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Database: PDB
Entry: 1HOV
LinkDB: 1HOV
Original site: 1HOV 
HEADER    HYDROLASE/HYDROLASE INHIBITOR           11-DEC-00   1HOV              
TITLE     SOLUTION STRUCTURE OF A CATALYTIC DOMAIN OF MMP-2 COMPLEXED WITH SC-  
TITLE    2 74020                                                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MATRIX METALLOPROTEINASE-2;                                
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: CATALYTIC DOMAIN;                                          
COMPND   5 EC: 3.4.24.24;                                                       
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: W3110-II5;                                 
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: RECA                                  
KEYWDS    ENZYME-INHIBITOR COMPLEX, HYDROLASE-HYDROLASE INHIBITOR COMPLEX       
EXPDTA    SOLUTION NMR                                                          
NUMMDL    11                                                                    
AUTHOR    Y.FENG,J.J.LIKOS,L.ZHU,H.WOODWARD,G.MUNIE,J.J.MCDONALD,A.M.STEVENS,   
AUTHOR   2 C.P.HOWARD,G.A.DE CRESCENZO,D.WELSCH,H.-S.SHIEH,W.C.STALLINGS        
REVDAT   4   23-FEB-22 1HOV    1       REMARK LINK                              
REVDAT   3   24-FEB-09 1HOV    1       VERSN                                    
REVDAT   2   20-DEC-02 1HOV    1       AUTHOR JRNL   REMARK                     
REVDAT   1   12-DEC-01 1HOV    0                                                
JRNL        AUTH   Y.FENG,J.J.LIKOS,L.ZHU,H.WOODWARD,G.MUNIE,J.J.MCDONALD,      
JRNL        AUTH 2 A.M.STEVENS,C.P.HOWARD,G.A.DE CRESCENZO,D.WELSCH,H.-S.SHIEH, 
JRNL        AUTH 3 W.C.STALLINGS                                                
JRNL        TITL   SOLUTION STRUCTURE AND BACKBONE DYNAMICS OF THE CATALYTIC    
JRNL        TITL 2 DOMAIN OF MATRIX METALLOPROTEINASE-2 COMPLEXED WITH A        
JRNL        TITL 3 HYDROXAMIC ACID INHIBITOR                                    
JRNL        REF    BIOCHIM.BIOPHYS.ACTA          V.1598    10 2002              
JRNL        REFN                   ISSN 0006-3002                               
JRNL        PMID   12147339                                                     
JRNL        DOI    10.1016/S0167-4838(02)00307-2                                
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  TITL   1H, 13C AND 15N RESONANCE ASSIGNMENTS FOR A TRUNCATED AND    
REMARK   1  TITL 2 INHIBITED CATALYTIC DOMAIN OF MATRIX METALLOPROTEINASE-2     
REMARK   1  REF    J.BIOMOL.NMR                  V.  17    85 2000              
REMARK   1  REFN                   ISSN 0925-2738                               
REMARK   2                                                                      
REMARK   2 RESOLUTION. NOT APPLICABLE.                                          
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR 98.1                                          
REMARK   3   AUTHORS     : MSI                                                  
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1HOV COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-DEC-00.                  
REMARK 100 THE DEPOSITION ID IS D_1000012486.                                   
REMARK 210                                                                      
REMARK 210 EXPERIMENTAL DETAILS                                                 
REMARK 210  EXPERIMENT TYPE                : NMR                                
REMARK 210  TEMPERATURE           (KELVIN) : 303                                
REMARK 210  PH                             : 7.4                                
REMARK 210  IONIC STRENGTH                 : 50                                 
REMARK 210  PRESSURE                       : 1 ATM                              
REMARK 210  SAMPLE CONTENTS                : 0.3-0.4MM U-15N, 13C MMP-2C:       
REMARK 210                                   UNLABELED SC-74020 IN 20MM TRIS-   
REMARK 210                                   D11-HCL, 5MM CACL2, 10UM ZNCL2,    
REMARK 210                                   20UM UNLABELED SC-74020            
REMARK 210                                                                      
REMARK 210  NMR EXPERIMENTS CONDUCTED      : NULL                               
REMARK 210  SPECTROMETER FIELD STRENGTH    : 600 MHZ; 500 MHZ                   
REMARK 210  SPECTROMETER MODEL             : INOVA; UNITY                       
REMARK 210  SPECTROMETER MANUFACTURER      : VARIAN                             
REMARK 210                                                                      
REMARK 210  STRUCTURE DETERMINATION.                                            
REMARK 210   SOFTWARE USED                 : VNMR 6.1B, FELIX 97                
REMARK 210   METHOD USED                   : DISTANCE GEOMETRY, SIMULATED       
REMARK 210                                   ANNEALING, MOLECULAR DYNAMICS,     
REMARK 210                                   TORSION ANGLE DYNAMICS             
REMARK 210                                                                      
REMARK 210 CONFORMERS, NUMBER CALCULATED   : 14                                 
REMARK 210 CONFORMERS, NUMBER SUBMITTED    : 11                                 
REMARK 210 CONFORMERS, SELECTION CRITERIA  : STRUCTURES WITH THE LEAST          
REMARK 210                                   RESTRAINT VIOLATIONS               
REMARK 210                                                                      
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 3                   
REMARK 210                                                                      
REMARK 210 REMARK: NULL                                                         
REMARK 215                                                                      
REMARK 215 NMR STUDY                                                            
REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION           
REMARK 215 NMR DATA.  PROTEIN DATA BANK CONVENTIONS REQUIRE THAT                
REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON              
REMARK 215 THESE RECORDS ARE MEANINGLESS.                                       
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   H    ILE A    21     O    ILE A    63              1.60            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500  1 TYR A   2      -89.33     53.48                                   
REMARK 500  1 PRO A   6       41.86    -76.03                                   
REMARK 500  1 ARG A   7      -49.23     71.79                                   
REMARK 500  1 LYS A  10      134.05    -30.88                                   
REMARK 500  1 ASP A  12       74.65   -175.87                                   
REMARK 500  1 ASN A  14     -173.81    -53.98                                   
REMARK 500  1 GLN A  15       98.49     47.67                                   
REMARK 500  1 THR A  47      148.15   -178.13                                   
REMARK 500  1 ILE A  54     -168.73   -124.38                                   
REMARK 500  1 HIS A  55       30.23   -176.15                                   
REMARK 500  1 ASP A  56      -32.83   -163.31                                   
REMARK 500  1 GLU A  58      170.42     58.04                                   
REMARK 500  1 ASN A  64     -138.71    178.85                                   
REMARK 500  1 ARG A  67      170.49     60.75                                   
REMARK 500  1 GLU A  69      -96.23    -75.85                                   
REMARK 500  1 HIS A  70      -80.06     78.17                                   
REMARK 500  1 ASP A  72      -90.10    -37.72                                   
REMARK 500  1 TYR A  74       74.32   -179.67                                   
REMARK 500  1 PHE A  76      158.96     50.53                                   
REMARK 500  1 ASP A  77      -29.39    178.56                                   
REMARK 500  1 LYS A  79     -173.56     43.56                                   
REMARK 500  1 ASP A  80      -95.85    -67.15                                   
REMARK 500  1 ALA A  84     -178.07    169.40                                   
REMARK 500  1 HIS A  85      175.86    179.05                                   
REMARK 500  1 ALA A  88      172.78    -48.55                                   
REMARK 500  1 ASP A 101      -78.56    -76.29                                   
REMARK 500  1 ASP A 102       91.16    -66.04                                   
REMARK 500  1 THR A 108     -145.28    -91.89                                   
REMARK 500  1 SER A 109       37.99    -89.90                                   
REMARK 500  1 ALA A 110      -97.30    -64.14                                   
REMARK 500  1 ASN A 111      -46.45   -178.31                                   
REMARK 500  1 SER A 113      110.12     62.20                                   
REMARK 500  1 MET A 126      -96.37    -78.99                                   
REMARK 500  1 GLN A 132      -24.80     82.48                                   
REMARK 500  1 PRO A 140       21.66    -78.97                                   
REMARK 500  1 ASN A 147       20.61   -160.00                                   
REMARK 500  1 PHE A 148       94.05     36.24                                   
REMARK 500  1 TYR A 162      -93.30   -140.11                                   
REMARK 500  2 TYR A   2      -94.28    -58.49                                   
REMARK 500  2 ASN A   3       98.06     60.21                                   
REMARK 500  2 PRO A   6     -161.09    -74.18                                   
REMARK 500  2 ARG A   7       54.44     77.44                                   
REMARK 500  2 LYS A   8      144.59     60.52                                   
REMARK 500  2 LYS A  10     -137.11    -62.34                                   
REMARK 500  2 TRP A  11       44.18   -163.00                                   
REMARK 500  2 ASN A  14      -85.71    -34.18                                   
REMARK 500  2 GLN A  15      106.97    -51.88                                   
REMARK 500  2 TYR A  23     -114.33    -58.07                                   
REMARK 500  2 ASP A  26       81.73   -158.64                                   
REMARK 500  2 THR A  47      149.32   -179.33                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     404 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 168  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  60   O                                                      
REMARK 620 2 GLY A  92   O   100.0                                              
REMARK 620 3 GLY A  94   O    82.5 112.6                                        
REMARK 620 4 GLY A  95   N   115.7 132.2  48.0                                  
REMARK 620 5 ASP A  96   N   124.4 125.4 103.8  56.7                            
REMARK 620 6 ASP A  96   OD1 104.2  68.7 173.0 125.7  70.8                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 165  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  70   NE2                                                    
REMARK 620 2 ASP A  72   OD2  84.2                                              
REMARK 620 3 HIS A  85   NE2 134.6  90.5                                        
REMARK 620 4 HIS A  98   ND1  72.8 150.0  92.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 167  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  77   OD2                                                    
REMARK 620 2 ASP A  77   OD1  45.5                                              
REMARK 620 3 GLY A  78   O    66.6  77.9                                        
REMARK 620 4 LYS A  79   O   108.7 130.4  52.9                                  
REMARK 620 5 ASP A  80   O    82.2 127.3  87.4  62.7                            
REMARK 620 6 LEU A  82   O    83.3  95.3 143.9 127.0  68.6                      
REMARK 620 7 ASP A 100   OD1  92.3  67.3 144.5 158.8 119.0  50.5                
REMARK 620 8 ASP A 100   OD2 104.0  59.2 109.8 127.8 162.8  95.9  45.6          
REMARK 620 9 GLU A 103   OE1 141.9 103.0  88.8  73.5 127.2 127.0  92.2  56.0    
REMARK 620 N                    1     2     3     4     5     6     7     8     
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 166  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 120   NE2                                                    
REMARK 620 2 HIS A 124   NE2 100.3                                              
REMARK 620 3 HIS A 130   NE2 111.5  71.9                                        
REMARK 620 4 I52 A 800   O26 145.1 106.8  97.8                                  
REMARK 620 5 I52 A 800   O1   85.8  81.2 149.9  77.2                            
REMARK 620 N                    1     2     3     4                             
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 165                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 166                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 167                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 168                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE I52 A 800                 
DBREF  1HOV A    2   148  UNP    P08253   MMP2_HUMAN     110    256             
SEQRES   1 A  163  MET TYR ASN PHE PHE PRO ARG LYS PRO LYS TRP ASP LYS          
SEQRES   2 A  163  ASN GLN ILE THR TYR ARG ILE ILE GLY TYR THR PRO ASP          
SEQRES   3 A  163  LEU ASP PRO GLU THR VAL ASP ASP ALA PHE ALA ARG ALA          
SEQRES   4 A  163  PHE GLN VAL TRP SER ASP VAL THR PRO LEU ARG PHE SER          
SEQRES   5 A  163  ARG ILE HIS ASP GLY GLU ALA ASP ILE MET ILE ASN PHE          
SEQRES   6 A  163  GLY ARG TRP GLU HIS GLY ASP GLY TYR PRO PHE ASP GLY          
SEQRES   7 A  163  LYS ASP GLY LEU LEU ALA HIS ALA PHE ALA PRO GLY THR          
SEQRES   8 A  163  GLY VAL GLY GLY ASP SER HIS PHE ASP ASP ASP GLU LEU          
SEQRES   9 A  163  TRP THR ASN THR SER ALA ASN TYR SER LEU PHE LEU VAL          
SEQRES  10 A  163  ALA ALA HIS GLU PHE GLY HIS ALA MET GLY LEU GLU HIS          
SEQRES  11 A  163  SER GLN ASP PRO GLY ALA LEU MET ALA PRO ILE TYR THR          
SEQRES  12 A  163  TYR THR LYS ASN PHE ARG LEU SER GLN ASP ASP ILE LYS          
SEQRES  13 A  163  GLY ILE GLN GLU LEU TYR GLY                                  
HET     ZN  A 165       1                                                       
HET     ZN  A 166       1                                                       
HET     CA  A 167       1                                                       
HET     CA  A 168       1                                                       
HET    I52  A 800      82                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM      CA CALCIUM ION                                                      
HETNAM     I52 N-{4-[(1-HYDROXYCARBAMOYL-2-METHYL-PROPYL)-(2-                   
HETNAM   2 I52  MORPHOLIN-4-YL-ETHYL)-SULFAMOYL]-4-PENTYL-BENZAMIDE             
HETSYN     I52 SC-74020                                                         
FORMUL   2   ZN    2(ZN 2+)                                                     
FORMUL   4   CA    2(CA 2+)                                                     
FORMUL   6  I52    C29 H42 N4 O6 S                                              
HELIX    1   1 ASP A   28  ASP A   45  1                                  18    
HELIX    2   2 SER A  113  ALA A  125  1                                  13    
HELIX    3   3 SER A  151  TYR A  162  1                                  12    
SHEET    1   A 5 PHE A  51  ARG A  53  0                                        
SHEET    2   A 5 ILE A  16  ILE A  20  1  O  ILE A  16   N  SER A  52           
SHEET    3   A 5 ILE A  61  PHE A  65  1  N  ILE A  61   O  THR A  17           
SHEET    4   A 5 SER A  97  PHE A  99  1  N  SER A  97   O  MET A  62           
SHEET    5   A 5 ALA A  84  ALA A  86 -1  O  HIS A  85   N  HIS A  98           
LINK         O   ASP A  60                CA    CA A 168     1555   1555  2.45  
LINK         NE2 HIS A  70                ZN    ZN A 165     1555   1555  2.13  
LINK         OD2 ASP A  72                ZN    ZN A 165     1555   1555  2.29  
LINK         OD2 ASP A  77                CA    CA A 167     1555   1555  2.64  
LINK         OD1 ASP A  77                CA    CA A 167     1555   1555  2.90  
LINK         O   GLY A  78                CA    CA A 167     1555   1555  2.59  
LINK         O   LYS A  79                CA    CA A 167     1555   1555  2.50  
LINK         O   ASP A  80                CA    CA A 167     1555   1555  2.57  
LINK         O   LEU A  82                CA    CA A 167     1555   1555  2.57  
LINK         NE2 HIS A  85                ZN    ZN A 165     1555   1555  2.07  
LINK         O   GLY A  92                CA    CA A 168     1555   1555  2.47  
LINK         O   GLY A  94                CA    CA A 168     1555   1555  2.54  
LINK         N   GLY A  95                CA    CA A 168     1555   1555  2.83  
LINK         N   ASP A  96                CA    CA A 168     1555   1555  2.84  
LINK         OD1 ASP A  96                CA    CA A 168     1555   1555  2.44  
LINK         ND1 HIS A  98                ZN    ZN A 165     1555   1555  2.26  
LINK         OD1 ASP A 100                CA    CA A 167     1555   1555  2.87  
LINK         OD2 ASP A 100                CA    CA A 167     1555   1555  2.67  
LINK         OE1 GLU A 103                CA    CA A 167     1555   1555  3.13  
LINK         OE2 GLU A 103                CA    CA A 167     1555   1555  2.48  
LINK         NE2 HIS A 120                ZN    ZN A 166     1555   1555  2.16  
LINK         NE2 HIS A 124                ZN    ZN A 166     1555   1555  2.30  
LINK         NE2 HIS A 130                ZN    ZN A 166     1555   1555  2.06  
LINK        ZN    ZN A 166                 O26 I52 A 800     1555   1555  2.13  
LINK        ZN    ZN A 166                 O1  I52 A 800     1555   1555  2.08  
SITE     1 AC1  4 HIS A  70  ASP A  72  HIS A  85  HIS A  98                    
SITE     1 AC2  4 HIS A 120  HIS A 124  HIS A 130  I52 A 800                    
SITE     1 AC3  7 ASP A  77  GLY A  78  LYS A  79  ASP A  80                    
SITE     2 AC3  7 LEU A  82  ASP A 100  GLU A 103                               
SITE     1 AC4  6 ASP A  60  GLY A  92  VAL A  93  GLY A  94                    
SITE     2 AC4  6 GLY A  95  ASP A  96                                          
SITE     1 AC5 19 GLY A  81  LEU A  82  LEU A  83  ALA A  84                    
SITE     2 AC5 19 HIS A  85  HIS A 120  GLU A 121  HIS A 124                    
SITE     3 AC5 19 HIS A 130  ALA A 136  LEU A 137  ALA A 139                    
SITE     4 AC5 19 ILE A 141  TYR A 142  THR A 143  THR A 145                    
SITE     5 AC5 19 PHE A 148  ARG A 149   ZN A 166                               
CRYST1    1.000    1.000    1.000  90.00  90.00  90.00 P 1           1          
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      1.000000  0.000000  0.000000        0.00000                         
SCALE2      0.000000  1.000000  0.000000        0.00000                         
SCALE3      0.000000  0.000000  1.000000        0.00000                         
MODEL        1                                                                  
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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