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Database: PDB
Entry: 3GZO
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Original site: 3GZO 
HEADER    OXIDOREDUCTASE                          07-APR-09   3GZO              
TITLE     HUMAN SOD1 G93A VARIANT                                               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SUPEROXIDE DISMUTASE [CU-ZN];                              
COMPND   3 CHAIN: A, B, C, D, E, F, G, H, I, J;                                 
COMPND   4 EC: 1.15.1.1;                                                        
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: SOD1;                                                          
SOURCE   6 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE;                         
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 4932;                                       
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: EGY118;                                    
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: YEP351-HSOD                               
KEYWDS    OXIDOREDUCTASE, HUMAN CU, ZN SUPEROXIDE DISMUTASE, ANTIOXIDANT,       
KEYWDS   2 METAL-BINDING, AMYOTROPHIC LATERAL SCLEROSIS, DISEASE MUTATION,      
KEYWDS   3 DISULFIDE BOND, PHOSPHOPROTEIN                                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.GALALELDEEN,A.B.TAYLOR,N.NARAYANA,L.J.WHITSON,P.J.HART              
REVDAT   3   13-JUL-11 3GZO    1       VERSN                                    
REVDAT   2   22-DEC-09 3GZO    1       JRNL                                     
REVDAT   1   13-OCT-09 3GZO    0                                                
JRNL        AUTH   A.GALALELDEEN,R.W.STRANGE,L.J.WHITSON,S.V.ANTONYUK,          
JRNL        AUTH 2 N.NARAYANA,A.B.TAYLOR,J.P.SCHUERMANN,S.P.HOLLOWAY,           
JRNL        AUTH 3 S.S.HASNAIN,P.J.HART                                         
JRNL        TITL   STRUCTURAL AND BIOPHYSICAL PROPERTIES OF METAL-FREE          
JRNL        TITL 2 PATHOGENIC SOD1 MUTANTS A4V AND G93A.                        
JRNL        REF    ARCH.BIOCHEM.BIOPHYS.         V. 492    40 2009              
JRNL        REFN                   ISSN 0003-9861                               
JRNL        PMID   19800308                                                     
JRNL        DOI    10.1016/J.ABB.2009.09.020                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.4_4)                        
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 41.49                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.020                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 135446                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.174                           
REMARK   3   R VALUE            (WORKING SET) : 0.172                           
REMARK   3   FREE R VALUE                     : 0.214                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.990                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 6759                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 41.5006 -  6.5185    0.98     4625   226  0.1668 0.1977        
REMARK   3     2  6.5185 -  5.1771    0.99     4508   217  0.1446 0.1750        
REMARK   3     3  5.1771 -  4.5236    0.99     4458   228  0.1200 0.1398        
REMARK   3     4  4.5236 -  4.1104    0.99     4469   231  0.1147 0.1438        
REMARK   3     5  4.1104 -  3.8160    0.99     4430   217  0.1222 0.1629        
REMARK   3     6  3.8160 -  3.5912    0.99     4455   231  0.1300 0.1611        
REMARK   3     7  3.5912 -  3.4114    0.99     4398   242  0.1382 0.1823        
REMARK   3     8  3.4114 -  3.2630    0.99     4414   237  0.1401 0.1809        
REMARK   3     9  3.2630 -  3.1374    0.99     4374   220  0.1507 0.1915        
REMARK   3    10  3.1374 -  3.0292    0.98     4368   241  0.1604 0.2195        
REMARK   3    11  3.0292 -  2.9345    0.98     4332   243  0.1711 0.2141        
REMARK   3    12  2.9345 -  2.8506    0.98     4350   223  0.1812 0.2071        
REMARK   3    13  2.8506 -  2.7756    0.97     4323   219  0.1773 0.2168        
REMARK   3    14  2.7756 -  2.7079    0.97     4338   217  0.1816 0.2439        
REMARK   3    15  2.7079 -  2.6463    0.96     4238   217  0.1965 0.2568        
REMARK   3    16  2.6463 -  2.5900    0.96     4238   243  0.2002 0.2567        
REMARK   3    17  2.5900 -  2.5382    0.96     4208   257  0.2030 0.2475        
REMARK   3    18  2.5382 -  2.4903    0.96     4276   214  0.2076 0.2625        
REMARK   3    19  2.4903 -  2.4459    0.96     4242   229  0.2090 0.2766        
REMARK   3    20  2.4459 -  2.4044    0.95     4203   248  0.2139 0.2534        
REMARK   3    21  2.4044 -  2.3656    0.95     4189   221  0.2144 0.2750        
REMARK   3    22  2.3656 -  2.3292    0.95     4220   213  0.2202 0.2828        
REMARK   3    23  2.3292 -  2.2950    0.94     4183   221  0.2116 0.2476        
REMARK   3    24  2.2950 -  2.2627    0.94     4156   187  0.2208 0.2761        
REMARK   3    25  2.2627 -  2.2321    0.94     4163   237  0.2283 0.2788        
REMARK   3    26  2.2321 -  2.2031    0.94     4159   232  0.2402 0.2759        
REMARK   3    27  2.2031 -  2.1756    0.94     4143   223  0.2362 0.2723        
REMARK   3    28  2.1756 -  2.1493    0.93     4091   214  0.2418 0.2670        
REMARK   3    29  2.1493 -  2.1243    0.93     4129   210  0.2443 0.2989        
REMARK   3    30  2.1243 -  2.1000    0.91     4007   201  0.2522 0.2955        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : 0.40                                          
REMARK   3   B_SOL              : 40.00                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 1.750            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL             
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 20.60                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 25.70                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.43610                                             
REMARK   3    B22 (A**2) : -2.06830                                             
REMARK   3    B33 (A**2) : 3.27780                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.009           NULL                                  
REMARK   3   ANGLE     :   NULL           NULL                                  
REMARK   3   CHIRALITY :   NULL           NULL                                  
REMARK   3   PLANARITY :   NULL           NULL                                  
REMARK   3   DIHEDRAL  :   NULL           NULL                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3GZO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-APR-09.                  
REMARK 100 THE RCSB ID CODE IS RCSB052507.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 09-OCT-03                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6                                  
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU FR-D                        
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : CONFOCAL OPTICS                    
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS VII                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 140272                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 3.500                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.12100                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.8000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.18                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.20                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.50800                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.300                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1SOS                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 67.74                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.81                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.4 M SODIUM MALONATE, PH 6, VAPOR       
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 298K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       71.65950            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       71.65950            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       83.07400            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000      101.63150            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       83.07400            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000      101.63150            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       71.65950            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       83.07400            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000      101.63150            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       71.65950            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       83.07400            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000      101.63150            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5                                           
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1950 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13960 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -16.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1620 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13870 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -14.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
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 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1650 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13850 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -14.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F                                  
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 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1920 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13930 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H                                  
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 350                                                                      
REMARK 350 BIOMOLECULE: 5                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1990 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13850 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: I, J                                  
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: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG B  79   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.4 DEGREES          
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    HIS A 110       17.95    -67.48                                   
REMARK 500    ASN G  26        5.80     58.28                                   
REMARK 500    ASN H  65       58.49   -143.09                                   
REMARK 500    HIS H 110      -92.51    -49.62                                   
REMARK 500    CYS H 111      137.96     75.49                                   
REMARK 500    LYS I 128       13.82   -143.34                                   
REMARK 500    ASP J  92       46.54    -98.87                                   
REMARK 500    ALA J  93       14.40     57.51                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH B1038        DISTANCE =  6.12 ANGSTROMS                       
REMARK 525    HOH D1190        DISTANCE =  5.27 ANGSTROMS                       
REMARK 525    HOH D1445        DISTANCE =  5.77 ANGSTROMS                       
REMARK 525    HOH D1543        DISTANCE =  6.82 ANGSTROMS                       
REMARK 525    HOH D1559        DISTANCE =  5.77 ANGSTROMS                       
REMARK 525    HOH E1156        DISTANCE =  5.06 ANGSTROMS                       
REMARK 525    HOH E1192        DISTANCE =  5.26 ANGSTROMS                       
REMARK 525    HOH E1444        DISTANCE =  5.08 ANGSTROMS                       
REMARK 525    HOH E1456        DISTANCE =  5.07 ANGSTROMS                       
REMARK 525    HOH E1589        DISTANCE =  7.20 ANGSTROMS                       
REMARK 525    HOH F1595        DISTANCE =  5.13 ANGSTROMS                       
REMARK 525    HOH G 522        DISTANCE =  5.10 ANGSTROMS                       
REMARK 525    HOH H1242        DISTANCE =  5.21 ANGSTROMS                       
REMARK 525    HOH I1184        DISTANCE =  5.28 ANGSTROMS                       
REMARK 525    HOH I1237        DISTANCE =  5.07 ANGSTROMS                       
REMARK 525    HOH I1601        DISTANCE =  5.33 ANGSTROMS                       
REMARK 525    HOH J1394        DISTANCE =  5.37 ANGSTROMS                       
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                              CU A 154  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  46   ND1                                                    
REMARK 620 2 HIS A  48   NE2 153.8                                              
REMARK 620 3 HIS A 120   NE2  99.3  98.1                                        
REMARK 620 4 HIS A  63   NE2  79.0 104.0 130.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 155  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  63   ND1                                                    
REMARK 620 2 HIS A  71   ND1 100.2                                              
REMARK 620 3 HIS A  80   ND1 111.5 121.7                                        
REMARK 620 4 ASP A  83   OD1 109.7  99.2 113.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU B 154  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B  46   ND1                                                    
REMARK 620 2 HIS B  48   NE2 159.8                                              
REMARK 620 3 HIS B 120   NE2 102.2  97.9                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 155  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B  63   ND1                                                    
REMARK 620 2 HIS B  71   ND1 103.7                                              
REMARK 620 3 HIS B  80   ND1 114.7 121.0                                        
REMARK 620 4 ASP B  83   OD1 104.8  96.4 113.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU C 154  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS C  46   ND1                                                    
REMARK 620 2 HIS C  48   NE2 162.1                                              
REMARK 620 3 HIS C 120   NE2 100.7  95.2                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN C 155  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS C  63   ND1                                                    
REMARK 620 2 HIS C  71   ND1 100.3                                              
REMARK 620 3 HIS C  80   ND1 115.3 123.0                                        
REMARK 620 4 ASP C  83   OD1  97.5  94.0 121.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU D 154  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS D  46   ND1                                                    
REMARK 620 2 HIS D  48   NE2 145.0                                              
REMARK 620 3 HIS D 120   NE2 108.2  96.5                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN D 155  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS D  63   ND1                                                    
REMARK 620 2 HIS D  71   ND1 101.4                                              
REMARK 620 3 HIS D  80   ND1 109.7 125.2                                        
REMARK 620 4 ASP D  83   OD1 103.0  99.8 115.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU E 154  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS E  46   ND1                                                    
REMARK 620 2 HIS E  48   NE2 161.9                                              
REMARK 620 3 HIS E 120   NE2  96.4  98.9                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN E 155  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS E  63   ND1                                                    
REMARK 620 2 HIS E  71   ND1 102.1                                              
REMARK 620 3 HIS E  80   ND1 108.9 127.4                                        
REMARK 620 4 ASP E  83   OD1 104.2  93.3 117.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU F 154  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS F  46   ND1                                                    
REMARK 620 2 HIS F  48   NE2 168.0                                              
REMARK 620 3 HIS F 120   NE2  96.8  95.0                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN F 155  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS F  63   ND1                                                    
REMARK 620 2 HIS F  71   ND1 105.0                                              
REMARK 620 3 HIS F  80   ND1 111.5 123.1                                        
REMARK 620 4 ASP F  83   OD1 107.5  94.0 113.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU G 154  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS G  46   ND1                                                    
REMARK 620 2 HIS G  48   NE2 148.7                                              
REMARK 620 3 HIS G 120   NE2 104.2  99.6                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN G 155  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS G  63   ND1                                                    
REMARK 620 2 HIS G  71   ND1 102.7                                              
REMARK 620 3 HIS G  80   ND1 113.3 121.1                                        
REMARK 620 4 ASP G  83   OD1 100.5  95.4 120.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU H 154  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS H  46   ND1                                                    
REMARK 620 2 HIS H  48   NE2 153.4                                              
REMARK 620 3 HIS H 120   NE2 101.3  93.7                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN H 155  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS H  63   ND1                                                    
REMARK 620 2 HIS H  71   ND1 101.1                                              
REMARK 620 3 HIS H  80   ND1 112.8 126.7                                        
REMARK 620 4 ASP H  83   OD1 100.2  98.0 114.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU I 154  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS I  46   ND1                                                    
REMARK 620 2 HIS I  48   NE2 138.3                                              
REMARK 620 3 HIS I 120   NE2  93.4  95.4                                        
REMARK 620 4 HIS I  63   NE2  92.4 110.1 133.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN I 155  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS I  63   ND1                                                    
REMARK 620 2 HIS I  71   ND1 113.0                                              
REMARK 620 3 HIS I  80   ND1 111.8 120.7                                        
REMARK 620 4 ASP I  83   OD1 101.1  93.6 113.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU J 154  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS J  46   ND1                                                    
REMARK 620 2 HIS J  48   NE2 165.0                                              
REMARK 620 3 HIS J 120   NE2  95.9  96.2                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN J 155  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS J  63   ND1                                                    
REMARK 620 2 HIS J  71   ND1 100.6                                              
REMARK 620 3 HIS J  80   ND1 111.8 122.4                                        
REMARK 620 4 ASP J  83   OD1 105.3 100.8 114.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU A 154                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 155                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU B 154                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 155                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU C 154                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 155                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU D 154                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 155                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU E 154                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN E 155                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU F 154                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN F 155                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU G 154                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN G 155                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU H 154                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN H 155                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU I 154                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN I 155                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU J 154                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN J 155                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MLI H 156                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 156                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL J 156                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3GZP   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3GZQ   RELATED DB: PDB                                   
DBREF  3GZO A    1   153  UNP    P00441   SODC_HUMAN       2    154             
DBREF  3GZO B    1   153  UNP    P00441   SODC_HUMAN       2    154             
DBREF  3GZO C    1   153  UNP    P00441   SODC_HUMAN       2    154             
DBREF  3GZO D    1   153  UNP    P00441   SODC_HUMAN       2    154             
DBREF  3GZO E    1   153  UNP    P00441   SODC_HUMAN       2    154             
DBREF  3GZO F    1   153  UNP    P00441   SODC_HUMAN       2    154             
DBREF  3GZO G    1   153  UNP    P00441   SODC_HUMAN       2    154             
DBREF  3GZO H    1   153  UNP    P00441   SODC_HUMAN       2    154             
DBREF  3GZO I    1   153  UNP    P00441   SODC_HUMAN       2    154             
DBREF  3GZO J    1   153  UNP    P00441   SODC_HUMAN       2    154             
SEQADV 3GZO ACE A    0  UNP  P00441              INSERTION                      
SEQADV 3GZO ALA A   93  UNP  P00441    GLY    94 ENGINEERED                     
SEQADV 3GZO ACE B    0  UNP  P00441              INSERTION                      
SEQADV 3GZO ALA B   93  UNP  P00441    GLY    94 ENGINEERED                     
SEQADV 3GZO ACE C    0  UNP  P00441              INSERTION                      
SEQADV 3GZO ALA C   93  UNP  P00441    GLY    94 ENGINEERED                     
SEQADV 3GZO ACE D    0  UNP  P00441              INSERTION                      
SEQADV 3GZO ALA D   93  UNP  P00441    GLY    94 ENGINEERED                     
SEQADV 3GZO ACE E    0  UNP  P00441              INSERTION                      
SEQADV 3GZO ALA E   93  UNP  P00441    GLY    94 ENGINEERED                     
SEQADV 3GZO ACE F    0  UNP  P00441              INSERTION                      
SEQADV 3GZO ALA F   93  UNP  P00441    GLY    94 ENGINEERED                     
SEQADV 3GZO ACE G    0  UNP  P00441              INSERTION                      
SEQADV 3GZO ALA G   93  UNP  P00441    GLY    94 ENGINEERED                     
SEQADV 3GZO ACE H    0  UNP  P00441              INSERTION                      
SEQADV 3GZO ALA H   93  UNP  P00441    GLY    94 ENGINEERED                     
SEQADV 3GZO ACE I    0  UNP  P00441              INSERTION                      
SEQADV 3GZO ALA I   93  UNP  P00441    GLY    94 ENGINEERED                     
SEQADV 3GZO ACE J    0  UNP  P00441              INSERTION                      
SEQADV 3GZO ALA J   93  UNP  P00441    GLY    94 ENGINEERED                     
SEQRES   1 A  154  ACE ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY          
SEQRES   2 A  154  PRO VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER          
SEQRES   3 A  154  ASN GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU          
SEQRES   4 A  154  THR GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY          
SEQRES   5 A  154  ASP ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE          
SEQRES   6 A  154  ASN PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU          
SEQRES   7 A  154  GLU ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP          
SEQRES   8 A  154  LYS ASP ALA VAL ALA ASP VAL SER ILE GLU ASP SER VAL          
SEQRES   9 A  154  ILE SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR          
SEQRES  10 A  154  LEU VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY          
SEQRES  11 A  154  GLY ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER          
SEQRES  12 A  154  ARG LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                  
SEQRES   1 B  154  ACE ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY          
SEQRES   2 B  154  PRO VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER          
SEQRES   3 B  154  ASN GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU          
SEQRES   4 B  154  THR GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY          
SEQRES   5 B  154  ASP ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE          
SEQRES   6 B  154  ASN PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU          
SEQRES   7 B  154  GLU ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP          
SEQRES   8 B  154  LYS ASP ALA VAL ALA ASP VAL SER ILE GLU ASP SER VAL          
SEQRES   9 B  154  ILE SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR          
SEQRES  10 B  154  LEU VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY          
SEQRES  11 B  154  GLY ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER          
SEQRES  12 B  154  ARG LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                  
SEQRES   1 C  154  ACE ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY          
SEQRES   2 C  154  PRO VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER          
SEQRES   3 C  154  ASN GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU          
SEQRES   4 C  154  THR GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY          
SEQRES   5 C  154  ASP ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE          
SEQRES   6 C  154  ASN PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU          
SEQRES   7 C  154  GLU ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP          
SEQRES   8 C  154  LYS ASP ALA VAL ALA ASP VAL SER ILE GLU ASP SER VAL          
SEQRES   9 C  154  ILE SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR          
SEQRES  10 C  154  LEU VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY          
SEQRES  11 C  154  GLY ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER          
SEQRES  12 C  154  ARG LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                  
SEQRES   1 D  154  ACE ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY          
SEQRES   2 D  154  PRO VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER          
SEQRES   3 D  154  ASN GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU          
SEQRES   4 D  154  THR GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY          
SEQRES   5 D  154  ASP ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE          
SEQRES   6 D  154  ASN PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU          
SEQRES   7 D  154  GLU ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP          
SEQRES   8 D  154  LYS ASP ALA VAL ALA ASP VAL SER ILE GLU ASP SER VAL          
SEQRES   9 D  154  ILE SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR          
SEQRES  10 D  154  LEU VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY          
SEQRES  11 D  154  GLY ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER          
SEQRES  12 D  154  ARG LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                  
SEQRES   1 E  154  ACE ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY          
SEQRES   2 E  154  PRO VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER          
SEQRES   3 E  154  ASN GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU          
SEQRES   4 E  154  THR GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY          
SEQRES   5 E  154  ASP ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE          
SEQRES   6 E  154  ASN PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU          
SEQRES   7 E  154  GLU ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP          
SEQRES   8 E  154  LYS ASP ALA VAL ALA ASP VAL SER ILE GLU ASP SER VAL          
SEQRES   9 E  154  ILE SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR          
SEQRES  10 E  154  LEU VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY          
SEQRES  11 E  154  GLY ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER          
SEQRES  12 E  154  ARG LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                  
SEQRES   1 F  154  ACE ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY          
SEQRES   2 F  154  PRO VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER          
SEQRES   3 F  154  ASN GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU          
SEQRES   4 F  154  THR GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY          
SEQRES   5 F  154  ASP ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE          
SEQRES   6 F  154  ASN PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU          
SEQRES   7 F  154  GLU ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP          
SEQRES   8 F  154  LYS ASP ALA VAL ALA ASP VAL SER ILE GLU ASP SER VAL          
SEQRES   9 F  154  ILE SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR          
SEQRES  10 F  154  LEU VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY          
SEQRES  11 F  154  GLY ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER          
SEQRES  12 F  154  ARG LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                  
SEQRES   1 G  154  ACE ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY          
SEQRES   2 G  154  PRO VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER          
SEQRES   3 G  154  ASN GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU          
SEQRES   4 G  154  THR GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY          
SEQRES   5 G  154  ASP ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE          
SEQRES   6 G  154  ASN PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU          
SEQRES   7 G  154  GLU ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP          
SEQRES   8 G  154  LYS ASP ALA VAL ALA ASP VAL SER ILE GLU ASP SER VAL          
SEQRES   9 G  154  ILE SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR          
SEQRES  10 G  154  LEU VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY          
SEQRES  11 G  154  GLY ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER          
SEQRES  12 G  154  ARG LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                  
SEQRES   1 H  154  ACE ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY          
SEQRES   2 H  154  PRO VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER          
SEQRES   3 H  154  ASN GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU          
SEQRES   4 H  154  THR GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY          
SEQRES   5 H  154  ASP ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE          
SEQRES   6 H  154  ASN PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU          
SEQRES   7 H  154  GLU ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP          
SEQRES   8 H  154  LYS ASP ALA VAL ALA ASP VAL SER ILE GLU ASP SER VAL          
SEQRES   9 H  154  ILE SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR          
SEQRES  10 H  154  LEU VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY          
SEQRES  11 H  154  GLY ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER          
SEQRES  12 H  154  ARG LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                  
SEQRES   1 I  154  ACE ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY          
SEQRES   2 I  154  PRO VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER          
SEQRES   3 I  154  ASN GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU          
SEQRES   4 I  154  THR GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY          
SEQRES   5 I  154  ASP ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE          
SEQRES   6 I  154  ASN PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU          
SEQRES   7 I  154  GLU ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP          
SEQRES   8 I  154  LYS ASP ALA VAL ALA ASP VAL SER ILE GLU ASP SER VAL          
SEQRES   9 I  154  ILE SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR          
SEQRES  10 I  154  LEU VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY          
SEQRES  11 I  154  GLY ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER          
SEQRES  12 I  154  ARG LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                  
SEQRES   1 J  154  ACE ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY          
SEQRES   2 J  154  PRO VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER          
SEQRES   3 J  154  ASN GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU          
SEQRES   4 J  154  THR GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY          
SEQRES   5 J  154  ASP ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE          
SEQRES   6 J  154  ASN PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU          
SEQRES   7 J  154  GLU ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP          
SEQRES   8 J  154  LYS ASP ALA VAL ALA ASP VAL SER ILE GLU ASP SER VAL          
SEQRES   9 J  154  ILE SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR          
SEQRES  10 J  154  LEU VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY          
SEQRES  11 J  154  GLY ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER          
SEQRES  12 J  154  ARG LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                  
HET    ACE  A   0       3                                                       
HET    ACE  B   0       3                                                       
HET    ACE  C   0       3                                                       
HET    ACE  D   0       3                                                       
HET    ACE  E   0       3                                                       
HET    ACE  F   0       3                                                       
HET    ACE  G   0       3                                                       
HET    ACE  H   0       3                                                       
HET    ACE  I   0       3                                                       
HET    ACE  J   0       3                                                       
HET     CU  A 154       1                                                       
HET     ZN  A 155       1                                                       
HET     CU  B 154       1                                                       
HET     ZN  B 155       1                                                       
HET    GOL  B 156       6                                                       
HET     CU  C 154       1                                                       
HET     ZN  C 155       1                                                       
HET     CU  D 154       1                                                       
HET     ZN  D 155       1                                                       
HET     CU  E 154       1                                                       
HET     ZN  E 155       1                                                       
HET     CU  F 154       1                                                       
HET     ZN  F 155       1                                                       
HET     CU  G 154       1                                                       
HET     ZN  G 155       1                                                       
HET     CU  H 154       1                                                       
HET     ZN  H 155       1                                                       
HET    MLI  H 156       7                                                       
HET     CU  I 154       1                                                       
HET     ZN  I 155       1                                                       
HET     CU  J 154       1                                                       
HET     ZN  J 155       1                                                       
HET    GOL  J 156       6                                                       
HETNAM     ACE ACETYL GROUP                                                     
HETNAM      CU COPPER (II) ION                                                  
HETNAM      ZN ZINC ION                                                         
HETNAM     GOL GLYCEROL                                                         
HETNAM     MLI MALONATE ION                                                     
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   1  ACE    10(C2 H4 O)                                                  
FORMUL  11   CU    10(CU 2+)                                                    
FORMUL  12   ZN    10(ZN 2+)                                                    
FORMUL  15  GOL    2(C3 H8 O3)                                                  
FORMUL  28  MLI    C3 H2 O4 2-                                                  
FORMUL  34  HOH   *1621(H2 O)                                                   
HELIX    1   1 ALA A   55  GLY A   61  5                                   7    
HELIX    2   2 ASN A  131  GLY A  138  1                                   8    
HELIX    3   3 ALA B   55  GLY B   61  5                                   7    
HELIX    4   4 SER B  107  CYS B  111  5                                   5    
HELIX    5   5 GLU B  132  LYS B  136  5                                   5    
HELIX    6   6 ALA C   55  GLY C   61  5                                   7    
HELIX    7   7 GLU C  133  GLY C  138  1                                   6    
HELIX    8   8 ALA D   55  GLY D   61  5                                   7    
HELIX    9   9 SER D  107  CYS D  111  5                                   5    
HELIX   10  10 ASN D  131  GLY D  138  1                                   8    
HELIX   11  11 ALA E   55  GLY E   61  5                                   7    
HELIX   12  12 GLU E  132  LYS E  136  5                                   5    
HELIX   13  13 ALA F   55  GLY F   61  5                                   7    
HELIX   14  14 SER F  107  CYS F  111  5                                   5    
HELIX   15  15 GLU F  133  GLY F  138  1                                   6    
HELIX   16  16 ALA G   55  GLY G   61  5                                   7    
HELIX   17  17 GLU G  132  LYS G  136  5                                   5    
HELIX   18  18 ALA H   55  GLY H   61  5                                   7    
HELIX   19  19 GLU H  133  GLY H  138  1                                   6    
HELIX   20  20 ALA I   55  GLY I   61  5                                   7    
HELIX   21  21 GLU I  133  GLY I  138  1                                   6    
HELIX   22  22 ALA J   55  GLY J   61  5                                   7    
HELIX   23  23 ASN J  131  LYS J  136  5                                   6    
SHEET    1   A 5 VAL A  94  ASP A 101  0                                        
SHEET    2   A 5 VAL A  29  LYS A  36 -1  N  VAL A  29   O  ASP A 101           
SHEET    3   A 5 GLN A  15  GLU A  21 -1  N  ASN A  19   O  TRP A  32           
SHEET    4   A 5 LYS A   3  LEU A   8 -1  N  CYS A   6   O  ILE A  18           
SHEET    5   A 5 GLY A 150  ILE A 151 -1  O  GLY A 150   N  VAL A   5           
SHEET    1   B 4 ASP A  83  ALA A  89  0                                        
SHEET    2   B 4 GLY A  41  HIS A  48 -1  N  GLY A  41   O  ALA A  89           
SHEET    3   B 4 THR A 116  HIS A 120 -1  O  THR A 116   N  HIS A  48           
SHEET    4   B 4 ARG A 143  VAL A 148 -1  O  ALA A 145   N  VAL A 119           
SHEET    1   C 5 ALA B  95  ASP B 101  0                                        
SHEET    2   C 5 VAL B  29  LYS B  36 -1  N  VAL B  29   O  ASP B 101           
SHEET    3   C 5 GLN B  15  GLU B  21 -1  N  ASN B  19   O  TRP B  32           
SHEET    4   C 5 LYS B   3  LEU B   8 -1  N  CYS B   6   O  ILE B  18           
SHEET    5   C 5 GLY B 150  ILE B 151 -1  O  GLY B 150   N  VAL B   5           
SHEET    1   D 4 ASP B  83  ALA B  89  0                                        
SHEET    2   D 4 GLY B  41  HIS B  48 -1  N  GLY B  41   O  ALA B  89           
SHEET    3   D 4 THR B 116  HIS B 120 -1  O  THR B 116   N  HIS B  48           
SHEET    4   D 4 ARG B 143  VAL B 148 -1  O  ALA B 145   N  VAL B 119           
SHEET    1   E 5 ALA C  95  ASP C 101  0                                        
SHEET    2   E 5 VAL C  29  LYS C  36 -1  N  VAL C  29   O  ASP C 101           
SHEET    3   E 5 GLN C  15  GLU C  21 -1  N  ASN C  19   O  TRP C  32           
SHEET    4   E 5 LYS C   3  LEU C   8 -1  N  LEU C   8   O  GLY C  16           
SHEET    5   E 5 GLY C 150  ILE C 151 -1  O  GLY C 150   N  VAL C   5           
SHEET    1   F 4 ASP C  83  ALA C  89  0                                        
SHEET    2   F 4 GLY C  41  HIS C  48 -1  N  GLY C  41   O  ALA C  89           
SHEET    3   F 4 THR C 116  HIS C 120 -1  O  THR C 116   N  HIS C  48           
SHEET    4   F 4 ARG C 143  VAL C 148 -1  O  GLY C 147   N  LEU C 117           
SHEET    1   G 5 ALA D  95  ASP D 101  0                                        
SHEET    2   G 5 VAL D  29  LYS D  36 -1  N  VAL D  31   O  ILE D  99           
SHEET    3   G 5 GLN D  15  GLU D  21 -1  N  ASN D  19   O  TRP D  32           
SHEET    4   G 5 LYS D   3  LEU D   8 -1  N  CYS D   6   O  ILE D  18           
SHEET    5   G 5 GLY D 150  ILE D 151 -1  O  GLY D 150   N  VAL D   5           
SHEET    1   H 4 ASP D  83  ALA D  89  0                                        
SHEET    2   H 4 GLY D  41  HIS D  48 -1  N  PHE D  45   O  GLY D  85           
SHEET    3   H 4 THR D 116  HIS D 120 -1  O  THR D 116   N  HIS D  48           
SHEET    4   H 4 ARG D 143  VAL D 148 -1  O  GLY D 147   N  LEU D 117           
SHEET    1   I 5 VAL E  94  ASP E 101  0                                        
SHEET    2   I 5 VAL E  29  LYS E  36 -1  N  VAL E  29   O  ASP E 101           
SHEET    3   I 5 GLN E  15  GLU E  21 -1  N  ASN E  19   O  TRP E  32           
SHEET    4   I 5 LYS E   3  LYS E   9 -1  N  LEU E   8   O  GLY E  16           
SHEET    5   I 5 GLY E 150  ILE E 151 -1  O  GLY E 150   N  VAL E   5           
SHEET    1   J 4 ASP E  83  ALA E  89  0                                        
SHEET    2   J 4 GLY E  41  HIS E  48 -1  N  GLY E  41   O  ALA E  89           
SHEET    3   J 4 THR E 116  HIS E 120 -1  O  THR E 116   N  HIS E  48           
SHEET    4   J 4 ARG E 143  VAL E 148 -1  O  ALA E 145   N  VAL E 119           
SHEET    1   K 5 VAL F  94  ASP F 101  0                                        
SHEET    2   K 5 VAL F  29  LYS F  36 -1  N  VAL F  31   O  ILE F  99           
SHEET    3   K 5 GLN F  15  GLU F  21 -1  N  ASN F  19   O  TRP F  32           
SHEET    4   K 5 LYS F   3  LEU F   8 -1  N  ALA F   4   O  PHE F  20           
SHEET    5   K 5 GLY F 150  ILE F 151 -1  O  GLY F 150   N  VAL F   5           
SHEET    1   L 4 ASP F  83  ALA F  89  0                                        
SHEET    2   L 4 GLY F  41  HIS F  48 -1  N  GLY F  41   O  ALA F  89           
SHEET    3   L 4 THR F 116  HIS F 120 -1  O  THR F 116   N  HIS F  48           
SHEET    4   L 4 ARG F 143  VAL F 148 -1  O  ALA F 145   N  VAL F 119           
SHEET    1   M 8 ASP G  83  ALA G  89  0                                        
SHEET    2   M 8 GLY G  41  HIS G  48 -1  N  GLY G  41   O  ALA G  89           
SHEET    3   M 8 THR G 116  HIS G 120 -1  O  THR G 116   N  HIS G  48           
SHEET    4   M 8 ARG G 143  ILE G 151 -1  O  GLY G 147   N  LEU G 117           
SHEET    5   M 8 LYS G   3  LEU G   8 -1  N  VAL G   5   O  GLY G 150           
SHEET    6   M 8 GLN G  15  GLN G  22 -1  O  GLY G  16   N  LEU G   8           
SHEET    7   M 8 VAL G  29  LYS G  36 -1  O  TRP G  32   N  ASN G  19           
SHEET    8   M 8 VAL G  94  ASP G 101 -1  O  VAL G  97   N  GLY G  33           
SHEET    1   N 5 VAL H  94  ASP H 101  0                                        
SHEET    2   N 5 VAL H  29  LYS H  36 -1  N  ILE H  35   O  ALA H  95           
SHEET    3   N 5 GLN H  15  GLN H  22 -1  N  ASN H  19   O  TRP H  32           
SHEET    4   N 5 LYS H   3  LEU H   8 -1  N  LEU H   8   O  GLY H  16           
SHEET    5   N 5 GLY H 150  ILE H 151 -1  O  GLY H 150   N  VAL H   5           
SHEET    1   O 4 ASP H  83  ALA H  89  0                                        
SHEET    2   O 4 GLY H  41  HIS H  48 -1  N  GLY H  41   O  ALA H  89           
SHEET    3   O 4 THR H 116  HIS H 120 -1  O  THR H 116   N  HIS H  48           
SHEET    4   O 4 ARG H 143  VAL H 148 -1  O  GLY H 147   N  LEU H 117           
SHEET    1   P 5 ALA I  95  ASP I 101  0                                        
SHEET    2   P 5 VAL I  29  LYS I  36 -1  N  VAL I  29   O  ASP I 101           
SHEET    3   P 5 GLN I  15  GLN I  22 -1  N  ASN I  19   O  TRP I  32           
SHEET    4   P 5 LYS I   3  LYS I   9 -1  N  LEU I   8   O  GLY I  16           
SHEET    5   P 5 GLY I 150  ILE I 151 -1  O  GLY I 150   N  VAL I   5           
SHEET    1   Q 4 ASP I  83  ALA I  89  0                                        
SHEET    2   Q 4 GLY I  41  HIS I  48 -1  N  GLY I  41   O  ALA I  89           
SHEET    3   Q 4 THR I 116  HIS I 120 -1  O  THR I 116   N  HIS I  48           
SHEET    4   Q 4 ARG I 143  VAL I 148 -1  O  ALA I 145   N  VAL I 119           
SHEET    1   R 5 ALA J  95  ASP J 101  0                                        
SHEET    2   R 5 VAL J  29  LYS J  36 -1  N  VAL J  31   O  ILE J  99           
SHEET    3   R 5 GLN J  15  GLU J  21 -1  N  ASN J  19   O  TRP J  32           
SHEET    4   R 5 LYS J   3  LYS J   9 -1  N  LEU J   8   O  GLY J  16           
SHEET    5   R 5 GLY J 150  ILE J 151 -1  O  GLY J 150   N  VAL J   5           
SHEET    1   S 4 ASP J  83  ALA J  89  0                                        
SHEET    2   S 4 GLY J  41  HIS J  48 -1  N  GLY J  41   O  ALA J  89           
SHEET    3   S 4 THR J 116  HIS J 120 -1  O  THR J 116   N  HIS J  48           
SHEET    4   S 4 ARG J 143  VAL J 148 -1  O  GLY J 147   N  LEU J 117           
SSBOND   1 CYS A   57    CYS A  146                          1555   1555  2.60  
SSBOND   2 CYS B   57    CYS B  146                          1555   1555  2.61  
SSBOND   3 CYS C   57    CYS C  146                          1555   1555  2.67  
SSBOND   4 CYS D   57    CYS D  146                          1555   1555  2.61  
SSBOND   5 CYS E   57    CYS E  146                          1555   1555  2.67  
SSBOND   6 CYS F   57    CYS F  146                          1555   1555  2.60  
SSBOND   7 CYS G   57    CYS G  146                          1555   1555  2.62  
SSBOND   8 CYS H   57    CYS H  146                          1555   1555  2.65  
SSBOND   9 CYS I   57    CYS I  146                          1555   1555  2.77  
SSBOND  10 CYS J   57    CYS J  146                          1555   1555  2.64  
LINK         C   ACE A   0                 N   ALA A   1     1555   1555  1.33  
LINK         C   ACE B   0                 N   ALA B   1     1555   1555  1.34  
LINK         C   ACE C   0                 N   ALA C   1     1555   1555  1.34  
LINK         C   ACE D   0                 N   ALA D   1     1555   1555  1.34  
LINK         C   ACE E   0                 N   ALA E   1     1555   1555  1.34  
LINK         C   ACE F   0                 N   ALA F   1     1555   1555  1.34  
LINK         C   ACE G   0                 N   ALA G   1     1555   1555  1.36  
LINK         C   ACE H   0                 N   ALA H   1     1555   1555  1.34  
LINK         C   ACE I   0                 N   ALA I   1     1555   1555  1.35  
LINK         C   ACE J   0                 N   ALA J   1     1555   1555  1.34  
LINK         ND1 HIS A  46                CU    CU A 154     1555   1555  2.30  
LINK         NE2 HIS A  48                CU    CU A 154     1555   1555  2.05  
LINK         ND1 HIS A  63                ZN    ZN A 155     1555   1555  2.14  
LINK         ND1 HIS A  71                ZN    ZN A 155     1555   1555  2.13  
LINK         ND1 HIS A  80                ZN    ZN A 155     1555   1555  2.07  
LINK         OD1 ASP A  83                ZN    ZN A 155     1555   1555  1.89  
LINK         NE2 HIS A 120                CU    CU A 154     1555   1555  2.00  
LINK         ND1 HIS B  46                CU    CU B 154     1555   1555  2.24  
LINK         NE2 HIS B  48                CU    CU B 154     1555   1555  2.06  
LINK         ND1 HIS B  63                ZN    ZN B 155     1555   1555  2.06  
LINK         ND1 HIS B  71                ZN    ZN B 155     1555   1555  2.06  
LINK         ND1 HIS B  80                ZN    ZN B 155     1555   1555  2.11  
LINK         OD1 ASP B  83                ZN    ZN B 155     1555   1555  1.94  
LINK         NE2 HIS B 120                CU    CU B 154     1555   1555  2.06  
LINK         ND1 HIS C  46                CU    CU C 154     1555   1555  2.32  
LINK         NE2 HIS C  48                CU    CU C 154     1555   1555  2.10  
LINK         ND1 HIS C  63                ZN    ZN C 155     1555   1555  2.34  
LINK         ND1 HIS C  71                ZN    ZN C 155     1555   1555  2.22  
LINK         ND1 HIS C  80                ZN    ZN C 155     1555   1555  2.00  
LINK         OD1 ASP C  83                ZN    ZN C 155     1555   1555  2.05  
LINK         NE2 HIS C 120                CU    CU C 154     1555   1555  2.10  
LINK         ND1 HIS D  46                CU    CU D 154     1555   1555  2.20  
LINK         NE2 HIS D  48                CU    CU D 154     1555   1555  2.15  
LINK         ND1 HIS D  63                ZN    ZN D 155     1555   1555  2.16  
LINK         ND1 HIS D  71                ZN    ZN D 155     1555   1555  2.09  
LINK         ND1 HIS D  80                ZN    ZN D 155     1555   1555  2.12  
LINK         OD1 ASP D  83                ZN    ZN D 155     1555   1555  2.07  
LINK         NE2 HIS D 120                CU    CU D 154     1555   1555  2.12  
LINK         ND1 HIS E  46                CU    CU E 154     1555   1555  2.27  
LINK         NE2 HIS E  48                CU    CU E 154     1555   1555  2.09  
LINK         ND1 HIS E  63                ZN    ZN E 155     1555   1555  2.07  
LINK         ND1 HIS E  71                ZN    ZN E 155     1555   1555  2.07  
LINK         ND1 HIS E  80                ZN    ZN E 155     1555   1555  2.08  
LINK         OD1 ASP E  83                ZN    ZN E 155     1555   1555  1.97  
LINK         NE2 HIS E 120                CU    CU E 154     1555   1555  2.06  
LINK         ND1 HIS F  46                CU    CU F 154     1555   1555  2.27  
LINK         NE2 HIS F  48                CU    CU F 154     1555   1555  2.11  
LINK         ND1 HIS F  63                ZN    ZN F 155     1555   1555  2.02  
LINK         ND1 HIS F  71                ZN    ZN F 155     1555   1555  2.22  
LINK         ND1 HIS F  80                ZN    ZN F 155     1555   1555  2.19  
LINK         OD1 ASP F  83                ZN    ZN F 155     1555   1555  1.88  
LINK         NE2 HIS F 120                CU    CU F 154     1555   1555  2.17  
LINK         ND1 HIS G  46                CU    CU G 154     1555   1555  2.30  
LINK         NE2 HIS G  48                CU    CU G 154     1555   1555  2.02  
LINK         ND1 HIS G  63                ZN    ZN G 155     1555   1555  2.16  
LINK         ND1 HIS G  71                ZN    ZN G 155     1555   1555  2.10  
LINK         ND1 HIS G  80                ZN    ZN G 155     1555   1555  2.10  
LINK         OD1 ASP G  83                ZN    ZN G 155     1555   1555  1.97  
LINK         NE2 HIS G 120                CU    CU G 154     1555   1555  1.98  
LINK         ND1 HIS H  46                CU    CU H 154     1555   1555  2.20  
LINK         NE2 HIS H  48                CU    CU H 154     1555   1555  2.14  
LINK         ND1 HIS H  63                ZN    ZN H 155     1555   1555  2.06  
LINK         ND1 HIS H  71                ZN    ZN H 155     1555   1555  2.10  
LINK         ND1 HIS H  80                ZN    ZN H 155     1555   1555  2.04  
LINK         OD1 ASP H  83                ZN    ZN H 155     1555   1555  2.00  
LINK         NE2 HIS H 120                CU    CU H 154     1555   1555  2.05  
LINK         ND1 HIS I  46                CU    CU I 154     1555   1555  2.23  
LINK         NE2 HIS I  48                CU    CU I 154     1555   1555  2.22  
LINK         ND1 HIS I  63                ZN    ZN I 155     1555   1555  2.08  
LINK         ND1 HIS I  71                ZN    ZN I 155     1555   1555  2.36  
LINK         ND1 HIS I  80                ZN    ZN I 155     1555   1555  2.12  
LINK         OD1 ASP I  83                ZN    ZN I 155     1555   1555  2.01  
LINK         NE2 HIS I 120                CU    CU I 154     1555   1555  2.08  
LINK         ND1 HIS J  46                CU    CU J 154     1555   1555  2.25  
LINK         NE2 HIS J  48                CU    CU J 154     1555   1555  2.08  
LINK         ND1 HIS J  63                ZN    ZN J 155     1555   1555  2.18  
LINK         ND1 HIS J  71                ZN    ZN J 155     1555   1555  2.18  
LINK         ND1 HIS J  80                ZN    ZN J 155     1555   1555  2.02  
LINK         OD1 ASP J  83                ZN    ZN J 155     1555   1555  2.02  
LINK         NE2 HIS J 120                CU    CU J 154     1555   1555  2.10  
LINK         NE2 HIS I  63                CU    CU I 154     1555   1555  2.59  
LINK         NE2 HIS A  63                CU    CU A 154     1555   1555  2.66  
SITE     1 AC1  5 HIS A  46  HIS A  48  HIS A  63  HIS A 120                    
SITE     2 AC1  5 HOH A 679                                                     
SITE     1 AC2  4 HIS A  63  HIS A  71  HIS A  80  ASP A  83                    
SITE     1 AC3  4 HIS B  46  HIS B  48  HIS B  63  HIS B 120                    
SITE     1 AC4  4 HIS B  63  HIS B  71  HIS B  80  ASP B  83                    
SITE     1 AC5  4 HIS C  46  HIS C  48  HIS C  63  HIS C 120                    
SITE     1 AC6  4 HIS C  63  HIS C  71  HIS C  80  ASP C  83                    
SITE     1 AC7  4 HIS D  46  HIS D  48  HIS D  63  HIS D 120                    
SITE     1 AC8  4 HIS D  63  HIS D  71  HIS D  80  ASP D  83                    
SITE     1 AC9  4 HIS E  46  HIS E  48  HIS E  63  HIS E 120                    
SITE     1 BC1  5 HIS E  63  HIS E  71  HIS E  80  ASP E  83                    
SITE     2 BC1  5 LYS E 136                                                     
SITE     1 BC2  4 HIS F  46  HIS F  48  HIS F  63  HIS F 120                    
SITE     1 BC3  5 HIS F  63  HIS F  71  HIS F  80  ASP F  83                    
SITE     2 BC3  5 LYS F 136                                                     
SITE     1 BC4  4 HIS G  46  HIS G  48  HIS G  63  HIS G 120                    
SITE     1 BC5  4 HIS G  63  HIS G  71  HIS G  80  ASP G  83                    
SITE     1 BC6  4 HIS H  46  HIS H  48  HIS H  63  HIS H 120                    
SITE     1 BC7  4 HIS H  63  HIS H  71  HIS H  80  ASP H  83                    
SITE     1 BC8  5 HIS I  46  HIS I  48  HIS I  63  HIS I 120                    
SITE     2 BC8  5 HOH I 394                                                     
SITE     1 BC9  4 HIS I  63  HIS I  71  HIS I  80  ASP I  83                    
SITE     1 CC1  4 HIS J  46  HIS J  48  HIS J  63  HIS J 120                    
SITE     1 CC2  4 HIS J  63  HIS J  71  HIS J  80  ASP J  83                    
SITE     1 CC3 10 LEU G  67  ARG G  69  PHE H  64  PRO H  66                    
SITE     2 CC3 10 VAL H 103  ILE H 104  SER H 105  CYS H 111                    
SITE     3 CC3 10 ILE H 112  HOH H 160                                          
SITE     1 CC4  7 HIS B  48  HIS B  63  HIS B 120  GLY B 141                    
SITE     2 CC4  7 ARG B 143  HOH B 381  HOH B 493                               
SITE     1 CC5  8 HIS J  48  HIS J  63  HIS J 120  THR J 137                    
SITE     2 CC5  8 GLY J 141  ARG J 143  HOH J 167  HOH J1325                    
CRYST1  166.148  203.263  143.319  90.00  90.00  90.00 C 2 2 21     80          
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      0.006019  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.004920  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006977        0.00000                         
HETATM    1  C   ACE A   0      54.923  48.666  30.354  1.00 40.25           C  
HETATM    2  O   ACE A   0      55.189  47.816  31.211  1.00 45.21           O  
HETATM    3  CH3 ACE A   0      55.477  50.062  30.363  1.00 35.59           C  
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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