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Database: PDB
Entry: 6NH2
LinkDB: 6NH2
Original site: 6NH2 
HEADER    OXIDOREDUCTASE/OXIDOREDUCTASE INHIBITOR 21-DEC-18   6NH2              
TITLE     STRUCTURE OF HUMAN ENDOTHELIAL NITRIC OXIDE SYNTHASE HEME DOMAIN IN   
TITLE    2 COMPLEX WITH (R)-6-(3-FLUORO-5-(2-(PYRROLIDIN-2-YL)ETHYL)PHENETHYL)- 
TITLE    3 4-METHYLPYRIDIN-2-AMINE                                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ENDOTHELIAL NITRIC OXIDE SYNTHASE SPLICE VARIANT ENOS13A;  
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 CELL_LINE: ENDOTHELIAL;                                              
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PCWORI                                    
KEYWDS    NITRIC OXIDE SYNTHASE INHIBITOR COMPLEX HEME ENZYME, OXIDOREDUCTASE,  
KEYWDS   2 OXIDOREDUCTASE-OXIDOREDUCTASE INHIBITOR COMPLEX                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    G.CHREIFI,H.LI,T.L.POULOS                                             
REVDAT   3   04-DEC-19 6NH2    1       REMARK                                   
REVDAT   2   27-MAR-19 6NH2    1       JRNL                                     
REVDAT   1   13-MAR-19 6NH2    0                                                
JRNL        AUTH   H.T.DO,H.LI,G.CHREIFI,T.L.POULOS,R.B.SILVERMAN               
JRNL        TITL   OPTIMIZATION OF BLOOD-BRAIN BARRIER PERMEABILITY WITH POTENT 
JRNL        TITL 2 AND SELECTIVE HUMAN NEURONAL NITRIC OXIDE SYNTHASE           
JRNL        TITL 3 INHIBITORS HAVING A 2-AMINOPYRIDINE SCAFFOLD.                
JRNL        REF    J. MED. CHEM.                 V.  62  2690 2019              
JRNL        REFN                   ISSN 1520-4804                               
JRNL        PMID   30802056                                                     
JRNL        DOI    10.1021/ACS.JMEDCHEM.8B02032                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.29 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.11.1-2575_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 : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.29                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 88.89                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.010                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 88652                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.175                           
REMARK   3   R VALUE            (WORKING SET) : 0.173                           
REMARK   3   FREE R VALUE                     : 0.222                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 8644                            
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 88.9520 -  7.1143    0.99     5621   246  0.1767 0.1803        
REMARK   3     2  7.1143 -  5.6471    0.98     5463   283  0.1562 0.1976        
REMARK   3     3  5.6471 -  4.9334    0.98     5450   306  0.1363 0.1878        
REMARK   3     4  4.9334 -  4.4823    0.98     5513   272  0.1211 0.1637        
REMARK   3     5  4.4823 -  4.1611    0.98     5511   270  0.1200 0.1653        
REMARK   3     6  4.1611 -  3.9157    0.99     5432   336  0.1246 0.1582        
REMARK   3     7  3.9157 -  3.7196    0.98     5538   248  0.1340 0.1523        
REMARK   3     8  3.7196 -  3.5577    0.99     5458   290  0.1470 0.2065        
REMARK   3     9  3.5577 -  3.4207    0.98     5509   302  0.1568 0.2046        
REMARK   3    10  3.4207 -  3.3027    0.98     5446   312  0.1641 0.2412        
REMARK   3    11  3.3027 -  3.1994    0.99     5508   292  0.1708 0.2353        
REMARK   3    12  3.1994 -  3.1080    0.98     5541   266  0.1857 0.2414        
REMARK   3    13  3.1080 -  3.0261    0.99     5524   246  0.1900 0.2758        
REMARK   3    14  3.0261 -  2.9523    0.98     5494   252  0.1820 0.2377        
REMARK   3    15  2.9523 -  2.8852    0.99     5489   311  0.1848 0.2400        
REMARK   3    16  2.8852 -  2.8238    0.97     5469   292  0.2049 0.2426        
REMARK   3    17  2.8238 -  2.7673    0.98     5523   270  0.2043 0.2731        
REMARK   3    18  2.7673 -  2.7151    0.98     5420   288  0.1992 0.2410        
REMARK   3    19  2.7151 -  2.6666    0.98     5462   325  0.1972 0.2426        
REMARK   3    20  2.6666 -  2.6214    0.99     5392   323  0.2088 0.2576        
REMARK   3    21  2.6214 -  2.5791    0.97     5460   311  0.2164 0.2754        
REMARK   3    22  2.5791 -  2.5394    0.98     5515   248  0.2224 0.2889        
REMARK   3    23  2.5394 -  2.5021    0.98     5374   299  0.2283 0.2890        
REMARK   3    24  2.5021 -  2.4668    0.97     5453   311  0.2347 0.3034        
REMARK   3    25  2.4668 -  2.4335    0.98     5494   293  0.2454 0.2939        
REMARK   3    26  2.4335 -  2.4019    0.97     5394   303  0.2393 0.2929        
REMARK   3    27  2.4019 -  2.3718    0.97     5449   253  0.2561 0.3069        
REMARK   3    28  2.3718 -  2.3433    0.98     5498   291  0.2542 0.3165        
REMARK   3    29  2.3433 -  2.3160    0.98     5291   337  0.2593 0.3102        
REMARK   3    30  2.3160 -  2.2900    0.95     5430   268  0.2797 0.3442        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
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)     : 0.280            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.130           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.011          13854                                  
REMARK   3   ANGLE     :  1.055          18878                                  
REMARK   3   CHIRALITY :  0.051           1954                                  
REMARK   3   PLANARITY :  0.006           2424                                  
REMARK   3   DIHEDRAL  : 14.613           8100                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 4                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 68:480)                             
REMARK   3    ORIGIN FOR THE GROUP (A):  65.4605  32.2716-185.5584              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2301 T22:   0.2914                                     
REMARK   3      T33:   0.3059 T12:   0.0616                                     
REMARK   3      T13:   0.0495 T23:   0.0924                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3246 L22:   1.3953                                     
REMARK   3      L33:   1.2378 L12:   0.0029                                     
REMARK   3      L13:  -0.1002 L23:  -0.0294                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1133 S12:   0.1412 S13:   0.1387                       
REMARK   3      S21:  -0.0511 S22:   0.0104 S23:   0.2577                       
REMARK   3      S31:  -0.2665 S32:  -0.2559 S33:  -0.0670                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: (CHAIN B AND RESID 67:480)                             
REMARK   3    ORIGIN FOR THE GROUP (A):  75.8713   9.2323-157.8340              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1492 T22:   0.1551                                     
REMARK   3      T33:   0.2077 T12:  -0.0393                                     
REMARK   3      T13:   0.0097 T23:   0.0081                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8518 L22:   0.9448                                     
REMARK   3      L33:   1.5486 L12:  -0.2300                                     
REMARK   3      L13:  -0.2313 L23:  -0.2736                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0438 S12:  -0.0029 S13:   0.0514                       
REMARK   3      S21:   0.1125 S22:   0.0473 S23:   0.0856                       
REMARK   3      S31:  -0.0486 S32:   0.0011 S33:  -0.0513                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: (CHAIN C AND RESID 68:480)                             
REMARK   3    ORIGIN FOR THE GROUP (A):  94.9785 -33.1515-195.6170              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2987 T22:   0.2141                                     
REMARK   3      T33:   0.2218 T12:  -0.0030                                     
REMARK   3      T13:  -0.0119 T23:   0.0562                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3746 L22:   1.3258                                     
REMARK   3      L33:   1.3033 L12:   0.2093                                     
REMARK   3      L13:   0.1675 L23:   0.1114                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0733 S12:  -0.1360 S13:  -0.1144                       
REMARK   3      S21:   0.1444 S22:  -0.0630 S23:   0.0815                       
REMARK   3      S31:   0.4137 S32:  -0.1122 S33:   0.0484                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: (CHAIN D AND RESID 67:480)                             
REMARK   3    ORIGIN FOR THE GROUP (A): 105.6529  -9.7900-223.0131              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1389 T22:   0.1434                                     
REMARK   3      T33:   0.1864 T12:   0.0320                                     
REMARK   3      T13:   0.0001 T23:  -0.0001                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7993 L22:   0.7625                                     
REMARK   3      L33:   1.4593 L12:   0.2122                                     
REMARK   3      L13:   0.2269 L23:   0.0448                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0037 S12:   0.0041 S13:  -0.0410                       
REMARK   3      S21:  -0.0371 S22:   0.0628 S23:  -0.0493                       
REMARK   3      S31:   0.0007 S32:   0.0770 S33:  -0.0464                       
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 6NH2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-JAN-19.                  
REMARK 100 THE DEPOSITION ID IS D_1000236916.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 19-JUL-17                          
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               : ALS                                
REMARK 200  BEAMLINE                       : 8.2.2                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.000                              
REMARK 200  MONOCHROMATOR                  : GRAPHITE                           
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 88704                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.290                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 90.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY                : 3.700                              
REMARK 200  R MERGE                    (I) : 0.13800                            
REMARK 200  R SYM                      (I) : 0.13800                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.6000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.29                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.35                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 1.29500                            
REMARK 200  R SYM FOR SHELL            (I) : 1.29500                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.300                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS            
REMARK 200 SOFTWARE USED: REFMAC                                                
REMARK 200 STARTING MODEL: 4DIP                                                 
REMARK 200                                                                      
REMARK 200 REMARK: RODS                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 54.30                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.69                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 12-15% PEG3350, 0.1M BIS-TRIS 0.2-0.3M   
REMARK 280  MG ACETATE, 0.1M GDCL3 10% GLYCEROL, 5 MM TCEP, PH 7.5, VAPOR       
REMARK 280  DIFFUSION, SITTING DROP, TEMPERATURE 277K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,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       76.88450            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 10400 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 34230 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -187.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 10340 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 33340 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -188.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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    41                                                      
REMARK 465     PRO A    42                                                      
REMARK 465     ALA A    43                                                      
REMARK 465     SER A    44                                                      
REMARK 465     LEU A    45                                                      
REMARK 465     LEU A    46                                                      
REMARK 465     PRO A    47                                                      
REMARK 465     PRO A    48                                                      
REMARK 465     ALA A    49                                                      
REMARK 465     PRO A    50                                                      
REMARK 465     GLU A    51                                                      
REMARK 465     HIS A    52                                                      
REMARK 465     SER A    53                                                      
REMARK 465     PRO A    54                                                      
REMARK 465     PRO A    55                                                      
REMARK 465     SER A    56                                                      
REMARK 465     SER A    57                                                      
REMARK 465     PRO A    58                                                      
REMARK 465     LEU A    59                                                      
REMARK 465     THR A    60                                                      
REMARK 465     GLN A    61                                                      
REMARK 465     PRO A    62                                                      
REMARK 465     PRO A    63                                                      
REMARK 465     GLU A    64                                                      
REMARK 465     GLY A    65                                                      
REMARK 465     PRO A    66                                                      
REMARK 465     LYS A    67                                                      
REMARK 465     GLN A   110                                                      
REMARK 465     GLY A   111                                                      
REMARK 465     ARG A   112                                                      
REMARK 465     PRO A   113                                                      
REMARK 465     SER A   114                                                      
REMARK 465     PRO A   115                                                      
REMARK 465     GLY A   116                                                      
REMARK 465     PRO A   117                                                      
REMARK 465     PRO A   118                                                      
REMARK 465     ALA B    41                                                      
REMARK 465     PRO B    42                                                      
REMARK 465     ALA B    43                                                      
REMARK 465     SER B    44                                                      
REMARK 465     LEU B    45                                                      
REMARK 465     LEU B    46                                                      
REMARK 465     PRO B    47                                                      
REMARK 465     PRO B    48                                                      
REMARK 465     ALA B    49                                                      
REMARK 465     PRO B    50                                                      
REMARK 465     GLU B    51                                                      
REMARK 465     HIS B    52                                                      
REMARK 465     SER B    53                                                      
REMARK 465     PRO B    54                                                      
REMARK 465     PRO B    55                                                      
REMARK 465     SER B    56                                                      
REMARK 465     SER B    57                                                      
REMARK 465     PRO B    58                                                      
REMARK 465     LEU B    59                                                      
REMARK 465     THR B    60                                                      
REMARK 465     GLN B    61                                                      
REMARK 465     PRO B    62                                                      
REMARK 465     PRO B    63                                                      
REMARK 465     GLU B    64                                                      
REMARK 465     GLY B    65                                                      
REMARK 465     PRO B    66                                                      
REMARK 465     ARG B   107                                                      
REMARK 465     LYS B   108                                                      
REMARK 465     LEU B   109                                                      
REMARK 465     GLN B   110                                                      
REMARK 465     GLY B   111                                                      
REMARK 465     ARG B   112                                                      
REMARK 465     PRO B   113                                                      
REMARK 465     SER B   114                                                      
REMARK 465     PRO B   115                                                      
REMARK 465     GLY B   116                                                      
REMARK 465     PRO B   117                                                      
REMARK 465     PRO B   118                                                      
REMARK 465     ALA C    41                                                      
REMARK 465     PRO C    42                                                      
REMARK 465     ALA C    43                                                      
REMARK 465     SER C    44                                                      
REMARK 465     LEU C    45                                                      
REMARK 465     LEU C    46                                                      
REMARK 465     PRO C    47                                                      
REMARK 465     PRO C    48                                                      
REMARK 465     ALA C    49                                                      
REMARK 465     PRO C    50                                                      
REMARK 465     GLU C    51                                                      
REMARK 465     HIS C    52                                                      
REMARK 465     SER C    53                                                      
REMARK 465     PRO C    54                                                      
REMARK 465     PRO C    55                                                      
REMARK 465     SER C    56                                                      
REMARK 465     SER C    57                                                      
REMARK 465     PRO C    58                                                      
REMARK 465     LEU C    59                                                      
REMARK 465     THR C    60                                                      
REMARK 465     GLN C    61                                                      
REMARK 465     PRO C    62                                                      
REMARK 465     PRO C    63                                                      
REMARK 465     GLU C    64                                                      
REMARK 465     GLY C    65                                                      
REMARK 465     PRO C    66                                                      
REMARK 465     LYS C    67                                                      
REMARK 465     ARG C   107                                                      
REMARK 465     LYS C   108                                                      
REMARK 465     LEU C   109                                                      
REMARK 465     GLN C   110                                                      
REMARK 465     GLY C   111                                                      
REMARK 465     ARG C   112                                                      
REMARK 465     PRO C   113                                                      
REMARK 465     SER C   114                                                      
REMARK 465     PRO C   115                                                      
REMARK 465     GLY C   116                                                      
REMARK 465     PRO C   117                                                      
REMARK 465     PRO C   118                                                      
REMARK 465     ALA D    41                                                      
REMARK 465     PRO D    42                                                      
REMARK 465     ALA D    43                                                      
REMARK 465     SER D    44                                                      
REMARK 465     LEU D    45                                                      
REMARK 465     LEU D    46                                                      
REMARK 465     PRO D    47                                                      
REMARK 465     PRO D    48                                                      
REMARK 465     ALA D    49                                                      
REMARK 465     PRO D    50                                                      
REMARK 465     GLU D    51                                                      
REMARK 465     HIS D    52                                                      
REMARK 465     SER D    53                                                      
REMARK 465     PRO D    54                                                      
REMARK 465     PRO D    55                                                      
REMARK 465     SER D    56                                                      
REMARK 465     SER D    57                                                      
REMARK 465     PRO D    58                                                      
REMARK 465     LEU D    59                                                      
REMARK 465     THR D    60                                                      
REMARK 465     GLN D    61                                                      
REMARK 465     PRO D    62                                                      
REMARK 465     PRO D    63                                                      
REMARK 465     GLU D    64                                                      
REMARK 465     GLY D    65                                                      
REMARK 465     PRO D    66                                                      
REMARK 465     ARG D   107                                                      
REMARK 465     LYS D   108                                                      
REMARK 465     LEU D   109                                                      
REMARK 465     GLN D   110                                                      
REMARK 465     GLY D   111                                                      
REMARK 465     ARG D   112                                                      
REMARK 465     PRO D   113                                                      
REMARK 465     SER D   114                                                      
REMARK 465     PRO D   115                                                      
REMARK 465     GLY D   116                                                      
REMARK 465     PRO D   117                                                      
REMARK 465     PRO D   118                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH D   816     O    HOH D   830              1.98            
REMARK 500   OH   TYR A   475     O1D  HEM A   501              2.09            
REMARK 500   NH1  ARG C   365     O2A  HEM C   502              2.10            
REMARK 500   O    HOH D   608     O    HOH D   818              2.12            
REMARK 500   NH1  ARG A   285     O    HOH A   601              2.12            
REMARK 500   OD1  ASP B    91     O    HOH B   601              2.13            
REMARK 500   O    HOH C   604     O    HOH C   686              2.13            
REMARK 500   O    GLY A   282     O    HOH A   602              2.14            
REMARK 500   O    HOH A   626     O    HOH A   660              2.15            
REMARK 500   OH   TYR B   475     O1D  HEM B   501              2.15            
REMARK 500   O    HOH A   628     O    HOH A   747              2.17            
REMARK 500   O    TRP B   480     O    HOH B   602              2.17            
REMARK 500   O    HOH B   789     O    HOH C   723              2.17            
REMARK 500   O    GLY D   282     O    HOH D   601              2.18            
REMARK 500   O    HOH A   633     O    HOH A   734              2.18            
REMARK 500   OE2  GLU B   321     O4   BTB B   503              2.18            
REMARK 500   O1   BTB B   504     O    HOH B   603              2.19            
REMARK 500   O    HOH C   725     O    HOH C   736              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   OE2  GLU A   152     O4   BTB D   505     2851     2.11            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ASP B 369   CB  -  CG  -  OD1 ANGL. DEV. =   5.4 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    GLN A  89      -75.56   -106.34                                   
REMARK 500    ARG A 107      -99.09     57.63                                   
REMARK 500    PRO A 120       39.16    -83.38                                   
REMARK 500    LYS A 139      -26.10     70.94                                   
REMARK 500    ARG A 140       35.64    -82.87                                   
REMARK 500    SER A 143      179.81     58.60                                   
REMARK 500    GLN A 144     -160.98     70.89                                   
REMARK 500    ARG A 238      152.43     74.97                                   
REMARK 500    GLN A 256     -161.50   -161.40                                   
REMARK 500    ASN A 283      -96.77    -63.75                                   
REMARK 500    PHE A 286       48.80   -143.84                                   
REMARK 500    ASP A 297      -61.61     70.36                                   
REMARK 500    ARG A 372     -132.27   -121.74                                   
REMARK 500    PRO A 479       27.82    -75.67                                   
REMARK 500    LYS B 139       48.02     39.54                                   
REMARK 500    ASP B 258       12.15    -61.17                                   
REMARK 500    ASN B 283       22.11   -140.20                                   
REMARK 500    ALA B 351       72.52   -155.38                                   
REMARK 500    ARG B 372     -135.66   -115.85                                   
REMARK 500    SER C 260     -176.04    -69.18                                   
REMARK 500    PHE C 286       55.01   -140.70                                   
REMARK 500    ASP C 297      -33.25     76.01                                   
REMARK 500    ALA C 351       72.70   -156.61                                   
REMARK 500    ARG C 372     -132.54   -113.31                                   
REMARK 500    CYS C 441      117.14   -160.61                                   
REMARK 500    GLN D  89       59.11   -157.37                                   
REMARK 500    ASN D 283       20.54   -145.02                                   
REMARK 500    ALA D 351       64.58   -156.88                                   
REMARK 500    ARG D 372     -135.57   -114.43                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 ARG C  238     GLY C  239                  147.98                    
REMARK 500 GLN D   89     GLN D   90                  139.09                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 749        DISTANCE =  5.92 ANGSTROMS                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 505  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A  94   SG                                                     
REMARK 620 2 CYS A  99   SG  111.9                                              
REMARK 620 3 CYS B  94   SG  122.3 109.8                                        
REMARK 620 4 CYS B  99   SG  105.0 104.1 101.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM A 501  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 184   SG                                                     
REMARK 620 2 HEM A 501   NA  102.0                                              
REMARK 620 3 HEM A 501   NB  100.4  89.8                                        
REMARK 620 4 HEM A 501   NC   95.7 162.3  87.3                                  
REMARK 620 5 HEM A 501   ND   98.9  88.9 160.5  88.0                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 506  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 369   OD1                                                    
REMARK 620 2 ASP A 369   OD2  60.0                                              
REMARK 620 3 HOH A 707   O   155.6  97.0                                        
REMARK 620 4 HOH A 726   O    87.4 132.3 104.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 510  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 461   NE2                                                    
REMARK 620 2 ASP B 369   OD1  83.8                                              
REMARK 620 3 ASP B 369   OD2 114.0  58.8                                        
REMARK 620 4 HOH B 755   O   117.6  84.6 110.8                                  
REMARK 620 5 HOH B 766   O   103.9 157.5  99.1 109.3                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM B 501  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 184   SG                                                     
REMARK 620 2 HEM B 501   NA  103.2                                              
REMARK 620 3 HEM B 501   NB  102.3  87.8                                        
REMARK 620 4 HEM B 501   NC   99.0 157.8  86.6                                  
REMARK 620 5 HEM B 501   ND  101.1  88.8 156.4  87.9                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              GD B 507  GD                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR B 319   O                                                      
REMARK 620 2 GLU B 321   OE1  83.7                                              
REMARK 620 3 BTB B 503   O3   85.4 135.9                                        
REMARK 620 4 BTB B 503   O4   93.6  64.7  73.5                                  
REMARK 620 5 BTB B 503   N   141.8 103.7  63.0  58.5                            
REMARK 620 6 BTB B 503   O6  149.1 115.4  94.9 116.2  60.5                      
REMARK 620 7 BTB B 503   O8  143.3  60.2 124.0  77.2  61.1  58.2                
REMARK 620 8 HOH C 619   O    80.9  75.7 143.8 140.4 137.3  80.8  84.1          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN D 501  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS C  94   SG                                                     
REMARK 620 2 CYS C  99   SG  112.3                                              
REMARK 620 3 CYS D  94   SG  113.0 110.4                                        
REMARK 620 4 CYS D  99   SG  102.9 110.4 107.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM C 502  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS C 184   SG                                                     
REMARK 620 2 HEM C 502   NA  104.7                                              
REMARK 620 3 HEM C 502   NB  100.6  86.1                                        
REMARK 620 4 HEM C 502   NC   96.9 158.3  87.9                                  
REMARK 620 5 HEM C 502   ND  102.4  88.8 157.0  88.7                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN C 507  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP C 369   OD2                                                    
REMARK 620 2 HOH C 692   O   105.2                                              
REMARK 620 3 HOH C 718   O   115.8 127.5                                        
REMARK 620 4 HOH C 724   O   150.5  73.5  54.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN C 511  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS C 461   NE2                                                    
REMARK 620 2 ASP D 369   OD1  84.1                                              
REMARK 620 3 ASP D 369   OD2 110.9  57.4                                        
REMARK 620 4 HOH D 789   O    99.0 149.8  94.1                                  
REMARK 620 5 HOH D 794   O   124.2  89.5 111.5 112.4                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM D 502  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS D 184   SG                                                     
REMARK 620 2 HEM D 502   NA  102.5                                              
REMARK 620 3 HEM D 502   NB  105.4  90.8                                        
REMARK 620 4 HEM D 502   NC  100.2 157.2  85.7                                  
REMARK 620 5 HEM D 502   ND   97.9  88.9 156.2  85.4                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              GD D 507  GD                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR D 319   O                                                      
REMARK 620 2 GLU D 321   OE1  90.2                                              
REMARK 620 3 BTB D 504   O3   72.7 131.0                                        
REMARK 620 4 BTB D 504   O4   91.7  76.0  59.6                                  
REMARK 620 5 BTB D 504   N   133.4 110.9  61.9  56.9                            
REMARK 620 6 BTB D 504   O6  127.7 128.0  97.0 127.7  70.8                      
REMARK 620 7 BTB D 504   O8  150.4  60.8 121.0  76.7  61.4  79.2                
REMARK 620 8 HOH D 621   O    58.6 139.4  67.7 125.4 109.4  69.9 148.9          
REMARK 620 9 HOH D 604   O   142.5  78.2 140.1 118.9  83.7  49.9  42.5 110.0    
REMARK 620 N                    1     2     3     4     5     6     7     8     
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue HEM A 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue H4B A 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue KMA A 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BTB A 504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 505                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 506                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 507                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 508                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue KMA A 509                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 510                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue HEM B 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue KMA B 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BTB B 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BTB B 504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BTB B 505                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 506                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GD B 507                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BTB B 508                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BTB C 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue HEM C 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue H4B C 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue KMA C 504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BTB C 505                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BTB C 506                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN C 507                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 508                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL C 509                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue KMA C 510                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN C 511                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN D 501                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue HEM D 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue KMA D 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BTB D 504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BTB D 505                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BTB D 506                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GD D 507                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL D 508                  
DBREF  6NH2 A   41   480  UNP    A0S0A6   A0S0A6_HUMAN    41    480             
DBREF  6NH2 B   41   480  UNP    A0S0A6   A0S0A6_HUMAN    41    480             
DBREF  6NH2 C   41   480  UNP    A0S0A6   A0S0A6_HUMAN    41    480             
DBREF  6NH2 D   41   480  UNP    A0S0A6   A0S0A6_HUMAN    41    480             
SEQRES   1 A  440  ALA PRO ALA SER LEU LEU PRO PRO ALA PRO GLU HIS SER          
SEQRES   2 A  440  PRO PRO SER SER PRO LEU THR GLN PRO PRO GLU GLY PRO          
SEQRES   3 A  440  LYS PHE PRO ARG VAL LYS ASN TRP GLU VAL GLY SER ILE          
SEQRES   4 A  440  THR TYR ASP THR LEU SER ALA GLN ALA GLN GLN ASP GLY          
SEQRES   5 A  440  PRO CYS THR PRO ARG ARG CYS LEU GLY SER LEU VAL PHE          
SEQRES   6 A  440  PRO ARG LYS LEU GLN GLY ARG PRO SER PRO GLY PRO PRO          
SEQRES   7 A  440  ALA PRO GLU GLN LEU LEU SER GLN ALA ARG ASP PHE ILE          
SEQRES   8 A  440  ASN GLN TYR TYR SER SER ILE LYS ARG SER GLY SER GLN          
SEQRES   9 A  440  ALA HIS GLU GLN ARG LEU GLN GLU VAL GLU ALA GLU VAL          
SEQRES  10 A  440  ALA ALA THR GLY THR TYR GLN LEU ARG GLU SER GLU LEU          
SEQRES  11 A  440  VAL PHE GLY ALA LYS GLN ALA TRP ARG ASN ALA PRO ARG          
SEQRES  12 A  440  CYS VAL GLY ARG ILE GLN TRP GLY LYS LEU GLN VAL PHE          
SEQRES  13 A  440  ASP ALA ARG ASP CYS ARG SER ALA GLN GLU MET PHE THR          
SEQRES  14 A  440  TYR ILE CYS ASN HIS ILE LYS TYR ALA THR ASN ARG GLY          
SEQRES  15 A  440  ASN LEU ARG SER ALA ILE THR VAL PHE PRO GLN ARG CYS          
SEQRES  16 A  440  PRO GLY ARG GLY ASP PHE ARG ILE TRP ASN SER GLN LEU          
SEQRES  17 A  440  VAL ARG TYR ALA GLY TYR ARG GLN GLN ASP GLY SER VAL          
SEQRES  18 A  440  ARG GLY ASP PRO ALA ASN VAL GLU ILE THR GLU LEU CYS          
SEQRES  19 A  440  ILE GLN HIS GLY TRP THR PRO GLY ASN GLY ARG PHE ASP          
SEQRES  20 A  440  VAL LEU PRO LEU LEU LEU GLN ALA PRO ASP GLU PRO PRO          
SEQRES  21 A  440  GLU LEU PHE LEU LEU PRO PRO GLU LEU VAL LEU GLU VAL          
SEQRES  22 A  440  PRO LEU GLU HIS PRO THR LEU GLU TRP PHE ALA ALA LEU          
SEQRES  23 A  440  GLY LEU ARG TRP TYR ALA LEU PRO ALA VAL SER ASN MET          
SEQRES  24 A  440  LEU LEU GLU ILE GLY GLY LEU GLU PHE PRO ALA ALA PRO          
SEQRES  25 A  440  PHE SER GLY TRP TYR MET SER THR GLU ILE GLY THR ARG          
SEQRES  26 A  440  ASN LEU CYS ASP PRO HIS ARG TYR ASN ILE LEU GLU ASP          
SEQRES  27 A  440  VAL ALA VAL CYS MET ASP LEU ASP THR ARG THR THR SER          
SEQRES  28 A  440  SER LEU TRP LYS ASP LYS ALA ALA VAL GLU ILE ASN VAL          
SEQRES  29 A  440  ALA VAL LEU HIS SER TYR GLN LEU ALA LYS VAL THR ILE          
SEQRES  30 A  440  VAL ASP HIS HIS ALA ALA THR ALA SER PHE MET LYS HIS          
SEQRES  31 A  440  LEU GLU ASN GLU GLN LYS ALA ARG GLY GLY CYS PRO ALA          
SEQRES  32 A  440  ASP TRP ALA TRP ILE VAL PRO PRO ILE SER GLY SER LEU          
SEQRES  33 A  440  THR PRO VAL PHE HIS GLN GLU MET VAL ASN TYR PHE LEU          
SEQRES  34 A  440  SER PRO ALA PHE ARG TYR GLN PRO ASP PRO TRP                  
SEQRES   1 B  440  ALA PRO ALA SER LEU LEU PRO PRO ALA PRO GLU HIS SER          
SEQRES   2 B  440  PRO PRO SER SER PRO LEU THR GLN PRO PRO GLU GLY PRO          
SEQRES   3 B  440  LYS PHE PRO ARG VAL LYS ASN TRP GLU VAL GLY SER ILE          
SEQRES   4 B  440  THR TYR ASP THR LEU SER ALA GLN ALA GLN GLN ASP GLY          
SEQRES   5 B  440  PRO CYS THR PRO ARG ARG CYS LEU GLY SER LEU VAL PHE          
SEQRES   6 B  440  PRO ARG LYS LEU GLN GLY ARG PRO SER PRO GLY PRO PRO          
SEQRES   7 B  440  ALA PRO GLU GLN LEU LEU SER GLN ALA ARG ASP PHE ILE          
SEQRES   8 B  440  ASN GLN TYR TYR SER SER ILE LYS ARG SER GLY SER GLN          
SEQRES   9 B  440  ALA HIS GLU GLN ARG LEU GLN GLU VAL GLU ALA GLU VAL          
SEQRES  10 B  440  ALA ALA THR GLY THR TYR GLN LEU ARG GLU SER GLU LEU          
SEQRES  11 B  440  VAL PHE GLY ALA LYS GLN ALA TRP ARG ASN ALA PRO ARG          
SEQRES  12 B  440  CYS VAL GLY ARG ILE GLN TRP GLY LYS LEU GLN VAL PHE          
SEQRES  13 B  440  ASP ALA ARG ASP CYS ARG SER ALA GLN GLU MET PHE THR          
SEQRES  14 B  440  TYR ILE CYS ASN HIS ILE LYS TYR ALA THR ASN ARG GLY          
SEQRES  15 B  440  ASN LEU ARG SER ALA ILE THR VAL PHE PRO GLN ARG CYS          
SEQRES  16 B  440  PRO GLY ARG GLY ASP PHE ARG ILE TRP ASN SER GLN LEU          
SEQRES  17 B  440  VAL ARG TYR ALA GLY TYR ARG GLN GLN ASP GLY SER VAL          
SEQRES  18 B  440  ARG GLY ASP PRO ALA ASN VAL GLU ILE THR GLU LEU CYS          
SEQRES  19 B  440  ILE GLN HIS GLY TRP THR PRO GLY ASN GLY ARG PHE ASP          
SEQRES  20 B  440  VAL LEU PRO LEU LEU LEU GLN ALA PRO ASP GLU PRO PRO          
SEQRES  21 B  440  GLU LEU PHE LEU LEU PRO PRO GLU LEU VAL LEU GLU VAL          
SEQRES  22 B  440  PRO LEU GLU HIS PRO THR LEU GLU TRP PHE ALA ALA LEU          
SEQRES  23 B  440  GLY LEU ARG TRP TYR ALA LEU PRO ALA VAL SER ASN MET          
SEQRES  24 B  440  LEU LEU GLU ILE GLY GLY LEU GLU PHE PRO ALA ALA PRO          
SEQRES  25 B  440  PHE SER GLY TRP TYR MET SER THR GLU ILE GLY THR ARG          
SEQRES  26 B  440  ASN LEU CYS ASP PRO HIS ARG TYR ASN ILE LEU GLU ASP          
SEQRES  27 B  440  VAL ALA VAL CYS MET ASP LEU ASP THR ARG THR THR SER          
SEQRES  28 B  440  SER LEU TRP LYS ASP LYS ALA ALA VAL GLU ILE ASN VAL          
SEQRES  29 B  440  ALA VAL LEU HIS SER TYR GLN LEU ALA LYS VAL THR ILE          
SEQRES  30 B  440  VAL ASP HIS HIS ALA ALA THR ALA SER PHE MET LYS HIS          
SEQRES  31 B  440  LEU GLU ASN GLU GLN LYS ALA ARG GLY GLY CYS PRO ALA          
SEQRES  32 B  440  ASP TRP ALA TRP ILE VAL PRO PRO ILE SER GLY SER LEU          
SEQRES  33 B  440  THR PRO VAL PHE HIS GLN GLU MET VAL ASN TYR PHE LEU          
SEQRES  34 B  440  SER PRO ALA PHE ARG TYR GLN PRO ASP PRO TRP                  
SEQRES   1 C  440  ALA PRO ALA SER LEU LEU PRO PRO ALA PRO GLU HIS SER          
SEQRES   2 C  440  PRO PRO SER SER PRO LEU THR GLN PRO PRO GLU GLY PRO          
SEQRES   3 C  440  LYS PHE PRO ARG VAL LYS ASN TRP GLU VAL GLY SER ILE          
SEQRES   4 C  440  THR TYR ASP THR LEU SER ALA GLN ALA GLN GLN ASP GLY          
SEQRES   5 C  440  PRO CYS THR PRO ARG ARG CYS LEU GLY SER LEU VAL PHE          
SEQRES   6 C  440  PRO ARG LYS LEU GLN GLY ARG PRO SER PRO GLY PRO PRO          
SEQRES   7 C  440  ALA PRO GLU GLN LEU LEU SER GLN ALA ARG ASP PHE ILE          
SEQRES   8 C  440  ASN GLN TYR TYR SER SER ILE LYS ARG SER GLY SER GLN          
SEQRES   9 C  440  ALA HIS GLU GLN ARG LEU GLN GLU VAL GLU ALA GLU VAL          
SEQRES  10 C  440  ALA ALA THR GLY THR TYR GLN LEU ARG GLU SER GLU LEU          
SEQRES  11 C  440  VAL PHE GLY ALA LYS GLN ALA TRP ARG ASN ALA PRO ARG          
SEQRES  12 C  440  CYS VAL GLY ARG ILE GLN TRP GLY LYS LEU GLN VAL PHE          
SEQRES  13 C  440  ASP ALA ARG ASP CYS ARG SER ALA GLN GLU MET PHE THR          
SEQRES  14 C  440  TYR ILE CYS ASN HIS ILE LYS TYR ALA THR ASN ARG GLY          
SEQRES  15 C  440  ASN LEU ARG SER ALA ILE THR VAL PHE PRO GLN ARG CYS          
SEQRES  16 C  440  PRO GLY ARG GLY ASP PHE ARG ILE TRP ASN SER GLN LEU          
SEQRES  17 C  440  VAL ARG TYR ALA GLY TYR ARG GLN GLN ASP GLY SER VAL          
SEQRES  18 C  440  ARG GLY ASP PRO ALA ASN VAL GLU ILE THR GLU LEU CYS          
SEQRES  19 C  440  ILE GLN HIS GLY TRP THR PRO GLY ASN GLY ARG PHE ASP          
SEQRES  20 C  440  VAL LEU PRO LEU LEU LEU GLN ALA PRO ASP GLU PRO PRO          
SEQRES  21 C  440  GLU LEU PHE LEU LEU PRO PRO GLU LEU VAL LEU GLU VAL          
SEQRES  22 C  440  PRO LEU GLU HIS PRO THR LEU GLU TRP PHE ALA ALA LEU          
SEQRES  23 C  440  GLY LEU ARG TRP TYR ALA LEU PRO ALA VAL SER ASN MET          
SEQRES  24 C  440  LEU LEU GLU ILE GLY GLY LEU GLU PHE PRO ALA ALA PRO          
SEQRES  25 C  440  PHE SER GLY TRP TYR MET SER THR GLU ILE GLY THR ARG          
SEQRES  26 C  440  ASN LEU CYS ASP PRO HIS ARG TYR ASN ILE LEU GLU ASP          
SEQRES  27 C  440  VAL ALA VAL CYS MET ASP LEU ASP THR ARG THR THR SER          
SEQRES  28 C  440  SER LEU TRP LYS ASP LYS ALA ALA VAL GLU ILE ASN VAL          
SEQRES  29 C  440  ALA VAL LEU HIS SER TYR GLN LEU ALA LYS VAL THR ILE          
SEQRES  30 C  440  VAL ASP HIS HIS ALA ALA THR ALA SER PHE MET LYS HIS          
SEQRES  31 C  440  LEU GLU ASN GLU GLN LYS ALA ARG GLY GLY CYS PRO ALA          
SEQRES  32 C  440  ASP TRP ALA TRP ILE VAL PRO PRO ILE SER GLY SER LEU          
SEQRES  33 C  440  THR PRO VAL PHE HIS GLN GLU MET VAL ASN TYR PHE LEU          
SEQRES  34 C  440  SER PRO ALA PHE ARG TYR GLN PRO ASP PRO TRP                  
SEQRES   1 D  440  ALA PRO ALA SER LEU LEU PRO PRO ALA PRO GLU HIS SER          
SEQRES   2 D  440  PRO PRO SER SER PRO LEU THR GLN PRO PRO GLU GLY PRO          
SEQRES   3 D  440  LYS PHE PRO ARG VAL LYS ASN TRP GLU VAL GLY SER ILE          
SEQRES   4 D  440  THR TYR ASP THR LEU SER ALA GLN ALA GLN GLN ASP GLY          
SEQRES   5 D  440  PRO CYS THR PRO ARG ARG CYS LEU GLY SER LEU VAL PHE          
SEQRES   6 D  440  PRO ARG LYS LEU GLN GLY ARG PRO SER PRO GLY PRO PRO          
SEQRES   7 D  440  ALA PRO GLU GLN LEU LEU SER GLN ALA ARG ASP PHE ILE          
SEQRES   8 D  440  ASN GLN TYR TYR SER SER ILE LYS ARG SER GLY SER GLN          
SEQRES   9 D  440  ALA HIS GLU GLN ARG LEU GLN GLU VAL GLU ALA GLU VAL          
SEQRES  10 D  440  ALA ALA THR GLY THR TYR GLN LEU ARG GLU SER GLU LEU          
SEQRES  11 D  440  VAL PHE GLY ALA LYS GLN ALA TRP ARG ASN ALA PRO ARG          
SEQRES  12 D  440  CYS VAL GLY ARG ILE GLN TRP GLY LYS LEU GLN VAL PHE          
SEQRES  13 D  440  ASP ALA ARG ASP CYS ARG SER ALA GLN GLU MET PHE THR          
SEQRES  14 D  440  TYR ILE CYS ASN HIS ILE LYS TYR ALA THR ASN ARG GLY          
SEQRES  15 D  440  ASN LEU ARG SER ALA ILE THR VAL PHE PRO GLN ARG CYS          
SEQRES  16 D  440  PRO GLY ARG GLY ASP PHE ARG ILE TRP ASN SER GLN LEU          
SEQRES  17 D  440  VAL ARG TYR ALA GLY TYR ARG GLN GLN ASP GLY SER VAL          
SEQRES  18 D  440  ARG GLY ASP PRO ALA ASN VAL GLU ILE THR GLU LEU CYS          
SEQRES  19 D  440  ILE GLN HIS GLY TRP THR PRO GLY ASN GLY ARG PHE ASP          
SEQRES  20 D  440  VAL LEU PRO LEU LEU LEU GLN ALA PRO ASP GLU PRO PRO          
SEQRES  21 D  440  GLU LEU PHE LEU LEU PRO PRO GLU LEU VAL LEU GLU VAL          
SEQRES  22 D  440  PRO LEU GLU HIS PRO THR LEU GLU TRP PHE ALA ALA LEU          
SEQRES  23 D  440  GLY LEU ARG TRP TYR ALA LEU PRO ALA VAL SER ASN MET          
SEQRES  24 D  440  LEU LEU GLU ILE GLY GLY LEU GLU PHE PRO ALA ALA PRO          
SEQRES  25 D  440  PHE SER GLY TRP TYR MET SER THR GLU ILE GLY THR ARG          
SEQRES  26 D  440  ASN LEU CYS ASP PRO HIS ARG TYR ASN ILE LEU GLU ASP          
SEQRES  27 D  440  VAL ALA VAL CYS MET ASP LEU ASP THR ARG THR THR SER          
SEQRES  28 D  440  SER LEU TRP LYS ASP LYS ALA ALA VAL GLU ILE ASN VAL          
SEQRES  29 D  440  ALA VAL LEU HIS SER TYR GLN LEU ALA LYS VAL THR ILE          
SEQRES  30 D  440  VAL ASP HIS HIS ALA ALA THR ALA SER PHE MET LYS HIS          
SEQRES  31 D  440  LEU GLU ASN GLU GLN LYS ALA ARG GLY GLY CYS PRO ALA          
SEQRES  32 D  440  ASP TRP ALA TRP ILE VAL PRO PRO ILE SER GLY SER LEU          
SEQRES  33 D  440  THR PRO VAL PHE HIS GLN GLU MET VAL ASN TYR PHE LEU          
SEQRES  34 D  440  SER PRO ALA PHE ARG TYR GLN PRO ASP PRO TRP                  
HET    HEM  A 501      43                                                       
HET    H4B  A 502      17                                                       
HET    KMA  A 503      24                                                       
HET    BTB  A 504      14                                                       
HET     ZN  A 505       1                                                       
HET     ZN  A 506       1                                                       
HET    GOL  A 507       6                                                       
HET     CL  A 508       1                                                       
HET    KMA  A 509      24                                                       
HET     ZN  A 510       1                                                       
HET    HEM  B 501      43                                                       
HET    KMA  B 502      24                                                       
HET    BTB  B 503      14                                                       
HET    BTB  B 504      14                                                       
HET    BTB  B 505      14                                                       
HET     CL  B 506       1                                                       
HET     GD  B 507       1                                                       
HET    BTB  B 508      14                                                       
HET    BTB  C 501      14                                                       
HET    HEM  C 502      43                                                       
HET    H4B  C 503      17                                                       
HET    KMA  C 504      24                                                       
HET    BTB  C 505      14                                                       
HET    BTB  C 506      14                                                       
HET     ZN  C 507       1                                                       
HET    GOL  C 508       6                                                       
HET     CL  C 509       1                                                       
HET    KMA  C 510      24                                                       
HET     ZN  C 511       1                                                       
HET     ZN  D 501       1                                                       
HET    HEM  D 502      43                                                       
HET    KMA  D 503      24                                                       
HET    BTB  D 504      14                                                       
HET    BTB  D 505      14                                                       
HET    BTB  D 506      14                                                       
HET     GD  D 507       1                                                       
HET     CL  D 508       1                                                       
HETNAM     HEM PROTOPORPHYRIN IX CONTAINING FE                                  
HETNAM     H4B 5,6,7,8-TETRAHYDROBIOPTERIN                                      
HETNAM     KMA 6-[2-(3-FLUORO-5-{2-[(2R)-PYRROLIDIN-2-                          
HETNAM   2 KMA  YL]ETHYL}PHENYL)ETHYL]-4-METHYLPYRIDIN-2-AMINE                  
HETNAM     BTB 2-[BIS-(2-HYDROXY-ETHYL)-AMINO]-2-HYDROXYMETHYL-                 
HETNAM   2 BTB  PROPANE-1,3-DIOL                                                
HETNAM      ZN ZINC ION                                                         
HETNAM     GOL GLYCEROL                                                         
HETNAM      CL CHLORIDE ION                                                     
HETNAM      GD GADOLINIUM ATOM                                                  
HETSYN     HEM HEME                                                             
HETSYN     BTB BIS-TRIS BUFFER                                                  
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   5  HEM    4(C34 H32 FE N4 O4)                                          
FORMUL   6  H4B    2(C9 H15 N5 O3)                                              
FORMUL   7  KMA    6(C20 H26 F N3)                                              
FORMUL   8  BTB    11(C8 H19 N O5)                                              
FORMUL   9   ZN    6(ZN 2+)                                                     
FORMUL  11  GOL    2(C3 H8 O3)                                                  
FORMUL  12   CL    4(CL 1-)                                                     
FORMUL  21   GD    2(GD)                                                        
FORMUL  42  HOH   *711(H2 O)                                                    
HELIX    1 AA1 THR A   83  ALA A   88  5                                   6    
HELIX    2 AA2 PRO A  120  SER A  137  1                                  18    
HELIX    3 AA3 SER A  143  GLY A  161  1                                  19    
HELIX    4 AA4 ARG A  166  ASN A  180  1                                  15    
HELIX    5 AA5 GLY A  186  TRP A  190  5                                   5    
HELIX    6 AA6 SER A  203  ASN A  220  1                                  18    
HELIX    7 AA7 ARG A  221  ASN A  223  5                                   3    
HELIX    8 AA8 ASN A  267  HIS A  277  1                                  11    
HELIX    9 AA9 PRO A  306  VAL A  310  5                                   5    
HELIX   10 AB1 LEU A  320  GLY A  327  5                                   8    
HELIX   11 AB2 SER A  359  THR A  364  1                                   6    
HELIX   12 AB3 THR A  364  ASP A  369  1                                   6    
HELIX   13 AB4 ILE A  375  MET A  383  1                                   9    
HELIX   14 AB5 THR A  389  SER A  392  5                                   4    
HELIX   15 AB6 LEU A  393  ALA A  413  1                                  21    
HELIX   16 AB7 ASP A  419  GLY A  439  1                                  21    
HELIX   17 AB8 ASP A  444  VAL A  449  1                                   6    
HELIX   18 AB9 SER A  453  THR A  457  5                                   5    
HELIX   19 AC1 THR B   83  ALA B   88  5                                   6    
HELIX   20 AC2 PRO B  120  ILE B  138  1                                  19    
HELIX   21 AC3 SER B  143  GLY B  161  1                                  19    
HELIX   22 AC4 ARG B  166  ASN B  180  1                                  15    
HELIX   23 AC5 GLY B  186  TRP B  190  5                                   5    
HELIX   24 AC6 SER B  203  ASN B  220  1                                  18    
HELIX   25 AC7 ARG B  221  ASN B  223  5                                   3    
HELIX   26 AC8 ASN B  267  HIS B  277  1                                  11    
HELIX   27 AC9 PRO B  306  VAL B  310  5                                   5    
HELIX   28 AD1 LEU B  320  GLY B  327  5                                   8    
HELIX   29 AD2 MET B  358  THR B  364  1                                   7    
HELIX   30 AD3 THR B  364  ASP B  369  1                                   6    
HELIX   31 AD4 ILE B  375  MET B  383  1                                   9    
HELIX   32 AD5 THR B  389  SER B  392  5                                   4    
HELIX   33 AD6 LEU B  393  ALA B  413  1                                  21    
HELIX   34 AD7 ASP B  419  GLY B  439  1                                  21    
HELIX   35 AD8 ASP B  444  VAL B  449  1                                   6    
HELIX   36 AD9 SER B  453  THR B  457  5                                   5    
HELIX   37 AE1 LEU C   84  ALA C   88  5                                   5    
HELIX   38 AE2 PRO C  120  SER C  137  1                                  18    
HELIX   39 AE3 SER C  143  GLY C  161  1                                  19    
HELIX   40 AE4 ARG C  166  ASN C  180  1                                  15    
HELIX   41 AE5 GLY C  186  TRP C  190  5                                   5    
HELIX   42 AE6 SER C  203  ASN C  220  1                                  18    
HELIX   43 AE7 ARG C  221  ASN C  223  5                                   3    
HELIX   44 AE8 ASN C  267  HIS C  277  1                                  11    
HELIX   45 AE9 PRO C  306  VAL C  310  5                                   5    
HELIX   46 AF1 LEU C  320  GLY C  327  5                                   8    
HELIX   47 AF2 SER C  359  THR C  364  1                                   6    
HELIX   48 AF3 ILE C  375  MET C  383  1                                   9    
HELIX   49 AF4 THR C  389  SER C  392  5                                   4    
HELIX   50 AF5 LEU C  393  ALA C  413  1                                  21    
HELIX   51 AF6 ASP C  419  GLY C  439  1                                  21    
HELIX   52 AF7 ASP C  444  VAL C  449  1                                   6    
HELIX   53 AF8 SER C  453  THR C  457  5                                   5    
HELIX   54 AF9 THR D   83  ALA D   88  5                                   6    
HELIX   55 AG1 PRO D  120  ILE D  138  1                                  19    
HELIX   56 AG2 SER D  143  GLY D  161  1                                  19    
HELIX   57 AG3 ARG D  166  ASN D  180  1                                  15    
HELIX   58 AG4 GLY D  186  TRP D  190  5                                   5    
HELIX   59 AG5 SER D  203  ASN D  220  1                                  18    
HELIX   60 AG6 ARG D  221  ASN D  223  5                                   3    
HELIX   61 AG7 ASN D  267  HIS D  277  1                                  11    
HELIX   62 AG8 PRO D  306  VAL D  310  5                                   5    
HELIX   63 AG9 LEU D  320  GLY D  327  5                                   8    
HELIX   64 AH1 SER D  359  THR D  364  1                                   6    
HELIX   65 AH2 THR D  364  ASP D  369  1                                   6    
HELIX   66 AH3 ILE D  375  MET D  383  1                                   9    
HELIX   67 AH4 THR D  389  SER D  392  5                                   4    
HELIX   68 AH5 LEU D  393  ALA D  413  1                                  21    
HELIX   69 AH6 ASP D  419  GLY D  439  1                                  21    
HELIX   70 AH7 ASP D  444  VAL D  449  1                                   6    
HELIX   71 AH8 SER D  453  GLN D  462  5                                  10    
SHEET    1 AA1 2 ARG A  70  LYS A  72  0                                        
SHEET    2 AA1 2 ILE A  79  TYR A  81 -1  O  THR A  80   N  VAL A  71           
SHEET    1 AA2 4 GLN A 194  ASP A 197  0                                        
SHEET    2 AA2 4 ALA A 227  VAL A 230  1  O  ILE A 228   N  PHE A 196           
SHEET    3 AA2 4 PHE A 353  SER A 354 -1  O  SER A 354   N  ALA A 227           
SHEET    4 AA2 4 ALA A 335  VAL A 336 -1  N  VAL A 336   O  PHE A 353           
SHEET    1 AA3 3 ARG A 242  ILE A 243  0                                        
SHEET    2 AA3 3 LEU A 291  GLN A 294 -1  O  GLN A 294   N  ARG A 242           
SHEET    3 AA3 3 GLU A 301  PHE A 303 -1  O  PHE A 303   N  LEU A 291           
SHEET    1 AA4 2 GLY A 253  TYR A 254  0                                        
SHEET    2 AA4 2 ARG A 262  GLY A 263 -1  O  ARG A 262   N  TYR A 254           
SHEET    1 AA5 2 GLU A 312  PRO A 314  0                                        
SHEET    2 AA5 2 ARG A 329  TYR A 331 -1  O  TRP A 330   N  VAL A 313           
SHEET    1 AA6 3 LEU A 346  PHE A 348  0                                        
SHEET    2 AA6 3 LEU A 340  ILE A 343 -1  N  LEU A 341   O  PHE A 348           
SHEET    3 AA6 3 ALA A 472  ARG A 474 -1  O  ARG A 474   N  LEU A 340           
SHEET    1 AA7 2 TYR A 357  MET A 358  0                                        
SHEET    2 AA7 2 ILE A 417  VAL A 418  1  O  VAL A 418   N  TYR A 357           
SHEET    1 AA8 2 ARG B  70  LYS B  72  0                                        
SHEET    2 AA8 2 ILE B  79  TYR B  81 -1  O  THR B  80   N  VAL B  71           
SHEET    1 AA9 4 GLN B 194  ASP B 197  0                                        
SHEET    2 AA9 4 ALA B 227  VAL B 230  1  O  ILE B 228   N  PHE B 196           
SHEET    3 AA9 4 PHE B 353  SER B 354 -1  O  SER B 354   N  ALA B 227           
SHEET    4 AA9 4 ALA B 335  VAL B 336 -1  N  VAL B 336   O  PHE B 353           
SHEET    1 AB1 3 ARG B 242  ILE B 243  0                                        
SHEET    2 AB1 3 LEU B 291  GLN B 294 -1  O  GLN B 294   N  ARG B 242           
SHEET    3 AB1 3 GLU B 301  PHE B 303 -1  O  PHE B 303   N  LEU B 291           
SHEET    1 AB2 2 GLY B 253  ARG B 255  0                                        
SHEET    2 AB2 2 VAL B 261  GLY B 263 -1  O  ARG B 262   N  TYR B 254           
SHEET    1 AB3 2 GLU B 312  PRO B 314  0                                        
SHEET    2 AB3 2 ARG B 329  TYR B 331 -1  O  TRP B 330   N  VAL B 313           
SHEET    1 AB4 3 LEU B 346  PHE B 348  0                                        
SHEET    2 AB4 3 LEU B 340  ILE B 343 -1  N  LEU B 341   O  PHE B 348           
SHEET    3 AB4 3 ALA B 472  ARG B 474 -1  O  ARG B 474   N  LEU B 340           
SHEET    1 AB5 2 ARG C  70  LYS C  72  0                                        
SHEET    2 AB5 2 ILE C  79  TYR C  81 -1  O  THR C  80   N  VAL C  71           
SHEET    1 AB6 4 GLN C 194  ASP C 197  0                                        
SHEET    2 AB6 4 ALA C 227  VAL C 230  1  O  ILE C 228   N  PHE C 196           
SHEET    3 AB6 4 PHE C 353  SER C 354 -1  O  SER C 354   N  ALA C 227           
SHEET    4 AB6 4 ALA C 335  VAL C 336 -1  N  VAL C 336   O  PHE C 353           
SHEET    1 AB7 3 ARG C 242  ILE C 243  0                                        
SHEET    2 AB7 3 LEU C 291  GLN C 294 -1  O  GLN C 294   N  ARG C 242           
SHEET    3 AB7 3 GLU C 301  PHE C 303 -1  O  PHE C 303   N  LEU C 291           
SHEET    1 AB8 2 GLY C 253  ARG C 255  0                                        
SHEET    2 AB8 2 VAL C 261  GLY C 263 -1  O  ARG C 262   N  TYR C 254           
SHEET    1 AB9 2 GLU C 312  PRO C 314  0                                        
SHEET    2 AB9 2 ARG C 329  TYR C 331 -1  O  TRP C 330   N  VAL C 313           
SHEET    1 AC1 3 LEU C 346  PHE C 348  0                                        
SHEET    2 AC1 3 LEU C 340  ILE C 343 -1  N  ILE C 343   O  LEU C 346           
SHEET    3 AC1 3 ALA C 472  ARG C 474 -1  O  ARG C 474   N  LEU C 340           
SHEET    1 AC2 2 TYR C 357  MET C 358  0                                        
SHEET    2 AC2 2 ILE C 417  VAL C 418  1  O  VAL C 418   N  TYR C 357           
SHEET    1 AC3 2 ARG D  70  LYS D  72  0                                        
SHEET    2 AC3 2 ILE D  79  TYR D  81 -1  O  THR D  80   N  VAL D  71           
SHEET    1 AC4 4 GLN D 194  ASP D 197  0                                        
SHEET    2 AC4 4 ALA D 227  VAL D 230  1  O  ILE D 228   N  PHE D 196           
SHEET    3 AC4 4 PHE D 353  SER D 354 -1  O  SER D 354   N  ALA D 227           
SHEET    4 AC4 4 ALA D 335  VAL D 336 -1  N  VAL D 336   O  PHE D 353           
SHEET    1 AC5 3 ARG D 242  ILE D 243  0                                        
SHEET    2 AC5 3 LEU D 291  GLN D 294 -1  O  GLN D 294   N  ARG D 242           
SHEET    3 AC5 3 GLU D 301  PHE D 303 -1  O  GLU D 301   N  LEU D 293           
SHEET    1 AC6 2 GLY D 253  ARG D 255  0                                        
SHEET    2 AC6 2 VAL D 261  GLY D 263 -1  O  ARG D 262   N  TYR D 254           
SHEET    1 AC7 2 GLU D 312  PRO D 314  0                                        
SHEET    2 AC7 2 ARG D 329  TYR D 331 -1  O  TRP D 330   N  VAL D 313           
SHEET    1 AC8 3 LEU D 346  PHE D 348  0                                        
SHEET    2 AC8 3 LEU D 340  ILE D 343 -1  N  LEU D 341   O  PHE D 348           
SHEET    3 AC8 3 ALA D 472  ARG D 474 -1  O  ARG D 474   N  LEU D 340           
SHEET    1 AC9 2 TYR D 357  MET D 358  0                                        
SHEET    2 AC9 2 ILE D 417  VAL D 418  1  O  VAL D 418   N  TYR D 357           
LINK         SG  CYS A  94                ZN    ZN A 505     1555   1555  2.40  
LINK         SG  CYS A  99                ZN    ZN A 505     1555   1555  2.38  
LINK         SG  CYS A 184                FE   HEM A 501     1555   1555  2.31  
LINK         OD1 ASP A 369                ZN    ZN A 506     1555   1555  2.23  
LINK         OD2 ASP A 369                ZN    ZN A 506     1555   1555  2.03  
LINK         NE2 HIS A 461                ZN    ZN A 510     1555   1555  2.12  
LINK         SG  CYS B  94                ZN    ZN A 505     1555   1555  2.36  
LINK         SG  CYS B  99                ZN    ZN A 505     1555   1555  2.46  
LINK         SG  CYS B 184                FE   HEM B 501     1555   1555  2.37  
LINK         O   THR B 319                GD    GD B 507     1555   1555  2.63  
LINK         OE1 GLU B 321                GD    GD B 507     1555   1555  2.73  
LINK         OD1 ASP B 369                ZN    ZN A 510     1555   1555  2.31  
LINK         OD2 ASP B 369                ZN    ZN A 510     1555   1555  2.03  
LINK         SG  CYS C  94                ZN    ZN D 501     1555   1555  2.41  
LINK         SG  CYS C  99                ZN    ZN D 501     1555   1555  2.37  
LINK         SG  CYS C 184                FE   HEM C 502     1555   1555  2.36  
LINK         OD2 ASP C 369                ZN    ZN C 507     1555   1555  2.09  
LINK         NE2 HIS C 461                ZN    ZN C 511     1555   1555  2.19  
LINK         SG  CYS D  94                ZN    ZN D 501     1555   1555  2.40  
LINK         SG  CYS D  99                ZN    ZN D 501     1555   1555  2.37  
LINK         SG  CYS D 184                FE   HEM D 502     1555   1555  2.36  
LINK         O   THR D 319                GD    GD D 507     1555   1555  2.71  
LINK         OE1 GLU D 321                GD    GD D 507     1555   1555  2.63  
LINK         OD1 ASP D 369                ZN    ZN C 511     1555   1555  2.35  
LINK         OD2 ASP D 369                ZN    ZN C 511     1555   1555  2.06  
LINK        ZN    ZN A 506                 O   HOH A 707     1555   1555  1.86  
LINK        ZN    ZN A 506                 O   HOH A 726     1555   1555  2.25  
LINK        ZN    ZN A 510                 O   HOH B 755     1555   1555  2.32  
LINK        ZN    ZN A 510                 O   HOH B 766     1555   1555  2.28  
LINK         O3  BTB B 503                GD    GD B 507     1555   1555  2.69  
LINK         O4  BTB B 503                GD    GD B 507     1555   1555  2.56  
LINK         N   BTB B 503                GD    GD B 507     1555   1555  2.84  
LINK         O6  BTB B 503                GD    GD B 507     1555   1555  2.97  
LINK         O8  BTB B 503                GD    GD B 507     1555   1555  2.71  
LINK        GD    GD B 507                 O   HOH C 619     1555   1555  2.74  
LINK        ZN    ZN C 507                 O   HOH C 692     1555   1555  1.93  
LINK        ZN    ZN C 507                 O   HOH C 718     1555   1555  2.23  
LINK        ZN    ZN C 507                 O   HOH C 724     1555   1555  2.54  
LINK        ZN    ZN C 511                 O   HOH D 789     1555   1555  2.34  
LINK        ZN    ZN C 511                 O   HOH D 794     1555   1555  2.30  
LINK         O3  BTB D 504                GD    GD D 507     1555   1555  2.67  
LINK         O4  BTB D 504                GD    GD D 507     1555   1555  2.62  
LINK         N   BTB D 504                GD    GD D 507     1555   1555  2.87  
LINK         O6  BTB D 504                GD    GD D 507     1555   1555  2.74  
LINK         O8  BTB D 504                GD    GD D 507     1555   1555  3.00  
LINK        GD    GD D 507                 O   HOH D 621     1555   1555  2.49  
LINK        GD    GD D 507                 O   HOH D 604     1555   1555  3.49  
LINK        GD    GD D 507                 O   HOH A 624     1555   1655  2.72  
CISPEP   1 SER A  470    PRO A  471          0         0.30                     
CISPEP   2 SER B  470    PRO B  471          0        -3.61                     
CISPEP   3 SER C  470    PRO C  471          0        -2.12                     
CISPEP   4 SER D  470    PRO D  471          0         0.80                     
SITE     1 AC1 14 TRP A 178  CYS A 184  SER A 226  PHE A 353                    
SITE     2 AC1 14 SER A 354  TRP A 356  GLU A 361  ARG A 365                    
SITE     3 AC1 14 TRP A 447  PHE A 473  TYR A 475  H4B A 502                    
SITE     4 AC1 14 KMA A 503  HOH A 666                                          
SITE     1 AC2 15 SER A 102  VAL A 104  ALA A 446  TRP A 447                    
SITE     2 AC2 15 HEM A 501  KMA A 503  HOH A 616  HOH A 632                    
SITE     3 AC2 15 HOH A 719  HOH A 722  TRP B 445  PHE B 460                    
SITE     4 AC2 15 HIS B 461  GLN B 462  GLU B 463                               
SITE     1 AC3 12 VAL A 104  PHE A 105  PRO A 334  GLY A 355                    
SITE     2 AC3 12 TRP A 356  TYR A 357  GLU A 361  ARG A 365                    
SITE     3 AC3 12 TRP A 447  TYR A 475  HEM A 501  H4B A 502                    
SITE     1 AC4  4 GLU A 377  THR A 387  ARG A 388  ASP D 384                    
SITE     1 AC5  4 CYS A  94  CYS A  99  CYS B  94  CYS B  99                    
SITE     1 AC6  4 ASP A 369  HOH A 707  HOH A 726  HIS B 461                    
SITE     1 AC7  1 GLU A 167                                                     
SITE     1 AC8  4 GLN A 247  TYR A 357  ARG A 365  ASN A 366                    
SITE     1 AC9  9 TRP A  74  TRP A 445  PHE A 460  SER B 102                    
SITE     2 AC9  9 VAL B 104  ARG B 365  ALA B 446  KMA B 502                    
SITE     3 AC9  9 HOH B 766                                                     
SITE     1 AD1  4 HIS A 461  ASP B 369  HOH B 755  HOH B 766                    
SITE     1 AD2 18 TRP B 178  ARG B 183  CYS B 184  VAL B 185                    
SITE     2 AD2 18 SER B 226  PHE B 353  SER B 354  TRP B 356                    
SITE     3 AD2 18 MET B 358  GLU B 361  ARG B 365  TRP B 447                    
SITE     4 AD2 18 PHE B 473  TYR B 475  KMA B 502  HOH B 621                    
SITE     5 AD2 18 HOH B 722  HOH B 729                                          
SITE     1 AD3 10 KMA A 509  VAL B 104  TRP B 356  TYR B 357                    
SITE     2 AD3 10 GLU B 361  ARG B 365  TRP B 447  TYR B 475                    
SITE     3 AD3 10 HEM B 501  HOH B 761                                          
SITE     1 AD4  9 THR B 319  GLU B 321   GD B 507  HOH B 605                    
SITE     2 AD4  9 SER C 260  VAL C 261  TYR C 373  ASN C 374                    
SITE     3 AD4  9 ASP C 378                                                     
SITE     1 AD5  5 GLU B 298  HOH B 603  HOH B 604  HOH B 752                    
SITE     2 AD5  5 GLU D 167                                                     
SITE     1 AD6  3 ASN B 374  GLU B 377  ASP B 378                               
SITE     1 AD7  5 GLN B 247  TYR B 357  ARG B 365  ASN B 366                    
SITE     2 AD7  5 HOH B 719                                                     
SITE     1 AD8  4 THR B 319  GLU B 321  BTB B 503  HOH C 619                    
SITE     1 AD9  2 ASP B 384  GLU C 377                                          
SITE     1 AE1  7 ASP A 384  THR A 387  ARG A 388  HOH A 611                    
SITE     2 AE1  7 GLN C 257  VAL D 381  ASP D 384                               
SITE     1 AE2 17 TRP C 178  ARG C 183  CYS C 184  VAL C 185                    
SITE     2 AE2 17 SER C 226  PHE C 353  SER C 354  TRP C 356                    
SITE     3 AE2 17 MET C 358  GLU C 361  ARG C 365  PHE C 473                    
SITE     4 AE2 17 TYR C 475  H4B C 503  KMA C 504  HOH C 620                    
SITE     5 AE2 17 HOH C 641                                                     
SITE     1 AE3 13 SER C 102  VAL C 104  ALA C 446  TRP C 447                    
SITE     2 AE3 13 HEM C 502  KMA C 504  HOH C 654  HOH C 692                    
SITE     3 AE3 13 HOH C 719  TRP D 445  PHE D 460  HIS D 461                    
SITE     4 AE3 13 GLU D 463                                                     
SITE     1 AE4 10 PHE C 105  PRO C 334  GLY C 355  TRP C 356                    
SITE     2 AE4 10 TYR C 357  GLU C 361  ARG C 365  TYR C 475                    
SITE     3 AE4 10 HEM C 502  H4B C 503                                          
SITE     1 AE5  6 GLN A 257  VAL B 381  ASP C 384  LEU C 385                    
SITE     2 AE5  6 ASP C 386  THR C 387                                          
SITE     1 AE6  1 GLU C 298                                                     
SITE     1 AE7  6 ARG C 365  ASP C 369  HOH C 692  HOH C 718                    
SITE     2 AE7  6 HOH C 724  HIS D 461                                          
SITE     1 AE8  1 GLU C 167                                                     
SITE     1 AE9  4 GLN C 247  TYR C 357  ARG C 365  ASN C 366                    
SITE     1 AF1 12 TRP C  74  TRP C 445  PHE C 460  SER D 102                    
SITE     2 AF1 12 VAL D 104  ARG D 365  ALA D 446  TRP D 447                    
SITE     3 AF1 12 KMA D 503  HOH D 649  HOH D 730  HOH D 816                    
SITE     1 AF2  4 HIS C 461  ASP D 369  HOH D 789  HOH D 794                    
SITE     1 AF3  4 CYS C  94  CYS C  99  CYS D  94  CYS D  99                    
SITE     1 AF4 16 TRP D 178  ARG D 183  CYS D 184  VAL D 185                    
SITE     2 AF4 16 SER D 226  PHE D 353  SER D 354  TRP D 356                    
SITE     3 AF4 16 GLU D 361  ARG D 365  TRP D 447  PHE D 473                    
SITE     4 AF4 16 TYR D 475  KMA D 503  HOH D 676  HOH D 743                    
SITE     1 AF5 11 KMA C 510  VAL D 104  PRO D 334  GLY D 355                    
SITE     2 AF5 11 TRP D 356  GLU D 361  ARG D 365  TRP D 447                    
SITE     3 AF5 11 TYR D 475  HEM D 502  HOH D 706                               
SITE     1 AF6  8 TYR A 373  ASN A 374  ASP A 378  THR D 319                    
SITE     2 AF6  8 GLU D 321   GD D 507  HOH D 604  HOH D 621                    
SITE     1 AF7  3 ASP D 297  GLU D 298  HOH D 802                               
SITE     1 AF8  3 GLU D 377  ASP D 378  HOH D 728                               
SITE     1 AF9  5 HOH A 624  THR D 319  GLU D 321  BTB D 504                    
SITE     2 AF9  5 HOH D 621                                                     
SITE     1 AG1  6 GLN D 247  ARG D 250  TYR D 357  ARG D 365                    
SITE     2 AG1  6 ASN D 366  HOH D 753                                          
CRYST1   60.329  153.769  108.939  90.00  90.86  90.00 P 1 21 1      8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.016576  0.000000  0.000249        0.00000                         
SCALE2      0.000000  0.006503  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009180        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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