HEADER    APOPTOSIS/PEPTIDE                       03-APR-03   XXXX              
TITLE     STRUCTURE AND FUNCTION ANALYSIS OF PEPTIDE ANTAGONISTS OF MELANOMA    
TITLE    2 INHIBITOR OF APOPTOSIS (ML-IAP)                                      
COMPND    Baculoviral IAP repeat-containing protein 7, AEVVAVKSE peptide        
KEYWDS    ZINC BINDING, PEPTIDE COMPLEX, APOPTOSIS INHIBITION, APOPTOSIS-       
KEYWDS   2 PEPTIDE COMPLEX                                                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.C.FRANKLIN, S.KADKHODAYAN, H.ACKERLY, D.ALEXANDRU, M.D.DISTEFANO,   
AUTHOR   2 L.O.ELLIOTT, J.A.FLYGARE, D.VUCIC, K.DESHAYES, W.J.FAIRBROTHER       
JRNL        AUTH   M.C.FRANKLIN, S.KADKHODAYAN, H.ACKERLY, D.ALEXANDRU,         
JRNL        AUTH 2 M.D.DISTEFANO, L.O.ELLIOTT, J.A.FLYGARE, G.MAUSISA,          
JRNL        AUTH 3 D.C.OKAWA, D.ONG, D.VUCIC, K.DESHAYES, W.J.FAIRBROTHER       
JRNL        TITL   STRUCTURE AND FUNCTION ANALYSIS OF PEPTIDE ANTAGONISTS OF    
JRNL        TITL 2 MELANOMA INHIBITOR OF APOPTOSIS (ML-IAP)                     
JRNL        REF    BIOCHEMISTRY                  V.  42  8223 2003              
JRNL        REFN   ASTM BICHAW  US ISSN 0006-2960                               
JRNL        PMID   12846571                                                     
JRNL        DOI    10.1021/BI034227T                                            
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   D.VUCIC, H.R.STENNICKE, M.T.PISABARRO, G.S.SALVESEN,         
REMARK   1  AUTH 2 V.M.DIXIT                                                    
REMARK   1  TITL   ML-IAP, A NOVEL INHIBITOR OF APOPTOSIS THAT IS               
REMARK   1  TITL 2 PREFERENTIALLY EXPRESSED IN HUMAN MELANOMAS                  
REMARK   1  REF    CURR.BIOL.                    V.  10  1359 2000              
REMARK   1  REFN   ASTM CUBLE2  UK ISSN 0960-9822                               
JRNL        DOI    10.1016/S0960-9822(00)00781-8                                
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   D.VUCIC, K.DESHAYES, H.ACKERLY, M.T.PISABARRO,               
REMARK   1  AUTH 2 S.KADKHODAYAN, W.J.FAIRBROTHER, V.M.DIXIT                    
REMARK   1  TITL   SMAC NEGATIVELY REGULATES THE ANTI-APOPTOTIC ACTIVITY OF     
REMARK   1  TITL 2 MELANOMA INHIBITOR OF APOPTOSIS (ML-IAP)                     
REMARK   1  REF    J.BIOL.CHEM.                  V. 277 12275 2002              
REMARK   1  REFN   ASTM JBCHA3  US ISSN 0021-9258                               
JRNL        DOI    10.1074/JBC.M112045200                                       
SEQRES   1 A  140  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 A  140  LEU VAL PRO ARG GLY SER HIS MET LEU GLU THR GLU GLU          
SEQRES   3 A  140  GLU GLU GLU GLU GLY ALA GLY ALA THR LEU SER ARG GLY          
SEQRES   4 A  140  PRO ALA PHE PRO GLY MET GLY SER GLU GLU LEU ARG LEU          
SEQRES   5 A  140  ALA SER PHE TYR ASP TRP PRO LEU THR ALA GLU VAL PRO          
SEQRES   6 A  140  PRO GLU LEU LEU ALA ALA ALA GLY PHE PHE HIS THR GLY          
SEQRES   7 A  140  HIS GLN ASP LYS VAL ARG CYS PHE PHE CYS TYR GLY GLY          
SEQRES   8 A  140  LEU GLN SER TRP LYS ARG GLY ASP ASP PRO TRP THR GLU          
SEQRES   9 A  140  HIS ALA LYS TRP PHE PRO SER CYS GLN PHE LEU LEU ARG          
SEQRES  10 A  140  SER LYS GLY ARG ASP PHE VAL HIS SER VAL GLN GLU THR          
SEQRES  11 A  140  HIS SER GLN LEU LEU GLY SER TRP ASP PRO                      
SEQRES   1 B  140  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 B  140  LEU VAL PRO ARG GLY SER HIS MET LEU GLU THR GLU GLU          
SEQRES   3 B  140  GLU GLU GLU GLU GLY ALA GLY ALA THR LEU SER ARG GLY          
SEQRES   4 B  140  PRO ALA PHE PRO GLY MET GLY SER GLU GLU LEU ARG LEU          
SEQRES   5 B  140  ALA SER PHE TYR ASP TRP PRO LEU THR ALA GLU VAL PRO          
SEQRES   6 B  140  PRO GLU LEU LEU ALA ALA ALA GLY PHE PHE HIS THR GLY          
SEQRES   7 B  140  HIS GLN ASP LYS VAL ARG CYS PHE PHE CYS TYR GLY GLY          
SEQRES   8 B  140  LEU GLN SER TRP LYS ARG GLY ASP ASP PRO TRP THR GLU          
SEQRES   9 B  140  HIS ALA LYS TRP PHE PRO SER CYS GLN PHE LEU LEU ARG          
SEQRES  10 B  140  SER LYS GLY ARG ASP PHE VAL HIS SER VAL GLN GLU THR          
SEQRES  11 B  140  HIS SER GLN LEU LEU GLY SER TRP ASP PRO                      
SEQRES   1 C  140  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 C  140  LEU VAL PRO ARG GLY SER HIS MET LEU GLU THR GLU GLU          
SEQRES   3 C  140  GLU GLU GLU GLU GLY ALA GLY ALA THR LEU SER ARG GLY          
SEQRES   4 C  140  PRO ALA PHE PRO GLY MET GLY SER GLU GLU LEU ARG LEU          
SEQRES   5 C  140  ALA SER PHE TYR ASP TRP PRO LEU THR ALA GLU VAL PRO          
SEQRES   6 C  140  PRO GLU LEU LEU ALA ALA ALA GLY PHE PHE HIS THR GLY          
SEQRES   7 C  140  HIS GLN ASP LYS VAL ARG CYS PHE PHE CYS TYR GLY GLY          
SEQRES   8 C  140  LEU GLN SER TRP LYS ARG GLY ASP ASP PRO TRP THR GLU          
SEQRES   9 C  140  HIS ALA LYS TRP PHE PRO SER CYS GLN PHE LEU LEU ARG          
SEQRES  10 C  140  SER LYS GLY ARG ASP PHE VAL HIS SER VAL GLN GLU THR          
SEQRES  11 C  140  HIS SER GLN LEU LEU GLY SER TRP ASP PRO                      
SEQRES   1 D  140  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 D  140  LEU VAL PRO ARG GLY SER HIS MET LEU GLU THR GLU GLU          
SEQRES   3 D  140  GLU GLU GLU GLU GLY ALA GLY ALA THR LEU SER ARG GLY          
SEQRES   4 D  140  PRO ALA PHE PRO GLY MET GLY SER GLU GLU LEU ARG LEU          
SEQRES   5 D  140  ALA SER PHE TYR ASP TRP PRO LEU THR ALA GLU VAL PRO          
SEQRES   6 D  140  PRO GLU LEU LEU ALA ALA ALA GLY PHE PHE HIS THR GLY          
SEQRES   7 D  140  HIS GLN ASP LYS VAL ARG CYS PHE PHE CYS TYR GLY GLY          
SEQRES   8 D  140  LEU GLN SER TRP LYS ARG GLY ASP ASP PRO TRP THR GLU          
SEQRES   9 D  140  HIS ALA LYS TRP PHE PRO SER CYS GLN PHE LEU LEU ARG          
SEQRES  10 D  140  SER LYS GLY ARG ASP PHE VAL HIS SER VAL GLN GLU THR          
SEQRES  11 D  140  HIS SER GLN LEU LEU GLY SER TRP ASP PRO                      
SEQRES   1 E  140  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 E  140  LEU VAL PRO ARG GLY SER HIS MET LEU GLU THR GLU GLU          
SEQRES   3 E  140  GLU GLU GLU GLU GLY ALA GLY ALA THR LEU SER ARG GLY          
SEQRES   4 E  140  PRO ALA PHE PRO GLY MET GLY SER GLU GLU LEU ARG LEU          
SEQRES   5 E  140  ALA SER PHE TYR ASP TRP PRO LEU THR ALA GLU VAL PRO          
SEQRES   6 E  140  PRO GLU LEU LEU ALA ALA ALA GLY PHE PHE HIS THR GLY          
SEQRES   7 E  140  HIS GLN ASP LYS VAL ARG CYS PHE PHE CYS TYR GLY GLY          
SEQRES   8 E  140  LEU GLN SER TRP LYS ARG GLY ASP ASP PRO TRP THR GLU          
SEQRES   9 E  140  HIS ALA LYS TRP PHE PRO SER CYS GLN PHE LEU LEU ARG          
SEQRES  10 E  140  SER LYS GLY ARG ASP PHE VAL HIS SER VAL GLN GLU THR          
SEQRES  11 E  140  HIS SER GLN LEU LEU GLY SER TRP ASP PRO                      
SEQRES   1 F    9  ALA GLU VAL VAL ALA VAL LYS SER GLU                          
HETNAM      ZN ZINC ION                                                         
HETNAM     P33 3,6,9,12,15,18-HEXAOXAICOSANE-1,20-DIOL                          
HETSYN     P33 HEPTAETHYLENE GLYCOL, PEG330                                     
FORMUL   7   ZN    5(ZN 2+)                                                     
FORMUL  12  P33    C14 H30 O8                                                   
FORMUL  13  HOH   *403(H2 O)                                                    
HELIX    1   1 PHE A   81  GLY A   85  5                                   5    
HELIX    2   2 SER A   86  SER A   93  1                                   8    
HELIX    3   3 PHE A   94  TRP A   97  5                                   4    
HELIX    4   4 PRO A  104  ALA A  111  1                                   8    
HELIX    5   5 ASP A  139  PHE A  148  1                                  10    
HELIX    6   6 CYS A  151  GLU A  168  1                                  18    
HELIX    7   7 PHE B   81  GLY B   85  5                                   5    
HELIX    8   8 SER B   86  SER B   93  1                                   8    
HELIX    9   9 PHE B   94  TRP B   97  5                                   4    
HELIX   10  10 PRO B  104  ALA B  111  1                                   8    
HELIX   11  11 ASP B  139  PHE B  148  1                                  10    
HELIX   12  12 CYS B  151  HIS B  170  1                                  20    
HELIX   13  13 PHE C   81  GLY C   85  5                                   5    
HELIX   14  14 SER C   86  SER C   93  1                                   8    
HELIX   15  15 PRO C  104  ALA C  111  1                                   8    
HELIX   16  16 ASP C  139  PHE C  148  1                                  10    
HELIX   17  17 CYS C  151  GLY C  159  1                                   9    
HELIX   18  18 GLY C  159  HIS C  170  1                                  12    
HELIX   19  19 PHE D   81  GLY D   85  5                                   5    
HELIX   20  20 SER D   86  SER D   93  1                                   8    
HELIX   21  21 PRO D  104  ALA D  111  1                                   8    
HELIX   22  22 ASP D  139  PHE D  148  1                                  10    
HELIX   23  23 CYS D  151  THR D  169  1                                  19    
HELIX   24  24 PHE E   81  GLY E   85  5                                   5    
HELIX   25  25 SER E   86  SER E   93  1                                   8    
HELIX   26  26 PRO E  104  ALA E  111  1                                   8    
HELIX   27  27 ASP E  139  PHE E  148  1                                  10    
HELIX   28  28 CYS E  151  THR E  169  1                                  19    
SHEET    1   A 4 THR A  74  LEU A  75  0                                        
SHEET    2   A 4 GLY D 130  GLN D 132 -1  O  GLN D 132   N  THR A  74           
SHEET    3   A 4 VAL D 122  CYS D 124 -1  N  VAL D 122   O  LEU D 131           
SHEET    4   A 4 PHE D 113  HIS D 115 -1  N  PHE D 114   O  ARG D 123           
SHEET    1   B 4 PHE A 113  HIS A 115  0                                        
SHEET    2   B 4 VAL A 122  CYS A 124 -1  O  ARG A 123   N  PHE A 114           
SHEET    3   B 4 GLY A 130  GLN A 132 -1  O  LEU A 131   N  VAL A 122           
SHEET    4   B 4 THR D  74  LEU D  75 -1  O  THR D  74   N  GLN A 132           
SHEET    1   C 4 THR B  74  LEU B  75  0                                        
SHEET    2   C 4 GLY C 130  GLN C 132 -1  O  GLN C 132   N  THR B  74           
SHEET    3   C 4 VAL C 122  CYS C 124 -1  N  VAL C 122   O  LEU C 131           
SHEET    4   C 4 PHE C 113  HIS C 115 -1  N  PHE C 114   O  ARG C 123           
SHEET    1   D 4 PHE B 113  THR B 116  0                                        
SHEET    2   D 4 LYS B 121  CYS B 124 -1  O  ARG B 123   N  PHE B 114           
SHEET    3   D 4 GLY B 130  GLN B 132 -1  O  LEU B 131   N  VAL B 122           
SHEET    4   D 4 THR C  74  LEU C  75 -1  O  THR C  74   N  GLN B 132           
SHEET    1   E 4 PHE E 113  HIS E 115  0                                        
SHEET    2   E 4 VAL E 122  CYS E 124 -1  O  ARG E 123   N  PHE E 114           
SHEET    3   E 4 GLY E 130  GLN E 132 -1  O  LEU E 131   N  VAL E 122           
SHEET    4   E 4 GLU F   2  VAL F   3 -1  O  GLU F   2   N  GLN E 132           
LINK         NE2 HIS A 144                ZN    ZN A1001     1555   1555  2.28  
LINK         SG  CYS A 124                ZN    ZN A1001     1555   1555  2.40  
LINK         SG  CYS A 127                ZN    ZN A1001     1555   1555  2.28  
LINK         SG  CYS A 151                ZN    ZN A1001     1555   1555  2.24  
LINK         NE2 HIS B 144                ZN    ZN B1002     1555   1555  2.11  
LINK         SG  CYS B 124                ZN    ZN B1002     1555   1555  2.35  
LINK         SG  CYS B 127                ZN    ZN B1002     1555   1555  2.29  
LINK         SG  CYS B 151                ZN    ZN B1002     1555   1555  2.15  
LINK         NE2 HIS C 144                ZN    ZN C1003     1555   1555  2.11  
LINK         SG  CYS C 124                ZN    ZN C1003     1555   1555  2.31  
LINK         SG  CYS C 127                ZN    ZN C1003     1555   1555  2.30  
LINK         SG  CYS C 151                ZN    ZN C1003     1555   1555  2.29  
LINK         NE2 HIS D 144                ZN    ZN D1004     1555   1555  2.10  
LINK         SG  CYS D 124                ZN    ZN D1004     1555   1555  2.45  
LINK         SG  CYS D 127                ZN    ZN D1004     1555   1555  2.26  
LINK         SG  CYS D 151                ZN    ZN D1004     1555   1555  2.37  
LINK         NE2 HIS E 144                ZN    ZN E1005     1555   1555  2.10  
LINK         SG  CYS E 124                ZN    ZN E1005     1555   1555  2.37  
LINK         SG  CYS E 127                ZN    ZN E1005     1555   1555  2.24  
LINK         SG  CYS E 151                ZN    ZN E1005     1555   1555  2.29  
SITE     1 AC1  4 CYS A 124  CYS A 127  HIS A 144  CYS A 151                    
SITE     1 AC2  4 CYS B 124  CYS B 127  HIS B 144  CYS B 151                    
SITE     1 AC3  4 CYS C 124  CYS C 127  HIS C 144  CYS C 151                    
SITE     1 AC4  4 CYS D 124  CYS D 127  HIS D 144  CYS D 151                    
SITE     1 AC5  4 CYS E 124  CYS E 127  HIS E 144  CYS E 151                    
SITE     1 AC6 17 PHE A  81  TYR A 128  PHE B  81  GLY B  83                    
SITE     2 AC6 17 TYR B 128  TYR C 128  ALA D  80  PHE D  81                    
SITE     3 AC6 17 PHE D 114  THR D 116  TYR D 128  HOH D1331                    
SITE     4 AC6 17 HOH D1332  HOH D1347  HOH D1359  HOH D1391                    
SITE     5 AC6 17 HOH D1392                                                     
SITE     1 AC7 11 ARG D 136  GLY E 130  LEU E 131  GLN E 132                    
SITE     2 AC7 11 SER E 133  ASP E 138  GLU E 143  TRP E 147                    
SITE     3 AC7 11 HOH E1068  HOH E1093  HOH F 183                               
CRYST1   83.878   83.878   94.340  90.00  90.00 120.00 P 32         15          
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      0.011922  0.006883  0.000000        0.00000                         
SCALE2      0.000000  0.013766  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010600        0.00000                         
MODEL        1                                                                  
ATOM      1  N   ALA F   1      22.437  48.742  -7.802  1.00 41.79           N  
ATOM      2  CA  ALA F   1      22.864  48.400  -6.424  1.00 42.72           C  
ATOM      3  C   ALA F   1      22.213  47.099  -5.983  1.00 44.29           C  
ATOM      4  O   ALA F   1      21.154  46.725  -6.489  1.00 45.70           O  
ATOM      5  CB  ALA F   1      22.522  49.531  -5.461  1.00 40.21           C  
ATOM      6  N   GLU F   2      22.860  46.401  -5.057  1.00 47.75           N  
ATOM      7  CA  GLU F   2      22.324  45.155  -4.512  1.00 54.17           C  
ATOM      8  C   GLU F   2      22.374  45.181  -3.001  1.00 54.03           C  
ATOM      9  O   GLU F   2      23.235  45.828  -2.408  1.00 55.21           O  
ATOM     10  CB  GLU F   2      23.075  43.926  -5.044  1.00 60.01           C  
ATOM     11  CG  GLU F   2      24.540  44.158  -5.373  1.00 69.66           C  
ATOM     12  CD  GLU F   2      25.452  43.052  -4.860  1.00 75.48           C  
ATOM     13  OE1 GLU F   2      25.507  42.832  -3.621  1.00 76.20           O  
ATOM     14  OE2 GLU F   2      26.121  42.408  -5.705  1.00 76.75           O  
ATOM     15  N   VAL F   3      21.434  44.479  -2.384  1.00 56.27           N  
ATOM     16  CA  VAL F   3      21.352  44.387  -0.935  1.00 56.06           C  
ATOM     17  C   VAL F   3      22.587  43.692  -0.385  1.00 57.02           C  
ATOM     18  O   VAL F   3      23.114  42.776  -1.008  1.00 57.96           O  
ATOM     19  CB  VAL F   3      20.092  43.623  -0.523  1.00 55.66           C  
ATOM     20  CG1 VAL F   3      20.240  43.028   0.861  1.00 60.63           C  
ATOM     21  CG2 VAL F   3      18.900  44.546  -0.577  1.00 57.11           C  
ATOM     22  N   VAL F   4      23.069  44.151   0.764  1.00 62.93           N  
ATOM     23  CA  VAL F   4      24.131  43.435   1.459  1.00 71.97           C  
ATOM     24  C   VAL F   4      23.499  42.476   2.467  1.00 77.29           C  
ATOM     25  O   VAL F   4      22.901  42.925   3.455  1.00 82.00           O  
ATOM     26  CB  VAL F   4      25.205  44.376   2.106  1.00 73.52           C  
ATOM     27  CG1 VAL F   4      24.580  45.435   3.018  1.00 73.62           C  
ATOM     28  CG2 VAL F   4      26.270  43.557   2.847  1.00 75.17           C  
TER      29      VAL F   4                                                      
HETATM   30  O   HOH F 183      21.359  43.531  -7.487  1.00 63.48           O  
ENDMDL                                                                          
MASTER       15    0    0   28   20    0   13    6 4410    6    0   56          
END                                                                             
