GenomeNet

Database: PDB
Entry: 6NH5
LinkDB: 6NH5
Original site: 6NH5 
HEADER    OXIDOREDUCTASE/OXIDOREDUCTASE INHIBITOR 21-DEC-18   6NH5              
TITLE     STRUCTURE OF HUMAN ENDOTHELIAL NITRIC OXIDE SYNTHASE HEME DOMAIN IN   
TITLE    2 COMPLEX WITH 6-(3-FLUORO-5-(2-((2R,4S)-4-FLUORO-1-METHYLPYRROLIDIN-2-
TITLE    3 YL)ETHYL)PHENETHYL)-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 6NH5    1       REMARK                                   
REVDAT   2   27-MAR-19 6NH5    1       JRNL                                     
REVDAT   1   13-MAR-19 6NH5    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.    1.96 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) : 1.96                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 88.71                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 139178                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.200                           
REMARK   3   R VALUE            (WORKING SET) : 0.197                           
REMARK   3   FREE R VALUE                     : 0.241                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.040                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 13718                           
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 88.8034 -  6.0864    0.99     8677   405  0.1777 0.1730        
REMARK   3     2  6.0864 -  4.8310    0.99     8657   472  0.1440 0.2055        
REMARK   3     3  4.8310 -  4.2204    0.99     8663   429  0.1277 0.1734        
REMARK   3     4  4.2204 -  3.8345    0.99     8714   479  0.1352 0.1627        
REMARK   3     5  3.8345 -  3.5596    0.99     8629   443  0.1592 0.2133        
REMARK   3     6  3.5596 -  3.3498    0.98     8557   475  0.1760 0.2231        
REMARK   3     7  3.3498 -  3.1820    0.99     8597   459  0.1889 0.2480        
REMARK   3     8  3.1820 -  3.0435    0.99     8705   432  0.1946 0.2635        
REMARK   3     9  3.0435 -  2.9263    0.99     8688   386  0.1996 0.2851        
REMARK   3    10  2.9263 -  2.8253    0.99     8573   487  0.2024 0.2356        
REMARK   3    11  2.8253 -  2.7370    0.99     8695   430  0.2035 0.2409        
REMARK   3    12  2.7370 -  2.6587    0.98     8480   464  0.2056 0.2397        
REMARK   3    13  2.6587 -  2.5887    0.98     8492   499  0.2025 0.2718        
REMARK   3    14  2.5887 -  2.5256    0.98     8611   448  0.2109 0.2613        
REMARK   3    15  2.5256 -  2.4682    0.99     8614   453  0.2252 0.2684        
REMARK   3    16  2.4682 -  2.4156    0.99     8640   482  0.2389 0.3134        
REMARK   3    17  2.4156 -  2.3673    0.99     8596   452  0.2389 0.2981        
REMARK   3    18  2.3673 -  2.3226    0.99     8666   457  0.2393 0.2857        
REMARK   3    19  2.3226 -  2.2811    0.99     8600   488  0.2440 0.2819        
REMARK   3    20  2.2811 -  2.2425    0.98     8718   393  0.2726 0.3071        
REMARK   3    21  2.2425 -  2.2063    0.98     8485   485  0.2776 0.3311        
REMARK   3    22  2.2063 -  2.1723    0.98     8706   413  0.2768 0.2947        
REMARK   3    23  2.1723 -  2.1404    0.98     8574   452  0.2970 0.3408        
REMARK   3    24  2.1404 -  2.1102    0.99     8569   494  0.3011 0.3364        
REMARK   3    25  2.1102 -  2.0817    0.99     8584   482  0.3131 0.3450        
REMARK   3    26  2.0817 -  2.0547    0.98     8478   520  0.3280 0.3394        
REMARK   3    27  2.0547 -  2.0290    0.98     8667   472  0.3232 0.3368        
REMARK   3    28  2.0290 -  2.0046    0.99     8617   459  0.3334 0.3450        
REMARK   3    29  2.0046 -  1.9812    0.99     8546   456  0.3481 0.4120        
REMARK   3    30  1.9812 -  1.9590    0.98     8654   452  0.3734 0.4060        
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)     : 0.260            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 30.170           
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          13904                                  
REMARK   3   ANGLE     :  1.030          18951                                  
REMARK   3   CHIRALITY :  0.055           1970                                  
REMARK   3   PLANARITY :  0.006           2426                                  
REMARK   3   DIHEDRAL  : 15.483           8129                                  
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):  64.1955  30.8927-185.5708              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4880 T22:   0.5932                                     
REMARK   3      T33:   0.4656 T12:   0.2545                                     
REMARK   3      T13:   0.1775 T23:   0.2715                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0959 L22:   2.2855                                     
REMARK   3      L33:   2.3559 L12:   0.2267                                     
REMARK   3      L13:  -0.6727 L23:  -0.6338                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3093 S12:   0.4758 S13:   0.3897                       
REMARK   3      S21:   0.0632 S22:   0.1921 S23:   0.4262                       
REMARK   3      S31:  -0.8010 S32:  -0.7961 S33:  -0.3109                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: ( CHAIN B AND RESID 67:480 )                           
REMARK   3    ORIGIN FOR THE GROUP (A):  74.2928   7.7711-157.8667              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2198 T22:   0.1979                                     
REMARK   3      T33:   0.2597 T12:  -0.0670                                     
REMARK   3      T13:  -0.0015 T23:   0.0152                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1824 L22:   1.7426                                     
REMARK   3      L33:   3.1170 L12:  -0.2527                                     
REMARK   3      L13:  -0.4592 L23:  -0.7857                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0540 S12:  -0.0525 S13:   0.0622                       
REMARK   3      S21:   0.3531 S22:   0.0959 S23:   0.0539                       
REMARK   3      S31:  -0.1698 S32:  -0.1243 S33:  -0.1313                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: ( CHAIN C AND RESID 68:480 )                           
REMARK   3    ORIGIN FOR THE GROUP (A):  93.0467 -34.8927-195.7255              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5576 T22:   0.3364                                     
REMARK   3      T33:   0.3626 T12:  -0.0253                                     
REMARK   3      T13:  -0.0685 T23:   0.0996                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7176 L22:   2.5133                                     
REMARK   3      L33:   1.9701 L12:   0.0568                                     
REMARK   3      L13:   0.2902 L23:   0.0238                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1307 S12:  -0.2649 S13:  -0.2784                       
REMARK   3      S21:   0.1613 S22:  -0.0057 S23:   0.2236                       
REMARK   3      S31:   0.7702 S32:  -0.1912 S33:  -0.0703                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: ( CHAIN D AND RESID 68:480 )                           
REMARK   3    ORIGIN FOR THE GROUP (A): 103.4811 -11.4044-223.1388              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2335 T22:   0.1676                                     
REMARK   3      T33:   0.2429 T12:   0.0520                                     
REMARK   3      T13:  -0.0095 T23:  -0.0131                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9271 L22:   0.9609                                     
REMARK   3      L33:   3.0069 L12:   0.3080                                     
REMARK   3      L13:   0.3923 L23:  -0.0013                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0244 S12:   0.0170 S13:  -0.0545                       
REMARK   3      S21:  -0.1240 S22:   0.0802 S23:  -0.0605                       
REMARK   3      S31:  -0.0760 S32:   0.2022 S33:  -0.0558                       
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 6NH5 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_1000236918.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 28-MAY-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                       : 5.0.2                              
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                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 300K               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 139289                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.959                              
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     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 5.600                              
REMARK 200  R MERGE                    (I) : 0.13300                            
REMARK 200  R SYM                      (I) : 0.13300                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.6000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.95                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.01                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 2.41200                            
REMARK 200  R SYM FOR SHELL            (I) : 2.41200                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 7.600                              
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       76.38000            
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: 11830 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 34620 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -133.0 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: 10450 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 32900 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -148.0 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     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     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     LYS D    67                                                      
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 C   606     O    HOH C   708              2.03            
REMARK 500   O2A  HEM C   501     F13  KLD C   503              2.07            
REMARK 500   O    HOH C   678     O    HOH C   708              2.09            
REMARK 500   OD1  ASP B   378     O4   BTB B   506              2.12            
REMARK 500   O    HOH C   631     O    HOH C   718              2.13            
REMARK 500   O    HOH D   694     O    HOH D   785              2.13            
REMARK 500   OH   TYR C   475     O1D  HEM C   501              2.14            
REMARK 500   O    HOH B   748     O    HOH B   761              2.15            
REMARK 500   O2A  HEM A   501     F13  KLD A   503              2.16            
REMARK 500   O    HOH B   775     O    HOH B   778              2.16            
REMARK 500   O    HOH D   726     O    HOH D   765              2.17            
REMARK 500   O    HOH B   684     O    HOH B   742              2.18            
REMARK 500   OE1  GLU C   298     O6   BTB C   505              2.18            
REMARK 500   O    HOH D   773     O    HOH D   783              2.18            
REMARK 500   O    HOH C   700     O    HOH D   751              2.19            
REMARK 500   NH2  ARG A   242     O    PRO A   477              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   OE1  GLU D   167     O8   BTB B   505     1554     2.13            
REMARK 500   O    HOH B   612     O    HOH D   608     1456     2.15            
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      -92.24   -116.98                                   
REMARK 500    GLN A  90      100.28    -40.83                                   
REMARK 500    PRO A 106      106.70    -58.53                                   
REMARK 500    ARG A 107     -120.84     64.18                                   
REMARK 500    LYS A 139      -27.74     71.40                                   
REMARK 500    SER A 143     -164.80     81.53                                   
REMARK 500    GLN A 144     -139.40     39.52                                   
REMARK 500    ARG A 238      145.17     66.83                                   
REMARK 500    ARG A 255     -165.72   -101.99                                   
REMARK 500    PRO A 281     -162.62    -71.49                                   
REMARK 500    ASP A 297       -7.97     72.62                                   
REMARK 500    ARG A 372     -135.18   -112.58                                   
REMARK 500    PRO A 479       45.22    -73.43                                   
REMARK 500    LYS B 192       74.84   -106.01                                   
REMARK 500    ASP B 258        5.84    -61.39                                   
REMARK 500    ASN B 283       16.85   -140.64                                   
REMARK 500    ALA B 351       72.37   -157.37                                   
REMARK 500    ARG B 372     -134.64   -115.28                                   
REMARK 500    GLN C  89      -81.08    -70.84                                   
REMARK 500    ALA C 145      -40.54   -175.83                                   
REMARK 500    ARG C 202      -51.52   -121.78                                   
REMARK 500    ARG C 238     -154.01     75.34                                   
REMARK 500    PRO C 296      112.30    -36.93                                   
REMARK 500    ASP C 297      -35.25     73.02                                   
REMARK 500    ARG C 372     -137.64   -112.12                                   
REMARK 500    CYS C 441      118.70   -164.41                                   
REMARK 500    ASN D 283       27.72   -140.94                                   
REMARK 500    ALA D 351       67.17   -154.50                                   
REMARK 500    ARG D 372     -131.35   -113.85                                   
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                 -144.32                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 507  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A  94   SG                                                     
REMARK 620 2 CYS A  99   SG  106.3                                              
REMARK 620 3 CYS B  94   SG  120.8 107.1                                        
REMARK 620 4 CYS B  99   SG  111.0 105.3 105.3                                  
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  104.4                                              
REMARK 620 3 HEM A 501   NB  103.1  88.0                                        
REMARK 620 4 HEM A 501   NC   92.2 163.3  88.9                                  
REMARK 620 5 HEM A 501   ND   96.3  89.6 160.4  87.9                            
REMARK 620 N                    1     2     3     4                             
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  94.3                                              
REMARK 620 3 ASP B 369   OD2 113.9  66.0                                        
REMARK 620 4 HOH B 761   O   132.3  95.6 112.7                                  
REMARK 620 5 HOH B 722   O   112.5 150.7  91.2  75.7                            
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  101.7                                              
REMARK 620 3 HEM B 501   NB  100.8  91.0                                        
REMARK 620 4 HEM B 501   NC   97.6 160.7  85.2                                  
REMARK 620 5 HEM B 501   ND  101.3  87.8 157.6  88.6                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              GD B 508  GD                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR B 319   O                                                      
REMARK 620 2 GLU B 321   OE1  74.3                                              
REMARK 620 3 BTB B 504   O3   85.2 129.9                                        
REMARK 620 4 BTB B 504   O4   81.6  76.4  55.3                                  
REMARK 620 5 BTB B 504   N   145.0 105.5  68.0  64.9                            
REMARK 620 6 BTB B 504   O6  146.4 113.2 109.1 131.7  67.0                      
REMARK 620 7 BTB B 504   O8  130.3  56.9 132.6  94.8  65.8  61.0                
REMARK 620 8 HOH B 749   O    76.5 134.0  81.2 132.7 118.7  76.0 131.1          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN C 506  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS C  94   SG                                                     
REMARK 620 2 CYS C  99   SG  104.9                                              
REMARK 620 3 CYS D  94   SG  120.4 110.5                                        
REMARK 620 4 CYS D  99   SG  106.6 105.1 108.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM C 501  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS C 184   SG                                                     
REMARK 620 2 HEM C 501   NA  103.8                                              
REMARK 620 3 HEM C 501   NB  101.1  85.2                                        
REMARK 620 4 HEM C 501   NC   96.7 159.5  90.6                                  
REMARK 620 5 HEM C 501   ND  100.7  90.8 158.2  85.7                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN C 510  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS C 461   NE2                                                    
REMARK 620 2 ASP D 369   OD1  86.8                                              
REMARK 620 3 ASP D 369   OD2 100.6  61.5                                        
REMARK 620 4 HOH C 685   O   106.0 156.0  95.8                                  
REMARK 620 5 HOH D 751   O   121.9  88.1 126.5 101.3                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM D 501  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS D 184   SG                                                     
REMARK 620 2 HEM D 501   NA  103.5                                              
REMARK 620 3 HEM D 501   NB  101.1  89.4                                        
REMARK 620 4 HEM D 501   NC   96.8 159.6  85.5                                  
REMARK 620 5 HEM D 501   ND  101.2  89.1 157.4  88.1                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              GD D 506  GD                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR D 319   O                                                      
REMARK 620 2 GLU D 321   OE1  79.7                                              
REMARK 620 3 BTB D 503   O3   81.2 138.2                                        
REMARK 620 4 BTB D 503   O4   85.2  74.5  67.1                                  
REMARK 620 5 BTB D 503   N   137.9 103.5  68.5  56.7                            
REMARK 620 6 BTB D 503   O6  136.9 119.5  99.7 135.2  78.5                      
REMARK 620 7 BTB D 503   O8  128.5  50.8 124.4  70.1  58.7  86.6                
REMARK 620 8 HOH D 613   O    82.4 136.0  76.9 143.3 116.4  56.6 141.6          
REMARK 620 9 HOH A 605   O    86.8  73.0 142.3 147.3 134.8  66.2  90.8  66.2    
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 KLD 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 BTB A 505                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BTB A 506                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 507                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 508                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL 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 BTB A 511                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue HEM B 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue H4B B 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue KLD B 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BTB B 504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BTB B 505                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BTB B 506                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 507                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GD B 508                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BTB B 509                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue HEM C 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue H4B C 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue KLD C 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BTB C 504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BTB C 505                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN C 506                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 507                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL C 508                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue H4B C 509                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN C 510                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue HEM D 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue KLD D 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BTB D 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BTB D 504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BTB D 505                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GD D 506                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL D 507                  
DBREF  6NH5 A   41   480  UNP    A0S0A6   A0S0A6_HUMAN    41    480             
DBREF  6NH5 B   41   480  UNP    A0S0A6   A0S0A6_HUMAN    41    480             
DBREF  6NH5 C   41   480  UNP    A0S0A6   A0S0A6_HUMAN    41    480             
DBREF  6NH5 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    KLD  A 503      26                                                       
HET    BTB  A 504      14                                                       
HET    BTB  A 505      14                                                       
HET    BTB  A 506      14                                                       
HET     ZN  A 507       1                                                       
HET    GOL  A 508       6                                                       
HET     CL  A 509       1                                                       
HET     ZN  A 510       1                                                       
HET    BTB  A 511      14                                                       
HET    HEM  B 501      43                                                       
HET    H4B  B 502      17                                                       
HET    KLD  B 503      26                                                       
HET    BTB  B 504      14                                                       
HET    BTB  B 505      14                                                       
HET    BTB  B 506      14                                                       
HET     CL  B 507       1                                                       
HET     GD  B 508       1                                                       
HET    BTB  B 509      14                                                       
HET    HEM  C 501      43                                                       
HET    H4B  C 502      17                                                       
HET    KLD  C 503      26                                                       
HET    BTB  C 504      14                                                       
HET    BTB  C 505      14                                                       
HET     ZN  C 506       1                                                       
HET    GOL  C 507       6                                                       
HET     CL  C 508       1                                                       
HET    H4B  C 509      17                                                       
HET     ZN  C 510       1                                                       
HET    HEM  D 501      43                                                       
HET    KLD  D 502      26                                                       
HET    BTB  D 503      14                                                       
HET    BTB  D 504      14                                                       
HET    BTB  D 505      14                                                       
HET     GD  D 506       1                                                       
HET     CL  D 507       1                                                       
HETNAM     HEM PROTOPORPHYRIN IX CONTAINING FE                                  
HETNAM     H4B 5,6,7,8-TETRAHYDROBIOPTERIN                                      
HETNAM     KLD 6-[2-(3-FLUORO-5-{2-[(2R,4S)-4-FLUORO-1-                         
HETNAM   2 KLD  METHYLPYRROLIDIN-2-YL]ETHYL}PHENYL)ETHYL]-4-                    
HETNAM   3 KLD  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    4(C9 H15 N5 O3)                                              
FORMUL   7  KLD    4(C21 H27 F2 N3)                                             
FORMUL   8  BTB    13(C8 H19 N O5)                                              
FORMUL  11   ZN    4(ZN 2+)                                                     
FORMUL  12  GOL    2(C3 H8 O3)                                                  
FORMUL  13   CL    4(CL 1-)                                                     
FORMUL  23   GD    2(GD)                                                        
FORMUL  42  HOH   *608(H2 O)                                                    
HELIX    1 AA1 THR A   83  ALA A   88  5                                   6    
HELIX    2 AA2 PRO A  120  ILE A  138  1                                  19    
HELIX    3 AA3 ALA A  145  GLY A  161  1                                  17    
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  GLN A  462  5                                  10    
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 SER B  359  THR B  364  1                                   6    
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  GLN B  462  5                                  10    
HELIX   37 AE1 LEU C   84  ALA C   88  5                                   5    
HELIX   38 AE2 PRO C  120  ILE C  138  1                                  19    
HELIX   39 AE3 ALA C  145  GLY C  161  1                                  17    
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 PHE C  323  GLY C  327  5                                   5    
HELIX   47 AF2 SER C  359  THR C  364  1                                   6    
HELIX   48 AF3 THR C  364  ASP C  369  1                                   6    
HELIX   49 AF4 ILE C  375  MET C  383  1                                   9    
HELIX   50 AF5 THR C  389  SER C  392  5                                   4    
HELIX   51 AF6 LEU C  393  LYS C  414  1                                  22    
HELIX   52 AF7 ASP C  419  GLY C  439  1                                  21    
HELIX   53 AF8 ASP C  444  VAL C  449  1                                   6    
HELIX   54 AF9 SER C  453  THR C  457  5                                   5    
HELIX   55 AG1 THR D   83  ALA D   88  5                                   6    
HELIX   56 AG2 PRO D  120  ILE D  138  1                                  19    
HELIX   57 AG3 SER D  143  GLY D  161  1                                  19    
HELIX   58 AG4 ARG D  166  ASN D  180  1                                  15    
HELIX   59 AG5 GLY D  186  TRP D  190  5                                   5    
HELIX   60 AG6 SER D  203  ASN D  220  1                                  18    
HELIX   61 AG7 ARG D  221  ASN D  223  5                                   3    
HELIX   62 AG8 ASN D  267  HIS D  277  1                                  11    
HELIX   63 AG9 PRO D  306  VAL D  310  5                                   5    
HELIX   64 AH1 LEU D  320  GLY D  327  5                                   8    
HELIX   65 AH2 MET D  358  THR D  364  1                                   7    
HELIX   66 AH3 THR D  364  ASP D  369  1                                   6    
HELIX   67 AH4 ILE D  375  MET D  383  1                                   9    
HELIX   68 AH5 THR D  389  SER D  392  5                                   4    
HELIX   69 AH6 LEU D  393  ALA D  413  1                                  21    
HELIX   70 AH7 ASP D  419  GLY D  439  1                                  21    
HELIX   71 AH8 ASP D  444  VAL D  449  1                                   6    
HELIX   72 AH9 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 ASN A 466  TYR A 467  0                                        
SHEET    2 AA8 2 ARG B  98  CYS B  99 -1  O  CYS B  99   N  ASN A 466           
SHEET    1 AA9 2 ARG B  70  LYS B  72  0                                        
SHEET    2 AA9 2 ILE B  79  TYR B  81 -1  O  THR B  80   N  VAL B  71           
SHEET    1 AB1 4 GLN B 194  ASP B 197  0                                        
SHEET    2 AB1 4 ALA B 227  VAL B 230  1  O  ILE B 228   N  PHE B 196           
SHEET    3 AB1 4 PHE B 353  SER B 354 -1  O  SER B 354   N  ALA B 227           
SHEET    4 AB1 4 ALA B 335  VAL B 336 -1  N  VAL B 336   O  PHE B 353           
SHEET    1 AB2 3 ARG B 242  ILE B 243  0                                        
SHEET    2 AB2 3 LEU B 291  GLN B 294 -1  O  GLN B 294   N  ARG B 242           
SHEET    3 AB2 3 GLU B 301  PHE B 303 -1  O  PHE B 303   N  LEU B 291           
SHEET    1 AB3 2 GLY B 253  ARG B 255  0                                        
SHEET    2 AB3 2 VAL B 261  GLY B 263 -1  O  ARG B 262   N  TYR B 254           
SHEET    1 AB4 2 GLU B 312  PRO B 314  0                                        
SHEET    2 AB4 2 ARG B 329  TYR B 331 -1  O  TRP B 330   N  VAL B 313           
SHEET    1 AB5 3 LEU B 346  PHE B 348  0                                        
SHEET    2 AB5 3 LEU B 340  ILE B 343 -1  N  LEU B 341   O  PHE B 348           
SHEET    3 AB5 3 ALA B 472  ARG B 474 -1  O  ALA B 472   N  GLU B 342           
SHEET    1 AB6 2 TYR B 357  MET B 358  0                                        
SHEET    2 AB6 2 ILE B 417  VAL B 418  1  O  VAL B 418   N  TYR B 357           
SHEET    1 AB7 2 ARG C  70  LYS C  72  0                                        
SHEET    2 AB7 2 ILE C  79  TYR C  81 -1  O  THR C  80   N  VAL C  71           
SHEET    1 AB8 4 GLN C 194  ASP C 197  0                                        
SHEET    2 AB8 4 ALA C 227  VAL C 230  1  O  ILE C 228   N  PHE C 196           
SHEET    3 AB8 4 PHE C 353  SER C 354 -1  O  SER C 354   N  ALA C 227           
SHEET    4 AB8 4 ALA C 335  VAL C 336 -1  N  VAL C 336   O  PHE C 353           
SHEET    1 AB9 3 ARG C 242  ILE C 243  0                                        
SHEET    2 AB9 3 LEU C 291  GLN C 294 -1  O  GLN C 294   N  ARG C 242           
SHEET    3 AB9 3 GLU C 301  PHE C 303 -1  O  PHE C 303   N  LEU C 291           
SHEET    1 AC1 2 GLY C 253  ARG C 255  0                                        
SHEET    2 AC1 2 VAL C 261  GLY C 263 -1  O  ARG C 262   N  TYR C 254           
SHEET    1 AC2 2 GLU C 312  PRO C 314  0                                        
SHEET    2 AC2 2 ARG C 329  TYR C 331 -1  O  TRP C 330   N  VAL C 313           
SHEET    1 AC3 3 LEU C 346  PHE C 348  0                                        
SHEET    2 AC3 3 LEU C 340  ILE C 343 -1  N  LEU C 341   O  PHE C 348           
SHEET    3 AC3 3 ALA C 472  ARG C 474 -1  O  ARG C 474   N  LEU C 340           
SHEET    1 AC4 2 TYR C 357  MET C 358  0                                        
SHEET    2 AC4 2 ILE C 417  VAL C 418  1  O  VAL C 418   N  TYR C 357           
SHEET    1 AC5 2 ARG D  70  LYS D  72  0                                        
SHEET    2 AC5 2 ILE D  79  TYR D  81 -1  O  THR D  80   N  VAL D  71           
SHEET    1 AC6 4 GLN D 194  ASP D 197  0                                        
SHEET    2 AC6 4 ALA D 227  VAL D 230  1  O  ILE D 228   N  PHE D 196           
SHEET    3 AC6 4 PHE D 353  SER D 354 -1  O  SER D 354   N  ALA D 227           
SHEET    4 AC6 4 ALA D 335  VAL D 336 -1  N  VAL D 336   O  PHE D 353           
SHEET    1 AC7 3 ARG D 242  ILE D 243  0                                        
SHEET    2 AC7 3 LEU D 291  GLN D 294 -1  O  GLN D 294   N  ARG D 242           
SHEET    3 AC7 3 GLU D 301  PHE D 303 -1  O  PHE D 303   N  LEU D 291           
SHEET    1 AC8 2 GLY D 253  ARG D 255  0                                        
SHEET    2 AC8 2 VAL D 261  GLY D 263 -1  O  ARG D 262   N  TYR D 254           
SHEET    1 AC9 2 GLU D 312  PRO D 314  0                                        
SHEET    2 AC9 2 ARG D 329  TYR D 331 -1  O  TRP D 330   N  VAL D 313           
SHEET    1 AD1 3 LEU D 346  PHE D 348  0                                        
SHEET    2 AD1 3 LEU D 340  ILE D 343 -1  N  LEU D 341   O  PHE D 348           
SHEET    3 AD1 3 ALA D 472  ARG D 474 -1  O  ARG D 474   N  LEU D 340           
LINK         SG  CYS A  94                ZN    ZN A 507     1555   1555  2.40  
LINK         SG  CYS A  99                ZN    ZN A 507     1555   1555  2.40  
LINK         SG  CYS A 184                FE   HEM A 501     1555   1555  2.28  
LINK         NE2 HIS A 461                ZN    ZN A 510     1555   1555  2.19  
LINK         SG  CYS B  94                ZN    ZN A 507     1555   1555  2.42  
LINK         SG  CYS B  99                ZN    ZN A 507     1555   1555  2.38  
LINK         SG  CYS B 184                FE   HEM B 501     1555   1555  2.32  
LINK         O   THR B 319                GD    GD B 508     1555   1555  2.52  
LINK         OE1 GLU B 321                GD    GD B 508     1555   1555  2.67  
LINK         OD1 ASP B 369                ZN    ZN A 510     1555   1555  2.05  
LINK         OD2 ASP B 369                ZN    ZN A 510     1555   1555  1.96  
LINK         SG  CYS C  94                ZN    ZN C 506     1555   1555  2.27  
LINK         SG  CYS C  99                ZN    ZN C 506     1555   1555  2.32  
LINK         SG  CYS C 184                FE   HEM C 501     1555   1555  2.32  
LINK         NE2 HIS C 461                ZN    ZN C 510     1555   1555  2.26  
LINK         SG  CYS D  94                ZN    ZN C 506     1555   1555  2.47  
LINK         SG  CYS D  99                ZN    ZN C 506     1555   1555  2.41  
LINK         SG  CYS D 184                FE   HEM D 501     1555   1555  2.28  
LINK         O   THR D 319                GD    GD D 506     1555   1555  2.49  
LINK         OE1 GLU D 321                GD    GD D 506     1555   1555  2.65  
LINK         OD1 ASP D 369                ZN    ZN C 510     1555   1555  2.25  
LINK         OD2 ASP D 369                ZN    ZN C 510     1555   1555  1.98  
LINK        ZN    ZN A 510                 O   HOH B 761     1555   1555  2.56  
LINK        ZN    ZN A 510                 O   HOH B 722     1555   1555  2.18  
LINK         O3  BTB B 504                GD    GD B 508     1555   1555  2.68  
LINK         O4  BTB B 504                GD    GD B 508     1555   1555  2.58  
LINK         N   BTB B 504                GD    GD B 508     1555   1555  2.69  
LINK         O6  BTB B 504                GD    GD B 508     1555   1555  2.81  
LINK         O8  BTB B 504                GD    GD B 508     1555   1555  2.73  
LINK        GD    GD B 508                 O   HOH B 749     1555   1555  2.59  
LINK        ZN    ZN C 510                 O   HOH C 685     1555   1555  2.36  
LINK        ZN    ZN C 510                 O   HOH D 751     1555   1555  2.25  
LINK         O3  BTB D 503                GD    GD D 506     1555   1555  2.68  
LINK         O4  BTB D 503                GD    GD D 506     1555   1555  2.45  
LINK         N   BTB D 503                GD    GD D 506     1555   1555  2.73  
LINK         O6  BTB D 503                GD    GD D 506     1555   1555  2.79  
LINK         O8  BTB D 503                GD    GD D 506     1555   1555  2.79  
LINK        GD    GD D 506                 O   HOH D 613     1555   1555  2.60  
LINK        GD    GD D 506                 O   HOH A 605     1555   1655  2.52  
CISPEP   1 SER A  470    PRO A  471          0        -0.92                     
CISPEP   2 SER B  470    PRO B  471          0         0.17                     
CISPEP   3 SER C  470    PRO C  471          0        -2.97                     
CISPEP   4 SER D  470    PRO D  471          0        -1.16                     
SITE     1 AC1 13 TRP A 178  ARG A 183  CYS A 184  SER A 226                    
SITE     2 AC1 13 PHE A 353  SER A 354  TRP A 356  GLU A 361                    
SITE     3 AC1 13 TRP A 447  PHE A 473  TYR A 475  H4B A 502                    
SITE     4 AC1 13 KLD A 503                                                     
SITE     1 AC2 14 SER A 102  VAL A 104  ARG A 365  ALA A 446                    
SITE     2 AC2 14 TRP A 447  HEM A 501  KLD A 503  HOH A 649                    
SITE     3 AC2 14 TRP B 445  PHE B 460  HIS B 461  GLN B 462                    
SITE     4 AC2 14 GLU B 463  HOH B 607                                          
SITE     1 AC3  9 VAL A 104  PHE A 105  GLY A 355  TRP A 356                    
SITE     2 AC3  9 TYR A 357  GLU A 361  TYR A 475  HEM A 501                    
SITE     3 AC3  9 H4B A 502                                                     
SITE     1 AC4  3 VAL A 381  CYS A 382  ASP A 384                               
SITE     1 AC5  3 GLU A 377  THR A 387  ASP D 384                               
SITE     1 AC6  1 GLU A 298                                                     
SITE     1 AC7  4 CYS A  94  CYS A  99  CYS B  94  CYS B  99                    
SITE     1 AC8  2 GLU A 167  HOH A 610                                          
SITE     1 AC9  3 GLN A 247  TYR A 357  ASN A 366                               
SITE     1 AD1  4 HIS A 461  ASP B 369  HOH B 722  HOH B 761                    
SITE     1 AD2  8 ASP A 384  LEU A 385  ARG A 388  HOH A 604                    
SITE     2 AD2  8 GLN C 257  VAL D 381  CYS D 382  ASP D 384                    
SITE     1 AD3 15 TRP B 178  ARG B 183  CYS B 184  VAL B 185                    
SITE     2 AD3 15 SER B 226  PHE B 353  SER B 354  TRP B 356                    
SITE     3 AD3 15 GLU B 361  ARG B 365  PHE B 473  TYR B 475                    
SITE     4 AD3 15 H4B B 502  KLD B 503  HOH B 613                               
SITE     1 AD4 12 TRP A 445  PHE A 460  HIS A 461  GLN A 462                    
SITE     2 AD4 12 GLU A 463  SER B 102  ALA B 446  TRP B 447                    
SITE     3 AD4 12 HEM B 501  KLD B 503  HOH B 673  HOH B 733                    
SITE     1 AD5 12 VAL B 104  PHE B 105  PRO B 334  GLY B 355                    
SITE     2 AD5 12 TRP B 356  TYR B 357  GLU B 361  ARG B 365                    
SITE     3 AD5 12 TYR B 475  HEM B 501  H4B B 502  HOH B 776                    
SITE     1 AD6  9 THR B 319  GLU B 321   GD B 508  HOH B 749                    
SITE     2 AD6  9 SER C 260  VAL C 261  TYR C 373  ASN C 374                    
SITE     3 AD6  9 ASP C 378                                                     
SITE     1 AD7  4 ASP B 297  GLU B 298  HOH B 635  GLU D 167                    
SITE     1 AD8  5 GLU B 377  ASP B 378  HOH B 603  HOH B 688                    
SITE     2 AD8  5 BTB C 504                                                     
SITE     1 AD9  6 GLN B 247  ARG B 250  TYR B 357  ARG B 365                    
SITE     2 AD9  6 ASN B 366  HOH B 670                                          
SITE     1 AE1  4 THR B 319  GLU B 321  BTB B 504  HOH B 749                    
SITE     1 AE2  4 ASP B 384  HOH B 630  GLU C 377  THR C 387                    
SITE     1 AE3 15 TRP C 178  ARG C 183  CYS C 184  VAL C 185                    
SITE     2 AE3 15 SER C 226  PHE C 353  SER C 354  GLY C 355                    
SITE     3 AE3 15 TRP C 356  MET C 358  TRP C 447  TYR C 475                    
SITE     4 AE3 15 H4B C 502  KLD C 503  HOH C 609                               
SITE     1 AE4 12 SER C 102  ARG C 365  ALA C 446  TRP C 447                    
SITE     2 AE4 12 HEM C 501  KLD C 503  HOH C 704  TRP D 445                    
SITE     3 AE4 12 PHE D 460  GLN D 462  GLU D 463  HOH D 614                    
SITE     1 AE5  8 PHE C 105  PRO C 334  GLY C 355  TRP C 356                    
SITE     2 AE5  8 GLU C 361  TYR C 475  HEM C 501  H4B C 502                    
SITE     1 AE6  4 ASP B 378  BTB B 506  CYS C 382  ASP C 384                    
SITE     1 AE7  1 GLU C 298                                                     
SITE     1 AE8  4 CYS C  94  CYS C  99  CYS D  94  CYS D  99                    
SITE     1 AE9  1 GLU C 167                                                     
SITE     1 AF1  4 GLN C 247  TYR C 357  ASN C 366  HOH C 673                    
SITE     1 AF2 15 TRP C 445  PHE C 460  HIS C 461  GLN C 462                    
SITE     2 AF2 15 GLU C 463  HOH C 631  HOH C 685  HOH C 700                    
SITE     3 AF2 15 HOH C 701  SER D 102  ALA D 446  TRP D 447                    
SITE     4 AF2 15 HEM D 501  KLD D 502  HOH D 671                               
SITE     1 AF3  5 HIS C 461  HOH C 685  HOH C 700  ASP D 369                    
SITE     2 AF3  5 HOH D 751                                                     
SITE     1 AF4 15 H4B C 509  TRP D 178  ARG D 183  CYS D 184                    
SITE     2 AF4 15 VAL D 185  SER D 226  PHE D 353  SER D 354                    
SITE     3 AF4 15 TRP D 356  MET D 358  GLU D 361  ARG D 365                    
SITE     4 AF4 15 PHE D 473  TYR D 475  KLD D 502                               
SITE     1 AF5 12 H4B C 509  VAL D 104  PHE D 105  VAL D 336                    
SITE     2 AF5 12 PHE D 353  TRP D 356  TYR D 357  GLU D 361                    
SITE     3 AF5 12 ARG D 365  TRP D 447  TYR D 475  HEM D 501                    
SITE     1 AF6  9 SER A 260  TYR A 373  ASN A 374  ASP A 378                    
SITE     2 AF6  9 HOH A 605  THR D 319  GLU D 321   GD D 506                    
SITE     3 AF6  9 HOH D 613                                                     
SITE     1 AF7  3 ASP D 297  GLU D 298  HOH D 601                               
SITE     1 AF8  2 GLU D 377  ASP D 378                                          
SITE     1 AF9  5 HOH A 605  THR D 319  GLU D 321  BTB D 503                    
SITE     2 AF9  5 HOH D 613                                                     
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 732                                          
CRYST1   59.528  152.760  108.980  90.00  90.76  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      0.016799  0.000000  0.000223        0.00000                         
SCALE2      0.000000  0.006546  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009177        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system