GenomeNet

Database: PDB
Entry: 4R8P
LinkDB: 4R8P
Original site: 4R8P 
HEADER    STRUCTURAL PROTEIN/DNA                  02-SEP-14   4R8P              
TITLE     CRYSTAL STRUCTURE OF THE RING1B/BMI1/UBCH5C PRC1 UBIQUITYLATION MODULE
TITLE    2 BOUND TO THE NUCLEOSOME CORE PARTICLE                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HISTONE H3.2;                                              
COMPND   3 CHAIN: A, E;                                                         
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MOL_ID: 2;                                                           
COMPND   6 MOLECULE: HISTONE H4;                                                
COMPND   7 CHAIN: B, F;                                                         
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MOL_ID: 3;                                                           
COMPND  10 MOLECULE: HISTONE H2A;                                               
COMPND  11 CHAIN: C, G;                                                         
COMPND  12 ENGINEERED: YES;                                                     
COMPND  13 MOL_ID: 4;                                                           
COMPND  14 MOLECULE: HISTONE H2B 1.1;                                           
COMPND  15 CHAIN: D, H;                                                         
COMPND  16 SYNONYM: H2B1.1;                                                     
COMPND  17 ENGINEERED: YES;                                                     
COMPND  18 MOL_ID: 5;                                                           
COMPND  19 MOLECULE: DNA (147-MER);                                             
COMPND  20 CHAIN: I;                                                            
COMPND  21 FRAGMENT: WIDOM 601 147-MER (+ STRAND);                              
COMPND  22 ENGINEERED: YES;                                                     
COMPND  23 MOL_ID: 6;                                                           
COMPND  24 MOLECULE: DNA (147-MER);                                             
COMPND  25 CHAIN: J;                                                            
COMPND  26 FRAGMENT: WIDOM 601 147-MER (- STRAND);                              
COMPND  27 ENGINEERED: YES;                                                     
COMPND  28 MOL_ID: 7;                                                           
COMPND  29 MOLECULE: POLYCOMB COMPLEX PROTEIN BMI-1;                            
COMPND  30 CHAIN: K, M;                                                         
COMPND  31 FRAGMENT: RESIDUES 2-109;                                            
COMPND  32 SYNONYM: POLYCOMB GROUP RING FINGER PROTEIN 4, RING FINGER PROTEIN   
COMPND  33 51;                                                                  
COMPND  34 ENGINEERED: YES;                                                     
COMPND  35 MOL_ID: 8;                                                           
COMPND  36 MOLECULE: E3 UBIQUITIN-PROTEIN LIGASE RING2, UBIQUITIN-CONJUGATING   
COMPND  37 ENZYME E2 D3;                                                        
COMPND  38 CHAIN: L, N;                                                         
COMPND  39 FRAGMENT: RESIDUES 2-116 OF RING1B AND RESIDUES 2-148 OF UBCH5C;     
COMPND  40 SYNONYM: HUNTINGTIN-INTERACTING PROTEIN 2-INTERACTING PROTEIN 3,     
COMPND  41 HIP2-INTERACTING PROTEIN 3, PROTEIN DING, RING FINGER PROTEIN 1B,    
COMPND  42 RING1B, RING FINGER PROTEIN 2, RING FINGER PROTEIN BAP-1, UBIQUITIN  
COMPND  43 CARRIER PROTEIN D3, UBIQUITIN-CONJUGATING ENZYME E2(17)KB 3,         
COMPND  44 UBIQUITIN-CONJUGATING ENZYME E2-17 KDA 3, UBIQUITIN-PROTEIN LIGASE   
COMPND  45 D3;                                                                  
COMPND  46 EC: 6.3.2.-, 6.3.2.19;                                               
COMPND  47 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: XENOPUS LAEVIS;                                 
SOURCE   3 ORGANISM_COMMON: CLAWED FROG,COMMON PLATANNA,PLATANNA;               
SOURCE   4 ORGANISM_TAXID: 8355;                                                
SOURCE   5 GENE: HISTONE H3.2;                                                  
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)PLYSS;                            
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET3D;                                    
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: XENOPUS LAEVIS;                                 
SOURCE  13 ORGANISM_COMMON: CLAWED FROG,COMMON PLATANNA,PLATANNA;               
SOURCE  14 ORGANISM_TAXID: 8355;                                                
SOURCE  15 GENE: HISTONE H4;                                                    
SOURCE  16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  18 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)PLYSS;                            
SOURCE  19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  20 EXPRESSION_SYSTEM_PLASMID: PET3A;                                    
SOURCE  21 MOL_ID: 3;                                                           
SOURCE  22 ORGANISM_SCIENTIFIC: XENOPUS LAEVIS;                                 
SOURCE  23 ORGANISM_COMMON: CLAWED FROG,COMMON PLATANNA,PLATANNA;               
SOURCE  24 ORGANISM_TAXID: 8355;                                                
SOURCE  25 GENE: HIST1H2AJ, LOC494591;                                          
SOURCE  26 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  27 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  28 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)PLYSS;                            
SOURCE  29 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  30 EXPRESSION_SYSTEM_PLASMID: PET3A;                                    
SOURCE  31 MOL_ID: 4;                                                           
SOURCE  32 ORGANISM_SCIENTIFIC: XENOPUS LAEVIS;                                 
SOURCE  33 ORGANISM_COMMON: CLAWED FROG,COMMON PLATANNA,PLATANNA;               
SOURCE  34 ORGANISM_TAXID: 8355;                                                
SOURCE  35 GENE: HISTONE H2B 1.1;                                               
SOURCE  36 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  37 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  38 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)PLYSS;                            
SOURCE  39 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  40 EXPRESSION_SYSTEM_PLASMID: PET3A;                                    
SOURCE  41 MOL_ID: 5;                                                           
SOURCE  42 ORGANISM_SCIENTIFIC: SYNTHETIC DNA;                                  
SOURCE  43 ORGANISM_TAXID: 32630;                                               
SOURCE  44 GENE: WIDOM 601 NUCLEOSOME POSITIONING SEQUENCE;                     
SOURCE  45 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  46 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  47 EXPRESSION_SYSTEM_STRAIN: HB101;                                     
SOURCE  48 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  49 EXPRESSION_SYSTEM_PLASMID: PST55;                                    
SOURCE  50 MOL_ID: 6;                                                           
SOURCE  51 ORGANISM_SCIENTIFIC: SYNTHETIC DNA;                                  
SOURCE  52 ORGANISM_TAXID: 32630;                                               
SOURCE  53 GENE: WIDOM 601 NUCLEOSOME POSITIONING SEQUENCE;                     
SOURCE  54 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  55 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  56 EXPRESSION_SYSTEM_STRAIN: HB101;                                     
SOURCE  57 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  58 EXPRESSION_SYSTEM_PLASMID: PST55;                                    
SOURCE  59 MOL_ID: 7;                                                           
SOURCE  60 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  61 ORGANISM_COMMON: HUMAN;                                              
SOURCE  62 ORGANISM_TAXID: 9606;                                                
SOURCE  63 GENE: BMI1, PCGF4, RNF51;                                            
SOURCE  64 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  65 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  66 EXPRESSION_SYSTEM_STRAIN: ROSETTA(DE3)PLYSS;                         
SOURCE  67 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  68 EXPRESSION_SYSTEM_PLASMID: PST44;                                    
SOURCE  69 MOL_ID: 8;                                                           
SOURCE  70 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  71 ORGANISM_COMMON: HUMAN;                                              
SOURCE  72 ORGANISM_TAXID: 9606;                                                
SOURCE  73 GENE: BAP1, DING, HIPI3, RING1B, RING1B-UBCH5C FUSION, RNF2, UBC5C,  
SOURCE  74 UBCH5C, UBE2D3;                                                      
SOURCE  75 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  76 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  77 EXPRESSION_SYSTEM_STRAIN: ROSETTA(DE3)PLYSS;                         
SOURCE  78 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  79 EXPRESSION_SYSTEM_PLASMID: PST44                                     
KEYWDS    RING DOMAIN, ARGININE ANCHOR, UBIQUITIN LIGASE, HISTONE MODIFICATION  
KEYWDS   2 ENZYME, STRUCTURAL PROTEIN-DNA COMPLEX                               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    R.K.MCGINTY,R.C.HENRICI,S.TAN                                         
REVDAT   3   02-AUG-17 4R8P    1       SOURCE REMARK                            
REVDAT   2   12-NOV-14 4R8P    1       JRNL                                     
REVDAT   1   05-NOV-14 4R8P    0                                                
JRNL        AUTH   R.K.MCGINTY,R.C.HENRICI,S.TAN                                
JRNL        TITL   CRYSTAL STRUCTURE OF THE PRC1 UBIQUITYLATION MODULE BOUND TO 
JRNL        TITL 2 THE NUCLEOSOME.                                              
JRNL        REF    NATURE                        V. 514   591 2014              
JRNL        REFN                   ISSN 0028-0836                               
JRNL        PMID   25355358                                                     
JRNL        DOI    10.1038/NATURE13890                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.28 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.8.4_1496                                    
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) : 3.28                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 45.00                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 54119                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.199                           
REMARK   3   R VALUE            (WORKING SET) : 0.197                           
REMARK   3   FREE R VALUE                     : 0.245                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.080                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2750                            
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 45.0038 -  8.8940    0.93     2602   106  0.1348 0.1724        
REMARK   3     2  8.8940 -  7.0683    0.98     2595   151  0.1520 0.2176        
REMARK   3     3  7.0683 -  6.1773    0.99     2602   135  0.2045 0.2377        
REMARK   3     4  6.1773 -  5.6137    0.99     2586   165  0.2097 0.2815        
REMARK   3     5  5.6137 -  5.2120    0.99     2568   127  0.1987 0.2096        
REMARK   3     6  5.2120 -  4.9051    0.99     2614   137  0.1847 0.2371        
REMARK   3     7  4.9051 -  4.6597    1.00     2590   133  0.1783 0.2281        
REMARK   3     8  4.6597 -  4.4570    1.00     2560   153  0.1794 0.1852        
REMARK   3     9  4.4570 -  4.2856    1.00     2572   126  0.1846 0.2471        
REMARK   3    10  4.2856 -  4.1378    1.00     2580   127  0.2000 0.2460        
REMARK   3    11  4.1378 -  4.0085    1.00     2513   146  0.2104 0.2771        
REMARK   3    12  4.0085 -  3.8940    0.99     2576   137  0.2327 0.2654        
REMARK   3    13  3.8940 -  3.7915    1.00     2570   142  0.2348 0.2898        
REMARK   3    14  3.7915 -  3.6991    1.00     2525   143  0.2403 0.2821        
REMARK   3    15  3.6991 -  3.6150    1.00     2564   127  0.2660 0.3247        
REMARK   3    16  3.6150 -  3.5381    1.00     2592   121  0.2661 0.2908        
REMARK   3    17  3.5381 -  3.4674    1.00     2518   151  0.2895 0.3391        
REMARK   3    18  3.4674 -  3.4020    0.99     2588   130  0.3119 0.3710        
REMARK   3    19  3.4020 -  3.3412    1.00     2537   141  0.3129 0.3451        
REMARK   3    20  3.3412 -  3.2846    0.99     2517   152  0.3283 0.3570        
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)     : 0.430            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.770           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 105.0                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 137.4                          
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      :  0.003          18059                                  
REMARK   3   ANGLE     :  0.504          25766                                  
REMARK   3   CHIRALITY :  0.020           2981                                  
REMARK   3   PLANARITY :  0.002           2282                                  
REMARK   3   DIHEDRAL  : 21.715           7054                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: ALL                                                    
REMARK   3    ORIGIN FOR THE GROUP (A):  29.2800  30.3205 -47.3430              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4614 T22:   0.3592                                     
REMARK   3      T33:   0.8379 T12:   0.0161                                     
REMARK   3      T13:   0.0646 T23:  -0.0613                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2820 L22:   0.8885                                     
REMARK   3      L33:   3.9550 L12:   0.2116                                     
REMARK   3      L13:   0.1594 L23:   0.1365                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0224 S12:   0.0905 S13:   0.1001                       
REMARK   3      S21:   0.3016 S22:  -0.0650 S23:   0.1810                       
REMARK   3      S31:   0.1288 S32:  -0.1509 S33:  -0.0273                       
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 4R8P COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-SEP-14.                  
REMARK 100 THE DEPOSITION ID IS D_1000087039.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 29-JUL-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
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) : 0.97918                            
REMARK 200  MONOCHROMATOR                  : SI(220)                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : SCALA 3.3.20                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 54142                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.285                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 45.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -4.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.4                               
REMARK 200  DATA REDUNDANCY                : 3.900                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.06300                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 16.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.28                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.46                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.64000                            
REMARK 200  R SYM FOR SHELL            (I) : 0.64000                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.200                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER 2.5.5                                          
REMARK 200 STARTING MODEL: POLYALANINE MODELS OF PDB ENTRIES 3RPG AND 3LZ0      
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 60.53                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.12                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 25 MM HEPES PH 7.5, 80 MM NH4NO3, 3 %    
REMARK 280  PEG2000-MME, MODIFIED MICRO BATCH UNDER OIL, TEMPERATURE 294K       
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      187.62550            
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      187.62550            
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       52.46150            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       90.02450            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       52.46150            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       90.02450            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000      187.62550            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       52.46150            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       90.02450            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000      187.62550            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       52.46150            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       90.02450            
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: TETRADECAMERIC                    
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I, J,         
REMARK 350                    AND CHAINS: K, L, M, N                            
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     ALA A     1                                                      
REMARK 465     ARG A     2                                                      
REMARK 465     THR A     3                                                      
REMARK 465     LYS A     4                                                      
REMARK 465     GLN A     5                                                      
REMARK 465     THR A     6                                                      
REMARK 465     ALA A     7                                                      
REMARK 465     ARG A     8                                                      
REMARK 465     LYS A     9                                                      
REMARK 465     SER A    10                                                      
REMARK 465     THR A    11                                                      
REMARK 465     GLY A    12                                                      
REMARK 465     GLY A    13                                                      
REMARK 465     LYS A    14                                                      
REMARK 465     ALA A    15                                                      
REMARK 465     PRO A    16                                                      
REMARK 465     ARG A    17                                                      
REMARK 465     LYS A    18                                                      
REMARK 465     GLN A    19                                                      
REMARK 465     LEU A    20                                                      
REMARK 465     ALA A    21                                                      
REMARK 465     THR A    22                                                      
REMARK 465     LYS A    23                                                      
REMARK 465     ALA A    24                                                      
REMARK 465     ALA A    25                                                      
REMARK 465     ARG A    26                                                      
REMARK 465     LYS A    27                                                      
REMARK 465     SER A    28                                                      
REMARK 465     ALA A    29                                                      
REMARK 465     PRO A    30                                                      
REMARK 465     ALA A    31                                                      
REMARK 465     THR A    32                                                      
REMARK 465     GLY A    33                                                      
REMARK 465     GLY A    34                                                      
REMARK 465     VAL A    35                                                      
REMARK 465     LYS A    36                                                      
REMARK 465     ALA A   135                                                      
REMARK 465     SER B     1                                                      
REMARK 465     GLY B     2                                                      
REMARK 465     ARG B     3                                                      
REMARK 465     GLY B     4                                                      
REMARK 465     LYS B     5                                                      
REMARK 465     GLY B     6                                                      
REMARK 465     GLY B     7                                                      
REMARK 465     LYS B     8                                                      
REMARK 465     GLY B     9                                                      
REMARK 465     LEU B    10                                                      
REMARK 465     GLY B    11                                                      
REMARK 465     LYS B    12                                                      
REMARK 465     GLY B    13                                                      
REMARK 465     GLY B    14                                                      
REMARK 465     ALA B    15                                                      
REMARK 465     LYS B    16                                                      
REMARK 465     SER C     1                                                      
REMARK 465     GLY C     2                                                      
REMARK 465     ARG C     3                                                      
REMARK 465     GLY C     4                                                      
REMARK 465     LYS C     5                                                      
REMARK 465     GLN C     6                                                      
REMARK 465     GLY C     7                                                      
REMARK 465     GLY C     8                                                      
REMARK 465     LYS C     9                                                      
REMARK 465     THR C    10                                                      
REMARK 465     ARG C    11                                                      
REMARK 465     ALA C    12                                                      
REMARK 465     LYS C    13                                                      
REMARK 465     ALA C    14                                                      
REMARK 465     LYS C    15                                                      
REMARK 465     THR C   120                                                      
REMARK 465     GLU C   121                                                      
REMARK 465     SER C   122                                                      
REMARK 465     SER C   123                                                      
REMARK 465     LYS C   124                                                      
REMARK 465     SER C   125                                                      
REMARK 465     ALA C   126                                                      
REMARK 465     LYS C   127                                                      
REMARK 465     SER C   128                                                      
REMARK 465     LYS C   129                                                      
REMARK 465     ALA D     4                                                      
REMARK 465     LYS D     5                                                      
REMARK 465     SER D     6                                                      
REMARK 465     ALA D     7                                                      
REMARK 465     PRO D     8                                                      
REMARK 465     ALA D     9                                                      
REMARK 465     PRO D    10                                                      
REMARK 465     LYS D    11                                                      
REMARK 465     LYS D    12                                                      
REMARK 465     GLY D    13                                                      
REMARK 465     SER D    14                                                      
REMARK 465     LYS D    15                                                      
REMARK 465     LYS D    16                                                      
REMARK 465     ALA D    17                                                      
REMARK 465     VAL D    18                                                      
REMARK 465     THR D    19                                                      
REMARK 465     LYS D    20                                                      
REMARK 465     THR D    21                                                      
REMARK 465     GLN D    22                                                      
REMARK 465     LYS D    23                                                      
REMARK 465     LYS D    24                                                      
REMARK 465     ASP D    25                                                      
REMARK 465     GLY D    26                                                      
REMARK 465     LYS D    27                                                      
REMARK 465     LYS D    28                                                      
REMARK 465     ARG D    29                                                      
REMARK 465     ARG D    30                                                      
REMARK 465     ALA E     1                                                      
REMARK 465     ARG E     2                                                      
REMARK 465     THR E     3                                                      
REMARK 465     LYS E     4                                                      
REMARK 465     GLN E     5                                                      
REMARK 465     THR E     6                                                      
REMARK 465     ALA E     7                                                      
REMARK 465     ARG E     8                                                      
REMARK 465     LYS E     9                                                      
REMARK 465     SER E    10                                                      
REMARK 465     THR E    11                                                      
REMARK 465     GLY E    12                                                      
REMARK 465     GLY E    13                                                      
REMARK 465     LYS E    14                                                      
REMARK 465     ALA E    15                                                      
REMARK 465     PRO E    16                                                      
REMARK 465     ARG E    17                                                      
REMARK 465     LYS E    18                                                      
REMARK 465     GLN E    19                                                      
REMARK 465     LEU E    20                                                      
REMARK 465     ALA E    21                                                      
REMARK 465     THR E    22                                                      
REMARK 465     LYS E    23                                                      
REMARK 465     ALA E    24                                                      
REMARK 465     ALA E    25                                                      
REMARK 465     ARG E    26                                                      
REMARK 465     LYS E    27                                                      
REMARK 465     SER E    28                                                      
REMARK 465     ALA E    29                                                      
REMARK 465     PRO E    30                                                      
REMARK 465     ALA E    31                                                      
REMARK 465     THR E    32                                                      
REMARK 465     GLY E    33                                                      
REMARK 465     GLY E    34                                                      
REMARK 465     VAL E    35                                                      
REMARK 465     LYS E    36                                                      
REMARK 465     LYS E    37                                                      
REMARK 465     ALA E   135                                                      
REMARK 465     SER F     1                                                      
REMARK 465     GLY F     2                                                      
REMARK 465     ARG F     3                                                      
REMARK 465     GLY F     4                                                      
REMARK 465     LYS F     5                                                      
REMARK 465     GLY F     6                                                      
REMARK 465     GLY F     7                                                      
REMARK 465     LYS F     8                                                      
REMARK 465     GLY F     9                                                      
REMARK 465     LEU F    10                                                      
REMARK 465     GLY F    11                                                      
REMARK 465     LYS F    12                                                      
REMARK 465     GLY F    13                                                      
REMARK 465     GLY F    14                                                      
REMARK 465     ALA F    15                                                      
REMARK 465     LYS F    16                                                      
REMARK 465     ARG F    17                                                      
REMARK 465     HIS F    18                                                      
REMARK 465     ARG F    19                                                      
REMARK 465     LYS F    20                                                      
REMARK 465     SER G     1                                                      
REMARK 465     GLY G     2                                                      
REMARK 465     ARG G     3                                                      
REMARK 465     GLY G     4                                                      
REMARK 465     LYS G     5                                                      
REMARK 465     GLN G     6                                                      
REMARK 465     GLY G     7                                                      
REMARK 465     GLY G     8                                                      
REMARK 465     LYS G     9                                                      
REMARK 465     THR G    10                                                      
REMARK 465     ARG G    11                                                      
REMARK 465     LYS G   119                                                      
REMARK 465     THR G   120                                                      
REMARK 465     GLU G   121                                                      
REMARK 465     SER G   122                                                      
REMARK 465     SER G   123                                                      
REMARK 465     LYS G   124                                                      
REMARK 465     SER G   125                                                      
REMARK 465     ALA G   126                                                      
REMARK 465     LYS G   127                                                      
REMARK 465     SER G   128                                                      
REMARK 465     LYS G   129                                                      
REMARK 465     ALA H     4                                                      
REMARK 465     LYS H     5                                                      
REMARK 465     SER H     6                                                      
REMARK 465     ALA H     7                                                      
REMARK 465     PRO H     8                                                      
REMARK 465     ALA H     9                                                      
REMARK 465     PRO H    10                                                      
REMARK 465     LYS H    11                                                      
REMARK 465     LYS H    12                                                      
REMARK 465     GLY H    13                                                      
REMARK 465     SER H    14                                                      
REMARK 465     LYS H    15                                                      
REMARK 465     LYS H    16                                                      
REMARK 465     ALA H    17                                                      
REMARK 465     VAL H    18                                                      
REMARK 465     THR H    19                                                      
REMARK 465     LYS H    20                                                      
REMARK 465     THR H    21                                                      
REMARK 465     GLN H    22                                                      
REMARK 465     LYS H    23                                                      
REMARK 465     LYS H    24                                                      
REMARK 465     ASP H    25                                                      
REMARK 465     GLY H    26                                                      
REMARK 465     LYS H    27                                                      
REMARK 465     LYS H    28                                                      
REMARK 465     ARG H    29                                                      
REMARK 465     ARG H    30                                                      
REMARK 465      DA I   -73                                                      
REMARK 465      DT I   -72                                                      
REMARK 465      DT I    73                                                      
REMARK 465      DA J   -73                                                      
REMARK 465      DT J    73                                                      
REMARK 465     GLY K     0                                                      
REMARK 465     SER K     1                                                      
REMARK 465     HIS K     2                                                      
REMARK 465     ASN K   108                                                      
REMARK 465     GLY K   109                                                      
REMARK 465     GLY L     1                                                      
REMARK 465     SER L     2                                                      
REMARK 465     GLN L     3                                                      
REMARK 465     ALA L     4                                                      
REMARK 465     VAL L     5                                                      
REMARK 465     GLN L     6                                                      
REMARK 465     THR L     7                                                      
REMARK 465     ASN L     8                                                      
REMARK 465     GLY L     9                                                      
REMARK 465     THR L    10                                                      
REMARK 465     GLN L    11                                                      
REMARK 465     PRO L    12                                                      
REMARK 465     LEU L    13                                                      
REMARK 465     SER L    14                                                      
REMARK 465     GLY M     0                                                      
REMARK 465     SER M     1                                                      
REMARK 465     HIS M     2                                                      
REMARK 465     ARG M     3                                                      
REMARK 465     THR M     4                                                      
REMARK 465     THR M     5                                                      
REMARK 465     SER M   103                                                      
REMARK 465     ALA M   104                                                      
REMARK 465     ASP M   105                                                      
REMARK 465     ALA M   106                                                      
REMARK 465     ALA M   107                                                      
REMARK 465     ASN M   108                                                      
REMARK 465     GLY M   109                                                      
REMARK 465     GLY N     1                                                      
REMARK 465     SER N     2                                                      
REMARK 465     GLN N     3                                                      
REMARK 465     ALA N     4                                                      
REMARK 465     VAL N     5                                                      
REMARK 465     GLN N     6                                                      
REMARK 465     THR N     7                                                      
REMARK 465     ASN N     8                                                      
REMARK 465     GLY N     9                                                      
REMARK 465     THR N    10                                                      
REMARK 465     GLN N    11                                                      
REMARK 465     PRO N    12                                                      
REMARK 465     LEU N    13                                                      
REMARK 465     SER N    14                                                      
REMARK 465     LYS N    15                                                      
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     LYS A  37    CG   CD   CE   NZ                                   
REMARK 470     ARG A  42    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A  83    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 134    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B  17    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     HIS B  18    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LYS B  20    CG   CD   CE   NZ                                   
REMARK 470     LYS B  44    CG   CD   CE   NZ                                   
REMARK 470     ARG C  20    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG C  35    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS C  36    CG   CD   CE   NZ                                   
REMARK 470     LYS C  74    CG   CD   CE   NZ                                   
REMARK 470     ARG C  77    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS C  95    CG   CD   CE   NZ                                   
REMARK 470     LYS C 118    CG   CD   CE   NZ                                   
REMARK 470     LYS C 119    CG   CD   CE   NZ                                   
REMARK 470     LYS D  31    CG   CD   CE   NZ                                   
REMARK 470     THR D  32    OG1  CG2                                            
REMARK 470     ARG D  33    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS D  34    CG   CD   CE   NZ                                   
REMARK 470     LYS D  57    CG   CD   CE   NZ                                   
REMARK 470     LYS D 125    CG   CD   CE   NZ                                   
REMARK 470     ARG E  53    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU E  59    CG   CD   OE1  OE2                                  
REMARK 470     LYS E  64    CG   CD   CE   NZ                                   
REMARK 470     ARG F  23    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS F  59    CG   CD   CE   NZ                                   
REMARK 470     LYS F  77    CG   CD   CE   NZ                                   
REMARK 470     LYS F  79    CG   CD   CE   NZ                                   
REMARK 470     LYS G  13    CG   CD   CE   NZ                                   
REMARK 470     LYS G  15    CG   CD   CE   NZ                                   
REMARK 470     LYS G  36    CG   CD   CE   NZ                                   
REMARK 470     LYS G  74    CG   CD   CE   NZ                                   
REMARK 470     LYS G  75    CG   CD   CE   NZ                                   
REMARK 470     ARG G  77    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS G 118    CG   CD   CE   NZ                                   
REMARK 470     LYS H  31    CG   CD   CE   NZ                                   
REMARK 470     ARG H  33    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS H  34    CG   CD   CE   NZ                                   
REMARK 470     LYS H  57    CG   CD   CE   NZ                                   
REMARK 470     LYS H  85    CG   CD   CE   NZ                                   
REMARK 470     LYS H 125    CG   CD   CE   NZ                                   
REMARK 470     ARG K   3    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG K   6    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS K  51    CG   CD   CE   NZ                                   
REMARK 470     LYS K  88    CG   CD   CE   NZ                                   
REMARK 470     LYS K  92    CG   CD   CE   NZ                                   
REMARK 470     ASP K 105    CG   OD1  OD2                                       
REMARK 470     ILE L  38    CG1  CG2  CD1                                       
REMARK 470     ARG L  43    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG L 101    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP L 212    CG   OD1  OD2                                       
REMARK 470     ARG L 215    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP L 228    CG   OD1  OD2                                       
REMARK 470     GLN L 234    CG   CD   OE1  NE2                                  
REMARK 470     MET L 238    CG   SD   CE                                        
REMARK 470     ASN L 241    CG   OD1  ND2                                       
REMARK 470     ASP L 242    CG   OD1  OD2                                       
REMARK 470     GLN L 246    CG   CD   OE1  NE2                                  
REMARK 470     LYS L 263    CG   CD   CE   NZ                                   
REMARK 470     ARG L 272    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ILE L 273    CG1  CG2  CD1                                       
REMARK 470     TYR L 274    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ILE L 278    CG1  CG2  CD1                                       
REMARK 470     LEU L 289    CG   CD1  CD2                                       
REMARK 470     ARG L 290    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASN L 314    CG   OD1  ND2                                       
REMARK 470     ASP L 317    CG   OD1  OD2                                       
REMARK 470     LEU L 319    CG   CD1  CD2                                       
REMARK 470     GLU L 322    CG   CD   OE1  OE2                                  
REMARK 470     ILE L 326    CG1  CG2  CD1                                       
REMARK 470     LYS L 328    CG   CD   CE   NZ                                   
REMARK 470     ASP L 330    CG   OD1  OD2                                       
REMARK 470     ARG L 331    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP L 332    CG   OD1  OD2                                       
REMARK 470     LYS L 333    CG   CD   CE   NZ                                   
REMARK 470     ASN L 335    CG   OD1  ND2                                       
REMARK 470     ARG L 336    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ILE L 337    CG1  CG2  CD1                                       
REMARK 470     ARG L 339    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU L 340    CG   CD   OE1  OE2                                  
REMARK 470     THR L 342    OG1  CG2                                            
REMARK 470     GLN L 343    CG   CD   OE1  NE2                                  
REMARK 470     LYS L 344    CG   CD   CE   NZ                                   
REMARK 470     TYR L 345    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     MET L 347    CG   SD   CE                                        
REMARK 470     ARG M   6    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ILE M   7    CG1  CG2  CD1                                       
REMARK 470     LYS M   8    CG   CD   CE   NZ                                   
REMARK 470     ILE M  26    CG1  CG2  CD1                                       
REMARK 470     GLU M  48    CG   CD   OE1  OE2                                  
REMARK 470     LYS M  51    CG   CD   CE   NZ                                   
REMARK 470     LYS M  62    CG   CD   CE   NZ                                   
REMARK 470     LYS M  88    CG   CD   CE   NZ                                   
REMARK 470     MET M  91    CG   SD   CE                                        
REMARK 470     LYS M  92    CG   CD   CE   NZ                                   
REMARK 470     ARG M  94    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP M  96    CG   OD1  OD2                                       
REMARK 470     GLU N  18    CG   CD   OE1  OE2                                  
REMARK 470     LEU N  21    CG   CD1  CD2                                       
REMARK 470     GLU N  23    CG   CD   OE1  OE2                                  
REMARK 470     ARG N  26    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU N  30    CG   CD   OE1  OE2                                  
REMARK 470     GLU N  37    CG   CD   OE1  OE2                                  
REMARK 470     ILE N  38    CG1  CG2  CD1                                       
REMARK 470     ARG N  43    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS N  59    CG   CD   CE   NZ                                   
REMARK 470     ARG N 101    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS N 112    CG   CD   CE   NZ                                   
REMARK 470     LYS N 204    CG   CD   CE   NZ                                   
REMARK 470     LYS N 208    CG   CD   CE   NZ                                   
REMARK 470     ASP N 212    CG   OD1  OD2                                       
REMARK 470     GLN N 220    CG   CD   OE1  NE2                                  
REMARK 470     ASP N 228    CG   OD1  OD2                                       
REMARK 470     ILE N 237    CG1  CG2  CD1                                       
REMARK 470     MET N 238    CG   SD   CE                                        
REMARK 470     ASN N 241    CG   OD1  ND2                                       
REMARK 470     ASP N 242    CG   OD1  OD2                                       
REMARK 470     ARG N 272    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG N 290    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP N 330    CG   OD1  OD2                                       
REMARK 470     ARG N 331    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN N 343    CG   CD   OE1  NE2                                  
REMARK 470     LYS N 344    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    ARG C  99       30.25    -97.76                                   
REMARK 500    THR D  32       11.02     59.39                                   
REMARK 500    ARG D  33       71.48     52.75                                   
REMARK 500    SER D  36     -164.17   -161.17                                   
REMARK 500    ASP D  51       50.28   -104.87                                   
REMARK 500    ALA D 124       62.93   -153.96                                   
REMARK 500    THR E  45      -62.26    -90.16                                   
REMARK 500    ARG F  23     -159.83    -73.70                                   
REMARK 500    ASN F  25       -3.20     58.15                                   
REMARK 500    PHE F 100      -17.49   -141.97                                   
REMARK 500    LYS G  13       85.29     56.01                                   
REMARK 500    PRO G 109       99.49    -64.35                                   
REMARK 500    THR H  32       82.47     53.41                                   
REMARK 500    CYS K  34        1.85   -159.23                                   
REMARK 500    ILE K  55      -62.69    -98.70                                   
REMARK 500    ASP K  57       17.96     57.26                                   
REMARK 500    THR K  63      -51.99   -128.81                                   
REMARK 500    ALA K 104       84.66     56.23                                   
REMARK 500    ALA K 106       92.47    -69.32                                   
REMARK 500    THR L  16       16.63     57.36                                   
REMARK 500    GLN L  25       24.30   -145.33                                   
REMARK 500    PRO L  42        5.14    -68.97                                   
REMARK 500    LEU L  45       42.75   -102.81                                   
REMARK 500    HIS L  46      -72.11    -62.40                                   
REMARK 500    LYS L  85       55.66    -92.73                                   
REMARK 500    SER L  96     -162.60   -161.14                                   
REMARK 500    SER L 116       79.70   -158.46                                   
REMARK 500    SER L 118       84.30     55.73                                   
REMARK 500    SER L 120      106.10   -162.98                                   
REMARK 500    SER L 122      144.34     66.51                                   
REMARK 500    ASP L 216       89.95   -150.20                                   
REMARK 500    THR L 270       67.94   -110.10                                   
REMARK 500    THR L 271        4.92   -151.00                                   
REMARK 500    ARG L 272       79.95     55.49                                   
REMARK 500    ARG L 290      -87.01   -112.85                                   
REMARK 500    GLN L 292       46.25    -88.43                                   
REMARK 500    ASP L 330      -90.98   -108.71                                   
REMARK 500    ASP L 332      -34.54   -142.33                                   
REMARK 500    ALA L 346      -55.16   -130.06                                   
REMARK 500    ASP M  27       81.68     55.72                                   
REMARK 500    CYS M  34      -10.22   -144.55                                   
REMARK 500    THR M  49      -67.68   -122.64                                   
REMARK 500    ILE M  55      -61.52   -122.74                                   
REMARK 500    THR M  63      -52.80   -130.24                                   
REMARK 500    SER N  44      -74.16    -69.55                                   
REMARK 500    LEU N  45       39.35    -88.19                                   
REMARK 500    LYS N  85       35.46    -93.36                                   
REMARK 500    PRO N 244       54.04    -66.45                                   
REMARK 500    TYR N 245       35.51   -141.92                                   
REMARK 500    ASP N 259       31.02    -93.65                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      54 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 K 202  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS K  36   ND1                                                    
REMARK 620 2 CYS K  34   SG  116.6                                              
REMARK 620 3 CYS K  56   SG  110.0 103.0                                        
REMARK 620 4 CYS K  53   SG   97.9 128.7  98.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN M 201  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS M  21   SG                                                     
REMARK 620 2 CYS M  18   SG  103.5                                              
REMARK 620 3 CYS M  42   SG  109.3 128.0                                        
REMARK 620 4 CYS M  39   SG  101.7  96.1 114.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN L 402  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS L  69   ND1                                                    
REMARK 620 2 CYS L  67   SG  116.7                                              
REMARK 620 3 CYS L  87   SG   99.0 112.6                                        
REMARK 620 4 CYS L  90   SG  105.3 110.2 112.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN M 202  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS M  36   ND1                                                    
REMARK 620 2 CYS M  34   SG  128.3                                              
REMARK 620 3 CYS M  53   SG  104.7 114.3                                        
REMARK 620 4 CYS M  56   SG   97.4 111.6  94.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN N 402  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS N  69   ND1                                                    
REMARK 620 2 CYS N  90   SG  133.8                                              
REMARK 620 3 CYS N  87   SG   93.5 120.2                                        
REMARK 620 4 CYS N  67   SG   98.7 104.5 100.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN N 401  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS N  54   SG                                                     
REMARK 620 2 CYS N  51   SG  119.3                                              
REMARK 620 3 CYS N  75   SG  104.5 114.7                                        
REMARK 620 4 CYS N  72   SG  110.8  97.2 110.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN K 201  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS K  39   SG                                                     
REMARK 620 2 CYS K  18   SG  106.8                                              
REMARK 620 3 CYS K  42   SG  117.2 118.4                                        
REMARK 620 4 CYS K  21   SG   99.6 101.7 110.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN L 401  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS L  54   SG                                                     
REMARK 620 2 CYS L  72   SG  112.2                                              
REMARK 620 3 CYS L  75   SG  109.9 117.3                                        
REMARK 620 4 CYS L  51   SG   98.8  96.8 120.1                                  
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 K 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN K 202                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN L 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN L 402                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN M 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN M 202                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN N 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN N 402                  
DBREF  4R8P A    1   135  UNP    P84233   H32_XENLA        2    136             
DBREF  4R8P B    1   102  UNP    P62799   H4_XENLA         2    103             
DBREF  4R8P C    1   129  UNP    Q6AZJ8   Q6AZJ8_XENLA     2    130             
DBREF  4R8P D    4   125  UNP    P02281   H2B11_XENLA      5    126             
DBREF  4R8P E    1   135  UNP    P84233   H32_XENLA        2    136             
DBREF  4R8P F    1   102  UNP    P62799   H4_XENLA         2    103             
DBREF  4R8P G    1   129  UNP    Q6AZJ8   Q6AZJ8_XENLA     2    130             
DBREF  4R8P H    4   125  UNP    P02281   H2B11_XENLA      5    126             
DBREF  4R8P K    2   109  UNP    P35226   BMI1_HUMAN       2    109             
DBREF  4R8P L    2   116  UNP    Q99496   RING2_HUMAN      2    116             
DBREF  4R8P L  202   347  UNP    P61077   UB2D3_HUMAN      2    147             
DBREF  4R8P M    2   109  UNP    P35226   BMI1_HUMAN       2    109             
DBREF  4R8P N    2   116  UNP    Q99496   RING2_HUMAN      2    116             
DBREF  4R8P N  202   347  UNP    P61077   UB2D3_HUMAN      2    147             
DBREF  4R8P I  -73    73  PDB    4R8P     4R8P           -73     73             
DBREF  4R8P J  -73    73  PDB    4R8P     4R8P           -73     73             
SEQADV 4R8P ALA A  102  UNP  P84233    GLY   103 CONFLICT                       
SEQADV 4R8P THR D   32  UNP  P02281    SER    33 CONFLICT                       
SEQADV 4R8P ALA E  102  UNP  P84233    GLY   103 CONFLICT                       
SEQADV 4R8P THR H   32  UNP  P02281    SER    33 CONFLICT                       
SEQADV 4R8P GLY K    0  UNP  P35226              EXPRESSION TAG                 
SEQADV 4R8P SER K    1  UNP  P35226              EXPRESSION TAG                 
SEQADV 4R8P GLY L    1  UNP  Q99496              EXPRESSION TAG                 
SEQADV 4R8P GLY L  117  UNP  Q99496              LINKER                         
SEQADV 4R8P SER L  118  UNP  Q99496              LINKER                         
SEQADV 4R8P GLY L  119  UNP  Q99496              LINKER                         
SEQADV 4R8P SER L  120  UNP  Q99496              LINKER                         
SEQADV 4R8P ARG L  121  UNP  Q99496              LINKER                         
SEQADV 4R8P SER L  122  UNP  Q99496              LINKER                         
SEQADV 4R8P GLY M    0  UNP  P35226              EXPRESSION TAG                 
SEQADV 4R8P SER M    1  UNP  P35226              EXPRESSION TAG                 
SEQADV 4R8P GLY N    1  UNP  Q99496              EXPRESSION TAG                 
SEQADV 4R8P GLY N  117  UNP  Q99496              LINKER                         
SEQADV 4R8P SER N  118  UNP  Q99496              LINKER                         
SEQADV 4R8P GLY N  119  UNP  Q99496              LINKER                         
SEQADV 4R8P SER N  120  UNP  Q99496              LINKER                         
SEQADV 4R8P ARG N  121  UNP  Q99496              LINKER                         
SEQADV 4R8P SER N  122  UNP  Q99496              LINKER                         
SEQRES   1 A  135  ALA ARG THR LYS GLN THR ALA ARG LYS SER THR GLY GLY          
SEQRES   2 A  135  LYS ALA PRO ARG LYS GLN LEU ALA THR LYS ALA ALA ARG          
SEQRES   3 A  135  LYS SER ALA PRO ALA THR GLY GLY VAL LYS LYS PRO HIS          
SEQRES   4 A  135  ARG TYR ARG PRO GLY THR VAL ALA LEU ARG GLU ILE ARG          
SEQRES   5 A  135  ARG TYR GLN LYS SER THR GLU LEU LEU ILE ARG LYS LEU          
SEQRES   6 A  135  PRO PHE GLN ARG LEU VAL ARG GLU ILE ALA GLN ASP PHE          
SEQRES   7 A  135  LYS THR ASP LEU ARG PHE GLN SER SER ALA VAL MET ALA          
SEQRES   8 A  135  LEU GLN GLU ALA SER GLU ALA TYR LEU VAL ALA LEU PHE          
SEQRES   9 A  135  GLU ASP THR ASN LEU CYS ALA ILE HIS ALA LYS ARG VAL          
SEQRES  10 A  135  THR ILE MET PRO LYS ASP ILE GLN LEU ALA ARG ARG ILE          
SEQRES  11 A  135  ARG GLY GLU ARG ALA                                          
SEQRES   1 B  102  SER GLY ARG GLY LYS GLY GLY LYS GLY LEU GLY LYS GLY          
SEQRES   2 B  102  GLY ALA LYS ARG HIS ARG LYS VAL LEU ARG ASP ASN ILE          
SEQRES   3 B  102  GLN GLY ILE THR LYS PRO ALA ILE ARG ARG LEU ALA ARG          
SEQRES   4 B  102  ARG GLY GLY VAL LYS ARG ILE SER GLY LEU ILE TYR GLU          
SEQRES   5 B  102  GLU THR ARG GLY VAL LEU LYS VAL PHE LEU GLU ASN VAL          
SEQRES   6 B  102  ILE ARG ASP ALA VAL THR TYR THR GLU HIS ALA LYS ARG          
SEQRES   7 B  102  LYS THR VAL THR ALA MET ASP VAL VAL TYR ALA LEU LYS          
SEQRES   8 B  102  ARG GLN GLY ARG THR LEU TYR GLY PHE GLY GLY                  
SEQRES   1 C  129  SER GLY ARG GLY LYS GLN GLY GLY LYS THR ARG ALA LYS          
SEQRES   2 C  129  ALA LYS THR ARG SER SER ARG ALA GLY LEU GLN PHE PRO          
SEQRES   3 C  129  VAL GLY ARG VAL HIS ARG LEU LEU ARG LYS GLY ASN TYR          
SEQRES   4 C  129  ALA GLU ARG VAL GLY ALA GLY ALA PRO VAL TYR LEU ALA          
SEQRES   5 C  129  ALA VAL LEU GLU TYR LEU THR ALA GLU ILE LEU GLU LEU          
SEQRES   6 C  129  ALA GLY ASN ALA ALA ARG ASP ASN LYS LYS THR ARG ILE          
SEQRES   7 C  129  ILE PRO ARG HIS LEU GLN LEU ALA VAL ARG ASN ASP GLU          
SEQRES   8 C  129  GLU LEU ASN LYS LEU LEU GLY ARG VAL THR ILE ALA GLN          
SEQRES   9 C  129  GLY GLY VAL LEU PRO ASN ILE GLN SER VAL LEU LEU PRO          
SEQRES  10 C  129  LYS LYS THR GLU SER SER LYS SER ALA LYS SER LYS              
SEQRES   1 D  122  ALA LYS SER ALA PRO ALA PRO LYS LYS GLY SER LYS LYS          
SEQRES   2 D  122  ALA VAL THR LYS THR GLN LYS LYS ASP GLY LYS LYS ARG          
SEQRES   3 D  122  ARG LYS THR ARG LYS GLU SER TYR ALA ILE TYR VAL TYR          
SEQRES   4 D  122  LYS VAL LEU LYS GLN VAL HIS PRO ASP THR GLY ILE SER          
SEQRES   5 D  122  SER LYS ALA MET SER ILE MET ASN SER PHE VAL ASN ASP          
SEQRES   6 D  122  VAL PHE GLU ARG ILE ALA GLY GLU ALA SER ARG LEU ALA          
SEQRES   7 D  122  HIS TYR ASN LYS ARG SER THR ILE THR SER ARG GLU ILE          
SEQRES   8 D  122  GLN THR ALA VAL ARG LEU LEU LEU PRO GLY GLU LEU ALA          
SEQRES   9 D  122  LYS HIS ALA VAL SER GLU GLY THR LYS ALA VAL THR LYS          
SEQRES  10 D  122  TYR THR SER ALA LYS                                          
SEQRES   1 E  135  ALA ARG THR LYS GLN THR ALA ARG LYS SER THR GLY GLY          
SEQRES   2 E  135  LYS ALA PRO ARG LYS GLN LEU ALA THR LYS ALA ALA ARG          
SEQRES   3 E  135  LYS SER ALA PRO ALA THR GLY GLY VAL LYS LYS PRO HIS          
SEQRES   4 E  135  ARG TYR ARG PRO GLY THR VAL ALA LEU ARG GLU ILE ARG          
SEQRES   5 E  135  ARG TYR GLN LYS SER THR GLU LEU LEU ILE ARG LYS LEU          
SEQRES   6 E  135  PRO PHE GLN ARG LEU VAL ARG GLU ILE ALA GLN ASP PHE          
SEQRES   7 E  135  LYS THR ASP LEU ARG PHE GLN SER SER ALA VAL MET ALA          
SEQRES   8 E  135  LEU GLN GLU ALA SER GLU ALA TYR LEU VAL ALA LEU PHE          
SEQRES   9 E  135  GLU ASP THR ASN LEU CYS ALA ILE HIS ALA LYS ARG VAL          
SEQRES  10 E  135  THR ILE MET PRO LYS ASP ILE GLN LEU ALA ARG ARG ILE          
SEQRES  11 E  135  ARG GLY GLU ARG ALA                                          
SEQRES   1 F  102  SER GLY ARG GLY LYS GLY GLY LYS GLY LEU GLY LYS GLY          
SEQRES   2 F  102  GLY ALA LYS ARG HIS ARG LYS VAL LEU ARG ASP ASN ILE          
SEQRES   3 F  102  GLN GLY ILE THR LYS PRO ALA ILE ARG ARG LEU ALA ARG          
SEQRES   4 F  102  ARG GLY GLY VAL LYS ARG ILE SER GLY LEU ILE TYR GLU          
SEQRES   5 F  102  GLU THR ARG GLY VAL LEU LYS VAL PHE LEU GLU ASN VAL          
SEQRES   6 F  102  ILE ARG ASP ALA VAL THR TYR THR GLU HIS ALA LYS ARG          
SEQRES   7 F  102  LYS THR VAL THR ALA MET ASP VAL VAL TYR ALA LEU LYS          
SEQRES   8 F  102  ARG GLN GLY ARG THR LEU TYR GLY PHE GLY GLY                  
SEQRES   1 G  129  SER GLY ARG GLY LYS GLN GLY GLY LYS THR ARG ALA LYS          
SEQRES   2 G  129  ALA LYS THR ARG SER SER ARG ALA GLY LEU GLN PHE PRO          
SEQRES   3 G  129  VAL GLY ARG VAL HIS ARG LEU LEU ARG LYS GLY ASN TYR          
SEQRES   4 G  129  ALA GLU ARG VAL GLY ALA GLY ALA PRO VAL TYR LEU ALA          
SEQRES   5 G  129  ALA VAL LEU GLU TYR LEU THR ALA GLU ILE LEU GLU LEU          
SEQRES   6 G  129  ALA GLY ASN ALA ALA ARG ASP ASN LYS LYS THR ARG ILE          
SEQRES   7 G  129  ILE PRO ARG HIS LEU GLN LEU ALA VAL ARG ASN ASP GLU          
SEQRES   8 G  129  GLU LEU ASN LYS LEU LEU GLY ARG VAL THR ILE ALA GLN          
SEQRES   9 G  129  GLY GLY VAL LEU PRO ASN ILE GLN SER VAL LEU LEU PRO          
SEQRES  10 G  129  LYS LYS THR GLU SER SER LYS SER ALA LYS SER LYS              
SEQRES   1 H  122  ALA LYS SER ALA PRO ALA PRO LYS LYS GLY SER LYS LYS          
SEQRES   2 H  122  ALA VAL THR LYS THR GLN LYS LYS ASP GLY LYS LYS ARG          
SEQRES   3 H  122  ARG LYS THR ARG LYS GLU SER TYR ALA ILE TYR VAL TYR          
SEQRES   4 H  122  LYS VAL LEU LYS GLN VAL HIS PRO ASP THR GLY ILE SER          
SEQRES   5 H  122  SER LYS ALA MET SER ILE MET ASN SER PHE VAL ASN ASP          
SEQRES   6 H  122  VAL PHE GLU ARG ILE ALA GLY GLU ALA SER ARG LEU ALA          
SEQRES   7 H  122  HIS TYR ASN LYS ARG SER THR ILE THR SER ARG GLU ILE          
SEQRES   8 H  122  GLN THR ALA VAL ARG LEU LEU LEU PRO GLY GLU LEU ALA          
SEQRES   9 H  122  LYS HIS ALA VAL SER GLU GLY THR LYS ALA VAL THR LYS          
SEQRES  10 H  122  TYR THR SER ALA LYS                                          
SEQRES   1 I  147   DA  DT  DC  DG  DA  DG  DA  DA  DT  DC  DC  DC  DG          
SEQRES   2 I  147   DG  DT  DG  DC  DC  DG  DA  DG  DG  DC  DC  DG  DC          
SEQRES   3 I  147   DT  DC  DA  DA  DT  DT  DG  DG  DT  DC  DG  DT  DA          
SEQRES   4 I  147   DG  DA  DC  DA  DG  DC  DT  DC  DT  DA  DG  DC  DA          
SEQRES   5 I  147   DC  DC  DG  DC  DT  DT  DA  DA  DA  DC  DG  DC  DA          
SEQRES   6 I  147   DC  DG  DT  DA  DC  DG  DC  DG  DC  DT  DG  DT  DC          
SEQRES   7 I  147   DC  DC  DC  DC  DG  DC  DG  DT  DT  DT  DT  DA  DA          
SEQRES   8 I  147   DC  DC  DG  DC  DC  DA  DA  DG  DG  DG  DG  DA  DT          
SEQRES   9 I  147   DT  DA  DC  DT  DC  DC  DC  DT  DA  DG  DT  DC  DT          
SEQRES  10 I  147   DC  DC  DA  DG  DG  DC  DA  DC  DG  DT  DG  DT  DC          
SEQRES  11 I  147   DA  DG  DA  DT  DA  DT  DA  DT  DA  DC  DA  DT  DC          
SEQRES  12 I  147   DC  DG  DA  DT                                              
SEQRES   1 J  147   DA  DT  DC  DG  DG  DA  DT  DG  DT  DA  DT  DA  DT          
SEQRES   2 J  147   DA  DT  DC  DT  DG  DA  DC  DA  DC  DG  DT  DG  DC          
SEQRES   3 J  147   DC  DT  DG  DG  DA  DG  DA  DC  DT  DA  DG  DG  DG          
SEQRES   4 J  147   DA  DG  DT  DA  DA  DT  DC  DC  DC  DC  DT  DT  DG          
SEQRES   5 J  147   DG  DC  DG  DG  DT  DT  DA  DA  DA  DA  DC  DG  DC          
SEQRES   6 J  147   DG  DG  DG  DG  DG  DA  DC  DA  DG  DC  DG  DC  DG          
SEQRES   7 J  147   DT  DA  DC  DG  DT  DG  DC  DG  DT  DT  DT  DA  DA          
SEQRES   8 J  147   DG  DC  DG  DG  DT  DG  DC  DT  DA  DG  DA  DG  DC          
SEQRES   9 J  147   DT  DG  DT  DC  DT  DA  DC  DG  DA  DC  DC  DA  DA          
SEQRES  10 J  147   DT  DT  DG  DA  DG  DC  DG  DG  DC  DC  DT  DC  DG          
SEQRES  11 J  147   DG  DC  DA  DC  DC  DG  DG  DG  DA  DT  DT  DC  DT          
SEQRES  12 J  147   DC  DG  DA  DT                                              
SEQRES   1 K  110  GLY SER HIS ARG THR THR ARG ILE LYS ILE THR GLU LEU          
SEQRES   2 K  110  ASN PRO HIS LEU MET CYS VAL LEU CYS GLY GLY TYR PHE          
SEQRES   3 K  110  ILE ASP ALA THR THR ILE ILE GLU CYS LEU HIS SER PHE          
SEQRES   4 K  110  CYS LYS THR CYS ILE VAL ARG TYR LEU GLU THR SER LYS          
SEQRES   5 K  110  TYR CYS PRO ILE CYS ASP VAL GLN VAL HIS LYS THR ARG          
SEQRES   6 K  110  PRO LEU LEU ASN ILE ARG SER ASP LYS THR LEU GLN ASP          
SEQRES   7 K  110  ILE VAL TYR LYS LEU VAL PRO GLY LEU PHE LYS ASN GLU          
SEQRES   8 K  110  MET LYS ARG ARG ARG ASP PHE TYR ALA ALA HIS PRO SER          
SEQRES   9 K  110  ALA ASP ALA ALA ASN GLY                                      
SEQRES   1 L  268  GLY SER GLN ALA VAL GLN THR ASN GLY THR GLN PRO LEU          
SEQRES   2 L  268  SER LYS THR TRP GLU LEU SER LEU TYR GLU LEU GLN ARG          
SEQRES   3 L  268  THR PRO GLN GLU ALA ILE THR ASP GLY LEU GLU ILE VAL          
SEQRES   4 L  268  VAL SER PRO ARG SER LEU HIS SER GLU LEU MET CYS PRO          
SEQRES   5 L  268  ILE CYS LEU ASP MET LEU LYS ASN THR MET THR THR LYS          
SEQRES   6 L  268  GLU CYS LEU HIS ARG PHE CYS ALA ASP CYS ILE ILE THR          
SEQRES   7 L  268  ALA LEU ARG SER GLY ASN LYS GLU CYS PRO THR CYS ARG          
SEQRES   8 L  268  LYS LYS LEU VAL SER LYS ARG SER LEU ARG PRO ASP PRO          
SEQRES   9 L  268  ASN PHE ASP ALA LEU ILE SER LYS ILE TYR PRO SER GLY          
SEQRES  10 L  268  SER GLY SER ARG SER ALA LEU LYS ARG ILE ASN LYS GLU          
SEQRES  11 L  268  LEU SER ASP LEU ALA ARG ASP PRO PRO ALA GLN CYS SER          
SEQRES  12 L  268  ALA GLY PRO VAL GLY ASP ASP MET PHE HIS TRP GLN ALA          
SEQRES  13 L  268  THR ILE MET GLY PRO ASN ASP SER PRO TYR GLN GLY GLY          
SEQRES  14 L  268  VAL PHE PHE LEU THR ILE HIS PHE PRO THR ASP TYR PRO          
SEQRES  15 L  268  PHE LYS PRO PRO LYS VAL ALA PHE THR THR ARG ILE TYR          
SEQRES  16 L  268  HIS PRO ASN ILE ASN SER ASN GLY SER ILE CYS LEU ASP          
SEQRES  17 L  268  ILE LEU ARG SER GLN TRP SER PRO ALA LEU THR ILE SER          
SEQRES  18 L  268  LYS VAL LEU LEU SER ILE CYS SER LEU LEU CYS ASP PRO          
SEQRES  19 L  268  ASN PRO ASP ASP PRO LEU VAL PRO GLU ILE ALA ARG ILE          
SEQRES  20 L  268  TYR LYS THR ASP ARG ASP LYS TYR ASN ARG ILE SER ARG          
SEQRES  21 L  268  GLU TRP THR GLN LYS TYR ALA MET                              
SEQRES   1 M  110  GLY SER HIS ARG THR THR ARG ILE LYS ILE THR GLU LEU          
SEQRES   2 M  110  ASN PRO HIS LEU MET CYS VAL LEU CYS GLY GLY TYR PHE          
SEQRES   3 M  110  ILE ASP ALA THR THR ILE ILE GLU CYS LEU HIS SER PHE          
SEQRES   4 M  110  CYS LYS THR CYS ILE VAL ARG TYR LEU GLU THR SER LYS          
SEQRES   5 M  110  TYR CYS PRO ILE CYS ASP VAL GLN VAL HIS LYS THR ARG          
SEQRES   6 M  110  PRO LEU LEU ASN ILE ARG SER ASP LYS THR LEU GLN ASP          
SEQRES   7 M  110  ILE VAL TYR LYS LEU VAL PRO GLY LEU PHE LYS ASN GLU          
SEQRES   8 M  110  MET LYS ARG ARG ARG ASP PHE TYR ALA ALA HIS PRO SER          
SEQRES   9 M  110  ALA ASP ALA ALA ASN GLY                                      
SEQRES   1 N  268  GLY SER GLN ALA VAL GLN THR ASN GLY THR GLN PRO LEU          
SEQRES   2 N  268  SER LYS THR TRP GLU LEU SER LEU TYR GLU LEU GLN ARG          
SEQRES   3 N  268  THR PRO GLN GLU ALA ILE THR ASP GLY LEU GLU ILE VAL          
SEQRES   4 N  268  VAL SER PRO ARG SER LEU HIS SER GLU LEU MET CYS PRO          
SEQRES   5 N  268  ILE CYS LEU ASP MET LEU LYS ASN THR MET THR THR LYS          
SEQRES   6 N  268  GLU CYS LEU HIS ARG PHE CYS ALA ASP CYS ILE ILE THR          
SEQRES   7 N  268  ALA LEU ARG SER GLY ASN LYS GLU CYS PRO THR CYS ARG          
SEQRES   8 N  268  LYS LYS LEU VAL SER LYS ARG SER LEU ARG PRO ASP PRO          
SEQRES   9 N  268  ASN PHE ASP ALA LEU ILE SER LYS ILE TYR PRO SER GLY          
SEQRES  10 N  268  SER GLY SER ARG SER ALA LEU LYS ARG ILE ASN LYS GLU          
SEQRES  11 N  268  LEU SER ASP LEU ALA ARG ASP PRO PRO ALA GLN CYS SER          
SEQRES  12 N  268  ALA GLY PRO VAL GLY ASP ASP MET PHE HIS TRP GLN ALA          
SEQRES  13 N  268  THR ILE MET GLY PRO ASN ASP SER PRO TYR GLN GLY GLY          
SEQRES  14 N  268  VAL PHE PHE LEU THR ILE HIS PHE PRO THR ASP TYR PRO          
SEQRES  15 N  268  PHE LYS PRO PRO LYS VAL ALA PHE THR THR ARG ILE TYR          
SEQRES  16 N  268  HIS PRO ASN ILE ASN SER ASN GLY SER ILE CYS LEU ASP          
SEQRES  17 N  268  ILE LEU ARG SER GLN TRP SER PRO ALA LEU THR ILE SER          
SEQRES  18 N  268  LYS VAL LEU LEU SER ILE CYS SER LEU LEU CYS ASP PRO          
SEQRES  19 N  268  ASN PRO ASP ASP PRO LEU VAL PRO GLU ILE ALA ARG ILE          
SEQRES  20 N  268  TYR LYS THR ASP ARG ASP LYS TYR ASN ARG ILE SER ARG          
SEQRES  21 N  268  GLU TRP THR GLN LYS TYR ALA MET                              
HET     ZN  K 201       1                                                       
HET     ZN  K 202       1                                                       
HET     ZN  L 401       1                                                       
HET     ZN  L 402       1                                                       
HET     ZN  M 201       1                                                       
HET     ZN  M 202       1                                                       
HET     ZN  N 401       1                                                       
HET     ZN  N 402       1                                                       
HETNAM      ZN ZINC ION                                                         
FORMUL  15   ZN    8(ZN 2+)                                                     
HELIX    1   1 GLY A   44  GLN A   55  1                                  12    
HELIX    2   2 ARG A   63  GLN A   76  1                                  14    
HELIX    3   3 GLN A   85  ALA A  114  1                                  30    
HELIX    4   4 MET A  120  ARG A  131  1                                  12    
HELIX    5   5 ASN B   25  ILE B   29  5                                   5    
HELIX    6   6 THR B   30  GLY B   42  1                                  13    
HELIX    7   7 LEU B   49  ALA B   76  1                                  28    
HELIX    8   8 THR B   82  GLN B   93  1                                  12    
HELIX    9   9 ARG C   17  ALA C   21  1                                   5    
HELIX   10  10 PRO C   26  LYS C   36  1                                  11    
HELIX   11  11 GLY C   46  ASN C   73  1                                  28    
HELIX   12  12 ILE C   79  ASN C   89  1                                  11    
HELIX   13  13 ASP C   90  LEU C   97  1                                   8    
HELIX   14  14 GLN C  112  LEU C  116  5                                   5    
HELIX   15  15 TYR D   37  HIS D   49  1                                  13    
HELIX   16  16 SER D   55  ASN D   84  1                                  30    
HELIX   17  17 THR D   90  LEU D  102  1                                  13    
HELIX   18  18 GLY D  104  TYR D  121  1                                  18    
HELIX   19  19 THR D  122  ALA D  124  5                                   3    
HELIX   20  20 GLY E   44  SER E   57  1                                  14    
HELIX   21  21 ARG E   63  GLN E   76  1                                  14    
HELIX   22  22 GLN E   85  ALA E  114  1                                  30    
HELIX   23  23 MET E  120  GLY E  132  1                                  13    
HELIX   24  24 ASN F   25  ILE F   29  5                                   5    
HELIX   25  25 THR F   30  GLY F   42  1                                  13    
HELIX   26  26 LEU F   49  ALA F   76  1                                  28    
HELIX   27  27 THR F   82  GLY F   94  1                                  13    
HELIX   28  28 THR G   16  ALA G   21  1                                   6    
HELIX   29  29 PRO G   26  LYS G   36  1                                  11    
HELIX   30  30 ALA G   45  ASN G   73  1                                  29    
HELIX   31  31 ILE G   79  ASP G   90  1                                  12    
HELIX   32  32 ASP G   90  LEU G   97  1                                   8    
HELIX   33  33 TYR H   37  HIS H   49  1                                  13    
HELIX   34  34 SER H   55  ASN H   84  1                                  30    
HELIX   35  35 THR H   90  LEU H  102  1                                  13    
HELIX   36  36 GLY H  104  ALA H  124  1                                  21    
HELIX   37  37 ILE K    9  ASN K   13  1                                   5    
HELIX   38  38 PRO K   14  LEU K   16  5                                   3    
HELIX   39  39 LYS K   40  LEU K   47  1                                   8    
HELIX   40  40 ARG K   64  LEU K   67  5                                   4    
HELIX   41  41 ASP K   72  VAL K   83  1                                  12    
HELIX   42  42 GLY K   85  TYR K   98  1                                  14    
HELIX   43  43 LEU L   45  MET L   50  1                                   6    
HELIX   44  44 ALA L   73  SER L   82  1                                  10    
HELIX   45  45 SER L   96  ARG L   98  5                                   3    
HELIX   46  46 ASP L  103  TYR L  114  1                                  12    
HELIX   47  47 ALA L  202  ASP L  216  1                                  15    
HELIX   48  48 LEU L  286  ARG L  290  5                                   5    
HELIX   49  49 THR L  298  ASP L  312  1                                  15    
HELIX   50  50 LYS M   40  LEU M   47  1                                   8    
HELIX   51  51 ARG M   64  LEU M   67  5                                   4    
HELIX   52  52 ASP M   72  VAL M   83  1                                  12    
HELIX   53  53 GLY M   85  TYR M   98  1                                  14    
HELIX   54  54 TYR N   22  ARG N   26  5                                   5    
HELIX   55  55 LEU N   45  LEU N   49  1                                   5    
HELIX   56  56 ALA N   73  SER N   82  1                                  10    
HELIX   57  57 SER N   96  ARG N   98  5                                   3    
HELIX   58  58 ASP N  103  TYR N  114  1                                  12    
HELIX   59  59 SER N  122  ASP N  216  1                                  16    
HELIX   60  60 LEU N  286  ARG N  290  5                                   5    
HELIX   61  61 THR N  298  ASP N  312  1                                  15    
HELIX   62  62 VAL N  320  ASP N  330  1                                  11    
HELIX   63  63 ARG N  331  ALA N  346  1                                  16    
SHEET    1   A 2 ARG A  83  PHE A  84  0                                        
SHEET    2   A 2 THR B  80  VAL B  81  1  O  VAL B  81   N  ARG A  83           
SHEET    1   B 2 THR A 118  ILE A 119  0                                        
SHEET    2   B 2 ARG B  45  ILE B  46  1  O  ARG B  45   N  ILE A 119           
SHEET    1   C 2 THR B  96  TYR B  98  0                                        
SHEET    2   C 2 VAL G 100  ILE G 102  1  O  THR G 101   N  THR B  96           
SHEET    1   D 2 ARG C  42  VAL C  43  0                                        
SHEET    2   D 2 THR D  88  ILE D  89  1  O  ILE D  89   N  ARG C  42           
SHEET    1   E 2 ARG C  77  ILE C  78  0                                        
SHEET    2   E 2 GLY D  53  ILE D  54  1  O  GLY D  53   N  ILE C  78           
SHEET    1   F 2 VAL C 100  ILE C 102  0                                        
SHEET    2   F 2 THR F  96  TYR F  98  1  O  THR F  96   N  THR C 101           
SHEET    1   G 2 ARG E  83  PHE E  84  0                                        
SHEET    2   G 2 THR F  80  VAL F  81  1  O  VAL F  81   N  ARG E  83           
SHEET    1   H 2 THR E 118  ILE E 119  0                                        
SHEET    2   H 2 ARG F  45  ILE F  46  1  O  ARG F  45   N  ILE E 119           
SHEET    1   I 2 ARG G  42  VAL G  43  0                                        
SHEET    2   I 2 THR H  88  ILE H  89  1  O  ILE H  89   N  ARG G  42           
SHEET    1   J 2 ARG G  77  ILE G  78  0                                        
SHEET    2   J 2 GLY H  53  ILE H  54  1  O  GLY H  53   N  ILE G  78           
SHEET    1   K 2 THR K   5  LYS K   8  0                                        
SHEET    2   K 2 GLU L  37  VAL L  40 -1  O  ILE L  38   N  ILE K   7           
SHEET    1   L 3 HIS K  36  CYS K  39  0                                        
SHEET    2   L 3 ALA K  28  ILE K  31 -1  N  THR K  29   O  PHE K  38           
SHEET    3   L 3 ILE K  69  SER K  71 -1  O  ARG K  70   N  THR K  30           
SHEET    1   M 3 ARG L  70  CYS L  72  0                                        
SHEET    2   M 3 THR L  61  THR L  64 -1  N  MET L  62   O  PHE L  71           
SHEET    3   M 3 LEU L 100  PRO L 102 -1  O  ARG L 101   N  THR L  63           
SHEET    1   N 4 CYS L 221  PRO L 225  0                                        
SHEET    2   N 4 HIS L 232  MET L 238 -1  O  GLN L 234   N  GLY L 224           
SHEET    3   N 4 VAL L 249  HIS L 255 -1  O  LEU L 252   N  ALA L 235           
SHEET    4   N 4 LYS L 266  PHE L 269 -1  O  ALA L 268   N  THR L 253           
SHEET    1   O 2 ILE M   7  LYS M   8  0                                        
SHEET    2   O 2 GLU N  37  ILE N  38 -1  O  ILE N  38   N  ILE M   7           
SHEET    1   P 2 MET M  17  CYS M  18  0                                        
SHEET    2   P 2 GLY M  23  TYR M  24 -1  O  GLY M  23   N  CYS M  18           
SHEET    1   Q 3 SER M  37  CYS M  39  0                                        
SHEET    2   Q 3 ALA M  28  ILE M  31 -1  N  THR M  29   O  PHE M  38           
SHEET    3   Q 3 ILE M  69  SER M  71 -1  O  ARG M  70   N  THR M  30           
SHEET    1   R 2 MET N  50  CYS N  51  0                                        
SHEET    2   R 2 ASP N  56  MET N  57 -1  O  ASP N  56   N  CYS N  51           
SHEET    1   S 3 ARG N  70  CYS N  72  0                                        
SHEET    2   S 3 THR N  61  THR N  64 -1  N  MET N  62   O  PHE N  71           
SHEET    3   S 3 LEU N 100  PRO N 102 -1  O  ARG N 101   N  THR N  63           
SHEET    1   T 4 CYS N 221  PRO N 225  0                                        
SHEET    2   T 4 HIS N 232  ILE N 237 -1  O  GLN N 234   N  GLY N 224           
SHEET    3   T 4 PHE N 250  HIS N 255 -1  O  ILE N 254   N  TRP N 233           
SHEET    4   T 4 LYS N 266  PHE N 269 -1  O  ALA N 268   N  THR N 253           
LINK         ND1 HIS K  36                ZN    ZN K 202     1555   1555  2.13  
LINK         SG  CYS M  21                ZN    ZN M 201     1555   1555  2.14  
LINK         ND1 HIS L  69                ZN    ZN L 402     1555   1555  2.15  
LINK         ND1 HIS M  36                ZN    ZN M 202     1555   1555  2.22  
LINK         SG  CYS M  18                ZN    ZN M 201     1555   1555  2.22  
LINK         ND1 HIS N  69                ZN    ZN N 402     1555   1555  2.24  
LINK         SG  CYS L  67                ZN    ZN L 402     1555   1555  2.28  
LINK         SG  CYS L  87                ZN    ZN L 402     1555   1555  2.31  
LINK         SG  CYS L  90                ZN    ZN L 402     1555   1555  2.32  
LINK         SG  CYS N  54                ZN    ZN N 401     1555   1555  2.33  
LINK         SG  CYS K  34                ZN    ZN K 202     1555   1555  2.33  
LINK         SG  CYS N  90                ZN    ZN N 402     1555   1555  2.34  
LINK         SG  CYS K  56                ZN    ZN K 202     1555   1555  2.34  
LINK         SG  CYS K  39                ZN    ZN K 201     1555   1555  2.35  
LINK         SG  CYS M  34                ZN    ZN M 202     1555   1555  2.36  
LINK         SG  CYS K  53                ZN    ZN K 202     1555   1555  2.36  
LINK         SG  CYS L  54                ZN    ZN L 401     1555   1555  2.38  
LINK         SG  CYS L  72                ZN    ZN L 401     1555   1555  2.39  
LINK         SG  CYS L  75                ZN    ZN L 401     1555   1555  2.40  
LINK         SG  CYS K  18                ZN    ZN K 201     1555   1555  2.40  
LINK         SG  CYS K  42                ZN    ZN K 201     1555   1555  2.42  
LINK         SG  CYS M  53                ZN    ZN M 202     1555   1555  2.43  
LINK         SG  CYS K  21                ZN    ZN K 201     1555   1555  2.43  
LINK         SG  CYS N  51                ZN    ZN N 401     1555   1555  2.43  
LINK         SG  CYS L  51                ZN    ZN L 401     1555   1555  2.44  
LINK         SG  CYS M  42                ZN    ZN M 201     1555   1555  2.44  
LINK         SG  CYS M  56                ZN    ZN M 202     1555   1555  2.44  
LINK         SG  CYS M  39                ZN    ZN M 201     1555   1555  2.44  
LINK         SG  CYS N  87                ZN    ZN N 402     1555   1555  2.46  
LINK         SG  CYS N  67                ZN    ZN N 402     1555   1555  2.54  
LINK         SG  CYS N  75                ZN    ZN N 401     1555   1555  2.54  
LINK         SG  CYS N  72                ZN    ZN N 401     1555   1555  2.59  
CISPEP   1 SER L  122    ALA L  202          0        -1.68                     
CISPEP   2 TYR L  260    PRO L  261          0         1.75                     
CISPEP   3 THR L  329    ASP L  330          0         3.60                     
CISPEP   4 TYR N  260    PRO N  261          0         2.01                     
SITE     1 AC1  4 CYS K  18  CYS K  21  CYS K  39  CYS K  42                    
SITE     1 AC2  4 CYS K  34  HIS K  36  CYS K  53  CYS K  56                    
SITE     1 AC3  4 CYS L  51  CYS L  54  CYS L  72  CYS L  75                    
SITE     1 AC4  5 CYS L  67  HIS L  69  CYS L  87  THR L  89                    
SITE     2 AC4  5 CYS L  90                                                     
SITE     1 AC5  4 CYS M  18  CYS M  21  CYS M  39  CYS M  42                    
SITE     1 AC6  4 CYS M  34  HIS M  36  CYS M  53  CYS M  56                    
SITE     1 AC7  5 CYS N  51  CYS N  54  CYS N  72  CYS N  75                    
SITE     2 AC7  5 ARG N 121                                                     
SITE     1 AC8  5 CYS N  67  HIS N  69  CYS N  87  THR N  89                    
SITE     2 AC8  5 CYS N  90                                                     
CRYST1  104.923  180.049  375.251  90.00  90.00  90.00 C 2 2 21     16          
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      0.009531  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.005554  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.002665        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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