HEADER    TRANSFERASE                             08-DEC-12   XXXX              
TITLE     STRUCTURE OF HUMAN PROTEIN KINASE CK2 CATALYTIC SUBUNIT IN COMPLEX    
TITLE    2 WITH A CK2BETA-COMPETITIVE CYCLIC PEPTIDE                            
KEYWDS    PROTEIN KINASE FOLD, PROTEIN PHOSPHORYLATION, BINDING OF CK2BETA,     
KEYWDS   2 PHOSPHORYLATION, NUCLEUS, TRANSFERASE                                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.RAAF, B.GUERRA, I.NEUNDORF, B.BOPP, O.-G.ISSINGER, J.JOSE,          
AUTHOR   2 M.PIETSCH, K.NIEFIND                                                 
JRNL        AUTH   J.RAAF, B.GUERRA, I.NEUNDORF, B.BOPP, O.G.ISSINGER, J.JOSE,  
JRNL        AUTH 2 M.PIETSCH, K.NIEFIND                                         
JRNL        TITL   FIRST STRUCTURE OF PROTEIN KINASE CK2 CATALYTIC SUBUNIT WITH 
JRNL        TITL 2 AN EFFECTIVE CK2 BETA-COMPETITIVE LIGAND                     
JRNL        REF    ACS CHEM.BIOL.                V.   8   901 2013              
JRNL        REFN                US ISSN 1554-8929                               
JRNL        PMID   23474121                                                     
JRNL        DOI    10.1021/CB3007133                                            
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   K.NIEFIND, B.GUERRA, I.ERMAKOWA, O.G.ISSINGER                
REMARK   1  TITL   CRYSTAL STRUCTURE OF HUMAN PROTEIN KINASE CK2: INSIGHTS INTO 
REMARK   1  TITL 2 BASIC PROPERTIES OF THE CK2 HOLOENZYME                       
REMARK   1  REF    EMBO J.                       V.  20  5320 2001              
REMARK   1  REFN   ASTM EMJODG  UK ISSN 0261-4189                               
REMARK   1  PMID   11574463                                                     
REMARK   1  DOI    10.1093/EMBOJ/20.19.5320                                     
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   B.LAUDET, C.BARETTE, V.DULERY, O.RENAUDET, P.DUMY, A.METZ,   
REMARK   1  AUTH 2 R.PRUDENT, A.DESHIERE, O.DIDEBERG, O.FILHOL, C.COCHET        
REMARK   1  TITL   STRUCTURE-BASED DESIGN OF SMALL PEPTIDE INHIBITORS OF        
REMARK   1  TITL 2 PROTEIN KINASE CK2 SUBUNIT INTERACTION.                      
REMARK   1  REF    BIOCHEM.J.                    V. 408   363 2007              
REMARK   1  REFN   ASTM BIJOAK  UK ISSN 0264-6021                               
REMARK   1  PMID   17714077                                                     
REMARK   1  DOI    10.1042/BJ20070825                                           
SEQRES   1 A  335  MET SER GLY PRO VAL PRO SER ARG ALA ARG VAL TYR THR          
SEQRES   2 A  335  ASP VAL ASN THR HIS ARG PRO ARG GLU TYR TRP ASP TYR          
SEQRES   3 A  335  GLU SER HIS VAL VAL GLU TRP GLY ASN GLN ASP ASP TYR          
SEQRES   4 A  335  GLN LEU VAL ARG LYS LEU GLY ARG GLY LYS TYR SER GLU          
SEQRES   5 A  335  VAL PHE GLU ALA ILE ASN ILE THR ASN ASN GLU LYS VAL          
SEQRES   6 A  335  VAL VAL LYS ILE LEU LYS PRO VAL LYS LYS LYS LYS ILE          
SEQRES   7 A  335  LYS ARG GLU ILE LYS ILE LEU GLU ASN LEU ARG GLY GLY          
SEQRES   8 A  335  PRO ASN ILE ILE THR LEU ALA ASP ILE VAL LYS ASP PRO          
SEQRES   9 A  335  VAL SER ARG THR PRO ALA LEU VAL PHE GLU HIS VAL ASN          
SEQRES  10 A  335  ASN THR ASP PHE LYS GLN LEU TYR GLN THR LEU THR ASP          
SEQRES  11 A  335  TYR ASP ILE ARG PHE TYR MET TYR GLU ILE LEU LYS ALA          
SEQRES  12 A  335  LEU ASP TYR CYS HIS SER MET GLY ILE MET HIS ARG ASP          
SEQRES  13 A  335  VAL LYS PRO HIS ASN VAL MET ILE ASP HIS GLU HIS ARG          
SEQRES  14 A  335  LYS LEU ARG LEU ILE ASP TRP GLY LEU ALA GLU PHE TYR          
SEQRES  15 A  335  HIS PRO GLY GLN GLU TYR ASN VAL ARG VAL ALA SER ARG          
SEQRES  16 A  335  TYR PHE LYS GLY PRO GLU LEU LEU VAL ASP TYR GLN MET          
SEQRES  17 A  335  TYR ASP TYR SER LEU ASP MET TRP SER LEU GLY CYS MET          
SEQRES  18 A  335  LEU ALA SER MET ILE PHE ARG LYS GLU PRO PHE PHE HIS          
SEQRES  19 A  335  GLY HIS ASP ASN TYR ASP GLN LEU VAL ARG ILE ALA LYS          
SEQRES  20 A  335  VAL LEU GLY THR GLU ASP LEU TYR ASP TYR ILE ASP LYS          
SEQRES  21 A  335  TYR ASN ILE GLU LEU ASP PRO ARG PHE ASN ASP ILE LEU          
SEQRES  22 A  335  GLY ARG HIS SER ARG LYS ARG TRP GLU ARG PHE VAL HIS          
SEQRES  23 A  335  SER GLU ASN GLN HIS LEU VAL SER PRO GLU ALA LEU ASP          
SEQRES  24 A  335  PHE LEU ASP LYS LEU LEU ARG TYR ASP HIS GLN SER ARG          
SEQRES  25 A  335  LEU THR ALA ARG GLU ALA MET GLU HIS PRO TYR PHE TYR          
SEQRES  26 A  335  THR VAL VAL LYS ASP GLN ALA ARG MET GLY                      
SEQRES   1 B  335  MET SER GLY PRO VAL PRO SER ARG ALA ARG VAL TYR THR          
SEQRES   2 B  335  ASP VAL ASN THR HIS ARG PRO ARG GLU TYR TRP ASP TYR          
SEQRES   3 B  335  GLU SER HIS VAL VAL GLU TRP GLY ASN GLN ASP ASP TYR          
SEQRES   4 B  335  GLN LEU VAL ARG LYS LEU GLY ARG GLY LYS TYR SER GLU          
SEQRES   5 B  335  VAL PHE GLU ALA ILE ASN ILE THR ASN ASN GLU LYS VAL          
SEQRES   6 B  335  VAL VAL LYS ILE LEU LYS PRO VAL LYS LYS LYS LYS ILE          
SEQRES   7 B  335  LYS ARG GLU ILE LYS ILE LEU GLU ASN LEU ARG GLY GLY          
SEQRES   8 B  335  PRO ASN ILE ILE THR LEU ALA ASP ILE VAL LYS ASP PRO          
SEQRES   9 B  335  VAL SER ARG THR PRO ALA LEU VAL PHE GLU HIS VAL ASN          
SEQRES  10 B  335  ASN THR ASP PHE LYS GLN LEU TYR GLN THR LEU THR ASP          
SEQRES  11 B  335  TYR ASP ILE ARG PHE TYR MET TYR GLU ILE LEU LYS ALA          
SEQRES  12 B  335  LEU ASP TYR CYS HIS SER MET GLY ILE MET HIS ARG ASP          
SEQRES  13 B  335  VAL LYS PRO HIS ASN VAL MET ILE ASP HIS GLU HIS ARG          
SEQRES  14 B  335  LYS LEU ARG LEU ILE ASP TRP GLY LEU ALA GLU PHE TYR          
SEQRES  15 B  335  HIS PRO GLY GLN GLU TYR ASN VAL ARG VAL ALA SER ARG          
SEQRES  16 B  335  TYR PHE LYS GLY PRO GLU LEU LEU VAL ASP TYR GLN MET          
SEQRES  17 B  335  TYR ASP TYR SER LEU ASP MET TRP SER LEU GLY CYS MET          
SEQRES  18 B  335  LEU ALA SER MET ILE PHE ARG LYS GLU PRO PHE PHE HIS          
SEQRES  19 B  335  GLY HIS ASP ASN TYR ASP GLN LEU VAL ARG ILE ALA LYS          
SEQRES  20 B  335  VAL LEU GLY THR GLU ASP LEU TYR ASP TYR ILE ASP LYS          
SEQRES  21 B  335  TYR ASN ILE GLU LEU ASP PRO ARG PHE ASN ASP ILE LEU          
SEQRES  22 B  335  GLY ARG HIS SER ARG LYS ARG TRP GLU ARG PHE VAL HIS          
SEQRES  23 B  335  SER GLU ASN GLN HIS LEU VAL SER PRO GLU ALA LEU ASP          
SEQRES  24 B  335  PHE LEU ASP LYS LEU LEU ARG TYR ASP HIS GLN SER ARG          
SEQRES  25 B  335  LEU THR ALA ARG GLU ALA MET GLU HIS PRO TYR PHE TYR          
SEQRES  26 B  335  THR VAL VAL LYS ASP GLN ALA ARG MET GLY                      
SEQRES   1 C  335  MET SER GLY PRO VAL PRO SER ARG ALA ARG VAL TYR THR          
SEQRES   2 C  335  ASP VAL ASN THR HIS ARG PRO ARG GLU TYR TRP ASP TYR          
SEQRES   3 C  335  GLU SER HIS VAL VAL GLU TRP GLY ASN GLN ASP ASP TYR          
SEQRES   4 C  335  GLN LEU VAL ARG LYS LEU GLY ARG GLY LYS TYR SER GLU          
SEQRES   5 C  335  VAL PHE GLU ALA ILE ASN ILE THR ASN ASN GLU LYS VAL          
SEQRES   6 C  335  VAL VAL LYS ILE LEU LYS PRO VAL LYS LYS LYS LYS ILE          
SEQRES   7 C  335  LYS ARG GLU ILE LYS ILE LEU GLU ASN LEU ARG GLY GLY          
SEQRES   8 C  335  PRO ASN ILE ILE THR LEU ALA ASP ILE VAL LYS ASP PRO          
SEQRES   9 C  335  VAL SER ARG THR PRO ALA LEU VAL PHE GLU HIS VAL ASN          
SEQRES  10 C  335  ASN THR ASP PHE LYS GLN LEU TYR GLN THR LEU THR ASP          
SEQRES  11 C  335  TYR ASP ILE ARG PHE TYR MET TYR GLU ILE LEU LYS ALA          
SEQRES  12 C  335  LEU ASP TYR CYS HIS SER MET GLY ILE MET HIS ARG ASP          
SEQRES  13 C  335  VAL LYS PRO HIS ASN VAL MET ILE ASP HIS GLU HIS ARG          
SEQRES  14 C  335  LYS LEU ARG LEU ILE ASP TRP GLY LEU ALA GLU PHE TYR          
SEQRES  15 C  335  HIS PRO GLY GLN GLU TYR ASN VAL ARG VAL ALA SER ARG          
SEQRES  16 C  335  TYR PHE LYS GLY PRO GLU LEU LEU VAL ASP TYR GLN MET          
SEQRES  17 C  335  TYR ASP TYR SER LEU ASP MET TRP SER LEU GLY CYS MET          
SEQRES  18 C  335  LEU ALA SER MET ILE PHE ARG LYS GLU PRO PHE PHE HIS          
SEQRES  19 C  335  GLY HIS ASP ASN TYR ASP GLN LEU VAL ARG ILE ALA LYS          
SEQRES  20 C  335  VAL LEU GLY THR GLU ASP LEU TYR ASP TYR ILE ASP LYS          
SEQRES  21 C  335  TYR ASN ILE GLU LEU ASP PRO ARG PHE ASN ASP ILE LEU          
SEQRES  22 C  335  GLY ARG HIS SER ARG LYS ARG TRP GLU ARG PHE VAL HIS          
SEQRES  23 C  335  SER GLU ASN GLN HIS LEU VAL SER PRO GLU ALA LEU ASP          
SEQRES  24 C  335  PHE LEU ASP LYS LEU LEU ARG TYR ASP HIS GLN SER ARG          
SEQRES  25 C  335  LEU THR ALA ARG GLU ALA MET GLU HIS PRO TYR PHE TYR          
SEQRES  26 C  335  THR VAL VAL LYS ASP GLN ALA ARG MET GLY                      
SEQRES   1 D   13  GLY CYS ARG LEU TYR GLY PHE LYS ILE HIS GLY CYS GLY          
SEQRES   1 E   13  GLY CYS ARG LEU TYR GLY PHE LYS ILE HIS GLY CYS GLY          
SEQRES   1 F   13  GLY CYS ARG LEU TYR GLY PHE LYS ILE HIS GLY CYS GLY          
SEQRES   1 G   13  GLY CYS ARG LEU TYR GLY PHE LYS ILE HIS GLY CYS GLY          
HETNAM     GOL GLYCEROL                                                         
HETNAM      CL CHLORIDE ION                                                     
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   8  GOL    9(C3 H8 O3)                                                  
FORMUL  13   CL    3(CL 1-)                                                     
FORMUL  20  HOH   *462(H2 O)                                                    
HELIX    1   1 PRO A   20  ASP A   25  1                                   6    
HELIX    2   2 TYR A   26  HIS A   29  5                                   4    
HELIX    3   3 ASN A   35  ASP A   37  5                                   3    
HELIX    4   4 LYS A   74  ARG A   89  1                                  16    
HELIX    5   5 ASP A  120  TYR A  125  1                                   6    
HELIX    6   6 GLN A  126  LEU A  128  5                                   3    
HELIX    7   7 THR A  129  MET A  150  1                                  22    
HELIX    8   8 LYS A  158  HIS A  160  5                                   3    
HELIX    9   9 SER A  194  LYS A  198  5                                   5    
HELIX   10  10 GLY A  199  VAL A  204  1                                   6    
HELIX   11  11 TYR A  211  PHE A  227  1                                  17    
HELIX   12  12 ASP A  237  GLY A  250  1                                  14    
HELIX   13  13 GLY A  250  TYR A  261  1                                  12    
HELIX   14  14 ASP A  266  ARG A  268  5                                   3    
HELIX   15  15 PHE A  269  GLY A  274  1                                   6    
HELIX   16  16 ARG A  280  VAL A  285  5                                   6    
HELIX   17  17 ASN A  289  VAL A  293  5                                   5    
HELIX   18  18 SER A  294  LYS A  303  1                                  10    
HELIX   19  19 ASP A  308  ARG A  312  5                                   5    
HELIX   20  20 THR A  314  GLU A  320  1                                   7    
HELIX   21  21 HIS A  321  TYR A  323  5                                   3    
HELIX   22  22 PHE A  324  ALA A  332  1                                   9    
HELIX   23  23 PRO B   20  ASP B   25  1                                   6    
HELIX   24  24 TYR B   26  HIS B   29  5                                   4    
HELIX   25  25 ASN B   35  ASP B   37  5                                   3    
HELIX   26  26 LYS B   74  ARG B   89  1                                  16    
HELIX   27  27 ASP B  120  TYR B  125  1                                   6    
HELIX   28  28 GLN B  126  LEU B  128  5                                   3    
HELIX   29  29 THR B  129  MET B  150  1                                  22    
HELIX   30  30 LYS B  158  HIS B  160  5                                   3    
HELIX   31  31 SER B  194  LYS B  198  5                                   5    
HELIX   32  32 GLY B  199  VAL B  204  1                                   6    
HELIX   33  33 TYR B  211  ARG B  228  1                                  18    
HELIX   34  34 ASP B  237  GLY B  250  1                                  14    
HELIX   35  35 GLY B  250  TYR B  261  1                                  12    
HELIX   36  36 ASP B  266  ASN B  270  5                                   5    
HELIX   37  37 ARG B  280  VAL B  285  5                                   6    
HELIX   38  38 ASN B  289  VAL B  293  5                                   5    
HELIX   39  39 SER B  294  LYS B  303  1                                  10    
HELIX   40  40 ASP B  308  ARG B  312  5                                   5    
HELIX   41  41 THR B  314  GLU B  320  1                                   7    
HELIX   42  42 HIS B  321  TYR B  323  5                                   3    
HELIX   43  43 PHE B  324  ASP B  330  1                                   7    
HELIX   44  44 PRO C   20  ASP C   25  1                                   6    
HELIX   45  45 TYR C   26  HIS C   29  5                                   4    
HELIX   46  46 ASN C   35  ASP C   37  5                                   3    
HELIX   47  47 LYS C   74  ARG C   89  1                                  16    
HELIX   48  48 ASP C  120  TYR C  125  1                                   6    
HELIX   49  49 GLN C  126  LEU C  128  5                                   3    
HELIX   50  50 THR C  129  MET C  150  1                                  22    
HELIX   51  51 LYS C  158  HIS C  160  5                                   3    
HELIX   52  52 SER C  194  LYS C  198  5                                   5    
HELIX   53  53 GLY C  199  VAL C  204  1                                   6    
HELIX   54  54 TYR C  211  ARG C  228  1                                  18    
HELIX   55  55 ASP C  237  GLY C  250  1                                  14    
HELIX   56  56 GLY C  250  TYR C  261  1                                  12    
HELIX   57  57 ASP C  266  ASN C  270  5                                   5    
HELIX   58  58 ARG C  280  VAL C  285  5                                   6    
HELIX   59  59 ASN C  289  VAL C  293  5                                   5    
HELIX   60  60 SER C  294  LYS C  303  1                                  10    
HELIX   61  61 THR C  314  GLU C  320  1                                   7    
HELIX   62  62 HIS C  321  TYR C  323  5                                   3    
HELIX   63  63 PHE C  324  ARG C  333  1                                  10    
HELIX   64  64 GLY G  184  TYR G  188  5                                   5    
SHEET    1   A 7 LEU A  97  LYS A 102  0                                        
SHEET    2   A 7 PRO A 109  GLU A 114 -1  O  ALA A 110   N  VAL A 101           
SHEET    3   A 7 LYS A  64  ILE A  69 -1  N  VAL A  66   O  PHE A 113           
SHEET    4   A 7 GLU A  52  ASN A  58 -1  N  ALA A  56   O  VAL A  65           
SHEET    5   A 7 TYR A  39  GLY A  46 -1  N  ARG A  43   O  GLU A  55           
SHEET    6   A 7 PHE D 190  ILE D 192  1  O  LYS D 191   N  LEU A  41           
SHEET    7   A 7 ARG D 186  LEU D 187 -1  N  LEU D 187   O  PHE D 190           
SHEET    1   B 2 ILE A 152  MET A 153  0                                        
SHEET    2   B 2 GLU A 180  PHE A 181 -1  O  GLU A 180   N  MET A 153           
SHEET    1   C 2 VAL A 162  ASP A 165  0                                        
SHEET    2   C 2 LYS A 170  LEU A 173 -1  O  ARG A 172   N  MET A 163           
SHEET    1   D 7 LEU B  97  LYS B 102  0                                        
SHEET    2   D 7 PRO B 109  GLU B 114 -1  O  VAL B 112   N  ASP B  99           
SHEET    3   D 7 LYS B  64  ILE B  69 -1  N  VAL B  66   O  PHE B 113           
SHEET    4   D 7 VAL B  53  ASN B  58 -1  N  ALA B  56   O  VAL B  65           
SHEET    5   D 7 TYR B  39  LYS B  44 -1  N  ARG B  43   O  GLU B  55           
SHEET    6   D 7 PHE E 190  ILE E 192  1  O  LYS E 191   N  LEU B  41           
SHEET    7   D 7 ARG E 186  LEU E 187 -1  N  LEU E 187   O  PHE E 190           
SHEET    1   E 2 ILE B 152  MET B 153  0                                        
SHEET    2   E 2 GLU B 180  PHE B 181 -1  O  GLU B 180   N  MET B 153           
SHEET    1   F 2 VAL B 162  ASP B 165  0                                        
SHEET    2   F 2 LYS B 170  LEU B 173 -1  O  ARG B 172   N  MET B 163           
SHEET    1   G 7 LEU C  97  LYS C 102  0                                        
SHEET    2   G 7 PRO C 109  GLU C 114 -1  O  VAL C 112   N  ALA C  98           
SHEET    3   G 7 LYS C  64  LEU C  70 -1  N  VAL C  66   O  PHE C 113           
SHEET    4   G 7 SER C  51  ASN C  58 -1  N  PHE C  54   O  VAL C  67           
SHEET    5   G 7 TYR C  39  GLY C  46 -1  N  ARG C  43   O  GLU C  55           
SHEET    6   G 7 PHE F 190  ILE F 192  1  O  LYS F 191   N  LEU C  41           
SHEET    7   G 7 ARG F 186  LEU F 187 -1  N  LEU F 187   O  PHE F 190           
SHEET    1   H 2 ILE C 152  MET C 153  0                                        
SHEET    2   H 2 GLU C 180  PHE C 181 -1  O  GLU C 180   N  MET C 153           
SHEET    1   I 2 VAL C 162  ASP C 165  0                                        
SHEET    2   I 2 LYS C 170  LEU C 173 -1  O  ARG C 172   N  MET C 163           
SSBOND   1 CYS D  185    CYS D  195                          1555   1555  2.03  
SSBOND   2 CYS E  185    CYS E  195                          1555   1555  2.03  
SSBOND   3 CYS F  185    CYS F  195                          1555   1555  2.03  
SSBOND   4 CYS G  185    CYS G  195                          1555   1555  2.03  
CISPEP   1 LYS A   71    PRO A   72          1        10.33                     
CISPEP   2 GLU A  230    PRO A  231          1        -5.29                     
CISPEP   3 LYS B   71    PRO B   72          1        -4.04                     
CISPEP   4 GLU B  230    PRO B  231          1        -5.32                     
CISPEP   5 GLU C  230    PRO C  231          1        -4.89                     
SITE     1 AC1  5 LYS A  68  PHE A 113  ILE A 174  ASP A 175                    
SITE     2 AC1  5 HOH A 503                                                     
SITE     1 AC2  9 ASN A  16  THR A  17  ARG A  43  LYS A  44                    
SITE     2 AC2  9 LEU A  45  GLY A  46  HIS A 183  HOH A 573                    
SITE     3 AC2  9 HOH A 654                                                     
SITE     1 AC3  6 TYR A  39  ALA A  98  HOH A 590  HOH A 593                    
SITE     2 AC3  6 HOH A 607  HOH B 510                                          
SITE     1 AC4  6 ILE A  94  ILE A  95  THR A  96  GLU A 114                    
SITE     2 AC4  6 HIS A 115  ARG A 172                                          
SITE     1 AC5  3 ASP A 156  LYS A 158  SER A 194                               
SITE     1 AC6  4 HIS A 148  ALA A 315  HOH A 517  HOH A 541                    
SITE     1 AC7  3 ARG A  80  ARG A 155  HOH A 528                               
SITE     1 AC8 10 ARG B  47  VAL B  53  VAL B  66  LYS B  68                    
SITE     2 AC8 10 ILE B  95  PHE B 113  ILE B 174  ASP B 175                    
SITE     3 AC8 10 HOH B 514  HOH B 600                                          
SITE     1 AC9  4 LYS C  49  ASP C 156  LYS C 158  SER C 194                    
SITE     1 BC1  3 LYS C  68  ILE C 174  ASP C 175                               
SITE     1 BC2  4 SER B 194  HOH B 570  GLU C 252  ASP C 256                    
SITE     1 BC3  5 HIS C 148  THR C 314  ALA C 315  HOH C 520                    
SITE     2 BC3  5 HOH C 544                                                     
SITE     1 BC4 20 PRO A   6  GLN A  36  TYR A  39  GLN A  40                    
SITE     2 BC4 20 LEU A  41  GLU A  52  PHE A  54  VAL A  67                    
SITE     3 BC4 20 ILE A  69  LYS A  71  VAL A 101  ASP A 103                    
SITE     4 BC4 20 HOH A 554  HOH A 591  TYR C 146  ASP C 271                    
SITE     5 BC4 20 HOH D 203  HOH D 204  HOH D 205  HOH D 206                    
SITE     1 BC5 16 GLN B  36  TYR B  39  GLN B  40  LEU B  41                    
SITE     2 BC5 16 GLU B  52  ILE B  57  ILE B  69  VAL B 101                    
SITE     3 BC5 16 ASP B 103  HOH B 509  PRO C 322  TYR C 325                    
SITE     4 BC5 16 LYS C 329  HOH E 203  HOH E 204  LEU G 187                    
SITE     1 BC6  8 GLN C  36  TYR C  39  GLN C  40  LEU C  41                    
SITE     2 BC6  8 GLU C  52  VAL C 101  ASP C 103  THR C 108                    
SITE     1 BC7 11 VAL B  42  ARG B  43  LYS B  44  PHE B  54                    
SITE     2 BC7 11 ARG C 280  GLU C 282  PRO C 295  ASP C 299                    
SITE     3 BC7 11 PRO C 322  ILE E 192  HOH G 201                               
CRYST1   77.380  105.420  152.110  90.00  90.00  90.00 P 21 21 21   16          
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      0.012923  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009486  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006574        0.00000                         
MODEL        1                                                                  
ATOM      1  N   GLY G 184      14.909 -31.920  51.679  1.00 99.08           N  
ANISOU    1  N   GLY G 184    11998  11545  14101  -3682  -1603    -13       N  
ATOM      2  CA  GLY G 184      14.953 -32.521  52.999  1.00 96.79           C  
ANISOU    2  CA  GLY G 184    11933  11408  13435  -3455  -2053   -259       C  
ATOM      3  C   GLY G 184      14.115 -33.782  53.085  1.00 85.88           C  
ANISOU    3  C   GLY G 184    10734  10238  11659  -2846  -1799   -160       C  
ATOM      4  O   GLY G 184      13.078 -33.893  52.433  1.00 81.51           O  
ANISOU    4  O   GLY G 184    10432   9509  11029  -2604  -1345     -8       O  
ATOM      5  N   CYS G 185      14.565 -34.733  53.897  1.00 81.70           N  
ANISOU    5  N   CYS G 185    10080  10054  10907  -2615  -2146   -225       N  
ATOM      6  CA  CYS G 185      13.874 -36.009  54.039  1.00 77.28           C  
ANISOU    6  CA  CYS G 185     9663   9696  10005  -2075  -1996    -89       C  
ATOM      7  C   CYS G 185      12.556 -35.860  54.792  1.00 71.03           C  
ANISOU    7  C   CYS G 185     9581   8610   8797  -1815  -1859   -171       C  
ATOM      8  O   CYS G 185      11.666 -36.702  54.675  1.00 66.35           O  
ANISOU    8  O   CYS G 185     9129   8055   8024  -1431  -1611     50       O  
ATOM      9  CB  CYS G 185      14.770 -37.031  54.745  1.00 79.84           C  
ANISOU    9  CB  CYS G 185     9683  10455  10196  -1908  -2439   -137       C  
ATOM     10  SG  CYS G 185      15.280 -36.557  56.416  1.00113.14           S  
ANISOU   10  SG  CYS G 185    14249  14602  14139  -2069  -3115   -544       S  
ATOM     11  N   ARG G 186      12.438 -34.786  55.566  1.00 71.62           N  
ANISOU   11  N   ARG G 186    10106   8378   8727  -2004  -2039   -455       N  
ATOM     12  CA  ARG G 186      11.238 -34.529  56.356  1.00 78.82           C  
ANISOU   12  CA  ARG G 186    11717   9036   9195  -1683  -1866   -524       C  
ATOM     13  C   ARG G 186      10.049 -34.172  55.467  1.00 76.09           C  
ANISOU   13  C   ARG G 186    11523   8413   8975  -1587  -1293   -301       C  
ATOM     14  O   ARG G 186       8.900 -34.189  55.909  1.00 75.36           O  
ANISOU   14  O   ARG G 186    11860   8184   8587  -1236  -1017   -207       O  
ATOM     15  CB  ARG G 186      11.500 -33.400  57.353  1.00 85.48           C  
ANISOU   15  CB  ARG G 186    13095   9574   9808  -1851  -2258   -919       C  
ATOM     16  CG  ARG G 186      11.788 -32.062  56.696  1.00 91.44           C  
ANISOU   16  CG  ARG G 186    13856   9951  10938  -2346  -2290  -1044       C  
ATOM     17  CD  ARG G 186      12.438 -31.090  57.665  1.00103.22           C  
ANISOU   17  CD  ARG G 186    15785  11142  12292  -2604  -2935  -1444       C  
ATOM     18  NE  ARG G 186      12.688 -29.792  57.043  1.00107.68           N  
ANISOU   18  NE  ARG G 186    16386  11287  13241  -3116  -3019  -1528       N  
ATOM     19  CZ  ARG G 186      13.745 -29.516  56.287  1.00111.66           C  
ANISOU   19  CZ  ARG G 186    16224  11854  14349  -3683  -3214  -1410       C  
ATOM     20  NH1 ARG G 186      14.658 -30.448  56.050  1.00111.71           N  
ANISOU   20  NH1 ARG G 186    15468  12352  14624  -3758  -3323  -1221       N  
ATOM     21  NH2 ARG G 186      13.889 -28.306  55.762  1.00116.27           N  
ANISOU   21  NH2 ARG G 186    16896  12014  15269  -4154  -3283  -1445       N  
ATOM     22  N   LEU G 187      10.335 -33.853  54.209  1.00 74.01           N  
ANISOU   22  N   LEU G 187    10891   8074   9157  -1875  -1107   -181       N  
ATOM     23  CA  LEU G 187       9.303 -33.446  53.265  1.00 72.54           C  
ANISOU   23  CA  LEU G 187    10853   7580   9130  -1819   -630     10       C  
ATOM     24  C   LEU G 187       8.745 -34.622  52.467  1.00 66.28           C  
ANISOU   24  C   LEU G 187     9816   6933   8435  -1506   -382    385       C  
ATOM     25  O   LEU G 187       7.872 -34.440  51.620  1.00 69.60           O  
ANISOU   25  O   LEU G 187    10340   7088   9017  -1430    -50    580       O  
ATOM     26  CB  LEU G 187       9.855 -32.387  52.307  1.00 70.95           C  
ANISOU   26  CB  LEU G 187    10489   7145   9324  -2281   -566    -49       C  
ATOM     27  CG  LEU G 187      10.146 -31.012  52.910  1.00 78.41           C  
ANISOU   27  CG  LEU G 187    11802   7753  10237  -2632   -827   -383       C  
ATOM     28  CD1 LEU G 187      10.962 -30.168  51.949  1.00 81.95           C  
ANISOU   28  CD1 LEU G 187    11922   8055  11161  -3166   -839   -349       C  
ATOM     29  CD2 LEU G 187       8.847 -30.308  53.268  1.00 76.45           C  
ANISOU   29  CD2 LEU G 187    12236   7109   9703  -2378   -579   -471       C  
ATOM     30  N   TYR G 188       9.241 -35.825  52.740  1.00 63.02           N  
ANISOU   30  N   TYR G 188     9128   6896   7922  -1316   -607    481       N  
ATOM     31  CA  TYR G 188       8.852 -36.994  51.952  1.00 62.09           C  
ANISOU   31  CA  TYR G 188     8826   6871   7896  -1024   -505    822       C  
ATOM     32  C   TYR G 188       8.343 -38.170  52.785  1.00 68.67           C  
ANISOU   32  C   TYR G 188     9759   7885   8448   -661   -656    999       C  
ATOM     33  O   TYR G 188       7.717 -39.088  52.255  1.00 75.12           O  
ANISOU   33  O   TYR G 188    10546   8655   9339   -415   -620   1325       O  
ATOM     34  CB  TYR G 188      10.006 -37.436  51.049  1.00 62.91           C  
ANISOU   34  CB  TYR G 188     8463   7226   8214  -1093   -603    863       C  
ATOM     35  CG  TYR G 188      10.380 -36.403  50.013  1.00 66.96           C  
ANISOU   35  CG  TYR G 188     8847   7552   9044  -1406   -359    836       C  
ATOM     36  CD1 TYR G 188       9.629 -36.252  48.855  1.00 65.08           C  
ANISOU   36  CD1 TYR G 188     8762   6999   8966  -1311    -37   1040       C  
ATOM     37  CD2 TYR G 188      11.479 -35.575  50.194  1.00 69.48           C  
ANISOU   37  CD2 TYR G 188     8897   7977   9523  -1811   -489    641       C  
ATOM     38  CE1 TYR G 188       9.964 -35.307  47.905  1.00 64.48           C  
ANISOU   38  CE1 TYR G 188     8609   6742   9147  -1579    209   1041       C  
ATOM     39  CE2 TYR G 188      11.823 -34.628  49.250  1.00 71.81           C  
ANISOU   39  CE2 TYR G 188     9053   8096  10135  -2128   -253    687       C  
ATOM     40  CZ  TYR G 188      11.061 -34.499  48.108  1.00 69.50           C  
ANISOU   40  CZ  TYR G 188     8951   7514   9942  -1994    127    883       C  
ATOM     41  OH  TYR G 188      11.399 -33.557  47.165  1.00 71.94           O  
ANISOU   41  OH  TYR G 188     9162   7639  10535  -2290    384    952       O  
ATOM     42  N   GLY G 189       8.613 -38.142  54.085  1.00 71.93           N  
ANISOU   42  N   GLY G 189    10328   8465   8537   -629   -868    801       N  
ATOM     43  CA  GLY G 189       8.117 -39.166  54.986  1.00 74.33           C  
ANISOU   43  CA  GLY G 189    10772   8936   8535   -288   -974    993       C  
ATOM     44  C   GLY G 189       8.741 -40.536  54.794  1.00 71.23           C  
ANISOU   44  C   GLY G 189    10076   8845   8142   -128  -1287   1133       C  
ATOM     45  O   GLY G 189       8.073 -41.557  54.958  1.00 67.81           O  
ANISOU   45  O   GLY G 189     9707   8434   7623    144  -1325   1460       O  
ATOM     46  N   PHE G 190      10.024 -40.562  54.448  1.00 71.23           N  
ANISOU   46  N   PHE G 190     9736   9073   8256   -285  -1524    922       N  
ATOM     47  CA  PHE G 190      10.746 -41.824  54.326  1.00 66.80           C  
ANISOU   47  CA  PHE G 190     8906   8831   7644    -69  -1842   1010       C  
ATOM     48  C   PHE G 190      11.855 -41.942  55.367  1.00 70.97           C  
ANISOU   48  C   PHE G 190     9312   9691   7961   -120  -2249    719       C  
ATOM     49  O   PHE G 190      12.569 -40.978  55.644  1.00 66.99           O  
ANISOU   49  O   PHE G 190     8710   9202   7542   -430  -2345    430       O  
ATOM     50  CB  PHE G 190      11.307 -42.005  52.913  1.00 64.26           C  
ANISOU   50  CB  PHE G 190     8246   8547   7623    -59  -1761   1103       C  
ATOM     51  CG  PHE G 190      10.259 -42.308  51.879  1.00 64.57           C  
ANISOU   51  CG  PHE G 190     8472   8253   7810    115  -1533   1421       C  
ATOM     52  CD1 PHE G 190       9.749 -43.588  51.744  1.00 60.71           C  
ANISOU   52  CD1 PHE G 190     8116   7722   7228    459  -1747   1709       C  
ATOM     53  CD2 PHE G 190       9.783 -41.312  51.042  1.00 63.98           C  
ANISOU   53  CD2 PHE G 190     8471   7857   7981    -77  -1176   1439       C  
ATOM     54  CE1 PHE G 190       8.783 -43.869  50.794  1.00 56.02           C  
ANISOU   54  CE1 PHE G 190     7722   6752   6813    598  -1659   2013       C  
ATOM     55  CE2 PHE G 190       8.819 -41.588  50.089  1.00 60.24           C  
ANISOU   55  CE2 PHE G 190     8197   7034   7656     89  -1042   1725       C  
ATOM     56  CZ  PHE G 190       8.318 -42.867  49.966  1.00 57.20           C  
ANISOU   56  CZ  PHE G 190     7939   6589   7205    422  -1309   2013       C  
ATOM     57  N   LYS G 191      11.989 -43.135  55.939  1.00 75.60           N  
ANISOU   57  N   LYS G 191     9927  10503   8296    175  -2549    812       N  
ATOM     58  CA  LYS G 191      12.963 -43.394  56.996  1.00 82.22           C  
ANISOU   58  CA  LYS G 191    10706  11638   8895    191  -2995    554       C  
ATOM     59  C   LYS G 191      14.385 -43.557  56.468  1.00 86.34           C  
ANISOU   59  C   LYS G 191    10664  12483   9659    109  -3250    426       C  
ATOM     60  O   LYS G 191      14.970 -44.636  56.566  1.00 89.66           O  
ANISOU   60  O   LYS G 191    10909  13191   9965    381  -3554    473       O  
ATOM     61  CB  LYS G 191      12.567 -44.649  57.775  1.00 83.01           C  
ANISOU   61  CB  LYS G 191    11059  11852   8629    557  -3217    737       C  
ATOM     62  CG  LYS G 191      11.579 -44.416  58.902  1.00 82.75           C  
ANISOU   62  CG  LYS G 191    11550  11655   8237    656  -3078    799       C  
ATOM     63  CD  LYS G 191      12.251 -44.645  60.245  1.00 81.85           C  
ANISOU   63  CD  LYS G 191    11647  11747   7706    767  -3504    543       C  
ATOM     64  CE  LYS G 191      12.957 -45.993  60.287  1.00 75.65           C  
ANISOU   64  CE  LYS G 191    10645  11259   6839    991  -3928    613       C  
ATOM     65  NZ  LYS G 191      13.738 -46.179  61.541  1.00 75.39           N  
ANISOU   65  NZ  LYS G 191    10734  11406   6505   1035  -4274    334       N  
ATOM     66  N   ILE G 192      14.941 -42.483  55.920  1.00 85.27           N  
ANISOU   66  N   ILE G 192    10229  12303   9868   -252  -3120    300       N  
ATOM     67  CA  ILE G 192      16.305 -42.506  55.406  1.00 85.03           C  
ANISOU   67  CA  ILE G 192     9558  12608  10142   -356  -3287    265       C  
ATOM     68  C   ILE G 192      16.891 -41.093  55.444  1.00 84.37           C  
ANISOU   68  C   ILE G 192     9252  12411  10394   -891  -3313     82       C  
ATOM     69  O   ILE G 192      16.150 -40.116  55.561  1.00 80.35           O  
ANISOU   69  O   ILE G 192     9128  11521   9878  -1129  -3119     -6       O  
ATOM     70  CB  ILE G 192      16.358 -43.100  53.974  1.00 84.44           C  
ANISOU   70  CB  ILE G 192     9202  12635  10247    -85  -2963    559       C  
ATOM     71  CG1 ILE G 192      17.795 -43.450  53.569  1.00 96.22           C  
ANISOU   71  CG1 ILE G 192    10014  14592  11953      3  -3119    598       C  
ATOM     72  CG2 ILE G 192      15.720 -42.149  52.974  1.00 76.21           C  
ANISOU   72  CG2 ILE G 192     8245  11253   9458   -304  -2465    671       C  
ATOM     73  CD1 ILE G 192      18.561 -44.240  54.617  1.00101.52           C  
ANISOU   73  CD1 ILE G 192    10552  15600  12421    171  -3674    448       C  
ATOM     74  N   HIS G 193      18.217 -41.000  55.374  1.00 87.49           N  
ANISOU   74  N   HIS G 193     9021  13123  11096  -1072  -3590     53       N  
ATOM     75  CA  HIS G 193      18.934 -39.725  55.415  1.00 90.40           C  
ANISOU   75  CA  HIS G 193     9079  13386  11884  -1641  -3739    -54       C  
ATOM     76  C   HIS G 193      18.721 -38.971  56.726  1.00 92.21           C  
ANISOU   76  C   HIS G 193     9853  13286  11897  -1903  -4194   -410       C  
ATOM     77  O   HIS G 193      18.811 -37.744  56.766  1.00 97.58           O  
ANISOU   77  O   HIS G 193    10606  13649  12820  -2365  -4278   -526       O  
ATOM     78  CB  HIS G 193      18.579 -38.841  54.212  1.00 87.72           C  
ANISOU   78  CB  HIS G 193     8640  12813  11878  -1889  -3183    138       C  
ATOM     79  CG  HIS G 193      19.153 -39.321  52.915  1.00 91.02           C  
ANISOU   79  CG  HIS G 193     8448  13567  12570  -1686  -2799    487       C  
ATOM     80  ND1 HIS G 193      19.649 -40.596  52.747  1.00 94.91           N  
ANISOU   80  ND1 HIS G 193     8651  14493  12918  -1186  -2868    619       N  
ATOM     81  CD2 HIS G 193      19.318 -38.694  51.726  1.00 88.38           C  
ANISOU   81  CD2 HIS G 193     7794  13192  12593  -1854  -2331    740       C  
ATOM     82  CE1 HIS G 193      20.089 -40.736  51.509  1.00 91.41           C  
ANISOU   82  CE1 HIS G 193     7762  14269  12702  -1005  -2444    932       C  
ATOM     83  NE2 HIS G 193      19.898 -39.596  50.868  1.00 87.85           N  
ANISOU   83  NE2 HIS G 193     7276  13546  12558  -1407  -2093   1025       N  
ATOM     84  N   GLY G 194      18.437 -39.710  57.794  1.00 89.87           N  
ANISOU   84  N   GLY G 194     9999  13038  11109  -1570  -4505   -573       N  
ATOM     85  CA  GLY G 194      18.326 -39.121  59.117  1.00 94.03           C  
ANISOU   85  CA  GLY G 194    11124  13282  11321  -1682  -4979   -919       C  
ATOM     86  C   GLY G 194      16.923 -39.095  59.696  1.00 89.58           C  
ANISOU   86  C   GLY G 194    11424  12414  10200  -1368  -4683   -974       C  
ATOM     87  O   GLY G 194      16.748 -38.861  60.892  1.00 90.43           O  
ANISOU   87  O   GLY G 194    12144  12340   9877  -1261  -5030  -1234       O  
ATOM     88  N   CYS G 195      15.921 -39.334  58.856  1.00 83.50           N  
ANISOU   88  N   CYS G 195    10713  11581   9433  -1186  -4051   -702       N  
ATOM     89  CA  CYS G 195      14.531 -39.271  59.300  1.00 85.35           C  
ANISOU   89  CA  CYS G 195    11641  11549   9241   -897  -3695   -649       C  
ATOM     90  C   CYS G 195      14.071 -40.548  59.993  1.00 88.31           C  
ANISOU   90  C   CYS G 195    12258  12129   9168   -414  -3732   -498       C  
ATOM     91  O   CYS G 195      14.419 -41.653  59.578  1.00 89.84           O  
ANISOU   91  O   CYS G 195    12067  12621   9448   -245  -3799   -309       O  
ATOM     92  CB  CYS G 195      13.602 -38.941  58.130  1.00 81.46           C  
ANISOU   92  CB  CYS G 195    11101  10853   8999   -934  -3067   -389       C  
ATOM     93  SG  CYS G 195      13.741 -37.237  57.556  1.00117.23           S  
ANISOU   93  SG  CYS G 195    15640  14997  13905  -1456  -2952   -564       S  
ATOM     94  N   GLY G 196      13.283 -40.382  61.051  1.00 91.95           N  
ANISOU   94  N   GLY G 196    13392  12418   9128   -160  -3682   -558       N  
ATOM     95  CA  GLY G 196      12.754 -41.503  61.804  1.00 92.88           C  
ANISOU   95  CA  GLY G 196    13791  12698   8799    289  -3671   -352       C  
ATOM     96  C   GLY G 196      13.836 -42.311  62.494  1.00102.46           C  
ANISOU   96  C   GLY G 196    14881  14208   9841    380  -4285   -522       C  
ATOM     97  O   GLY G 196      14.594 -41.785  63.308  1.00110.63           O  
ANISOU   97  O   GLY G 196    16122  15195  10717    275  -4779   -891       O  
TER      98      GLY G 196                                                      
HETATM   99  O   HOH G 201      17.189 -42.640  58.844  1.00 75.25           O  
ENDMDL                                                                          
MASTER       14    0    0   64   33    0   34    6 9286    7    0   82          
END                                                                             
