GenomeNet

Database: PDB
Entry: 2HYE
LinkDB: 2HYE
Original site: 2HYE 
HEADER    PROTEIN BINDING                         05-AUG-06   2HYE              
TITLE     CRYSTAL STRUCTURE OF THE DDB1-CUL4A-RBX1-SV5V COMPLEX                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: DNA DAMAGE-BINDING PROTEIN 1;                              
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: DAMAGE-SPECIFIC DNA-BINDING PROTEIN 1, UV-DAMAGED DNA-      
COMPND   5 BINDING FACTOR, DDB P127 SUBUNIT, DDBA, UV-DAMAGED DNA-BINDING       
COMPND   6 PROTEIN 1, UV-DDB 1, XERODERMA PIGMENTOSUM GROUP E- COMPLEMENTING    
COMPND   7 PROTEIN, XPCE, XPE-BINDING FACTOR, XPE-BF, X- ASSOCIATED PROTEIN 1,  
COMPND   8 XAP-1;                                                               
COMPND   9 ENGINEERED: YES;                                                     
COMPND  10 MOL_ID: 2;                                                           
COMPND  11 MOLECULE: NONSTRUCTURAL PROTEIN V;                                   
COMPND  12 CHAIN: B;                                                            
COMPND  13 ENGINEERED: YES;                                                     
COMPND  14 MOL_ID: 3;                                                           
COMPND  15 MOLECULE: CULLIN-4A;                                                 
COMPND  16 CHAIN: C;                                                            
COMPND  17 SYNONYM: CUL-4A;                                                     
COMPND  18 ENGINEERED: YES;                                                     
COMPND  19 MOL_ID: 4;                                                           
COMPND  20 MOLECULE: RING-BOX PROTEIN 1;                                        
COMPND  21 CHAIN: D;                                                            
COMPND  22 SYNONYM: RBX1, REGULATOR OF CULLINS 1, RING FINGER PROTEIN 75, ZYP   
COMPND  23 PROTEIN;                                                             
COMPND  24 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: DDB1;                                                          
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: SIMIAN VIRUS 5;                                 
SOURCE  11 ORGANISM_TAXID: 11207;                                               
SOURCE  12 GENE: P/V;                                                           
SOURCE  13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  15 MOL_ID: 3;                                                           
SOURCE  16 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  17 ORGANISM_COMMON: HUMAN;                                              
SOURCE  18 ORGANISM_TAXID: 9606;                                                
SOURCE  19 GENE: CUL4A;                                                         
SOURCE  20 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  21 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  22 MOL_ID: 4;                                                           
SOURCE  23 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  24 ORGANISM_COMMON: HUMAN;                                              
SOURCE  25 ORGANISM_TAXID: 9606;                                                
SOURCE  26 GENE: RBX1;                                                          
SOURCE  27 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  28 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    BETA PROPELLER, RING FINGER, ZINC FINGER, PROPELLER CLUSTER, HELICAL  
KEYWDS   2 REPEATS, CULLIN REPEATS, PROTEIN BINDING                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.ANGERS,T.LI,X.YI,M.J.MACCOSS,R.T.MOON,N.ZHENG                       
REVDAT   4   18-OCT-17 2HYE    1       REMARK                                   
REVDAT   3   24-FEB-09 2HYE    1       VERSN                                    
REVDAT   2   30-OCT-07 2HYE    1       JRNL                                     
REVDAT   1   03-OCT-06 2HYE    0                                                
JRNL        AUTH   S.ANGERS,T.LI,X.YI,M.J.MACCOSS,R.T.MOON,N.ZHENG              
JRNL        TITL   MOLECULAR ARCHITECTURE AND ASSEMBLY OF THE DDB1-CUL4A        
JRNL        TITL 2 UBIQUITIN LIGASE MACHINERY.                                  
JRNL        REF    NATURE                        V. 443   590 2006              
JRNL        REFN                   ISSN 0028-0836                               
JRNL        PMID   16964240                                                     
JRNL        DOI    10.1038/NATURE05175                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS                                                  
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 59833                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.250                           
REMARK   3   FREE R VALUE                     : 0.316                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 56809                           
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 16938                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 5                                       
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 75.92                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : NULL                            
REMARK   3   BOND ANGLES            (DEGREES) : NULL                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : NULL                                                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2HYE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-AUG-06.                  
REMARK 100 THE DEPOSITION ID IS D_1000038907.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : 8.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 8.2.2                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 62466                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.100                              
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     (%) : 92.0                               
REMARK 200  DATA REDUNDANCY                : 5.400                              
REMARK 200  R MERGE                    (I) : 0.07900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.21                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 62.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.40600                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 65.68                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.58                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM NAHEPES, 7-9% PEG4000, 10% ISO     
REMARK 280  -PROPANOL, 5MM DTT, PH 8.0, VAPOR DIFFUSION, HANGING DROP,          
REMARK 280  TEMPERATURE 277K                                                    
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      212.43750            
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      212.43750            
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       41.72600            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000      101.58250            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       41.72600            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000      101.58250            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000      212.43750            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       41.72600            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000      101.58250            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000      212.43750            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       41.72600            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000      101.58250            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
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: TETRAMERIC                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, 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 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET B     1                                                      
REMARK 465     ASP B     2                                                      
REMARK 465     PRO B     3                                                      
REMARK 465     THR B     4                                                      
REMARK 465     ASP B     5                                                      
REMARK 465     LEU B     6                                                      
REMARK 465     SER B     7                                                      
REMARK 465     PHE B     8                                                      
REMARK 465     SER B     9                                                      
REMARK 465     ALA B    55                                                      
REMARK 465     GLU B    56                                                      
REMARK 465     ALA B    57                                                      
REMARK 465     LYS B    58                                                      
REMARK 465     ILE B    59                                                      
REMARK 465     GLN B    60                                                      
REMARK 465     GLU B    61                                                      
REMARK 465     SER B    62                                                      
REMARK 465     THR B    63                                                      
REMARK 465     ASN B    64                                                      
REMARK 465     HIS B    65                                                      
REMARK 465     GLN B    66                                                      
REMARK 465     LYS B    67                                                      
REMARK 465     GLY B    68                                                      
REMARK 465     SER B    69                                                      
REMARK 465     VAL B    70                                                      
REMARK 465     GLY B    71                                                      
REMARK 465     GLY B    72                                                      
REMARK 465     GLY B    73                                                      
REMARK 465     ALA B    74                                                      
REMARK 465     LYS B    75                                                      
REMARK 465     PRO B    76                                                      
REMARK 465     LYS B    77                                                      
REMARK 465     LYS B    78                                                      
REMARK 465     PRO B    79                                                      
REMARK 465     ARG B    80                                                      
REMARK 465     ILE B   153                                                      
REMARK 465     ALA B   154                                                      
REMARK 465     THR B   155                                                      
REMARK 465     SER B   156                                                      
REMARK 465     SER B   157                                                      
REMARK 465     PRO B   158                                                      
REMARK 465     ILE B   159                                                      
REMARK 465     MET C     1                                                      
REMARK 465     ALA C     2                                                      
REMARK 465     ASP C     3                                                      
REMARK 465     GLU C     4                                                      
REMARK 465     ALA C     5                                                      
REMARK 465     PRO C     6                                                      
REMARK 465     ARG C     7                                                      
REMARK 465     LYS C     8                                                      
REMARK 465     GLY C     9                                                      
REMARK 465     SER C    10                                                      
REMARK 465     PHE C    11                                                      
REMARK 465     SER C    12                                                      
REMARK 465     ALA C    13                                                      
REMARK 465     LEU C    14                                                      
REMARK 465     VAL C    15                                                      
REMARK 465     GLY C    16                                                      
REMARK 465     ARG C    17                                                      
REMARK 465     THR C    18                                                      
REMARK 465     ASN C    19                                                      
REMARK 465     GLY C    20                                                      
REMARK 465     LEU C    21                                                      
REMARK 465     THR C    22                                                      
REMARK 465     LYS C    23                                                      
REMARK 465     PRO C    24                                                      
REMARK 465     ALA C    25                                                      
REMARK 465     ALA C    26                                                      
REMARK 465     LEU C    27                                                      
REMARK 465     ALA C    28                                                      
REMARK 465     ALA C    29                                                      
REMARK 465     ALA C    30                                                      
REMARK 465     PRO C    31                                                      
REMARK 465     ALA C    32                                                      
REMARK 465     LYS C    33                                                      
REMARK 465     PRO C    34                                                      
REMARK 465     GLY C    35                                                      
REMARK 465     GLY C    36                                                      
REMARK 465     ALA C    37                                                      
REMARK 465     GLY C    38                                                      
REMARK 465     GLY C    39                                                      
REMARK 465     SER C    40                                                      
REMARK 465     MET D     1                                                      
REMARK 465     ALA D     2                                                      
REMARK 465     ALA D     3                                                      
REMARK 465     ALA D     4                                                      
REMARK 465     MET D     5                                                      
REMARK 465     ASP D     6                                                      
REMARK 465     VAL D     7                                                      
REMARK 465     ASP D     8                                                      
REMARK 465     THR D     9                                                      
REMARK 465     PRO D    10                                                      
REMARK 465     SER D    11                                                      
REMARK 465     GLY D    12                                                      
REMARK 465     THR D    13                                                      
REMARK 465     ASN D    14                                                      
REMARK 465     SER D    15                                                      
REMARK 465     GLY D    16                                                      
REMARK 465     ALA D    17                                                      
REMARK 465     GLY D    18                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
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   O    LYS C   416     OE2  GLU C   423              1.40            
REMARK 500   O    THR A   745     O    SER A   746              1.50            
REMARK 500   ND1  HIS A   189     O    GLU A   210              1.85            
REMARK 500   O    ALA A   381     CB   SER A   720              1.90            
REMARK 500   ND2  ASN D    41     O    ASN D    47              1.98            
REMARK 500   O    ALA A   381     OG   SER A   720              1.99            
REMARK 500   O    ASN A   149     O    GLU A   151              2.04            
REMARK 500   C    ASN A   149     O    GLU A   151              2.14            
REMARK 500   O    MET C   148     OG   SER C   151              2.17            
REMARK 500   CE1  PHE A   226     O    GLY A   268              2.17            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   NE2  GLN C    60     NE2  GLN C    60     3554     2.09            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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    GLU A 151   N   -  CA  -  C   ANGL. DEV. = -44.9 DEGREES          
REMARK 500    PRO A 266   CA  -  N   -  CD  ANGL. DEV. = -13.2 DEGREES          
REMARK 500    PHE A 382   CB  -  CG  -  CD2 ANGL. DEV. =  -5.7 DEGREES          
REMARK 500    PHE A 382   CB  -  CG  -  CD1 ANGL. DEV. =   4.8 DEGREES          
REMARK 500    PRO A 412   C   -  N   -  CA  ANGL. DEV. =  11.4 DEGREES          
REMARK 500    TRP A 561   CB  -  CA  -  C   ANGL. DEV. = -31.0 DEGREES          
REMARK 500    TRP A 561   N   -  CA  -  C   ANGL. DEV. =  42.0 DEGREES          
REMARK 500    THR A 562   N   -  CA  -  CB  ANGL. DEV. = -11.9 DEGREES          
REMARK 500    SER A 624   N   -  CA  -  C   ANGL. DEV. =  18.8 DEGREES          
REMARK 500    PRO A 656   C   -  N   -  CA  ANGL. DEV. =   9.5 DEGREES          
REMARK 500    PRO A 688   CA  -  N   -  CD  ANGL. DEV. =  -8.5 DEGREES          
REMARK 500    PRO A 688   N   -  CA  -  C   ANGL. DEV. =  17.1 DEGREES          
REMARK 500    ASP A 689   N   -  CA  -  C   ANGL. DEV. = -17.4 DEGREES          
REMARK 500    SER A 767   CB  -  CA  -  C   ANGL. DEV. = -21.2 DEGREES          
REMARK 500    SER A 767   N   -  CA  -  C   ANGL. DEV. = -32.3 DEGREES          
REMARK 500    THR A 916   CB  -  CA  -  C   ANGL. DEV. = -23.3 DEGREES          
REMARK 500    THR A 916   N   -  CA  -  C   ANGL. DEV. =  26.5 DEGREES          
REMARK 500    LYS A 917   N   -  CA  -  CB  ANGL. DEV. = -11.0 DEGREES          
REMARK 500    THR A1020   N   -  CA  -  C   ANGL. DEV. =  16.5 DEGREES          
REMARK 500    PRO A1023   CA  -  N   -  CD  ANGL. DEV. = -15.0 DEGREES          
REMARK 500    TYR A1114   N   -  CA  -  C   ANGL. DEV. =  21.4 DEGREES          
REMARK 500    ASP A1115   C   -  N   -  CA  ANGL. DEV. =  23.1 DEGREES          
REMARK 500    ASP A1115   N   -  CA  -  C   ANGL. DEV. =  28.5 DEGREES          
REMARK 500    PRO B  10   CA  -  N   -  CD  ANGL. DEV. = -24.6 DEGREES          
REMARK 500    SER B 107   N   -  CA  -  C   ANGL. DEV. = -27.6 DEGREES          
REMARK 500    PRO B 109   C   -  N   -  CD  ANGL. DEV. = -16.1 DEGREES          
REMARK 500    PRO B 109   CA  -  N   -  CD  ANGL. DEV. = -21.9 DEGREES          
REMARK 500    GLU B 150   CB  -  CA  -  C   ANGL. DEV. =  13.8 DEGREES          
REMARK 500    PRO B 152   CA  -  N   -  CD  ANGL. DEV. = -14.0 DEGREES          
REMARK 500    TRP B 179   CB  -  CA  -  C   ANGL. DEV. = -24.8 DEGREES          
REMARK 500    LEU C  83   N   -  CA  -  C   ANGL. DEV. =  16.9 DEGREES          
REMARK 500    GLU C  84   N   -  CA  -  CB  ANGL. DEV. = -10.9 DEGREES          
REMARK 500    LEU C 126   CB  -  CA  -  C   ANGL. DEV. = -22.6 DEGREES          
REMARK 500    LEU C 126   N   -  CA  -  C   ANGL. DEV. =  20.8 DEGREES          
REMARK 500    PRO C 168   C   -  N   -  CA  ANGL. DEV. =  10.3 DEGREES          
REMARK 500    HIS C 181   CB  -  CA  -  C   ANGL. DEV. =  14.2 DEGREES          
REMARK 500    ILE C 182   N   -  CA  -  C   ANGL. DEV. =  25.1 DEGREES          
REMARK 500    GLY C 206   N   -  CA  -  C   ANGL. DEV. =  17.3 DEGREES          
REMARK 500    HIS C 298   CB  -  CA  -  C   ANGL. DEV. = -21.4 DEGREES          
REMARK 500    ASN C 421   C   -  N   -  CA  ANGL. DEV. =  18.8 DEGREES          
REMARK 500    ALA C 616   N   -  CA  -  C   ANGL. DEV. =  17.4 DEGREES          
REMARK 500    PHE D  22   CB  -  CA  -  C   ANGL. DEV. = -25.8 DEGREES          
REMARK 500    PHE D  22   CB  -  CG  -  CD1 ANGL. DEV. =  -4.4 DEGREES          
REMARK 500    CYS D  42   N   -  CA  -  C   ANGL. DEV. = -19.7 DEGREES          
REMARK 500    CYS D  45   CA  -  CB  -  SG  ANGL. DEV. =  11.7 DEGREES          
REMARK 500    ASN D  47   N   -  CA  -  C   ANGL. DEV. = -16.9 DEGREES          
REMARK 500    CYS D  75   CA  -  CB  -  SG  ANGL. DEV. =   8.5 DEGREES          
REMARK 500    ASP D  97   CB  -  CA  -  C   ANGL. DEV. =  13.4 DEGREES          
REMARK 500    PHE D 103   CB  -  CA  -  C   ANGL. DEV. = -15.5 DEGREES          
REMARK 500    PHE D 103   CB  -  CG  -  CD2 ANGL. DEV. =   4.2 DEGREES          
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      53 ANGLE DEVIATIONS.                             
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  22       78.55   -107.65                                   
REMARK 500    ASN A  36      -72.48   -170.09                                   
REMARK 500    THR A  45      -57.67   -147.18                                   
REMARK 500    ALA A  46      -84.27   -173.29                                   
REMARK 500    TYR A  58       61.19   -101.77                                   
REMARK 500    ILE A  61      106.82    -49.35                                   
REMARK 500    CYS A  87      158.28    172.19                                   
REMARK 500    SER A  94       79.46   -108.87                                   
REMARK 500    ALA A 104      164.55    170.41                                   
REMARK 500    HIS A 105      143.54    175.10                                   
REMARK 500    ILE A 112     -123.13    -81.57                                   
REMARK 500    PRO A 115       90.30    -48.29                                   
REMARK 500    SER A 116      156.77    -44.10                                   
REMARK 500    THR A 118       -4.72     77.03                                   
REMARK 500    LEU A 135      -67.82    -93.66                                   
REMARK 500    LEU A 145       43.57    -86.33                                   
REMARK 500    ARG A 147       29.61    -58.71                                   
REMARK 500    ASP A 148       17.11   -156.49                                   
REMARK 500    ASN A 149       56.44    -94.30                                   
REMARK 500    LYS A 153      137.26    -29.45                                   
REMARK 500    GLN A 186       12.80    -69.21                                   
REMARK 500    ASN A 203      -81.99    -98.21                                   
REMARK 500    LYS A 204      114.49    177.22                                   
REMARK 500    GLN A 209       85.27   -160.86                                   
REMARK 500    GLU A 213      117.63    -17.73                                   
REMARK 500    GLU A 224      -61.74    -18.57                                   
REMARK 500    GLU A 235       -6.23   -146.14                                   
REMARK 500    ASN A 241       38.36   -140.48                                   
REMARK 500    ALA A 247      139.13   -178.26                                   
REMARK 500    PRO A 266        0.73    -55.84                                   
REMARK 500    SER A 269      -78.08   -148.85                                   
REMARK 500    GLU A 277       20.15   -141.15                                   
REMARK 500    ARG A 279      155.24    -36.72                                   
REMARK 500    GLU A 286      108.59    -48.42                                   
REMARK 500    LYS A 287      179.89    -58.02                                   
REMARK 500    GLU A 288      105.70   -167.26                                   
REMARK 500    GLN A 290     -100.28    -66.73                                   
REMARK 500    MET A 291      -11.46   -146.36                                   
REMARK 500    ASP A 292      -14.55    177.05                                   
REMARK 500    THR A 294     -156.00   -162.23                                   
REMARK 500    LYS A 298     -103.47    -86.36                                   
REMARK 500    THR A 308     -145.48   -124.02                                   
REMARK 500    ALA A 311      103.96    -56.96                                   
REMARK 500    LEU A 317      -89.65   -119.37                                   
REMARK 500    SER A 340      115.94    -37.70                                   
REMARK 500    ASN A 341     -168.51    -76.77                                   
REMARK 500    ALA A 381      -68.14   -124.46                                   
REMARK 500    PHE A 382     -101.60   -104.55                                   
REMARK 500    ASP A 403       62.01   -107.81                                   
REMARK 500    LEU A 413     -164.58   -102.95                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     341 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                              ZN B3002  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 190   SG                                                     
REMARK 620 2 CYS B 215   SG  137.8                                              
REMARK 620 3 CYS B 218   SG   73.9  96.3                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B3001  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 194   SG                                                     
REMARK 620 2 CYS B 206   SG  160.7                                              
REMARK 620 3 CYS B 208   SG   49.2 144.6                                        
REMARK 620 4 CYS B 211   SG  102.4  94.7  80.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN D4001  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS D  42   SG                                                     
REMARK 620 2 CYS D  45   SG   59.8                                              
REMARK 620 3 CYS D  83   SG  109.0  54.1                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN D4003  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS D  53   SG                                                     
REMARK 620 2 CYS D  56   SG   80.0                                              
REMARK 620 3 CYS D  68   SG   88.9 125.6                                        
REMARK 620 4 HIS D  82   ND1 103.1  82.5 151.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN D4002  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS D  75   SG                                                     
REMARK 620 2 HIS D  77   ND1 126.2                                              
REMARK 620 3 CYS D  94   SG   52.6 152.5                                        
REMARK 620 4 ASP D  97   OD2  62.3  76.7  81.1                                  
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 ZN B 3001                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 3002                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 4001                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 4003                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 4002                 
DBREF  2HYE A    1  1140  UNP    Q16531   DDB1_HUMAN       1   1140             
DBREF  2HYE B    1   222  UNP    P11207   V_SV5            1    222             
DBREF  2HYE C    1   759  UNP    Q13619   CUL4A_HUMAN      1    759             
DBREF  2HYE D    1   108  UNP    P62877   RBX1_HUMAN       1    108             
SEQADV 2HYE TYR A  422  UNP  Q16531    ASP   422 CONFLICT                       
SEQADV 2HYE ASP A  898  UNP  Q16531    GLU   898 CONFLICT                       
SEQADV 2HYE VAL A  899  UNP  Q16531    LEU   899 CONFLICT                       
SEQRES   1 A 1140  MET SER TYR ASN TYR VAL VAL THR ALA GLN LYS PRO THR          
SEQRES   2 A 1140  ALA VAL ASN GLY CYS VAL THR GLY HIS PHE THR SER ALA          
SEQRES   3 A 1140  GLU ASP LEU ASN LEU LEU ILE ALA LYS ASN THR ARG LEU          
SEQRES   4 A 1140  GLU ILE TYR VAL VAL THR ALA GLU GLY LEU ARG PRO VAL          
SEQRES   5 A 1140  LYS GLU VAL GLY MET TYR GLY LYS ILE ALA VAL MET GLU          
SEQRES   6 A 1140  LEU PHE ARG PRO LYS GLY GLU SER LYS ASP LEU LEU PHE          
SEQRES   7 A 1140  ILE LEU THR ALA LYS TYR ASN ALA CYS ILE LEU GLU TYR          
SEQRES   8 A 1140  LYS GLN SER GLY GLU SER ILE ASP ILE ILE THR ARG ALA          
SEQRES   9 A 1140  HIS GLY ASN VAL GLN ASP ARG ILE GLY ARG PRO SER GLU          
SEQRES  10 A 1140  THR GLY ILE ILE GLY ILE ILE ASP PRO GLU CYS ARG MET          
SEQRES  11 A 1140  ILE GLY LEU ARG LEU TYR ASP GLY LEU PHE LYS VAL ILE          
SEQRES  12 A 1140  PRO LEU ASP ARG ASP ASN LYS GLU LEU LYS ALA PHE ASN          
SEQRES  13 A 1140  ILE ARG LEU GLU GLU LEU HIS VAL ILE ASP VAL LYS PHE          
SEQRES  14 A 1140  LEU TYR GLY CYS GLN ALA PRO THR ILE CYS PHE VAL TYR          
SEQRES  15 A 1140  GLN ASP PRO GLN GLY ARG HIS VAL LYS THR TYR GLU VAL          
SEQRES  16 A 1140  SER LEU ARG GLU LYS GLU PHE ASN LYS GLY PRO TRP LYS          
SEQRES  17 A 1140  GLN GLU ASN VAL GLU ALA GLU ALA SER MET VAL ILE ALA          
SEQRES  18 A 1140  VAL PRO GLU PRO PHE GLY GLY ALA ILE ILE ILE GLY GLN          
SEQRES  19 A 1140  GLU SER ILE THR TYR HIS ASN GLY ASP LYS TYR LEU ALA          
SEQRES  20 A 1140  ILE ALA PRO PRO ILE ILE LYS GLN SER THR ILE VAL CYS          
SEQRES  21 A 1140  HIS ASN ARG VAL ASP PRO ASN GLY SER ARG TYR LEU LEU          
SEQRES  22 A 1140  GLY ASP MET GLU GLY ARG LEU PHE MET LEU LEU LEU GLU          
SEQRES  23 A 1140  LYS GLU GLU GLN MET ASP GLY THR VAL THR LEU LYS ASP          
SEQRES  24 A 1140  LEU ARG VAL GLU LEU LEU GLY GLU THR SER ILE ALA GLU          
SEQRES  25 A 1140  CYS LEU THR TYR LEU ASP ASN GLY VAL VAL PHE VAL GLY          
SEQRES  26 A 1140  SER ARG LEU GLY ASP SER GLN LEU VAL LYS LEU ASN VAL          
SEQRES  27 A 1140  ASP SER ASN GLU GLN GLY SER TYR VAL VAL ALA MET GLU          
SEQRES  28 A 1140  THR PHE THR ASN LEU GLY PRO ILE VAL ASP MET CYS VAL          
SEQRES  29 A 1140  VAL ASP LEU GLU ARG GLN GLY GLN GLY GLN LEU VAL THR          
SEQRES  30 A 1140  CYS SER GLY ALA PHE LYS GLU GLY SER LEU ARG ILE ILE          
SEQRES  31 A 1140  ARG ASN GLY ILE GLY ILE HIS GLU HIS ALA SER ILE ASP          
SEQRES  32 A 1140  LEU PRO GLY ILE LYS GLY LEU TRP PRO LEU ARG SER ASP          
SEQRES  33 A 1140  PRO ASN ARG GLU THR TYR ASP THR LEU VAL LEU SER PHE          
SEQRES  34 A 1140  VAL GLY GLN THR ARG VAL LEU MET LEU ASN GLY GLU GLU          
SEQRES  35 A 1140  VAL GLU GLU THR GLU LEU MET GLY PHE VAL ASP ASP GLN          
SEQRES  36 A 1140  GLN THR PHE PHE CYS GLY ASN VAL ALA HIS GLN GLN LEU          
SEQRES  37 A 1140  ILE GLN ILE THR SER ALA SER VAL ARG LEU VAL SER GLN          
SEQRES  38 A 1140  GLU PRO LYS ALA LEU VAL SER GLU TRP LYS GLU PRO GLN          
SEQRES  39 A 1140  ALA LYS ASN ILE SER VAL ALA SER CYS ASN SER SER GLN          
SEQRES  40 A 1140  VAL VAL VAL ALA VAL GLY ARG ALA LEU TYR TYR LEU GLN          
SEQRES  41 A 1140  ILE HIS PRO GLN GLU LEU ARG GLN ILE SER HIS THR GLU          
SEQRES  42 A 1140  MET GLU HIS GLU VAL ALA CYS LEU ASP ILE THR PRO LEU          
SEQRES  43 A 1140  GLY ASP SER ASN GLY LEU SER PRO LEU CYS ALA ILE GLY          
SEQRES  44 A 1140  LEU TRP THR ASP ILE SER ALA ARG ILE LEU LYS LEU PRO          
SEQRES  45 A 1140  SER PHE GLU LEU LEU HIS LYS GLU MET LEU GLY GLY GLU          
SEQRES  46 A 1140  ILE ILE PRO ARG SER ILE LEU MET THR THR PHE GLU SER          
SEQRES  47 A 1140  SER HIS TYR LEU LEU CYS ALA LEU GLY ASP GLY ALA LEU          
SEQRES  48 A 1140  PHE TYR PHE GLY LEU ASN ILE GLU THR GLY LEU LEU SER          
SEQRES  49 A 1140  ASP ARG LYS LYS VAL THR LEU GLY THR GLN PRO THR VAL          
SEQRES  50 A 1140  LEU ARG THR PHE ARG SER LEU SER THR THR ASN VAL PHE          
SEQRES  51 A 1140  ALA CYS SER ASP ARG PRO THR VAL ILE TYR SER SER ASN          
SEQRES  52 A 1140  HIS LYS LEU VAL PHE SER ASN VAL ASN LEU LYS GLU VAL          
SEQRES  53 A 1140  ASN TYR MET CYS PRO LEU ASN SER ASP GLY TYR PRO ASP          
SEQRES  54 A 1140  SER LEU ALA LEU ALA ASN ASN SER THR LEU THR ILE GLY          
SEQRES  55 A 1140  THR ILE ASP GLU ILE GLN LYS LEU HIS ILE ARG THR VAL          
SEQRES  56 A 1140  PRO LEU TYR GLU SER PRO ARG LYS ILE CYS TYR GLN GLU          
SEQRES  57 A 1140  VAL SER GLN CYS PHE GLY VAL LEU SER SER ARG ILE GLU          
SEQRES  58 A 1140  VAL GLN ASP THR SER GLY GLY THR THR ALA LEU ARG PRO          
SEQRES  59 A 1140  SER ALA SER THR GLN ALA LEU SER SER SER VAL SER SER          
SEQRES  60 A 1140  SER LYS LEU PHE SER SER SER THR ALA PRO HIS GLU THR          
SEQRES  61 A 1140  SER PHE GLY GLU GLU VAL GLU VAL HIS ASN LEU LEU ILE          
SEQRES  62 A 1140  ILE ASP GLN HIS THR PHE GLU VAL LEU HIS ALA HIS GLN          
SEQRES  63 A 1140  PHE LEU GLN ASN GLU TYR ALA LEU SER LEU VAL SER CYS          
SEQRES  64 A 1140  LYS LEU GLY LYS ASP PRO ASN THR TYR PHE ILE VAL GLY          
SEQRES  65 A 1140  THR ALA MET VAL TYR PRO GLU GLU ALA GLU PRO LYS GLN          
SEQRES  66 A 1140  GLY ARG ILE VAL VAL PHE GLN TYR SER ASP GLY LYS LEU          
SEQRES  67 A 1140  GLN THR VAL ALA GLU LYS GLU VAL LYS GLY ALA VAL TYR          
SEQRES  68 A 1140  SER MET VAL GLU PHE ASN GLY LYS LEU LEU ALA SER ILE          
SEQRES  69 A 1140  ASN SER THR VAL ARG LEU TYR GLU TRP THR THR GLU LYS          
SEQRES  70 A 1140  ASP VAL ARG THR GLU CYS ASN HIS TYR ASN ASN ILE MET          
SEQRES  71 A 1140  ALA LEU TYR LEU LYS THR LYS GLY ASP PHE ILE LEU VAL          
SEQRES  72 A 1140  GLY ASP LEU MET ARG SER VAL LEU LEU LEU ALA TYR LYS          
SEQRES  73 A 1140  PRO MET GLU GLY ASN PHE GLU GLU ILE ALA ARG ASP PHE          
SEQRES  74 A 1140  ASN PRO ASN TRP MET SER ALA VAL GLU ILE LEU ASP ASP          
SEQRES  75 A 1140  ASP ASN PHE LEU GLY ALA GLU ASN ALA PHE ASN LEU PHE          
SEQRES  76 A 1140  VAL CYS GLN LYS ASP SER ALA ALA THR THR ASP GLU GLU          
SEQRES  77 A 1140  ARG GLN HIS LEU GLN GLU VAL GLY LEU PHE HIS LEU GLY          
SEQRES  78 A 1140  GLU PHE VAL ASN VAL PHE CYS HIS GLY SER LEU VAL MET          
SEQRES  79 A 1140  GLN ASN LEU GLY GLU THR SER THR PRO THR GLN GLY SER          
SEQRES  80 A 1140  VAL LEU PHE GLY THR VAL ASN GLY MET ILE GLY LEU VAL          
SEQRES  81 A 1140  THR SER LEU SER GLU SER TRP TYR ASN LEU LEU LEU ASP          
SEQRES  82 A 1140  MET GLN ASN ARG LEU ASN LYS VAL ILE LYS SER VAL GLY          
SEQRES  83 A 1140  LYS ILE GLU HIS SER PHE TRP ARG SER PHE HIS THR GLU          
SEQRES  84 A 1140  ARG LYS THR GLU PRO ALA THR GLY PHE ILE ASP GLY ASP          
SEQRES  85 A 1140  LEU ILE GLU SER PHE LEU ASP ILE SER ARG PRO LYS MET          
SEQRES  86 A 1140  GLN GLU VAL VAL ALA ASN LEU GLN TYR ASP ASP GLY SER          
SEQRES  87 A 1140  GLY MET LYS ARG GLU ALA THR ALA ASP ASP LEU ILE LYS          
SEQRES  88 A 1140  VAL VAL GLU GLU LEU THR ARG ILE HIS                          
SEQRES   1 B  222  MET ASP PRO THR ASP LEU SER PHE SER PRO ASP GLU ILE          
SEQRES   2 B  222  ASN LYS LEU ILE GLU THR GLY LEU ASN THR VAL GLU TYR          
SEQRES   3 B  222  PHE THR SER GLN GLN VAL THR GLY THR SER SER LEU GLY          
SEQRES   4 B  222  LYS ASN THR ILE PRO PRO GLY VAL THR GLY LEU LEU THR          
SEQRES   5 B  222  ASN ALA ALA GLU ALA LYS ILE GLN GLU SER THR ASN HIS          
SEQRES   6 B  222  GLN LYS GLY SER VAL GLY GLY GLY ALA LYS PRO LYS LYS          
SEQRES   7 B  222  PRO ARG PRO LYS ILE ALA ILE VAL PRO ALA ASP ASP LYS          
SEQRES   8 B  222  THR VAL PRO GLY LYS PRO ILE PRO ASN PRO LEU LEU GLY          
SEQRES   9 B  222  LEU ASP SER THR PRO SER THR GLN THR VAL LEU ASP LEU          
SEQRES  10 B  222  SER GLY LYS THR LEU PRO SER GLY SER TYR LYS GLY VAL          
SEQRES  11 B  222  LYS LEU ALA LYS PHE GLY LYS GLU ASN LEU MET THR ARG          
SEQRES  12 B  222  PHE ILE GLU GLU PRO ARG GLU ASN PRO ILE ALA THR SER          
SEQRES  13 B  222  SER PRO ILE ASP PHE LYS ARG GLY ARG ASP THR GLY GLY          
SEQRES  14 B  222  PHE HIS ARG ARG GLU TYR SER ILE GLY TRP VAL GLY ASP          
SEQRES  15 B  222  GLU VAL LYS VAL THR GLU TRP CYS ASN PRO SER CYS SER          
SEQRES  16 B  222  PRO ILE THR ALA ALA ALA ARG ARG PHE GLU CYS THR CYS          
SEQRES  17 B  222  HIS GLN CYS PRO VAL THR CYS SER GLU CYS GLU ARG ASP          
SEQRES  18 B  222  THR                                                          
SEQRES   1 C  759  MET ALA ASP GLU ALA PRO ARG LYS GLY SER PHE SER ALA          
SEQRES   2 C  759  LEU VAL GLY ARG THR ASN GLY LEU THR LYS PRO ALA ALA          
SEQRES   3 C  759  LEU ALA ALA ALA PRO ALA LYS PRO GLY GLY ALA GLY GLY          
SEQRES   4 C  759  SER LYS LYS LEU VAL ILE LYS ASN PHE ARG ASP ARG PRO          
SEQRES   5 C  759  ARG LEU PRO ASP ASN TYR THR GLN ASP THR TRP ARG LYS          
SEQRES   6 C  759  LEU HIS GLU ALA VAL ARG ALA VAL GLN SER SER THR SER          
SEQRES   7 C  759  ILE ARG TYR ASN LEU GLU GLU LEU TYR GLN ALA VAL GLU          
SEQRES   8 C  759  ASN LEU CYS SER HIS LYS VAL SER PRO MET LEU TYR LYS          
SEQRES   9 C  759  GLN LEU ARG GLN ALA CYS GLU ASP HIS VAL GLN ALA GLN          
SEQRES  10 C  759  ILE LEU PRO PHE ARG GLU ASP SER LEU ASP SER VAL LEU          
SEQRES  11 C  759  PHE LEU LYS LYS ILE ASN THR CYS TRP GLN ASP HIS CYS          
SEQRES  12 C  759  ARG GLN MET ILE MET ILE ARG SER ILE PHE LEU PHE LEU          
SEQRES  13 C  759  ASP ARG THR TYR VAL LEU GLN ASN SER THR LEU PRO SER          
SEQRES  14 C  759  ILE TRP ASP MET GLY LEU GLU LEU PHE ARG THR HIS ILE          
SEQRES  15 C  759  ILE SER ASP LYS MET VAL GLN SER LYS THR ILE ASP GLY          
SEQRES  16 C  759  ILE LEU LEU LEU ILE GLU ARG GLU ARG SER GLY GLU ALA          
SEQRES  17 C  759  VAL ASP ARG SER LEU LEU ARG SER LEU LEU GLY MET LEU          
SEQRES  18 C  759  SER ASP LEU GLN VAL TYR LYS ASP SER PHE GLU LEU LYS          
SEQRES  19 C  759  PHE LEU GLU GLU THR ASN CYS LEU TYR ALA ALA GLU GLY          
SEQRES  20 C  759  GLN ARG LEU MET GLN GLU ARG GLU VAL PRO GLU TYR LEU          
SEQRES  21 C  759  ASN HIS VAL SER LYS ARG LEU GLU GLU GLU GLY ASP ARG          
SEQRES  22 C  759  VAL ILE THR TYR LEU ASP HIS SER THR GLN LYS PRO LEU          
SEQRES  23 C  759  ILE ALA CYS VAL GLU LYS GLN LEU LEU GLY GLU HIS LEU          
SEQRES  24 C  759  THR ALA ILE LEU GLN LYS GLY LEU ASP HIS LEU LEU ASP          
SEQRES  25 C  759  GLU ASN ARG VAL PRO ASP LEU ALA GLN MET TYR GLN LEU          
SEQRES  26 C  759  PHE SER ARG VAL ARG GLY GLY GLN GLN ALA LEU LEU GLN          
SEQRES  27 C  759  HIS TRP SER GLU TYR ILE LYS THR PHE GLY THR ALA ILE          
SEQRES  28 C  759  VAL ILE ASN PRO GLU LYS ASP LYS ASP MET VAL GLN ASP          
SEQRES  29 C  759  LEU LEU ASP PHE LYS ASP LYS VAL ASP HIS VAL ILE GLU          
SEQRES  30 C  759  VAL CYS PHE GLN LYS ASN GLU ARG PHE VAL ASN LEU MET          
SEQRES  31 C  759  LYS GLU SER PHE GLU THR PHE ILE ASN LYS ARG PRO ASN          
SEQRES  32 C  759  LYS PRO ALA GLU LEU ILE ALA LYS HIS VAL ASP SER LYS          
SEQRES  33 C  759  LEU ARG ALA GLY ASN LYS GLU ALA THR ASP GLU GLU LEU          
SEQRES  34 C  759  GLU ARG THR LEU ASP LYS ILE MET ILE LEU PHE ARG PHE          
SEQRES  35 C  759  ILE HIS GLY LYS ASP VAL PHE GLU ALA PHE TYR LYS LYS          
SEQRES  36 C  759  ASP LEU ALA LYS ARG LEU LEU VAL GLY LYS SER ALA SER          
SEQRES  37 C  759  VAL ASP ALA GLU LYS SER MET LEU SER LYS LEU LYS HIS          
SEQRES  38 C  759  GLU CYS GLY ALA ALA PHE THR SER LYS LEU GLU GLY MET          
SEQRES  39 C  759  PHE LYS ASP MET GLU LEU SER LYS ASP ILE MET VAL HIS          
SEQRES  40 C  759  PHE LYS GLN HIS MET GLN ASN GLN SER ASP SER GLY PRO          
SEQRES  41 C  759  ILE ASP LEU THR VAL ASN ILE LEU THR MET GLY TYR TRP          
SEQRES  42 C  759  PRO THR TYR THR PRO MET GLU VAL HIS LEU THR PRO GLU          
SEQRES  43 C  759  MET ILE LYS LEU GLN GLU VAL PHE LYS ALA PHE TYR LEU          
SEQRES  44 C  759  GLY LYS HIS SER GLY ARG LYS LEU GLN TRP GLN THR THR          
SEQRES  45 C  759  LEU GLY HIS ALA VAL LEU LYS ALA GLU PHE LYS GLU GLY          
SEQRES  46 C  759  LYS LYS GLU PHE GLN VAL SER LEU PHE GLN THR LEU VAL          
SEQRES  47 C  759  LEU LEU MET PHE ASN GLU GLY ASP GLY PHE SER PHE GLU          
SEQRES  48 C  759  GLU ILE LYS MET ALA THR GLY ILE GLU ASP SER GLU LEU          
SEQRES  49 C  759  ARG ARG THR LEU GLN SER LEU ALA CYS GLY LYS ALA ARG          
SEQRES  50 C  759  VAL LEU ILE LYS SER PRO LYS GLY LYS GLU VAL GLU ASP          
SEQRES  51 C  759  GLY ASP LYS PHE ILE PHE ASN GLY GLU PHE LYS HIS LYS          
SEQRES  52 C  759  LEU PHE ARG ILE LYS ILE ASN GLN ILE GLN MET LYS GLU          
SEQRES  53 C  759  THR VAL GLU GLU GLN VAL SER THR THR GLU ARG VAL PHE          
SEQRES  54 C  759  GLN ASP ARG GLN TYR GLN ILE ASP ALA ALA ILE VAL ARG          
SEQRES  55 C  759  ILE MET LYS MET ARG LYS THR LEU GLY HIS ASN LEU LEU          
SEQRES  56 C  759  VAL SER GLU LEU TYR ASN GLN LEU LYS PHE PRO VAL LYS          
SEQRES  57 C  759  PRO GLY ASP LEU LYS LYS ARG ILE GLU SER LEU ILE ASP          
SEQRES  58 C  759  ARG ASP TYR MET GLU ARG ASP LYS ASP ASN PRO ASN GLN          
SEQRES  59 C  759  TYR HIS TYR VAL ALA                                          
SEQRES   1 D  108  MET ALA ALA ALA MET ASP VAL ASP THR PRO SER GLY THR          
SEQRES   2 D  108  ASN SER GLY ALA GLY LYS LYS ARG PHE GLU VAL LYS LYS          
SEQRES   3 D  108  TRP ASN ALA VAL ALA LEU TRP ALA TRP ASP ILE VAL VAL          
SEQRES   4 D  108  ASP ASN CYS ALA ILE CYS ARG ASN HIS ILE MET ASP LEU          
SEQRES   5 D  108  CYS ILE GLU CYS GLN ALA ASN GLN ALA SER ALA THR SER          
SEQRES   6 D  108  GLU GLU CYS THR VAL ALA TRP GLY VAL CYS ASN HIS ALA          
SEQRES   7 D  108  PHE HIS PHE HIS CYS ILE SER ARG TRP LEU LYS THR ARG          
SEQRES   8 D  108  GLN VAL CYS PRO LEU ASP ASN ARG GLU TRP GLU PHE GLN          
SEQRES   9 D  108  LYS TYR GLY HIS                                              
HET     ZN  B3001       1                                                       
HET     ZN  B3002       1                                                       
HET     ZN  D4001       1                                                       
HET     ZN  D4003       1                                                       
HET     ZN  D4002       1                                                       
HETNAM      ZN ZINC ION                                                         
FORMUL   5   ZN    5(ZN 2+)                                                     
HELIX    1   1 PRO A  250  GLN A  255  1                                   6    
HELIX    2   2 ASN A  341  SER A  345  5                                   5    
HELIX    3   3 SER A  755  GLN A  759  5                                   5    
HELIX    4   4 SER A 1044  ILE A 1062  1                                  19    
HELIX    5   5 GLU A 1069  ARG A 1074  1                                   6    
HELIX    6   6 ASP A 1092  SER A 1096  5                                   5    
HELIX    7   7 SER A 1101  ALA A 1110  1                                  10    
HELIX    8   8 THR A 1125  THR A 1137  1                                  13    
HELIX    9   9 ARG A 1138  HIS A 1140  5                                   3    
HELIX   10  10 ASN B   22  THR B   33  1                                  12    
HELIX   11  11 SER B  126  GLU B  138  1                                  13    
HELIX   12  12 ASP C   61  ALA C   72  1                                  12    
HELIX   13  13 ASN C   82  CYS C   94  1                                  13    
HELIX   14  14 VAL C   98  ARG C  122  1                                  25    
HELIX   15  15 VAL C  129  PHE C  153  1                                  25    
HELIX   16  16 PHE C  153  ARG C  158  1                                   6    
HELIX   17  17 SER C  169  HIS C  181  1                                  13    
HELIX   18  18 VAL C  188  LYS C  191  5                                   4    
HELIX   19  19 THR C  192  ARG C  202  1                                  11    
HELIX   20  20 ASP C  210  LEU C  224  1                                  15    
HELIX   21  21 PHE C  231  ARG C  254  1                                  24    
HELIX   22  22 GLU C  255  GLU C  270  1                                  16    
HELIX   23  23 GLU C  270  ILE C  275  1                                   6    
HELIX   24  24 THR C  282  LEU C  295  1                                  14    
HELIX   25  25 LEU C  299  LYS C  305  1                                   7    
HELIX   26  26 GLY C  306  ASP C  312  1                                   7    
HELIX   27  27 ARG C  315  VAL C  329  1                                  15    
HELIX   28  28 GLY C  331  ILE C  353  1                                  23    
HELIX   29  29 ASN C  354  ASP C  358  5                                   5    
HELIX   30  30 ASP C  360  VAL C  378  1                                  19    
HELIX   31  31 ASN C  383  ASN C  399  1                                  17    
HELIX   32  32 ASN C  403  ARG C  418  1                                  16    
HELIX   33  33 GLY C  420  ALA C  424  5                                   5    
HELIX   34  34 GLU C  428  ARG C  441  1                                  14    
HELIX   35  35 GLY C  445  VAL C  463  1                                  19    
HELIX   36  36 SER C  468  HIS C  481  1                                  14    
HELIX   37  37 THR C  488  ASN C  514  1                                  27    
HELIX   38  38 THR C  544  GLY C  560  1                                  17    
HELIX   39  39 GLN C  570  LEU C  573  5                                   4    
HELIX   40  40 LEU C  593  PHE C  602  1                                  10    
HELIX   41  41 PHE C  610  THR C  617  1                                   8    
HELIX   42  42 GLU C  620  SER C  630  1                                  11    
HELIX   43  43 ASN C  670  LYS C  675  5                                   6    
HELIX   44  44 THR C  677  ARG C  707  1                                  31    
HELIX   45  45 HIS C  712  LEU C  723  1                                  12    
HELIX   46  46 LYS C  728  ARG C  742  1                                  15    
HELIX   47  47 THR D   64  CYS D   68  5                                   5    
SHEET    1   A 5 VAL A1004  HIS A1009  0                                        
SHEET    2   A 5 THR A1024  THR A1032 -1  O  LEU A1029   N  CYS A1008           
SHEET    3   A 5 ILE A1037  LEU A1043 -1  O  SER A1042   N  GLN A1025           
SHEET    4   A 5 ASN A   4  GLN A  10 -1  N  TYR A   5   O  THR A1041           
SHEET    5   A 5 PHE A1088  ASP A1090  1  O  ILE A1089   N  VAL A   6           
SHEET    1   B 4 GLY A  17  GLY A  21  0                                        
SHEET    2   B 4 ASN A  30  ALA A  34 -1  O  LEU A  32   N  VAL A  19           
SHEET    3   B 4 ARG A  38  VAL A  44 -1  O  GLU A  40   N  ILE A  33           
SHEET    4   B 4 LEU A  49  GLY A  56 -1  O  VAL A  55   N  LEU A  39           
SHEET    1   C 4 VAL A  63  PHE A  67  0                                        
SHEET    2   C 4 LEU A  76  LEU A  80 -1  O  PHE A  78   N  GLU A  65           
SHEET    3   C 4 ASN A  85  GLN A  93 -1  O  CYS A  87   N  ILE A  79           
SHEET    4   C 4 ILE A  98  ASN A 107 -1  O  ASP A  99   N  LYS A  92           
SHEET    1   D 4 ILE A 121  ILE A 124  0                                        
SHEET    2   D 4 MET A 130  ARG A 134 -1  O  GLY A 132   N  ILE A 123           
SHEET    3   D 4 LEU A 139  PRO A 144 -1  O  ILE A 143   N  ILE A 131           
SHEET    4   D 4 PHE A 155  ARG A 158 -1  O  PHE A 155   N  VAL A 142           
SHEET    1   E 3 VAL A 164  LEU A 170  0                                        
SHEET    2   E 3 THR A 177  ASP A 184 -1  O  VAL A 181   N  ILE A 165           
SHEET    3   E 3 GLY A 187  HIS A 189 -1  O  HIS A 189   N  TYR A 182           
SHEET    1   F 2 VAL A 195  SER A 196  0                                        
SHEET    2   F 2 GLU A 201  PHE A 202 -1  O  GLU A 201   N  SER A 196           
SHEET    1   G 3 MET A 218  ALA A 221  0                                        
SHEET    2   G 3 ALA A 229  ILE A 232 -1  O  ILE A 230   N  ILE A 220           
SHEET    3   G 3 ILE A 237  HIS A 240 -1  O  THR A 238   N  ILE A 231           
SHEET    1   H 4 ILE A 258  ARG A 263  0                                        
SHEET    2   H 4 ARG A 270  ASP A 275 -1  O  GLY A 274   N  VAL A 259           
SHEET    3   H 4 ARG A 279  GLU A 286 -1  O  PHE A 281   N  LEU A 273           
SHEET    4   H 4 ASP A 299  GLU A 307 -1  O  LEU A 305   N  LEU A 280           
SHEET    1   I 4 ALA A 311  TYR A 316  0                                        
SHEET    2   I 4 VAL A 321  SER A 326 -1  O  PHE A 323   N  THR A 315           
SHEET    3   I 4 SER A 331  LEU A 336 -1  O  GLN A 332   N  VAL A 324           
SHEET    4   I 4 VAL A 347  PHE A 353 -1  O  GLU A 351   N  LEU A 333           
SHEET    1   J 4 ASP A 361  VAL A 365  0                                        
SHEET    2   J 4 GLN A 374  SER A 379 -1  O  GLN A 374   N  VAL A 365           
SHEET    3   J 4 SER A 386  GLY A 393 -1  O  ILE A 390   N  LEU A 375           
SHEET    4   J 4 LYS A 709  PRO A 716 -1  O  HIS A 711   N  ARG A 391           
SHEET    1   K 4 ILE A 396  SER A 401  0                                        
SHEET    2   K 4 LEU A 699  ILE A 704 -1  O  THR A 703   N  HIS A 397           
SHEET    3   K 4 SER A 690  ALA A 694 -1  N  LEU A 693   O  THR A 700           
SHEET    4   K 4 TYR A 678  LEU A 682 -1  N  LEU A 682   O  SER A 690           
SHEET    1   L 5 LEU A 410  LEU A 413  0                                        
SHEET    2   L 5 THR A 424  LEU A 427 -1  O  VAL A 426   N  TRP A 411           
SHEET    3   L 5 VAL A 435  ASN A 439 -1  O  LEU A 436   N  LEU A 425           
SHEET    4   L 5 GLU A 442  GLU A 445 -1  O  GLU A 444   N  MET A 437           
SHEET    5   L 5 ILE C  45  LYS C  46  1  O  LYS C  46   N  VAL A 443           
SHEET    1   M 4 THR A 457  VAL A 463  0                                        
SHEET    2   M 4 GLN A 467  THR A 472 -1  O  ILE A 471   N  PHE A 458           
SHEET    3   M 4 VAL A 476  SER A 480 -1  O  ARG A 477   N  GLN A 470           
SHEET    4   M 4 LEU A 486  SER A 488 -1  O  SER A 488   N  LEU A 478           
SHEET    1   N 4 VAL A 500  ALA A 501  0                                        
SHEET    2   N 4 GLN A 507  VAL A 512 -1  O  ALA A 511   N  VAL A 500           
SHEET    3   N 4 ALA A 515  HIS A 522 -1  O  ALA A 515   N  VAL A 512           
SHEET    4   N 4 GLU A 525  GLU A 533 -1  O  THR A 532   N  LEU A 516           
SHEET    1   O 4 VAL A 538  ASP A 542  0                                        
SHEET    2   O 4 LEU A 555  LEU A 560 -1  O  GLY A 559   N  ALA A 539           
SHEET    3   O 4 ILE A 568  LYS A 570 -1  O  LEU A 569   N  CYS A 556           
SHEET    4   O 4 GLU A 575  HIS A 578 -1  O  GLU A 575   N  LYS A 570           
SHEET    1   P 2 PRO A 588  SER A 590  0                                        
SHEET    2   P 2 ALA A 605  LEU A 606 -1  O  ALA A 605   N  ARG A 589           
SHEET    1   Q 4 MET A 593  THR A 595  0                                        
SHEET    2   Q 4 HIS A 600  LEU A 603 -1  O  TYR A 601   N  THR A 594           
SHEET    3   Q 4 ALA A 610  PHE A 614 -1  O  PHE A 614   N  LEU A 602           
SHEET    4   Q 4 LYS A 627  THR A 630 -1  O  VAL A 629   N  LEU A 611           
SHEET    1   R 2 PHE A 641  ARG A 642  0                                        
SHEET    2   R 2 THR A 647  ASN A 648 -1  O  ASN A 648   N  PHE A 641           
SHEET    1   S 2 TYR A 660  SER A 661  0                                        
SHEET    2   S 2 LEU A 666  VAL A 667 -1  O  VAL A 667   N  TYR A 660           
SHEET    1   T 4 LYS A 723  GLN A 727  0                                        
SHEET    2   T 4 CYS A 732  LEU A 736 -1  O  GLY A 734   N  CYS A 725           
SHEET    3   T 4 ASN A 790  ASP A 795 -1  O  ILE A 794   N  PHE A 733           
SHEET    4   T 4 VAL A 801  GLN A 806 -1  O  HIS A 803   N  ILE A 793           
SHEET    1   U 3 GLY A 748  THR A 750  0                                        
SHEET    2   U 3 ARG A 739  ASP A 744 -1  N  VAL A 742   O  THR A 750           
SHEET    3   U 3 VAL A 786  VAL A 788 -1  O  VAL A 788   N  ARG A 739           
SHEET    1   V 4 GLU A 811  CYS A 819  0                                        
SHEET    2   V 4 TYR A 828  MET A 835 -1  O  GLY A 832   N  LEU A 814           
SHEET    3   V 4 GLY A 846  PHE A 851 -1  O  ARG A 847   N  THR A 833           
SHEET    4   V 4 GLU A 863  VAL A 866 -1  O  VAL A 866   N  GLY A 846           
SHEET    1   W 2 SER A 872  PHE A 876  0                                        
SHEET    2   W 2 LYS A 879  SER A 883 -1  O  LYS A 879   N  PHE A 876           
SHEET    1   X 2 LEU A 890  TRP A 893  0                                        
SHEET    2   X 2 VAL A 899  CYS A 903 -1  O  CYS A 903   N  LEU A 890           
SHEET    1   Y 4 ALA A 911  TYR A 913  0                                        
SHEET    2   Y 4 PHE A 920  ASP A 925 -1  O  GLY A 924   N  TYR A 913           
SHEET    3   Y 4 VAL A 930  LYS A 936 -1  O  LEU A 931   N  VAL A 923           
SHEET    4   Y 4 ASN A 941  PHE A 942 -1  O  ASN A 941   N  LYS A 936           
SHEET    1   Z 4 ALA A 911  TYR A 913  0                                        
SHEET    2   Z 4 PHE A 920  ASP A 925 -1  O  GLY A 924   N  TYR A 913           
SHEET    3   Z 4 VAL A 930  LYS A 936 -1  O  LEU A 931   N  VAL A 923           
SHEET    4   Z 4 ALA A 946  ARG A 947 -1  O  ALA A 946   N  LEU A 932           
SHEET    1  AA 4 MET A 954  ASP A 961  0                                        
SHEET    2  AA 4 ASN A 964  GLU A 969 -1  O  LEU A 966   N  GLU A 958           
SHEET    3  AA 4 ASN A 973  LYS A 979 -1  O  CYS A 977   N  PHE A 965           
SHEET    4  AA 4 LEU A 992  HIS A 999 -1  O  PHE A 998   N  LEU A 974           
SHEET    1  AB 2 GLU B  18  THR B  19  0                                        
SHEET    2  AB 2 THR B  42  ILE B  43  1  O  ILE B  43   N  GLU B  18           
SHEET    1  AC 5 THR B  48  GLY B  49  0                                        
SHEET    2  AC 5 ARG B 143  GLU B 146 -1  O  ILE B 145   N  THR B  48           
SHEET    3  AC 5 ARG B 173  GLY B 178 -1  O  ARG B 173   N  GLU B 146           
SHEET    4  AC 5 LYS B 185  CYS B 190 -1  O  TRP B 189   N  GLU B 174           
SHEET    5  AC 5 THR B 111  VAL B 114 -1  N  THR B 113   O  VAL B 186           
SHEET    1  AD 2 LYS B  96  PRO B  97  0                                        
SHEET    2  AD 2 ARG B 202  ARG B 203 -1  O  ARG B 203   N  LYS B  96           
SHEET    1  AE 3 ASP C 522  THR C 529  0                                        
SHEET    2  AE 3 VAL D  24  TRP D  35  1  O  ALA D  31   N  LEU C 528           
SHEET    3  AE 3 ARG C 565  LYS C 566 -1  N  LYS C 566   O  ALA D  34           
SHEET    1  AF 5 ASP C 522  THR C 529  0                                        
SHEET    2  AF 5 VAL D  24  TRP D  35  1  O  ALA D  31   N  LEU C 528           
SHEET    3  AF 5 HIS C 575  LYS C 579 -1  N  VAL C 577   O  LYS D  25           
SHEET    4  AF 5 GLU C 588  SER C 592 -1  O  VAL C 591   N  ALA C 576           
SHEET    5  AF 5 ILE C 667  LYS C 668  1  O  ILE C 667   N  GLN C 590           
SHEET    1  AG 3 PHE C 608  SER C 609  0                                        
SHEET    2  AG 3 LYS C 653  PHE C 656 -1  O  PHE C 654   N  PHE C 608           
SHEET    3  AG 3 LEU C 639  LYS C 641 -1  N  ILE C 640   O  ILE C 655           
SHEET    1  AH 2 THR C 709  GLY C 711  0                                        
SHEET    2  AH 2 GLN C 754  HIS C 756 -1  O  TYR C 755   N  LEU C 710           
SHEET    1  AI 2 VAL D  70  TRP D  72  0                                        
SHEET    2  AI 2 ALA D  78  HIS D  80 -1  O  PHE D  79   N  ALA D  71           
SSBOND   1 CYS A   18    CYS A  313                          1555   1555  2.05  
SSBOND   2 CYS B  190    CYS B  218                          1555   1555  2.90  
SSBOND   3 CYS B  194    CYS B  208                          1555   1555  2.04  
SSBOND   4 CYS D   42    CYS D   45                          1555   1555  2.14  
SSBOND   5 CYS D   45    CYS D   83                          1555   1555  2.06  
SSBOND   6 CYS D   75    CYS D   94                          1555   1555  2.06  
LINK         SG  CYS B 190                ZN    ZN B3002     1555   1555  2.38  
LINK         SG  CYS B 194                ZN    ZN B3001     1555   1555  2.44  
LINK         SG  CYS B 206                ZN    ZN B3001     1555   1555  2.95  
LINK         SG  CYS B 208                ZN    ZN B3001     1555   1555  2.45  
LINK         SG  CYS B 211                ZN    ZN B3001     1555   1555  2.72  
LINK         SG  CYS B 215                ZN    ZN B3002     1555   1555  2.94  
LINK         SG  CYS B 218                ZN    ZN B3002     1555   1555  2.45  
LINK         SG  CYS D  42                ZN    ZN D4001     1555   1555  2.16  
LINK         SG  CYS D  45                ZN    ZN D4001     1555   1555  2.12  
LINK         SG  CYS D  53                ZN    ZN D4003     1555   1555  2.68  
LINK         SG  CYS D  56                ZN    ZN D4003     1555   1555  2.25  
LINK         SG  CYS D  68                ZN    ZN D4003     1555   1555  2.50  
LINK         SG  CYS D  75                ZN    ZN D4002     1555   1555  2.37  
LINK         ND1 HIS D  77                ZN    ZN D4002     1555   1555  1.99  
LINK         ND1 HIS D  82                ZN    ZN D4003     1555   1555  2.27  
LINK         SG  CYS D  83                ZN    ZN D4001     1555   1555  2.37  
LINK         SG  CYS D  94                ZN    ZN D4002     1555   1555  2.27  
LINK         OD2 ASP D  97                ZN    ZN D4002     1555   1555  2.17  
CISPEP   1 GLY A  357    PRO A  358          0        -0.03                     
SITE     1 AC1  4 CYS B 194  CYS B 206  CYS B 208  CYS B 211                    
SITE     1 AC2  4 HIS B 171  CYS B 190  CYS B 215  CYS B 218                    
SITE     1 AC3  4 CYS D  42  CYS D  45  HIS D  80  CYS D  83                    
SITE     1 AC4  4 CYS D  53  CYS D  56  CYS D  68  HIS D  82                    
SITE     1 AC5  4 CYS D  75  HIS D  77  CYS D  94  ASP D  97                    
CRYST1   83.452  203.165  424.875  90.00  90.00  90.00 C 2 2 21      8          
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      0.011983  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.004922  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.002354        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system