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Database: PDB
Entry: 4G45
LinkDB: 4G45
Original site: 4G45 
HEADER    OXIDOREDUCTASE/OXIDOREDUCTASE INHIBITOR 16-JUL-12   4G45              
TITLE     STRUCTURE OF CYTOCHROME CYP121 IN COMPLEX WITH 2-METHYLQUINOLIN-6-    
TITLE    2 AMINE                                                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CYTOCHROME P450 121;                                       
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: CYTOCHROME P450 MT2;                                        
COMPND   5 EC: 1.14.-.-;                                                        
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;                     
SOURCE   3 ORGANISM_TAXID: 1773;                                                
SOURCE   4 STRAIN: H37RV;                                                       
SOURCE   5 GENE: RV2276;                                                        
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    P450, OXIDOREDUCTASE-OXIDOREDUCTASE INHIBITOR COMPLEX                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.A.HUDSON,K.J.MCLEAN,S.SURADE,Y.-Q.YANG,D.LEYS,A.CIULLI,A.W.MUNRO,   
AUTHOR   2 C.ABELL                                                              
REVDAT   3   20-MAR-24 4G45    1       REMARK                                   
REVDAT   2   19-SEP-12 4G45    1       JRNL                                     
REVDAT   1   05-SEP-12 4G45    0                                                
JRNL        AUTH   S.A.HUDSON,K.J.MCLEAN,S.SURADE,Y.-Q.YANG,D.LEYS,A.CIULLI,    
JRNL        AUTH 2 A.W.MUNRO,C.ABELL                                            
JRNL        TITL   APPLICATION OF FRAGMENT SCREENING AND MERGING TO THE         
JRNL        TITL 2 DISCOVERY OF INHIBITORS OF THE MYCOBACTERIUM TUBERCULOSIS    
JRNL        TITL 3 CYTOCHROME P450 CYP121                                       
JRNL        REF    ANGEW.CHEM.INT.ED.ENGL.       V.  51  9311 2012              
JRNL        REFN                   ISSN 1433-7851                               
JRNL        PMID   22890978                                                     
JRNL        DOI    10.1002/ANIE.201202544                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.53 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.6.0117                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.53                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 36.87                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 69154                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.155                           
REMARK   3   R VALUE            (WORKING SET) : 0.153                           
REMARK   3   FREE R VALUE                     : 0.178                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3677                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.53                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.57                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 4382                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 96.07                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2020                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 208                          
REMARK   3   BIN FREE R VALUE                    : 0.2490                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2980                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 92                                      
REMARK   3   SOLVENT ATOMS            : 784                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 15.52                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.00000                                              
REMARK   3    B22 (A**2) : 0.00000                                              
REMARK   3    B33 (A**2) : 0.00000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.065         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.066         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.038         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.007         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.965                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.957                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3242 ; 0.030 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4442 ; 3.127 ; 2.020       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   393 ; 5.282 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   131 ;29.929 ;23.206       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   536 ;12.552 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    29 ;17.357 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   521 ; 0.179 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2423 ; 0.016 ; 0.022       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN USED IF PRESENT IN    
REMARK   3  THE INPUT                                                           
REMARK   4                                                                      
REMARK   4 4G45 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 26-JUL-12.                  
REMARK 100 THE DEPOSITION ID IS D_1000073714.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 02-FEB-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6                                  
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I02                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1                                  
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 2M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 69154                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.530                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 36.870                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS            
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 53.86                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.67                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 2M AMMONIUM SULPHATE, PH 6, VAPOR        
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 277K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65 2 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+1/6                                            
REMARK 290       6555   X-Y,X,Z+5/6                                             
REMARK 290       7555   Y,X,-Z+2/3                                              
REMARK 290       8555   X-Y,-Y,-Z                                               
REMARK 290       9555   -X,-X+Y,-Z+1/3                                          
REMARK 290      10555   -Y,-X,-Z+1/6                                            
REMARK 290      11555   -X+Y,Y,-Z+1/2                                           
REMARK 290      12555   X,X-Y,-Z+5/6                                            
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      176.20000            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       88.10000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      132.15000            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       44.05000            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000      220.25000            
REMARK 290   SMTRY1   7 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000      176.20000            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   9 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   9  0.000000  0.000000 -1.000000       88.10000            
REMARK 290   SMTRY1  10  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  10 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000       44.05000            
REMARK 290   SMTRY1  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  11  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000      132.15000            
REMARK 290   SMTRY1  12  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  12  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000      220.25000            
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: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2280 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 32260 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
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   BIOMT1   2  0.500000 -0.866025  0.000000        0.00000            
REMARK 350   BIOMT2   2 -0.866025 -0.500000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       44.05000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A 673  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 927  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 960  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A1113  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A1116  LIES ON A SPECIAL POSITION.                          
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     THR A   2    N    CA   CB   OG1  CG2                             
REMARK 470     ARG A  17    CZ   NH1  NH2                                       
REMARK 470     GLU A  24    CD   OE1  OE2                                       
REMARK 470     ARG A  28    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A  96    CE   NZ                                             
REMARK 470     LYS A 100    NZ                                                  
REMARK 470     LYS A 105    CG   CD   CE   NZ                                   
REMARK 470     GLU A 127    CD   OE1  OE2                                       
REMARK 470     LYS A 148    CE   NZ                                             
REMARK 470     LYS A 159    CD   CE   NZ                                        
REMARK 470     ARG A 162    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 184    CD   NE   CZ   NH1  NH2                             
REMARK 470     GLU A 261    CD   OE1  OE2                                       
REMARK 470     LYS A 262    CE   NZ                                             
REMARK 470     GLU A 317    CD   OE1  OE2                                       
REMARK 470     ARG A 353    CD   NE   CZ   NH1  NH2                             
REMARK 470     LYS A 364    CE   NZ                                             
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     ARG A  300   CG                                                  
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 A   643     O    HOH A   810              1.55            
REMARK 500   O    HOH A  1057     O    HOH A  1067              1.77            
REMARK 500   O    HOH A   828     O    HOH A  1077              1.83            
REMARK 500   OE2  GLU A   221     O    HOH A   847              1.88            
REMARK 500   O    HOH A   874     O    HOH A  1145              1.89            
REMARK 500   O    HOH A   606     O    HOH A  1098              1.90            
REMARK 500   O    HOH A   823     O    HOH A  1129              1.95            
REMARK 500   O    HOH A   988     O    HOH A  1091              1.95            
REMARK 500   O3   SO4 A   404     O    HOH A  1133              1.98            
REMARK 500   O    HOH A   666     O    HOH A  1160              2.01            
REMARK 500   O    HOH A  1022     O    HOH A  1230              2.02            
REMARK 500   O    HOH A   792     O    HOH A   833              2.02            
REMARK 500   O    HOH A   962     O    HOH A  1095              2.07            
REMARK 500   O    HOH A   850     O    HOH A  1170              2.11            
REMARK 500   O    HOH A  1051     O    HOH A  1203              2.11            
REMARK 500   O    HOH A   829     O    HOH A  1225              2.11            
REMARK 500   O    HOH A   797     O    HOH A  1155              2.13            
REMARK 500   OE2  GLU A   326     O    HOH A   849              2.15            
REMARK 500   O    HOH A  1017     O    HOH A  1023              2.17            
REMARK 500   O    HOH A  1206     O    HOH A  1242              2.17            
REMARK 500   O    HOH A   715     O    HOH A  1170              2.18            
REMARK 500   OD1  ASN A   197     O    HOH A  1150              2.18            
REMARK 500   O    HOH A   989     O    HOH A  1059              2.18            
REMARK 500   O    HOH A   763     O    HOH A  1227              2.19            
REMARK 500   O    HOH A   829     O    HOH A   965              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   CAF  MQN A   407     O    HOH A  1206     8555     1.82            
REMARK 500   O    HOH A   791     O    HOH A  1041    10555     1.91            
REMARK 500   O    HOH A  1073     O    HOH A  1073    10665     1.99            
REMARK 500   O    HOH A  1147     O    HOH A  1224     8555     2.09            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    HIS A 146   CG    HIS A 146   CD2     0.060                       
REMARK 500    TRP A 182   CE2   TRP A 182   CD2     0.089                       
REMARK 500    TRP A 182   CE3   TRP A 182   CZ3     0.123                       
REMARK 500    GLU A 221   CG    GLU A 221   CD      0.114                       
REMARK 500    HIS A 335   CG    HIS A 335   CD2     0.065                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG A  26   NE  -  CZ  -  NH2 ANGL. DEV. =   4.5 DEGREES          
REMARK 500    GLU A  29   OE1 -  CD  -  OE2 ANGL. DEV. =   8.4 DEGREES          
REMARK 500    ARG A  32   CD  -  NE  -  CZ  ANGL. DEV. =  16.3 DEGREES          
REMARK 500    ARG A  32   NE  -  CZ  -  NH1 ANGL. DEV. =  16.3 DEGREES          
REMARK 500    ARG A  32   NE  -  CZ  -  NH2 ANGL. DEV. = -10.3 DEGREES          
REMARK 500    ARG A  35   NE  -  CZ  -  NH1 ANGL. DEV. =   5.9 DEGREES          
REMARK 500    ARG A  35   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.1 DEGREES          
REMARK 500    GLU A  56   OE1 -  CD  -  OE2 ANGL. DEV. =   9.8 DEGREES          
REMARK 500    ASP A  57   CB  -  CG  -  OD2 ANGL. DEV. =  -6.5 DEGREES          
REMARK 500    ARG A 134   NE  -  CZ  -  NH1 ANGL. DEV. =   3.9 DEGREES          
REMARK 500    ASP A 139   CB  -  CG  -  OD2 ANGL. DEV. =  -5.7 DEGREES          
REMARK 500    ASP A 183   CB  -  CG  -  OD1 ANGL. DEV. =   6.2 DEGREES          
REMARK 500    ASP A 183   CB  -  CG  -  OD2 ANGL. DEV. =  -7.2 DEGREES          
REMARK 500    ARG A 208   CD  -  NE  -  CZ  ANGL. DEV. =   9.2 DEGREES          
REMARK 500    GLU A 221   OE1 -  CD  -  OE2 ANGL. DEV. =  -7.6 DEGREES          
REMARK 500    ARG A 256   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.3 DEGREES          
REMARK 500    ARG A 286   NE  -  CZ  -  NH1 ANGL. DEV. =   5.6 DEGREES          
REMARK 500    ARG A 286   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.9 DEGREES          
REMARK 500    ASP A 291   CB  -  CG  -  OD1 ANGL. DEV. =   6.5 DEGREES          
REMARK 500    ARG A 352   NE  -  CZ  -  NH1 ANGL. DEV. =  -4.4 DEGREES          
REMARK 500    ASP A 376   CB  -  CG  -  OD1 ANGL. DEV. =   6.4 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ALA A   3      146.00    -36.44                                   
REMARK 500    GLU A  29       74.61   -156.62                                   
REMARK 500    PHE A 137      -73.48   -141.86                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    ARG A  72         0.09    SIDE CHAIN                              
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                             HEM A 401  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 345   SG                                                     
REMARK 620 2 HEM A 401   NA   99.7                                              
REMARK 620 3 HEM A 401   NB   91.1  90.7                                        
REMARK 620 4 HEM A 401   NC   87.3 173.0  89.0                                  
REMARK 620 5 HEM A 401   ND   98.2  90.3 170.4  88.9                            
REMARK 620 6 MQN A 408   NAB 174.1  86.1  87.6  86.9  83.0                      
REMARK 620 N                    1     2     3     4     5                       
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 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 405                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 406                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MQN A 407                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MQN A 408                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4G44   RELATED DB: PDB                                   
REMARK 900 CYP121 WITH ANOTHER LEAD TARGET                                      
REMARK 900 RELATED ID: 4G46   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4G47   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4G48   RELATED DB: PDB                                   
DBREF  4G45 A    1   396  UNP    P0A514   CP121_MYCTU      1    396             
SEQRES   1 A  396  MET THR ALA THR VAL LEU LEU GLU VAL PRO PHE SER ALA          
SEQRES   2 A  396  ARG GLY ASP ARG ILE PRO ASP ALA VAL ALA GLU LEU ARG          
SEQRES   3 A  396  THR ARG GLU PRO ILE ARG LYS VAL ARG THR ILE THR GLY          
SEQRES   4 A  396  ALA GLU ALA TRP LEU VAL SER SER TYR ALA LEU CYS THR          
SEQRES   5 A  396  GLN VAL LEU GLU ASP ARG ARG PHE SER MET LYS GLU THR          
SEQRES   6 A  396  ALA ALA ALA GLY ALA PRO ARG LEU ASN ALA LEU THR VAL          
SEQRES   7 A  396  PRO PRO GLU VAL VAL ASN ASN MET GLY ASN ILE ALA ASP          
SEQRES   8 A  396  ALA GLY LEU ARG LYS ALA VAL MET LYS ALA ILE THR PRO          
SEQRES   9 A  396  LYS ALA PRO GLY LEU GLU GLN PHE LEU ARG ASP THR ALA          
SEQRES  10 A  396  ASN SER LEU LEU ASP ASN LEU ILE THR GLU GLY ALA PRO          
SEQRES  11 A  396  ALA ASP LEU ARG ASN ASP PHE ALA ASP PRO LEU ALA THR          
SEQRES  12 A  396  ALA LEU HIS CYS LYS VAL LEU GLY ILE PRO GLN GLU ASP          
SEQRES  13 A  396  GLY PRO LYS LEU PHE ARG SER LEU SER ILE ALA PHE MET          
SEQRES  14 A  396  SER SER ALA ASP PRO ILE PRO ALA ALA LYS ILE ASN TRP          
SEQRES  15 A  396  ASP ARG ASP ILE GLU TYR MET ALA GLY ILE LEU GLU ASN          
SEQRES  16 A  396  PRO ASN ILE THR THR GLY LEU MET GLY GLU LEU SER ARG          
SEQRES  17 A  396  LEU ARG LYS ASP PRO ALA TYR SER HIS VAL SER ASP GLU          
SEQRES  18 A  396  LEU PHE ALA THR ILE GLY VAL THR PHE PHE GLY ALA GLY          
SEQRES  19 A  396  VAL ILE SER THR GLY SER PHE LEU THR THR ALA LEU ILE          
SEQRES  20 A  396  SER LEU ILE GLN ARG PRO GLN LEU ARG ASN LEU LEU HIS          
SEQRES  21 A  396  GLU LYS PRO GLU LEU ILE PRO ALA GLY VAL GLU GLU LEU          
SEQRES  22 A  396  LEU ARG ILE ASN LEU SER PHE ALA ASP GLY LEU PRO ARG          
SEQRES  23 A  396  LEU ALA THR ALA ASP ILE GLN VAL GLY ASP VAL LEU VAL          
SEQRES  24 A  396  ARG LYS GLY GLU LEU VAL LEU VAL LEU LEU GLU GLY ALA          
SEQRES  25 A  396  ASN PHE ASP PRO GLU HIS PHE PRO ASN PRO GLY SER ILE          
SEQRES  26 A  396  GLU LEU ASP ARG PRO ASN PRO THR SER HIS LEU ALA PHE          
SEQRES  27 A  396  GLY ARG GLY GLN HIS PHE CYS PRO GLY SER ALA LEU GLY          
SEQRES  28 A  396  ARG ARG HIS ALA GLN ILE GLY ILE GLU ALA LEU LEU LYS          
SEQRES  29 A  396  LYS MET PRO GLY VAL ASP LEU ALA VAL PRO ILE ASP GLN          
SEQRES  30 A  396  LEU VAL TRP ARG THR ARG PHE GLN ARG ARG ILE PRO GLU          
SEQRES  31 A  396  ARG LEU PRO VAL LEU TRP                                      
HET    HEM  A 401      43                                                       
HET    SO4  A 402       5                                                       
HET    SO4  A 403       5                                                       
HET    SO4  A 404       5                                                       
HET    SO4  A 405       5                                                       
HET    SO4  A 406       5                                                       
HET    MQN  A 407      12                                                       
HET    MQN  A 408      12                                                       
HETNAM     HEM PROTOPORPHYRIN IX CONTAINING FE                                  
HETNAM     SO4 SULFATE ION                                                      
HETNAM     MQN 2-METHYLQUINOLIN-6-AMINE                                         
HETSYN     HEM HEME                                                             
FORMUL   2  HEM    C34 H32 FE N4 O4                                             
FORMUL   3  SO4    5(O4 S 2-)                                                   
FORMUL   8  MQN    2(C10 H10 N2)                                                
FORMUL  10  HOH   *784(H2 O)                                                    
HELIX    1   1 ASP A   20  GLU A   29  1                                  10    
HELIX    2   2 SER A   47  GLU A   56  1                                  10    
HELIX    3   3 MET A   62  ALA A   67  5                                   6    
HELIX    4   4 PRO A   79  VAL A   83  5                                   5    
HELIX    5   5 ASN A   84  ALA A   92  1                                   9    
HELIX    6   6 LEU A   94  ILE A  102  1                                   9    
HELIX    7   7 GLY A  108  GLY A  128  1                                  21    
HELIX    8   8 PHE A  137  GLY A  151  1                                  15    
HELIX    9   9 PRO A  153  GLU A  155  5                                   3    
HELIX   10  10 ASP A  156  SER A  163  1                                   8    
HELIX   11  11 SER A  163  PHE A  168  1                                   6    
HELIX   12  12 ILE A  175  GLU A  194  1                                  20    
HELIX   13  13 THR A  200  LYS A  211  1                                  12    
HELIX   14  14 ASP A  212  SER A  216  5                                   5    
HELIX   15  15 SER A  219  GLN A  251  1                                  33    
HELIX   16  16 ARG A  252  LYS A  262  1                                  11    
HELIX   17  17 LEU A  265  ILE A  276  1                                  12    
HELIX   18  18 LEU A  308  PHE A  314  1                                   7    
HELIX   19  19 ARG A  340  PHE A  344  5                                   5    
HELIX   20  20 GLY A  347  MET A  366  1                                  20    
HELIX   21  21 PRO A  374  LEU A  378  5                                   5    
SHEET    1   A 5 ILE A  31  ARG A  35  0                                        
SHEET    2   A 5 GLU A  41  VAL A  45 -1  O  LEU A  44   N  ARG A  32           
SHEET    3   A 5 LEU A 304  VAL A 307  1  O  LEU A 306   N  TRP A  43           
SHEET    4   A 5 LEU A 284  ALA A 288 -1  N  ARG A 286   O  VAL A 305           
SHEET    5   A 5 PHE A  60  SER A  61 -1  N  SER A  61   O  LEU A 287           
SHEET    1   B 3 ALA A 131  ASP A 132  0                                        
SHEET    2   B 3 PRO A 393  LEU A 395 -1  O  VAL A 394   N  ALA A 131           
SHEET    3   B 3 ASP A 370  LEU A 371 -1  N  ASP A 370   O  LEU A 395           
SHEET    1   C 2 ILE A 292  VAL A 294  0                                        
SHEET    2   C 2 VAL A 297  VAL A 299 -1  O  VAL A 297   N  VAL A 294           
LINK         SG  CYS A 345                FE   HEM A 401     1555   1555  2.23  
LINK        FE   HEM A 401                 NAB MQN A 408     1555   1555  2.32  
CISPEP   1 VAL A    9    PRO A   10          0        -1.00                     
CISPEP   2 ALA A  129    PRO A  130          0        -1.94                     
SITE     1 AC1 22 MET A  62  MET A  86  HIS A 146  PHE A 230                    
SITE     2 AC1 22 GLY A 234  SER A 237  PHE A 280  LEU A 284                    
SITE     3 AC1 22 ARG A 286  ALA A 337  PHE A 338  GLY A 339                    
SITE     4 AC1 22 HIS A 343  CYS A 345  PRO A 346  GLY A 347                    
SITE     5 AC1 22 MQN A 408  HOH A 549  HOH A 558  HOH A 602                    
SITE     6 AC1 22 HOH A 637  HOH A 787                                          
SITE     1 AC2  8 LYS A 211  PRO A 330  ASN A 331  PRO A 332                    
SITE     2 AC2  8 THR A 333  SER A 334  HOH A 668  HOH A 750                    
SITE     1 AC3  6 SER A  12  HOH A 692  HOH A 789  HOH A 843                    
SITE     2 AC3  6 HOH A 978  HOH A1172                                          
SITE     1 AC4  9 ARG A  58  SER A  61  MET A  62  LYS A  63                    
SITE     2 AC4  9 HIS A 343  HOH A 586  HOH A 609  HOH A 713                    
SITE     3 AC4  9 HOH A1133                                                     
SITE     1 AC5  8 ARG A  32  MQN A 407  HOH A 646  HOH A1016                    
SITE     2 AC5  8 HOH A1117  HOH A1169  HOH A1192  HOH A1206                    
SITE     1 AC6  7 LYS A  33  ARG A 300  MQN A 407  HOH A 781                    
SITE     2 AC6  7 HOH A 968  HOH A1168  HOH A1196                               
SITE     1 AC7 10 THR A   4  VAL A   5  LEU A   6  ARG A 300                    
SITE     2 AC7 10 LYS A 301  GLU A 303  SO4 A 405  SO4 A 406                    
SITE     3 AC7 10 HOH A1204  HOH A1206                                          
SITE     1 AC8  6 ALA A 233  SER A 237  ARG A 386  HEM A 401                    
SITE     2 AC8  6 HOH A 549  HOH A 707                                          
CRYST1   77.800   77.800  264.300  90.00  90.00 120.00 P 65 2 2     12          
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      0.012853  0.007421  0.000000        0.00000                         
SCALE2      0.000000  0.014842  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003784        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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