   2082       C  
ATOM   1934  CG2 ILE B  54      58.349  62.429  46.312  1.00 43.55           C  
ANISOU 1934  CG2 ILE B  54     6210   5316   5020  -1014   1038   1565       C  
ATOM   1935  CD1 ILE B  54      56.214  65.497  46.312  1.00 51.29           C  
ANISOU 1935  CD1 ILE B  54     7535   5644   6307   -739    782   2158       C  
ATOM   1936  N   THR B  55      56.383  59.619  45.544  1.00 39.83           N  
ANISOU 1936  N   THR B  55     5751   5449   3931   -800    820   1422       N  
ATOM   1937  CA  THR B  55      56.584  58.356  46.271  1.00 38.15           C  
ANISOU 1937  CA  THR B  55     5387   5348   3757   -746    828   1137       C  
ATOM   1938  C   THR B  55      57.963  57.791  45.927  1.00 38.42           C  
ANISOU 1938  C   THR B  55     5346   5437   3813   -888   1081   1002       C  
ATOM   1939  O   THR B  55      58.525  58.140  44.888  1.00 40.66           O  
ANISOU 1939  O   THR B  55     5731   5745   3972  -1040   1270   1119       O  
ATOM   1940  CB  THR B  55      55.424  57.283  46.043  1.00 37.59           C  
ANISOU 1940  CB  THR B  55     5343   5476   3462   -667    685   1092       C  
ATOM   1941  OG1 THR B  55      55.452  56.765  44.705  1.00 42.14           O  
ANISOU 1941  OG1 THR B  55     6071   6234   3707   -811    769   1144       O  
ATOM   1942  CG2 THR B  55      54.003  57.878  46.316  1.00 37.66           C  
ANISOU 1942  CG2 THR B  55     5361   5436   3509   -516    447   1261       C  
ATOM   1943  N   ASP B  56      58.514  56.966  46.830  1.00 36.01           N  
ANISOU 1943  N   ASP B  56     4854   5137   3689   -834   1093    778       N  
ATOM   1944  CA  ASP B  56      59.815  56.324  46.671  1.00 37.03           C  
ANISOU 1944  CA  ASP B  56     4830   5298   3942   -918   1323    646       C  
ATOM   1945  C   ASP B  56      59.738  54.939  47.301  1.00 34.93           C  
ANISOU 1945  C   ASP B  56     4443   5107   3722   -802   1274    442       C  
ATOM   1946  O   ASP B  56      58.894  54.706  48.170  1.00 33.48           O  
ANISOU 1946  O   ASP B  56     4265   4915   3540   -679   1053    402       O  
ATOM   1947  CB  ASP B  56      60.943  57.119  47.359  1.00 36.82           C  
ANISOU 1947  CB  ASP B  56     4620   5111   4256   -993   1350    646       C  
ATOM   1948  CG  ASP B  56      61.468  58.308  46.515  1.00 41.84           C  
ANISOU 1948  CG  ASP B  56     5339   5657   4899  -1168   1522    834       C  
ATOM   1949  OD1 ASP B  56      62.205  58.068  45.514  1.00 39.16           O  
ANISOU 1949  OD1 ASP B  56     4991   5392   4494  -1294   1816    856       O  
ATOM   1950  OD2 ASP B  56      61.184  59.493  46.892  1.00 40.23           O  
ANISOU 1950  OD2 ASP B  56     5217   5281   4785  -1186   1391    955       O  
ATOM   1951  N   GLN B  57      60.628  54.054  46.877  1.00 35.31           N  
ANISOU 1951  N   GLN B  57     4381   5203   3830   -838   1508    323       N  
ATOM   1952  CA  GLN B  57      60.693  52.674  47.298  1.00 35.36           C  
ANISOU 1952  CA  GLN B  57     4280   5242   3910   -732   1517    146       C  
ATOM   1953  C   GLN B  57      61.398  52.508  48.646  1.00 35.27           C  
ANISOU 1953  C   GLN B  57     4007   5136   4258   -646   1371     94       C  
ATOM   1954  O   GLN B  57      62.414  53.154  48.899  1.00 35.55           O  
ANISOU 1954  O   GLN B  57     3861   5098   4545   -715   1406    137       O  
ATOM   1955  CB  GLN B  57      61.401  51.837  46.225  1.00 36.73           C  
ANISOU 1955  CB  GLN B  57     4454   5465   4037   -795   1877     37       C  
ATOM   1956  CG  GLN B  57      60.750  51.948  44.864  1.00 41.93           C  
ANISOU 1956  CG  GLN B  57     5426   6239   4264   -925   2006     80       C  
ATOM   1957  CD  GLN B  57      61.339  50.990  43.802  1.00 50.37           C  
ANISOU 1957  CD  GLN B  57     6574   7351   5213  -1002   2403    -87       C  
ATOM   1958  OE1 GLN B  57      60.636  50.584  42.875  1.00 52.84           O  
ANISOU 1958  OE1 GLN B  57     7178   7770   5130  -1098   2453   -133       O  
ATOM   1959  NE2 GLN B  57      62.625  50.652  43.927  1.00 50.31           N  
ANISOU 1959  NE2 GLN B  57     6305   7255   5553   -971   2687   -179       N  
ATOM   1960  N   GLY B  58      60.826  51.670  49.521  1.00 34.36           N  
ANISOU 1960  N   GLY B  58     3880   5023   4151   -518   1185     18       N  
ATOM   1961  CA  GLY B  58      61.512  51.236  50.746  1.00 35.68           C  
ANISOU 1961  CA  GLY B  58     3826   5120   4609   -440   1034    -18       C  
ATOM   1962  C   GLY B  58      62.446  50.069  50.437  1.00 38.99           C  
ANISOU 1962  C   GLY B  58     4043   5519   5250   -384   1240   -102       C  
ATOM   1963  O   GLY B  58      62.914  49.949  49.308  1.00 40.53           O  
ANISOU 1963  O   GLY B  58     4231   5733   5434   -443   1553   -140       O  
ATOM   1964  N   GLU B  59      62.712  49.198  51.414  1.00 39.42           N  
ANISOU 1964  N   GLU B  59     3947   5520   5507   -266   1087   -125       N  
ATOM   1965  CA  GLU B  59      63.576  48.028  51.161  1.00 42.55           C  
ANISOU 1965  CA  GLU B  59     4129   5851   6185   -170   1289   -189       C  
ATOM   1966  C   GLU B  59      62.859  46.776  50.621  1.00 41.77           C  
ANISOU 1966  C   GLU B  59     4208   5735   5928    -93   1451   -315       C  
ATOM   1967  O   GLU B  59      63.519  45.874  50.070  1.00 42.41           O  
ANISOU 1967  O   GLU B  59     4172   5732   6209    -27   1732   -407       O  
ATOM   1968  CB  GLU B  59      64.389  47.654  52.404  1.00 44.86           C  
ANISOU 1968  CB  GLU B  59     4137   6069   6837    -76   1039   -109       C  
ATOM   1969  CG  GLU B  59      63.571  47.256  53.588  1.00 47.02           C  
ANISOU 1969  CG  GLU B  59     4554   6338   6971     -6    709    -71       C  
ATOM   1970  CD  GLU B  59      64.397  46.485  54.630  1.00 55.49           C  
ANISOU 1970  CD  GLU B  59     5370   7330   8384    105    494     24       C  
ATOM   1971  OE1 GLU B  59      64.616  47.045  55.752  1.00 55.71           O  
ANISOU 1971  OE1 GLU B  59     5358   7380   8427     50    146    124       O  
ATOM   1972  OE2 GLU B  59      64.819  45.328  54.315  1.00 56.35           O  
ANISOU 1972  OE2 GLU B  59     5333   7339   8738    243    668      2       O  
ATOM   1973  N   VAL B  60      61.532  46.702  50.808  1.00 38.45           N  
ANISOU 1973  N   VAL B  60     4050   5371   5186   -105   1288   -326       N  
ATOM   1974  CA  VAL B  60      60.746  45.644  50.148  1.00 38.88           C  
ANISOU 1974  CA  VAL B  60     4302   5420   5050    -99   1431   -455       C  
ATOM   1975  C   VAL B  60      59.566  46.155  49.323  1.00 37.94           C  
ANISOU 1975  C   VAL B  60     4464   5435   4516   -230   1421   -467       C  
ATOM   1976  O   VAL B  60      58.397  45.897  49.665  1.00 36.60           O  
ANISOU 1976  O   VAL B  60     4431   5304   4170   -229   1239   -460       O  
ATOM   1977  CB  VAL B  60      60.333  44.523  51.103  1.00 37.74           C  
ANISOU 1977  CB  VAL B  60     4152   5180   5006     19   1275   -464       C  
ATOM   1978  CG1 VAL B  60      61.552  43.679  51.401  1.00 42.26           C  
ANISOU 1978  CG1 VAL B  60     4466   5594   5997    155   1385   -469       C  
ATOM   1979  CG2 VAL B  60      59.656  45.088  52.429  1.00 33.17           C  
ANISOU 1979  CG2 VAL B  60     3606   4648   4348     37    915   -331       C  
ATOM   1980  N   PRO B  61      59.866  46.922  48.261  1.00 39.11           N  
ANISOU 1980  N   PRO B  61     4681   5654   4522   -348   1601   -455       N  
ATOM   1981  CA  PRO B  61      58.819  47.521  47.412  1.00 39.18           C  
ANISOU 1981  CA  PRO B  61     4947   5798   4139   -479   1548   -408       C  
ATOM   1982  C   PRO B  61      58.057  46.483  46.566  1.00 40.17           C  
ANISOU 1982  C   PRO B  61     5297   5970   3994   -560   1637   -556       C  
ATOM   1983  O   PRO B  61      56.904  46.731  46.205  1.00 39.43           O  
ANISOU 1983  O   PRO B  61     5377   5992   3611   -647   1460   -499       O  
ATOM   1984  CB  PRO B  61      59.619  48.454  46.456  1.00 41.36           C  
ANISOU 1984  CB  PRO B  61     5244   6111   4359   -597   1772   -347       C  
ATOM   1985  CG  PRO B  61      61.017  47.893  46.423  1.00 41.38           C  
ANISOU 1985  CG  PRO B  61     5027   6007   4688   -547   2068   -450       C  
ATOM   1986  CD  PRO B  61      61.227  47.322  47.822  1.00 41.48           C  
ANISOU 1986  CD  PRO B  61     4805   5914   5042   -375   1856   -449       C  
ATOM   1987  N   ASN B  62      58.703  45.351  46.267  1.00 41.66           N  
ANISOU 1987  N   ASN B  62     5471   6053   4305   -535   1902   -741       N  
ATOM   1988  CA  ASN B  62      58.208  44.373  45.287  1.00 44.38           C  
ANISOU 1988  CA  ASN B  62     6072   6406   4382   -657   2065   -937       C  
ATOM   1989  C   ASN B  62      56.854  43.780  45.632  1.00 42.64           C  
ANISOU 1989  C   ASN B  62     5967   6221   4014   -690   1791   -955       C  
ATOM   1990  O   ASN B  62      56.672  43.220  46.721  1.00 40.87           O  
ANISOU 1990  O   ASN B  62     5603   5891   4032   -558   1654   -939       O  
ATOM   1991  CB  ASN B  62      59.211  43.216  45.092  1.00 46.45           C  
ANISOU 1991  CB  ASN B  62     6269   6476   4902   -580   2436  -1151       C  
ATOM   1992  CG  ASN B  62      60.394  43.606  44.243  1.00 53.70           C  
ANISOU 1992  CG  ASN B  62     7150   7384   5868   -621   2830  -1199       C  
ATOM   1993  OD1 ASN B  62      60.383  44.659  43.572  1.00 57.46           O  
ANISOU 1993  OD1 ASN B  62     7736   8011   6084   -759   2850  -1092       O  
ATOM   1994  ND2 ASN B  62      61.452  42.760  44.261  1.00 57.92           N  
ANISOU 1994  ND2 ASN B  62     7513   7722   6769   -493   3174  -1345       N  
ATOM   1995  N   GLY B  63      55.937  43.865  44.670  1.00 44.13           N  
ANISOU 1995  N   GLY B  63     6410   6556   3799   -886   1716   -979       N  
ATOM   1996  CA  GLY B  63      54.598  43.303  44.783  1.00 43.22           C  
ANISOU 1996  CA  GLY B  63     6393   6497   3531   -973   1461   -999       C  
ATOM   1997  C   GLY B  63      53.625  44.341  45.306  1.00 41.85           C  
ANISOU 1997  C   GLY B  63     6117   6463   3319   -942   1109   -747       C  
ATOM   1998  O   GLY B  63      52.423  44.043  45.482  1.00 41.95           O  
ANISOU 1998  O   GLY B  63     6140   6543   3254  -1003    874   -716       O  
ATOM   1999  N   TYR B  64      54.127  45.555  45.558  1.00 40.03           N  
ANISOU 1999  N   TYR B  64     5774   6257   3176   -850   1089   -571       N  
ATOM   2000  CA  TYR B  64      53.291  46.630  46.124  1.00 39.04           C  
ANISOU 2000  CA  TYR B  64     5548   6209   3074   -785    807   -341       C  
ATOM   2001  C   TYR B  64      53.424  47.908  45.284  1.00 40.47           C  
ANISOU 2001  C   TYR B  64     5818   6485   3072   -856    791   -164       C  
ATOM   2002  O   TYR B  64      54.499  48.226  44.813  1.00 41.64           O  
ANISOU 2002  O   TYR B  64     6005   6599   3215   -887   1017   -186       O  
ATOM   2003  CB  TYR B  64      53.677  46.946  47.580  1.00 35.49           C  
ANISOU 2003  CB  TYR B  64     4885   5637   2962   -588    763   -285       C  
ATOM   2004  CG  TYR B  64      53.684  45.746  48.532  1.00 33.60           C  
ANISOU 2004  CG  TYR B  64     4567   5283   2916   -506    777   -406       C  
ATOM   2005  CD1 TYR B  64      52.522  45.340  49.147  1.00 27.94           C  
ANISOU 2005  CD1 TYR B  64     3826   4587   2200   -496    609   -379       C  
ATOM   2006  CD2 TYR B  64      54.868  45.063  48.835  1.00 30.45           C  
ANISOU 2006  CD2 TYR B  64     4095   4744   2729   -431    961   -515       C  
ATOM   2007  CE1 TYR B  64      52.518  44.285  49.992  1.00 29.86           C  
ANISOU 2007  CE1 TYR B  64     4027   4715   2601   -438    630   -456       C  
ATOM   2008  CE2 TYR B  64      54.885  43.987  49.689  1.00 28.57           C  
ANISOU 2008  CE2 TYR B  64     3799   4381   2676   -348    953   -578       C  
ATOM   2009  CZ  TYR B  64      53.688  43.588  50.256  1.00 31.23           C  
ANISOU 2009  CZ  TYR B  64     4164   4740   2962   -363    789   -548       C  
ATOM   2010  OH  TYR B  64      53.631  42.525  51.125  1.00 29.11           O  
ANISOU 2010  OH  TYR B  64     3865   4337   2856   -299    783   -579       O  
ATOM   2011  N   ASN B  65      52.321  48.616  45.096  1.00 40.90           N  
ANISOU 2011  N   ASN B  65     5888   6647   3005   -880    531     28       N  
ATOM   2012  CA  ASN B  65      52.340  49.963  44.534  1.00 42.00           C  
ANISOU 2012  CA  ASN B  65     6083   6832   3043   -902    468    263       C  
ATOM   2013  C   ASN B  65      51.742  50.928  45.548  1.00 40.36           C  
ANISOU 2013  C   ASN B  65     5693   6550   3092   -723    285    441       C  
ATOM   2014  O   ASN B  65      50.957  50.541  46.410  1.00 38.47           O  
ANISOU 2014  O   ASN B  65     5319   6294   3002   -627    165    410       O  
ATOM   2015  CB  ASN B  65      51.501  50.061  43.281  1.00 44.29           C  
ANISOU 2015  CB  ASN B  65     6567   7301   2957  -1086    294    387       C  
ATOM   2016  CG  ASN B  65      52.147  49.383  42.058  1.00 50.49           C  
ANISOU 2016  CG  ASN B  65     7631   8164   3387  -1310    515    222       C  
ATOM   2017  OD1 ASN B  65      53.381  49.342  41.900  1.00 52.68           O  
ANISOU 2017  OD1 ASN B  65     7953   8357   3706  -1315    845    105       O  
ATOM   2018  ND2 ASN B  65      51.297  48.907  41.156  1.00 50.58           N  
ANISOU 2018  ND2 ASN B  65     7834   8340   3043  -1511    334    218       N  
ATOM   2019  N   VAL B  66      52.030  52.205  45.359  1.00 41.02           N  
ANISOU 2019  N   VAL B  66     5796   6580   3210   -694    283    633       N  
ATOM   2020  CA  VAL B  66      51.638  53.185  46.310  1.00 40.13           C  
ANISOU 2020  CA  VAL B  66     5547   6341   3359   -525    180    762       C  
ATOM   2021  C   VAL B  66      51.249  54.455  45.532  1.00 42.58           C  
ANISOU 2021  C   VAL B  66     5937   6646   3593   -540     65   1057       C  
ATOM   2022  O   VAL B  66      51.619  54.618  44.363  1.00 44.79           O  
ANISOU 2022  O   VAL B  66     6394   7011   3612   -696    108   1152       O  
ATOM   2023  CB  VAL B  66      52.808  53.309  47.324  1.00 38.42           C  
ANISOU 2023  CB  VAL B  66     5247   5964   3386   -454    352    619       C  
ATOM   2024  CG1 VAL B  66      53.700  54.521  47.053  1.00 39.80           C  
ANISOU 2024  CG1 VAL B  66     5468   6025   3627   -491    453    739       C  
ATOM   2025  CG2 VAL B  66      52.333  53.151  48.727  1.00 35.22           C  
ANISOU 2025  CG2 VAL B  66     4712   5475   3195   -306    280    541       C  
ATOM   2026  N   SER B  67      50.458  55.328  46.147  1.00 42.01           N  
ANISOU 2026  N   SER B  67     5753   6467   3741   -379    -66   1214       N  
ATOM   2027  CA  SER B  67      50.119  56.605  45.499  1.00 44.31           C  
ANISOU 2027  CA  SER B  67     6105   6693   4036   -355   -173   1527       C  
ATOM   2028  C   SER B  67      49.940  57.666  46.569  1.00 43.14           C  
ANISOU 2028  C   SER B  67     5849   6293   4249   -154   -145   1578       C  
ATOM   2029  O   SER B  67      49.608  57.344  47.717  1.00 40.26           O  
ANISOU 2029  O   SER B  67     5353   5866   4074    -31   -114   1410       O  
ATOM   2030  CB  SER B  67      48.863  56.457  44.606  1.00 46.70           C  
ANISOU 2030  CB  SER B  67     6400   7177   4164   -393   -457   1752       C  
ATOM   2031  OG  SER B  67      48.330  57.716  44.292  1.00 52.77           O  
ANISOU 2031  OG  SER B  67     7157   7837   5055   -292   -600   2090       O  
ATOM   2032  N   ARG B  68      50.231  58.915  46.217  1.00 44.98           N  
ANISOU 2032  N   ARG B  68     6170   6357   4561   -141   -125   1791       N  
ATOM   2033  CA  ARG B  68      50.096  60.012  47.148  1.00 45.20           C  
ANISOU 2033  CA  ARG B  68     6145   6097   4930     30    -71   1824       C  
ATOM   2034  C   ARG B  68      49.682  61.183  46.314  1.00 49.15           C  
ANISOU 2034  C   ARG B  68     6717   6476   5481     71   -176   2192       C  
ATOM   2035  O   ARG B  68      50.509  62.049  45.988  1.00 51.58           O  
ANISOU 2035  O   ARG B  68     7168   6618   5811    -10    -70   2294       O  
ATOM   2036  CB  ARG B  68      51.411  60.317  47.880  1.00 43.76           C  
ANISOU 2036  CB  ARG B  68     6024   5744   4857    -38    134   1613       C  
ATOM   2037  CG  ARG B  68      51.291  61.352  49.033  1.00 42.40           C  
ANISOU 2037  CG  ARG B  68     5841   5255   5011    106    203   1557       C  
ATOM   2038  CD  ARG B  68      51.034  60.653  50.358  1.00 39.72           C  
ANISOU 2038  CD  ARG B  68     5413   4934   4745    193    239   1275       C  
ATOM   2039  NE  ARG B  68      50.764  61.593  51.447  1.00 40.08           N  
ANISOU 2039  NE  ARG B  68     5493   4687   5046    323    327   1195       N  
ATOM   2040  CZ  ARG B  68      51.704  62.226  52.145  1.00 39.14           C  
ANISOU 2040  CZ  ARG B  68     5489   4360   5020    237    423   1041       C  
ATOM   2041  NH1 ARG B  68      52.988  62.038  51.872  1.00 39.54           N  
ANISOU 2041  NH1 ARG B  68     5573   4470   4979     34    435    980       N  
ATOM   2042  NH2 ARG B  68      51.366  63.060  53.121  1.00 39.98           N  
ANISOU 2042  NH2 ARG B  68     5673   4189   5326    341    517    938       N  
ATOM   2043  N   SER B  69      48.407  61.205  45.931  1.00 51.04           N  
ANISOU 2043  N   SER B  69     6843   6797   5753    187   -399   2421       N  
ATOM   2044  CA  SER B  69      47.870  62.360  45.194  1.00 55.00           C  
ANISOU 2044  CA  SER B  69     7379   7157   6359    271   -548   2834       C  
ATOM   2045  C   SER B  69      47.478  63.476  46.167  1.00 55.13           C  
ANISOU 2045  C   SER B  69     7299   6797   6848    529   -443   2868       C  
ATOM   2046  O   SER B  69      47.563  64.655  45.820  1.00 57.28           O  
ANISOU 2046  O   SER B  69     7668   6813   7283    587   -439   3133       O  
ATOM   2047  CB  SER B  69      46.711  61.959  44.282  1.00 57.72           C  
ANISOU 2047  CB  SER B  69     7624   7752   6555    271   -880   3112       C  
ATOM   2048  OG  SER B  69      45.855  61.054  44.959  1.00 58.85           O  
ANISOU 2048  OG  SER B  69     7522   8032   6805    362   -940   2928       O  
ATOM   2049  N   THR B  70      47.101  63.106  47.398  1.00 52.33           N  
ANISOU 2049  N   THR B  70     6791   6387   6702    670   -324   2586       N  
ATOM   2050  CA  THR B  70      46.887  64.114  48.454  1.00 52.75           C  
ANISOU 2050  CA  THR B  70     6818   6059   7162    884   -140   2518       C  
ATOM   2051  C   THR B  70      47.751  63.928  49.720  1.00 49.65           C  
ANISOU 2051  C   THR B  70     6526   5555   6782    821    104   2095       C  
ATOM   2052  O   THR B  70      48.357  62.853  49.956  1.00 44.81           O  
ANISOU 2052  O   THR B  70     5930   5178   5919    662    120   1850       O  
ATOM   2053  CB  THR B  70      45.395  64.294  48.852  1.00 54.79           C  
ANISOU 2053  CB  THR B  70     6809   6245   7765   1172   -189   2645       C  
ATOM   2054  OG1 THR B  70      45.014  63.255  49.764  1.00 52.82           O  
ANISOU 2054  OG1 THR B  70     6419   6161   7486   1191   -103   2343       O  
ATOM   2055  CG2 THR B  70      44.497  64.274  47.621  1.00 57.46           C  
ANISOU 2055  CG2 THR B  70     6995   6763   8071   1208   -517   3072       C  
ATOM   2056  N   THR B  71      47.799  64.996  50.518  1.00 50.58           N  
ANISOU 2056  N   THR B  71     6723   5296   7198    942    281   2023       N  
ATOM   2057  CA  THR B  71      48.576  65.000  51.727  1.00 49.28           C  
ANISOU 2057  CA  THR B  71     6690   4997   7036    861    472   1647       C  
ATOM   2058  C   THR B  71      47.954  64.082  52.783  1.00 48.11           C  
ANISOU 2058  C   THR B  71     6430   4988   6858    947    542   1388       C  
ATOM   2059  O   THR B  71      48.689  63.439  53.521  1.00 45.94           O  
ANISOU 2059  O   THR B  71     6239   4810   6405    805    590   1107       O  
ATOM   2060  CB  THR B  71      48.992  66.435  52.212  1.00 51.71           C  
ANISOU 2060  CB  THR B  71     7189   4841   7614    888    642   1608       C  
ATOM   2061  OG1 THR B  71      49.211  66.444  53.630  1.00 50.19           O  
ANISOU 2061  OG1 THR B  71     7105   4505   7458    877    818   1227       O  
ATOM   2062  CG2 THR B  71      47.975  67.495  51.828  1.00 56.93           C  
ANISOU 2062  CG2 THR B  71     7791   5209   8629   1147    660   1912       C  
ATOM   2063  N   GLU B  72      46.632  63.920  52.768  1.00 50.30           N  
ANISOU 2063  N   GLU B  72     6498   5311   7299   1159    524   1518       N  
ATOM   2064  CA  GLU B  72      45.937  63.108  53.783  1.00 50.13           C  
ANISOU 2064  CA  GLU B  72     6363   5400   7282   1241    638   1297       C  
ATOM   2065  C   GLU B  72      46.021  61.597  53.583  1.00 47.24           C  
ANISOU 2065  C   GLU B  72     5905   5428   6614   1090    499   1224       C  
ATOM   2066  O   GLU B  72      45.985  60.857  54.547  1.00 45.75           O  
ANISOU 2066  O   GLU B  72     5730   5315   6336   1064    606    984       O  
ATOM   2067  CB  GLU B  72      44.462  63.514  53.930  1.00 53.44           C  
ANISOU 2067  CB  GLU B  72     6542   5698   8064   1528    721   1453       C  
ATOM   2068  CG  GLU B  72      44.240  64.836  54.625  1.00 57.39           C  
ANISOU 2068  CG  GLU B  72     7144   5748   8911   1722    987   1395       C  
ATOM   2069  CD  GLU B  72      44.035  65.965  53.644  1.00 65.70           C  
ANISOU 2069  CD  GLU B  72     8155   6567  10238   1854    882   1759       C  
ATOM   2070  OE1 GLU B  72      42.939  66.602  53.655  1.00 70.33           O  
ANISOU 2070  OE1 GLU B  72     8535   6943  11242   2142    969   1946       O  
ATOM   2071  OE2 GLU B  72      44.968  66.213  52.842  1.00 65.74           O  
ANISOU 2071  OE2 GLU B  72     8322   6593  10061   1672    721   1882       O  
ATOM   2072  N   ASP B  73      46.165  61.153  52.337  1.00 46.96           N  
ANISOU 2072  N   ASP B  73     5815   5620   6406    977    274   1427       N  
ATOM   2073  CA  ASP B  73      45.878  59.773  51.956  1.00 45.02           C  
ANISOU 2073  CA  ASP B  73     5450   5715   5940    869    135   1405       C  
ATOM   2074  C   ASP B  73      47.062  59.141  51.287  1.00 42.20           C  
ANISOU 2074  C   ASP B  73     5241   5525   5266    634     60   1339       C  
ATOM   2075  O   ASP B  73      47.664  59.747  50.397  1.00 43.17           O  
ANISOU 2075  O   ASP B  73     5473   5610   5318    554      4   1494       O  
ATOM   2076  CB  ASP B  73      44.696  59.743  50.960  1.00 47.85           C  
ANISOU 2076  CB  ASP B  73     5584   6212   6385    944    -82   1719       C  
ATOM   2077  CG  ASP B  73      43.360  59.708  51.643  1.00 51.66           C  
ANISOU 2077  CG  ASP B  73     5799   6655   7172   1147    -12   1744       C  
ATOM   2078  OD1 ASP B  73      42.454  60.464  51.211  1.00 58.02           O  
ANISOU 2078  OD1 ASP B  73     6414   7368   8263   1324   -102   2027       O  
ATOM   2079  OD2 ASP B  73      43.204  58.924  52.610  1.00 52.96           O  
ANISOU 2079  OD2 ASP B  73     5932   6877   7313   1135    140   1501       O  
ATOM   2080  N   PHE B  74      47.379  57.914  51.703  1.00 38.78           N  
ANISOU 2080  N   PHE B  74     4808   5263   4662    529     82   1123       N  
ATOM   2081  CA  PHE B  74      48.533  57.172  51.188  1.00 36.73           C  
ANISOU 2081  CA  PHE B  74     4660   5142   4155    332     64   1022       C  
ATOM   2082  C   PHE B  74      48.145  55.719  51.023  1.00 34.98           C  
ANISOU 2082  C   PHE B  74     4361   5152   3778    254     -1    935       C  
ATOM   2083  O   PHE B  74      48.574  54.892  51.806  1.00 32.45           O  
ANISOU 2083  O   PHE B  74     4057   4850   3421    221     76    733       O  
ATOM   2084  CB  PHE B  74      49.699  57.286  52.170  1.00 35.30           C  
ANISOU 2084  CB  PHE B  74     4588   4826   3996    286    196    805       C  
ATOM   2085  CG  PHE B  74      51.011  56.815  51.634  1.00 33.87           C  
ANISOU 2085  CG  PHE B  74     4473   4728   3668    116    211    736       C  
ATOM   2086  CD1 PHE B  74      51.936  56.262  52.478  1.00 29.31           C  
ANISOU 2086  CD1 PHE B  74     3909   4136   3089     59    262    537       C  
ATOM   2087  CD2 PHE B  74      51.323  56.934  50.284  1.00 36.42           C  
ANISOU 2087  CD2 PHE B  74     4840   5139   3858     11    183    886       C  
ATOM   2088  CE1 PHE B  74      53.143  55.833  52.023  1.00 32.23           C  
ANISOU 2088  CE1 PHE B  74     4280   4563   3400    -69    299    483       C  
ATOM   2089  CE2 PHE B  74      52.550  56.496  49.803  1.00 38.18           C  
ANISOU 2089  CE2 PHE B  74     5106   5423   3974   -138    268    806       C  
ATOM   2090  CZ  PHE B  74      53.475  55.926  50.684  1.00 32.05           C  
ANISOU 2090  CZ  PHE B  74     4286   4618   3270   -165    334    601       C  
ATOM   2091  N   PRO B  75      47.332  55.403  49.999  1.00 36.46           N  
ANISOU 2091  N   PRO B  75     4473   5506   3871    209   -164   1098       N  
ATOM   2092  CA  PRO B  75      46.818  54.029  49.896  1.00 35.15           C  
ANISOU 2092  CA  PRO B  75     4235   5531   3587    116   -230    998       C  
ATOM   2093  C   PRO B  75      47.882  53.057  49.422  1.00 34.15           C  
ANISOU 2093  C   PRO B  75     4256   5494   3223    -59   -174    828       C  
ATOM   2094  O   PRO B  75      48.743  53.421  48.577  1.00 35.48           O  
ANISOU 2094  O   PRO B  75     4563   5670   3248   -152   -146    870       O  
ATOM   2095  CB  PRO B  75      45.670  54.144  48.871  1.00 38.07           C  
ANISOU 2095  CB  PRO B  75     4489   6046   3927     88   -468   1240       C  
ATOM   2096  CG  PRO B  75      45.912  55.383  48.089  1.00 40.47           C  
ANISOU 2096  CG  PRO B  75     4877   6277   4221    118   -538   1479       C  
ATOM   2097  CD  PRO B  75      46.903  56.258  48.862  1.00 38.88           C  
ANISOU 2097  CD  PRO B  75     4783   5832   4155    211   -322   1390       C  
ATOM   2098  N   LEU B  76      47.852  51.839  49.951  1.00 32.54           N  
ANISOU 2098  N   LEU B  76     4026   5337   3000   -102   -126    646       N  
ATOM   2099  CA  LEU B  76      48.813  50.801  49.559  1.00 32.90           C  
ANISOU 2099  CA  LEU B  76     4189   5427   2883   -237    -40    472       C  
ATOM   2100  C   LEU B  76      48.083  49.761  48.723  1.00 34.73           C  
ANISOU 2100  C   LEU B  76     4434   5816   2945   -390   -148    442       C  
ATOM   2101  O   LEU B  76      46.961  49.310  49.045  1.00 34.97           O  
ANISOU 2101  O   LEU B  76     4335   5900   3052   -388   -251    466       O  
ATOM   2102  CB  LEU B  76      49.524  50.165  50.769  1.00 29.97           C  
ANISOU 2102  CB  LEU B  76     3809   4946   2630   -178     91    295       C  
ATOM   2103  CG  LEU B  76      50.406  48.922  50.529  1.00 29.65           C  
ANISOU 2103  CG  LEU B  76     3837   4909   2520   -270    191    123       C  
ATOM   2104  CD1 LEU B  76      51.747  49.259  49.890  1.00 28.37           C  
ANISOU 2104  CD1 LEU B  76     3745   4714   2319   -316    311     93       C  
ATOM   2105  CD2 LEU B  76      50.629  48.118  51.804  1.00 25.51           C  
ANISOU 2105  CD2 LEU B  76     3272   4290   2129   -201    241     18       C  
ATOM   2106  N   ARG B  77      48.707  49.374  47.626  1.00 37.32           N  
ANISOU 2106  N   ARG B  77     4926   6214   3040   -547   -111    379       N  
ATOM   2107  CA  ARG B  77      48.002  48.477  46.748  1.00 40.78           C  
ANISOU 2107  CA  ARG B  77     5428   6796   3270   -734   -233    334       C  
ATOM   2108  C   ARG B  77      48.787  47.216  46.454  1.00 41.63           C  
ANISOU 2108  C   ARG B  77     5688   6868   3260   -857    -50     73       C  
ATOM   2109  O   ARG B  77      50.003  47.248  46.155  1.00 42.80           O  
ANISOU 2109  O   ARG B  77     5950   6951   3360   -860    159    -19       O  
ATOM   2110  CB  ARG B  77      47.547  49.225  45.500  1.00 43.49           C  
ANISOU 2110  CB  ARG B  77     5859   7287   3377   -848   -427    541       C  
ATOM   2111  CG  ARG B  77      46.752  48.387  44.572  1.00 50.02           C  
ANISOU 2111  CG  ARG B  77     6770   8285   3950  -1083   -618    506       C  
ATOM   2112  CD  ARG B  77      45.645  49.184  43.925  1.00 57.67           C  
ANISOU 2112  CD  ARG B  77     7652   9405   4853  -1121   -959    811       C  
ATOM   2113  NE  ARG B  77      45.108  48.452  42.778  1.00 63.60           N  
ANISOU 2113  NE  ARG B  77     8563  10350   5251  -1419  -1176    777       N  
ATOM   2114  CZ  ARG B  77      44.287  47.404  42.866  1.00 65.87           C  
ANISOU 2114  CZ  ARG B  77     8766  10704   5555  -1564  -1310    652       C  
ATOM   2115  NH1 ARG B  77      43.850  46.818  41.751  1.00 71.45           N  
ANISOU 2115  NH1 ARG B  77     9661  11586   5899  -1877  -1533    610       N  
ATOM   2116  NH2 ARG B  77      43.894  46.945  44.055  1.00 63.51           N  
ANISOU 2116  NH2 ARG B  77     8219  10298   5614  -1425  -1225    571       N  
ATOM   2117  N   LEU B  78      48.067  46.110  46.540  1.00 42.74           N  
ANISOU 2117  N   LEU B  78     5812   7033   3393   -957   -114    -40       N  
ATOM   2118  CA  LEU B  78      48.588  44.785  46.260  1.00 44.09           C  
ANISOU 2118  CA  LEU B  78     6134   7130   3486  -1079     52   -298       C  
ATOM   2119  C   LEU B  78      47.948  44.333  44.985  1.00 47.41           C  
ANISOU 2119  C   LEU B  78     6732   7699   3581  -1351    -86   -353       C  
ATOM   2120  O   LEU B  78      46.838  43.873  45.027  1.00 50.29           O  
ANISOU 2120  O   LEU B  78     7017   8135   3954  -1461   -290   -334       O  
ATOM   2121  CB  LEU B  78      48.184  43.815  47.395  1.00 42.87           C  
ANISOU 2121  CB  LEU B  78     5854   6855   3577  -1017     76   -382       C  
ATOM   2122  CG  LEU B  78      48.934  43.603  48.709  1.00 40.65           C  
ANISOU 2122  CG  LEU B  78     5481   6393   3569   -814    235   -413       C  
ATOM   2123  CD1 LEU B  78      48.947  44.853  49.619  1.00 38.45           C  
ANISOU 2123  CD1 LEU B  78     5057   6118   3434   -622    183   -231       C  
ATOM   2124  CD2 LEU B  78      48.363  42.388  49.512  1.00 38.92           C  
ANISOU 2124  CD2 LEU B  78     5218   6069   3499   -838    246   -490       C  
ATOM   2125  N   LEU B  79      48.637  44.476  43.854  1.00 50.42           N  
ANISOU 2125  N   LEU B  79     7360   8134   3664  -1483     23   -420       N  
ATOM   2126  CA  LEU B  79      48.169  44.033  42.509  1.00 54.19           C  
ANISOU 2126  CA  LEU B  79     8104   8762   3723  -1795    -95   -505       C  
ATOM   2127  C   LEU B  79      47.615  42.606  42.356  1.00 54.40           C  
ANISOU 2127  C   LEU B  79     8234   8746   3688  -2006   -119   -759       C  
ATOM   2128  O   LEU B  79      46.646  42.389  41.607  1.00 56.30           O  
ANISOU 2128  O   LEU B  79     8568   9152   3669  -2267   -404   -741       O  
ATOM   2129  CB  LEU B  79      49.286  44.233  41.453  1.00 56.95           C  
ANISOU 2129  CB  LEU B  79     8755   9120   3761  -1895    172   -608       C  
ATOM   2130  CG  LEU B  79      50.768  43.957  41.834  1.00 59.25           C  
ANISOU 2130  CG  LEU B  79     9047   9200   4264  -1731    616   -790       C  
ATOM   2131  CD1 LEU B  79      51.201  42.539  41.466  1.00 64.04           C  
ANISOU 2131  CD1 LEU B  79     9859   9663   4809  -1855    897  -1151       C  
ATOM   2132  CD2 LEU B  79      51.781  44.974  41.171  1.00 61.21           C  
ANISOU 2132  CD2 LEU B  79     9405   9488   4363  -1719    821   -687       C  
ATOM   2133  N   SER B  80      48.276  41.654  43.016  1.00 51.33           N  
ANISOU 2133  N   SER B  80     7839   8125   3537  -1907    166   -983       N  
ATOM   2134  CA  SER B  80      47.973  40.229  42.896  1.00 52.40           C  
ANISOU 2134  CA  SER B  80     8112   8137   3658  -2093    228  -1256       C  
ATOM   2135  C   SER B  80      48.541  39.504  44.096  1.00 49.79           C  
ANISOU 2135  C   SER B  80     7635   7535   3746  -1866    462  -1342       C  
ATOM   2136  O   SER B  80      49.739  39.213  44.156  1.00 49.06           O  
ANISOU 2136  O   SER B  80     7611   7263   3764  -1734    788  -1479       O  
ATOM   2137  CB  SER B  80      48.540  39.634  41.586  1.00 56.41           C  
ANISOU 2137  CB  SER B  80     9026   8623   3781  -2342    442  -1546       C  
ATOM   2138  OG  SER B  80      48.322  38.231  41.513  1.00 56.30           O  
ANISOU 2138  OG  SER B  80     9171   8428   3792  -2515    545  -1845       O  
ATOM   2139  N   ALA B  81      47.666  39.240  45.060  1.00 48.12           N  
ANISOU 2139  N   ALA B  81     7205   7300   3777  -1820    291  -1235       N  
ATOM   2140  CA  ALA B  81      48.034  38.652  46.337  1.00 46.11           C  
ANISOU 2140  CA  ALA B  81     6808   6816   3894  -1611    444  -1238       C  
ATOM   2141  C   ALA B  81      48.770  37.333  46.212  1.00 47.99           C  
ANISOU 2141  C   ALA B  81     7234   6773   4227  -1643    730  -1511       C  
ATOM   2142  O   ALA B  81      48.318  36.419  45.526  1.00 50.00           O  
ANISOU 2142  O   ALA B  81     7687   6967   4343  -1897    739  -1721       O  
ATOM   2143  CB  ALA B  81      46.813  38.450  47.179  1.00 45.60           C  
ANISOU 2143  CB  ALA B  81     6542   6785   3997  -1642    240  -1103       C  
ATOM   2144  N   ALA B  82      49.898  37.247  46.913  1.00 46.97           N  
ANISOU 2144  N   ALA B  82     7027   6456   4360  -1383    951  -1498       N  
ATOM   2145  CA  ALA B  82      50.638  35.997  47.069  1.00 48.04           C  
ANISOU 2145  CA  ALA B  82     7263   6268   4720  -1327   1227  -1693       C  
ATOM   2146  C   ALA B  82      50.662  35.672  48.552  1.00 46.18           C  
ANISOU 2146  C   ALA B  82     6831   5879   4834  -1120   1180  -1515       C  
ATOM   2147  O   ALA B  82      50.651  36.593  49.377  1.00 42.27           O  
ANISOU 2147  O   ALA B  82     6145   5517   4398   -965   1036  -1283       O  
ATOM   2148  CB  ALA B  82      52.042  36.167  46.569  1.00 49.70           C  
ANISOU 2148  CB  ALA B  82     7519   6388   4974  -1190   1526  -1798       C  
ATOM   2149  N   PRO B  83      50.705  34.364  48.900  1.00 47.49           N  
ANISOU 2149  N   PRO B  83     7075   5747   5219  -1128   1311  -1621       N  
ATOM   2150  CA  PRO B  83      50.660  33.981  50.306  1.00 46.29           C  
ANISOU 2150  CA  PRO B  83     6783   5448   5356   -964   1251  -1421       C  
ATOM   2151  C   PRO B  83      51.683  34.681  51.200  1.00 44.11           C  
ANISOU 2151  C   PRO B  83     6322   5182   5255   -669   1239  -1216       C  
ATOM   2152  O   PRO B  83      51.399  34.905  52.387  1.00 41.23           O  
ANISOU 2152  O   PRO B  83     5844   4847   4972   -575   1090   -995       O  
ATOM   2153  CB  PRO B  83      50.942  32.475  50.263  1.00 49.20           C  
ANISOU 2153  CB  PRO B  83     7303   5432   5955   -988   1464  -1588       C  
ATOM   2154  CG  PRO B  83      50.450  32.063  48.895  1.00 51.48           C  
ANISOU 2154  CG  PRO B  83     7833   5735   5992  -1287   1542  -1894       C  
ATOM   2155  CD  PRO B  83      50.930  33.188  48.043  1.00 50.77           C  
ANISOU 2155  CD  PRO B  83     7739   5910   5640  -1273   1552  -1928       C  
ATOM   2156  N   SER B  84      52.848  35.021  50.641  1.00 44.86           N  
ANISOU 2156  N   SER B  84     6392   5257   5397   -551   1400  -1292       N  
ATOM   2157  CA  SER B  84      53.908  35.606  51.444  1.00 44.64           C  
ANISOU 2157  CA  SER B  84     6164   5221   5575   -302   1372  -1109       C  
ATOM   2158  C   SER B  84      53.617  37.084  51.739  1.00 42.11           C  
ANISOU 2158  C   SER B  84     5737   5204   5058   -298   1161   -947       C  
ATOM   2159  O   SER B  84      54.413  37.748  52.406  1.00 41.63           O  
ANISOU 2159  O   SER B  84     5525   5170   5120   -140   1095   -802       O  
ATOM   2160  CB  SER B  84      55.260  35.448  50.760  1.00 46.76           C  
ANISOU 2160  CB  SER B  84     6388   5350   6025   -183   1642  -1239       C  
ATOM   2161  OG  SER B  84      55.450  36.481  49.822  1.00 48.62           O  
ANISOU 2161  OG  SER B  84     6640   5814   6018   -266   1695  -1306       O  
ATOM   2162  N   GLN B  85      52.504  37.593  51.201  1.00 40.60           N  
ANISOU 2162  N   GLN B  85     5620   5220   4584   -479   1051   -972       N  
ATOM   2163  CA  GLN B  85      52.008  38.919  51.547  1.00 38.16           C  
ANISOU 2163  CA  GLN B  85     5216   5150   4132   -466    858   -807       C  
ATOM   2164  C   GLN B  85      51.087  38.876  52.780  1.00 36.60           C  
ANISOU 2164  C   GLN B  85     4961   4968   3978   -445    706   -651       C  
ATOM   2165  O   GLN B  85      50.578  39.919  53.201  1.00 35.15           O  
ANISOU 2165  O   GLN B  85     4701   4943   3709   -419    582   -527       O  
ATOM   2166  CB  GLN B  85      51.326  39.574  50.353  1.00 37.82           C  
ANISOU 2166  CB  GLN B  85     5248   5316   3805   -640    805   -863       C  
ATOM   2167  CG  GLN B  85      52.314  39.859  49.216  1.00 43.42           C  
ANISOU 2167  CG  GLN B  85     6040   6040   4416   -662    983   -984       C  
ATOM   2168  CD  GLN B  85      51.646  40.465  48.030  1.00 45.96           C  
ANISOU 2168  CD  GLN B  85     6484   6572   4407   -855    902  -1006       C  
ATOM   2169  OE1 GLN B  85      50.592  39.988  47.620  1.00 47.20           O  
ANISOU 2169  OE1 GLN B  85     6729   6790   4412  -1039    785  -1061       O  
ATOM   2170  NE2 GLN B  85      52.219  41.558  47.493  1.00 44.93           N  
ANISOU 2170  NE2 GLN B  85     6350   6557   4164   -832    934   -934       N  
ATOM   2171  N   THR B  86      50.863  37.668  53.313  1.00 35.71           N  
ANISOU 2171  N   THR B  86     4898   4668   4001   -463    751   -664       N  
ATOM   2172  CA  THR B  86      50.255  37.477  54.634  1.00 35.19           C  
ANISOU 2172  CA  THR B  86     4802   4571   3996   -428    668   -499       C  
ATOM   2173  C   THR B  86      51.117  38.137  55.706  1.00 34.67           C  
ANISOU 2173  C   THR B  86     4675   4505   3990   -242    597   -343       C  
ATOM   2174  O   THR B  86      52.271  37.725  55.935  1.00 36.12           O  
ANISOU 2174  O   THR B  86     4840   4535   4345   -118    626   -322       O  
ATOM   2175  CB  THR B  86      50.115  36.007  54.980  1.00 35.01           C  
ANISOU 2175  CB  THR B  86     4871   4299   4133   -475    750   -518       C  
ATOM   2176  OG1 THR B  86      49.227  35.424  54.033  1.00 38.08           O  
ANISOU 2176  OG1 THR B  86     5329   4689   4449   -696    788   -678       O  
ATOM   2177  CG2 THR B  86      49.553  35.816  56.371  1.00 35.13           C  
ANISOU 2177  CG2 THR B  86     4887   4282   4178   -452    691   -320       C  
ATOM   2178  N   SER B  87      50.562  39.133  56.385  1.00 32.32           N  
ANISOU 2178  N   SER B  87     4341   4365   3574   -226    503   -236       N  
ATOM   2179  CA  SER B  87      51.384  39.936  57.272  1.00 31.55           C  
ANISOU 2179  CA  SER B  87     4220   4288   3478    -96    416   -130       C  
ATOM   2180  C   SER B  87      50.516  40.924  57.993  1.00 29.51           C  
ANISOU 2180  C   SER B  87     3970   4168   3073   -107    371    -57       C  
ATOM   2181  O   SER B  87      49.320  40.911  57.822  1.00 29.95           O  
ANISOU 2181  O   SER B  87     4007   4296   3077   -191    416    -66       O  
ATOM   2182  CB  SER B  87      52.492  40.668  56.454  1.00 31.60           C  
ANISOU 2182  CB  SER B  87     4146   4334   3525    -39    420   -196       C  
ATOM   2183  OG  SER B  87      53.403  41.365  57.317  1.00 32.26           O  
ANISOU 2183  OG  SER B  87     4189   4419   3648     55    308   -100       O  
ATOM   2184  N   VAL B  88      51.115  41.776  58.811  1.00 28.78           N  
ANISOU 2184  N   VAL B  88     3900   4100   2933    -31    290      6       N  
ATOM   2185  CA  VAL B  88      50.419  42.959  59.352  1.00 28.44           C  
ANISOU 2185  CA  VAL B  88     3882   4164   2759    -27    292     27       C  
ATOM   2186  C   VAL B  88      51.112  44.158  58.750  1.00 28.43           C  
ANISOU 2186  C   VAL B  88     3822   4217   2763     10    243    -17       C  
ATOM   2187  O   VAL B  88      52.342  44.249  58.810  1.00 28.84           O  
ANISOU 2187  O   VAL B  88     3855   4221   2880     45    164    -13       O  
ATOM   2188  CB  VAL B  88      50.502  43.085  60.877  1.00 29.03           C  
ANISOU 2188  CB  VAL B  88     4103   4206   2720    -10    255    110       C  
ATOM   2189  CG1 VAL B  88      49.719  44.324  61.352  1.00 28.51           C  
ANISOU 2189  CG1 VAL B  88     4083   4216   2533     -3    331     83       C  
ATOM   2190  CG2 VAL B  88      49.972  41.787  61.602  1.00 27.83           C  
ANISOU 2190  CG2 VAL B  88     4046   3973   2554    -59    309    199       C  
ATOM   2191  N   TYR B  89      50.318  45.064  58.179  1.00 28.24           N  
ANISOU 2191  N   TYR B  89     3746   4280   2700      2    285    -35       N  
ATOM   2192  CA  TYR B  89      50.800  46.262  57.511  1.00 26.78           C  
ANISOU 2192  CA  TYR B  89     3521   4130   2521     25    257    -51       C  
ATOM   2193  C   TYR B  89      50.521  47.457  58.373  1.00 27.74           C  
ANISOU 2193  C   TYR B  89     3706   4234   2597     71    264    -35       C  
ATOM   2194  O   TYR B  89      49.384  47.656  58.816  1.00 27.58           O  
ANISOU 2194  O   TYR B  89     3693   4231   2554     93    347    -18       O  
ATOM   2195  CB  TYR B  89      50.100  46.452  56.179  1.00 25.77           C  
ANISOU 2195  CB  TYR B  89     3313   4092   2384    -16    277    -50       C  
ATOM   2196  CG  TYR B  89      50.483  45.360  55.236  1.00 27.62           C  
ANISOU 2196  CG  TYR B  89     3540   4328   2623    -90    297   -114       C  
ATOM   2197  CD1 TYR B  89      49.800  44.136  55.266  1.00 30.05           C  
ANISOU 2197  CD1 TYR B  89     3857   4620   2940   -155    324   -144       C  
ATOM   2198  CD2 TYR B  89      51.553  45.505  54.341  1.00 23.77           C  
ANISOU 2198  CD2 TYR B  89     3051   3833   2145   -107    326   -160       C  
ATOM   2199  CE1 TYR B  89      50.153  43.087  54.424  1.00 27.55           C  
ANISOU 2199  CE1 TYR B  89     3574   4260   2634   -233    371   -240       C  
ATOM   2200  CE2 TYR B  89      51.900  44.465  53.487  1.00 26.12           C  
ANISOU 2200  CE2 TYR B  89     3373   4105   2444   -173    405   -256       C  
ATOM   2201  CZ  TYR B  89      51.193  43.252  53.550  1.00 29.25           C  
ANISOU 2201  CZ  TYR B  89     3805   4464   2844   -233    423   -306       C  
ATOM   2202  OH  TYR B  89      51.498  42.192  52.740  1.00 28.52           O  
ANISOU 2202  OH  TYR B  89     3773   4303   2758   -308    525   -434       O  
ATOM   2203  N   PHE B  90      51.554  48.259  58.592  1.00 26.96           N  
ANISOU 2203  N   PHE B  90     3647   4088   2509     77    198    -53       N  
ATOM   2204  CA  PHE B  90      51.389  49.478  59.333  1.00 27.41           C  
ANISOU 2204  CA  PHE B  90     3802   4090   2520     98    215    -76       C  
ATOM   2205  C   PHE B  90      51.650  50.699  58.448  1.00 28.99           C  
ANISOU 2205  C   PHE B  90     3953   4265   2797    106    218    -66       C  
ATOM   2206  O   PHE B  90      52.627  50.789  57.665  1.00 26.17           O  
ANISOU 2206  O   PHE B  90     3527   3913   2500     64    167    -55       O  
ATOM   2207  CB  PHE B  90      52.309  49.487  60.558  1.00 27.42           C  
ANISOU 2207  CB  PHE B  90     3941   4033   2442     53    106   -106       C  
ATOM   2208  CG  PHE B  90      51.880  48.526  61.668  1.00 26.70           C  
ANISOU 2208  CG  PHE B  90     3972   3949   2222     40    114    -82       C  
ATOM   2209  CD1 PHE B  90      50.939  48.913  62.641  1.00 24.78           C  
ANISOU 2209  CD1 PHE B  90     3893   3685   1835     43    248   -120       C  
ATOM   2210  CD2 PHE B  90      52.435  47.263  61.752  1.00 25.96           C  
ANISOU 2210  CD2 PHE B  90     3841   3860   2160     27     19    -15       C  
ATOM   2211  CE1 PHE B  90      50.578  48.057  63.679  1.00 27.20           C  
ANISOU 2211  CE1 PHE B  90     4346   3999   1988      6    282    -81       C  
ATOM   2212  CE2 PHE B  90      52.086  46.385  62.786  1.00 27.48           C  
ANISOU 2212  CE2 PHE B  90     4172   4040   2229      4     18     45       C  
ATOM   2213  CZ  PHE B  90      51.146  46.785  63.754  1.00 27.15           C  
ANISOU 2213  CZ  PHE B  90     4315   4001   1998    -18    150     17       C  
ATOM   2214  N   CYS B  91      50.749  51.660  58.594  1.00 29.99           N  
ANISOU 2214  N   CYS B  91     4111   4342   2940    167    307    -59       N  
ATOM   2215  CA  CYS B  91      50.975  52.954  57.971  1.00 30.81           C  
ANISOU 2215  CA  CYS B  91     4210   4368   3129    182    312    -28       C  
ATOM   2216  C   CYS B  91      51.479  53.870  59.115  1.00 30.46           C  
ANISOU 2216  C   CYS B  91     4341   4173   3058    155    320   -132       C  
ATOM   2217  O   CYS B  91      50.942  53.815  60.235  1.00 28.90           O  
ANISOU 2217  O   CYS B  91     4271   3935   2772    176    397   -209       O  
ATOM   2218  CB  CYS B  91      49.635  53.482  57.412  1.00 31.78           C  
ANISOU 2218  CB  CYS B  91     4245   4492   3339    285    395     65       C  
ATOM   2219  SG  CYS B  91      49.841  55.095  56.588  1.00 40.85           S  
ANISOU 2219  SG  CYS B  91     5403   5504   4615    320    395    162       S  
ATOM   2220  N   ALA B  92      52.478  54.708  58.819  1.00 29.34           N  
ANISOU 2220  N   ALA B  92     4221   3946   2979     83    256   -141       N  
ATOM   2221  CA  ALA B  92      53.021  55.666  59.791  1.00 31.09           C  
ANISOU 2221  CA  ALA B  92     4624   4009   3180     10    235   -257       C  
ATOM   2222  C   ALA B  92      53.236  57.076  59.201  1.00 32.66           C  
ANISOU 2222  C   ALA B  92     4847   4036   3526     -3    282   -232       C  
ATOM   2223  O   ALA B  92      53.459  57.250  58.010  1.00 31.87           O  
ANISOU 2223  O   ALA B  92     4619   3966   3524     -2    276   -105       O  
ATOM   2224  CB  ALA B  92      54.332  55.132  60.379  1.00 30.66           C  
ANISOU 2224  CB  ALA B  92     4581   4001   3065   -130     44   -304       C  
ATOM   2225  N   SER B  93      53.159  58.090  60.035  1.00 35.61           N  
ANISOU 2225  N   SER B  93     5418   4210   3900    -28    344   -354       N  
ATOM   2226  CA  SER B  93      53.348  59.429  59.538  1.00 38.56           C  
ANISOU 2226  CA  SER B  93     5838   4371   4442    -44    400   -328       C  
ATOM   2227  C   SER B  93      54.178  60.275  60.502  1.00 41.40           C  
ANISOU 2227  C   SER B  93     6418   4537   4773   -220    347   -512       C  
ATOM   2228  O   SER B  93      54.346  59.923  61.691  1.00 41.75           O  
ANISOU 2228  O   SER B  93     6627   4608   4626   -306    284   -671       O  
ATOM   2229  CB  SER B  93      51.995  60.089  59.208  1.00 39.51           C  
ANISOU 2229  CB  SER B  93     5953   4361   4697    159    595   -251       C  
ATOM   2230  OG  SER B  93      51.390  60.734  60.324  1.00 42.50           O  
ANISOU 2230  OG  SER B  93     6543   4535   5070    214    767   -425       O  
ATOM   2231  N   ARG B  94      54.721  61.363  59.964  1.00 43.29           N  
ANISOU 2231  N   ARG B  94     6676   4586   5184   -301    354   -478       N  
ATOM   2232  CA  ARG B  94      55.438  62.368  60.753  1.00 47.11           C  
ANISOU 2232  CA  ARG B  94     7382   4832   5683   -495    313   -660       C  
ATOM   2233  C   ARG B  94      55.450  63.720  60.049  1.00 49.09           C  
ANISOU 2233  C   ARG B  94     7680   4790   6180   -498    433   -590       C  
ATOM   2234  O   ARG B  94      55.427  63.764  58.830  1.00 46.63           O  
ANISOU 2234  O   ARG B  94     7187   4526   6002   -430    458   -362       O  
ATOM   2235  CB  ARG B  94      56.857  61.927  61.087  1.00 47.16           C  
ANISOU 2235  CB  ARG B  94     7318   4968   5632   -745     48   -706       C  
ATOM   2236  CG  ARG B  94      57.838  61.994  59.958  1.00 48.84           C  
ANISOU 2236  CG  ARG B  94     7278   5235   6043   -841    -19   -539       C  
ATOM   2237  CD  ARG B  94      59.227  61.958  60.552  1.00 55.16           C  
ANISOU 2237  CD  ARG B  94     8026   6064   6865  -1113   -268   -624       C  
ATOM   2238  NE  ARG B  94      60.118  61.185  59.710  1.00 54.13           N  
ANISOU 2238  NE  ARG B  94     7559   6140   6868  -1143   -342   -464       N  
ATOM   2239  CZ  ARG B  94      60.950  61.721  58.836  1.00 55.04           C  
ANISOU 2239  CZ  ARG B  94     7506   6196   7209  -1270   -301   -362       C  
ATOM   2240  NH1 ARG B  94      61.000  63.040  58.703  1.00 54.59           N  
ANISOU 2240  NH1 ARG B  94     7598   5871   7271  -1386   -220   -387       N  
ATOM   2241  NH2 ARG B  94      61.714  60.931  58.095  1.00 55.25           N  
ANISOU 2241  NH2 ARG B  94     7226   6411   7353  -1277   -307   -236       N  
ATOM   2242  N   PRO B  95      55.483  64.827  60.824  1.00 53.60           N  
ANISOU 2242  N   PRO B  95     8529   5041   6795   -592    513   -786       N  
ATOM   2243  CA  PRO B  95      55.377  66.191  60.234  1.00 57.85           C  
ANISOU 2243  CA  PRO B  95     9151   5223   7606   -574    661   -717       C  
ATOM   2244  C   PRO B  95      56.211  66.423  58.955  1.00 59.34           C  
ANISOU 2244  C   PRO B  95     9136   5444   7967   -680    578   -469       C  
ATOM   2245  O   PRO B  95      55.763  67.161  58.057  1.00 60.18           O  
ANISOU 2245  O   PRO B  95     9225   5367   8271   -560    707   -265       O  
ATOM   2246  CB  PRO B  95      55.820  67.111  61.379  1.00 61.02           C  
ANISOU 2246  CB  PRO B  95     9891   5315   7977   -791    675  -1028       C  
ATOM   2247  CG  PRO B  95      55.410  66.365  62.617  1.00 59.66           C  
ANISOU 2247  CG  PRO B  95     9880   5293   7494   -778    667  -1252       C  
ATOM   2248  CD  PRO B  95      55.600  64.877  62.295  1.00 54.98           C  
ANISOU 2248  CD  PRO B  95     8995   5144   6749   -733    479  -1087       C  
ATOM   2249  N   GLY B  96      57.390  65.792  58.881  1.00 60.63           N  
ANISOU 2249  N   GLY B  96     9140   5831   8062   -896    379   -468       N  
ATOM   2250  CA  GLY B  96      58.156  65.661  57.632  1.00 62.58           C  
ANISOU 2250  CA  GLY B  96     9147   6202   8428   -978    349   -232       C  
ATOM   2251  C   GLY B  96      59.230  66.699  57.340  1.00 67.61           C  
ANISOU 2251  C   GLY B  96     9802   6607   9278  -1248    340   -209       C  
ATOM   2252  O   GLY B  96      59.421  67.073  56.183  1.00 68.25           O  
ANISOU 2252  O   GLY B  96     9791   6649   9490  -1259    441     26       O  
ATOM   2253  N   LEU B  97      59.937  67.147  58.380  1.00 71.74           N  
ANISOU 2253  N   LEU B  97    10454   6982   9819  -1492    212   -446       N  
ATOM   2254  CA  LEU B  97      61.105  68.087  58.273  1.00 77.00           C  
ANISOU 2254  CA  LEU B  97    11114   7431  10710  -1825    159   -462       C  
ATOM   2255  C   LEU B  97      60.829  69.558  57.926  1.00 80.70           C  
ANISOU 2255  C   LEU B  97    11812   7448  11399  -1862    348   -417       C  
ATOM   2256  O   LEU B  97      61.751  70.378  57.947  1.00 84.13           O  
ANISOU 2256  O   LEU B  97    12274   7663  12028  -2166    310   -456       O  
ATOM   2257  CB  LEU B  97      62.259  67.524  57.406  1.00 76.57           C  
ANISOU 2257  CB  LEU B  97    10692   7625  10773  -1975     96   -277       C  
ATOM   2258  CG  LEU B  97      63.263  66.550  58.052  1.00 77.84           C  
ANISOU 2258  CG  LEU B  97    10609   8072  10894  -2133   -167   -379       C  
ATOM   2259  CD1 LEU B  97      64.596  66.625  57.297  1.00 80.54           C  
ANISOU 2259  CD1 LEU B  97    10618   8474  11510  -2373   -168   -234       C  
ATOM   2260  CD2 LEU B  97      63.485  66.815  59.561  1.00 79.67           C  
ANISOU 2260  CD2 LEU B  97    11054   8198  11017  -2328   -418   -668       C  
ATOM   2261  N   ALA B  98      59.581  69.878  57.587  1.00 81.43           N  
ANISOU 2261  N   ALA B  98    12044   7394  11502  -1558    545   -314       N  
ATOM   2262  CA  ALA B  98      59.093  71.257  57.646  1.00 85.87           C  
ANISOU 2262  CA  ALA B  98    12887   7458  12278  -1531    726   -335       C  
ATOM   2263  C   ALA B  98      58.444  71.463  59.025  1.00 87.95           C  
ANISOU 2263  C   ALA B  98    13450   7537  12430  -1471    769   -690       C  
ATOM   2264  O   ALA B  98      58.452  72.578  59.581  1.00 91.69           O  
ANISOU 2264  O   ALA B  98    14222   7568  13047  -1588    874   -884       O  
ATOM   2265  CB  ALA B  98      58.103  71.547  56.522  1.00 85.76           C  
ANISOU 2265  CB  ALA B  98    12836   7361  12385  -1222    903      5       C  
ATOM   2266  N   GLY B  99      57.907  70.367  59.577  1.00 85.56           N  
ANISOU 2266  N   GLY B  99    13087   7562  11860  -1308    711   -785       N  
ATOM   2267  CA  GLY B  99      57.359  70.341  60.940  1.00 87.32           C  
ANISOU 2267  CA  GLY B  99    13594   7693  11889  -1281    762  -1127       C  
ATOM   2268  C   GLY B  99      58.246  69.765  62.047  1.00 87.98           C  
ANISOU 2268  C   GLY B  99    13756   7980  11693  -1584    493  -1392       C  
ATOM   2269  O   GLY B  99      57.746  69.482  63.151  1.00 88.95           O  
ANISOU 2269  O   GLY B  99    14115   8123  11556  -1555    524  -1643       O  
ATOM   2270  N   GLY B 100      59.536  69.546  61.738  1.00 87.89           N  
ANISOU 2270  N   GLY B 100    13527   8132  11732  -1867    234  -1312       N  
ATOM   2271  CA  GLY B 100      60.611  69.344  62.743  1.00 89.25           C  
ANISOU 2271  CA  GLY B 100    13763   8407  11741  -2234    -84  -1536       C  
ATOM   2272  C   GLY B 100      60.922  67.969  63.338  1.00 86.72           C  
ANISOU 2272  C   GLY B 100    13286   8524  11137  -2248   -357  -1544       C  
ATOM   2273  O   GLY B 100      61.980  67.386  63.057  1.00 86.43           O  
ANISOU 2273  O   GLY B 100    12925   8733  11180  -2406   -611  -1413       O  
ATOM   2274  N   ARG B 101      60.011  67.466  64.176  1.00 85.15           N  
ANISOU 2274  N   ARG B 101    13314   8403  10636  -2082   -284  -1688       N  
ATOM   2275  CA  ARG B 101      60.256  66.273  65.005  1.00 83.18           C  
ANISOU 2275  CA  ARG B 101    13032   8502  10070  -2132   -550  -1725       C  
ATOM   2276  C   ARG B 101      60.376  64.946  64.229  1.00 77.77           C  
ANISOU 2276  C   ARG B 101    11914   8197   9437  -1934   -631  -1434       C  
ATOM   2277  O   ARG B 101      59.659  64.732  63.245  1.00 75.25           O  
ANISOU 2277  O   ARG B 101    11429   7913   9249  -1654   -394  -1251       O  
ATOM   2278  CB  ARG B 101      59.192  66.159  66.102  1.00 84.05           C  
ANISOU 2278  CB  ARG B 101    13542   8561   9830  -2023   -384  -1953       C  
ATOM   2279  CG  ARG B 101      59.575  65.230  67.251  1.00 85.82           C  
ANISOU 2279  CG  ARG B 101    13887   9059   9661  -2188   -695  -2041       C  
ATOM   2280  CD  ARG B 101      60.674  65.824  68.151  1.00 90.53           C  
ANISOU 2280  CD  ARG B 101    14714   9563  10119  -2638  -1047  -2255       C  
ATOM   2281  NE  ARG B 101      60.220  67.005  68.882  1.00 95.11           N  
ANISOU 2281  NE  ARG B 101    15814   9764  10558  -2778   -831  -2605       N  
ATOM   2282  CZ  ARG B 101      59.466  66.980  69.982  1.00 97.39           C  
ANISOU 2282  CZ  ARG B 101    16568  10000  10435  -2779   -675  -2860       C  
ATOM   2283  NH1 ARG B 101      59.056  65.825  70.500  1.00 94.61           N  
ANISOU 2283  NH1 ARG B 101    16225   9961   9760  -2656   -728  -2777       N  
ATOM   2284  NH2 ARG B 101      59.119  68.122  70.570  1.00101.12           N  
ANISOU 2284  NH2 ARG B 101    17517  10082  10821  -2911   -433  -3206       N  
ATOM   2285  N   PRO B 102      61.303  64.064  64.670  1.00 76.62           N  
ANISOU 2285  N   PRO B 102    11591   8319   9199  -2091   -980  -1388       N  
ATOM   2286  CA  PRO B 102      61.525  62.686  64.136  1.00 72.05           C  
ANISOU 2286  CA  PRO B 102    10633   8076   8664  -1923  -1074  -1150       C  
ATOM   2287  C   PRO B 102      60.603  61.535  64.619  1.00 67.64           C  
ANISOU 2287  C   PRO B 102    10157   7716   7823  -1691  -1025  -1126       C  
ATOM   2288  O   PRO B 102      60.690  60.433  64.064  1.00 64.83           O  
ANISOU 2288  O   PRO B 102     9507   7585   7538  -1536  -1051   -938       O  
ATOM   2289  CB  PRO B 102      62.982  62.395  64.537  1.00 74.76           C  
ANISOU 2289  CB  PRO B 102    10754   8553   9096  -2209  -1487  -1113       C  
ATOM   2290  CG  PRO B 102      63.202  63.253  65.769  1.00 79.75           C  
ANISOU 2290  CG  PRO B 102    11780   9012   9509  -2521  -1685  -1376       C  
ATOM   2291  CD  PRO B 102      62.451  64.518  65.485  1.00 80.65           C  
ANISOU 2291  CD  PRO B 102    12184   8780   9679  -2487  -1335  -1530       C  
ATOM   2292  N   GLU B 103      59.755  61.774  65.628  1.00 66.89           N  
ANISOU 2292  N   GLU B 103    10464   7525   7425  -1681   -926  -1322       N  
ATOM   2293  CA  GLU B 103      58.753  60.780  66.088  1.00 63.09           C  
ANISOU 2293  CA  GLU B 103    10083   7201   6685  -1472   -809  -1299       C  
ATOM   2294  C   GLU B 103      57.813  60.293  64.970  1.00 58.34           C  
ANISOU 2294  C   GLU B 103     9242   6667   6256  -1149   -523  -1124       C  
ATOM   2295  O   GLU B 103      57.101  61.093  64.331  1.00 57.54           O  
ANISOU 2295  O   GLU B 103     9162   6384   6314  -1015   -250  -1131       O  
ATOM   2296  CB  GLU B 103      57.904  61.316  67.252  1.00 65.17           C  
ANISOU 2296  CB  GLU B 103    10832   7304   6623  -1512   -634  -1558       C  
ATOM   2297  CG  GLU B 103      56.660  60.419  67.634  1.00 62.70           C  
ANISOU 2297  CG  GLU B 103    10614   7118   6090  -1278   -397  -1530       C  
ATOM   2298  CD  GLU B 103      56.218  60.546  69.124  1.00 64.30           C  
ANISOU 2298  CD  GLU B 103    11318   7265   5847  -1413   -329  -1772       C  
ATOM   2299  OE1 GLU B 103      56.643  61.540  69.783  1.00 65.62           O  
ANISOU 2299  OE1 GLU B 103    11814   7235   5883  -1656   -387  -2013       O  
ATOM   2300  OE2 GLU B 103      55.463  59.646  69.625  1.00 59.37           O  
ANISOU 2300  OE2 GLU B 103    10778   6787   4990  -1299   -207  -1727       O  
ATOM   2301  N   GLN B 104      57.784  58.979  64.758  1.00 54.30           N  
ANISOU 2301  N   GLN B 104     8516   6401   5712  -1031   -601   -962       N  
ATOM   2302  CA  GLN B 104      56.848  58.422  63.791  1.00 48.98           C  
ANISOU 2302  CA  GLN B 104     7652   5806   5149   -768   -366   -821       C  
ATOM   2303  C   GLN B 104      55.581  57.952  64.510  1.00 46.95           C  
ANISOU 2303  C   GLN B 104     7592   5580   4666   -632   -178   -880       C  
ATOM   2304  O   GLN B 104      55.671  57.239  65.474  1.00 47.04           O  
ANISOU 2304  O   GLN B 104     7741   5694   4435   -701   -299   -910       O  
ATOM   2305  CB  GLN B 104      57.520  57.336  62.965  1.00 46.94           C  
ANISOU 2305  CB  GLN B 104     7048   5751   5036   -726   -497   -632       C  
ATOM   2306  CG  GLN B 104      57.207  57.463  61.491  1.00 46.70           C  
ANISOU 2306  CG  GLN B 104     6799   5723   5220   -590   -311   -505       C  
ATOM   2307  CD  GLN B 104      58.279  56.919  60.602  1.00 45.28           C  
ANISOU 2307  CD  GLN B 104     6319   5657   5228   -634   -406   -380       C  
ATOM   2308  OE1 GLN B 104      59.359  57.512  60.448  1.00 50.30           O  
ANISOU 2308  OE1 GLN B 104     6859   6231   6021   -795   -507   -380       O  
ATOM   2309  NE2 GLN B 104      57.998  55.806  59.991  1.00 39.65           N  
ANISOU 2309  NE2 GLN B 104     5449   5093   4521   -504   -346   -285       N  
ATOM   2310  N   TYR B 105      54.411  58.408  64.057  1.00 44.91           N  
ANISOU 2310  N   TYR B 105     7339   5221   4504   -446    118   -881       N  
ATOM   2311  CA  TYR B 105      53.096  57.968  64.558  1.00 43.18           C  
ANISOU 2311  CA  TYR B 105     7215   5031   4157   -293    356   -910       C  
ATOM   2312  C   TYR B 105      52.520  56.847  63.688  1.00 39.15           C  
ANISOU 2312  C   TYR B 105     6410   4718   3744   -135    384   -716       C  
ATOM   2313  O   TYR B 105      52.390  57.009  62.467  1.00 36.95           O  
ANISOU 2313  O   TYR B 105     5903   4450   3684    -43    407   -587       O  
ATOM   2314  CB  TYR B 105      52.104  59.132  64.582  1.00 45.22           C  
ANISOU 2314  CB  TYR B 105     7599   5046   4537   -167    672  -1013       C  
ATOM   2315  CG  TYR B 105      52.498  60.284  65.509  1.00 51.64           C  
ANISOU 2315  CG  TYR B 105     8771   5606   5242   -326    715  -1261       C  
ATOM   2316  CD1 TYR B 105      52.180  60.260  66.855  1.00 57.14           C  
ANISOU 2316  CD1 TYR B 105     9822   6260   5627   -411    833  -1471       C  
ATOM   2317  CD2 TYR B 105      53.173  61.397  65.020  1.00 55.88           C  
ANISOU 2317  CD2 TYR B 105     9320   5935   5975   -413    654  -1291       C  
ATOM   2318  CE1 TYR B 105      52.531  61.337  67.705  1.00 63.59           C  
ANISOU 2318  CE1 TYR B 105    11024   6827   6308   -590    881  -1740       C  
ATOM   2319  CE2 TYR B 105      53.522  62.471  65.847  1.00 60.85           C  
ANISOU 2319  CE2 TYR B 105    10300   6299   6519   -587    696  -1544       C  
ATOM   2320  CZ  TYR B 105      53.205  62.423  67.181  1.00 64.85           C  
ANISOU 2320  CZ  TYR B 105    11176   6769   6695   -678    802  -1780       C  
ATOM   2321  OH  TYR B 105      53.563  63.466  67.998  1.00 71.57           O  
ANISOU 2321  OH  TYR B 105    12421   7351   7422   -884    842  -2065       O  
ATOM   2322  N   PHE B 106      52.153  55.733  64.327  1.00 37.34           N  
ANISOU 2322  N   PHE B 106     6221   4632   3334   -128    384   -695       N  
ATOM   2323  CA  PHE B 106      51.704  54.504  63.630  1.00 34.08           C  
ANISOU 2323  CA  PHE B 106     5562   4394   2991    -29    382   -535       C  
ATOM   2324  C   PHE B 106      50.178  54.319  63.641  1.00 34.45           C  
ANISOU 2324  C   PHE B 106     5562   4450   3075    117    656   -515       C  
ATOM   2325  O   PHE B 106      49.544  54.546  64.658  1.00 35.09           O  
ANISOU 2325  O   PHE B 106     5848   4463   3021    122    848   -622       O  
ATOM   2326  CB  PHE B 106      52.364  53.265  64.290  1.00 33.06           C  
ANISOU 2326  CB  PHE B 106     5477   4394   2687   -125    184   -486       C  
ATOM   2327  CG  PHE B 106      53.796  53.007  63.828  1.00 31.20           C  
ANISOU 2327  CG  PHE B 106     5094   4205   2555   -212    -94   -419       C  
ATOM   2328  CD1 PHE B 106      54.859  53.694  64.384  1.00 31.05           C  
ANISOU 2328  CD1 PHE B 106     5187   4122   2488   -364   -290   -490       C  
ATOM   2329  CD2 PHE B 106      54.049  52.102  62.799  1.00 31.11           C  
ANISOU 2329  CD2 PHE B 106     4820   4289   2710   -149   -136   -297       C  
ATOM   2330  CE1 PHE B 106      56.152  53.482  63.939  1.00 34.11           C  
ANISOU 2330  CE1 PHE B 106     5371   4551   3035   -438   -523   -413       C  
ATOM   2331  CE2 PHE B 106      55.342  51.879  62.342  1.00 29.21           C  
ANISOU 2331  CE2 PHE B 106     4410   4073   2613   -206   -322   -242       C  
ATOM   2332  CZ  PHE B 106      56.404  52.564  62.926  1.00 28.56           C  
ANISOU 2332  CZ  PHE B 106     4386   3938   2526   -344   -518   -286       C  
ATOM   2333  N   GLY B 107      49.607  53.865  62.526  1.00 33.14           N  
ANISOU 2333  N   GLY B 107     5127   4377   3087    215    675   -380       N  
ATOM   2334  CA  GLY B 107      48.198  53.481  62.484  1.00 33.34           C  
ANISOU 2334  CA  GLY B 107     5031   4447   3186    326    878   -328       C  
ATOM   2335  C   GLY B 107      47.978  52.194  63.232  1.00 34.11           C  
ANISOU 2335  C   GLY B 107     5189   4653   3116    263    896   -316       C  
ATOM   2336  O   GLY B 107      48.925  51.617  63.754  1.00 34.82           O  
ANISOU 2336  O   GLY B 107     5416   4776   3036    154    730   -329       O  
ATOM   2337  N   PRO B 108      46.723  51.713  63.312  1.00 35.25           N  
ANISOU 2337  N   PRO B 108     5216   4846   3331    325   1092   -269       N  
ATOM   2338  CA  PRO B 108      46.603  50.548  64.214  1.00 34.97           C  
ANISOU 2338  CA  PRO B 108     5304   4878   3105    235   1132   -256       C  
ATOM   2339  C   PRO B 108      46.886  49.242  63.506  1.00 32.78           C  
ANISOU 2339  C   PRO B 108     4873   4710   2871    179    949   -143       C  
ATOM   2340  O   PRO B 108      46.784  48.180  64.101  1.00 33.32           O  
ANISOU 2340  O   PRO B 108     5018   4810   2829    109    966    -96       O  
ATOM   2341  CB  PRO B 108      45.149  50.611  64.725  1.00 36.82           C  
ANISOU 2341  CB  PRO B 108     5483   5096   3409    302   1474   -265       C  
ATOM   2342  CG  PRO B 108      44.429  51.585  63.837  1.00 39.35           C  
ANISOU 2342  CG  PRO B 108     5549   5368   4033    452   1556   -238       C  
ATOM   2343  CD  PRO B 108      45.411  52.254  62.879  1.00 35.50           C  
ANISOU 2343  CD  PRO B 108     5032   4851   3606    463   1299   -223       C  
ATOM   2344  N   GLY B 109      47.241  49.294  62.241  1.00 30.45           N  
ANISOU 2344  N   GLY B 109     4387   4454   2728    202    794    -99       N  
ATOM   2345  CA  GLY B 109      47.555  48.045  61.561  1.00 29.08           C  
ANISOU 2345  CA  GLY B 109     4108   4352   2586    141    660    -34       C  
ATOM   2346  C   GLY B 109      46.356  47.391  60.869  1.00 29.83           C  
ANISOU 2346  C   GLY B 109     3996   4524   2813    130    733     25       C  
ATOM   2347  O   GLY B 109      45.204  47.586  61.247  1.00 30.69           O  
ANISOU 2347  O   GLY B 109     4030   4643   2987    161    909     45       O  
ATOM   2348  N   THR B 110      46.680  46.625  59.836  1.00 28.50           N  
ANISOU 2348  N   THR B 110     3731   4404   2694     72    602     45       N  
ATOM   2349  CA  THR B 110      45.758  45.896  59.015  1.00 28.69           C  
ANISOU 2349  CA  THR B 110     3582   4504   2815      5    598     82       C  
ATOM   2350  C   THR B 110      46.311  44.480  58.889  1.00 28.90           C  
ANISOU 2350  C   THR B 110     3676   4493   2812    -91    542     60       C  
ATOM   2351  O   THR B 110      47.436  44.266  58.378  1.00 25.28           O  
ANISOU 2351  O   THR B 110     3273   3999   2333    -92    446     18       O  
ATOM   2352  CB  THR B 110      45.665  46.506  57.597  1.00 28.68           C  
ANISOU 2352  CB  THR B 110     3442   4582   2872      8    479    105       C  
ATOM   2353  OG1 THR B 110      45.064  47.802  57.699  1.00 28.48           O  
ANISOU 2353  OG1 THR B 110     3334   4554   2931    121    533    159       O  
ATOM   2354  CG2 THR B 110      44.776  45.586  56.708  1.00 28.60           C  
ANISOU 2354  CG2 THR B 110     3284   4666   2916   -119    415    130       C  
ATOM   2355  N   ARG B 111      45.547  43.529  59.422  1.00 29.46           N  
ANISOU 2355  N   ARG B 111     3740   4543   2908   -167    634     93       N  
ATOM   2356  CA  ARG B 111      45.962  42.152  59.315  1.00 30.75           C  
ANISOU 2356  CA  ARG B 111     3975   4622   3085   -256    602     81       C  
ATOM   2357  C   ARG B 111      45.398  41.496  58.051  1.00 31.03           C  
ANISOU 2357  C   ARG B 111     3885   4700   3201   -385    550     31       C  
ATOM   2358  O   ARG B 111      44.202  41.550  57.763  1.00 32.58           O  
ANISOU 2358  O   ARG B 111     3922   4987   3468   -463    567     60       O  
ATOM   2359  CB  ARG B 111      45.668  41.358  60.589  1.00 31.56           C  
ANISOU 2359  CB  ARG B 111     4200   4638   3152   -296    716    158       C  
ATOM   2360  CG  ARG B 111      46.272  39.980  60.496  1.00 34.99           C  
ANISOU 2360  CG  ARG B 111     4726   4930   3637   -357    671    168       C  
ATOM   2361  CD  ARG B 111      46.338  39.281  61.871  1.00 39.02           C  
ANISOU 2361  CD  ARG B 111     5421   5329   4076   -373    738    296       C  
ATOM   2362  NE  ARG B 111      46.960  37.952  61.731  1.00 42.46           N  
ANISOU 2362  NE  ARG B 111     5933   5581   4617   -403    688    332       N  
ATOM   2363  CZ  ARG B 111      47.122  37.088  62.729  1.00 43.75           C  
ANISOU 2363  CZ  ARG B 111     6263   5603   4756   -424    710    481       C  
ATOM   2364  NH1 ARG B 111      46.691  37.388  63.949  1.00 43.55           N  
ANISOU 2364  NH1 ARG B 111     6374   5625   4547   -447    791    596       N  
ATOM   2365  NH2 ARG B 111      47.689  35.916  62.504  1.00 45.84           N  
ANISOU 2365  NH2 ARG B 111     6578   5662   5175   -427    671    519       N  
ATOM   2366  N   LEU B 112      46.286  40.876  57.302  1.00 31.69           N  
ANISOU 2366  N   LEU B 112     4040   4716   3282   -415    487    -49       N  
ATOM   2367  CA  LEU B 112      45.967  40.336  55.984  1.00 33.47           C  
ANISOU 2367  CA  LEU B 112     4222   4977   3515   -560    432   -144       C  
ATOM   2368  C   LEU B 112      46.346  38.866  55.943  1.00 33.83           C  
ANISOU 2368  C   LEU B 112     4387   4838   3628   -647    490   -220       C  
ATOM   2369  O   LEU B 112      47.483  38.522  56.210  1.00 35.01           O  
ANISOU 2369  O   LEU B 112     4637   4849   3815   -546    523   -235       O  
ATOM   2370  CB  LEU B 112      46.769  41.146  54.948  1.00 32.64           C  
ANISOU 2370  CB  LEU B 112     4132   4946   3323   -512    362   -203       C  
ATOM   2371  CG  LEU B 112      46.340  41.260  53.482  1.00 38.00           C  
ANISOU 2371  CG  LEU B 112     4783   5751   3905   -654    268   -266       C  
ATOM   2372  CD1 LEU B 112      44.857  41.137  53.363  1.00 42.46           C  
ANISOU 2372  CD1 LEU B 112     5199   6425   4509   -786    183   -205       C  
ATOM   2373  CD2 LEU B 112      46.821  42.568  52.786  1.00 40.77           C  
ANISOU 2373  CD2 LEU B 112     5123   6213   4153   -578    205   -226       C  
ATOM   2374  N   THR B 113      45.409  37.995  55.640  1.00 34.57           N  
ANISOU 2374  N   THR B 113     4454   4908   3772   -832    499   -257       N  
ATOM   2375  CA  THR B 113      45.723  36.610  55.400  1.00 35.37           C  
ANISOU 2375  CA  THR B 113     4689   4796   3953   -937    564   -359       C  
ATOM   2376  C   THR B 113      45.379  36.210  53.953  1.00 37.42           C  
ANISOU 2376  C   THR B 113     4977   5094   4145  -1149    506   -542       C  
ATOM   2377  O   THR B 113      44.218  36.338  53.531  1.00 39.07           O  
ANISOU 2377  O   THR B 113     5064   5454   4324  -1327    400   -533       O  
ATOM   2378  CB  THR B 113      45.019  35.722  56.412  1.00 36.19           C  
ANISOU 2378  CB  THR B 113     4804   4769   4174  -1017    648   -258       C  
ATOM   2379  OG1 THR B 113      45.601  35.964  57.697  1.00 36.35           O  
ANISOU 2379  OG1 THR B 113     4887   4730   4193   -834    697   -104       O  
ATOM   2380  CG2 THR B 113      45.189  34.270  56.103  1.00 36.65           C  
ANISOU 2380  CG2 THR B 113     5004   4569   4351  -1150    720   -361       C  
ATOM   2381  N   VAL B 114      46.381  35.713  53.208  1.00 36.83           N  
ANISOU 2381  N   VAL B 114     5061   4882   4050  -1140    579   -707       N  
ATOM   2382  CA  VAL B 114      46.185  35.282  51.816  1.00 37.29           C  
ANISOU 2382  CA  VAL B 114     5231   4957   3978  -1364    557   -922       C  
ATOM   2383  C   VAL B 114      46.072  33.779  51.811  1.00 39.73           C  
ANISOU 2383  C   VAL B 114     5688   4982   4424  -1517    673  -1061       C  
ATOM   2384  O   VAL B 114      46.989  33.104  52.280  1.00 40.44           O  
ANISOU 2384  O   VAL B 114     5872   4806   4684  -1368    836  -1077       O  
ATOM   2385  CB  VAL B 114      47.399  35.728  50.928  1.00 37.62           C  
ANISOU 2385  CB  VAL B 114     5385   5010   3897  -1266    640  -1047       C  
ATOM   2386  CG1 VAL B 114      47.324  35.115  49.490  1.00 39.32           C  
ANISOU 2386  CG1 VAL B 114     5810   5202   3926  -1520    679  -1313       C  
ATOM   2387  CG2 VAL B 114      47.514  37.247  50.869  1.00 32.51           C  
ANISOU 2387  CG2 VAL B 114     4610   4615   3124  -1140    527   -902       C  
ATOM   2388  N   THR B 115      44.962  33.234  51.306  1.00 41.65           N  
ANISOU 2388  N   THR B 115     5940   5259   4626  -1816    579  -1147       N  
ATOM   2389  CA  THR B 115      44.789  31.787  51.263  1.00 44.35           C  
ANISOU 2389  CA  THR B 115     6445   5297   5109  -2004    694  -1299       C  
ATOM   2390  C   THR B 115      44.538  31.219  49.837  1.00 48.56           C  
ANISOU 2390  C   THR B 115     7183   5808   5457  -2325    661  -1605       C  
ATOM   2391  O   THR B 115      44.115  31.974  48.947  1.00 48.65           O  
ANISOU 2391  O   THR B 115     7162   6113   5209  -2461    469  -1638       O  
ATOM   2392  CB  THR B 115      43.698  31.338  52.238  1.00 45.74           C  
ANISOU 2392  CB  THR B 115     6477   5436   5465  -2117    658  -1128       C  
ATOM   2393  OG1 THR B 115      43.519  29.924  52.107  1.00 47.90           O  
ANISOU 2393  OG1 THR B 115     6929   5385   5884  -2334    767  -1281       O  
ATOM   2394  CG2 THR B 115      42.349  32.076  51.997  1.00 44.26           C  
ANISOU 2394  CG2 THR B 115     6036   5587   5191  -2302    428  -1030       C  
ATOM   2395  N   GLU B 116      44.814  29.921  49.613  1.00 56.46           N  
ANISOU 2395  N   GLU B 116     6820  10134   4496   -589    997  -2609       N  
ATOM   2396  CA  GLU B 116      44.591  29.315  48.280  1.00 60.56           C  
ANISOU 2396  CA  GLU B 116     7422  10836   4750   -606   1009  -2839       C  
ATOM   2397  C   GLU B 116      43.097  29.264  47.971  1.00 60.08           C  
ANISOU 2397  C   GLU B 116     7518  10653   4656   -738    823  -2764       C  
ATOM   2398  O   GLU B 116      42.693  29.476  46.851  1.00 61.87           O  
ANISOU 2398  O   GLU B 116     7794  11114   4599   -849    807  -2783       O  
ATOM   2399  CB  GLU B 116      45.203  27.891  48.082  1.00 62.78           C  
ANISOU 2399  CB  GLU B 116     7726  11074   5051   -374   1068  -3231       C  
ATOM   2400  CG  GLU B 116      46.469  27.527  48.877  1.00 64.95           C  
ANISOU 2400  CG  GLU B 116     7851  11343   5483   -125   1184  -3340       C  
ATOM   2401  CD  GLU B 116      47.576  26.856  48.037  1.00 71.09           C  
ANISOU 2401  CD  GLU B 116     8540  12417   6053     68   1351  -3676       C  
ATOM   2402  OE1 GLU B 116      48.700  27.404  48.003  1.00 72.08           O  
ANISOU 2402  OE1 GLU B 116     8425  12882   6078     95   1508  -3665       O  
ATOM   2403  OE2 GLU B 116      47.338  25.800  47.395  1.00 75.72           O  
ANISOU 2403  OE2 GLU B 116     9289  12922   6558    181   1334  -3964       O  
ATOM   2404  N   ASP B 117      42.280  29.030  48.989  1.00 58.64           N  
ANISOU 2404  N   ASP B 117     7392  10141   4746   -730    682  -2670       N  
ATOM   2405  CA  ASP B 117      40.884  28.638  48.766  1.00 59.16           C  
ANISOU 2405  CA  ASP B 117     7572  10105   4799   -842    506  -2691       C  
ATOM   2406  C   ASP B 117      39.998  29.252  49.835  1.00 55.40           C  
ANISOU 2406  C   ASP B 117     7081   9428   4539   -898    380  -2404       C  
ATOM   2407  O   ASP B 117      40.213  29.008  51.026  1.00 54.59           O  
ANISOU 2407  O   ASP B 117     6967   9056   4718   -811    382  -2363       O  
ATOM   2408  CB  ASP B 117      40.786  27.099  48.786  1.00 61.14           C  
ANISOU 2408  CB  ASP B 117     7951  10133   5146   -770    484  -3035       C  
ATOM   2409  CG  ASP B 117      39.395  26.576  48.411  1.00 65.54           C  
ANISOU 2409  CG  ASP B 117     8617  10638   5646   -949    319  -3124       C  
ATOM   2410  OD1 ASP B 117      38.429  27.371  48.351  1.00 68.45           O  
ANISOU 2410  OD1 ASP B 117     8925  11133   5948  -1086    199  -2898       O  
ATOM   2411  OD2 ASP B 117      39.270  25.351  48.166  1.00 70.57           O  
ANISOU 2411  OD2 ASP B 117     9404  11118   6290   -952    311  -3433       O  
ATOM   2412  N   LEU B 118      39.008  30.052  49.424  1.00 54.24           N  
ANISOU 2412  N   LEU B 118     6933   9429   4243  -1015    269  -2207       N  
ATOM   2413  CA  LEU B 118      38.123  30.742  50.381  1.00 51.40           C  
ANISOU 2413  CA  LEU B 118     6547   8925   4055  -1037    152  -1932       C  
ATOM   2414  C   LEU B 118      37.168  29.776  51.104  1.00 50.70           C  
ANISOU 2414  C   LEU B 118     6482   8601   4179  -1080     27  -2042       C  
ATOM   2415  O   LEU B 118      36.541  30.146  52.095  1.00 47.78           O  
ANISOU 2415  O   LEU B 118     6076   8084   3994  -1082    -47  -1854       O  
ATOM   2416  CB  LEU B 118      37.348  31.911  49.735  1.00 51.09           C  
ANISOU 2416  CB  LEU B 118     6509   9126   3775  -1090     68  -1681       C  
ATOM   2417  CG  LEU B 118      38.177  33.100  49.225  1.00 51.97           C  
ANISOU 2417  CG  LEU B 118     6652   9404   3690  -1084    196  -1483       C  
ATOM   2418  CD1 LEU B 118      37.360  34.039  48.285  1.00 51.58           C  
ANISOU 2418  CD1 LEU B 118     6670   9605   3322  -1108    103  -1276       C  
ATOM   2419  CD2 LEU B 118      38.919  33.870  50.354  1.00 44.98           C  
ANISOU 2419  CD2 LEU B 118     5750   8316   3024  -1048    296  -1286       C  
ATOM   2420  N   LYS B 119      37.082  28.535  50.620  1.00 52.47           N  
ANISOU 2420  N   LYS B 119     6786   8782   4368  -1128     18  -2353       N  
ATOM   2421  CA  LYS B 119      36.398  27.474  51.380  1.00 52.35           C  
ANISOU 2421  CA  LYS B 119     6846   8476   4567  -1200    -55  -2485       C  
ATOM   2422  C   LYS B 119      37.080  27.182  52.725  1.00 50.42           C  
ANISOU 2422  C   LYS B 119     6637   7884   4635  -1062     16  -2431       C  
ATOM   2423  O   LYS B 119      36.582  26.405  53.526  1.00 49.81           O  
ANISOU 2423  O   LYS B 119     6646   7529   4749  -1113    -28  -2485       O  
ATOM   2424  CB  LYS B 119      36.298  26.197  50.536  1.00 55.17           C  
ANISOU 2424  CB  LYS B 119     7342   8815   4804  -1289    -55  -2852       C  
ATOM   2425  CG  LYS B 119      35.135  26.222  49.564  1.00 56.39           C  
ANISOU 2425  CG  LYS B 119     7456   9262   4705  -1497   -192  -2922       C  
ATOM   2426  CD  LYS B 119      34.980  24.885  48.811  1.00 60.79           C  
ANISOU 2426  CD  LYS B 119     8180   9765   5151  -1631   -194  -3320       C  
ATOM   2427  CE  LYS B 119      36.090  24.689  47.770  1.00 61.01           C  
ANISOU 2427  CE  LYS B 119     8276   9933   4972  -1497    -63  -3522       C  
ATOM   2428  NZ  LYS B 119      35.696  23.689  46.740  1.00 66.18           N  
ANISOU 2428  NZ  LYS B 119     9067  10664   5413  -1657    -97  -3891       N  
ATOM   2429  N   ASN B 120      38.221  27.834  52.973  1.00 49.71           N  
ANISOU 2429  N   ASN B 120     6478   7834   4575   -903    131  -2320       N  
ATOM   2430  CA  ASN B 120      38.972  27.643  54.213  1.00 47.44           C  
ANISOU 2430  CA  ASN B 120     6192   7288   4544   -748    193  -2269       C  
ATOM   2431  C   ASN B 120      38.426  28.494  55.356  1.00 44.36           C  
ANISOU 2431  C   ASN B 120     5726   6800   4327   -778    129  -1972       C  
ATOM   2432  O   ASN B 120      38.765  28.258  56.517  1.00 43.07           O  
ANISOU 2432  O   ASN B 120     5576   6403   4385   -679    147  -1919       O  
ATOM   2433  CB  ASN B 120      40.467  27.949  53.992  1.00 47.69           C  
ANISOU 2433  CB  ASN B 120     6138   7468   4512   -583    345  -2311       C  
ATOM   2434  CG  ASN B 120      41.163  26.924  53.095  1.00 53.38           C  
ANISOU 2434  CG  ASN B 120     6935   8247   5100   -479    429  -2641       C  
ATOM   2435  OD1 ASN B 120      40.728  25.776  52.998  1.00 57.44           O  
ANISOU 2435  OD1 ASN B 120     7619   8550   5653   -479    386  -2853       O  
ATOM   2436  ND2 ASN B 120      42.253  27.346  52.420  1.00 53.76           N  
ANISOU 2436  ND2 ASN B 120     6867   8585   4974   -402    562  -2695       N  
ATOM   2437  N   VAL B 121      37.586  29.477  55.028  1.00 43.22           N  
ANISOU 2437  N   VAL B 121     5514   6840   4065   -887     52  -1782       N  
ATOM   2438  CA  VAL B 121      37.075  30.448  56.013  1.00 39.80           C  
ANISOU 2438  CA  VAL B 121     5015   6346   3760   -885      0  -1499       C  
ATOM   2439  C   VAL B 121      35.917  29.865  56.857  1.00 39.59           C  
ANISOU 2439  C   VAL B 121     5002   6140   3899   -964   -109  -1488       C  
ATOM   2440  O   VAL B 121      34.970  29.322  56.302  1.00 40.63           O  
ANISOU 2440  O   VAL B 121     5146   6353   3939  -1098   -195  -1602       O  
ATOM   2441  CB  VAL B 121      36.623  31.769  55.328  1.00 39.86           C  
ANISOU 2441  CB  VAL B 121     4979   6608   3556   -920    -37  -1290       C  
ATOM   2442  CG1 VAL B 121      36.184  32.799  56.354  1.00 35.82           C  
ANISOU 2442  CG1 VAL B 121     4434   6005   3170   -879    -75  -1015       C  
ATOM   2443  CG2 VAL B 121      37.728  32.325  54.448  1.00 40.14           C  
ANISOU 2443  CG2 VAL B 121     5025   6827   3399   -899     88  -1295       C  
ATOM   2444  N   PHE B 122      36.003  30.016  58.186  1.00 37.32           N  
ANISOU 2444  N   PHE B 122     4702   5642   3834   -902    -99  -1354       N  
ATOM   2445  CA  PHE B 122      35.070  29.432  59.141  1.00 37.12           C  
ANISOU 2445  CA  PHE B 122     4696   5432   3974   -981   -169  -1336       C  
ATOM   2446  C   PHE B 122      34.934  30.426  60.312  1.00 35.29           C  
ANISOU 2446  C   PHE B 122     4386   5147   3874   -907   -177  -1079       C  
ATOM   2447  O   PHE B 122      35.940  30.863  60.888  1.00 33.80           O  
ANISOU 2447  O   PHE B 122     4196   4876   3768   -784   -100  -1003       O  
ATOM   2448  CB  PHE B 122      35.615  28.092  59.676  1.00 37.67           C  
ANISOU 2448  CB  PHE B 122     4917   5200   4196   -947   -116  -1514       C  
ATOM   2449  CG  PHE B 122      35.551  26.928  58.682  1.00 42.52           C  
ANISOU 2449  CG  PHE B 122     5666   5787   4702  -1037   -114  -1798       C  
ATOM   2450  CD1 PHE B 122      34.446  26.063  58.663  1.00 44.13           C  
ANISOU 2450  CD1 PHE B 122     5955   5901   4911  -1259   -182  -1913       C  
ATOM   2451  CD2 PHE B 122      36.600  26.687  57.786  1.00 44.26           C  
ANISOU 2451  CD2 PHE B 122     5931   6081   4804   -918    -33  -1968       C  
ATOM   2452  CE1 PHE B 122      34.376  24.981  57.770  1.00 48.70           C  
ANISOU 2452  CE1 PHE B 122     6693   6426   5383  -1371   -175  -2197       C  
ATOM   2453  CE2 PHE B 122      36.539  25.579  56.883  1.00 49.35           C  
ANISOU 2453  CE2 PHE B 122     6729   6679   5340   -989    -25  -2257       C  
ATOM   2454  CZ  PHE B 122      35.423  24.740  56.867  1.00 48.66           C  
ANISOU 2454  CZ  PHE B 122     6757   6468   5262  -1221    -99  -2374       C  
ATOM   2455  N   PRO B 123      33.691  30.795  60.676  1.00 35.04           N  
ANISOU 2455  N   PRO B 123     4276   5189   3849   -983   -268   -959       N  
ATOM   2456  CA  PRO B 123      33.529  31.638  61.863  1.00 33.24           C  
ANISOU 2456  CA  PRO B 123     3993   4887   3748   -900   -268   -743       C  
ATOM   2457  C   PRO B 123      33.790  30.794  63.133  1.00 32.58           C  
ANISOU 2457  C   PRO B 123     3975   4520   3882   -897   -230   -770       C  
ATOM   2458  O   PRO B 123      33.790  29.529  63.056  1.00 33.69           O  
ANISOU 2458  O   PRO B 123     4219   4514   4065   -981   -222   -944       O  
ATOM   2459  CB  PRO B 123      32.066  32.064  61.776  1.00 33.78           C  
ANISOU 2459  CB  PRO B 123     3944   5157   3732   -963   -376   -656       C  
ATOM   2460  CG  PRO B 123      31.389  30.842  61.104  1.00 35.17           C  
ANISOU 2460  CG  PRO B 123     4121   5400   3841  -1160   -430   -874       C  
ATOM   2461  CD  PRO B 123      32.395  30.305  60.144  1.00 37.10           C  
ANISOU 2461  CD  PRO B 123     4481   5606   4007  -1153   -370  -1048       C  
ATOM   2462  N   PRO B 124      34.012  31.466  64.281  1.00 30.66           N  
ANISOU 2462  N   PRO B 124     3705   4185   3760   -800   -206   -605       N  
ATOM   2463  CA  PRO B 124      34.215  30.728  65.526  1.00 30.92           C  
ANISOU 2463  CA  PRO B 124     3804   3972   3970   -782   -179   -604       C  
ATOM   2464  C   PRO B 124      32.933  30.212  66.141  1.00 32.90           C  
ANISOU 2464  C   PRO B 124     4039   4187   4274   -929   -229   -580       C  
ATOM   2465  O   PRO B 124      31.903  30.859  66.040  1.00 33.72           O  
ANISOU 2465  O   PRO B 124     4013   4487   4309   -983   -287   -496       O  
ATOM   2466  CB  PRO B 124      34.778  31.790  66.486  1.00 28.16           C  
ANISOU 2466  CB  PRO B 124     3406   3599   3691   -651   -145   -434       C  
ATOM   2467  CG  PRO B 124      34.224  33.095  65.988  1.00 27.44           C  
ANISOU 2467  CG  PRO B 124     3235   3708   3481   -644   -177   -308       C  
ATOM   2468  CD  PRO B 124      34.234  32.920  64.464  1.00 29.50           C  
ANISOU 2468  CD  PRO B 124     3503   4129   3574   -699   -192   -422       C  
ATOM   2469  N   GLU B 125      33.031  29.074  66.816  1.00 34.85           N  
ANISOU 2469  N   GLU B 125     4420   4189   4630   -981   -201   -646       N  
ATOM   2470  CA  GLU B 125      32.034  28.652  67.780  1.00 36.72           C  
ANISOU 2470  CA  GLU B 125     4660   4350   4938  -1125   -214   -583       C  
ATOM   2471  C   GLU B 125      32.532  29.260  69.091  1.00 35.58           C  
ANISOU 2471  C   GLU B 125     4501   4113   4903   -960   -181   -413       C  
ATOM   2472  O   GLU B 125      33.762  29.358  69.302  1.00 34.95           O  
ANISOU 2472  O   GLU B 125     4482   3930   4867   -779   -144   -412       O  
ATOM   2473  CB  GLU B 125      32.062  27.139  67.880  1.00 39.80           C  
ANISOU 2473  CB  GLU B 125     5278   4464   5378  -1255   -182   -723       C  
ATOM   2474  CG  GLU B 125      31.635  26.412  66.555  1.00 46.01           C  
ANISOU 2474  CG  GLU B 125     6118   5315   6048  -1447   -208   -937       C  
ATOM   2475  CD  GLU B 125      31.279  24.956  66.792  1.00 55.19           C  
ANISOU 2475  CD  GLU B 125     7534   6185   7251  -1662   -174  -1065       C  
ATOM   2476  OE1 GLU B 125      32.202  24.150  67.070  1.00 58.26           O  
ANISOU 2476  OE1 GLU B 125     8180   6245   7711  -1526   -118  -1122       O  
ATOM   2477  OE2 GLU B 125      30.072  24.615  66.713  1.00 59.23           O  
ANISOU 2477  OE2 GLU B 125     7995   6799   7710  -1969   -200  -1110       O  
ATOM   2478  N   VAL B 126      31.622  29.656  69.970  1.00 33.84           N  
ANISOU 2478  N   VAL B 126     4185   3962   4710  -1021   -194   -287       N  
ATOM   2479  CA  VAL B 126      32.013  30.362  71.154  1.00 31.59           C  
ANISOU 2479  CA  VAL B 126     3874   3628   4498   -871   -169   -138       C  
ATOM   2480  C   VAL B 126      31.223  29.849  72.332  1.00 32.18           C  
ANISOU 2480  C   VAL B 126     3971   3623   4631   -986   -149    -65       C  
ATOM   2481  O   VAL B 126      30.001  29.802  72.272  1.00 32.64           O  
ANISOU 2481  O   VAL B 126     3918   3840   4640  -1157   -169    -62       O  
ATOM   2482  CB  VAL B 126      31.753  31.868  71.021  1.00 31.12           C  
ANISOU 2482  CB  VAL B 126     3657   3790   4377   -767   -194    -31       C  
ATOM   2483  CG1 VAL B 126      32.039  32.588  72.396  1.00 26.87           C  
ANISOU 2483  CG1 VAL B 126     3109   3189   3911   -642   -163    105       C  
ATOM   2484  CG2 VAL B 126      32.655  32.475  69.926  1.00 32.40           C  
ANISOU 2484  CG2 VAL B 126     3828   4016   4465   -671   -192    -76       C  
ATOM   2485  N   ALA B 127      31.917  29.519  73.410  1.00 30.98           N  
ANISOU 2485  N   ALA B 127     3942   3266   4562   -888   -111     -2       N  
ATOM   2486  CA  ALA B 127      31.288  28.973  74.577  1.00 32.19           C  
ANISOU 2486  CA  ALA B 127     4157   3319   4753   -997    -78     81       C  
ATOM   2487  C   ALA B 127      31.900  29.562  75.807  1.00 31.42           C  
ANISOU 2487  C   ALA B 127     4057   3180   4699   -812    -60    209       C  
ATOM   2488  O   ALA B 127      33.104  29.878  75.800  1.00 29.55           O  
ANISOU 2488  O   ALA B 127     3849   2894   4483   -614    -67    198       O  
ATOM   2489  CB  ALA B 127      31.463  27.439  74.594  1.00 34.84           C  
ANISOU 2489  CB  ALA B 127     4760   3359   5118  -1111    -45      6       C  
ATOM   2490  N   VAL B 128      31.077  29.681  76.860  1.00 31.33           N  
ANISOU 2490  N   VAL B 128     3999   3220   4684   -892    -33    316       N  
ATOM   2491  CA  VAL B 128      31.500  30.111  78.172  1.00 31.62           C  
ANISOU 2491  CA  VAL B 128     4050   3222   4742   -751    -12    434       C  
ATOM   2492  C   VAL B 128      31.355  28.946  79.150  1.00 33.53           C  
ANISOU 2492  C   VAL B 128     4490   3253   4994   -845     33    500       C  
ATOM   2493  O   VAL B 128      30.352  28.223  79.111  1.00 36.48           O  
ANISOU 2493  O   VAL B 128     4903   3610   5344  -1095     69    494       O  
ATOM   2494  CB  VAL B 128      30.676  31.348  78.666  1.00 31.99           C  
ANISOU 2494  CB  VAL B 128     3891   3515   4747   -729     -8    510       C  
ATOM   2495  CG1 VAL B 128      31.029  31.694  80.104  1.00 32.28           C  
ANISOU 2495  CG1 VAL B 128     3960   3516   4789   -614     19    614       C  
ATOM   2496  CG2 VAL B 128      31.027  32.553  77.842  1.00 31.94           C  
ANISOU 2496  CG2 VAL B 128     3774   3641   4719   -593    -47    475       C  
ATOM   2497  N   PHE B 129      32.365  28.733  79.991  1.00 32.32           N  
ANISOU 2497  N   PHE B 129     4471   2947   4860   -659     32    560       N  
ATOM   2498  CA  PHE B 129      32.328  27.695  81.014  1.00 33.42           C  
ANISOU 2498  CA  PHE B 129     4843   2867   4985   -699     73    657       C  
ATOM   2499  C   PHE B 129      32.292  28.388  82.404  1.00 32.89           C  
ANISOU 2499  C   PHE B 129     4701   2916   4879   -609     88    791       C  
ATOM   2500  O   PHE B 129      33.100  29.235  82.715  1.00 30.04           O  
ANISOU 2500  O   PHE B 129     4240   2656   4518   -403     50    793       O  
ATOM   2501  CB  PHE B 129      33.505  26.714  80.829  1.00 33.71           C  
ANISOU 2501  CB  PHE B 129     5134   2630   5044   -514     51    616       C  
ATOM   2502  CG  PHE B 129      33.531  26.012  79.455  1.00 35.39           C  
ANISOU 2502  CG  PHE B 129     5441   2722   5282   -597     46    460       C  
ATOM   2503  CD1 PHE B 129      33.214  24.682  79.333  1.00 37.36           C  
ANISOU 2503  CD1 PHE B 129     5994   2674   5526   -743     86    438       C  
ATOM   2504  CD2 PHE B 129      33.873  26.701  78.297  1.00 33.62           C  
ANISOU 2504  CD2 PHE B 129     5028   2674   5070   -541      7    334       C  
ATOM   2505  CE1 PHE B 129      33.218  24.040  78.073  1.00 39.62           C  
ANISOU 2505  CE1 PHE B 129     6383   2846   5821   -831     84    269       C  
ATOM   2506  CE2 PHE B 129      33.872  26.072  77.041  1.00 34.46           C  
ANISOU 2506  CE2 PHE B 129     5217   2697   5176   -620      4    180       C  
ATOM   2507  CZ  PHE B 129      33.547  24.738  76.934  1.00 37.95           C  
ANISOU 2507  CZ  PHE B 129     5952   2849   5616   -761     40    137       C  
ATOM   2508  N   GLU B 130      31.317  28.039  83.226  1.00 35.73           N  
ANISOU 2508  N   GLU B 130     5102   3282   5190   -796    153    889       N  
ATOM   2509  CA  GLU B 130      31.085  28.671  84.557  1.00 35.12           C  
ANISOU 2509  CA  GLU B 130     4946   3345   5050   -743    183   1007       C  
ATOM   2510  C   GLU B 130      32.098  28.183  85.572  1.00 35.47           C  
ANISOU 2510  C   GLU B 130     5201   3215   5058   -546    166   1105       C  
ATOM   2511  O   GLU B 130      32.598  27.086  85.433  1.00 37.58           O  
ANISOU 2511  O   GLU B 130     5725   3218   5333   -510    159   1120       O  
ATOM   2512  CB  GLU B 130      29.679  28.320  85.029  1.00 36.67           C  
ANISOU 2512  CB  GLU B 130     5113   3634   5184  -1036    274   1072       C  
ATOM   2513  CG  GLU B 130      28.610  28.821  84.001  1.00 40.76           C  
ANISOU 2513  CG  GLU B 130     5372   4402   5712  -1207    275    964       C  
ATOM   2514  CD  GLU B 130      27.183  28.663  84.494  1.00 42.92           C  
ANISOU 2514  CD  GLU B 130     5518   4886   5901  -1486    365   1005       C  
ATOM   2515  OE1 GLU B 130      26.990  27.854  85.411  1.00 41.95           O  
ANISOU 2515  OE1 GLU B 130     5579   4636   5722  -1636    444   1110       O  
ATOM   2516  OE2 GLU B 130      26.274  29.352  83.958  1.00 45.40           O  
ANISOU 2516  OE2 GLU B 130     5549   5511   6189  -1545    359    934       O  
ATOM   2517  N   PRO B 131      32.408  29.001  86.587  1.00 34.26           N  
ANISOU 2517  N   PRO B 131     4951   3214   4849   -398    153   1164       N  
ATOM   2518  CA  PRO B 131      33.420  28.734  87.582  1.00 34.76           C  
ANISOU 2518  CA  PRO B 131     5158   3199   4850   -178    115   1247       C  
ATOM   2519  C   PRO B 131      33.182  27.461  88.367  1.00 37.93           C  
ANISOU 2519  C   PRO B 131     5864   3370   5176   -243    165   1398       C  
ATOM   2520  O   PRO B 131      32.040  27.143  88.692  1.00 39.56           O  
ANISOU 2520  O   PRO B 131     6111   3578   5340   -506    258   1471       O  
ATOM   2521  CB  PRO B 131      33.299  29.929  88.540  1.00 33.47           C  
ANISOU 2521  CB  PRO B 131     4808   3289   4617   -120    119   1270       C  
ATOM   2522  CG  PRO B 131      32.602  31.011  87.718  1.00 32.36           C  
ANISOU 2522  CG  PRO B 131     4425   3331   4537   -217    135   1161       C  
ATOM   2523  CD  PRO B 131      31.711  30.280  86.824  1.00 32.39           C  
ANISOU 2523  CD  PRO B 131     4459   3256   4590   -432    176   1143       C  
ATOM   2524  N   SER B 132      34.267  26.748  88.675  1.00 38.73           N  
ANISOU 2524  N   SER B 132     6183   3290   5243      0    106   1447       N  
ATOM   2525  CA  SER B 132      34.244  25.622  89.639  1.00 41.66           C  
ANISOU 2525  CA  SER B 132     6902   3422   5503     20    141   1628       C  
ATOM   2526  C   SER B 132      33.823  26.060  91.047  1.00 41.97           C  
ANISOU 2526  C   SER B 132     6902   3638   5406    -15    183   1768       C  
ATOM   2527  O   SER B 132      34.235  27.092  91.561  1.00 40.73           O  
ANISOU 2527  O   SER B 132     6517   3746   5212    128    132   1731       O  
ATOM   2528  CB  SER B 132      35.623  24.956  89.672  1.00 42.41           C  
ANISOU 2528  CB  SER B 132     7195   3347   5569    392     44   1640       C  
ATOM   2529  OG  SER B 132      35.923  24.360  90.928  1.00 49.71           O  
ANISOU 2529  OG  SER B 132     8376   4171   6340    552     35   1831       O  
ATOM   2530  N   GLU B 133      32.982  25.264  91.681  1.00 45.23           N  
ANISOU 2530  N   GLU B 133     7552   3902   5729   -235    287   1922       N  
ATOM   2531  CA  GLU B 133      32.584  25.506  93.055  1.00 46.31           C  
ANISOU 2531  CA  GLU B 133     7697   4191   5705   -274    342   2071       C  
ATOM   2532  C   GLU B 133      33.743  25.155  94.017  1.00 46.65           C  
ANISOU 2532  C   GLU B 133     7947   4163   5613     81    251   2197       C  
ATOM   2533  O   GLU B 133      33.797  25.651  95.154  1.00 47.19           O  
ANISOU 2533  O   GLU B 133     7950   4441   5537    159    247   2279       O  
ATOM   2534  CB  GLU B 133      31.271  24.721  93.324  1.00 50.68           C  
ANISOU 2534  CB  GLU B 133     8434   4629   6192   -678    502   2190       C  
ATOM   2535  CG  GLU B 133      30.154  25.132  92.249  1.00 53.79           C  
ANISOU 2535  CG  GLU B 133     8545   5179   6710  -1006    566   2028       C  
ATOM   2536  CD  GLU B 133      29.090  24.029  91.957  1.00 61.63           C  
ANISOU 2536  CD  GLU B 133     9756   5978   7682  -1440    700   2078       C  
ATOM   2537  OE1 GLU B 133      28.982  23.051  92.745  1.00 66.55           O  
ANISOU 2537  OE1 GLU B 133    10750   6358   8177  -1557    782   2261       O  
ATOM   2538  OE2 GLU B 133      28.353  24.156  90.931  1.00 60.79           O  
ANISOU 2538  OE2 GLU B 133     9454   5973   7670  -1680    725   1931       O  
ATOM   2539  N   ALA B 134      34.694  24.337  93.556  1.00 46.42           N  
ANISOU 2539  N   ALA B 134     8150   3872   5614    327    169   2199       N  
ATOM   2540  CA  ALA B 134      35.910  24.107  94.350  1.00 47.39           C  
ANISOU 2540  CA  ALA B 134     8399   4004   5602    740     51   2289       C  
ATOM   2541  C   ALA B 134      36.800  25.355  94.389  1.00 44.18           C  
ANISOU 2541  C   ALA B 134     7591   3985   5210    963    -67   2129       C  
ATOM   2542  O   ALA B 134      37.284  25.744  95.454  1.00 44.27           O  
ANISOU 2542  O   ALA B 134     7543   4210   5065   1139   -128   2191       O  
ATOM   2543  CB  ALA B 134      36.689  22.860  93.883  1.00 49.00           C  
ANISOU 2543  CB  ALA B 134     8970   3834   5811    999     -2   2332       C  
ATOM   2544  N   GLU B 135      36.984  26.008  93.239  1.00 42.22           N  
ANISOU 2544  N   GLU B 135     7075   3835   5132    923    -93   1922       N  
ATOM   2545  CA  GLU B 135      37.741  27.273  93.207  1.00 38.24           C  
ANISOU 2545  CA  GLU B 135     6205   3681   4641   1049   -180   1760       C  
ATOM   2546  C   GLU B 135      37.051  28.249  94.166  1.00 37.00           C  
ANISOU 2546  C   GLU B 135     5893   3767   4398    889   -128   1786       C  
ATOM   2547  O   GLU B 135      37.664  28.786  95.073  1.00 35.30           O  
ANISOU 2547  O   GLU B 135     5580   3779   4051   1044   -195   1785       O  
ATOM   2548  CB  GLU B 135      37.829  27.856  91.793  1.00 36.03           C  
ANISOU 2548  CB  GLU B 135     5702   3444   4543    959   -183   1557       C  
ATOM   2549  CG  GLU B 135      38.681  29.176  91.762  1.00 33.60           C  
ANISOU 2549  CG  GLU B 135     5060   3473   4234   1051   -258   1392       C  
ATOM   2550  CD  GLU B 135      38.563  30.044  90.546  1.00 32.20           C  
ANISOU 2550  CD  GLU B 135     4664   3367   4201    902   -235   1220       C  
ATOM   2551  OE1 GLU B 135      37.672  29.859  89.674  1.00 32.39           O  
ANISOU 2551  OE1 GLU B 135     4726   3244   4335    708   -164   1207       O  
ATOM   2552  OE2 GLU B 135      39.373  30.994  90.488  1.00 32.58           O  
ANISOU 2552  OE2 GLU B 135     4497   3647   4235    962   -288   1091       O  
ATOM   2553  N   ILE B 136      35.757  28.457  93.958  1.00 36.60           N  
ANISOU 2553  N   ILE B 136     5810   3688   4407    586     -8   1797       N  
ATOM   2554  CA  ILE B 136      34.999  29.347  94.827  1.00 37.02           C  
ANISOU 2554  CA  ILE B 136     5719   3973   4372    454     58   1810       C  
ATOM   2555  C   ILE B 136      35.292  29.082  96.302  1.00 38.88           C  
ANISOU 2555  C   ILE B 136     6095   4286   4388    585     40   1962       C  
ATOM   2556  O   ILE B 136      35.607  29.998  97.022  1.00 38.57           O  
ANISOU 2556  O   ILE B 136     5896   4501   4254    667      2   1901       O  
ATOM   2557  CB  ILE B 136      33.459  29.307  94.533  1.00 37.76           C  
ANISOU 2557  CB  ILE B 136     5784   4044   4516    126    201   1835       C  
ATOM   2558  CG1 ILE B 136      33.179  30.087  93.246  1.00 35.99           C  
ANISOU 2558  CG1 ILE B 136     5325   3882   4466     43    197   1655       C  
ATOM   2559  CG2 ILE B 136      32.631  29.865  95.686  1.00 34.63           C  
ANISOU 2559  CG2 ILE B 136     5311   3872   3973     24    291   1896       C  
ATOM   2560  CD1 ILE B 136      31.902  29.582  92.535  1.00 39.30           C  
ANISOU 2560  CD1 ILE B 136     5751   4224   4954   -247    300   1667       C  
ATOM   2561  N   SER B 137      35.231  27.831  96.749  1.00 41.62           N  
ANISOU 2561  N   SER B 137     6768   4406   4639    610     65   2158       N  
ATOM   2562  CA  SER B 137      35.355  27.608  98.175  1.00 43.17           C  
ANISOU 2562  CA  SER B 137     7113   4689   4597    713     61   2326       C  
ATOM   2563  C   SER B 137      36.797  27.619  98.746  1.00 44.01           C  
ANISOU 2563  C   SER B 137     7225   4923   4574   1099   -107   2328       C  
ATOM   2564  O   SER B 137      36.993  27.920  99.925  1.00 44.12           O  
ANISOU 2564  O   SER B 137     7231   5151   4382   1196   -137   2394       O  
ATOM   2565  CB  SER B 137      34.511  26.399  98.615  1.00 47.29           C  
ANISOU 2565  CB  SER B 137     8000   4945   5020    528    187   2562       C  
ATOM   2566  OG  SER B 137      35.256  25.206  98.659  1.00 49.94           O  
ANISOU 2566  OG  SER B 137     8699   4982   5294    753    121   2708       O  
ATOM   2567  N   HIS B 138      37.806  27.333  97.921  1.00 42.99           N  
ANISOU 2567  N   HIS B 138     7076   4712   4543   1323   -219   2238       N  
ATOM   2568  CA  HIS B 138      39.191  27.430  98.402  1.00 44.05           C  
ANISOU 2568  CA  HIS B 138     7133   5059   4545   1692   -387   2203       C  
ATOM   2569  C   HIS B 138      39.813  28.822  98.249  1.00 41.16           C  
ANISOU 2569  C   HIS B 138     6360   5063   4217   1691   -460   1957       C  
ATOM   2570  O   HIS B 138      40.723  29.175  99.000  1.00 41.92           O  
ANISOU 2570  O   HIS B 138     6334   5447   4145   1898   -578   1917       O  
ATOM   2571  CB  HIS B 138      40.099  26.382  97.747  1.00 45.33           C  
ANISOU 2571  CB  HIS B 138     7471   5008   4742   1995   -478   2229       C  
ATOM   2572  CG  HIS B 138      40.069  25.057  98.436  1.00 51.85           C  
ANISOU 2572  CG  HIS B 138     8747   5551   5402   2178   -476   2495       C  
ATOM   2573  ND1 HIS B 138      39.543  23.925  97.849  1.00 54.74           N  
ANISOU 2573  ND1 HIS B 138     9484   5460   5852   2096   -387   2609       N  
ATOM   2574  CD2 HIS B 138      40.460  24.692  99.683  1.00 54.28           C  
ANISOU 2574  CD2 HIS B 138     9228   5948   5445   2422   -545   2678       C  
ATOM   2575  CE1 HIS B 138      39.640  22.913  98.694  1.00 59.39           C  
ANISOU 2575  CE1 HIS B 138    10487   5836   6241   2287   -396   2858       C  
ATOM   2576  NE2 HIS B 138      40.188  23.353  99.813  1.00 59.91           N  
ANISOU 2576  NE2 HIS B 138    10436   6235   6089   2501   -495   2914       N  
ATOM   2577  N   THR B 139      39.314  29.606  97.304  1.00 38.33           N  
ANISOU 2577  N   THR B 139     5809   4698   4055   1451   -389   1795       N  
ATOM   2578  CA  THR B 139      39.987  30.871  96.925  1.00 37.06           C  
ANISOU 2578  CA  THR B 139     5319   4811   3949   1432   -447   1556       C  
ATOM   2579  C   THR B 139      39.185  32.132  97.134  1.00 36.03           C  
ANISOU 2579  C   THR B 139     5038   4807   3842   1183   -360   1456       C  
ATOM   2580  O   THR B 139      39.762  33.205  97.125  1.00 36.46           O  
ANISOU 2580  O   THR B 139     4886   5078   3887   1162   -405   1277       O  
ATOM   2581  CB  THR B 139      40.501  30.876  95.441  1.00 35.23           C  
ANISOU 2581  CB  THR B 139     4972   4498   3914   1438   -469   1409       C  
ATOM   2582  OG1 THR B 139      39.413  31.038  94.517  1.00 28.95           O  
ANISOU 2582  OG1 THR B 139     4195   3505   3299   1181   -352   1389       O  
ATOM   2583  CG2 THR B 139      41.316  29.600  95.108  1.00 36.92           C  
ANISOU 2583  CG2 THR B 139     5343   4573   4112   1728   -550   1480       C  
ATOM   2584  N   GLN B 140      37.866  32.000  97.275  1.00 36.56           N  
ANISOU 2584  N   GLN B 140     5212   4740   3936    993   -231   1559       N  
ATOM   2585  CA  GLN B 140      36.903  33.132  97.342  1.00 36.10           C  
ANISOU 2585  CA  GLN B 140     5022   4780   3911    790   -130   1466       C  
ATOM   2586  C   GLN B 140      36.916  33.991  96.065  1.00 33.43           C  
ANISOU 2586  C   GLN B 140     4519   4414   3766    696   -121   1286       C  
ATOM   2587  O   GLN B 140      36.546  35.194  96.068  1.00 31.96           O  
ANISOU 2587  O   GLN B 140     4215   4332   3594    606    -77   1161       O  
ATOM   2588  CB  GLN B 140      37.070  33.982  98.629  1.00 37.39           C  
ANISOU 2588  CB  GLN B 140     5121   5206   3880    827   -146   1416       C  
ATOM   2589  CG  GLN B 140      36.813  33.217  99.935  1.00 42.48           C  
ANISOU 2589  CG  GLN B 140     5940   5897   4304    891   -128   1613       C  
ATOM   2590  CD  GLN B 140      38.077  32.530 100.511  1.00 52.72           C  
ANISOU 2590  CD  GLN B 140     7316   7270   5444   1150   -277   1686       C  
ATOM   2591  OE1 GLN B 140      39.173  33.138 100.592  1.00 54.85           O  
ANISOU 2591  OE1 GLN B 140     7421   7753   5664   1267   -398   1530       O  
ATOM   2592  NE2 GLN B 140      37.925  31.256 100.932  1.00 54.46           N  
ANISOU 2592  NE2 GLN B 140     7796   7327   5566   1239   -269   1923       N  
ATOM   2593  N   LYS B 141      37.317  33.354  94.968  1.00 32.27           N  
ANISOU 2593  N   LYS B 141     4394   4111   3754    726   -157   1278       N  
ATOM   2594  CA  LYS B 141      37.338  33.983  93.637  1.00 30.57           C  
ANISOU 2594  CA  LYS B 141     4053   3851   3708    637   -146   1135       C  
ATOM   2595  C   LYS B 141      36.732  32.990  92.668  1.00 30.13           C  
ANISOU 2595  C   LYS B 141     4101   3568   3777    566   -103   1208       C  
ATOM   2596  O   LYS B 141      36.517  31.858  93.033  1.00 30.01           O  
ANISOU 2596  O   LYS B 141     4266   3417   3718    593    -91   1350       O  
ATOM   2597  CB  LYS B 141      38.762  34.347  93.208  1.00 30.43           C  
ANISOU 2597  CB  LYS B 141     3913   3948   3697    745   -246    993       C  
ATOM   2598  CG  LYS B 141      39.398  35.479  94.039  1.00 33.17           C  
ANISOU 2598  CG  LYS B 141     4140   4540   3920    747   -285    872       C  
ATOM   2599  CD  LYS B 141      40.953  35.564  93.834  1.00 34.98           C  
ANISOU 2599  CD  LYS B 141     4227   4957   4105    853   -396    743       C  
ATOM   2600  CE  LYS B 141      41.647  36.157  95.088  1.00 35.84           C  
ANISOU 2600  CE  LYS B 141     4251   5347   4016    894   -465    670       C  
ATOM   2601  NZ  LYS B 141      42.086  35.090  96.087  1.00 46.24           N  
ANISOU 2601  NZ  LYS B 141     5636   6761   5170   1137   -557    807       N  
ATOM   2602  N   ALA B 142      36.487  33.425  91.428  1.00 29.81           N  
ANISOU 2602  N   ALA B 142     3969   3480   3875    469    -81   1108       N  
ATOM   2603  CA  ALA B 142      35.649  32.693  90.473  1.00 28.46           C  
ANISOU 2603  CA  ALA B 142     3864   3136   3811    344    -29   1147       C  
ATOM   2604  C   ALA B 142      36.082  33.021  89.052  1.00 26.91           C  
ANISOU 2604  C   ALA B 142     3576   2914   3735    333    -57   1016       C  
ATOM   2605  O   ALA B 142      35.912  34.145  88.583  1.00 23.92           O  
ANISOU 2605  O   ALA B 142     3069   2628   3389    278    -42    925       O  
ATOM   2606  CB  ALA B 142      34.196  33.076  90.664  1.00 27.91           C  
ANISOU 2606  CB  ALA B 142     3747   3122   3735    172     67   1186       C  
ATOM   2607  N   THR B 143      36.678  32.029  88.386  1.00 27.72           N  
ANISOU 2607  N   THR B 143     3768   2877   3884    404    -94   1009       N  
ATOM   2608  CA  THR B 143      37.126  32.203  87.027  1.00 26.55           C  
ANISOU 2608  CA  THR B 143     3543   2716   3828    397   -113    886       C  
ATOM   2609  C   THR B 143      36.172  31.621  86.002  1.00 26.91           C  
ANISOU 2609  C   THR B 143     3648   2619   3956    242    -67    887       C  
ATOM   2610  O   THR B 143      36.049  30.409  85.948  1.00 30.07           O  
ANISOU 2610  O   THR B 143     4225   2834   4365    239    -59    941       O  
ATOM   2611  CB  THR B 143      38.464  31.474  86.806  1.00 26.61           C  
ANISOU 2611  CB  THR B 143     3589   2698   3822    601   -183    839       C  
ATOM   2612  OG1 THR B 143      39.358  31.786  87.889  1.00 29.02           O  
ANISOU 2612  OG1 THR B 143     3836   3170   4020    758   -242    846       O  
ATOM   2613  CG2 THR B 143      39.109  31.883  85.463  1.00 21.94           C  
ANISOU 2613  CG2 THR B 143     2868   2171   3296    594   -194    688       C  
ATOM   2614  N   LEU B 144      35.661  32.451  85.096  1.00 25.25           N  
ANISOU 2614  N   LEU B 144     3311   2487   3796    131    -46    814       N  
ATOM   2615  CA  LEU B 144      34.923  31.986  83.896  1.00 26.13           C  
ANISOU 2615  CA  LEU B 144     3437   2522   3970     -5    -24    777       C  
ATOM   2616  C   LEU B 144      35.920  31.800  82.761  1.00 25.62           C  
ANISOU 2616  C   LEU B 144     3365   2423   3944     72    -61    664       C  
ATOM   2617  O   LEU B 144      36.898  32.557  82.648  1.00 24.47           O  
ANISOU 2617  O   LEU B 144     3122   2390   3783    169    -87    598       O  
ATOM   2618  CB  LEU B 144      33.894  33.053  83.441  1.00 25.95           C  
ANISOU 2618  CB  LEU B 144     3266   2643   3948   -113      4    758       C  
ATOM   2619  CG  LEU B 144      32.676  33.459  84.293  1.00 26.87           C  
ANISOU 2619  CG  LEU B 144     3321   2870   4015   -188     54    836       C  
ATOM   2620  CD1 LEU B 144      32.988  34.418  85.500  1.00 25.28           C  
ANISOU 2620  CD1 LEU B 144     3089   2762   3752    -75     61    863       C  
ATOM   2621  CD2 LEU B 144      31.686  34.111  83.372  1.00 30.83           C  
ANISOU 2621  CD2 LEU B 144     3691   3499   4521   -258     63    795       C  
ATOM   2622  N   VAL B 145      35.733  30.768  81.962  1.00 26.04           N  
ANISOU 2622  N   VAL B 145     3527   2332   4033     18    -56    628       N  
ATOM   2623  CA  VAL B 145      36.509  30.696  80.722  1.00 27.37           C  
ANISOU 2623  CA  VAL B 145     3666   2507   4226     75    -78    500       C  
ATOM   2624  C   VAL B 145      35.673  30.837  79.462  1.00 27.39           C  
ANISOU 2624  C   VAL B 145     3617   2541   4246    -92    -62    437       C  
ATOM   2625  O   VAL B 145      34.555  30.335  79.392  1.00 27.99           O  
ANISOU 2625  O   VAL B 145     3743   2563   4328   -257    -41    467       O  
ATOM   2626  CB  VAL B 145      37.701  29.635  80.687  1.00 28.79           C  
ANISOU 2626  CB  VAL B 145     3974   2562   4401    281   -106    449       C  
ATOM   2627  CG1 VAL B 145      37.979  28.963  82.009  1.00 30.49           C  
ANISOU 2627  CG1 VAL B 145     4335   2669   4578    422   -123    560       C  
ATOM   2628  CG2 VAL B 145      37.719  28.710  79.457  1.00 31.46           C  
ANISOU 2628  CG2 VAL B 145     4425   2760   4766    259    -97    339       C  
ATOM   2629  N   CYS B 146      36.202  31.578  78.510  1.00 27.32           N  
ANISOU 2629  N   CYS B 146     3500   2653   4227    -66    -72    351       N  
ATOM   2630  CA  CYS B 146      35.636  31.655  77.170  1.00 27.85           C  
ANISOU 2630  CA  CYS B 146     3529   2768   4283   -183    -70    280       C  
ATOM   2631  C   CYS B 146      36.497  30.850  76.178  1.00 28.89           C  
ANISOU 2631  C   CYS B 146     3728   2835   4414   -122    -73    150       C  
ATOM   2632  O   CYS B 146      37.709  30.977  76.136  1.00 28.27           O  
ANISOU 2632  O   CYS B 146     3615   2803   4322     22    -73     95       O  
ATOM   2633  CB  CYS B 146      35.555  33.102  76.711  1.00 26.87           C  
ANISOU 2633  CB  CYS B 146     3273   2817   4119   -196    -68    290       C  
ATOM   2634  SG  CYS B 146      34.598  33.247  75.175  1.00 34.30           S  
ANISOU 2634  SG  CYS B 146     4168   3856   5009   -322    -83    240       S  
ATOM   2635  N   LEU B 147      35.851  29.988  75.400  1.00 30.52           N  
ANISOU 2635  N   LEU B 147     4023   2952   4621   -239    -72     85       N  
ATOM   2636  CA  LEU B 147      36.504  29.226  74.353  1.00 31.04           C  
ANISOU 2636  CA  LEU B 147     4167   2953   4670   -188    -68    -60       C  
ATOM   2637  C   LEU B 147      35.915  29.602  73.020  1.00 30.97           C  
ANISOU 2637  C   LEU B 147     4077   3085   4604   -331    -75   -136       C  
ATOM   2638  O   LEU B 147      34.718  29.486  72.854  1.00 30.10           O  
ANISOU 2638  O   LEU B 147     3958   2995   4480   -510    -89   -117       O  
ATOM   2639  CB  LEU B 147      36.287  27.742  74.580  1.00 33.74           C  
ANISOU 2639  CB  LEU B 147     4752   3024   5042   -209    -59    -94       C  
ATOM   2640  CG  LEU B 147      37.534  26.972  75.008  1.00 37.53           C  
ANISOU 2640  CG  LEU B 147     5373   3352   5534     58    -57   -129       C  
ATOM   2641  CD1 LEU B 147      37.325  25.471  74.802  1.00 39.04           C  
ANISOU 2641  CD1 LEU B 147     5874   3224   5734     40    -39   -201       C  
ATOM   2642  CD2 LEU B 147      38.727  27.467  74.186  1.00 37.73           C  
ANISOU 2642  CD2 LEU B 147     5244   3572   5516    225    -57   -250       C  
ATOM   2643  N   ALA B 148      36.743  30.108  72.096  1.00 30.72           N  
ANISOU 2643  N   ALA B 148     3966   3188   4517   -259    -65   -218       N  
ATOM   2644  CA  ALA B 148      36.347  30.299  70.679  1.00 30.63           C  
ANISOU 2644  CA  ALA B 148     3911   3307   4419   -368    -72   -306       C  
ATOM   2645  C   ALA B 148      37.147  29.288  69.847  1.00 32.51           C  
ANISOU 2645  C   ALA B 148     4250   3472   4629   -296    -49   -484       C  
ATOM   2646  O   ALA B 148      38.373  29.245  69.949  1.00 33.68           O  
ANISOU 2646  O   ALA B 148     4380   3637   4777   -120    -18   -535       O  
ATOM   2647  CB  ALA B 148      36.665  31.703  70.216  1.00 29.03           C  
ANISOU 2647  CB  ALA B 148     3575   3311   4143   -353    -60   -252       C  
ATOM   2648  N   THR B 149      36.460  28.458  69.058  1.00 33.52           N  
ANISOU 2648  N   THR B 149     4477   3535   4722   -427    -62   -595       N  
ATOM   2649  CA  THR B 149      37.072  27.340  68.339  1.00 35.23           C  
ANISOU 2649  CA  THR B 149     4846   3627   4912   -357    -36   -786       C  
ATOM   2650  C   THR B 149      36.724  27.268  66.844  1.00 35.37           C  
ANISOU 2650  C   THR B 149     4846   3785   4806   -486    -43   -934       C  
ATOM   2651  O   THR B 149      35.682  27.767  66.419  1.00 35.04           O  
ANISOU 2651  O   THR B 149     4712   3895   4705   -670    -86   -890       O  
ATOM   2652  CB  THR B 149      36.641  25.987  68.952  1.00 37.55           C  
ANISOU 2652  CB  THR B 149     5396   3593   5278   -403    -34   -819       C  
ATOM   2653  OG1 THR B 149      35.217  26.002  69.123  1.00 39.64           O  
ANISOU 2653  OG1 THR B 149     5646   3867   5546   -681    -64   -754       O  
ATOM   2654  CG2 THR B 149      37.334  25.761  70.278  1.00 35.68           C  
ANISOU 2654  CG2 THR B 149     5236   3191   5129   -194    -23   -711       C  
ATOM   2655  N   GLY B 150      37.604  26.630  66.070  1.00 35.87           N  
ANISOU 2655  N   GLY B 150     4992   3821   4815   -364     -3  -1115       N  
ATOM   2656  CA  GLY B 150      37.369  26.316  64.644  1.00 36.29           C  
ANISOU 2656  CA  GLY B 150     5072   3980   4734   -472     -2  -1297       C  
ATOM   2657  C   GLY B 150      37.263  27.502  63.690  1.00 35.05           C  
ANISOU 2657  C   GLY B 150     4716   4162   4436   -543    -12  -1254       C  
ATOM   2658  O   GLY B 150      36.563  27.436  62.691  1.00 36.28           O  
ANISOU 2658  O   GLY B 150     4868   4443   4471   -698    -46  -1337       O  
ATOM   2659  N   PHE B 151      37.932  28.598  63.990  1.00 32.23           N  
ANISOU 2659  N   PHE B 151     4212   3953   4078   -444     16  -1121       N  
ATOM   2660  CA  PHE B 151      37.916  29.717  63.067  1.00 31.98           C  
ANISOU 2660  CA  PHE B 151     4058   4197   3896   -508     23  -1065       C  
ATOM   2661  C   PHE B 151      39.163  29.830  62.192  1.00 31.78           C  
ANISOU 2661  C   PHE B 151     3987   4337   3748   -415    111  -1188       C  
ATOM   2662  O   PHE B 151      40.247  29.400  62.580  1.00 30.39           O  
ANISOU 2662  O   PHE B 151     3802   4116   3626   -252    170  -1271       O  
ATOM   2663  CB  PHE B 151      37.624  31.032  63.792  1.00 31.47           C  
ANISOU 2663  CB  PHE B 151     3894   4195   3866   -524      6   -831       C  
ATOM   2664  CG  PHE B 151      38.595  31.373  64.893  1.00 31.35           C  
ANISOU 2664  CG  PHE B 151     3837   4112   3961   -401     54   -758       C  
ATOM   2665  CD1 PHE B 151      38.384  30.934  66.193  1.00 31.00           C  
ANISOU 2665  CD1 PHE B 151     3832   3872   4072   -348     26   -697       C  
ATOM   2666  CD2 PHE B 151      39.699  32.192  64.632  1.00 32.47           C  
ANISOU 2666  CD2 PHE B 151     3893   4416   4028   -365    131   -748       C  
ATOM   2667  CE1 PHE B 151      39.274  31.297  67.224  1.00 28.03           C  
ANISOU 2667  CE1 PHE B 151     3401   3474   3772   -232     57   -633       C  
ATOM   2668  CE2 PHE B 151      40.585  32.554  65.653  1.00 28.84           C  
ANISOU 2668  CE2 PHE B 151     3364   3944   3648   -282    168   -698       C  
ATOM   2669  CZ  PHE B 151      40.362  32.126  66.932  1.00 27.97           C  
ANISOU 2669  CZ  PHE B 151     3284   3654   3688   -205    123   -642       C  
ATOM   2670  N   TYR B 152      38.951  30.377  60.996  1.00 32.58           N  
ANISOU 2670  N   TYR B 152     4054   4659   3666   -512    116  -1201       N  
ATOM   2671  CA  TYR B 152      40.004  30.673  60.004  1.00 35.08           C  
ANISOU 2671  CA  TYR B 152     4313   5199   3816   -477    212  -1296       C  
ATOM   2672  C   TYR B 152      39.481  31.840  59.148  1.00 35.66           C  
ANISOU 2672  C   TYR B 152     4361   5482   3703   -610    199  -1154       C  
ATOM   2673  O   TYR B 152      38.343  31.799  58.708  1.00 35.46           O  
ANISOU 2673  O   TYR B 152     4375   5484   3613   -695    106  -1129       O  
ATOM   2674  CB  TYR B 152      40.329  29.448  59.101  1.00 36.57           C  
ANISOU 2674  CB  TYR B 152     4578   5394   3920   -422    243  -1572       C  
ATOM   2675  CG  TYR B 152      41.450  29.791  58.130  1.00 38.61           C  
ANISOU 2675  CG  TYR B 152     4747   5929   3991   -382    359  -1672       C  
ATOM   2676  CD1 TYR B 152      42.818  29.573  58.471  1.00 37.47           C  
ANISOU 2676  CD1 TYR B 152     4507   5849   3879   -207    460  -1771       C  
ATOM   2677  CD2 TYR B 152      41.163  30.402  56.905  1.00 37.97           C  
ANISOU 2677  CD2 TYR B 152     4657   6088   3681   -517    372  -1655       C  
ATOM   2678  CE1 TYR B 152      43.838  29.954  57.639  1.00 37.55           C  
ANISOU 2678  CE1 TYR B 152     4395   6165   3705   -199    581  -1859       C  
ATOM   2679  CE2 TYR B 152      42.180  30.755  56.052  1.00 40.56           C  
ANISOU 2679  CE2 TYR B 152     4905   6683   3820   -511    495  -1730       C  
ATOM   2680  CZ  TYR B 152      43.509  30.531  56.419  1.00 41.86           C  
ANISOU 2680  CZ  TYR B 152     4955   6920   4026   -368    607  -1838       C  
ATOM   2681  OH  TYR B 152      44.485  30.899  55.529  1.00 45.47           O  
ANISOU 2681  OH  TYR B 152     5304   7698   4272   -394    743  -1922       O  
ATOM   2682  N   PRO B 153      40.292  32.910  58.934  1.00 36.72           N  
ANISOU 2682  N   PRO B 153     4440   5774   3738   -633    290  -1053       N  
ATOM   2683  CA  PRO B 153      41.657  33.110  59.372  1.00 37.08           C  
ANISOU 2683  CA  PRO B 153     4391   5878   3820   -577    404  -1089       C  
ATOM   2684  C   PRO B 153      41.626  33.583  60.815  1.00 36.09           C  
ANISOU 2684  C   PRO B 153     4241   5584   3887   -548    374   -936       C  
ATOM   2685  O   PRO B 153      40.525  33.665  61.427  1.00 34.62           O  
ANISOU 2685  O   PRO B 153     4117   5230   3805   -559    274   -814       O  
ATOM   2686  CB  PRO B 153      42.162  34.202  58.423  1.00 39.32           C  
ANISOU 2686  CB  PRO B 153     4661   6403   3875   -708    504  -1013       C  
ATOM   2687  CG  PRO B 153      40.920  35.041  58.165  1.00 37.94           C  
ANISOU 2687  CG  PRO B 153     4604   6181   3628   -791    413   -804       C  
ATOM   2688  CD  PRO B 153      39.737  34.136  58.324  1.00 36.15           C  
ANISOU 2688  CD  PRO B 153     4409   5826   3498   -736    274   -861       C  
ATOM   2689  N   ASP B 154      42.797  33.838  61.389  1.00 35.73           N  
ANISOU 2689  N   ASP B 154     4085   5610   3878   -512    458   -959       N  
ATOM   2690  CA  ASP B 154      42.825  34.156  62.791  1.00 35.40           C  
ANISOU 2690  CA  ASP B 154     4017   5424   4008   -475    425   -847       C  
ATOM   2691  C   ASP B 154      42.676  35.669  62.961  1.00 33.03           C  
ANISOU 2691  C   ASP B 154     3755   5142   3651   -636    454   -645       C  
ATOM   2692  O   ASP B 154      43.594  36.379  63.358  1.00 32.81           O  
ANISOU 2692  O   ASP B 154     3653   5209   3602   -712    536   -624       O  
ATOM   2693  CB  ASP B 154      44.037  33.515  63.491  1.00 37.53           C  
ANISOU 2693  CB  ASP B 154     4150   5755   4354   -320    467   -984       C  
ATOM   2694  CG  ASP B 154      45.313  34.313  63.332  1.00 45.58           C  
ANISOU 2694  CG  ASP B 154     5006   7055   5256   -410    588  -1016       C  
ATOM   2695  OD1 ASP B 154      45.611  34.688  62.176  1.00 50.93           O  
ANISOU 2695  OD1 ASP B 154     5670   7929   5752   -533    676  -1057       O  
ATOM   2696  OD2 ASP B 154      46.014  34.573  64.370  1.00 50.27           O  
ANISOU 2696  OD2 ASP B 154     5480   7696   5923   -379    599  -1004       O  
ATOM   2697  N   HIS B 155      41.500  36.136  62.574  1.00 30.93           N  
ANISOU 2697  N   HIS B 155     3616   4796   3339   -688    389   -511       N  
ATOM   2698  CA  HIS B 155      41.135  37.533  62.585  1.00 29.60           C  
ANISOU 2698  CA  HIS B 155     3558   4595   3094   -792    404   -309       C  
ATOM   2699  C   HIS B 155      39.916  37.592  63.495  1.00 28.50           C  
ANISOU 2699  C   HIS B 155     3471   4262   3095   -708    288   -189       C  
ATOM   2700  O   HIS B 155      38.777  37.504  63.023  1.00 27.05           O  
ANISOU 2700  O   HIS B 155     3339   4075   2863   -674    201   -137       O  
ATOM   2701  CB  HIS B 155      40.726  37.983  61.179  1.00 31.26           C  
ANISOU 2701  CB  HIS B 155     3873   4926   3078   -862    417   -254       C  
ATOM   2702  CG  HIS B 155      41.836  37.956  60.174  1.00 34.59           C  
ANISOU 2702  CG  HIS B 155     4247   5570   3323   -964    545   -366       C  
ATOM   2703  ND1 HIS B 155      41.625  38.217  58.838  1.00 37.89           N  
ANISOU 2703  ND1 HIS B 155     4753   6134   3507  -1029    570   -341       N  
ATOM   2704  CD2 HIS B 155      43.166  37.722  60.306  1.00 35.01           C  
ANISOU 2704  CD2 HIS B 155     4156   5766   3377  -1008    659   -506       C  
ATOM   2705  CE1 HIS B 155      42.771  38.125  58.184  1.00 40.37           C  
ANISOU 2705  CE1 HIS B 155     4988   6661   3689  -1124    706   -463       C  
ATOM   2706  NE2 HIS B 155      43.722  37.827  59.051  1.00 41.34           N  
ANISOU 2706  NE2 HIS B 155     4954   6799   3952  -1109    762   -571       N  
ATOM   2707  N   VAL B 156      40.173  37.694  64.797  1.00 26.38           N  
ANISOU 2707  N   VAL B 156     3163   3877   2981   -675    286   -162       N  
ATOM   2708  CA  VAL B 156      39.133  37.832  65.821  1.00 25.26           C  
ANISOU 2708  CA  VAL B 156     3057   3573   2966   -601    199    -51       C  
ATOM   2709  C   VAL B 156      39.534  38.896  66.845  1.00 25.17           C  
ANISOU 2709  C   VAL B 156     3088   3473   2999   -637    243     47       C  
ATOM   2710  O   VAL B 156      40.715  39.171  67.045  1.00 22.86           O  
ANISOU 2710  O   VAL B 156     2749   3245   2691   -719    327     -9       O  
ATOM   2711  CB  VAL B 156      38.849  36.485  66.599  1.00 23.87           C  
ANISOU 2711  CB  VAL B 156     2803   3309   2954   -508    133   -146       C  
ATOM   2712  CG1 VAL B 156      38.176  35.486  65.703  1.00 24.07           C  
ANISOU 2712  CG1 VAL B 156     2833   3372   2940   -507     80   -242       C  
ATOM   2713  CG2 VAL B 156      40.186  35.877  67.125  1.00 23.80           C  
ANISOU 2713  CG2 VAL B 156     2706   3323   3013   -461    188   -272       C  
ATOM   2714  N   GLU B 157      38.515  39.432  67.529  1.00 26.93           N  
ANISOU 2714  N   GLU B 157     3385   3574   3274   -573    184    176       N  
ATOM   2715  CA  GLU B 157      38.687  40.293  68.712  1.00 27.67           C  
ANISOU 2715  CA  GLU B 157     3532   3548   3430   -579    209    250       C  
ATOM   2716  C   GLU B 157      37.701  39.807  69.805  1.00 26.55           C  
ANISOU 2716  C   GLU B 157     3341   3321   3425   -456    125    284       C  
ATOM   2717  O   GLU B 157      36.505  39.789  69.597  1.00 26.24           O  
ANISOU 2717  O   GLU B 157     3317   3284   3369   -381     60    350       O  
ATOM   2718  CB  GLU B 157      38.431  41.748  68.353  1.00 28.99           C  
ANISOU 2718  CB  GLU B 157     3903   3638   3471   -620    251    390       C  
ATOM   2719  CG  GLU B 157      39.589  42.427  67.585  1.00 34.88           C  
ANISOU 2719  CG  GLU B 157     4733   4440   4078   -811    370    372       C  
ATOM   2720  CD  GLU B 157      39.121  43.722  66.938  1.00 41.07           C  
ANISOU 2720  CD  GLU B 157     5791   5112   4701   -831    404    537       C  
ATOM   2721  OE1 GLU B 157      37.883  43.927  66.881  1.00 43.15           O  
ANISOU 2721  OE1 GLU B 157     6134   5309   4949   -648    316    646       O  
ATOM   2722  OE2 GLU B 157      39.969  44.521  66.468  1.00 42.58           O  
ANISOU 2722  OE2 GLU B 157     6122   5291   4765  -1024    519    559       O  
ATOM   2723  N   LEU B 158      38.239  39.379  70.937  1.00 25.44           N  
ANISOU 2723  N   LEU B 158     3124   3142   3396   -442    129    232       N  
ATOM   2724  CA  LEU B 158      37.452  38.758  71.987  1.00 25.35           C  
ANISOU 2724  CA  LEU B 158     3067   3064   3499   -352     68    257       C  
ATOM   2725  C   LEU B 158      37.354  39.767  73.077  1.00 24.72           C  
ANISOU 2725  C   LEU B 158     3049   2905   3437   -333     85    334       C  
ATOM   2726  O   LEU B 158      38.360  40.345  73.455  1.00 24.58           O  
ANISOU 2726  O   LEU B 158     3051   2886   3402   -403    138    303       O  
ATOM   2727  CB  LEU B 158      38.125  37.456  72.477  1.00 25.09           C  
ANISOU 2727  CB  LEU B 158     2943   3031   3555   -318     56    153       C  
ATOM   2728  CG  LEU B 158      37.411  36.542  73.488  1.00 26.13           C  
ANISOU 2728  CG  LEU B 158     3060   3075   3789   -253      5    179       C  
ATOM   2729  CD1 LEU B 158      38.062  35.180  73.521  1.00 22.56           C  
ANISOU 2729  CD1 LEU B 158     2592   2590   3387   -200     -3     78       C  
ATOM   2730  CD2 LEU B 158      37.519  37.253  74.933  1.00 28.70           C  
ANISOU 2730  CD2 LEU B 158     3391   3360   4150   -219     13    249       C  
ATOM   2731  N   SER B 159      36.136  40.016  73.554  1.00 24.67           N  
ANISOU 2731  N   SER B 159     3066   2858   3447   -248     45    421       N  
ATOM   2732  CA  SER B 159      35.938  41.001  74.581  1.00 25.10           C  
ANISOU 2732  CA  SER B 159     3199   2831   3505   -203     65    482       C  
ATOM   2733  C   SER B 159      35.051  40.366  75.686  1.00 24.72           C  
ANISOU 2733  C   SER B 159     3064   2791   3537   -121     24    506       C  
ATOM   2734  O   SER B 159      34.288  39.454  75.406  1.00 22.99           O  
ANISOU 2734  O   SER B 159     2758   2634   3343   -112    -17    505       O  
ATOM   2735  CB  SER B 159      35.326  42.283  73.969  1.00 26.72           C  
ANISOU 2735  CB  SER B 159     3566   2985   3601   -146     80    575       C  
ATOM   2736  OG  SER B 159      34.126  41.992  73.278  1.00 26.64           O  
ANISOU 2736  OG  SER B 159     3502   3068   3550    -45     16    624       O  
ATOM   2737  N   TRP B 160      35.184  40.843  76.923  1.00 23.77           N  
ANISOU 2737  N   TRP B 160     2973   2617   3439    -91     45    519       N  
ATOM   2738  CA  TRP B 160      34.329  40.383  78.058  1.00 24.12           C  
ANISOU 2738  CA  TRP B 160     2948   2684   3530    -22     25    554       C  
ATOM   2739  C   TRP B 160      33.487  41.529  78.535  1.00 24.16           C  
ANISOU 2739  C   TRP B 160     3026   2671   3481     90     42    612       C  
ATOM   2740  O   TRP B 160      33.995  42.628  78.761  1.00 25.84           O  
ANISOU 2740  O   TRP B 160     3380   2787   3651     95     82    605       O  
ATOM   2741  CB  TRP B 160      35.159  39.931  79.275  1.00 23.48           C  
ANISOU 2741  CB  TRP B 160     2842   2583   3496    -45     32    518       C  
ATOM   2742  CG  TRP B 160      35.774  38.497  79.210  1.00 23.86           C  
ANISOU 2742  CG  TRP B 160     2821   2642   3601    -77      5    475       C  
ATOM   2743  CD1 TRP B 160      37.063  38.163  78.922  1.00 21.20           C  
ANISOU 2743  CD1 TRP B 160     2463   2323   3267   -101      5    397       C  
ATOM   2744  CD2 TRP B 160      35.110  37.267  79.548  1.00 22.30           C  
ANISOU 2744  CD2 TRP B 160     2591   2431   3449    -73    -16    506       C  
ATOM   2745  NE1 TRP B 160      37.245  36.801  79.062  1.00 22.04           N  
ANISOU 2745  NE1 TRP B 160     2545   2407   3420    -61    -23    380       N  
ATOM   2746  CE2 TRP B 160      36.054  36.231  79.426  1.00 20.49           C  
ANISOU 2746  CE2 TRP B 160     2368   2163   3252    -65    -33    451       C  
ATOM   2747  CE3 TRP B 160      33.809  36.951  79.932  1.00 22.19           C  
ANISOU 2747  CE3 TRP B 160     2548   2444   3438    -85    -16    569       C  
ATOM   2748  CZ2 TRP B 160      35.733  34.902  79.644  1.00 22.92           C  
ANISOU 2748  CZ2 TRP B 160     2714   2395   3599    -69    -47    468       C  
ATOM   2749  CZ3 TRP B 160      33.498  35.618  80.174  1.00 24.40           C  
ANISOU 2749  CZ3 TRP B 160     2837   2679   3755   -143    -22    583       C  
ATOM   2750  CH2 TRP B 160      34.449  34.608  80.018  1.00 21.36           C  
ANISOU 2750  CH2 TRP B 160     2517   2191   3404   -135    -37    537       C  
ATOM   2751  N   TRP B 161      32.217  41.266  78.771  1.00 24.56           N  
ANISOU 2751  N   TRP B 161     2985   2821   3526    175     21    657       N  
ATOM   2752  CA  TRP B 161      31.260  42.327  79.129  1.00 25.78           C  
ANISOU 2752  CA  TRP B 161     3185   3000   3610    345     34    704       C  
ATOM   2753  C   TRP B 161      30.549  41.972  80.414  1.00 25.84           C  
ANISOU 2753  C   TRP B 161     3083   3100   3632    387     51    712       C  
ATOM   2754  O   TRP B 161      29.992  40.896  80.496  1.00 26.89           O  
ANISOU 2754  O   TRP B 161     3064   3354   3796    312     35    718       O  
ATOM   2755  CB  TRP B 161      30.256  42.524  77.991  1.00 23.89           C  
ANISOU 2755  CB  TRP B 161     2897   2881   3297    449     -9    747       C  
ATOM   2756  CG  TRP B 161      30.929  42.988  76.709  1.00 26.74           C  
ANISOU 2756  CG  TRP B 161     3398   3151   3609    416    -16    757       C  
ATOM   2757  CD1 TRP B 161      31.710  42.232  75.838  1.00 26.13           C  
ANISOU 2757  CD1 TRP B 161     3293   3072   3561    253    -28    713       C  
ATOM   2758  CD2 TRP B 161      30.838  44.303  76.113  1.00 25.04           C  
ANISOU 2758  CD2 TRP B 161     3391   2836   3286    556     -4    818       C  
ATOM   2759  NE1 TRP B 161      32.105  43.004  74.773  1.00 26.10           N  
ANISOU 2759  NE1 TRP B 161     3442   3004   3468    261    -18    744       N  
ATOM   2760  CE2 TRP B 161      31.588  44.271  74.913  1.00 25.20           C  
ANISOU 2760  CE2 TRP B 161     3493   2812   3269    438     -4    819       C  
ATOM   2761  CE3 TRP B 161      30.206  45.493  76.491  1.00 25.95           C  
ANISOU 2761  CE3 TRP B 161     3657   2881   3320    783     13    872       C  
ATOM   2762  CZ2 TRP B 161      31.758  45.385  74.115  1.00 27.26           C  
ANISOU 2762  CZ2 TRP B 161     3997   2950   3411    504     18    889       C  
ATOM   2763  CZ3 TRP B 161      30.345  46.616  75.675  1.00 27.97           C  
ANISOU 2763  CZ3 TRP B 161     4182   2982   3462    884     28    942       C  
ATOM   2764  CH2 TRP B 161      31.107  46.544  74.482  1.00 30.00           C  
ANISOU 2764  CH2 TRP B 161     4528   3191   3679    730     31    960       C  
ATOM   2765  N   VAL B 162      30.623  42.830  81.432  1.00 26.30           N  
ANISOU 2765  N   VAL B 162     3237   3094   3659    478     94    703       N  
ATOM   2766  CA  VAL B 162      29.863  42.570  82.662  1.00 26.03           C  
ANISOU 2766  CA  VAL B 162     3097   3182   3610    532    122    711       C  
ATOM   2767  C   VAL B 162      28.808  43.571  82.959  1.00 26.47           C  
ANISOU 2767  C   VAL B 162     3163   3317   3576    759    148    722       C  
ATOM   2768  O   VAL B 162      29.067  44.768  82.974  1.00 27.57           O  
ANISOU 2768  O   VAL B 162     3502   3305   3666    885    171    704       O  
ATOM   2769  CB  VAL B 162      30.677  42.042  83.929  1.00 26.39           C  
ANISOU 2769  CB  VAL B 162     3155   3182   3688    425    145    687       C  
ATOM   2770  CG1 VAL B 162      32.123  41.619  83.675  1.00 24.45           C  
ANISOU 2770  CG1 VAL B 162     2972   2819   3499    285    120    650       C  
ATOM   2771  CG2 VAL B 162      30.380  42.803  85.279  1.00 28.23           C  
ANISOU 2771  CG2 VAL B 162     3438   3438   3849    537    198    664       C  
ATOM   2772  N   ASN B 163      27.569  43.097  83.083  1.00 28.51           N  
ANISOU 2772  N   ASN B 163     3210   3822   3800    818    147    746       N  
ATOM   2773  CA  ASN B 163      26.381  43.998  83.186  1.00 28.73           C  
ANISOU 2773  CA  ASN B 163     3186   4009   3720   1095    163    749       C  
ATOM   2774  C   ASN B 163      26.382  45.050  82.096  1.00 29.95           C  
ANISOU 2774  C   ASN B 163     3510   4049   3819   1289    125    772       C  
ATOM   2775  O   ASN B 163      26.016  46.222  82.308  1.00 31.39           O  
ANISOU 2775  O   ASN B 163     3842   4170   3915   1559    150    768       O  
ATOM   2776  CB  ASN B 163      26.285  44.602  84.617  1.00 29.08           C  
ANISOU 2776  CB  ASN B 163     3294   4040   3714   1211    237    710       C  
ATOM   2777  CG  ASN B 163      26.069  43.535  85.645  1.00 30.94           C  
ANISOU 2777  CG  ASN B 163     3351   4439   3965   1039    277    714       C  
ATOM   2778  OD1 ASN B 163      25.296  42.586  85.370  1.00 34.03           O  
ANISOU 2778  OD1 ASN B 163     3512   5059   4357    928    267    743       O  
ATOM   2779  ND2 ASN B 163      26.791  43.596  86.812  1.00 25.45           N  
ANISOU 2779  ND2 ASN B 163     2769   3629   3270    977    320    686       N  
ATOM   2780  N   GLY B 164      26.782  44.639  80.898  1.00 29.72           N  
ANISOU 2780  N   GLY B 164     3488   3980   3824   1166     69    798       N  
ATOM   2781  CA  GLY B 164      26.617  45.510  79.741  1.00 30.99           C  
ANISOU 2781  CA  GLY B 164     3791   4082   3901   1349     27    844       C  
ATOM   2782  C   GLY B 164      27.804  46.420  79.427  1.00 32.03           C  
ANISOU 2782  C   GLY B 164     4272   3862   4035   1311     59    853       C  
ATOM   2783  O   GLY B 164      27.688  47.273  78.550  1.00 33.46           O  
ANISOU 2783  O   GLY B 164     4641   3946   4125   1472     41    910       O  
ATOM   2784  N   LYS B 165      28.918  46.257  80.155  1.00 29.76           N  
ANISOU 2784  N   LYS B 165     4072   3404   3829   1097    108    798       N  
ATOM   2785  CA  LYS B 165      30.082  47.152  80.034  1.00 29.82           C  
ANISOU 2785  CA  LYS B 165     4388   3115   3826   1003    156    779       C  
ATOM   2786  C   LYS B 165      31.343  46.333  79.859  1.00 27.84           C  
ANISOU 2786  C   LYS B 165     4076   2836   3664    697    155    734       C  
ATOM   2787  O   LYS B 165      31.557  45.284  80.553  1.00 25.43           O  
ANISOU 2787  O   LYS B 165     3574   2647   3439    579    143    695       O  
ATOM   2788  CB  LYS B 165      30.251  48.002  81.281  1.00 31.53           C  
ANISOU 2788  CB  LYS B 165     4777   3183   4017   1065    221    719       C  
ATOM   2789  CG  LYS B 165      28.975  48.560  81.817  1.00 36.66           C  
ANISOU 2789  CG  LYS B 165     5417   3922   4588   1391    230    731       C  
ATOM   2790  CD  LYS B 165      29.130  49.957  82.423  1.00 45.81           C  
ANISOU 2790  CD  LYS B 165     6930   4808   5667   1535    301    684       C  
ATOM   2791  CE  LYS B 165      27.822  50.738  82.188  1.00 50.39           C  
ANISOU 2791  CE  LYS B 165     7580   5435   6129   1962    292    735       C  
ATOM   2792  NZ  LYS B 165      27.835  52.074  82.856  1.00 55.36           N  
ANISOU 2792  NZ  LYS B 165     8586   5776   6670   2156    367    677       N  
ATOM   2793  N   GLU B 166      32.193  46.787  78.952  1.00 26.79           N  
ANISOU 2793  N   GLU B 166     4117   2559   3502    578    174    742       N  
ATOM   2794  CA  GLU B 166      33.364  46.028  78.631  1.00 25.78           C  
ANISOU 2794  CA  GLU B 166     3901   2456   3436    325    175    689       C  
ATOM   2795  C   GLU B 166      34.314  46.124  79.832  1.00 26.38           C  
ANISOU 2795  C   GLU B 166     3996   2478   3548    187    215    597       C  
ATOM   2796  O   GLU B 166      34.506  47.186  80.380  1.00 27.67           O  
ANISOU 2796  O   GLU B 166     4367   2488   3657    190    266    567       O  
ATOM   2797  CB  GLU B 166      34.020  46.551  77.339  1.00 25.85           C  
ANISOU 2797  CB  GLU B 166     4079   2364   3376    218    202    716       C  
ATOM   2798  CG  GLU B 166      35.216  45.700  76.998  1.00 25.07           C  
ANISOU 2798  CG  GLU B 166     3844   2350   3332    -15    208    642       C  
ATOM   2799  CD  GLU B 166      35.832  45.887  75.619  1.00 30.94           C  
ANISOU 2799  CD  GLU B 166     4672   3079   4002   -141    237    659       C  
ATOM   2800  OE1 GLU B 166      35.499  46.827  74.878  1.00 33.55           O  
ANISOU 2800  OE1 GLU B 166     5231   3290   4225    -84    262    744       O  
ATOM   2801  OE2 GLU B 166      36.743  45.076  75.301  1.00 33.75           O  
ANISOU 2801  OE2 GLU B 166     4875   3550   4395   -295    241    583       O  
ATOM   2802  N   VAL B 167      34.862  45.006  80.277  1.00 26.77           N  
ANISOU 2802  N   VAL B 167     3841   2656   3673     84    186    549       N  
ATOM   2803  CA  VAL B 167      35.834  45.035  81.350  1.00 27.80           C  
ANISOU 2803  CA  VAL B 167     3959   2790   3811    -31    205    461       C  
ATOM   2804  C   VAL B 167      37.222  44.619  80.823  1.00 29.80           C  
ANISOU 2804  C   VAL B 167     4139   3107   4075   -226    207    390       C  
ATOM   2805  O   VAL B 167      37.338  43.890  79.802  1.00 29.48           O  
ANISOU 2805  O   VAL B 167     4006   3130   4064   -245    185    408       O  
ATOM   2806  CB  VAL B 167      35.405  44.137  82.517  1.00 27.03           C  
ANISOU 2806  CB  VAL B 167     3700   2810   3757     48    169    467       C  
ATOM   2807  CG1 VAL B 167      34.098  44.694  83.197  1.00 27.05           C  
ANISOU 2807  CG1 VAL B 167     3755   2799   3722    231    189    511       C  
ATOM   2808  CG2 VAL B 167      35.220  42.706  82.063  1.00 26.13           C  
ANISOU 2808  CG2 VAL B 167     3406   2805   3715     48    119    506       C  
ATOM   2809  N   HIS B 168      38.263  45.062  81.526  1.00 30.81           N  
ANISOU 2809  N   HIS B 168     4289   3250   4165   -367    233    293       N  
ATOM   2810  CA  HIS B 168      39.628  44.688  81.223  1.00 31.53           C  
ANISOU 2810  CA  HIS B 168     4255   3477   4245   -539    236    201       C  
ATOM   2811  C   HIS B 168      40.337  44.190  82.467  1.00 31.26           C  
ANISOU 2811  C   HIS B 168     4068   3602   4207   -545    193    121       C  
ATOM   2812  O   HIS B 168      41.251  43.378  82.361  1.00 33.16           O  
ANISOU 2812  O   HIS B 168     4124   4021   4454   -570    159     64       O  
ATOM   2813  CB  HIS B 168      40.378  45.877  80.618  1.00 34.88           C  
ANISOU 2813  CB  HIS B 168     4851   3821   4581   -767    320    145       C  
ATOM   2814  CG  HIS B 168      39.701  46.465  79.410  1.00 36.77           C  
ANISOU 2814  CG  HIS B 168     5289   3889   4790   -740    362    246       C  
ATOM   2815  ND1 HIS B 168      39.748  45.868  78.167  1.00 40.05           N  
ANISOU 2815  ND1 HIS B 168     5625   4378   5214   -739    354    287       N  
ATOM   2816  CD2 HIS B 168      38.950  47.581  79.261  1.00 39.64           C  
ANISOU 2816  CD2 HIS B 168     5943   4021   5098   -682    405    316       C  
ATOM   2817  CE1 HIS B 168      39.043  46.582  77.307  1.00 38.55           C  
ANISOU 2817  CE1 HIS B 168     5650   4028   4967   -689    384    387       C  
ATOM   2818  NE2 HIS B 168      38.555  47.633  77.942  1.00 40.62           N  
ANISOU 2818  NE2 HIS B 168     6147   4097   5190   -639    414    413       N  
ATOM   2819  N   SER B 169      39.909  44.611  83.651  1.00 30.71           N  
ANISOU 2819  N   SER B 169     4067   3490   4110   -491    189    115       N  
ATOM   2820  CA  SER B 169      40.530  44.152  84.886  1.00 31.02           C  
ANISOU 2820  CA  SER B 169     3970   3699   4117   -480    138     49       C  
ATOM   2821  C   SER B 169      40.090  42.725  85.208  1.00 28.58           C  
ANISOU 2821  C   SER B 169     3520   3466   3872   -288     69    140       C  
ATOM   2822  O   SER B 169      38.973  42.379  84.993  1.00 28.83           O  
ANISOU 2822  O   SER B 169     3591   3401   3959   -177     73    243       O  
ATOM   2823  CB  SER B 169      40.204  45.149  86.029  1.00 32.79           C  
ANISOU 2823  CB  SER B 169     4342   3849   4266   -498    167      1       C  
ATOM   2824  OG  SER B 169      40.137  44.521  87.319  1.00 35.21           O  
ANISOU 2824  OG  SER B 169     4542   4292   4544   -386    110      4       O  
ATOM   2825  N   GLY B 170      40.957  41.855  85.701  1.00 28.76           N  
ANISOU 2825  N   GLY B 170     3385   3666   3874   -246      7    104       N  
ATOM   2826  CA  GLY B 170      40.512  40.470  85.879  1.00 26.80           C  
ANISOU 2826  CA  GLY B 170     3079   3421   3683    -70    -43    208       C  
ATOM   2827  C   GLY B 170      40.446  39.549  84.639  1.00 24.67           C  
ANISOU 2827  C   GLY B 170     2774   3100   3496    -27    -49    244       C  
ATOM   2828  O   GLY B 170      39.919  38.427  84.717  1.00 25.23           O  
ANISOU 2828  O   GLY B 170     2856   3114   3616     86    -77    329       O  
ATOM   2829  N   VAL B 171      41.008  39.986  83.535  1.00 24.69           N  
ANISOU 2829  N   VAL B 171     2754   3125   3501   -136    -17    173       N  
ATOM   2830  CA  VAL B 171      40.927  39.323  82.230  1.00 25.71           C  
ANISOU 2830  CA  VAL B 171     2865   3214   3688   -119    -10    184       C  
ATOM   2831  C   VAL B 171      42.345  38.973  81.686  1.00 28.39           C  
ANISOU 2831  C   VAL B 171     3057   3739   3990   -134    -18     66       C  
ATOM   2832  O   VAL B 171      43.294  39.744  81.811  1.00 28.83           O  
ANISOU 2832  O   VAL B 171     3036   3946   3968   -263      4    -33       O  
ATOM   2833  CB  VAL B 171      40.235  40.284  81.152  1.00 26.99           C  
ANISOU 2833  CB  VAL B 171     3142   3257   3855   -231     51    211       C  
ATOM   2834  CG1 VAL B 171      40.339  39.719  79.729  1.00 26.42           C  
ANISOU 2834  CG1 VAL B 171     3040   3191   3806   -242     59    196       C  
ATOM   2835  CG2 VAL B 171      38.724  40.580  81.476  1.00 23.24           C  
ANISOU 2835  CG2 VAL B 171     2776   2646   3406   -166     56    320       C  
ATOM   2836  N   CYS B 172      42.500  37.760  81.153  1.00 30.13           N  
ANISOU 2836  N   CYS B 172     3232   3963   4250     -1    -48     64       N  
ATOM   2837  CA  CYS B 172      43.451  37.539  80.055  1.00 31.57           C  
ANISOU 2837  CA  CYS B 172     3304   4284   4405    -23    -24    -43       C  
ATOM   2838  C   CYS B 172      43.045  36.570  78.996  1.00 29.02           C  
ANISOU 2838  C   CYS B 172     3030   3858   4138     57    -22    -33       C  
ATOM   2839  O   CYS B 172      42.416  35.558  79.259  1.00 27.34           O  
ANISOU 2839  O   CYS B 172     2903   3500   3983    188    -62     30       O  
ATOM   2840  CB  CYS B 172      44.941  37.477  80.387  1.00 35.48           C  
ANISOU 2840  CB  CYS B 172     3594   5072   4812     12    -43   -174       C  
ATOM   2841  SG  CYS B 172      45.668  36.043  80.977  1.00 47.67           S  
ANISOU 2841  SG  CYS B 172     5034   6736   6340    330   -133   -203       S  
ATOM   2842  N   THR B 173      43.407  36.973  77.786  1.00 28.68           N  
ANISOU 2842  N   THR B 173     2949   3889   4057    -57     34   -102       N  
ATOM   2843  CA  THR B 173      43.156  36.295  76.559  1.00 28.22           C  
ANISOU 2843  CA  THR B 173     2925   3781   4017    -28     50   -129       C  
ATOM   2844  C   THR B 173      44.501  35.801  76.036  1.00 29.31           C  
ANISOU 2844  C   THR B 173     2898   4147   4091     49     69   -278       C  
ATOM   2845  O   THR B 173      45.506  36.539  76.104  1.00 29.49           O  
ANISOU 2845  O   THR B 173     2772   4401   4029    -55    109   -358       O  
ATOM   2846  CB  THR B 173      42.493  37.264  75.629  1.00 28.29           C  
ANISOU 2846  CB  THR B 173     3022   3729   3996   -208    104    -82       C  
ATOM   2847  OG1 THR B 173      41.290  37.698  76.279  1.00 29.23           O  
ANISOU 2847  OG1 THR B 173     3260   3681   4162   -220     79     43       O  
ATOM   2848  CG2 THR B 173      42.106  36.580  74.299  1.00 27.37           C  
ANISOU 2848  CG2 THR B 173     2943   3578   3876   -191    112   -111       C  
ATOM   2849  N   ASP B 174      44.559  34.554  75.569  1.00 29.45           N  
ANISOU 2849  N   ASP B 174     2937   4115   4135    230     46   -329       N  
ATOM   2850  CA  ASP B 174      45.799  34.069  74.899  1.00 32.67           C  
ANISOU 2850  CA  ASP B 174     3183   4762   4467    343     75   -491       C  
ATOM   2851  C   ASP B 174      46.312  35.081  73.874  1.00 33.59           C  
ANISOU 2851  C   ASP B 174     3191   5087   4486    109    171   -561       C  
ATOM   2852  O   ASP B 174      45.548  35.572  73.065  1.00 33.38           O  
ANISOU 2852  O   ASP B 174     3286   4940   4456    -55    210   -502       O  
ATOM   2853  CB  ASP B 174      45.595  32.720  74.196  1.00 32.61           C  
ANISOU 2853  CB  ASP B 174     3282   4616   4492    536     60   -550       C  
ATOM   2854  CG  ASP B 174      44.945  31.687  75.084  1.00 34.88           C  
ANISOU 2854  CG  ASP B 174     3754   4631   4867    715    -13   -461       C  
ATOM   2855  OD1 ASP B 174      45.145  31.682  76.336  1.00 38.24           O  
ANISOU 2855  OD1 ASP B 174     4161   5065   5301    817    -66   -392       O  
ATOM   2856  OD2 ASP B 174      44.204  30.850  74.528  1.00 39.18           O  
ANISOU 2856  OD2 ASP B 174     4479   4947   5458    734    -16   -461       O  
ATOM   2857  N   PRO B 175      47.595  35.431  73.923  1.00 37.05           N  
ANISOU 2857  N   PRO B 175     3399   5855   4823     79    211   -683       N  
ATOM   2858  CA  PRO B 175      48.089  36.375  72.905  1.00 39.89           C  
ANISOU 2858  CA  PRO B 175     3678   6408   5068   -191    325   -744       C  
ATOM   2859  C   PRO B 175      48.121  35.681  71.569  1.00 42.68           C  
ANISOU 2859  C   PRO B 175     4041   6794   5381   -117    371   -826       C  
ATOM   2860  O   PRO B 175      47.886  36.299  70.547  1.00 42.59           O  
ANISOU 2860  O   PRO B 175     4098   6784   5300   -325    450   -806       O  
ATOM   2861  CB  PRO B 175      49.524  36.649  73.339  1.00 41.90           C  
ANISOU 2861  CB  PRO B 175     3637   7068   5213   -221    355   -887       C  
ATOM   2862  CG  PRO B 175      49.880  35.515  74.213  1.00 41.80           C  
ANISOU 2862  CG  PRO B 175     3530   7108   5243    143    248   -931       C  
ATOM   2863  CD  PRO B 175      48.625  35.092  74.906  1.00 37.60           C  
ANISOU 2863  CD  PRO B 175     3265   6166   4853    258    159   -764       C  
ATOM   2864  N   GLN B 176      48.376  34.375  71.606  1.00 46.09           N  
ANISOU 2864  N   GLN B 176     4436   7228   5845    195    319   -914       N  
ATOM   2865  CA  GLN B 176      48.400  33.553  70.378  1.00 49.80           C  
ANISOU 2865  CA  GLN B 176     4939   7705   6275    305    358  -1023       C  
ATOM   2866  C   GLN B 176      47.340  32.443  70.306  1.00 48.71           C  
ANISOU 2866  C   GLN B 176     5054   7203   6249    476    285   -978       C  
ATOM   2867  O   GLN B 176      47.123  31.699  71.272  1.00 48.63           O  
ANISOU 2867  O   GLN B 176     5132   7012   6330    680    202   -932       O  
ATOM   2868  CB  GLN B 176      49.814  32.990  70.112  1.00 52.65           C  
ANISOU 2868  CB  GLN B 176     5035   8442   6525    511    400  -1229       C  
ATOM   2869  CG  GLN B 176      50.557  33.771  69.037  1.00 57.60           C  
ANISOU 2869  CG  GLN B 176     5479   9416   6989    267    537  -1332       C  
ATOM   2870  CD  GLN B 176      51.641  34.705  69.573  1.00 61.39           C  
ANISOU 2870  CD  GLN B 176     5674  10283   7366     84    590  -1385       C  
ATOM   2871  OE1 GLN B 176      51.929  34.738  70.769  1.00 62.93           O  
ANISOU 2871  OE1 GLN B 176     5777  10528   7605    174    512  -1365       O  
ATOM   2872  NE2 GLN B 176      52.268  35.455  68.663  1.00 63.73           N  
ANISOU 2872  NE2 GLN B 176     5829  10877   7505   -196    729  -1461       N  
ATOM   2873  N   PRO B 177      46.672  32.335  69.156  1.00 49.07           N  
ANISOU 2873  N   PRO B 177     5226   7149   6268    370    318   -991       N  
ATOM   2874  CA  PRO B 177      45.776  31.172  68.946  1.00 48.70           C  
ANISOU 2874  CA  PRO B 177     5404   6798   6301    497    261  -1001       C  
ATOM   2875  C   PRO B 177      46.521  29.850  68.804  1.00 50.61           C  
ANISOU 2875  C   PRO B 177     5656   7044   6527    818    258  -1174       C  
ATOM   2876  O   PRO B 177      47.667  29.814  68.362  1.00 52.79           O  
ANISOU 2876  O   PRO B 177     5738   7620   6696    937    319  -1324       O  
ATOM   2877  CB  PRO B 177      45.063  31.538  67.670  1.00 48.41           C  
ANISOU 2877  CB  PRO B 177     5443   6755   6193    287    299  -1001       C  
ATOM   2878  CG  PRO B 177      44.917  33.133  67.836  1.00 48.75           C  
ANISOU 2878  CG  PRO B 177     5419   6904   6197     27    331   -849       C  
ATOM   2879  CD  PRO B 177      46.334  33.466  68.264  1.00 48.58           C  
ANISOU 2879  CD  PRO B 177     5174   7165   6118     73    387   -932       C  
ATOM   2880  N   LEU B 178      45.879  28.785  69.259  1.00 49.78           N  
ANISOU 2880  N   LEU B 178     5786   6608   6519    962    193  -1149       N  
ATOM   2881  CA  LEU B 178      46.347  27.427  69.055  1.00 51.15           C  
ANISOU 2881  CA  LEU B 178     6086   6666   6682   1276    189  -1303       C  
ATOM   2882  C   LEU B 178      45.890  27.023  67.663  1.00 50.58           C  
ANISOU 2882  C   LEU B 178     6133   6532   6550   1172    236  -1436       C  
ATOM   2883  O   LEU B 178      44.765  27.328  67.277  1.00 48.40           O  
ANISOU 2883  O   LEU B 178     5962   6127   6300    899    221  -1357       O  
ATOM   2884  CB  LEU B 178      45.654  26.518  70.070  1.00 51.03           C  
ANISOU 2884  CB  LEU B 178     6351   6252   6783   1390    113  -1196       C  
ATOM   2885  CG  LEU B 178      46.386  25.652  71.092  1.00 55.04           C  
ANISOU 2885  CG  LEU B 178     6937   6669   7306   1775     65  -1195       C  
ATOM   2886  CD1 LEU B 178      47.794  26.161  71.495  1.00 57.67           C  
ANISOU 2886  CD1 LEU B 178     6930   7430   7551   1994     65  -1252       C  
ATOM   2887  CD2 LEU B 178      45.505  25.519  72.321  1.00 51.88           C  
ANISOU 2887  CD2 LEU B 178     6731   5972   7009   1701      0   -984       C  
ATOM   2888  N   LYS B 179      46.741  26.343  66.903  1.00 52.33           N  
ANISOU 2888  N   LYS B 179     6328   6876   6678   1400    288  -1648       N  
ATOM   2889  CA  LYS B 179      46.288  25.742  65.655  1.00 52.58           C  
ANISOU 2889  CA  LYS B 179     6524   6805   6647   1335    326  -1802       C  
ATOM   2890  C   LYS B 179      45.687  24.401  66.000  1.00 53.67           C  
ANISOU 2890  C   LYS B 179     7029   6489   6875   1474    276  -1836       C  
ATOM   2891  O   LYS B 179      46.383  23.542  66.537  1.00 56.11           O  
ANISOU 2891  O   LYS B 179     7437   6683   7197   1832    265  -1902       O  
ATOM   2892  CB  LYS B 179      47.445  25.538  64.692  1.00 54.72           C  
ANISOU 2892  CB  LYS B 179     6631   7396   6762   1531    416  -2035       C  
ATOM   2893  CG  LYS B 179      47.849  26.772  63.921  1.00 54.06           C  
ANISOU 2893  CG  LYS B 179     6256   7736   6546   1288    499  -2033       C  
ATOM   2894  CD  LYS B 179      48.897  26.410  62.870  1.00 55.18           C  
ANISOU 2894  CD  LYS B 179     6255   8197   6513   1470    604  -2288       C  
ATOM   2895  CE  LYS B 179      49.506  27.659  62.236  1.00 55.36           C  
ANISOU 2895  CE  LYS B 179     5969   8681   6381   1223    709  -2275       C  
ATOM   2896  NZ  LYS B 179      50.023  27.354  60.861  1.00 56.30           N  
ANISOU 2896  NZ  LYS B 179     6025   9061   6304   1268    821  -2506       N  
ATOM   2897  N   GLU B 180      44.409  24.204  65.685  1.00 52.40           N  
ANISOU 2897  N   GLU B 180     7076   6076   6755   1195    247  -1795       N  
ATOM   2898  CA  GLU B 180      43.786  22.865  65.803  1.00 54.41           C  
ANISOU 2898  CA  GLU B 180     7720   5885   7068   1244    223  -1865       C  
ATOM   2899  C   GLU B 180      44.564  21.740  65.097  1.00 57.18           C  
ANISOU 2899  C   GLU B 180     8247   6141   7336   1558    275  -2129       C  
ATOM   2900  O   GLU B 180      44.668  20.630  65.627  1.00 60.12           O  
ANISOU 2900  O   GLU B 180     8935   6150   7755   1796    262  -2168       O  
ATOM   2901  CB  GLU B 180      42.345  22.878  65.300  1.00 53.50           C  
ANISOU 2901  CB  GLU B 180     7735   5627   6964    843    196  -1839       C  
ATOM   2902  CG  GLU B 180      41.358  23.273  66.359  1.00 53.82           C  
ANISOU 2902  CG  GLU B 180     7791   5537   7121    628    138  -1599       C  
ATOM   2903  CD  GLU B 180      40.016  23.636  65.798  1.00 55.22           C  
ANISOU 2903  CD  GLU B 180     7953   5752   7276    240    108  -1566       C  
ATOM   2904  OE1 GLU B 180      39.623  23.077  64.753  1.00 61.85           O  
ANISOU 2904  OE1 GLU B 180     8913   6552   8034    115    118  -1746       O  
ATOM   2905  OE2 GLU B 180      39.349  24.481  66.402  1.00 53.68           O  
ANISOU 2905  OE2 GLU B 180     7617   5647   7130     74     70  -1372       O  
ATOM   2906  N   GLN B 181      45.096  22.020  63.915  1.00 56.81           N  
ANISOU 2906  N   GLN B 181     8025   6407   7151   1570    339  -2308       N  
ATOM   2907  CA  GLN B 181      45.912  21.034  63.204  1.00 60.66           C  
ANISOU 2907  CA  GLN B 181     8643   6864   7538   1902    400  -2583       C  
ATOM   2908  C   GLN B 181      47.269  21.671  62.868  1.00 60.85           C  
ANISOU 2908  C   GLN B 181     8274   7404   7440   2131    468  -2670       C  
ATOM   2909  O   GLN B 181      47.413  22.319  61.825  1.00 60.24           O  
ANISOU 2909  O   GLN B 181     7985   7668   7232   1954    533  -2754       O  
ATOM   2910  CB  GLN B 181      45.217  20.513  61.930  1.00 62.18           C  
ANISOU 2910  CB  GLN B 181     9044   6941   7641   1691    431  -2786       C  
ATOM   2911  CG  GLN B 181      43.683  20.362  61.991  1.00 63.47           C  
ANISOU 2911  CG  GLN B 181     9438   6797   7881   1271    368  -2691       C  
ATOM   2912  CD  GLN B 181      43.195  19.163  62.821  1.00 69.07           C  
ANISOU 2912  CD  GLN B 181    10587   6949   8707   1332    337  -2676       C  
ATOM   2913  OE1 GLN B 181      42.206  19.264  63.570  1.00 69.35           O  
ANISOU 2913  OE1 GLN B 181    10710   6788   8850   1061    282  -2485       O  
ATOM   2914  NE2 GLN B 181      43.868  18.020  62.673  1.00 73.49           N  
ANISOU 2914  NE2 GLN B 181    11442   7249   9231   1687    380  -2879       N  
ATOM   2915  N   PRO B 182      48.270  21.498  63.753  1.00 61.77           N  
ANISOU 2915  N   PRO B 182     8281   7610   7579   2513    456  -2648       N  
ATOM   2916  CA  PRO B 182      49.556  22.205  63.641  1.00 62.86           C  
ANISOU 2916  CA  PRO B 182     7980   8303   7601   2682    515  -2711       C  
ATOM   2917  C   PRO B 182      50.298  21.958  62.322  1.00 65.78           C  
ANISOU 2917  C   PRO B 182     8229   8980   7782   2823    628  -2999       C  
ATOM   2918  O   PRO B 182      50.853  22.911  61.747  1.00 65.49           O  
ANISOU 2918  O   PRO B 182     7829   9432   7621   2660    707  -3026       O  
ATOM   2919  CB  PRO B 182      50.372  21.643  64.813  1.00 64.95           C  
ANISOU 2919  CB  PRO B 182     8243   8526   7908   3147    459  -2682       C  
ATOM   2920  CG  PRO B 182      49.304  21.206  65.809  1.00 63.39           C  
ANISOU 2920  CG  PRO B 182     8419   7785   7881   3048    362  -2471       C  
ATOM   2921  CD  PRO B 182      48.270  20.579  64.904  1.00 63.29           C  
ANISOU 2921  CD  PRO B 182     8762   7404   7880   2814    387  -2570       C  
ATOM   2922  N   ALA B 183      50.274  20.721  61.834  1.00 67.83           N  
ANISOU 2922  N   ALA B 183     8814   8947   8009   3091    646  -3210       N  
ATOM   2923  CA  ALA B 183      51.009  20.405  60.619  1.00 71.72           C  
ANISOU 2923  CA  ALA B 183     9206   9732   8309   3274    759  -3508       C  
ATOM   2924  C   ALA B 183      50.311  20.840  59.323  1.00 70.64           C  
ANISOU 2924  C   ALA B 183     9080   9692   8068   2845    817  -3578       C  
ATOM   2925  O   ALA B 183      50.831  20.566  58.246  1.00 72.57           O  
ANISOU 2925  O   ALA B 183     9265  10173   8134   2962    917  -3832       O  
ATOM   2926  CB  ALA B 183      51.371  18.922  60.571  1.00 75.52           C  
ANISOU 2926  CB  ALA B 183    10044   9878   8769   3784    765  -3739       C  
ATOM   2927  N   LEU B 184      49.160  21.517  59.438  1.00 67.34           N  
ANISOU 2927  N   LEU B 184     8723   9121   7741   2380    752  -3357       N  
ATOM   2928  CA  LEU B 184      48.340  21.905  58.272  1.00 66.96           C  
ANISOU 2928  CA  LEU B 184     8715   9140   7586   1984    776  -3394       C  
ATOM   2929  C   LEU B 184      48.339  23.424  58.050  1.00 64.62           C  
ANISOU 2929  C   LEU B 184     8074   9255   7220   1641    805  -3200       C  
ATOM   2930  O   LEU B 184      48.317  24.212  59.006  1.00 62.98           O  
ANISOU 2930  O   LEU B 184     7720   9081   7127   1544    759  -2961       O  
ATOM   2931  CB  LEU B 184      46.921  21.332  58.387  1.00 65.77           C  
ANISOU 2931  CB  LEU B 184     8947   8489   7550   1743    680  -3339       C  
ATOM   2932  CG  LEU B 184      45.856  21.597  57.307  1.00 65.01           C  
ANISOU 2932  CG  LEU B 184     8926   8424   7350   1335    665  -3372       C  
ATOM   2933  CD1 LEU B 184      46.111  20.843  56.014  1.00 64.76           C  
ANISOU 2933  CD1 LEU B 184     9024   8456   7124   1427    742  -3705       C  
ATOM   2934  CD2 LEU B 184      44.437  21.306  57.850  1.00 62.63           C  
ANISOU 2934  CD2 LEU B 184     8888   7710   7198   1052    551  -3235       C  
ATOM   2935  N   ASN B 185      48.384  23.838  56.791  1.00 65.90           N  
ANISOU 2935  N   ASN B 185     8136   9721   7179   1462    886  -3304       N  
ATOM   2936  CA  ASN B 185      48.741  25.228  56.461  1.00 65.17           C  
ANISOU 2936  CA  ASN B 185     7728  10066   6965   1205    956  -3159       C  
ATOM   2937  C   ASN B 185      47.605  26.265  56.618  1.00 61.47           C  
ANISOU 2937  C   ASN B 185     7301   9498   6555    806    875  -2867       C  
ATOM   2938  O   ASN B 185      47.828  27.443  56.986  1.00 60.01           O  
ANISOU 2938  O   ASN B 185     6922   9509   6368    631    898  -2662       O  
ATOM   2939  CB  ASN B 185      49.331  25.289  55.050  1.00 68.45           C  
ANISOU 2939  CB  ASN B 185     8025  10877   7106   1186   1093  -3373       C  
ATOM   2940  CG  ASN B 185      50.228  26.481  54.864  1.00 70.61           C  
ANISOU 2940  CG  ASN B 185     7945  11647   7234   1036   1214  -3285       C  
ATOM   2941  OD1 ASN B 185      51.433  26.334  54.628  1.00 75.76           O  
ANISOU 2941  OD1 ASN B 185     8355  12670   7757   1241   1336  -3468       O  
ATOM   2942  ND2 ASN B 185      49.659  27.680  55.009  1.00 68.26           N  
ANISOU 2942  ND2 ASN B 185     7619  11365   6951    678   1185  -3006       N  
ATOM   2943  N   ASP B 186      46.392  25.813  56.332  1.00 59.82           N  
ANISOU 2943  N   ASP B 186     7350   8994   6383    667    782  -2864       N  
ATOM   2944  CA  ASP B 186      45.213  26.642  56.458  1.00 56.42           C  
ANISOU 2944  CA  ASP B 186     6964   8475   5996    350    690  -2615       C  
ATOM   2945  C   ASP B 186      44.400  26.071  57.622  1.00 53.43           C  
ANISOU 2945  C   ASP B 186     6766   7672   5859    378    571  -2516       C  
ATOM   2946  O   ASP B 186      43.184  26.032  57.607  1.00 52.99           O  
ANISOU 2946  O   ASP B 186     6847   7440   5846    177    478  -2436       O  
ATOM   2947  CB  ASP B 186      44.469  26.669  55.101  1.00 57.48           C  
ANISOU 2947  CB  ASP B 186     7189   8723   5925    144    681  -2698       C  
ATOM   2948  CG  ASP B 186      45.315  27.339  53.979  1.00 61.24           C  
ANISOU 2948  CG  ASP B 186     7490   9645   6134     97    817  -2762       C  
ATOM   2949  OD1 ASP B 186      45.634  28.543  54.139  1.00 59.29           O  
ANISOU 2949  OD1 ASP B 186     7081   9601   5845    -35    864  -2554       O  
ATOM   2950  OD2 ASP B 186      45.680  26.684  52.949  1.00 66.21           O  
ANISOU 2950  OD2 ASP B 186     8155  10418   6582    178    888  -3023       O  
ATOM   2951  N   SER B 187      45.111  25.611  58.636  1.00 52.66           N  
ANISOU 2951  N   SER B 187     6658   7446   5902    636    577  -2526       N  
ATOM   2952  CA  SER B 187      44.497  25.053  59.838  1.00 51.07           C  
ANISOU 2952  CA  SER B 187     6638   6851   5915    685    483  -2418       C  
ATOM   2953  C   SER B 187      43.605  26.068  60.504  1.00 47.63           C  
ANISOU 2953  C   SER B 187     6136   6387   5572    429    409  -2135       C  
ATOM   2954  O   SER B 187      43.935  27.265  60.549  1.00 46.24           O  
ANISOU 2954  O   SER B 187     5748   6471   5350    333    440  -1991       O  
ATOM   2955  CB  SER B 187      45.575  24.616  60.836  1.00 51.95           C  
ANISOU 2955  CB  SER B 187     6702   6917   6119   1038    503  -2441       C  
ATOM   2956  OG  SER B 187      45.026  24.243  62.091  1.00 49.57           O  
ANISOU 2956  OG  SER B 187     6565   6263   6005   1071    417  -2289       O  
ATOM   2957  N   ARG B 188      42.470  25.594  61.012  1.00 46.18           N  
ANISOU 2957  N   ARG B 188     6147   5892   5507    309    321  -2064       N  
ATOM   2958  CA  ARG B 188      41.589  26.406  61.848  1.00 42.97           C  
ANISOU 2958  CA  ARG B 188     5687   5432   5205    124    250  -1807       C  
ATOM   2959  C   ARG B 188      42.266  26.683  63.230  1.00 42.11           C  
ANISOU 2959  C   ARG B 188     5494   5270   5234    297    250  -1665       C  
ATOM   2960  O   ARG B 188      43.261  26.026  63.575  1.00 43.47           O  
ANISOU 2960  O   ARG B 188     5684   5403   5429    570    285  -1771       O  
ATOM   2961  CB  ARG B 188      40.195  25.745  61.956  1.00 42.87           C  
ANISOU 2961  CB  ARG B 188     5873   5160   5253    -72    169  -1801       C  
ATOM   2962  CG  ARG B 188      39.357  25.853  60.633  1.00 44.53           C  
ANISOU 2962  CG  ARG B 188     6084   5534   5299   -304    142  -1895       C  
ATOM   2963  CD  ARG B 188      38.281  24.804  60.456  1.00 43.42           C  
ANISOU 2963  CD  ARG B 188     6157   5169   5172   -486     87  -2018       C  
ATOM   2964  NE  ARG B 188      37.071  25.197  61.164  1.00 46.54           N  
ANISOU 2964  NE  ARG B 188     6503   5530   5648   -694      8  -1830       N  
ATOM   2965  CZ  ARG B 188      35.974  24.451  61.310  1.00 47.86           C  
ANISOU 2965  CZ  ARG B 188     6804   5533   5844   -919    -41  -1883       C  
ATOM   2966  NH1 ARG B 188      34.935  24.928  62.003  1.00 46.29           N  
ANISOU 2966  NH1 ARG B 188     6503   5378   5706  -1087   -102  -1704       N  
ATOM   2967  NH2 ARG B 188      35.908  23.239  60.775  1.00 52.03           N  
ANISOU 2967  NH2 ARG B 188     7572   5863   6331   -990    -22  -2125       N  
ATOM   2968  N   TYR B 189      41.724  27.640  64.001  1.00 39.54           N  
ANISOU 2968  N   TYR B 189     5079   4961   4981    161    207  -1439       N  
ATOM   2969  CA  TYR B 189      42.353  28.140  65.221  1.00 38.39           C  
ANISOU 2969  CA  TYR B 189     4823   4834   4928    277    208  -1306       C  
ATOM   2970  C   TYR B 189      41.401  28.017  66.407  1.00 36.89           C  
ANISOU 2970  C   TYR B 189     4741   4391   4882    215    135  -1140       C  
ATOM   2971  O   TYR B 189      40.210  28.033  66.215  1.00 36.59           O  
ANISOU 2971  O   TYR B 189     4778   4269   4854     20     92  -1086       O  
ATOM   2972  CB  TYR B 189      42.729  29.619  65.042  1.00 36.45           C  
ANISOU 2972  CB  TYR B 189     4367   4876   4604    154    249  -1196       C  
ATOM   2973  CG  TYR B 189      43.861  29.848  64.073  1.00 38.47           C  
ANISOU 2973  CG  TYR B 189     4481   5430   4706    199    345  -1339       C  
ATOM   2974  CD1 TYR B 189      43.627  30.040  62.701  1.00 39.29           C  
ANISOU 2974  CD1 TYR B 189     4596   5679   4652     66    385  -1412       C  
ATOM   2975  CD2 TYR B 189      45.183  29.871  64.524  1.00 39.99           C  
ANISOU 2975  CD2 TYR B 189     4504   5802   4885    372    400  -1408       C  
ATOM   2976  CE1 TYR B 189      44.703  30.244  61.800  1.00 40.45           C  
ANISOU 2976  CE1 TYR B 189     4605   6130   4634     92    493  -1548       C  
ATOM   2977  CE2 TYR B 189      46.263  30.082  63.638  1.00 42.61           C  
ANISOU 2977  CE2 TYR B 189     4664   6469   5057    396    505  -1555       C  
ATOM   2978  CZ  TYR B 189      46.018  30.262  62.283  1.00 41.69           C  
ANISOU 2978  CZ  TYR B 189     4577   6475   4787    249    560  -1622       C  
ATOM   2979  OH  TYR B 189      47.097  30.475  61.443  1.00 45.54           O  
ANISOU 2979  OH  TYR B 189     4887   7316   5097    257    680  -1764       O  
ATOM   2980  N   ALA B 190      41.953  27.865  67.610  1.00 36.42           N  
ANISOU 2980  N   ALA B 190     4673   4250   4912    386    123  -1072       N  
ATOM   2981  CA  ALA B 190      41.235  27.962  68.882  1.00 36.08           C  
ANISOU 2981  CA  ALA B 190     4693   4031   4984    335     69   -892       C  
ATOM   2982  C   ALA B 190      41.832  29.111  69.725  1.00 35.30           C  
ANISOU 2982  C   ALA B 190     4398   4119   4895    363     73   -767       C  
ATOM   2983  O   ALA B 190      43.059  29.189  69.842  1.00 37.52           O  
ANISOU 2983  O   ALA B 190     4551   4568   5136    533    102   -839       O  
ATOM   2984  CB  ALA B 190      41.402  26.711  69.638  1.00 36.48           C  
ANISOU 2984  CB  ALA B 190     4951   3804   5104    524     50   -918       C  
ATOM   2985  N   LEU B 191      40.988  29.915  70.364  1.00 32.99           N  
ANISOU 2985  N   LEU B 191     4082   3804   4648    208     44   -601       N  
ATOM   2986  CA  LEU B 191      41.426  30.897  71.382  1.00 32.73           C  
ANISOU 2986  CA  LEU B 191     3921   3879   4634    224     42   -487       C  
ATOM   2987  C   LEU B 191      40.748  30.719  72.758  1.00 31.77           C  
ANISOU 2987  C   LEU B 191     3884   3580   4604    237     -4   -346       C  
ATOM   2988  O   LEU B 191      39.537  30.476  72.803  1.00 31.21           O  
ANISOU 2988  O   LEU B 191     3915   3369   4571    111    -25   -281       O  
ATOM   2989  CB  LEU B 191      41.097  32.311  70.892  1.00 30.93           C  
ANISOU 2989  CB  LEU B 191     3601   3803   4344     34     68   -414       C  
ATOM   2990  CG  LEU B 191      41.707  33.485  71.627  1.00 32.44           C  
ANISOU 2990  CG  LEU B 191     3681   4124   4521      0     91   -343       C  
ATOM   2991  CD1 LEU B 191      43.153  33.634  71.212  1.00 34.99           C  
ANISOU 2991  CD1 LEU B 191     3856   4678   4759     46    150   -470       C  
ATOM   2992  CD2 LEU B 191      40.942  34.780  71.300  1.00 33.89           C  
ANISOU 2992  CD2 LEU B 191     3889   4326   4660   -175    106   -229       C  
ATOM   2993  N   SER B 192      41.493  30.887  73.863  1.00 30.45           N  
ANISOU 2993  N   SER B 192     3654   3462   4452    368    -18   -304       N  
ATOM   2994  CA  SER B 192      40.841  30.912  75.176  1.00 29.12           C  
ANISOU 2994  CA  SER B 192     3553   3167   4342    359    -54   -159       C  
ATOM   2995  C   SER B 192      40.989  32.255  75.909  1.00 28.08           C  
ANISOU 2995  C   SER B 192     3290   3188   4192    288    -50    -79       C  
ATOM   2996  O   SER B 192      42.002  32.944  75.763  1.00 26.57           O  
ANISOU 2996  O   SER B 192     2955   3196   3943    298    -28   -144       O  
ATOM   2997  CB  SER B 192      41.341  29.785  76.095  1.00 31.12           C  
ANISOU 2997  CB  SER B 192     3922   3285   4616    586    -87   -149       C  
ATOM   2998  OG  SER B 192      42.641  30.065  76.604  1.00 32.56           O  
ANISOU 2998  OG  SER B 192     3952   3672   4747    770   -103   -193       O  
ATOM   2999  N   SER B 193      39.978  32.601  76.722  1.00 26.64           N  
ANISOU 2999  N   SER B 193     3160   2915   4045    204    -64     47       N  
ATOM   3000  CA  SER B 193      40.109  33.723  77.627  1.00 26.23           C  
ANISOU 3000  CA  SER B 193     3031   2961   3973    170    -62    112       C  
ATOM   3001  C   SER B 193      39.576  33.394  79.006  1.00 25.61           C  
ANISOU 3001  C   SER B 193     3023   2786   3922    220    -90    221       C  
ATOM   3002  O   SER B 193      38.657  32.551  79.117  1.00 26.23           O  
ANISOU 3002  O   SER B 193     3219   2708   4040    195    -94    279       O  
ATOM   3003  CB  SER B 193      39.348  34.921  77.084  1.00 25.30           C  
ANISOU 3003  CB  SER B 193     2900   2877   3835     12    -32    153       C  
ATOM   3004  OG  SER B 193      39.565  36.059  77.892  1.00 25.44           O  
ANISOU 3004  OG  SER B 193     2883   2957   3823    -22    -19    190       O  
ATOM   3005  N   ARG B 194      40.094  34.100  80.033  1.00 23.23           N  
ANISOU 3005  N   ARG B 194     2653   2587   3582    253   -101    243       N  
ATOM   3006  CA  ARG B 194      39.566  33.950  81.406  1.00 23.34           C  
ANISOU 3006  CA  ARG B 194     2730   2543   3595    291   -120    352       C  
ATOM   3007  C   ARG B 194      39.128  35.317  81.935  1.00 22.88           C  
ANISOU 3007  C   ARG B 194     2628   2554   3507    188    -95    384       C  
ATOM   3008  O   ARG B 194      39.766  36.301  81.662  1.00 23.96           O  
ANISOU 3008  O   ARG B 194     2696   2799   3609    130    -78    314       O  
ATOM   3009  CB  ARG B 194      40.578  33.338  82.412  1.00 23.52           C  
ANISOU 3009  CB  ARG B 194     2744   2622   3567    479   -171    352       C  
ATOM   3010  CG  ARG B 194      41.438  32.136  81.926  1.00 28.51           C  
ANISOU 3010  CG  ARG B 194     3410   3224   4198    670   -202    287       C  
ATOM   3011  CD  ARG B 194      42.756  32.743  81.439  1.00 29.87           C  
ANISOU 3011  CD  ARG B 194     3376   3657   4315    708   -207    144       C  
ATOM   3012  NE  ARG B 194      43.700  31.779  80.962  1.00 34.57           N  
ANISOU 3012  NE  ARG B 194     3949   4299   4886    927   -232     54       N  
ATOM   3013  CZ  ARG B 194      43.973  31.617  79.688  1.00 36.36           C  
ANISOU 3013  CZ  ARG B 194     4137   4551   5125    906   -194    -55       C  
ATOM   3014  NH1 ARG B 194      43.360  32.360  78.772  1.00 33.21           N  
ANISOU 3014  NH1 ARG B 194     3726   4133   4757    669   -136    -69       N  
ATOM   3015  NH2 ARG B 194      44.864  30.715  79.341  1.00 39.05           N  
ANISOU 3015  NH2 ARG B 194     4456   4948   5430   1150   -214   -151       N  
ATOM   3016  N   LEU B 195      38.102  35.323  82.776  1.00 22.51           N  
ANISOU 3016  N   LEU B 195     2640   2447   3463    169    -86    483       N  
ATOM   3017  CA  LEU B 195      37.681  36.457  83.538  1.00 22.65           C  
ANISOU 3017  CA  LEU B 195     2645   2520   3441    129    -63    509       C  
ATOM   3018  C   LEU B 195      37.554  35.958  84.959  1.00 22.41           C  
ANISOU 3018  C   LEU B 195     2651   2493   3368    200    -78    585       C  
ATOM   3019  O   LEU B 195      36.873  34.959  85.217  1.00 24.55           O  
ANISOU 3019  O   LEU B 195     2994   2676   3656    206    -73    671       O  
ATOM   3020  CB  LEU B 195      36.305  36.931  83.027  1.00 21.38           C  
ANISOU 3020  CB  LEU B 195     2500   2320   3301     56    -25    556       C  
ATOM   3021  CG  LEU B 195      35.630  38.009  83.846  1.00 21.98           C  
ANISOU 3021  CG  LEU B 195     2587   2435   3330     65      6    587       C  
ATOM   3022  CD1 LEU B 195      36.458  39.326  83.927  1.00 25.01           C  
ANISOU 3022  CD1 LEU B 195     2995   2842   3666     47     20    509       C  
ATOM   3023  CD2 LEU B 195      34.276  38.252  83.269  1.00 24.40           C  
ANISOU 3023  CD2 LEU B 195     2876   2748   3644     49     30    630       C  
ATOM   3024  N   ARG B 196      38.220  36.620  85.886  1.00 22.76           N  
ANISOU 3024  N   ARG B 196     2661   2645   3340    233    -94    551       N  
ATOM   3025  CA  ARG B 196      38.118  36.223  87.294  1.00 22.25           C  
ANISOU 3025  CA  ARG B 196     2636   2614   3204    309   -112    627       C  
ATOM   3026  C   ARG B 196      37.497  37.370  88.088  1.00 23.67           C  
ANISOU 3026  C   ARG B 196     2818   2850   3326    258    -70    623       C  
ATOM   3027  O   ARG B 196      37.983  38.509  88.021  1.00 23.94           O  
ANISOU 3027  O   ARG B 196     2823   2941   3329    207    -63    522       O  
ATOM   3028  CB  ARG B 196      39.480  35.929  87.864  1.00 23.31           C  
ANISOU 3028  CB  ARG B 196     2717   2875   3262    426   -183    579       C  
ATOM   3029  CG  ARG B 196      39.445  35.191  89.221  1.00 21.21           C  
ANISOU 3029  CG  ARG B 196     2524   2631   2901    549   -218    687       C  
ATOM   3030  CD  ARG B 196      40.793  34.620  89.441  1.00 24.58           C  
ANISOU 3030  CD  ARG B 196     2893   3183   3260    724   -307    646       C  
ATOM   3031  NE  ARG B 196      40.708  33.439  90.269  1.00 24.84           N  
ANISOU 3031  NE  ARG B 196     3069   3141   3226    891   -343    789       N  
ATOM   3032  CZ  ARG B 196      41.731  32.792  90.781  1.00 26.53           C  
ANISOU 3032  CZ  ARG B 196     3276   3464   3339   1119   -433    800       C  
ATOM   3033  NH1 ARG B 196      42.987  33.236  90.647  1.00 29.75           N  
ANISOU 3033  NH1 ARG B 196     3480   4132   3689   1200   -502    654       N  
ATOM   3034  NH2 ARG B 196      41.481  31.700  91.474  1.00 29.58           N  
ANISOU 3034  NH2 ARG B 196     3864   3714   3661   1267   -451    962       N  
ATOM   3035  N   VAL B 197      36.461  37.048  88.847  1.00 23.76           N  
ANISOU 3035  N   VAL B 197     2876   2843   3307    264    -34    723       N  
ATOM   3036  CA  VAL B 197      35.764  37.971  89.722  1.00 23.73           C  
ANISOU 3036  CA  VAL B 197     2876   2907   3230    255     13    720       C  
ATOM   3037  C   VAL B 197      35.728  37.366  91.172  1.00 25.81           C  
ANISOU 3037  C   VAL B 197     3180   3245   3379    312      8    806       C  
ATOM   3038  O   VAL B 197      36.125  36.224  91.400  1.00 25.83           O  
ANISOU 3038  O   VAL B 197     3232   3212   3367    361    -31    888       O  
ATOM   3039  CB  VAL B 197      34.328  38.214  89.178  1.00 23.74           C  
ANISOU 3039  CB  VAL B 197     2861   2880   3277    213     80    759       C  
ATOM   3040  CG1 VAL B 197      34.354  38.809  87.793  1.00 22.13           C  
ANISOU 3040  CG1 VAL B 197     2641   2614   3153    184     76    695       C  
ATOM   3041  CG2 VAL B 197      33.514  36.906  89.102  1.00 23.09           C  
ANISOU 3041  CG2 VAL B 197     2783   2765   3222    158    101    873       C  
ATOM   3042  N   SER B 198      35.286  38.134  92.164  1.00 26.80           N  
ANISOU 3042  N   SER B 198     3309   3466   3405    322     48    788       N  
ATOM   3043  CA  SER B 198      35.179  37.572  93.509  1.00 28.76           C  
ANISOU 3043  CA  SER B 198     3602   3803   3521    367     52    878       C  
ATOM   3044  C   SER B 198      34.035  36.569  93.491  1.00 28.80           C  
ANISOU 3044  C   SER B 198     3644   3753   3545    307    119   1025       C  
ATOM   3045  O   SER B 198      33.167  36.625  92.614  1.00 27.00           O  
ANISOU 3045  O   SER B 198     3367   3480   3411    232    167   1023       O  
ATOM   3046  CB  SER B 198      34.963  38.638  94.614  1.00 29.57           C  
ANISOU 3046  CB  SER B 198     3703   4041   3489    389     89    805       C  
ATOM   3047  OG  SER B 198      33.746  39.329  94.419  1.00 31.54           O  
ANISOU 3047  OG  SER B 198     3930   4290   3761    371    182    784       O  
ATOM   3048  N   ALA B 199      34.102  35.614  94.413  1.00 29.93           N  
ANISOU 3048  N   ALA B 199     3880   3904   3585    329    117   1153       N  
ATOM   3049  CA  ALA B 199      33.036  34.643  94.589  1.00 31.82           C  
ANISOU 3049  CA  ALA B 199     4189   4095   3807    217    200   1300       C  
ATOM   3050  C   ALA B 199      31.703  35.351  94.815  1.00 31.69           C  
ANISOU 3050  C   ALA B 199     4057   4228   3755    132    310   1275       C  
ATOM   3051  O   ALA B 199      30.674  34.971  94.265  1.00 31.11           O  
ANISOU 3051  O   ALA B 199     3933   4153   3734      0    379   1312       O  
ATOM   3052  CB  ALA B 199      33.357  33.685  95.789  1.00 33.21           C  
ANISOU 3052  CB  ALA B 199     4530   4263   3825    265    192   1456       C  
ATOM   3053  N   THR B 200      31.752  36.396  95.620  1.00 33.20           N  
ANISOU 3053  N   THR B 200     4200   4567   3844    217    323   1195       N  
ATOM   3054  CA  THR B 200      30.555  37.177  95.975  1.00 35.42           C  
ANISOU 3054  CA  THR B 200     4374   5020   4063    206    429   1151       C  
ATOM   3055  C   THR B 200      29.904  37.840  94.758  1.00 33.78           C  
ANISOU 3055  C   THR B 200     4049   4798   3985    209    444   1061       C  
ATOM   3056  O   THR B 200      28.678  37.972  94.677  1.00 34.42           O  
ANISOU 3056  O   THR B 200     4011   5025   4042    178    530   1067       O  
ATOM   3057  CB  THR B 200      30.884  38.227  97.094  1.00 36.08           C  
ANISOU 3057  CB  THR B 200     4471   5235   3999    324    434   1053       C  
ATOM   3058  OG1 THR B 200      30.927  37.531  98.350  1.00 40.88           O  
ANISOU 3058  OG1 THR B 200     5154   5943   4435    305    460   1169       O  
ATOM   3059  CG2 THR B 200      29.786  39.282  97.227  1.00 39.67           C  
ANISOU 3059  CG2 THR B 200     4826   5835   4410    384    532    956       C  
ATOM   3060  N   PHE B 201      30.726  38.279  93.809  1.00 31.81           N  
ANISOU 3060  N   PHE B 201     3825   4407   3853    255    361    978       N  
ATOM   3061  CA  PHE B 201      30.159  38.917  92.623  1.00 30.53           C  
ANISOU 3061  CA  PHE B 201     3584   4225   3791    277    367    911       C  
ATOM   3062  C   PHE B 201      29.515  37.828  91.718  1.00 29.89           C  
ANISOU 3062  C   PHE B 201     3438   4123   3793    141    374    992       C  
ATOM   3063  O   PHE B 201      28.458  38.013  91.188  1.00 30.61           O  
ANISOU 3063  O   PHE B 201     3406   4329   3895    126    415    981       O  
ATOM   3064  CB  PHE B 201      31.224  39.750  91.915  1.00 27.75           C  
ANISOU 3064  CB  PHE B 201     3300   3731   3509    334    295    805       C  
ATOM   3065  CG  PHE B 201      30.682  40.644  90.844  1.00 28.20           C  
ANISOU 3065  CG  PHE B 201     3330   3757   3627    395    305    744       C  
ATOM   3066  CD1 PHE B 201      30.237  41.928  91.148  1.00 27.97           C  
ANISOU 3066  CD1 PHE B 201     3339   3757   3530    531    350    663       C  
ATOM   3067  CD2 PHE B 201      30.673  40.229  89.520  1.00 26.01           C  
ANISOU 3067  CD2 PHE B 201     3019   3406   3457    339    267    764       C  
ATOM   3068  CE1 PHE B 201      29.721  42.775  90.157  1.00 28.22           C  
ANISOU 3068  CE1 PHE B 201     3384   3742   3595    635    355    626       C  
ATOM   3069  CE2 PHE B 201      30.196  41.073  88.532  1.00 27.16           C  
ANISOU 3069  CE2 PHE B 201     3155   3533   3629    418    267    724       C  
ATOM   3070  CZ  PHE B 201      29.722  42.348  88.845  1.00 25.93           C  
ANISOU 3070  CZ  PHE B 201     3051   3399   3402    577    308    665       C  
ATOM   3071  N   TRP B 202      30.166  36.691  91.568  1.00 29.41           N  
ANISOU 3071  N   TRP B 202     3468   3926   3777     51    332   1063       N  
ATOM   3072  CA  TRP B 202      29.615  35.598  90.779  1.00 30.76           C  
ANISOU 3072  CA  TRP B 202     3628   4041   4015   -107    345   1122       C  
ATOM   3073  C   TRP B 202      28.357  34.960  91.420  1.00 33.16           C  
ANISOU 3073  C   TRP B 202     3875   4496   4228   -267    450   1209       C  
ATOM   3074  O   TRP B 202      27.530  34.353  90.735  1.00 33.24           O  
ANISOU 3074  O   TRP B 202     3813   4544   4270   -437    483   1221       O  
ATOM   3075  CB  TRP B 202      30.674  34.492  90.588  1.00 30.47           C  
ANISOU 3075  CB  TRP B 202     3760   3788   4029   -130    282   1173       C  
ATOM   3076  CG  TRP B 202      30.057  33.215  90.135  1.00 31.69           C  
ANISOU 3076  CG  TRP B 202     3978   3848   4215   -322    319   1244       C  
ATOM   3077  CD1 TRP B 202      29.844  32.091  90.875  1.00 35.62           C  
ANISOU 3077  CD1 TRP B 202     4631   4260   4642   -442    371   1371       C  
ATOM   3078  CD2 TRP B 202      29.549  32.940  88.825  1.00 30.63           C  
ANISOU 3078  CD2 TRP B 202     3777   3686   4171   -442    312   1186       C  
ATOM   3079  NE1 TRP B 202      29.218  31.130  90.109  1.00 35.38           N  
ANISOU 3079  NE1 TRP B 202     4650   4130   4660   -658    406   1385       N  
ATOM   3080  CE2 TRP B 202      29.040  31.629  88.839  1.00 33.34           C  
ANISOU 3080  CE2 TRP B 202     4240   3924   4502   -658    363   1263       C  
ATOM   3081  CE3 TRP B 202      29.482  33.682  87.630  1.00 29.14           C  
ANISOU 3081  CE3 TRP B 202     3461   3552   4059   -394    267   1078       C  
ATOM   3082  CZ2 TRP B 202      28.452  31.037  87.696  1.00 31.27           C  
ANISOU 3082  CZ2 TRP B 202     3950   3628   4302   -846    368   1209       C  
ATOM   3083  CZ3 TRP B 202      28.912  33.088  86.509  1.00 25.99           C  
ANISOU 3083  CZ3 TRP B 202     3022   3139   3711   -548    263   1042       C  
ATOM   3084  CH2 TRP B 202      28.408  31.788  86.551  1.00 28.38           C  
ANISOU 3084  CH2 TRP B 202     3424   3355   4002   -777    311   1094       C  
ATOM   3085  N   GLN B 203      28.251  35.051  92.733  1.00 33.88           N  
ANISOU 3085  N   GLN B 203     3995   4687   4188   -241    507   1264       N  
ATOM   3086  CA  GLN B 203      27.098  34.458  93.387  1.00 37.12           C  
ANISOU 3086  CA  GLN B 203     4348   5267   4489   -421    626   1350       C  
ATOM   3087  C   GLN B 203      25.855  35.360  93.362  1.00 37.13           C  
ANISOU 3087  C   GLN B 203     4093   5582   4433   -387    701   1268       C  
ATOM   3088  O   GLN B 203      24.832  34.958  93.857  1.00 41.08           O  
ANISOU 3088  O   GLN B 203     4485   6293   4828   -545    810   1316       O  
ATOM   3089  CB  GLN B 203      27.468  34.024  94.805  1.00 38.27           C  
ANISOU 3089  CB  GLN B 203     4648   5402   4487   -421    665   1464       C  
ATOM   3090  CG  GLN B 203      28.403  32.778  94.833  1.00 39.79           C  
ANISOU 3090  CG  GLN B 203     5108   5304   4703   -469    609   1585       C  
ATOM   3091  CD  GLN B 203      29.040  32.492  96.217  1.00 42.02           C  
ANISOU 3091  CD  GLN B 203     5567   5573   4822   -379    607   1700       C  
ATOM   3092  OE1 GLN B 203      29.187  33.389  97.054  1.00 41.99           O  
ANISOU 3092  OE1 GLN B 203     5491   5745   4714   -243    608   1650       O  
ATOM   3093  NE2 GLN B 203      29.439  31.244  96.434  1.00 41.60           N  
ANISOU 3093  NE2 GLN B 203     5768   5301   4734   -441    600   1851       N  
ATOM   3094  N   ASP B 204      25.952  36.582  92.831  1.00 34.97           N  
ANISOU 3094  N   ASP B 204     3733   5344   4210   -172    649   1148       N  
ATOM   3095  CA  ASP B 204      24.787  37.465  92.674  1.00 34.69           C  
ANISOU 3095  CA  ASP B 204     3468   5594   4116    -65    705   1066       C  
ATOM   3096  C   ASP B 204      24.057  37.073  91.367  1.00 33.70           C  
ANISOU 3096  C   ASP B 204     3186   5551   4067   -181    680   1047       C  
ATOM   3097  O   ASP B 204      24.612  37.209  90.283  1.00 32.89           O  
ANISOU 3097  O   ASP B 204     3142   5271   4081   -134    585   1011       O  
ATOM   3098  CB  ASP B 204      25.217  38.958  92.689  1.00 33.87           C  
ANISOU 3098  CB  ASP B 204     3411   5443   4014    233    663    954       C  
ATOM   3099  CG  ASP B 204      24.023  39.945  92.581  1.00 37.28           C  
ANISOU 3099  CG  ASP B 204     3644   6152   4366    431    718    870       C  
ATOM   3100  OD1 ASP B 204      22.891  39.531  92.250  1.00 35.18           O  
ANISOU 3100  OD1 ASP B 204     3148   6157   4060    346    765    882       O  
ATOM   3101  OD2 ASP B 204      24.219  41.163  92.816  1.00 41.18           O  
ANISOU 3101  OD2 ASP B 204     4219   6602   4825    683    713    780       O  
ATOM   3102  N   PRO B 205      22.812  36.568  91.464  1.00 34.92           N  
ANISOU 3102  N   PRO B 205     3125   6005   4134   -355    769   1062       N  
ATOM   3103  CA  PRO B 205      22.215  36.081  90.221  1.00 34.74           C  
ANISOU 3103  CA  PRO B 205     2958   6069   4170   -508    732   1031       C  
ATOM   3104  C   PRO B 205      21.772  37.174  89.233  1.00 34.09           C  
ANISOU 3104  C   PRO B 205     2702   6145   4103   -247    661    929       C  
ATOM   3105  O   PRO B 205      21.387  36.848  88.116  1.00 34.59           O  
ANISOU 3105  O   PRO B 205     2652   6283   4206   -344    607    896       O  
ATOM   3106  CB  PRO B 205      20.982  35.268  90.682  1.00 37.86           C  
ANISOU 3106  CB  PRO B 205     3148   6795   4441   -807    857   1060       C  
ATOM   3107  CG  PRO B 205      20.688  35.748  92.046  1.00 38.70           C  
ANISOU 3107  CG  PRO B 205     3210   7088   4406   -700    963   1081       C  
ATOM   3108  CD  PRO B 205      21.960  36.310  92.643  1.00 36.59           C  
ANISOU 3108  CD  PRO B 205     3219   6500   4183   -468    908   1103       C  
ATOM   3109  N   ARG B 206      21.808  38.439  89.624  1.00 33.06           N  
ANISOU 3109  N   ARG B 206     2575   6060   3927     81    661    880       N  
ATOM   3110  CA  ARG B 206      21.482  39.506  88.672  1.00 32.77           C  
ANISOU 3110  CA  ARG B 206     2452   6103   3893    369    590    806       C  
ATOM   3111  C   ARG B 206      22.707  40.055  87.922  1.00 30.55           C  
ANISOU 3111  C   ARG B 206     2438   5435   3733    493    487    800       C  
ATOM   3112  O   ARG B 206      22.593  41.031  87.239  1.00 31.39           O  
ANISOU 3112  O   ARG B 206     2559   5536   3829    742    437    759       O  
ATOM   3113  CB  ARG B 206      20.753  40.645  89.337  1.00 34.21           C  
ANISOU 3113  CB  ARG B 206     2522   6531   3945    692    648    744       C  
ATOM   3114  CG  ARG B 206      19.536  40.232  90.120  1.00 36.86           C  
ANISOU 3114  CG  ARG B 206     2558   7312   4133    594    766    734       C  
ATOM   3115  CD  ARG B 206      18.774  41.430  90.504  1.00 38.96           C  
ANISOU 3115  CD  ARG B 206     2690   7845   4268    986    808    649       C  
ATOM   3116  NE  ARG B 206      17.426  41.033  90.894  1.00 49.51           N  
ANISOU 3116  NE  ARG B 206     3637   9724   5449    902    909    617       N  
ATOM   3117  CZ  ARG B 206      16.857  41.354  92.045  1.00 56.02           C  
ANISOU 3117  CZ  ARG B 206     4339  10822   6122   1010   1034    576       C  
ATOM   3118  NH1 ARG B 206      15.601  40.956  92.328  1.00 56.25           N  
ANISOU 3118  NH1 ARG B 206     3970  11404   5995    902   1136    539       N  
ATOM   3119  NH2 ARG B 206      17.546  42.108  92.902  1.00 58.69           N  
ANISOU 3119  NH2 ARG B 206     4945  10904   6450   1222   1062    555       N  
ATOM   3120  N   ASN B 207      23.855  39.424  88.066  1.00 29.29           N  
ANISOU 3120  N   ASN B 207     2488   4972   3668    324    463    843       N  
ATOM   3121  CA  ASN B 207      25.047  39.811  87.347  1.00 28.77           C  
ANISOU 3121  CA  ASN B 207     2634   4593   3704    387    380    828       C  
ATOM   3122  C   ASN B 207      25.156  38.991  86.067  1.00 28.95           C  
ANISOU 3122  C   ASN B 207     2629   4560   3809    219    314    836       C  
ATOM   3123  O   ASN B 207      25.022  37.757  86.095  1.00 31.26           O  
ANISOU 3123  O   ASN B 207     2887   4863   4126    -29    331    870       O  
ATOM   3124  CB  ASN B 207      26.286  39.583  88.243  1.00 26.50           C  
ANISOU 3124  CB  ASN B 207     2550   4068   3448    324    385    849       C  
ATOM   3125  CG  ASN B 207      26.520  40.722  89.197  1.00 26.58           C  
ANISOU 3125  CG  ASN B 207     2654   4060   3385    518    420    800       C  
ATOM   3126  OD1 ASN B 207      26.028  41.839  88.978  1.00 30.34           O  
ANISOU 3126  OD1 ASN B 207     3122   4590   3814    734    429    744       O  
ATOM   3127  ND2 ASN B 207      27.263  40.469  90.248  1.00 24.76           N  
ANISOU 3127  ND2 ASN B 207     2530   3749   3127    461    436    815       N  
ATOM   3128  N   HIS B 208      25.414  39.685  84.968  1.00 28.93           N  
ANISOU 3128  N   HIS B 208     2674   4479   3835    350    246    805       N  
ATOM   3129  CA  HIS B 208      25.488  39.136  83.619  1.00 28.82           C  
ANISOU 3129  CA  HIS B 208     2635   4440   3874    238    177    794       C  
ATOM   3130  C   HIS B 208      26.908  39.166  83.040  1.00 27.72           C  
ANISOU 3130  C   HIS B 208     2709   3997   3824    214    130    784       C  
ATOM   3131  O   HIS B 208      27.613  40.198  83.055  1.00 27.49           O  
ANISOU 3131  O   HIS B 208     2826   3823   3794    361    124    771       O  
ATOM   3132  CB  HIS B 208      24.608  39.982  82.730  1.00 29.21           C  
ANISOU 3132  CB  HIS B 208     2560   4692   3845    436    135    773       C  
ATOM   3133  CG  HIS B 208      24.527  39.506  81.323  1.00 30.65           C  
ANISOU 3133  CG  HIS B 208     2689   4913   4042    338     60    754       C  
ATOM   3134  ND1 HIS B 208      25.116  40.184  80.275  1.00 31.09           N  
ANISOU 3134  ND1 HIS B 208     2884   4826   4103    461      0    754       N  
ATOM   3135  CD2 HIS B 208      23.914  38.423  80.784  1.00 28.28           C  
ANISOU 3135  CD2 HIS B 208     2223   4785   3735    107     40    726       C  
ATOM   3136  CE1 HIS B 208      24.869  39.536  79.151  1.00 31.96           C  
ANISOU 3136  CE1 HIS B 208     2903   5037   4203    335    -59    728       C  
ATOM   3137  NE2 HIS B 208      24.113  38.484  79.433  1.00 31.49           N  
ANISOU 3137  NE2 HIS B 208     2655   5173   4138    121    -39    700       N  
ATOM   3138  N   PHE B 209      27.310  38.060  82.449  1.00 26.70           N  
ANISOU 3138  N   PHE B 209     2599   3784   3760     22    103    777       N  
ATOM   3139  CA  PHE B 209      28.691  37.943  81.966  1.00 26.99           C  
ANISOU 3139  CA  PHE B 209     2802   3581   3871      0     69    754       C  
ATOM   3140  C   PHE B 209      28.550  37.499  80.527  1.00 27.84           C  
ANISOU 3140  C   PHE B 209     2871   3716   3990    -79     18    716       C  
ATOM   3141  O   PHE B 209      27.791  36.564  80.261  1.00 28.71           O  
ANISOU 3141  O   PHE B 209     2881   3932   4093   -233     15    704       O  
ATOM   3142  CB  PHE B 209      29.444  36.863  82.757  1.00 26.52           C  
ANISOU 3142  CB  PHE B 209     2833   3379   3863   -117     87    773       C  
ATOM   3143  CG  PHE B 209      29.537  37.134  84.236  1.00 26.81           C  
ANISOU 3143  CG  PHE B 209     2901   3422   3862    -59    133    815       C  
ATOM   3144  CD1 PHE B 209      28.514  36.770  85.088  1.00 28.93           C  
ANISOU 3144  CD1 PHE B 209     3081   3836   4073   -120    190    863       C  
ATOM   3145  CD2 PHE B 209      30.648  37.767  84.761  1.00 25.31           C  
ANISOU 3145  CD2 PHE B 209     2816   3126   3673     35    123    794       C  
ATOM   3146  CE1 PHE B 209      28.613  37.026  86.477  1.00 29.11           C  
ANISOU 3146  CE1 PHE B 209     3140   3882   4036    -63    237    900       C  
ATOM   3147  CE2 PHE B 209      30.753  38.030  86.126  1.00 26.04           C  
ANISOU 3147  CE2 PHE B 209     2938   3245   3708     85    158    817       C  
ATOM   3148  CZ  PHE B 209      29.727  37.665  86.981  1.00 26.76           C  
ANISOU 3148  CZ  PHE B 209     2957   3469   3738     49    215    874       C  
ATOM   3149  N   ARG B 210      29.221  38.192  79.606  1.00 26.72           N  
ANISOU 3149  N   ARG B 210     2812   3494   3846      1    -14    692       N  
ATOM   3150  CA  ARG B 210      29.181  37.803  78.203  1.00 26.01           C  
ANISOU 3150  CA  ARG B 210     2697   3439   3746    -67    -62    651       C  
ATOM   3151  C   ARG B 210      30.591  37.868  77.579  1.00 25.87           C  
ANISOU 3151  C   ARG B 210     2818   3244   3764    -79    -67    612       C  
ATOM   3152  O   ARG B 210      31.334  38.891  77.692  1.00 22.04           O  
ANISOU 3152  O   ARG B 210     2436   2673   3265      8    -48    624       O  
ATOM   3153  CB  ARG B 210      28.220  38.712  77.432  1.00 27.68           C  
ANISOU 3153  CB  ARG B 210     2825   3838   3855     69   -100    671       C  
ATOM   3154  CG  ARG B 210      28.157  38.441  75.921  1.00 27.36           C  
ANISOU 3154  CG  ARG B 210     2760   3868   3767     16   -159    631       C  
ATOM   3155  CD  ARG B 210      27.228  39.428  75.129  1.00 31.97           C  
ANISOU 3155  CD  ARG B 210     3275   4658   4214    208   -213    671       C  
ATOM   3156  NE  ARG B 210      25.824  39.334  75.523  1.00 35.30           N  
ANISOU 3156  NE  ARG B 210     3469   5371   4571    254   -232    674       N  
ATOM   3157  CZ  ARG B 210      24.920  40.320  75.481  1.00 36.35           C  
ANISOU 3157  CZ  ARG B 210     3521   5702   4588    511   -261    720       C  
ATOM   3158  NH1 ARG B 210      25.224  41.561  75.057  1.00 36.05           N  
ANISOU 3158  NH1 ARG B 210     3668   5548   4482    759   -275    786       N  
ATOM   3159  NH2 ARG B 210      23.669  40.050  75.843  1.00 33.38           N  
ANISOU 3159  NH2 ARG B 210     2880   5656   4147    521   -273    698       N  
ATOM   3160  N   CYS B 211      30.941  36.783  76.905  1.00 25.15           N  
ANISOU 3160  N   CYS B 211     2733   3111   3708   -202    -85    552       N  
ATOM   3161  CA  CYS B 211      32.175  36.730  76.127  1.00 26.07           C  
ANISOU 3161  CA  CYS B 211     2936   3128   3838   -211    -86    494       C  
ATOM   3162  C   CYS B 211      31.711  37.008  74.689  1.00 26.02           C  
ANISOU 3162  C   CYS B 211     2900   3237   3750   -220   -123    472       C  
ATOM   3163  O   CYS B 211      30.765  36.406  74.234  1.00 26.56           O  
ANISOU 3163  O   CYS B 211     2880   3420   3789   -292   -158    447       O  
ATOM   3164  CB  CYS B 211      32.741  35.319  76.198  1.00 25.67           C  
ANISOU 3164  CB  CYS B 211     2927   2971   3855   -296    -84    430       C  
ATOM   3165  SG  CYS B 211      34.171  35.198  75.179  1.00 37.49           S  
ANISOU 3165  SG  CYS B 211     4481   4416   5345   -278    -79    334       S  
ATOM   3166  N   GLN B 212      32.359  37.928  73.984  1.00 26.67           N  
ANISOU 3166  N   GLN B 212     3056   3303   3774   -165   -113    480       N  
ATOM   3167  CA  GLN B 212      31.955  38.324  72.675  1.00 27.41           C  
ANISOU 3167  CA  GLN B 212     3149   3505   3758   -147   -147    484       C  
ATOM   3168  C   GLN B 212      33.167  38.184  71.745  1.00 28.37           C  
ANISOU 3168  C   GLN B 212     3345   3579   3855   -214   -118    416       C  
ATOM   3169  O   GLN B 212      34.263  38.738  72.030  1.00 27.18           O  
ANISOU 3169  O   GLN B 212     3273   3336   3718   -218    -62    417       O  
ATOM   3170  CB  GLN B 212      31.542  39.807  72.718  1.00 29.29           C  
ANISOU 3170  CB  GLN B 212     3463   3756   3909      5   -144    590       C  
ATOM   3171  CG  GLN B 212      30.305  40.102  72.029  1.00 31.31           C  
ANISOU 3171  CG  GLN B 212     3645   4197   4051    107   -209    635       C  
ATOM   3172  CD  GLN B 212      29.720  41.481  72.354  1.00 35.24           C  
ANISOU 3172  CD  GLN B 212     4230   4690   4468    330   -209    744       C  
ATOM   3173  OE1 GLN B 212      28.775  41.597  73.187  1.00 36.19           O  
ANISOU 3173  OE1 GLN B 212     4243   4908   4596    440   -222    768       O  
ATOM   3174  NE2 GLN B 212      30.232  42.528  71.674  1.00 31.42           N  
ANISOU 3174  NE2 GLN B 212     3955   4094   3887    403   -187    810       N  
ATOM   3175  N   VAL B 213      32.983  37.473  70.618  1.00 28.20           N  
ANISOU 3175  N   VAL B 213     3285   3648   3778   -281   -151    343       N  
ATOM   3176  CA  VAL B 213      34.060  37.390  69.597  1.00 27.66           C  
ANISOU 3176  CA  VAL B 213     3274   3580   3653   -332   -115    269       C  
ATOM   3177  C   VAL B 213      33.626  37.939  68.228  1.00 29.12           C  
ANISOU 3177  C   VAL B 213     3487   3906   3670   -321   -146    298       C  
ATOM   3178  O   VAL B 213      32.780  37.322  67.549  1.00 29.42           O  
ANISOU 3178  O   VAL B 213     3451   4077   3651   -352   -212    249       O  
ATOM   3179  CB  VAL B 213      34.578  35.926  69.436  1.00 28.03           C  
ANISOU 3179  CB  VAL B 213     3293   3586   3768   -405   -111    123       C  
ATOM   3180  CG1 VAL B 213      35.738  35.881  68.488  1.00 27.71           C  
ANISOU 3180  CG1 VAL B 213     3285   3582   3660   -427    -60     33       C  
ATOM   3181  CG2 VAL B 213      34.996  35.374  70.757  1.00 24.26           C  
ANISOU 3181  CG2 VAL B 213     2818   2971   3427   -379    -90    118       C  
ATOM   3182  N   GLN B 214      34.205  39.092  67.852  1.00 27.83           N  
ANISOU 3182  N   GLN B 214     3443   3716   3414   -294    -96    377       N  
ATOM   3183  CA  GLN B 214      34.015  39.706  66.553  1.00 28.98           C  
ANISOU 3183  CA  GLN B 214     3669   3969   3374   -277   -109    430       C  
ATOM   3184  C   GLN B 214      34.945  38.987  65.611  1.00 29.66           C  
ANISOU 3184  C   GLN B 214     3737   4120   3412   -395    -65    299       C  
ATOM   3185  O   GLN B 214      36.168  39.051  65.806  1.00 30.64           O  
ANISOU 3185  O   GLN B 214     3886   4183   3572   -466     24    250       O  
ATOM   3186  CB  GLN B 214      34.428  41.191  66.617  1.00 29.65           C  
ANISOU 3186  CB  GLN B 214     3951   3939   3376   -237    -43    568       C  
ATOM   3187  CG  GLN B 214      34.462  41.959  65.271  1.00 31.25           C  
ANISOU 3187  CG  GLN B 214     4310   4206   3356   -230    -30    655       C  
ATOM   3188  CD  GLN B 214      33.072  42.262  64.729  1.00 30.50           C  
ANISOU 3188  CD  GLN B 214     4215   4243   3128    -44   -144    754       C  
ATOM   3189  OE1 GLN B 214      32.429  43.201  65.180  1.00 33.55           O  
ANISOU 3189  OE1 GLN B 214     4710   4553   3482    127   -167    886       O  
ATOM   3190  NE2 GLN B 214      32.600  41.461  63.755  1.00 28.69           N  
ANISOU 3190  NE2 GLN B 214     3858   4235   2807    -63   -220    677       N  
ATOM   3191  N   PHE B 215      34.384  38.264  64.644  1.00 29.63           N  
ANISOU 3191  N   PHE B 215     3670   4267   3321   -417   -127    221       N  
ATOM   3192  CA  PHE B 215      35.140  37.598  63.563  1.00 29.94           C  
ANISOU 3192  CA  PHE B 215     3705   4396   3273   -507    -88     81       C  
ATOM   3193  C   PHE B 215      35.093  38.452  62.256  1.00 31.37           C  
ANISOU 3193  C   PHE B 215     3987   4720   3211   -504    -82    165       C  
ATOM   3194  O   PHE B 215      34.084  39.047  61.944  1.00 31.94           O  
ANISOU 3194  O   PHE B 215     4090   4874   3171   -412   -162    284       O  
ATOM   3195  CB  PHE B 215      34.539  36.208  63.324  1.00 29.19           C  
ANISOU 3195  CB  PHE B 215     3512   4358   3219   -556   -158    -78       C  
ATOM   3196  CG  PHE B 215      35.099  35.469  62.113  1.00 30.29           C  
ANISOU 3196  CG  PHE B 215     3660   4604   3243   -627   -131   -247       C  
ATOM   3197  CD1 PHE B 215      36.392  34.906  62.138  1.00 29.34           C  
ANISOU 3197  CD1 PHE B 215     3549   4417   3178   -639    -36   -378       C  
ATOM   3198  CD2 PHE B 215      34.321  35.308  60.947  1.00 33.02           C  
ANISOU 3198  CD2 PHE B 215     3989   5149   3406   -664   -205   -291       C  
ATOM   3199  CE1 PHE B 215      36.921  34.204  61.032  1.00 28.09           C  
ANISOU 3199  CE1 PHE B 215     3399   4368   2904   -677      0   -555       C  
ATOM   3200  CE2 PHE B 215      34.819  34.608  59.828  1.00 31.79           C  
ANISOU 3200  CE2 PHE B 215     3852   5099   3128   -730   -177   -466       C  
ATOM   3201  CZ  PHE B 215      36.145  34.062  59.870  1.00 31.96           C  
ANISOU 3201  CZ  PHE B 215     3897   5031   3214   -732    -66   -601       C  
ATOM   3202  N   TYR B 216      36.190  38.519  61.515  1.00 31.31           N  
ANISOU 3202  N   TYR B 216     4029   4761   3104   -590     15    108       N  
ATOM   3203  CA  TYR B 216      36.224  39.215  60.236  1.00 33.22           C  
ANISOU 3203  CA  TYR B 216     4387   5143   3093   -612     36    185       C  
ATOM   3204  C   TYR B 216      36.429  38.182  59.152  1.00 35.06           C  
ANISOU 3204  C   TYR B 216     4542   5557   3220   -676     32     -3       C  
ATOM   3205  O   TYR B 216      37.401  37.417  59.206  1.00 33.90           O  
ANISOU 3205  O   TYR B 216     4326   5406   3148   -736    111   -173       O  
ATOM   3206  CB  TYR B 216      37.379  40.242  60.181  1.00 33.44           C  
ANISOU 3206  CB  TYR B 216     4555   5104   3046   -711    182    274       C  
ATOM   3207  CG  TYR B 216      37.221  41.344  61.190  1.00 31.91           C  
ANISOU 3207  CG  TYR B 216     4488   4703   2930   -668    197    445       C  
ATOM   3208  CD1 TYR B 216      37.646  41.153  62.474  1.00 26.49           C  
ANISOU 3208  CD1 TYR B 216     3720   3884   2461   -684    223    392       C  
ATOM   3209  CD2 TYR B 216      36.615  42.567  60.851  1.00 34.74           C  
ANISOU 3209  CD2 TYR B 216     5073   4995   3128   -588    181    658       C  
ATOM   3210  CE1 TYR B 216      37.516  42.106  63.409  1.00 29.20           C  
ANISOU 3210  CE1 TYR B 216     4181   4044   2868   -653    239    518       C  
ATOM   3211  CE2 TYR B 216      36.477  43.574  61.805  1.00 34.61           C  
ANISOU 3211  CE2 TYR B 216     5212   4754   3182   -534    202    794       C  
ATOM   3212  CZ  TYR B 216      36.949  43.327  63.097  1.00 31.66           C  
ANISOU 3212  CZ  TYR B 216     4733   4262   3034   -584    235    710       C  
ATOM   3213  OH  TYR B 216      36.839  44.240  64.134  1.00 32.64           O  
ANISOU 3213  OH  TYR B 216     4997   4171   3234   -542    257    809       O  
ATOM   3214  N   GLY B 217      35.523  38.163  58.176  1.00 37.07           N  
ANISOU 3214  N   GLY B 217     4808   5989   3288   -641    -63     15       N  
ATOM   3215  CA  GLY B 217      35.466  37.070  57.214  1.00 39.93           C  
ANISOU 3215  CA  GLY B 217     5094   6526   3551   -704    -93   -192       C  
ATOM   3216  C   GLY B 217      35.139  37.547  55.813  1.00 43.74           C  
ANISOU 3216  C   GLY B 217     5652   7247   3717   -700   -127   -133       C  
ATOM   3217  O   GLY B 217      35.810  38.450  55.297  1.00 43.46           O  
ANISOU 3217  O   GLY B 217     5755   7235   3523   -722    -30     -7       O  
ATOM   3218  N   LEU B 218      34.118  36.931  55.202  1.00 46.15           N  
ANISOU 3218  N   LEU B 218     5873   7744   3916   -693   -261   -226       N  
ATOM   3219  CA  LEU B 218      33.685  37.329  53.853  1.00 51.59           C  
ANISOU 3219  CA  LEU B 218     6618   8710   4273   -666   -323   -174       C  
ATOM   3220  C   LEU B 218      32.657  38.450  53.959  1.00 54.20           C  
ANISOU 3220  C   LEU B 218     7002   9098   4494   -488   -434     87       C  
ATOM   3221  O   LEU B 218      31.935  38.562  54.973  1.00 52.64           O  
ANISOU 3221  O   LEU B 218     6723   8805   4473   -401   -505    150       O  
ATOM   3222  CB  LEU B 218      33.153  36.142  53.045  1.00 51.72           C  
ANISOU 3222  CB  LEU B 218     6516   8950   4185   -756   -415   -427       C  
ATOM   3223  CG  LEU B 218      34.130  34.971  52.944  1.00 52.68           C  
ANISOU 3223  CG  LEU B 218     6622   8983   4410   -884   -305   -705       C  
ATOM   3224  CD1 LEU B 218      33.594  33.899  51.966  1.00 54.28           C  
ANISOU 3224  CD1 LEU B 218     6768   9403   4453   -986   -390   -965       C  
ATOM   3225  CD2 LEU B 218      35.537  35.431  52.522  1.00 52.86           C  
ANISOU 3225  CD2 LEU B 218     6746   8989   4347   -901   -127   -681       C  
ATOM   3226  N   SER B 219      32.606  39.292  52.937  1.00 59.22           N  
ANISOU 3226  N   SER B 219     7786   9887   4824   -413   -445    244       N  
ATOM   3227  CA  SER B 219      31.865  40.540  53.074  1.00 63.97           C  
ANISOU 3227  CA  SER B 219     8519  10475   5311   -189   -520    530       C  
ATOM   3228  C   SER B 219      31.120  40.991  51.822  1.00 68.75           C  
ANISOU 3228  C   SER B 219     9189  11395   5536    -44   -645    643       C  
ATOM   3229  O   SER B 219      30.108  40.383  51.432  1.00 70.30           O  
ANISOU 3229  O   SER B 219     9178  11898   5634      2   -812    529       O  
ATOM   3230  CB  SER B 219      32.799  41.660  53.596  1.00 63.97           C  
ANISOU 3230  CB  SER B 219     8779  10153   5371   -192   -357    732       C  
ATOM   3231  OG  SER B 219      33.703  42.121  52.595  1.00 68.03           O  
ANISOU 3231  OG  SER B 219     9498  10702   5646   -302   -231    798       O  
ATOM   3232  N   GLU B 220      31.670  42.044  51.208  1.00 72.28           N  
ANISOU 3232  N   GLU B 220     9932  11771   5760      3   -555    863       N  
ATOM   3233  CA  GLU B 220      31.107  42.812  50.080  1.00 76.93           C  
ANISOU 3233  CA  GLU B 220    10694  12584   5950    193   -649   1066       C  
ATOM   3234  C   GLU B 220      30.721  41.935  48.858  1.00 79.48           C  
ANISOU 3234  C   GLU B 220    10844  13337   6017    132   -761    877       C  
ATOM   3235  O   GLU B 220      31.200  42.142  47.717  1.00 81.78           O  
ANISOU 3235  O   GLU B 220    11297  13772   6002     76   -706    923       O  
ATOM   3236  CB  GLU B 220      32.073  43.998  49.754  1.00 78.16           C  
ANISOU 3236  CB  GLU B 220    11256  12492   5949    157   -468   1318       C  
ATOM   3237  CG  GLU B 220      31.709  44.992  48.606  1.00 83.62           C  
ANISOU 3237  CG  GLU B 220    12254  13316   6199    353   -521   1597       C  
ATOM   3238  CD  GLU B 220      30.277  45.575  48.651  1.00 86.76           C  
ANISOU 3238  CD  GLU B 220    12661  13847   6454    768   -748   1782       C  
ATOM   3239  OE1 GLU B 220      29.625  45.611  49.737  1.00 84.11           O  
ANISOU 3239  OE1 GLU B 220    12183  13405   6369    924   -826   1772       O  
ATOM   3240  OE2 GLU B 220      29.811  46.006  47.565  1.00 89.36           O  
ANISOU 3240  OE2 GLU B 220    13136  14421   6393    955   -848   1939       O  
ATOM   3241  N   ASN B 221      29.818  40.976  49.121  1.00 79.45           N  
ANISOU 3241  N   ASN B 221    10518  13545   6122    127   -915    663       N  
ATOM   3242  CA  ASN B 221      29.352  40.003  48.123  1.00 81.76           C  
ANISOU 3242  CA  ASN B 221    10613  14241   6209     25  -1034    425       C  
ATOM   3243  C   ASN B 221      30.532  39.255  47.433  1.00 81.56           C  
ANISOU 3243  C   ASN B 221    10642  14198   6148   -245   -874    208       C  
ATOM   3244  O   ASN B 221      30.846  39.481  46.250  1.00 84.12           O  
ANISOU 3244  O   ASN B 221    11098  14727   6136   -257   -850    244       O  
ATOM   3245  CB  ASN B 221      28.389  40.689  47.117  1.00 86.07           C  
ANISOU 3245  CB  ASN B 221    11197  15173   6332    283  -1219    605       C  
ATOM   3246  CG  ASN B 221      27.475  39.697  46.361  1.00 89.60           C  
ANISOU 3246  CG  ASN B 221    11344  16110   6587    209  -1411    344       C  
ATOM   3247  OD1 ASN B 221      27.154  38.613  46.860  1.00 91.01           O  
ANISOU 3247  OD1 ASN B 221    11265  16324   6990     12  -1447     65       O  
ATOM   3248  ND2 ASN B 221      27.049  40.085  45.152  1.00 92.71           N  
ANISOU 3248  ND2 ASN B 221    11794  16882   6546    355  -1533    438       N  
ATOM   3249  N   ASP B 222      31.222  38.417  48.216  1.00 78.46           N  
ANISOU 3249  N   ASP B 222    10162  13557   6092   -433   -755     -1       N  
ATOM   3250  CA  ASP B 222      32.078  37.350  47.678  1.00 77.77           C  
ANISOU 3250  CA  ASP B 222    10037  13503   6006   -653   -646   -300       C  
ATOM   3251  C   ASP B 222      31.071  36.282  47.251  1.00 78.42           C  
ANISOU 3251  C   ASP B 222     9912  13872   6012   -728   -820   -562       C  
ATOM   3252  O   ASP B 222      29.974  36.204  47.822  1.00 78.21           O  
ANISOU 3252  O   ASP B 222     9725  13913   6076   -670   -973   -544       O  
ATOM   3253  CB  ASP B 222      32.998  36.739  48.758  1.00 74.76           C  
ANISOU 3253  CB  ASP B 222     9621  12769   6012   -770   -494   -441       C  
ATOM   3254  CG  ASP B 222      34.082  37.697  49.266  1.00 73.70           C  
ANISOU 3254  CG  ASP B 222     9653  12376   5971   -754   -313   -233       C  
ATOM   3255  OD1 ASP B 222      35.114  37.860  48.574  1.00 74.99           O  
ANISOU 3255  OD1 ASP B 222     9920  12592   5978   -844   -160   -253       O  
ATOM   3256  OD2 ASP B 222      33.934  38.234  50.393  1.00 71.58           O  
ANISOU 3256  OD2 ASP B 222     9400  11864   5933   -678   -313    -77       O  
ATOM   3257  N   GLU B 223      31.417  35.459  46.272  1.00 79.02           N  
ANISOU 3257  N   GLU B 223     9980  14132   5911   -874   -793   -820       N  
ATOM   3258  CA  GLU B 223      30.533  34.350  45.941  1.00 79.67           C  
ANISOU 3258  CA  GLU B 223     9886  14443   5943  -1007   -941  -1114       C  
ATOM   3259  C   GLU B 223      30.636  33.211  46.965  1.00 76.73           C  
ANISOU 3259  C   GLU B 223     9435  13765   5953  -1166   -894  -1356       C  
ATOM   3260  O   GLU B 223      31.708  32.956  47.506  1.00 74.00           O  
ANISOU 3260  O   GLU B 223     9184  13097   5836  -1188   -723  -1403       O  
ATOM   3261  CB  GLU B 223      30.797  33.829  44.536  1.00 82.56           C  
ANISOU 3261  CB  GLU B 223    10292  15107   5968  -1112   -936  -1333       C  
ATOM   3262  CG  GLU B 223      29.627  33.045  43.982  1.00 85.56           C  
ANISOU 3262  CG  GLU B 223    10497  15839   6172  -1233  -1138  -1574       C  
ATOM   3263  CD  GLU B 223      29.917  32.464  42.618  1.00 89.56           C  
ANISOU 3263  CD  GLU B 223    11055  16632   6339  -1351  -1128  -1829       C  
ATOM   3264  OE1 GLU B 223      31.028  32.722  42.101  1.00 89.99           O  
ANISOU 3264  OE1 GLU B 223    11275  16624   6289  -1318   -958  -1796       O  
ATOM   3265  OE2 GLU B 223      29.041  31.755  42.064  1.00 90.93           O  
ANISOU 3265  OE2 GLU B 223    11097  17115   6338  -1493  -1286  -2073       O  
ATOM   3266  N   TRP B 224      29.516  32.527  47.204  1.00 76.86           N  
ANISOU 3266  N   TRP B 224     9281  13909   6013  -1280  -1045  -1509       N  
ATOM   3267  CA  TRP B 224      29.474  31.385  48.112  1.00 74.91           C  
ANISOU 3267  CA  TRP B 224     8999  13376   6088  -1463  -1008  -1736       C  
ATOM   3268  C   TRP B 224      28.577  30.264  47.607  1.00 77.84           C  
ANISOU 3268  C   TRP B 224     9263  13969   6342  -1717  -1130  -2060       C  
ATOM   3269  O   TRP B 224      27.348  30.318  47.719  1.00 78.68           O  
ANISOU 3269  O   TRP B 224     9168  14349   6375  -1777  -1295  -2046       O  
ATOM   3270  CB  TRP B 224      29.033  31.807  49.512  1.00 71.88           C  
ANISOU 3270  CB  TRP B 224     8532  12781   5997  -1385  -1025  -1530       C  
ATOM   3271  CG  TRP B 224      29.296  30.756  50.548  1.00 68.28           C  
ANISOU 3271  CG  TRP B 224     8111  11946   5883  -1540   -940  -1701       C  
ATOM   3272  CD1 TRP B 224      28.364  30.027  51.227  1.00 66.77           C  
ANISOU 3272  CD1 TRP B 224     7805  11730   5832  -1721  -1015  -1817       C  
ATOM   3273  CD2 TRP B 224      30.580  30.308  51.019  1.00 64.30           C  
ANISOU 3273  CD2 TRP B 224     7778  11050   5601  -1521   -762  -1771       C  
ATOM   3274  NE1 TRP B 224      28.982  29.155  52.093  1.00 64.28           N  
ANISOU 3274  NE1 TRP B 224     7624  10988   5811  -1813   -893  -1935       N  
ATOM   3275  CE2 TRP B 224      30.344  29.312  51.989  1.00 63.46           C  
ANISOU 3275  CE2 TRP B 224     7687  10662   5762  -1665   -746  -1910       C  
ATOM   3276  CE3 TRP B 224      31.905  30.660  50.724  1.00 62.89           C  
ANISOU 3276  CE3 TRP B 224     7731  10759   5405  -1397   -613  -1729       C  
ATOM   3277  CZ2 TRP B 224      31.392  28.660  52.667  1.00 59.52           C  
ANISOU 3277  CZ2 TRP B 224     7345   9761   5507  -1637   -601  -1996       C  
ATOM   3278  CZ3 TRP B 224      32.945  30.004  51.403  1.00 59.94           C  
ANISOU 3278  CZ3 TRP B 224     7461  10034   5277  -1380   -469  -1839       C  
ATOM   3279  CH2 TRP B 224      32.675  29.021  52.358  1.00 57.89           C  
ANISOU 3279  CH2 TRP B 224     7229   9489   5275  -1475   -473  -1964       C  
ATOM   3280  N   THR B 225      29.206  29.225  47.076  1.00 79.45           N  
ANISOU 3280  N   THR B 225     9600  14061   6524  -1873  -1043  -2371       N  
ATOM   3281  CA  THR B 225      28.452  28.156  46.417  1.00 83.17           C  
ANISOU 3281  CA  THR B 225    10024  14741   6837  -2149  -1146  -2717       C  
ATOM   3282  C   THR B 225      28.188  26.928  47.314  1.00 83.12           C  
ANISOU 3282  C   THR B 225    10071  14388   7123  -2403  -1112  -2949       C  
ATOM   3283  O   THR B 225      27.718  25.896  46.829  1.00 86.57           O  
ANISOU 3283  O   THR B 225    10536  14896   7457  -2683  -1159  -3278       O  
ATOM   3284  CB  THR B 225      29.080  27.782  45.033  1.00 85.51           C  
ANISOU 3284  CB  THR B 225    10447  15213   6827  -2182  -1100  -2951       C  
ATOM   3285  OG1 THR B 225      29.112  26.360  44.882  1.00 87.84           O  
ANISOU 3285  OG1 THR B 225    10865  15333   7175  -2442  -1063  -3358       O  
ATOM   3286  CG2 THR B 225      30.517  28.341  44.876  1.00 84.00           C  
ANISOU 3286  CG2 THR B 225    10416  14843   6655  -1954   -911  -2812       C  
ATOM   3287  N   GLN B 226      28.440  27.067  48.617  1.00 80.13           N  
ANISOU 3287  N   GLN B 226     9719  13642   7085  -2319  -1033  -2771       N  
ATOM   3288  CA  GLN B 226      28.474  25.935  49.561  1.00 79.79           C  
ANISOU 3288  CA  GLN B 226     9808  13171   7337  -2510   -957  -2943       C  
ATOM   3289  C   GLN B 226      27.214  25.713  50.397  1.00 79.70           C  
ANISOU 3289  C   GLN B 226     9628  13217   7436  -2731  -1057  -2918       C  
ATOM   3290  O   GLN B 226      26.337  26.577  50.498  1.00 79.54           O  
ANISOU 3290  O   GLN B 226     9348  13553   7319  -2668  -1182  -2719       O  
ATOM   3291  CB  GLN B 226      29.653  26.081  50.544  1.00 76.66           C  
ANISOU 3291  CB  GLN B 226     9567  12315   7244  -2285   -793  -2787       C  
ATOM   3292  CG  GLN B 226      31.020  26.280  49.909  1.00 77.72           C  
ANISOU 3292  CG  GLN B 226     9838  12385   7305  -2072   -663  -2812       C  
ATOM   3293  CD  GLN B 226      31.370  25.222  48.890  1.00 81.75           C  
ANISOU 3293  CD  GLN B 226    10515  12894   7650  -2191   -621  -3184       C  
ATOM   3294  OE1 GLN B 226      31.283  24.020  49.160  1.00 84.04           O  
ANISOU 3294  OE1 GLN B 226    10978  12893   8060  -2358   -590  -3440       O  
ATOM   3295  NE2 GLN B 226      31.780  25.665  47.710  1.00 83.35           N  
ANISOU 3295  NE2 GLN B 226    10698  13406   7563  -2105   -611  -3216       N  
ATOM   3296  N   ASP B 227      27.190  24.548  51.038  1.00 79.54           N  
ANISOU 3296  N   ASP B 227     9779  12823   7616  -2969   -987  -3114       N  
ATOM   3297  CA  ASP B 227      26.103  24.112  51.896  1.00 79.59           C  
ANISOU 3297  CA  ASP B 227     9677  12820   7741  -3251  -1038  -3130       C  
ATOM   3298  C   ASP B 227      25.974  24.985  53.162  1.00 75.55           C  
ANISOU 3298  C   ASP B 227     9022  12231   7450  -3050  -1024  -2780       C  
ATOM   3299  O   ASP B 227      24.924  25.601  53.395  1.00 75.84           O  
ANISOU 3299  O   ASP B 227     8765  12638   7413  -3079  -1139  -2647       O  
ATOM   3300  CB  ASP B 227      26.356  22.655  52.278  1.00 81.38           C  
ANISOU 3300  CB  ASP B 227    10230  12557   8132  -3525   -927  -3401       C  
ATOM   3301  CG  ASP B 227      25.155  21.783  52.078  1.00 85.88           C  
ANISOU 3301  CG  ASP B 227    10746  13298   8586  -4012  -1005  -3663       C  
ATOM   3302  OD1 ASP B 227      25.086  21.124  51.030  1.00 87.45           O  
ANISOU 3302  OD1 ASP B 227    11048  13602   8576  -4215  -1033  -3974       O  
ATOM   3303  OD2 ASP B 227      24.277  21.742  52.962  1.00 87.98           O  
ANISOU 3303  OD2 ASP B 227    10862  13609   8955  -4217  -1031  -3575       O  
ATOM   3304  N   ARG B 228      27.036  25.038  53.978  1.00 71.52           N  
ANISOU 3304  N   ARG B 228     8709  11271   7192  -2834   -887  -2645       N  
ATOM   3305  CA  ARG B 228      27.049  25.858  55.199  1.00 66.45           C  
ANISOU 3305  CA  ARG B 228     7967  10524   6757  -2637   -862  -2331       C  
ATOM   3306  C   ARG B 228      26.838  27.350  54.919  1.00 64.13           C  
ANISOU 3306  C   ARG B 228     7441  10600   6323  -2360   -946  -2064       C  
ATOM   3307  O   ARG B 228      27.072  27.821  53.803  1.00 64.52           O  
ANISOU 3307  O   ARG B 228     7471  10902   6141  -2248   -990  -2077       O  
ATOM   3308  CB  ARG B 228      28.352  25.649  55.980  1.00 64.51           C  
ANISOU 3308  CB  ARG B 228     7972   9776   6763  -2440   -710  -2263       C  
ATOM   3309  CG  ARG B 228      29.623  26.013  55.184  1.00 63.26           C  
ANISOU 3309  CG  ARG B 228     7921   9591   6521  -2185   -641  -2274       C  
ATOM   3310  CD  ARG B 228      30.854  25.785  56.016  1.00 59.24           C  
ANISOU 3310  CD  ARG B 228     7600   8659   6246  -1990   -503  -2221       C  
ATOM   3311  NE  ARG B 228      32.104  25.967  55.266  1.00 58.14           N  
ANISOU 3311  NE  ARG B 228     7546   8521   6021  -1782   -419  -2280       N  
ATOM   3312  CZ  ARG B 228      32.924  27.009  55.396  1.00 53.13           C  
ANISOU 3312  CZ  ARG B 228     6840   7946   5400  -1546   -365  -2075       C  
ATOM   3313  NH1 ARG B 228      34.052  27.051  54.673  1.00 51.99           N  
ANISOU 3313  NH1 ARG B 228     6759   7838   5157  -1407   -272  -2164       N  
ATOM   3314  NH2 ARG B 228      32.626  27.999  56.242  1.00 45.70           N  
ANISOU 3314  NH2 ARG B 228     5770   7034   4557  -1466   -393  -1798       N  
ATOM   3315  N   ALA B 229      26.409  28.083  55.948  1.00 61.17           N  
ANISOU 3315  N   ALA B 229     6924  10238   6077  -2242   -961  -1820       N  
ATOM   3316  CA  ALA B 229      26.170  29.523  55.848  1.00 59.00           C  
ANISOU 3316  CA  ALA B 229     6483  10242   5690  -1950  -1032  -1551       C  
ATOM   3317  C   ALA B 229      27.468  30.284  55.513  1.00 56.16           C  
ANISOU 3317  C   ALA B 229     6301   9711   5326  -1678   -942  -1411       C  
ATOM   3318  O   ALA B 229      28.524  29.966  56.041  1.00 53.75           O  
ANISOU 3318  O   ALA B 229     6175   9029   5217  -1641   -812  -1422       O  
ATOM   3319  CB  ALA B 229      25.577  30.050  57.153  1.00 57.33           C  
ANISOU 3319  CB  ALA B 229     6134   9999   5648  -1870  -1035  -1347       C  
ATOM   3320  N   LYS B 230      27.368  31.277  54.630  1.00 55.64           N  
ANISOU 3320  N   LYS B 230     6180   9944   5016  -1497  -1012  -1282       N  
ATOM   3321  CA  LYS B 230      28.501  32.123  54.271  1.00 53.79           C  
ANISOU 3321  CA  LYS B 230     6107   9591   4737  -1283   -920  -1128       C  
ATOM   3322  C   LYS B 230      29.234  32.574  55.544  1.00 50.21           C  
ANISOU 3322  C   LYS B 230     5743   8769   4566  -1158   -802   -954       C  
ATOM   3323  O   LYS B 230      28.606  33.109  56.468  1.00 49.69           O  
ANISOU 3323  O   LYS B 230     5582   8690   4606  -1074   -839   -791       O  
ATOM   3324  CB  LYS B 230      28.019  33.336  53.451  1.00 55.07           C  
ANISOU 3324  CB  LYS B 230     6213  10103   4608  -1080  -1022   -928       C  
ATOM   3325  CG  LYS B 230      29.077  34.036  52.579  1.00 55.06           C  
ANISOU 3325  CG  LYS B 230     6400  10081   4437   -955   -935   -828       C  
ATOM   3326  CD  LYS B 230      28.529  35.332  51.971  1.00 57.38           C  
ANISOU 3326  CD  LYS B 230     6696  10649   4454   -722  -1034   -570       C  
ATOM   3327  CE  LYS B 230      29.524  36.022  51.060  1.00 59.43           C  
ANISOU 3327  CE  LYS B 230     7171  10896   4511   -646   -936   -458       C  
ATOM   3328  NZ  LYS B 230      29.019  37.348  50.598  1.00 62.20           N  
ANISOU 3328  NZ  LYS B 230     7599  11430   4601   -394  -1020   -164       N  
ATOM   3329  N   PRO B 231      30.558  32.337  55.615  1.00 48.13           N  
ANISOU 3329  N   PRO B 231     5641   8234   4410  -1143   -660  -1004       N  
ATOM   3330  CA  PRO B 231      31.300  32.771  56.796  1.00 45.01           C  
ANISOU 3330  CA  PRO B 231     5310   7538   4255  -1035   -557   -855       C  
ATOM   3331  C   PRO B 231      31.645  34.270  56.668  1.00 43.58           C  
ANISOU 3331  C   PRO B 231     5180   7407   3971   -852   -530   -594       C  
ATOM   3332  O   PRO B 231      32.761  34.666  56.268  1.00 43.64           O  
ANISOU 3332  O   PRO B 231     5300   7356   3924   -818   -420   -566       O  
ATOM   3333  CB  PRO B 231      32.528  31.861  56.791  1.00 44.61           C  
ANISOU 3333  CB  PRO B 231     5379   7257   4312  -1082   -433  -1043       C  
ATOM   3334  CG  PRO B 231      32.732  31.515  55.337  1.00 47.48           C  
ANISOU 3334  CG  PRO B 231     5778   7832   4427  -1142   -437  -1215       C  
ATOM   3335  CD  PRO B 231      31.435  31.722  54.608  1.00 49.17           C  
ANISOU 3335  CD  PRO B 231     5883   8375   4425  -1205   -588  -1205       C  
ATOM   3336  N   VAL B 232      30.642  35.081  56.968  1.00 41.90           N  
ANISOU 3336  N   VAL B 232     4891   7318   3710   -743   -627   -414       N  
ATOM   3337  CA  VAL B 232      30.757  36.529  56.951  1.00 40.76           C  
ANISOU 3337  CA  VAL B 232     4845   7173   3466   -552   -612   -152       C  
ATOM   3338  C   VAL B 232      31.352  37.075  58.249  1.00 37.62           C  
ANISOU 3338  C   VAL B 232     4520   6467   3304   -490   -514    -25       C  
ATOM   3339  O   VAL B 232      31.418  36.379  59.262  1.00 35.42           O  
ANISOU 3339  O   VAL B 232     4176   6022   3259   -559   -488   -109       O  
ATOM   3340  CB  VAL B 232      29.367  37.222  56.695  1.00 41.89           C  
ANISOU 3340  CB  VAL B 232     4888   7600   3428   -390   -770    -13       C  
ATOM   3341  CG1 VAL B 232      28.973  37.120  55.242  1.00 45.85           C  
ANISOU 3341  CG1 VAL B 232     5364   8442   3615   -398   -865    -73       C  
ATOM   3342  CG2 VAL B 232      28.273  36.624  57.567  1.00 41.21           C  
ANISOU 3342  CG2 VAL B 232     4583   7590   3482   -435   -857    -86       C  
ATOM   3343  N   THR B 233      31.789  38.332  58.176  1.00 37.76           N  
ANISOU 3343  N   THR B 233     4699   6410   3238   -372   -458    178       N  
ATOM   3344  CA  THR B 233      32.194  39.142  59.318  1.00 35.93           C  
ANISOU 3344  CA  THR B 233     4561   5920   3168   -301   -382    323       C  
ATOM   3345  C   THR B 233      30.993  39.247  60.239  1.00 35.11           C  
ANISOU 3345  C   THR B 233     4336   5839   3163   -178   -482    386       C  
ATOM   3346  O   THR B 233      29.938  39.694  59.820  1.00 36.90           O  
ANISOU 3346  O   THR B 233     4518   6275   3227    -29   -595    473       O  
ATOM   3347  CB  THR B 233      32.632  40.560  58.815  1.00 36.85           C  
ANISOU 3347  CB  THR B 233     4922   5976   3101   -213   -318    537       C  
ATOM   3348  OG1 THR B 233      33.867  40.447  58.088  1.00 38.06           O  
ANISOU 3348  OG1 THR B 233     5164   6123   3173   -372   -193    469       O  
ATOM   3349  CG2 THR B 233      32.773  41.566  59.964  1.00 34.76           C  
ANISOU 3349  CG2 THR B 233     4788   5452   2966   -124   -262    695       C  
ATOM   3350  N   GLN B 234      31.162  38.862  61.489  1.00 33.75           N  
ANISOU 3350  N   GLN B 234     4104   5484   3234   -223   -440    343       N  
ATOM   3351  CA  GLN B 234      30.059  38.760  62.416  1.00 34.86           C  
ANISOU 3351  CA  GLN B 234     4099   5673   3472   -148   -515    368       C  
ATOM   3352  C   GLN B 234      30.612  38.697  63.826  1.00 33.73           C  
ANISOU 3352  C   GLN B 234     3979   5266   3568   -177   -430    375       C  
ATOM   3353  O   GLN B 234      31.803  38.410  64.037  1.00 32.39           O  
ANISOU 3353  O   GLN B 234     3888   4918   3500   -278   -333    314       O  
ATOM   3354  CB  GLN B 234      29.227  37.475  62.106  1.00 35.84           C  
ANISOU 3354  CB  GLN B 234     4015   6012   3589   -294   -603    188       C  
ATOM   3355  CG  GLN B 234      30.017  36.163  62.282  1.00 34.71           C  
ANISOU 3355  CG  GLN B 234     3882   5703   3601   -509   -533     -5       C  
ATOM   3356  CD  GLN B 234      29.263  34.960  61.735  1.00 40.65           C  
ANISOU 3356  CD  GLN B 234     4507   6636   4302   -689   -609   -196       C  
ATOM   3357  OE1 GLN B 234      28.362  34.429  62.408  1.00 40.99           O  
ANISOU 3357  OE1 GLN B 234     4417   6736   4422   -778   -651   -237       O  
ATOM   3358  NE2 GLN B 234      29.606  34.532  60.496  1.00 38.29           N  
ANISOU 3358  NE2 GLN B 234     4252   6443   3853   -769   -619   -325       N  
ATOM   3359  N   ILE B 235      29.736  38.971  64.790  1.00 34.10           N  
ANISOU 3359  N   ILE B 235     3939   5330   3685    -75   -468    444       N  
ATOM   3360  CA  ILE B 235      29.992  38.705  66.203  1.00 32.55           C  
ANISOU 3360  CA  ILE B 235     3723   4943   3701   -113   -409    433       C  
ATOM   3361  C   ILE B 235      29.323  37.413  66.609  1.00 32.68           C  
ANISOU 3361  C   ILE B 235     3563   5043   3809   -261   -446    307       C  
ATOM   3362  O   ILE B 235      28.163  37.230  66.295  1.00 33.85           O  
ANISOU 3362  O   ILE B 235     3553   5443   3864   -260   -531    287       O  
ATOM   3363  CB  ILE B 235      29.462  39.850  67.096  1.00 33.28           C  
ANISOU 3363  CB  ILE B 235     3853   4991   3799     89   -408    583       C  
ATOM   3364  CG1 ILE B 235      30.253  41.144  66.762  1.00 34.23           C  
ANISOU 3364  CG1 ILE B 235     4227   4945   3834    191   -347    706       C  
ATOM   3365  CG2 ILE B 235      29.511  39.438  68.612  1.00 30.61           C  
ANISOU 3365  CG2 ILE B 235     3454   4517   3657     40   -359    558       C  
ATOM   3366  CD1 ILE B 235      29.819  42.381  67.493  1.00 34.08           C  
ANISOU 3366  CD1 ILE B 235     4327   4827   3794    408   -337    845       C  
ATOM   3367  N   VAL B 236      30.063  36.542  67.311  1.00 31.34           N  
ANISOU 3367  N   VAL B 236     3429   4671   3805   -388   -380    224       N  
ATOM   3368  CA  VAL B 236      29.540  35.297  67.902  1.00 32.11           C  
ANISOU 3368  CA  VAL B 236     3437   4758   4003   -550   -388    125       C  
ATOM   3369  C   VAL B 236      29.766  35.434  69.436  1.00 31.58           C  
ANISOU 3369  C   VAL B 236     3397   4512   4088   -504   -329    203       C  
ATOM   3370  O   VAL B 236      30.872  35.777  69.868  1.00 31.83           O  
ANISOU 3370  O   VAL B 236     3544   4359   4190   -439   -269    234       O  
ATOM   3371  CB  VAL B 236      30.288  34.064  67.340  1.00 31.84           C  
ANISOU 3371  CB  VAL B 236     3488   4602   4006   -704   -361    -38       C  
ATOM   3372  CG1 VAL B 236      29.598  32.718  67.733  1.00 31.28           C  
ANISOU 3372  CG1 VAL B 236     3383   4499   4002   -912   -370   -149       C  
ATOM   3373  CG2 VAL B 236      30.391  34.147  65.785  1.00 34.86           C  
ANISOU 3373  CG2 VAL B 236     3878   5147   4218   -719   -400   -113       C  
ATOM   3374  N   SER B 237      28.758  35.206  70.273  1.00 32.07           N  
ANISOU 3374  N   SER B 237     3342   4660   4182   -544   -342    230       N  
ATOM   3375  CA  SER B 237      28.967  35.437  71.704  1.00 31.55           C  
ANISOU 3375  CA  SER B 237     3308   4450   4228   -485   -285    310       C  
ATOM   3376  C   SER B 237      28.386  34.304  72.507  1.00 31.56           C  
ANISOU 3376  C   SER B 237     3260   4431   4300   -666   -263    271       C  
ATOM   3377  O   SER B 237      27.605  33.535  71.979  1.00 32.58           O  
ANISOU 3377  O   SER B 237     3303   4696   4379   -841   -295    187       O  
ATOM   3378  CB  SER B 237      28.368  36.777  72.129  1.00 31.47           C  
ANISOU 3378  CB  SER B 237     3241   4558   4158   -283   -296    429       C  
ATOM   3379  OG  SER B 237      26.955  36.666  72.277  1.00 39.08           O  
ANISOU 3379  OG  SER B 237     4002   5791   5053   -299   -338    431       O  
ATOM   3380  N   ALA B 238      28.779  34.180  73.779  1.00 30.49           N  
ANISOU 3380  N   ALA B 238     3193   4128   4263   -645   -206    328       N  
ATOM   3381  CA  ALA B 238      28.075  33.274  74.730  1.00 30.79           C  
ANISOU 3381  CA  ALA B 238     3198   4159   4341   -813   -170    333       C  
ATOM   3382  C   ALA B 238      27.984  34.011  76.054  1.00 30.57           C  
ANISOU 3382  C   ALA B 238     3143   4133   4336   -682   -128    444       C  
ATOM   3383  O   ALA B 238      28.771  34.941  76.273  1.00 28.76           O  
ANISOU 3383  O   ALA B 238     2982   3820   4125   -496   -123    491       O  
ATOM   3384  CB  ALA B 238      28.835  31.977  74.911  1.00 30.41           C  
ANISOU 3384  CB  ALA B 238     3342   3834   4376   -941   -134    276       C  
ATOM   3385  N   GLU B 239      27.052  33.616  76.931  1.00 30.74           N  
ANISOU 3385  N   GLU B 239     3072   4260   4346   -799    -90    476       N  
ATOM   3386  CA  GLU B 239      26.858  34.355  78.176  1.00 31.00           C  
ANISOU 3386  CA  GLU B 239     3064   4339   4375   -666    -46    568       C  
ATOM   3387  C   GLU B 239      26.413  33.476  79.328  1.00 32.11           C  
ANISOU 3387  C   GLU B 239     3214   4456   4527   -844     24    607       C  
ATOM   3388  O   GLU B 239      26.018  32.349  79.129  1.00 32.93           O  
ANISOU 3388  O   GLU B 239     3342   4538   4631  -1096     43    566       O  
ATOM   3389  CB  GLU B 239      25.824  35.461  77.987  1.00 33.11           C  
ANISOU 3389  CB  GLU B 239     3125   4911   4540   -511    -73    587       C  
ATOM   3390  CG  GLU B 239      24.398  35.053  77.506  1.00 37.36           C  
ANISOU 3390  CG  GLU B 239     3412   5801   4980   -661    -97    534       C  
ATOM   3391  CD  GLU B 239      23.547  36.337  77.168  1.00 42.49           C  
ANISOU 3391  CD  GLU B 239     3869   6766   5510   -387   -147    555       C  
ATOM   3392  OE1 GLU B 239      23.807  37.021  76.133  1.00 40.86           O  
ANISOU 3392  OE1 GLU B 239     3707   6561   5258   -217   -218    554       O  
ATOM   3393  OE2 GLU B 239      22.649  36.673  77.979  1.00 46.10           O  
ANISOU 3393  OE2 GLU B 239     4149   7461   5904   -319   -109    579       O  
ATOM   3394  N   ALA B 240      26.468  33.991  80.542  1.00 31.54           N  
ANISOU 3394  N   ALA B 240     3149   4384   4451   -730     72    685       N  
ATOM   3395  CA  ALA B 240      25.935  33.238  81.691  1.00 32.72           C  
ANISOU 3395  CA  ALA B 240     3301   4552   4577   -902    152    741       C  
ATOM   3396  C   ALA B 240      25.524  34.280  82.694  1.00 31.52           C  
ANISOU 3396  C   ALA B 240     3036   4575   4365   -723    191    794       C  
ATOM   3397  O   ALA B 240      26.061  35.357  82.632  1.00 29.12           O  
ANISOU 3397  O   ALA B 240     2760   4232   4071   -482    157    792       O  
ATOM   3398  CB  ALA B 240      27.042  32.346  82.309  1.00 32.90           C  
ANISOU 3398  CB  ALA B 240     3596   4236   4668   -941    174    788       C  
ATOM   3399  N   TRP B 241      24.632  33.919  83.627  1.00 31.63           N  
ANISOU 3399  N   TRP B 241     2948   4759   4308   -861    272    835       N  
ATOM   3400  CA  TRP B 241      24.283  34.708  84.796  1.00 30.66           C  
ANISOU 3400  CA  TRP B 241     2746   4789   4114   -710    332    880       C  
ATOM   3401  C   TRP B 241      25.020  34.158  86.029  1.00 30.81           C  
ANISOU 3401  C   TRP B 241     2976   4588   4142   -758    387    967       C  
ATOM   3402  O   TRP B 241      25.305  32.976  86.120  1.00 31.09           O  
ANISOU 3402  O   TRP B 241     3172   4435   4205   -965    407   1009       O  
ATOM   3403  CB  TRP B 241      22.719  34.689  85.010  1.00 32.73           C  
ANISOU 3403  CB  TRP B 241     2708   5473   4254   -827    397    859       C  
ATOM   3404  CG  TRP B 241      22.013  35.410  83.881  1.00 34.90           C  
ANISOU 3404  CG  TRP B 241     2755   6017   4488   -687    323    779       C  
ATOM   3405  CD1 TRP B 241      21.613  34.868  82.682  1.00 37.88           C  
ANISOU 3405  CD1 TRP B 241     3031   6497   4863   -854    264    712       C  
ATOM   3406  CD2 TRP B 241      21.757  36.819  83.778  1.00 35.29           C  
ANISOU 3406  CD2 TRP B 241     2702   6223   4483   -321    288    759       C  
ATOM   3407  NE1 TRP B 241      21.053  35.826  81.888  1.00 38.52           N  
ANISOU 3407  NE1 TRP B 241     2919   6839   4876   -613    190    665       N  
ATOM   3408  CE2 TRP B 241      21.154  37.041  82.513  1.00 36.69           C  
ANISOU 3408  CE2 TRP B 241     2707   6617   4616   -267    203    700       C  
ATOM   3409  CE3 TRP B 241      21.958  37.917  84.644  1.00 34.72           C  
ANISOU 3409  CE3 TRP B 241     2690   6121   4379    -28    321    780       C  
ATOM   3410  CZ2 TRP B 241      20.772  38.316  82.072  1.00 35.29           C  
ANISOU 3410  CZ2 TRP B 241     2440   6605   4364    100    147    685       C  
ATOM   3411  CZ3 TRP B 241      21.559  39.178  84.224  1.00 35.25           C  
ANISOU 3411  CZ3 TRP B 241     2683   6326   4381    315    277    749       C  
ATOM   3412  CH2 TRP B 241      20.965  39.371  82.941  1.00 37.26           C  
ANISOU 3412  CH2 TRP B 241     2785   6780   4590    393    190    712       C  
ATOM   3413  N   GLY B 242      25.320  35.045  86.974  1.00 30.80           N  
ANISOU 3413  N   GLY B 242     2993   4606   4100   -550    407    990       N  
ATOM   3414  CA  GLY B 242      25.695  34.676  88.310  1.00 33.24           C  
ANISOU 3414  CA  GLY B 242     3435   4833   4359   -578    467   1073       C  
ATOM   3415  C   GLY B 242      24.780  33.583  88.852  1.00 38.46           C  
ANISOU 3415  C   GLY B 242     4063   5607   4942   -871    567   1143       C  
ATOM   3416  O   GLY B 242      23.702  33.394  88.339  1.00 39.32           O  
ANISOU 3416  O   GLY B 242     3974   5948   5016  -1030    601   1102       O  
ATOM   3417  N   ARG B 243      25.226  32.886  89.895  1.00 41.10           N  
ANISOU 3417  N   ARG B 243     4595   5791   5229   -947    616   1249       N  
ATOM   3418  CA  ARG B 243      24.549  31.713  90.433  1.00 47.55           C  
ANISOU 3418  CA  ARG B 243     5478   6623   5962  -1265    723   1342       C  
ATOM   3419  C   ARG B 243      24.740  31.749  91.943  1.00 49.03           C  
ANISOU 3419  C   ARG B 243     5771   6832   6024  -1210    793   1452       C  
ATOM   3420  O   ARG B 243      25.880  31.715  92.418  1.00 47.61           O  
ANISOU 3420  O   ARG B 243     5805   6425   5858  -1038    733   1505       O  
ATOM   3421  CB  ARG B 243      25.201  30.450  89.837  1.00 48.16           C  
ANISOU 3421  CB  ARG B 243     5836   6335   6125  -1422    685   1381       C  
ATOM   3422  CG  ARG B 243      24.426  29.175  90.064  1.00 57.10           C  
ANISOU 3422  CG  ARG B 243     7084   7424   7184  -1816    798   1457       C  
ATOM   3423  CD  ARG B 243      23.480  28.925  88.880  1.00 65.36           C  
ANISOU 3423  CD  ARG B 243     7935   8635   8263  -2072    804   1337       C  
ATOM   3424  NE  ARG B 243      24.106  28.116  87.825  1.00 68.48           N  
ANISOU 3424  NE  ARG B 243     8553   8694   8771  -2141    732   1287       N  
ATOM   3425  CZ  ARG B 243      23.887  26.807  87.636  1.00 72.91           C  
ANISOU 3425  CZ  ARG B 243     9357   9024   9318  -2481    793   1312       C  
ATOM   3426  NH1 ARG B 243      24.513  26.174  86.641  1.00 72.94           N  
ANISOU 3426  NH1 ARG B 243     9568   8722   9423  -2486    722   1241       N  
ATOM   3427  NH2 ARG B 243      23.052  26.120  88.429  1.00 73.33           N  
ANISOU 3427  NH2 ARG B 243     9473   9142   9247  -2828    935   1401       N  
ATOM   3428  N   ALA B 244      23.649  31.863  92.698  1.00 53.63           N  
ANISOU 3428  N   ALA B 244     6183   7729   6465  -1340    918   1476       N  
ATOM   3429  CA  ALA B 244      23.709  31.867  94.187  1.00 57.77           C  
ANISOU 3429  CA  ALA B 244     6800   8317   6831  -1314   1004   1582       C  
ATOM   3430  C   ALA B 244      24.336  30.554  94.698  1.00 60.49           C  
ANISOU 3430  C   ALA B 244     7513   8330   7140  -1479   1024   1752       C  
ATOM   3431  O   ALA B 244      24.670  30.414  95.873  1.00 62.21           O  
ANISOU 3431  O   ALA B 244     7887   8524   7226  -1428   1065   1867       O  
ATOM   3432  CB  ALA B 244      22.314  32.118  94.799  1.00 59.87           C  
ANISOU 3432  CB  ALA B 244     6789   9024   6935  -1462   1156   1567       C  
ATOM   3433  N   ASP B 245      24.460  29.619  93.750  1.00 63.43           N  
ANISOU 3433  N   ASP B 245     8030   8451   7621  -1660    992   1757       N  
ATOM   3434  CA  ASP B 245      25.325  28.407  93.735  1.00 66.26           C  
ANISOU 3434  CA  ASP B 245     8791   8374   8009  -1715    959   1876       C  
ATOM   3435  C   ASP B 245      24.577  27.111  93.978  1.00 70.12           C  
ANISOU 3435  C   ASP B 245     9488   8750   8402  -2134   1098   1995       C  
ATOM   3436  O   ASP B 245      24.050  26.546  93.009  1.00 71.70           O  
ANISOU 3436  O   ASP B 245     9672   8895   8675  -2400   1117   1922       O  
ATOM   3437  CB  ASP B 245      26.626  28.520  94.574  1.00 66.26           C  
ANISOU 3437  CB  ASP B 245     9014   8191   7969  -1391    874   1966       C  
ATOM   3438  CG  ASP B 245      27.912  28.467  93.702  1.00 65.76           C  
ANISOU 3438  CG  ASP B 245     9069   7851   8062  -1139    716   1898       C  
ATOM   3439  OD1 ASP B 245      28.788  27.581  93.973  1.00 69.17           O  
ANISOU 3439  OD1 ASP B 245     9825   7982   8471  -1044    672   2008       O  
ATOM   3440  OD2 ASP B 245      28.028  29.288  92.757  1.00 58.51           O  
ANISOU 3440  OD2 ASP B 245     7929   7029   7271  -1030    642   1741       O  
ATOM   3441  OXT ASP B 245      24.480  26.615  95.100  1.00 72.71           O  
ANISOU 3441  OXT ASP B 245    10013   9041   8570  -2234   1195   2159       O  
TER    3442      ASP B 245                                                      
HETATM 3443  C1  EDO A 195      57.326  55.619  82.939  1.00 61.24           C  
HETATM 3444  O1  EDO A 195      57.934  54.385  83.331  1.00 56.39           O  
HETATM 3445  C2  EDO A 195      55.902  55.319  82.472  1.00 60.55           C  
HETATM 3446  O2  EDO A 195      55.997  54.225  81.571  1.00 61.73           O  
HETATM 3447  C1  EDO A 196      54.114  55.953  67.808  1.00 45.86           C  
HETATM 3448  O1  EDO A 196      54.694  56.749  68.867  1.00 42.27           O  
HETATM 3449  C2  EDO A 196      52.622  55.754  68.026  1.00 47.58           C  
HETATM 3450  O2  EDO A 196      52.222  54.807  67.058  1.00 50.27           O  
HETATM 3451  C1  EDO A 197      69.713  62.961  74.304  1.00 48.01           C  
HETATM 3452  O1  EDO A 197      70.124  63.777  73.199  1.00 55.11           O  
HETATM 3453  C2  EDO A 197      69.427  63.954  75.425  1.00 53.02           C  
HETATM 3454  O2  EDO A 197      68.197  64.626  75.107  1.00 54.88           O  
HETATM 3455  C1  GOL A 198      69.445  34.645  76.329  1.00 56.30           C  
HETATM 3456  O1  GOL A 198      69.744  36.029  76.512  1.00 52.51           O  
HETATM 3457  C2  GOL A 198      67.944  34.389  76.180  1.00 61.74           C  
HETATM 3458  O2  GOL A 198      67.435  34.906  74.947  1.00 63.29           O  
HETATM 3459  C3  GOL A 198      67.635  32.893  76.341  1.00 63.88           C  
HETATM 3460  O3  GOL A 198      68.581  32.143  75.605  1.00 65.15           O  
HETATM 3461  C1  GOL B 246      36.167  46.829  85.410  1.00 48.51           C  
HETATM 3462  O1  GOL B 246      36.216  45.603  86.142  1.00 43.64           O  
HETATM 3463  C2  GOL B 246      37.578  47.183  84.899  1.00 45.04           C  
HETATM 3464  O2  GOL B 246      37.970  46.260  83.917  1.00 42.54           O  
HETATM 3465  C3  GOL B 246      37.641  48.446  84.107  1.00 43.00           C  
HETATM 3466  O3  GOL B 246      38.683  48.052  83.293  1.00 39.84           O  
HETATM 3467  C1  EDO B 247      25.286  30.991  75.463  1.00 55.59           C  
HETATM 3468  O1  EDO B 247      24.858  32.344  75.632  1.00 57.58           O  
HETATM 3469  C2  EDO B 247      25.452  30.417  76.856  1.00 57.68           C  
HETATM 3470  O2  EDO B 247      26.811  30.044  77.092  1.00 56.31           O  
HETATM 3471  C1  EDO B 248      27.868  27.950  73.902  1.00 47.85           C  
HETATM 3472  O1  EDO B 248      27.499  29.302  73.601  1.00 49.08           O  
HETATM 3473  C2  EDO B 248      27.596  27.687  75.385  1.00 46.58           C  
HETATM 3474  O2  EDO B 248      28.307  28.557  76.286  1.00 39.28           O  
HETATM 3475  C1  EDO B 249      29.756  28.555  64.241  1.00 41.49           C  
HETATM 3476  O1  EDO B 249      29.323  29.928  64.384  1.00 40.71           O  
HETATM 3477  C2  EDO B 249      29.746  27.977  62.824  1.00 42.02           C  
HETATM 3478  O2  EDO B 249      30.858  27.043  62.609  1.00 45.43           O  
HETATM 3479  O   HOH A 199      49.287  32.397  90.270  1.00 21.09           O  
HETATM 3480  O   HOH A 200      52.827  50.772  73.846  1.00 32.68           O  
HETATM 3481  O   HOH A 201      76.416  49.402  78.781  1.00 20.98           O  
HETATM 3482  O   HOH A 202      56.440  49.358  79.468  1.00 24.90           O  
HETATM 3483  O   HOH A 203      51.420  49.027  71.901  1.00 30.78           O  
HETATM 3484  O   HOH A 204      43.652  27.845  93.644  1.00 29.20           O  
HETATM 3485  O   HOH A 205      51.560  45.238  86.241  1.00 27.90           O  
HETATM 3486  O   HOH A 206      45.504  33.897  84.265  1.00 23.23           O  
HETATM 3487  O   HOH A 207      70.324  39.573  66.435  1.00 23.56           O  
HETATM 3488  O   HOH A 208      47.589  43.638  90.913  1.00 29.83           O  
HETATM 3489  O   HOH A 209      47.453  43.774  74.149  1.00 45.69           O  
HETATM 3490  O   HOH A 210      53.781  42.644  70.682  1.00 41.17           O  
HETATM 3491  O   HOH A 211      48.179  33.691  92.286  1.00 29.77           O  
HETATM 3492  O   HOH A 212      51.990  42.261  75.189  1.00 31.66           O  
HETATM 3493  O   HOH A 213      61.520  37.836  71.208  1.00 30.65           O  
HETATM 3494  O   HOH A 214      53.342  39.037  82.624  1.00 29.76           O  
HETATM 3495  O   HOH A 215      55.922  33.474  91.340  1.00 29.50           O  
HETATM 3496  O   HOH A 216      64.176  51.224  56.351  1.00 30.71           O  
HETATM 3497  O   HOH A 217      55.215  39.313  76.479  1.00 28.33           O  
HETATM 3498  O   HOH A 218      54.134  34.107  84.685  1.00 31.12           O  
HETATM 3499  O   HOH A 219      50.118  36.869  80.212  1.00 31.74           O  
HETATM 3500  O   HOH A 220      73.545  49.334  78.664  1.00 31.24           O  
HETATM 3501  O   HOH A 221      64.629  34.756  79.476  1.00 36.16           O  
HETATM 3502  O   HOH A 222      47.852  24.213  96.795  1.00 37.34           O  
HETATM 3503  O   HOH A 223      71.407  59.082  60.262  1.00 53.61           O  
HETATM 3504  O   HOH A 224      51.999  48.974  86.085  1.00 35.90           O  
HETATM 3505  O   HOH A 225      49.036  44.276  85.519  1.00 33.09           O  
HETATM 3506  O   HOH A 226      53.711  49.207  82.503  1.00 37.26           O  
HETATM 3507  O   HOH A 227      52.655  26.138  76.516  1.00 45.21           O  
HETATM 3508  O   HOH A 228      44.516  33.270  86.637  1.00 33.33           O  
HETATM 3509  O   HOH A 229      66.977  41.733  81.673  1.00 44.31           O  
HETATM 3510  O   HOH A 230      47.965  29.020 100.039  1.00 54.17           O  
HETATM 3511  O   HOH A 231      49.553  44.880  65.990  1.00 38.79           O  
HETATM 3512  O   HOH A 232      49.276  36.656  94.141  1.00 46.88           O  
HETATM 3513  O   HOH A 233      63.673  37.945  69.700  1.00 34.91           O  
HETATM 3514  O   HOH A 234      58.415  36.856  89.417  1.00 32.91           O  
HETATM 3515  O   HOH A 235      51.481  41.815  68.086  1.00 41.93           O  
HETATM 3516  O   HOH A 236      47.467  32.664  94.673  1.00 28.21           O  
HETATM 3517  O   HOH A 237      48.356  29.664  74.165  1.00 44.14           O  
HETATM 3518  O   HOH A 238      67.344  45.452  60.453  1.00 36.48           O  
HETATM 3519  O   HOH A 239      48.825  49.659  72.950  1.00 32.36           O  
HETATM 3520  O   HOH A 240      53.613  38.154  78.176  1.00 24.85           O  
HETATM 3521  O   HOH A 241      52.542  37.582  80.493  1.00 33.39           O  
HETATM 3522  O   HOH A 242      47.588  46.520  75.582  1.00 47.64           O  
HETATM 3523  O   HOH A 243      53.603  40.544  74.474  1.00 36.84           O  
HETATM 3524  O   HOH A 244      52.314  38.369  74.163  1.00 34.78           O  
HETATM 3525  O   HOH A 245      53.967  35.013  81.990  1.00 45.06           O  
HETATM 3526  O   HOH A 246      50.101  33.534  77.458  1.00 50.89           O  
HETATM 3527  O   HOH A 247      51.228  43.947  95.041  1.00 38.56           O  
HETATM 3528  O   HOH A 248      47.744  37.024  97.645  1.00 47.19           O  
HETATM 3529  O   HOH A 249      68.827  42.894  83.172  1.00 41.38           O  
HETATM 3530  O   HOH A 250      62.630  41.027  91.838  1.00 41.93           O  
HETATM 3531  O   HOH B 250      27.358  42.031  80.143  1.00 29.96           O  
HETATM 3532  O   HOH B 251      37.139  42.851  77.199  1.00 31.54           O  
HETATM 3533  O   HOH B 252      39.274  38.322  57.542  1.00 25.05           O  
HETATM 3534  O   HOH B 253      41.310  38.983  71.046  1.00 24.56           O  
HETATM 3535  O   HOH B 254      42.091  31.925  87.328  1.00 27.65           O  
HETATM 3536  O   HOH B 255      58.992  59.778  48.824  1.00 29.87           O  
HETATM 3537  O   HOH B 256      35.051  41.763  70.606  1.00 21.79           O  
HETATM 3538  O   HOH B 257      34.629  40.967  91.475  1.00 33.93           O  
HETATM 3539  O   HOH B 258      44.088  41.387  83.634  1.00 27.51           O  
HETATM 3540  O   HOH B 259      58.668  42.270  58.416  1.00 31.12           O  
HETATM 3541  O   HOH B 260      20.837  39.964  93.672  1.00 35.93           O  
HETATM 3542  O   HOH B 261      25.887  38.100  68.057  1.00 40.04           O  
HETATM 3543  O   HOH B 262      36.821  28.130  88.036  1.00 35.48           O  
HETATM 3544  O   HOH B 263      26.219  34.381  68.745  1.00 33.35           O  
HETATM 3545  O   HOH B 264      26.883  41.985  92.953  1.00 35.23           O  
HETATM 3546  O   HOH B 265      33.092  44.427  67.580  1.00 30.36           O  
HETATM 3547  O   HOH B 266      56.551  68.325  48.012  1.00 43.30           O  
HETATM 3548  O   HOH B 267      44.715  55.915  51.608  1.00 41.66           O  
HETATM 3549  O   HOH B 268      39.206  43.158  89.455  1.00 38.30           O  
HETATM 3550  O   HOH B 269      31.747  49.591  77.678  1.00 36.02           O  
HETATM 3551  O   HOH B 270      47.682  32.125  77.091  1.00 40.19           O  
HETATM 3552  O   HOH B 271      40.391  40.066  75.189  1.00 28.68           O  
HETATM 3553  O   HOH B 272      28.025  42.908  74.981  1.00 25.77           O  
HETATM 3554  O   HOH B 273      62.340  55.278  45.259  1.00 36.09           O  
HETATM 3555  O   HOH B 274      63.350  48.805  56.436  1.00 31.11           O  
HETATM 3556  O   HOH B 275      26.573  37.095  96.226  1.00 34.83           O  
HETATM 3557  O   HOH B 276      43.339  38.217  65.588  1.00 40.34           O  
HETATM 3558  O   HOH B 277      50.237  42.490  44.670  1.00 56.34           O  
HETATM 3559  O   HOH B 278      27.539  35.262  97.934  1.00 38.76           O  
HETATM 3560  O   HOH B 279      57.417  54.172  45.414  1.00 44.07           O  
HETATM 3561  O   HOH B 280      46.751  60.601  48.473  1.00 49.68           O  
HETATM 3562  O   HOH B 281      33.967  30.515  99.043  1.00 55.01           O  
HETATM 3563  O   HOH B 282      37.718  46.227  59.074  1.00 54.07           O  
HETATM 3564  O   HOH B 283      20.120  34.756  77.525  1.00 46.26           O  
HETATM 3565  O   HOH B 284      29.468  23.619  52.696  1.00 70.28           O  
HETATM 3566  O   HOH B 285      23.029  31.477  82.830  1.00 46.98           O  
HETATM 3567  O   HOH B 286      34.213  48.213  82.995  1.00 45.26           O  
HETATM 3568  O   HOH B 287      37.918  39.987  56.125  1.00 42.13           O  
HETATM 3569  O   HOH B 288      33.885  42.580  56.521  1.00 47.52           O  
HETATM 3570  O   HOH B 289      28.945  29.325  69.203  1.00 31.22           O  
HETATM 3571  O   HOH B 290      28.866  27.820  89.617  1.00 52.42           O  
HETATM 3572  O   HOH B 291      52.277  67.510  51.089  1.00 45.43           O  
HETATM 3573  O   HOH B 292      44.396  39.810  77.785  1.00 38.77           O  
HETATM 3574  O   HOH B 293      52.961  39.913  61.922  1.00 41.95           O  
HETATM 3575  O   HOH B 294      61.440  43.966  47.490  1.00 39.91           O  
HETATM 3576  O   HOH B 295      41.666  43.836  78.417  1.00 45.68           O  
HETATM 3577  O   HOH B 296      39.908  41.960  76.705  1.00 30.05           O  
HETATM 3578  O   HOH B 297      55.812  39.616  49.485  1.00 40.55           O  
HETATM 3579  O   HOH B 298      43.612  37.359  69.163  1.00 40.14           O  
HETATM 3580  O   HOH B 299      20.142  34.892  87.134  1.00 44.61           O  
HETATM 3581  O   HOH B 300      50.522  35.968  42.920  1.00 46.94           O  
HETATM 3582  O   HOH B 301      51.409  59.864  43.975  1.00 46.72           O  
HETATM 3583  O   HOH B 302      46.489  44.440  63.947  1.00 50.72           O  
HETATM 3584  O   HOH B 303      25.447  35.441  74.024  1.00 45.51           O  
HETATM 3585  O   HOH B 304      48.566  40.770  65.440  1.00 49.64           O  
HETATM 3586  O   HOH B 305      47.934  33.148  65.117  1.00 49.38           O  
HETATM 3587  O   HOH B 306      41.543  22.738  60.587  1.00 45.25           O  
HETATM 3588  O   HOH B 307      41.664  42.367  70.334  1.00 38.08           O  
HETATM 3589  O   HOH B 308      34.142  42.444  89.279  1.00 40.97           O  
HETATM 3590  O   HOH B 309      57.258  59.733  42.875  1.00 44.12           O  
HETATM 3591  O   HOH B 310      55.604  50.877  42.611  1.00 48.17           O  
HETATM 3592  O   HOH B 311      33.512  26.794  63.634  1.00 49.20           O  
HETATM 3593  O   HOH B 312      37.030  42.158  56.488  1.00 44.39           O  
ENDMDL                                                                          
MASTER        0    0    0   13   96    0   20    6 7160    4    0   68          
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.