GenomeNet

Database: PDB
Entry: 5JNE
LinkDB: 5JNE
Original site: 5JNE 
HEADER    LIGASE/SIGNALING PROTEIN                29-APR-16   5JNE              
TITLE     E2-SUMO-SIZ1 E3-SUMO-PCNA COMPLEX                                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: E3 SUMO-PROTEIN LIGASE SIZ1,UBIQUITIN-LIKE PROTEIN SMT3;   
COMPND   3 CHAIN: A, E;                                                         
COMPND   4 FRAGMENT: UNP RESIDUES 167-445;                                      
COMPND   5 SYNONYM: SAP AND MIZ-FINGER DOMAIN-CONTAINING PROTEIN 1,UBIQUITIN-   
COMPND   6 LIKE PROTEIN LIGASE 1;                                               
COMPND   7 EC: 6.3.2.-;                                                         
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MUTATION: YES;                                                       
COMPND  10 MOL_ID: 2;                                                           
COMPND  11 MOLECULE: SUMO-CONJUGATING ENZYME UBC9;                              
COMPND  12 CHAIN: B, F;                                                         
COMPND  13 FRAGMENT: UNP RESIDUES 20-98;                                        
COMPND  14 SYNONYM: UBIQUITIN CARRIER PROTEIN 9,UBIQUITIN-CONJUGATING ENZYME E2-
COMPND  15 18 KDA,UBIQUITIN-PROTEIN LIGASE;                                     
COMPND  16 EC: 6.3.2.-;                                                         
COMPND  17 ENGINEERED: YES;                                                     
COMPND  18 MUTATION: YES;                                                       
COMPND  19 MOL_ID: 3;                                                           
COMPND  20 MOLECULE: UBIQUITIN-LIKE PROTEIN SMT3;                               
COMPND  21 CHAIN: C, G;                                                         
COMPND  22 ENGINEERED: YES;                                                     
COMPND  23 MUTATION: YES;                                                       
COMPND  24 MOL_ID: 4;                                                           
COMPND  25 MOLECULE: PROLIFERATING CELL NUCLEAR ANTIGEN;                        
COMPND  26 CHAIN: D, H;                                                         
COMPND  27 SYNONYM: PCNA;                                                       
COMPND  28 ENGINEERED: YES;                                                     
COMPND  29 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;                       
SOURCE   3 ORGANISM_COMMON: BAKER'S YEAST;                                      
SOURCE   4 ORGANISM_TAXID: 559292;                                              
SOURCE   5 STRAIN: ATCC 204508 / S288C;                                         
SOURCE   6 GENE: SIZ1, ULL1, YDR409W, SMT3, YDR510W, D9719.15;                  
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /  
SOURCE  11 S288C);                                                              
SOURCE  12 ORGANISM_COMMON: BAKER'S YEAST;                                      
SOURCE  13 ORGANISM_TAXID: 559292;                                              
SOURCE  14 STRAIN: ATCC 204508 / S288C;                                         
SOURCE  15 GENE: UBC9, YDL064W;                                                 
SOURCE  16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  18 MOL_ID: 3;                                                           
SOURCE  19 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;                       
SOURCE  20 ORGANISM_COMMON: BAKER'S YEAST;                                      
SOURCE  21 ORGANISM_TAXID: 559292;                                              
SOURCE  22 STRAIN: ATCC 204508 / S288C;                                         
SOURCE  23 GENE: SMT3, YDR510W, D9719.15;                                       
SOURCE  24 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  25 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  26 MOL_ID: 4;                                                           
SOURCE  27 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /  
SOURCE  28 S288C);                                                              
SOURCE  29 ORGANISM_COMMON: BAKER'S YEAST;                                      
SOURCE  30 ORGANISM_TAXID: 559292;                                              
SOURCE  31 STRAIN: ATCC 204508 / S288C;                                         
SOURCE  32 GENE: POL30, YBR088C, YBR0811;                                       
SOURCE  33 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  34 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    UBIQUITIN, UBIQUITIN-LIKE, SUMO, E3 LIGASE, SUBSTRATE COMPLEX, E2     
KEYWDS   2 CONJUGATING ENZYME, LIGASE-SIGNALING PROTEIN COMPLEX, SIZ, PIAS      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.D.LIMA,F.C.STREICH JR.                                              
REVDAT   6   25-DEC-19 5JNE    1       REMARK                                   
REVDAT   5   20-SEP-17 5JNE    1       REMARK                                   
REVDAT   4   21-SEP-16 5JNE    1       REMARK                                   
REVDAT   3   31-AUG-16 5JNE    1       JRNL                                     
REVDAT   2   24-AUG-16 5JNE    1       JRNL                                     
REVDAT   1   10-AUG-16 5JNE    0                                                
JRNL        AUTH   F.C.STREICH,C.D.LIMA                                         
JRNL        TITL   CAPTURING A SUBSTRATE IN AN ACTIVATED RING E3/E2-SUMO        
JRNL        TITL 2 COMPLEX.                                                     
JRNL        REF    NATURE                        V. 536   304 2016              
JRNL        REFN                   ESSN 1476-4687                               
JRNL        PMID   27509863                                                     
JRNL        DOI    10.1038/NATURE19071                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.85 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (1.10_2155: ???)                              
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.85                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 48.39                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.410                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 61968                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.214                           
REMARK   3   R VALUE            (WORKING SET) : 0.212                           
REMARK   3   FREE R VALUE                     : 0.250                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.070                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3139                            
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 48.3924 -  7.9744    1.00     2740   146  0.1794 0.2129        
REMARK   3     2  7.9744 -  6.3340    1.00     2720   133  0.2032 0.2307        
REMARK   3     3  6.3340 -  5.5347    1.00     2694   146  0.1859 0.2140        
REMARK   3     4  5.5347 -  5.0292    1.00     2697   147  0.1726 0.2119        
REMARK   3     5  5.0292 -  4.6691    1.00     2666   158  0.1614 0.1939        
REMARK   3     6  4.6691 -  4.3940    1.00     2702   147  0.1638 0.2004        
REMARK   3     7  4.3940 -  4.1740    1.00     2670   150  0.1822 0.2079        
REMARK   3     8  4.1740 -  3.9924    1.00     2697   160  0.1940 0.2612        
REMARK   3     9  3.9924 -  3.8388    0.99     2672   151  0.2069 0.2276        
REMARK   3    10  3.8388 -  3.7064    1.00     2638   157  0.2042 0.2685        
REMARK   3    11  3.7064 -  3.5905    1.00     2685   140  0.2148 0.2656        
REMARK   3    12  3.5905 -  3.4879    1.00     2668   122  0.2294 0.2652        
REMARK   3    13  3.4879 -  3.3961    0.99     2717   127  0.2295 0.2514        
REMARK   3    14  3.3961 -  3.3133    1.00     2660   135  0.2386 0.2983        
REMARK   3    15  3.3133 -  3.2380    1.00     2653   147  0.2508 0.2993        
REMARK   3    16  3.2380 -  3.1691    0.99     2712   132  0.2619 0.3337        
REMARK   3    17  3.1691 -  3.1057    0.99     2635   150  0.2606 0.3057        
REMARK   3    18  3.1057 -  3.0471    0.99     2634   142  0.2869 0.3385        
REMARK   3    19  3.0471 -  2.9927    0.99     2671   134  0.2979 0.3434        
REMARK   3    20  2.9927 -  2.9420    0.99     2661   151  0.3098 0.3641        
REMARK   3    21  2.9420 -  2.8945    0.98     2619   123  0.3296 0.3439        
REMARK   3    22  2.8945 -  2.8500    0.98     2618   141  0.3342 0.3837        
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              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.440            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.470           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
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  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      :  0.002          13746                                  
REMARK   3   ANGLE     :  0.411          18537                                  
REMARK   3   CHIRALITY :  0.041           2049                                  
REMARK   3   PLANARITY :  0.003           2397                                  
REMARK   3   DIHEDRAL  :  7.866           8433                                  
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 5JNE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-MAY-16.                  
REMARK 100 THE DEPOSITION ID IS D_1000220896.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-MAR-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 24-ID-E                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.979                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 61981                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.850                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 48.385                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.0                               
REMARK 200  DATA REDUNDANCY                : 3.600                              
REMARK 200  R MERGE                    (I) : 0.10700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.1000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.85                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.95                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.55600                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.820                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHENIX                                                
REMARK 200 STARTING MODEL: 3ID2, 1PLQ, 2EKE                                     
REMARK 200                                                                      
REMARK 200 REMARK: PLATES                                                       
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 64.34                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.45                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M TRIS-HCL (PH 8.5), 5% PEG          
REMARK 280  10,000, 0.2 M NACL, 10% GLYCEROL, 3% DIOXANE, VAPOR DIFFUSION,      
REMARK 280  HANGING DROP, TEMPERATURE 291K                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -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        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       46.71050            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000      102.94100            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       46.71050            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000      102.94100            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 8440 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 40750 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -26.0 KCAL/MOL                        
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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 7980 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 40620 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -26.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F, 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 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     SER A   165                                                      
REMARK 465     LEU A   166                                                      
REMARK 465     SER A   167                                                      
REMARK 465     SER A   168                                                      
REMARK 465     SER A   169                                                      
REMARK 465     PHE A   170                                                      
REMARK 465     ALA A   171                                                      
REMARK 465     VAL A   172                                                      
REMARK 465     GLU A   445                                                      
REMARK 465     ASP A   446                                                      
REMARK 465     ASP A   447                                                      
REMARK 465     ASP A   448                                                      
REMARK 465     GLN A   528                                                      
REMARK 465     ILE A   529                                                      
REMARK 465     GLY A   530                                                      
REMARK 465     GLY A   531                                                      
REMARK 465     GLY B    -2                                                      
REMARK 465     SER B    -1                                                      
REMARK 465     LYS B   157                                                      
REMARK 465     GLY C    15                                                      
REMARK 465     SER C    16                                                      
REMARK 465     HIS C    17                                                      
REMARK 465     MET C    18                                                      
REMARK 465     ARG C    19                                                      
REMARK 465     ASN D   255                                                      
REMARK 465     ASP D   256                                                      
REMARK 465     GLU D   257                                                      
REMARK 465     GLU D   258                                                      
REMARK 465     SER E   165                                                      
REMARK 465     LEU E   166                                                      
REMARK 465     SER E   167                                                      
REMARK 465     SER E   168                                                      
REMARK 465     SER E   169                                                      
REMARK 465     PHE E   170                                                      
REMARK 465     ALA E   171                                                      
REMARK 465     VAL E   172                                                      
REMARK 465     GLU E   445                                                      
REMARK 465     ASP E   446                                                      
REMARK 465     ASP E   447                                                      
REMARK 465     ASP E   448                                                      
REMARK 465     ASP E   449                                                      
REMARK 465     LYS E   450                                                      
REMARK 465     GLN E   528                                                      
REMARK 465     ILE E   529                                                      
REMARK 465     GLY E   530                                                      
REMARK 465     GLY E   531                                                      
REMARK 465     GLY F    -2                                                      
REMARK 465     SER F    -1                                                      
REMARK 465     HIS F     0                                                      
REMARK 465     LYS F   157                                                      
REMARK 465     GLY G    15                                                      
REMARK 465     SER G    16                                                      
REMARK 465     HIS G    17                                                      
REMARK 465     MET G    18                                                      
REMARK 465     ARG G    19                                                      
REMARK 465     PRO G    20                                                      
REMARK 465     GLU G    21                                                      
REMARK 465     GLU H   257                                                      
REMARK 465     GLU H   258                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ASP A 449    CG   OD1  OD2                                       
REMARK 470     LYS A 450    CG   CD   CE   NZ                                   
REMARK 470     LEU A 451    CG   CD1  CD2                                       
REMARK 470     HIS B   0    CG   ND1  CD2  CE1  NE2                             
REMARK 470     PRO C  20    N    CB   CG   CD                                   
REMARK 470     ASP D 122    CG   OD1  OD2                                       
REMARK 470     PHE D 125    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LEU D 126    CG   CD1  CD2                                       
REMARK 470     ILE D 128    CG1  CG2  CD1                                       
REMARK 470     LYS D 253    CG   CD   CE   NZ                                   
REMARK 470     PRO E 173    N    CA   CB   CG   CD                              
REMARK 470     LEU E 451    CG   CD1  CD2                                       
REMARK 470     ARG G  47    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     PHE H 125    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LYS H 253    CG   CD   CE   NZ                                   
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    GLN A 186      -69.81   -105.09                                   
REMARK 500    LYS A 378       51.79    -97.38                                   
REMARK 500    LYS A 471       86.57   -152.51                                   
REMARK 500    GLN B 101     -109.75   -127.07                                   
REMARK 500    SER B 127       78.73   -156.13                                   
REMARK 500    ARG B 139        3.99   -158.83                                   
REMARK 500    ASN B 140       81.54   -163.10                                   
REMARK 500    TYR B 155       57.31    -96.92                                   
REMARK 500    SER C  32      -62.15   -130.94                                   
REMARK 500    GLU D   3       82.17   -154.71                                   
REMARK 500    PHE D  19       31.45   -150.99                                   
REMARK 500    THR D  95       76.67   -118.23                                   
REMARK 500    LYS D 107      -63.20   -103.89                                   
REMARK 500    ALA D 123      177.93     61.57                                   
REMARK 500    GLU D 232       45.31    -99.36                                   
REMARK 500    GLN E 186      -71.32    -99.94                                   
REMARK 500    THR E 353      -80.38    -78.83                                   
REMARK 500    LYS E 378       42.50    -97.89                                   
REMARK 500    VAL E 402      -62.91   -126.94                                   
REMARK 500    THR E 435     -169.63   -125.36                                   
REMARK 500    SER E 465      -72.54   -125.97                                   
REMARK 500    GLN F 101     -103.13   -117.17                                   
REMARK 500    ASN F 126       31.00    -82.28                                   
REMARK 500    SER F 127       67.47   -167.88                                   
REMARK 500    ASN F 140       78.80   -161.04                                   
REMARK 500    TYR F 155       57.61    -97.89                                   
REMARK 500    SER G  32      -61.36   -152.79                                   
REMARK 500    GLU H   3       86.98   -154.93                                   
REMARK 500    PHE H  19       40.01   -155.14                                   
REMARK 500    LYS H  31     -163.75   -110.75                                   
REMARK 500    THR H  85       30.35    -95.50                                   
REMARK 500    LYS H 107      -63.33   -124.01                                   
REMARK 500    PHE H 125     -166.29     59.03                                   
REMARK 500    SER H 243       78.49   -152.08                                   
REMARK 500    ASN H 255     -163.48     58.45                                   
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 A 601  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 377   SG                                                     
REMARK 620 2 HIS A 379   NE2 112.2                                              
REMARK 620 3 CYS A 400   SG  117.7 107.3                                        
REMARK 620 4 CYS A 403   SG  115.8 102.5  99.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN E 601  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS E 377   SG                                                     
REMARK 620 2 HIS E 379   NE2 109.5                                              
REMARK 620 3 CYS E 400   SG  123.2  99.1                                        
REMARK 620 4 CYS E 403   SG  117.6  99.9 103.8                                  
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 A 601                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 604                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 6LN B 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL D 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL D 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL D 303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN E 601                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL E 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL E 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 6LN F 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL H 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL H 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide GLY G 98 and LYS F     
REMARK 800  129                                                                 
DBREF  5JNE A  167   445  UNP    Q04195   SIZ1_YEAST     167    445             
DBREF  5JNE A  453   531  UNP    Q12306   SMT3_YEAST      20     98             
DBREF  5JNE B    1   157  UNP    P50623   UBC9_YEAST       1    157             
DBREF  5JNE C   19    98  UNP    Q12306   SMT3_YEAST      19     98             
DBREF  5JNE D    1   258  UNP    P15873   PCNA_YEAST       1    258             
DBREF  5JNE E  167   445  UNP    Q04195   SIZ1_YEAST     167    445             
DBREF  5JNE E  453   531  UNP    Q12306   SMT3_YEAST      20     98             
DBREF  5JNE F    1   157  UNP    P50623   UBC9_YEAST       1    157             
DBREF  5JNE G   19    98  UNP    Q12306   SMT3_YEAST      19     98             
DBREF  5JNE H    1   258  UNP    P15873   PCNA_YEAST       1    258             
SEQADV 5JNE SER A  165  UNP  Q04195              EXPRESSION TAG                 
SEQADV 5JNE LEU A  166  UNP  Q04195              EXPRESSION TAG                 
SEQADV 5JNE ASP A  361  UNP  Q04195    CYS   361 ENGINEERED MUTATION            
SEQADV 5JNE ASP A  446  UNP  Q04195              LINKER                         
SEQADV 5JNE ASP A  447  UNP  Q04195              LINKER                         
SEQADV 5JNE ASP A  448  UNP  Q04195              LINKER                         
SEQADV 5JNE ASP A  449  UNP  Q04195              LINKER                         
SEQADV 5JNE LYS A  450  UNP  Q04195              LINKER                         
SEQADV 5JNE LEU A  451  UNP  Q04195              LINKER                         
SEQADV 5JNE ARG A  452  UNP  Q04195              LINKER                         
SEQADV 5JNE GLY B   -2  UNP  P50623              EXPRESSION TAG                 
SEQADV 5JNE SER B   -1  UNP  P50623              EXPRESSION TAG                 
SEQADV 5JNE HIS B    0  UNP  P50623              EXPRESSION TAG                 
SEQADV 5JNE SER B    5  UNP  P50623    CYS     5 ENGINEERED MUTATION            
SEQADV 5JNE LYS B  129  UNP  P50623    ALA   129 ENGINEERED MUTATION            
SEQADV 5JNE ARG B  153  UNP  P50623    LYS   153 ENGINEERED MUTATION            
SEQADV 5JNE GLY C   15  UNP  Q12306              EXPRESSION TAG                 
SEQADV 5JNE SER C   16  UNP  Q12306              EXPRESSION TAG                 
SEQADV 5JNE HIS C   17  UNP  Q12306              EXPRESSION TAG                 
SEQADV 5JNE MET C   18  UNP  Q12306              EXPRESSION TAG                 
SEQADV 5JNE ARG C   19  UNP  Q12306    LYS    19 ENGINEERED MUTATION            
SEQADV 5JNE ASP D   77  UNP  P15873    LYS    77 ENGINEERED MUTATION            
SEQADV 5JNE GLU D   81  UNP  P15873    CYS    81 ENGINEERED MUTATION            
SEQADV 5JNE ASP D  110  UNP  P15873    ARG   110 ENGINEERED MUTATION            
SEQADV 5JNE GLY D  127  UNP  P15873    LYS   127 ENGINEERED MUTATION            
SEQADV 5JNE CYS D  164  UNP  P15873    LYS   164 ENGINEERED MUTATION            
SEQADV 5JNE SER E  165  UNP  Q04195              EXPRESSION TAG                 
SEQADV 5JNE LEU E  166  UNP  Q04195              EXPRESSION TAG                 
SEQADV 5JNE ASP E  361  UNP  Q04195    CYS   361 ENGINEERED MUTATION            
SEQADV 5JNE ASP E  446  UNP  Q04195              LINKER                         
SEQADV 5JNE ASP E  447  UNP  Q04195              LINKER                         
SEQADV 5JNE ASP E  448  UNP  Q04195              LINKER                         
SEQADV 5JNE ASP E  449  UNP  Q04195              LINKER                         
SEQADV 5JNE LYS E  450  UNP  Q04195              LINKER                         
SEQADV 5JNE LEU E  451  UNP  Q04195              LINKER                         
SEQADV 5JNE ARG E  452  UNP  Q04195              LINKER                         
SEQADV 5JNE GLY F   -2  UNP  P50623              EXPRESSION TAG                 
SEQADV 5JNE SER F   -1  UNP  P50623              EXPRESSION TAG                 
SEQADV 5JNE HIS F    0  UNP  P50623              EXPRESSION TAG                 
SEQADV 5JNE SER F    5  UNP  P50623    CYS     5 ENGINEERED MUTATION            
SEQADV 5JNE LYS F  129  UNP  P50623    ALA   129 ENGINEERED MUTATION            
SEQADV 5JNE ARG F  153  UNP  P50623    LYS   153 ENGINEERED MUTATION            
SEQADV 5JNE GLY G   15  UNP  Q12306              EXPRESSION TAG                 
SEQADV 5JNE SER G   16  UNP  Q12306              EXPRESSION TAG                 
SEQADV 5JNE HIS G   17  UNP  Q12306              EXPRESSION TAG                 
SEQADV 5JNE MET G   18  UNP  Q12306              EXPRESSION TAG                 
SEQADV 5JNE ARG G   19  UNP  Q12306    LYS    19 ENGINEERED MUTATION            
SEQADV 5JNE ASP H   77  UNP  P15873    LYS    77 ENGINEERED MUTATION            
SEQADV 5JNE GLU H   81  UNP  P15873    CYS    81 ENGINEERED MUTATION            
SEQADV 5JNE ASP H  110  UNP  P15873    ARG   110 ENGINEERED MUTATION            
SEQADV 5JNE GLY H  127  UNP  P15873    LYS   127 ENGINEERED MUTATION            
SEQADV 5JNE CYS H  164  UNP  P15873    LYS   164 ENGINEERED MUTATION            
SEQRES   1 A  367  SER LEU SER SER SER PHE ALA VAL PRO THR ILE HIS PHE          
SEQRES   2 A  367  LYS GLU SER PRO PHE TYR LYS ILE GLN ARG LEU ILE PRO          
SEQRES   3 A  367  GLU LEU VAL MET ASN VAL GLU VAL THR GLY GLY ARG GLY          
SEQRES   4 A  367  MET CYS SER ALA LYS PHE LYS LEU SER LYS ALA ASP TYR          
SEQRES   5 A  367  ASN LEU LEU SER ASN PRO ASN SER LYS HIS ARG LEU TYR          
SEQRES   6 A  367  LEU PHE SER GLY MET ILE ASN PRO LEU GLY SER ARG GLY          
SEQRES   7 A  367  ASN GLU PRO ILE GLN PHE PRO PHE PRO ASN GLU LEU ARG          
SEQRES   8 A  367  CYS ASN ASN VAL GLN ILE LYS ASP ASN ILE ARG GLY PHE          
SEQRES   9 A  367  LYS SER LYS PRO GLY THR ALA LYS PRO ALA ASP LEU THR          
SEQRES  10 A  367  PRO HIS LEU LYS PRO TYR THR GLN GLN ASN ASN VAL GLU          
SEQRES  11 A  367  LEU ILE TYR ALA PHE THR THR LYS GLU TYR LYS LEU PHE          
SEQRES  12 A  367  GLY TYR ILE VAL GLU MET ILE THR PRO GLU GLN LEU LEU          
SEQRES  13 A  367  GLU LYS VAL LEU GLN HIS PRO LYS ILE ILE LYS GLN ALA          
SEQRES  14 A  367  THR LEU LEU TYR LEU LYS LYS THR LEU ARG GLU ASP GLU          
SEQRES  15 A  367  GLU MET GLY LEU THR THR THR SER THR ILE MET SER LEU          
SEQRES  16 A  367  GLN ASP PRO ILE SER TYR THR ARG MET LYS TYR PRO SER          
SEQRES  17 A  367  LYS SER ILE ASN CYS LYS HIS LEU GLN CYS PHE ASP ALA          
SEQRES  18 A  367  LEU TRP PHE LEU HIS SER GLN LEU GLN ILE PRO THR TRP          
SEQRES  19 A  367  GLN CYS PRO VAL CYS GLN ILE ASP ILE ALA LEU GLU ASN          
SEQRES  20 A  367  LEU ALA ILE SER GLU PHE VAL ASP ASP ILE LEU GLN ASN          
SEQRES  21 A  367  CYS GLN LYS ASN VAL GLU GLN VAL GLU LEU THR SER ASP          
SEQRES  22 A  367  GLY LYS TRP THR ALA ILE LEU GLU ASP ASP ASP ASP LYS          
SEQRES  23 A  367  LEU ARG PRO GLU THR HIS ILE ASN LEU LYS VAL SER ASP          
SEQRES  24 A  367  GLY SER SER GLU ILE PHE PHE LYS ILE LYS LYS THR THR          
SEQRES  25 A  367  PRO LEU ARG ARG LEU MET GLU ALA PHE ALA LYS ARG GLN          
SEQRES  26 A  367  GLY LYS GLU MET ASP SER LEU ARG PHE LEU TYR ASP GLY          
SEQRES  27 A  367  ILE ARG ILE GLN ALA ASP GLN THR PRO GLU ASP LEU ASP          
SEQRES  28 A  367  MET GLU ASP ASN ASP ILE ILE GLU ALA HIS ARG GLU GLN          
SEQRES  29 A  367  ILE GLY GLY                                                  
SEQRES   1 B  160  GLY SER HIS MET SER SER LEU SER LEU GLN ARG LEU GLN          
SEQRES   2 B  160  GLU GLU ARG LYS LYS TRP ARG LYS ASP HIS PRO PHE GLY          
SEQRES   3 B  160  PHE TYR ALA LYS PRO VAL LYS LYS ALA ASP GLY SER MET          
SEQRES   4 B  160  ASP LEU GLN LYS TRP GLU ALA GLY ILE PRO GLY LYS GLU          
SEQRES   5 B  160  GLY THR ASN TRP ALA GLY GLY VAL TYR PRO ILE THR VAL          
SEQRES   6 B  160  GLU TYR PRO ASN GLU TYR PRO SER LYS PRO PRO LYS VAL          
SEQRES   7 B  160  LYS PHE PRO ALA GLY PHE TYR HIS PRO ASN VAL TYR PRO          
SEQRES   8 B  160  SER GLY THR ILE CYS LEU SER ILE LEU ASN GLU ASP GLN          
SEQRES   9 B  160  ASP TRP ARG PRO ALA ILE THR LEU LYS GLN ILE VAL LEU          
SEQRES  10 B  160  GLY VAL GLN ASP LEU LEU ASP SER PRO ASN PRO ASN SER          
SEQRES  11 B  160  PRO LYS GLN GLU PRO ALA TRP ARG SER PHE SER ARG ASN          
SEQRES  12 B  160  LYS ALA GLU TYR ASP LYS LYS VAL LEU LEU GLN ALA ARG          
SEQRES  13 B  160  GLN TYR SER LYS                                              
SEQRES   1 C   84  GLY SER HIS MET ARG PRO GLU THR HIS ILE ASN LEU LYS          
SEQRES   2 C   84  VAL SER ASP GLY SER SER GLU ILE PHE PHE LYS ILE LYS          
SEQRES   3 C   84  LYS THR THR PRO LEU ARG ARG LEU MET GLU ALA PHE ALA          
SEQRES   4 C   84  LYS ARG GLN GLY LYS GLU MET ASP SER LEU ARG PHE LEU          
SEQRES   5 C   84  TYR ASP GLY ILE ARG ILE GLN ALA ASP GLN THR PRO GLU          
SEQRES   6 C   84  ASP LEU ASP MET GLU ASP ASN ASP ILE ILE GLU ALA HIS          
SEQRES   7 C   84  ARG GLU GLN ILE GLY GLY                                      
SEQRES   1 D  258  MET LEU GLU ALA LYS PHE GLU GLU ALA SER LEU PHE LYS          
SEQRES   2 D  258  ARG ILE ILE ASP GLY PHE LYS ASP CYS VAL GLN LEU VAL          
SEQRES   3 D  258  ASN PHE GLN CYS LYS GLU ASP GLY ILE ILE ALA GLN ALA          
SEQRES   4 D  258  VAL ASP ASP SER ARG VAL LEU LEU VAL SER LEU GLU ILE          
SEQRES   5 D  258  GLY VAL GLU ALA PHE GLN GLU TYR ARG CYS ASP HIS PRO          
SEQRES   6 D  258  VAL THR LEU GLY MET ASP LEU THR SER LEU SER ASP ILE          
SEQRES   7 D  258  LEU ARG GLU GLY ASN ASN THR ASP THR LEU THR LEU ILE          
SEQRES   8 D  258  ALA ASP ASN THR PRO ASP SER ILE ILE LEU LEU PHE GLU          
SEQRES   9 D  258  ASP THR LYS LYS ASP ASP ILE ALA GLU TYR SER LEU LYS          
SEQRES  10 D  258  LEU MET ASP ILE ASP ALA ASP PHE LEU GLY ILE GLU GLU          
SEQRES  11 D  258  LEU GLN TYR ASP SER THR LEU SER LEU PRO SER SER GLU          
SEQRES  12 D  258  PHE SER LYS ILE VAL ARG ASP LEU SER GLN LEU SER ASP          
SEQRES  13 D  258  SER ILE ASN ILE MET ILE THR CYS GLU THR ILE LYS PHE          
SEQRES  14 D  258  VAL ALA ASP GLY ASP ILE GLY SER GLY SER VAL ILE ILE          
SEQRES  15 D  258  LYS PRO PHE VAL ASP MET GLU HIS PRO GLU THR SER ILE          
SEQRES  16 D  258  LYS LEU GLU MET ASP GLN PRO VAL ASP LEU THR PHE GLY          
SEQRES  17 D  258  ALA LYS TYR LEU LEU ASP ILE ILE LYS GLY SER SER LEU          
SEQRES  18 D  258  SER ASP ARG VAL GLY ILE ARG LEU SER SER GLU ALA PRO          
SEQRES  19 D  258  ALA LEU PHE GLN PHE ASP LEU LYS SER GLY PHE LEU GLN          
SEQRES  20 D  258  PHE PHE LEU ALA PRO LYS PHE ASN ASP GLU GLU                  
SEQRES   1 E  367  SER LEU SER SER SER PHE ALA VAL PRO THR ILE HIS PHE          
SEQRES   2 E  367  LYS GLU SER PRO PHE TYR LYS ILE GLN ARG LEU ILE PRO          
SEQRES   3 E  367  GLU LEU VAL MET ASN VAL GLU VAL THR GLY GLY ARG GLY          
SEQRES   4 E  367  MET CYS SER ALA LYS PHE LYS LEU SER LYS ALA ASP TYR          
SEQRES   5 E  367  ASN LEU LEU SER ASN PRO ASN SER LYS HIS ARG LEU TYR          
SEQRES   6 E  367  LEU PHE SER GLY MET ILE ASN PRO LEU GLY SER ARG GLY          
SEQRES   7 E  367  ASN GLU PRO ILE GLN PHE PRO PHE PRO ASN GLU LEU ARG          
SEQRES   8 E  367  CYS ASN ASN VAL GLN ILE LYS ASP ASN ILE ARG GLY PHE          
SEQRES   9 E  367  LYS SER LYS PRO GLY THR ALA LYS PRO ALA ASP LEU THR          
SEQRES  10 E  367  PRO HIS LEU LYS PRO TYR THR GLN GLN ASN ASN VAL GLU          
SEQRES  11 E  367  LEU ILE TYR ALA PHE THR THR LYS GLU TYR LYS LEU PHE          
SEQRES  12 E  367  GLY TYR ILE VAL GLU MET ILE THR PRO GLU GLN LEU LEU          
SEQRES  13 E  367  GLU LYS VAL LEU GLN HIS PRO LYS ILE ILE LYS GLN ALA          
SEQRES  14 E  367  THR LEU LEU TYR LEU LYS LYS THR LEU ARG GLU ASP GLU          
SEQRES  15 E  367  GLU MET GLY LEU THR THR THR SER THR ILE MET SER LEU          
SEQRES  16 E  367  GLN ASP PRO ILE SER TYR THR ARG MET LYS TYR PRO SER          
SEQRES  17 E  367  LYS SER ILE ASN CYS LYS HIS LEU GLN CYS PHE ASP ALA          
SEQRES  18 E  367  LEU TRP PHE LEU HIS SER GLN LEU GLN ILE PRO THR TRP          
SEQRES  19 E  367  GLN CYS PRO VAL CYS GLN ILE ASP ILE ALA LEU GLU ASN          
SEQRES  20 E  367  LEU ALA ILE SER GLU PHE VAL ASP ASP ILE LEU GLN ASN          
SEQRES  21 E  367  CYS GLN LYS ASN VAL GLU GLN VAL GLU LEU THR SER ASP          
SEQRES  22 E  367  GLY LYS TRP THR ALA ILE LEU GLU ASP ASP ASP ASP LYS          
SEQRES  23 E  367  LEU ARG PRO GLU THR HIS ILE ASN LEU LYS VAL SER ASP          
SEQRES  24 E  367  GLY SER SER GLU ILE PHE PHE LYS ILE LYS LYS THR THR          
SEQRES  25 E  367  PRO LEU ARG ARG LEU MET GLU ALA PHE ALA LYS ARG GLN          
SEQRES  26 E  367  GLY LYS GLU MET ASP SER LEU ARG PHE LEU TYR ASP GLY          
SEQRES  27 E  367  ILE ARG ILE GLN ALA ASP GLN THR PRO GLU ASP LEU ASP          
SEQRES  28 E  367  MET GLU ASP ASN ASP ILE ILE GLU ALA HIS ARG GLU GLN          
SEQRES  29 E  367  ILE GLY GLY                                                  
SEQRES   1 F  160  GLY SER HIS MET SER SER LEU SER LEU GLN ARG LEU GLN          
SEQRES   2 F  160  GLU GLU ARG LYS LYS TRP ARG LYS ASP HIS PRO PHE GLY          
SEQRES   3 F  160  PHE TYR ALA LYS PRO VAL LYS LYS ALA ASP GLY SER MET          
SEQRES   4 F  160  ASP LEU GLN LYS TRP GLU ALA GLY ILE PRO GLY LYS GLU          
SEQRES   5 F  160  GLY THR ASN TRP ALA GLY GLY VAL TYR PRO ILE THR VAL          
SEQRES   6 F  160  GLU TYR PRO ASN GLU TYR PRO SER LYS PRO PRO LYS VAL          
SEQRES   7 F  160  LYS PHE PRO ALA GLY PHE TYR HIS PRO ASN VAL TYR PRO          
SEQRES   8 F  160  SER GLY THR ILE CYS LEU SER ILE LEU ASN GLU ASP GLN          
SEQRES   9 F  160  ASP TRP ARG PRO ALA ILE THR LEU LYS GLN ILE VAL LEU          
SEQRES  10 F  160  GLY VAL GLN ASP LEU LEU ASP SER PRO ASN PRO ASN SER          
SEQRES  11 F  160  PRO LYS GLN GLU PRO ALA TRP ARG SER PHE SER ARG ASN          
SEQRES  12 F  160  LYS ALA GLU TYR ASP LYS LYS VAL LEU LEU GLN ALA ARG          
SEQRES  13 F  160  GLN TYR SER LYS                                              
SEQRES   1 G   84  GLY SER HIS MET ARG PRO GLU THR HIS ILE ASN LEU LYS          
SEQRES   2 G   84  VAL SER ASP GLY SER SER GLU ILE PHE PHE LYS ILE LYS          
SEQRES   3 G   84  LYS THR THR PRO LEU ARG ARG LEU MET GLU ALA PHE ALA          
SEQRES   4 G   84  LYS ARG GLN GLY LYS GLU MET ASP SER LEU ARG PHE LEU          
SEQRES   5 G   84  TYR ASP GLY ILE ARG ILE GLN ALA ASP GLN THR PRO GLU          
SEQRES   6 G   84  ASP LEU ASP MET GLU ASP ASN ASP ILE ILE GLU ALA HIS          
SEQRES   7 G   84  ARG GLU GLN ILE GLY GLY                                      
SEQRES   1 H  258  MET LEU GLU ALA LYS PHE GLU GLU ALA SER LEU PHE LYS          
SEQRES   2 H  258  ARG ILE ILE ASP GLY PHE LYS ASP CYS VAL GLN LEU VAL          
SEQRES   3 H  258  ASN PHE GLN CYS LYS GLU ASP GLY ILE ILE ALA GLN ALA          
SEQRES   4 H  258  VAL ASP ASP SER ARG VAL LEU LEU VAL SER LEU GLU ILE          
SEQRES   5 H  258  GLY VAL GLU ALA PHE GLN GLU TYR ARG CYS ASP HIS PRO          
SEQRES   6 H  258  VAL THR LEU GLY MET ASP LEU THR SER LEU SER ASP ILE          
SEQRES   7 H  258  LEU ARG GLU GLY ASN ASN THR ASP THR LEU THR LEU ILE          
SEQRES   8 H  258  ALA ASP ASN THR PRO ASP SER ILE ILE LEU LEU PHE GLU          
SEQRES   9 H  258  ASP THR LYS LYS ASP ASP ILE ALA GLU TYR SER LEU LYS          
SEQRES  10 H  258  LEU MET ASP ILE ASP ALA ASP PHE LEU GLY ILE GLU GLU          
SEQRES  11 H  258  LEU GLN TYR ASP SER THR LEU SER LEU PRO SER SER GLU          
SEQRES  12 H  258  PHE SER LYS ILE VAL ARG ASP LEU SER GLN LEU SER ASP          
SEQRES  13 H  258  SER ILE ASN ILE MET ILE THR CYS GLU THR ILE LYS PHE          
SEQRES  14 H  258  VAL ALA ASP GLY ASP ILE GLY SER GLY SER VAL ILE ILE          
SEQRES  15 H  258  LYS PRO PHE VAL ASP MET GLU HIS PRO GLU THR SER ILE          
SEQRES  16 H  258  LYS LEU GLU MET ASP GLN PRO VAL ASP LEU THR PHE GLY          
SEQRES  17 H  258  ALA LYS TYR LEU LEU ASP ILE ILE LYS GLY SER SER LEU          
SEQRES  18 H  258  SER ASP ARG VAL GLY ILE ARG LEU SER SER GLU ALA PRO          
SEQRES  19 H  258  ALA LEU PHE GLN PHE ASP LEU LYS SER GLY PHE LEU GLN          
SEQRES  20 H  258  PHE PHE LEU ALA PRO LYS PHE ASN ASP GLU GLU                  
HET     ZN  A 601       1                                                       
HET    GOL  A 602       6                                                       
HET    GOL  A 603       6                                                       
HET    GOL  A 604       6                                                       
HET    6LN  B 201       4                                                       
HET    GOL  D 301       6                                                       
HET    GOL  D 302       6                                                       
HET    GOL  D 303       6                                                       
HET     ZN  E 601       1                                                       
HET    GOL  E 602       6                                                       
HET    GOL  E 603       6                                                       
HET    6LN  F 201       4                                                       
HET    GOL  H 301       6                                                       
HET    GOL  H 302       6                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM     GOL GLYCEROL                                                         
HETNAM     6LN ETHANE-1,2-DITHIOL                                               
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   9   ZN    2(ZN 2+)                                                     
FORMUL  10  GOL    10(C3 H8 O3)                                                 
FORMUL  13  6LN    2(C2 H6 S2)                                                  
FORMUL  23  HOH   *271(H2 O)                                                    
HELIX    1 AA1 SER A  212  ASN A  221  1                                  10    
HELIX    2 AA2 THR A  281  LEU A  284  5                                   4    
HELIX    3 AA3 THR A  315  HIS A  326  1                                  12    
HELIX    4 AA4 ILE A  330  MET A  348  1                                  19    
HELIX    5 AA5 ALA A  385  ILE A  395  1                                  11    
HELIX    6 AA6 ALA A  408  GLU A  410  5                                   3    
HELIX    7 AA7 SER A  415  ASN A  424  1                                  10    
HELIX    8 AA8 LEU A  478  GLN A  489  1                                  12    
HELIX    9 AA9 GLU A  492  LEU A  496  5                                   5    
HELIX   10 AB1 SER B    2  ASP B   19  1                                  18    
HELIX   11 AB2 LEU B   94  ASN B   98  5                                   5    
HELIX   12 AB3 THR B  108  ASP B  121  1                                  14    
HELIX   13 AB4 GLU B  131  ASN B  140  1                                  10    
HELIX   14 AB5 ASN B  140  TYR B  155  1                                  16    
HELIX   15 AB6 PRO C   44  ARG C   55  1                                  12    
HELIX   16 AB7 GLU C   59  ASP C   61  5                                   3    
HELIX   17 AB8 GLU D    8  GLY D   18  1                                  11    
HELIX   18 AB9 LEU D   72  GLY D   82  1                                  11    
HELIX   19 AC1 SER D  141  GLN D  153  1                                  13    
HELIX   20 AC2 HIS D  190  SER D  194  5                                   5    
HELIX   21 AC3 ALA D  209  ILE D  216  1                                   8    
HELIX   22 AC4 LYS D  217  LEU D  221  5                                   5    
HELIX   23 AC5 SER E  212  ASN E  221  1                                  10    
HELIX   24 AC6 THR E  281  LEU E  284  5                                   4    
HELIX   25 AC7 THR E  315  HIS E  326  1                                  12    
HELIX   26 AC8 ILE E  330  GLY E  349  1                                  20    
HELIX   27 AC9 ALA E  385  ILE E  395  1                                  11    
HELIX   28 AD1 ALA E  408  GLU E  410  5                                   3    
HELIX   29 AD2 SER E  415  ASN E  424  1                                  10    
HELIX   30 AD3 LEU E  478  GLN E  489  1                                  12    
HELIX   31 AD4 GLU E  492  ASP E  494  5                                   3    
HELIX   32 AD5 SER F    2  ASP F   19  1                                  18    
HELIX   33 AD6 LEU F   94  ASN F   98  5                                   5    
HELIX   34 AD7 THR F  108  ASP F  121  1                                  14    
HELIX   35 AD8 GLU F  131  ASN F  140  1                                  10    
HELIX   36 AD9 ASN F  140  TYR F  155  1                                  16    
HELIX   37 AE1 LEU G   45  GLN G   56  1                                  12    
HELIX   38 AE2 GLU G   59  ASP G   61  5                                   3    
HELIX   39 AE3 GLU H    8  GLY H   18  1                                  11    
HELIX   40 AE4 LEU H   72  GLY H   82  1                                  11    
HELIX   41 AE5 SER H  141  GLN H  153  1                                  13    
HELIX   42 AE6 HIS H  190  SER H  194  5                                   5    
HELIX   43 AE7 ALA H  209  ILE H  216  1                                   8    
HELIX   44 AE8 LYS H  217  SER H  219  5                                   3    
SHEET    1 AA1 4 TYR A 183  VAL A 196  0                                        
SHEET    2 AA1 4 TYR A 304  MET A 313 -1  O  ILE A 310   N  GLN A 186           
SHEET    3 AA1 4 HIS A 226  MET A 234 -1  N  GLY A 233   O  LYS A 305           
SHEET    4 AA1 4 ALA A 278  ASP A 279 -1  O  ALA A 278   N  LEU A 230           
SHEET    1 AA2 4 THR A 199  PHE A 209  0                                        
SHEET    2 AA2 4 ASN A 291  THR A 300 -1  O  TYR A 297   N  GLY A 203           
SHEET    3 AA2 4 ASN A 252  CYS A 256 -1  N  ARG A 255   O  GLU A 294           
SHEET    4 AA2 4 VAL A 259  GLN A 260 -1  O  VAL A 259   N  CYS A 256           
SHEET    1 AA3 8 TRP A 440  ALA A 442  0                                        
SHEET    2 AA3 8 GLN A 431  LEU A 434 -1  N  GLU A 433   O  THR A 441           
SHEET    3 AA3 8 SER A 354  SER A 358 -1  N  THR A 355   O  LEU A 434           
SHEET    4 AA3 8 GLU C  34  LYS C  40 -1  O  GLU C  34   N  ILE A 356           
SHEET    5 AA3 8 HIS C  23  SER C  29 -1  N  LEU C  26   O  PHE C  37           
SHEET    6 AA3 8 ASP C  87  ARG C  93  1  O  ILE C  89   N  LYS C  27           
SHEET    7 AA3 8 LEU C  63  TYR C  67 -1  N  ARG C  64   O  HIS C  92           
SHEET    8 AA3 8 ILE C  70  ARG C  71 -1  O  ILE C  70   N  TYR C  67           
SHEET    1 AA4 3 PHE A 383  ASP A 384  0                                        
SHEET    2 AA4 3 PRO A 371  SER A 374 -1  N  SER A 372   O  PHE A 383           
SHEET    3 AA4 3 LEU A 412  ILE A 414 -1  O  ALA A 413   N  LYS A 373           
SHEET    1 AA5 5 GLU A 467  LYS A 473  0                                        
SHEET    2 AA5 5 HIS A 456  SER A 462 -1  N  VAL A 461   O  ILE A 468           
SHEET    3 AA5 5 ASP A 520  HIS A 525  1  O  ALA A 524   N  SER A 462           
SHEET    4 AA5 5 ARG A 497  TYR A 500 -1  N  LEU A 499   O  GLU A 523           
SHEET    5 AA5 5 ILE A 503  ARG A 504 -1  O  ILE A 503   N  TYR A 500           
SHEET    1 AA6 4 TYR B  25  LYS B  30  0                                        
SHEET    2 AA6 4 MET B  36  PRO B  46 -1  O  GLU B  42   N  LYS B  27           
SHEET    3 AA6 4 VAL B  57  GLU B  63 -1  O  TYR B  58   N  ILE B  45           
SHEET    4 AA6 4 LYS B  74  LYS B  76 -1  O  LYS B  74   N  GLU B  63           
SHEET    1 AA7 4 LEU D   2  LYS D   5  0                                        
SHEET    2 AA7 4 ASP D  86  ALA D  92 -1  O  LEU D  90   N  ALA D   4           
SHEET    3 AA7 4 SER D  98  ASP D 105 -1  O  LEU D 102   N  THR D  89           
SHEET    4 AA7 4 ILE D 111  LYS D 117 -1  O  ALA D 112   N  PHE D 103           
SHEET    1 AA8 9 VAL D  66  ASP D  71  0                                        
SHEET    2 AA8 9 LEU D  25  LYS D  31 -1  N  PHE D  28   O  LEU D  68           
SHEET    3 AA8 9 GLY D  34  VAL D  40 -1  O  ILE D  36   N  GLN D  29           
SHEET    4 AA8 9 LEU D  46  GLY D  53 -1  O  LEU D  50   N  ALA D  37           
SHEET    5 AA8 9 PHE D 245  LEU D 250 -1  O  GLN D 247   N  SER D  49           
SHEET    6 AA8 9 ALA D 235  ASP D 240 -1  N  ALA D 235   O  LEU D 250           
SHEET    7 AA8 9 ARG D 224  LEU D 229 -1  N  ARG D 228   O  LEU D 236           
SHEET    8 AA8 9 SER D 135  PRO D 140 -1  N  LEU D 137   O  ILE D 227           
SHEET    9 AA8 9 LYS D 196  MET D 199 -1  O  GLU D 198   N  THR D 136           
SHEET    1 AA9 4 SER D 177  ILE D 182  0                                        
SHEET    2 AA9 4 ILE D 167  ASP D 172 -1  N  PHE D 169   O  VAL D 180           
SHEET    3 AA9 4 SER D 157  ILE D 162 -1  N  ASN D 159   O  VAL D 170           
SHEET    4 AA9 4 ASP D 204  GLY D 208 -1  O  PHE D 207   N  ILE D 158           
SHEET    1 AB1 4 TYR E 183  VAL E 196  0                                        
SHEET    2 AB1 4 GLU E 303  MET E 313 -1  O  ILE E 310   N  GLN E 186           
SHEET    3 AB1 4 HIS E 226  ILE E 235 -1  N  ILE E 235   O  GLU E 303           
SHEET    4 AB1 4 ALA E 278  ASP E 279 -1  O  ALA E 278   N  LEU E 230           
SHEET    1 AB2 4 THR E 199  PHE E 209  0                                        
SHEET    2 AB2 4 ASN E 291  THR E 300 -1  O  VAL E 293   N  ALA E 207           
SHEET    3 AB2 4 ASN E 252  CYS E 256 -1  N  ARG E 255   O  GLU E 294           
SHEET    4 AB2 4 VAL E 259  ILE E 261 -1  O  ILE E 261   N  LEU E 254           
SHEET    1 AB3 8 TRP E 440  ALA E 442  0                                        
SHEET    2 AB3 8 GLN E 431  LEU E 434 -1  N  GLU E 433   O  THR E 441           
SHEET    3 AB3 8 THR E 351  SER E 358 -1  N  THR E 355   O  LEU E 434           
SHEET    4 AB3 8 GLU G  34  LYS G  40 -1  O  GLU G  34   N  ILE E 356           
SHEET    5 AB3 8 HIS G  23  SER G  29 -1  N  LEU G  26   O  PHE G  37           
SHEET    6 AB3 8 ASP G  87  ARG G  93  1  O  ILE G  89   N  LYS G  27           
SHEET    7 AB3 8 LEU G  63  TYR G  67 -1  N  ARG G  64   O  HIS G  92           
SHEET    8 AB3 8 ILE G  70  ARG G  71 -1  O  ILE G  70   N  TYR G  67           
SHEET    1 AB4 3 PHE E 383  ASP E 384  0                                        
SHEET    2 AB4 3 PRO E 371  SER E 374 -1  N  SER E 372   O  PHE E 383           
SHEET    3 AB4 3 LEU E 412  ILE E 414 -1  O  ALA E 413   N  LYS E 373           
SHEET    1 AB5 5 GLU E 467  LYS E 473  0                                        
SHEET    2 AB5 5 HIS E 456  SER E 462 -1  N  LEU E 459   O  PHE E 470           
SHEET    3 AB5 5 ASP E 520  ARG E 526  1  O  ASP E 520   N  LYS E 460           
SHEET    4 AB5 5 LEU E 496  TYR E 500 -1  N  LEU E 499   O  GLU E 523           
SHEET    5 AB5 5 ILE E 503  ARG E 504 -1  O  ILE E 503   N  TYR E 500           
SHEET    1 AB6 4 TYR F  25  LYS F  30  0                                        
SHEET    2 AB6 4 MET F  36  PRO F  46 -1  O  GLU F  42   N  LYS F  27           
SHEET    3 AB6 4 VAL F  57  GLU F  63 -1  O  ILE F  60   N  ALA F  43           
SHEET    4 AB6 4 LYS F  74  LYS F  76 -1  O  LYS F  74   N  GLU F  63           
SHEET    1 AB7 5 GLU H  59  CYS H  62  0                                        
SHEET    2 AB7 5 LEU H   2  LYS H   5 -1  N  LYS H   5   O  GLU H  59           
SHEET    3 AB7 5 ASP H  86  ALA H  92 -1  O  LEU H  90   N  ALA H   4           
SHEET    4 AB7 5 SER H  98  ASP H 105 -1  O  ILE H 100   N  ILE H  91           
SHEET    5 AB7 5 ILE H 111  LYS H 117 -1  O  ALA H 112   N  PHE H 103           
SHEET    1 AB8 9 VAL H  66  ASP H  71  0                                        
SHEET    2 AB8 9 LEU H  25  CYS H  30 -1  N  CYS H  30   O  VAL H  66           
SHEET    3 AB8 9 GLY H  34  VAL H  40 -1  O  ILE H  36   N  GLN H  29           
SHEET    4 AB8 9 LEU H  46  GLY H  53 -1  O  LEU H  50   N  ALA H  37           
SHEET    5 AB8 9 GLY H 244  LEU H 250 -1  O  PHE H 249   N  LEU H  47           
SHEET    6 AB8 9 ALA H 235  LEU H 241 -1  N  PHE H 237   O  PHE H 248           
SHEET    7 AB8 9 ARG H 224  LEU H 229 -1  N  GLY H 226   O  GLN H 238           
SHEET    8 AB8 9 SER H 135  PRO H 140 -1  N  LEU H 137   O  ILE H 227           
SHEET    9 AB8 9 LYS H 196  MET H 199 -1  O  GLU H 198   N  THR H 136           
SHEET    1 AB9 4 SER H 177  ILE H 182  0                                        
SHEET    2 AB9 4 THR H 166  ASP H 172 -1  N  PHE H 169   O  VAL H 180           
SHEET    3 AB9 4 SER H 157  THR H 163 -1  N  ASN H 159   O  VAL H 170           
SHEET    4 AB9 4 VAL H 203  GLY H 208 -1  O  LEU H 205   N  ILE H 160           
SSBOND   1 CYS B   93    6LN B  201                          1555   1555  2.08  
SSBOND   2 CYS D  164    6LN B  201                          1555   1555  2.05  
SSBOND   3 CYS F   93    6LN F  201                          1555   1555  2.11  
SSBOND   4 CYS H  164    6LN F  201                          1555   1555  2.04  
LINK         SG  CYS A 377                ZN    ZN A 601     1555   1555  2.30  
LINK         NE2 HIS A 379                ZN    ZN A 601     1555   1555  2.03  
LINK         SG  CYS A 400                ZN    ZN A 601     1555   1555  2.27  
LINK         SG  CYS A 403                ZN    ZN A 601     1555   1555  2.29  
LINK         NZ  LYS B 129                 C   GLY C  98     1555   1555  1.35  
LINK         SG  CYS E 377                ZN    ZN E 601     1555   1555  2.30  
LINK         NE2 HIS E 379                ZN    ZN E 601     1555   1555  2.02  
LINK         SG  CYS E 400                ZN    ZN E 601     1555   1555  2.29  
LINK         SG  CYS E 403                ZN    ZN E 601     1555   1555  2.30  
LINK         NZ  LYS F 129                 C   GLY G  98     1555   1555  1.34  
CISPEP   1 PHE A  250    PRO A  251          0         1.42                     
CISPEP   2 TYR B   68    PRO B   69          0         3.61                     
CISPEP   3 PHE E  250    PRO E  251          0        -0.48                     
CISPEP   4 TYR F   68    PRO F   69          0         3.29                     
SITE     1 AC1  4 CYS A 377  HIS A 379  CYS A 400  CYS A 403                    
SITE     1 AC2  4 ILE A 175  HIS A 176  PHE A 177  TYR A 309                    
SITE     1 AC3  4 LYS A 178  TRP A 398  LEU A 409  GLU A 410                    
SITE     1 AC4  6 ALA A 333  THR A 334  LYS A 373  CYS A 377                    
SITE     2 AC4  6 LYS A 378  HIS A 379                                          
SITE     1 AC5  7 CYS B  93  LEU B  94  ASN B  98  GLN B 101                    
SITE     2 AC5  7 GLY C  97  GLY C  98  CYS D 164                               
SITE     1 AC6  5 LYS A 471  GLU D  81  ASP D  86  ASP D 105                    
SITE     2 AC6  5 ALA D 112                                                     
SITE     1 AC7  3 ARG A 488  GLU D 104  THR D 106                               
SITE     1 AC8  5 LYS A 302  GLN D 132  THR D 136  GLU D 198                    
SITE     2 AC8  5 ASP D 200                                                     
SITE     1 AC9  4 CYS E 377  HIS E 379  CYS E 400  CYS E 403                    
SITE     1 AD1  5 ILE E 175  HIS E 176  PHE E 177  ILE E 185                    
SITE     2 AD1  5 TYR E 309                                                     
SITE     1 AD2  3 LYS E 178  TRP E 398  GLU E 410                               
SITE     1 AD3  8 CYS F  93  LEU F  94  ASN F  98  GLN F 101                    
SITE     2 AD3  8 ILE G  96  GLY G  97  GLY G  98  CYS H 164                    
SITE     1 AD4  6 LYS E 471  GLU H  81  ASP H  86  PHE H 103                    
SITE     2 AD4  6 ASP H 105  ALA H 112                                          
SITE     1 AD5  5 LYS E 302  TYR H 133  THR H 136  GLU H 198                    
SITE     2 AD5  5 ASP H 200                                                     
SITE     1 AD6 21 PRO F  84  VAL F  86  TYR F  87  PRO F  88                    
SITE     2 AD6 21 CYS F  93  LEU F  94  SER F  95  ILE F  96                    
SITE     3 AD6 21 LEU F  97  GLU F  99  ASP F 100  GLN F 101                    
SITE     4 AD6 21 ASP F 102  TRP F 103  SER F 127  PRO F 128                    
SITE     5 AD6 21 GLN F 130  6LN F 201  GLY G  97  THR H 166                    
SITE     6 AD6 21 LYS H 183                                                     
CRYST1   93.421  205.882  142.501  90.00  95.30  90.00 C 1 2 1       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      0.010704  0.000000  0.000993        0.00000                         
SCALE2      0.000000  0.004857  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007048        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system