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Database: PDB
Entry: 4O1Q
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Original site: 4O1Q 
HEADER    OXIDOREDUCTASE                          16-DEC-13   4O1Q              
TITLE     CRYSTAL STRUCTURE OF THE Q103N-MAUG/PRE-METHYLAMINE DEHYDROGENASE     
TITLE    2 COMPLEX                                                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: METHYLAMINE UTILIZATION PROTEIN MAUG;                      
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: UNP RESIDUES 21-387;                                       
COMPND   5 EC: 1.-.-.-;                                                         
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES;                                                       
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: METHYLAMINE DEHYDROGENASE LIGHT CHAIN;                     
COMPND  10 CHAIN: C, E;                                                         
COMPND  11 FRAGMENT: UNP RESIDUES 58-188;                                       
COMPND  12 EC: 1.4.99.3;                                                        
COMPND  13 ENGINEERED: YES;                                                     
COMPND  14 MOL_ID: 3;                                                           
COMPND  15 MOLECULE: METHYLAMINE DEHYDROGENASE HEAVY CHAIN;                     
COMPND  16 CHAIN: D, F;                                                         
COMPND  17 FRAGMENT: UNP RESIDUES 33-417;                                       
COMPND  18 EC: 1.4.99.3;                                                        
COMPND  19 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: PARACOCCUS DENITRIFICANS;                       
SOURCE   3 ORGANISM_TAXID: 318586;                                              
SOURCE   4 STRAIN: PD 1222;                                                     
SOURCE   5 GENE: MAUG, PDEN_4736;                                               
SOURCE   6 EXPRESSION_SYSTEM: PARACOCCUS DENITRIFICANS;                         
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 266;                                        
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: PARACOCCUS DENITRIFICANS;                       
SOURCE  10 ORGANISM_TAXID: 318586;                                              
SOURCE  11 STRAIN: PD 1222;                                                     
SOURCE  12 GENE: PDEN_4733;                                                     
SOURCE  13 EXPRESSION_SYSTEM: RHODOBACTER SPHAEROIDES;                          
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 1063;                                       
SOURCE  15 MOL_ID: 3;                                                           
SOURCE  16 ORGANISM_SCIENTIFIC: PARACOCCUS DENITRIFICANS;                       
SOURCE  17 ORGANISM_TAXID: 318586;                                              
SOURCE  18 STRAIN: PD 1222;                                                     
SOURCE  19 GENE: PDEN_4730;                                                     
SOURCE  20 EXPRESSION_SYSTEM: RHODOBACTER SPHAEROIDES;                          
SOURCE  21 EXPRESSION_SYSTEM_TAXID: 1063                                        
KEYWDS    OXIDOREDUCTASE                                                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    E.T.YUKL,C.W.WILMOT                                                   
REVDAT   3   06-DEC-23 4O1Q    1       REMARK                                   
REVDAT   2   20-SEP-23 4O1Q    1       REMARK SEQADV LINK                       
REVDAT   1   30-APR-14 4O1Q    0                                                
JRNL        AUTH   S.SHIN,E.T.YUKL,E.SEHANOBISH,C.M.WILMOT,V.L.DAVIDSON         
JRNL        TITL   SITE-DIRECTED MUTAGENESIS OF GLN103 REVEALS THE INFLUENCE OF 
JRNL        TITL 2 THIS RESIDUE ON THE REDOX PROPERTIES AND STABILITY OF MAUG.  
JRNL        REF    BIOCHEMISTRY                  V.  53  1342 2014              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   24517455                                                     
JRNL        DOI    10.1021/BI5000349                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.59 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.7.0029                                      
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) : 2.59                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 44.49                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 50437                          
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) : 0.201                           
REMARK   3   R VALUE            (WORKING SET) : 0.198                           
REMARK   3   FREE R VALUE                     : 0.254                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2653                            
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) : 2.59                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.66                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3621                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 93.64                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3090                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 166                          
REMARK   3   BIN FREE R VALUE                    : 0.3670                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 13231                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 226                                     
REMARK   3   SOLVENT ATOMS            : 397                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 52.60                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -2.80000                                             
REMARK   3    B22 (A**2) : 4.28000                                              
REMARK   3    B33 (A**2) : -2.58000                                             
REMARK   3    B12 (A**2) : 1.05000                                              
REMARK   3    B13 (A**2) : -0.50000                                             
REMARK   3    B23 (A**2) : 2.30000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.354         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.306         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 29.950        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.941                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.899                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 13877 ; 0.005 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A): 12614 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 18973 ; 1.400 ; 1.976       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 29022 ; 0.763 ; 3.001       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1715 ; 5.680 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   670 ;33.860 ;23.791       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  2044 ;13.861 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):   106 ;14.377 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1991 ; 0.092 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 16081 ; 0.004 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  3245 ; 0.002 ; 0.020       
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  : 6                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     6        A   359                          
REMARK   3    RESIDUE RANGE :   A   401        A   403                          
REMARK   3    ORIGIN FOR THE GROUP (A):  21.7454  28.0068 -76.7039              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6191 T22:   0.2130                                     
REMARK   3      T33:   0.5418 T12:   0.1022                                     
REMARK   3      T13:   0.0529 T23:  -0.2999                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4530 L22:   0.7306                                     
REMARK   3      L33:   3.0347 L12:   0.3710                                     
REMARK   3      L13:  -0.4236 L23:  -0.6516                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0125 S12:   0.2048 S13:  -0.0934                       
REMARK   3      S21:  -0.0845 S22:   0.0288 S23:  -0.0295                       
REMARK   3      S31:   0.2569 S32:   0.1301 S33:  -0.0414                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B     6        B   360                          
REMARK   3    RESIDUE RANGE :   B   401        B   403                          
REMARK   3    ORIGIN FOR THE GROUP (A):  23.9776  29.2943  23.6824              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4069 T22:   0.1310                                     
REMARK   3      T33:   0.4109 T12:  -0.0277                                     
REMARK   3      T13:   0.1006 T23:  -0.2145                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9357 L22:   1.2891                                     
REMARK   3      L33:   3.0503 L12:   0.1678                                     
REMARK   3      L13:  -0.2203 L23:  -1.1955                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0104 S12:  -0.0619 S13:   0.0815                       
REMARK   3      S21:   0.1520 S22:  -0.0884 S23:   0.0085                       
REMARK   3      S31:  -0.1335 S32:   0.1766 S33:   0.0780                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C     7        C   131                          
REMARK   3    ORIGIN FOR THE GROUP (A):   0.9112  29.0634 -48.2312              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5034 T22:   0.1675                                     
REMARK   3      T33:   0.4369 T12:  -0.0409                                     
REMARK   3      T13:   0.0069 T23:  -0.1856                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4950 L22:   1.6686                                     
REMARK   3      L33:   3.2797 L12:  -0.0913                                     
REMARK   3      L13:   0.2964 L23:  -1.6801                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2147 S12:   0.2469 S13:  -0.2252                       
REMARK   3      S21:  -0.3646 S22:   0.1023 S23:   0.2375                       
REMARK   3      S31:   0.4776 S32:  -0.3161 S33:  -0.3170                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D    11        D   386                          
REMARK   3    ORIGIN FOR THE GROUP (A):   2.8294  10.1442 -30.3745              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6232 T22:   0.1422                                     
REMARK   3      T33:   0.5335 T12:  -0.1779                                     
REMARK   3      T13:  -0.0989 T23:  -0.1314                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4128 L22:   0.6816                                     
REMARK   3      L33:   2.0026 L12:  -0.0690                                     
REMARK   3      L13:   0.0409 L23:  -0.6996                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1044 S12:   0.0275 S13:  -0.2261                       
REMARK   3      S21:  -0.3044 S22:   0.1703 S23:   0.1298                       
REMARK   3      S31:   0.7729 S32:  -0.3525 S33:  -0.2747                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   E     7        E   131                          
REMARK   3    ORIGIN FOR THE GROUP (A):   2.4735  33.8094  -3.6189              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1692 T22:   0.1016                                     
REMARK   3      T33:   0.2607 T12:  -0.0372                                     
REMARK   3      T13:   0.0802 T23:  -0.1064                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7350 L22:   1.0959                                     
REMARK   3      L33:   1.1311 L12:  -0.3209                                     
REMARK   3      L13:  -0.1626 L23:  -0.5747                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0880 S12:  -0.1876 S13:  -0.0177                       
REMARK   3      S21:   0.0365 S22:   0.0809 S23:   0.1197                       
REMARK   3      S31:  -0.0272 S32:  -0.0999 S33:  -0.1688                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   F    11        F   386                          
REMARK   3    ORIGIN FOR THE GROUP (A):   7.8675  51.7638 -21.7693              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3310 T22:   0.1037                                     
REMARK   3      T33:   0.3845 T12:   0.0011                                     
REMARK   3      T13:   0.1222 T23:  -0.1731                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4828 L22:   0.7625                                     
REMARK   3      L33:   1.6569 L12:  -0.0369                                     
REMARK   3      L13:   0.0747 L23:  -0.2636                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0467 S12:  -0.0572 S13:   0.1029                       
REMARK   3      S21:   0.0108 S22:   0.0257 S23:   0.0348                       
REMARK   3      S31:  -0.2512 S32:  -0.1576 S33:  -0.0724                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH 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 ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 4O1Q COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-JAN-14.                  
REMARK 100 THE DEPOSITION ID IS D_1000083931.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-MAR-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.4                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 23-ID-B                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.03324                            
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL CRYO-COOLED         
REMARK 200                                   SI(111)                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 300 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 53091                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.590                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.6                               
REMARK 200  DATA REDUNDANCY                : 3.800                              
REMARK 200  R MERGE                    (I) : 0.11500                            
REMARK 200  R SYM                      (I) : 0.11500                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.3750                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.59                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.63                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.80                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.59900                            
REMARK 200  R SYM FOR SHELL            (I) : 0.59900                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.130                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS            
REMARK 200 SOFTWARE USED: REFMAC 5.7.0029                                       
REMARK 200 STARTING MODEL: PDB ENTRY 3L4M                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 45.95                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.28                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M MES, PH 6.4, 0.1 M SODIUM          
REMARK 280  ACETATE, 24-30% W/V PEG8000, VAPOR DIFFUSION, HANGING DROP,         
REMARK 280  TEMPERATURE 293K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,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                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXAMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 25700 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 58270 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -177.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F                      
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     HIS A    -5                                                      
REMARK 465     HIS A    -4                                                      
REMARK 465     HIS A    -3                                                      
REMARK 465     HIS A    -2                                                      
REMARK 465     HIS A    -1                                                      
REMARK 465     HIS A     0                                                      
REMARK 465     GLU A     1                                                      
REMARK 465     GLN A     2                                                      
REMARK 465     ALA A     3                                                      
REMARK 465     ARG A     4                                                      
REMARK 465     PRO A     5                                                      
REMARK 465     GLU A   360                                                      
REMARK 465     SER A   361                                                      
REMARK 465     ARG A   362                                                      
REMARK 465     ALA A   363                                                      
REMARK 465     ALA A   364                                                      
REMARK 465     GLN A   365                                                      
REMARK 465     LYS A   366                                                      
REMARK 465     ASP A   367                                                      
REMARK 465     HIS B    -5                                                      
REMARK 465     HIS B    -4                                                      
REMARK 465     HIS B    -3                                                      
REMARK 465     HIS B    -2                                                      
REMARK 465     HIS B    -1                                                      
REMARK 465     HIS B     0                                                      
REMARK 465     GLU B     1                                                      
REMARK 465     GLN B     2                                                      
REMARK 465     ALA B     3                                                      
REMARK 465     ARG B     4                                                      
REMARK 465     PRO B     5                                                      
REMARK 465     SER B   361                                                      
REMARK 465     ARG B   362                                                      
REMARK 465     ALA B   363                                                      
REMARK 465     ALA B   364                                                      
REMARK 465     GLN B   365                                                      
REMARK 465     LYS B   366                                                      
REMARK 465     ASP B   367                                                      
REMARK 465     HIS C    -5                                                      
REMARK 465     HIS C    -4                                                      
REMARK 465     HIS C    -3                                                      
REMARK 465     HIS C    -2                                                      
REMARK 465     HIS C    -1                                                      
REMARK 465     HIS C     0                                                      
REMARK 465     ALA C     1                                                      
REMARK 465     ASP C     2                                                      
REMARK 465     ALA C     3                                                      
REMARK 465     PRO C     4                                                      
REMARK 465     ALA C     5                                                      
REMARK 465     GLY C     6                                                      
REMARK 465     ASP D     2                                                      
REMARK 465     ALA D     3                                                      
REMARK 465     PRO D     4                                                      
REMARK 465     GLU D     5                                                      
REMARK 465     ALA D     6                                                      
REMARK 465     GLU D     7                                                      
REMARK 465     THR D     8                                                      
REMARK 465     GLN D     9                                                      
REMARK 465     ALA D    10                                                      
REMARK 465     HIS E    -5                                                      
REMARK 465     HIS E    -4                                                      
REMARK 465     HIS E    -3                                                      
REMARK 465     HIS E    -2                                                      
REMARK 465     HIS E    -1                                                      
REMARK 465     HIS E     0                                                      
REMARK 465     ALA E     1                                                      
REMARK 465     ASP E     2                                                      
REMARK 465     ALA E     3                                                      
REMARK 465     PRO E     4                                                      
REMARK 465     ALA E     5                                                      
REMARK 465     GLY E     6                                                      
REMARK 465     ASP F     2                                                      
REMARK 465     ALA F     3                                                      
REMARK 465     PRO F     4                                                      
REMARK 465     GLU F     5                                                      
REMARK 465     ALA F     6                                                      
REMARK 465     GLU F     7                                                      
REMARK 465     THR F     8                                                      
REMARK 465     GLN F     9                                                      
REMARK 465     ALA F    10                                                      
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    HIS A  35       70.78   -116.49                                   
REMARK 500    ARG A  39       61.10   -115.05                                   
REMARK 500    PHE A  92      146.34     81.16                                   
REMARK 500    GLU A 113     -114.72   -126.55                                   
REMARK 500    HIS A 205       44.24   -101.88                                   
REMARK 500    GLU A 232      -65.73    -24.42                                   
REMARK 500    ASN A 271        7.38     57.94                                   
REMARK 500    MET A 279      171.08     68.00                                   
REMARK 500    HIS B  35       73.54   -115.59                                   
REMARK 500    PHE B  92      154.13     88.40                                   
REMARK 500    GLU B 113     -112.72   -114.41                                   
REMARK 500    ASP B 257      104.22    -45.06                                   
REMARK 500    ASN B 271       14.39     58.46                                   
REMARK 500    MET B 279      171.16     75.45                                   
REMARK 500    LEU B 358       83.18    -64.02                                   
REMARK 500    ASP C  19      109.84   -166.22                                   
REMARK 500    HIS C  28       31.39    -92.36                                   
REMARK 500    THR C  91       47.38   -144.04                                   
REMARK 500    ARG C  99       74.54   -105.62                                   
REMARK 500    LEU D  80       58.79     37.08                                   
REMARK 500    ILE D 102      -80.31     63.13                                   
REMARK 500    ALA D 130       63.98     36.48                                   
REMARK 500    TRP D 140       32.98    -97.27                                   
REMARK 500    LYS D 173      -73.34    -95.57                                   
REMARK 500    PRO D 179     -165.51    -70.79                                   
REMARK 500    HIS D 183      159.60     61.76                                   
REMARK 500    PRO D 189        0.15    -65.24                                   
REMARK 500    ASP D 190       21.70   -151.41                                   
REMARK 500    TRP D 282      -90.73   -103.58                                   
REMARK 500    GLN D 283       80.55    -69.57                                   
REMARK 500    ASP D 384       73.86   -102.41                                   
REMARK 500    ASP E  17       52.31   -114.72                                   
REMARK 500    ASP E  19      116.07   -161.12                                   
REMARK 500    SER E  39       26.95   -140.80                                   
REMARK 500    THR E  91       44.16   -146.15                                   
REMARK 500    ARG E  99       72.49   -107.53                                   
REMARK 500    ILE F 102      -83.11     65.98                                   
REMARK 500    ALA F 130       64.10     36.66                                   
REMARK 500    LYS F 173      -74.71    -91.18                                   
REMARK 500    ASP F 180       72.68    -68.91                                   
REMARK 500    HIS F 183      163.10     66.42                                   
REMARK 500    THR F 187      -54.57   -123.16                                   
REMARK 500    TRP F 282      -95.15   -102.72                                   
REMARK 500    GLN F 283       84.27    -69.84                                   
REMARK 500    ARG F 305       45.89   -108.90                                   
REMARK 500    LEU F 373       58.12    -96.22                                   
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                             HEC A 402  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  35   NE2                                                    
REMARK 620 2 HEC A 402   NA   87.7                                              
REMARK 620 3 HEC A 402   NB   90.5  89.4                                        
REMARK 620 4 HEC A 402   NC   94.9 177.4  90.3                                  
REMARK 620 5 HEC A 402   ND   92.4  90.5 177.1  89.6                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 401  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN A  66   OD1                                                    
REMARK 620 2 THR A 275   O   135.9                                              
REMARK 620 3 PRO A 277   O    83.4  83.6                                        
REMARK 620 4 HOH A 534   O    90.6  90.1 163.4                                  
REMARK 620 5 HOH A 550   O    77.0 144.8  90.1 103.7                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEC A 403  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 205   NE2                                                    
REMARK 620 2 HEC A 403   NA   87.5                                              
REMARK 620 3 HEC A 403   NB   91.2  90.5                                        
REMARK 620 4 HEC A 403   NC   90.3 177.8  89.5                                  
REMARK 620 5 HEC A 403   ND   86.5  90.3 177.5  89.5                            
REMARK 620 6 TYR A 294   OH  165.3  95.1 103.2  87.1  79.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEC B 402  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B  35   NE2                                                    
REMARK 620 2 HEC B 402   NA   88.8                                              
REMARK 620 3 HEC B 402   NB   94.2  89.8                                        
REMARK 620 4 HEC B 402   NC   94.0 177.1  90.2                                  
REMARK 620 5 HEC B 402   ND   88.9  90.1 177.0  89.7                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B 401  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN B  66   OD1                                                    
REMARK 620 2 THR B 275   O   131.3                                              
REMARK 620 3 PRO B 277   O    91.2 100.5                                        
REMARK 620 4 HOH B 542   O    84.8  81.9 175.9                                  
REMARK 620 5 HOH B 548   O   140.9  77.6 110.7  72.9                            
REMARK 620 6 HOH B 551   O    70.8 156.4  85.0  94.1  79.0                      
REMARK 620 7 HOH B 584   O    72.0  60.1  94.7  83.6 134.1 142.9                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEC B 403  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B 205   NE2                                                    
REMARK 620 2 HEC B 403   NA   87.8                                              
REMARK 620 3 HEC B 403   NB   94.3  90.3                                        
REMARK 620 4 HEC B 403   NC   90.1 177.9  89.6                                  
REMARK 620 5 HEC B 403   ND   83.5  89.9 177.8  90.1                            
REMARK 620 6 TYR B 294   OH  163.8  88.8 101.6  93.4  80.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA F 402  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP F 253   O                                                      
REMARK 620 2 ASP F 253   OD2  83.1                                              
REMARK 620 3 SER F 256   OG  138.8 136.0                                        
REMARK 620 4 ASP F 258   O    70.2 153.3  69.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEC A 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEC A 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 405                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEC B 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEC B 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 405                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGE C 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MES D 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MES F 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA F 402                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3L4M   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE WT MAUG/PRE-METHYLAMINE DEHYDROGENASE       
REMARK 900 COMPLEX                                                              
DBREF  4O1Q A    1   367  UNP    Q51658   MAUG_PARDP      21    387             
DBREF  4O1Q B    1   367  UNP    Q51658   MAUG_PARDP      21    387             
DBREF  4O1Q C    1   131  UNP    A1BBA0   A1BBA0_PARDP    58    188             
DBREF  4O1Q D    2   386  UNP    A1BB97   A1BB97_PARDP    33    417             
DBREF  4O1Q E    1   131  UNP    A1BBA0   A1BBA0_PARDP    58    188             
DBREF  4O1Q F    2   386  UNP    A1BB97   A1BB97_PARDP    33    417             
SEQADV 4O1Q HIS A   -5  UNP  Q51658              EXPRESSION TAG                 
SEQADV 4O1Q HIS A   -4  UNP  Q51658              EXPRESSION TAG                 
SEQADV 4O1Q HIS A   -3  UNP  Q51658              EXPRESSION TAG                 
SEQADV 4O1Q HIS A   -2  UNP  Q51658              EXPRESSION TAG                 
SEQADV 4O1Q HIS A   -1  UNP  Q51658              EXPRESSION TAG                 
SEQADV 4O1Q HIS A    0  UNP  Q51658              EXPRESSION TAG                 
SEQADV 4O1Q ASN A  103  UNP  Q51658    GLN   123 ENGINEERED MUTATION            
SEQADV 4O1Q HIS B   -5  UNP  Q51658              EXPRESSION TAG                 
SEQADV 4O1Q HIS B   -4  UNP  Q51658              EXPRESSION TAG                 
SEQADV 4O1Q HIS B   -3  UNP  Q51658              EXPRESSION TAG                 
SEQADV 4O1Q HIS B   -2  UNP  Q51658              EXPRESSION TAG                 
SEQADV 4O1Q HIS B   -1  UNP  Q51658              EXPRESSION TAG                 
SEQADV 4O1Q HIS B    0  UNP  Q51658              EXPRESSION TAG                 
SEQADV 4O1Q ASN B  103  UNP  Q51658    GLN   123 ENGINEERED MUTATION            
SEQADV 4O1Q HIS C   -5  UNP  A1BBA0              EXPRESSION TAG                 
SEQADV 4O1Q HIS C   -4  UNP  A1BBA0              EXPRESSION TAG                 
SEQADV 4O1Q HIS C   -3  UNP  A1BBA0              EXPRESSION TAG                 
SEQADV 4O1Q HIS C   -2  UNP  A1BBA0              EXPRESSION TAG                 
SEQADV 4O1Q HIS C   -1  UNP  A1BBA0              EXPRESSION TAG                 
SEQADV 4O1Q HIS C    0  UNP  A1BBA0              EXPRESSION TAG                 
SEQADV 4O1Q HIS E   -5  UNP  A1BBA0              EXPRESSION TAG                 
SEQADV 4O1Q HIS E   -4  UNP  A1BBA0              EXPRESSION TAG                 
SEQADV 4O1Q HIS E   -3  UNP  A1BBA0              EXPRESSION TAG                 
SEQADV 4O1Q HIS E   -2  UNP  A1BBA0              EXPRESSION TAG                 
SEQADV 4O1Q HIS E   -1  UNP  A1BBA0              EXPRESSION TAG                 
SEQADV 4O1Q HIS E    0  UNP  A1BBA0              EXPRESSION TAG                 
SEQRES   1 A  373  HIS HIS HIS HIS HIS HIS GLU GLN ALA ARG PRO ALA ASP          
SEQRES   2 A  373  ASP ALA LEU ALA ALA LEU GLY ALA GLN LEU PHE VAL ASP          
SEQRES   3 A  373  PRO ALA LEU SER ARG ASN ALA THR GLN SER CYS ALA THR          
SEQRES   4 A  373  CYS HIS ASP PRO ALA ARG ALA PHE THR ASP PRO ARG GLU          
SEQRES   5 A  373  GLY LYS ALA GLY LEU ALA VAL SER VAL GLY ASP ASP GLY          
SEQRES   6 A  373  GLN SER HIS GLY ASP ARG ASN THR PRO THR LEU GLY TYR          
SEQRES   7 A  373  ALA ALA LEU VAL PRO ALA PHE HIS ARG ASP ALA ASN GLY          
SEQRES   8 A  373  LYS TYR LYS GLY GLY GLN PHE TRP ASP GLY ARG ALA ASP          
SEQRES   9 A  373  ASP LEU LYS GLN ASN ALA GLY GLN PRO MET LEU ASN PRO          
SEQRES  10 A  373  VAL GLU MET ALA MET PRO ASP ARG ALA ALA VAL ALA ALA          
SEQRES  11 A  373  ARG LEU ARG ASP ASP PRO ALA TYR ARG THR GLY PHE GLU          
SEQRES  12 A  373  ALA LEU PHE GLY LYS GLY VAL LEU ASP ASP PRO GLU ARG          
SEQRES  13 A  373  ALA PHE ASP ALA ALA ALA GLU ALA LEU ALA ALA TYR GLN          
SEQRES  14 A  373  ALA THR GLY GLU PHE SER PRO PHE ASP SER LYS TYR ASP          
SEQRES  15 A  373  ARG VAL MET ARG GLY GLU GLU LYS PHE THR PRO LEU GLU          
SEQRES  16 A  373  GLU PHE GLY TYR THR VAL PHE ILE THR TRP ASN CYS ARG          
SEQRES  17 A  373  LEU CYS HIS MET GLN ARG LYS GLN GLY VAL ALA GLU ARG          
SEQRES  18 A  373  GLU THR PHE THR ASN PHE GLU TYR HIS ASN ILE GLY LEU          
SEQRES  19 A  373  PRO VAL ASN GLU THR ALA ARG GLU ALA SER GLY LEU GLY          
SEQRES  20 A  373  ALA ASP HIS VAL ASP HIS GLY LEU LEU ALA ARG PRO GLY          
SEQRES  21 A  373  ILE GLU ASP PRO ALA GLN SER GLY ARG PHE LYS VAL PRO          
SEQRES  22 A  373  SER LEU ARG ASN VAL ALA VAL THR GLY PRO TYR MET HIS          
SEQRES  23 A  373  ASN GLY VAL PHE THR ASP LEU ARG THR ALA ILE LEU PHE          
SEQRES  24 A  373  TYR ASN LYS TYR THR SER ARG ARG PRO GLU ALA LYS ILE          
SEQRES  25 A  373  ASN PRO GLU THR GLY ALA PRO TRP GLY GLU PRO GLU VAL          
SEQRES  26 A  373  ALA ARG ASN LEU SER LEU ALA GLU LEU GLN SER GLY LEU          
SEQRES  27 A  373  MET LEU ASP ASP GLY ARG VAL ASP ALA LEU VAL ALA PHE          
SEQRES  28 A  373  LEU GLU THR LEU THR ASP ARG ARG TYR GLU PRO LEU LEU          
SEQRES  29 A  373  GLU GLU SER ARG ALA ALA GLN LYS ASP                          
SEQRES   1 B  373  HIS HIS HIS HIS HIS HIS GLU GLN ALA ARG PRO ALA ASP          
SEQRES   2 B  373  ASP ALA LEU ALA ALA LEU GLY ALA GLN LEU PHE VAL ASP          
SEQRES   3 B  373  PRO ALA LEU SER ARG ASN ALA THR GLN SER CYS ALA THR          
SEQRES   4 B  373  CYS HIS ASP PRO ALA ARG ALA PHE THR ASP PRO ARG GLU          
SEQRES   5 B  373  GLY LYS ALA GLY LEU ALA VAL SER VAL GLY ASP ASP GLY          
SEQRES   6 B  373  GLN SER HIS GLY ASP ARG ASN THR PRO THR LEU GLY TYR          
SEQRES   7 B  373  ALA ALA LEU VAL PRO ALA PHE HIS ARG ASP ALA ASN GLY          
SEQRES   8 B  373  LYS TYR LYS GLY GLY GLN PHE TRP ASP GLY ARG ALA ASP          
SEQRES   9 B  373  ASP LEU LYS GLN ASN ALA GLY GLN PRO MET LEU ASN PRO          
SEQRES  10 B  373  VAL GLU MET ALA MET PRO ASP ARG ALA ALA VAL ALA ALA          
SEQRES  11 B  373  ARG LEU ARG ASP ASP PRO ALA TYR ARG THR GLY PHE GLU          
SEQRES  12 B  373  ALA LEU PHE GLY LYS GLY VAL LEU ASP ASP PRO GLU ARG          
SEQRES  13 B  373  ALA PHE ASP ALA ALA ALA GLU ALA LEU ALA ALA TYR GLN          
SEQRES  14 B  373  ALA THR GLY GLU PHE SER PRO PHE ASP SER LYS TYR ASP          
SEQRES  15 B  373  ARG VAL MET ARG GLY GLU GLU LYS PHE THR PRO LEU GLU          
SEQRES  16 B  373  GLU PHE GLY TYR THR VAL PHE ILE THR TRP ASN CYS ARG          
SEQRES  17 B  373  LEU CYS HIS MET GLN ARG LYS GLN GLY VAL ALA GLU ARG          
SEQRES  18 B  373  GLU THR PHE THR ASN PHE GLU TYR HIS ASN ILE GLY LEU          
SEQRES  19 B  373  PRO VAL ASN GLU THR ALA ARG GLU ALA SER GLY LEU GLY          
SEQRES  20 B  373  ALA ASP HIS VAL ASP HIS GLY LEU LEU ALA ARG PRO GLY          
SEQRES  21 B  373  ILE GLU ASP PRO ALA GLN SER GLY ARG PHE LYS VAL PRO          
SEQRES  22 B  373  SER LEU ARG ASN VAL ALA VAL THR GLY PRO TYR MET HIS          
SEQRES  23 B  373  ASN GLY VAL PHE THR ASP LEU ARG THR ALA ILE LEU PHE          
SEQRES  24 B  373  TYR ASN LYS TYR THR SER ARG ARG PRO GLU ALA LYS ILE          
SEQRES  25 B  373  ASN PRO GLU THR GLY ALA PRO TRP GLY GLU PRO GLU VAL          
SEQRES  26 B  373  ALA ARG ASN LEU SER LEU ALA GLU LEU GLN SER GLY LEU          
SEQRES  27 B  373  MET LEU ASP ASP GLY ARG VAL ASP ALA LEU VAL ALA PHE          
SEQRES  28 B  373  LEU GLU THR LEU THR ASP ARG ARG TYR GLU PRO LEU LEU          
SEQRES  29 B  373  GLU GLU SER ARG ALA ALA GLN LYS ASP                          
SEQRES   1 C  137  HIS HIS HIS HIS HIS HIS ALA ASP ALA PRO ALA GLY THR          
SEQRES   2 C  137  ASP PRO ARG ALA LYS TRP VAL PRO GLN ASP ASN ASP ILE          
SEQRES   3 C  137  GLN ALA CYS ASP TYR TRP ARG HIS CYS SER ILE ASP GLY          
SEQRES   4 C  137  ASN ILE CYS ASP CYS SER GLY GLY SER LEU THR ASN CYS          
SEQRES   5 C  137  PRO PRO GLY THR LYS LEU ALA THR ALA SER 0AF VAL ALA          
SEQRES   6 C  137  SER CYS TYR ASN PRO THR ASP GLY GLN SER TYR LEU ILE          
SEQRES   7 C  137  ALA TYR ARG ASP CYS CYS GLY TYR ASN VAL SER GLY ARG          
SEQRES   8 C  137  CYS PRO CYS LEU ASN THR GLU GLY GLU LEU PRO VAL TYR          
SEQRES   9 C  137  ARG PRO GLU PHE ALA ASN ASP ILE ILE TRP CYS PHE GLY          
SEQRES  10 C  137  ALA GLU ASP ASP ALA MET THR TYR HIS CYS THR ILE SER          
SEQRES  11 C  137  PRO ILE VAL GLY LYS ALA SER                                  
SEQRES   1 D  385  ASP ALA PRO GLU ALA GLU THR GLN ALA GLN GLU THR GLN          
SEQRES   2 D  385  GLY GLN ALA ALA ALA ARG ALA ALA ALA ALA ASP LEU ALA          
SEQRES   3 D  385  ALA GLY GLN ASP ASP GLU PRO ARG ILE LEU GLU ALA PRO          
SEQRES   4 D  385  ALA PRO ASP ALA ARG ARG VAL TYR VAL ASN ASP PRO ALA          
SEQRES   5 D  385  HIS PHE ALA ALA VAL THR GLN GLN PHE VAL ILE ASP GLY          
SEQRES   6 D  385  GLU ALA GLY ARG VAL ILE GLY MET ILE ASP GLY GLY PHE          
SEQRES   7 D  385  LEU PRO ASN PRO VAL VAL ALA ASP ASP GLY SER PHE ILE          
SEQRES   8 D  385  ALA HIS ALA SER THR VAL PHE SER ARG ILE ALA ARG GLY          
SEQRES   9 D  385  GLU ARG THR ASP TYR VAL GLU VAL PHE ASP PRO VAL THR          
SEQRES  10 D  385  LEU LEU PRO THR ALA ASP ILE GLU LEU PRO ASP ALA PRO          
SEQRES  11 D  385  ARG PHE LEU VAL GLY THR TYR PRO TRP MET THR SER LEU          
SEQRES  12 D  385  THR PRO ASP GLY LYS THR LEU LEU PHE TYR GLN PHE SER          
SEQRES  13 D  385  PRO ALA PRO ALA VAL GLY VAL VAL ASP LEU GLU GLY LYS          
SEQRES  14 D  385  ALA PHE LYS ARG MET LEU ASP VAL PRO ASP CYS TYR HIS          
SEQRES  15 D  385  ILE PHE PRO THR ALA PRO ASP THR PHE PHE MET HIS CYS          
SEQRES  16 D  385  ARG ASP GLY SER LEU ALA LYS VAL ALA PHE GLY THR GLU          
SEQRES  17 D  385  GLY THR PRO GLU ILE THR HIS THR GLU VAL PHE HIS PRO          
SEQRES  18 D  385  GLU ASP GLU PHE LEU ILE ASN HIS PRO ALA TYR SER GLN          
SEQRES  19 D  385  LYS ALA GLY ARG LEU VAL TRP PRO THR TYR THR GLY LYS          
SEQRES  20 D  385  ILE HIS GLN ILE ASP LEU SER SER GLY ASP ALA LYS PHE          
SEQRES  21 D  385  LEU PRO ALA VAL GLU ALA LEU THR GLU ALA GLU ARG ALA          
SEQRES  22 D  385  ASP GLY TRP ARG PRO GLY GLY TRP GLN GLN VAL ALA TYR          
SEQRES  23 D  385  HIS ARG ALA LEU ASP ARG ILE TYR LEU LEU VAL ASP GLN          
SEQRES  24 D  385  ARG ASP GLU TRP ARG HIS LYS THR ALA SER ARG PHE VAL          
SEQRES  25 D  385  VAL VAL LEU ASP ALA LYS THR GLY GLU ARG LEU ALA LYS          
SEQRES  26 D  385  PHE GLU MET GLY HIS GLU ILE ASP SER ILE ASN VAL SER          
SEQRES  27 D  385  GLN ASP GLU LYS PRO LEU LEU TYR ALA LEU SER THR GLY          
SEQRES  28 D  385  ASP LYS THR LEU TYR ILE HIS ASP ALA GLU SER GLY GLU          
SEQRES  29 D  385  GLU LEU ARG SER VAL ASN GLN LEU GLY HIS GLY PRO GLN          
SEQRES  30 D  385  VAL ILE THR THR ALA ASP MET GLY                              
SEQRES   1 E  137  HIS HIS HIS HIS HIS HIS ALA ASP ALA PRO ALA GLY THR          
SEQRES   2 E  137  ASP PRO ARG ALA LYS TRP VAL PRO GLN ASP ASN ASP ILE          
SEQRES   3 E  137  GLN ALA CYS ASP TYR TRP ARG HIS CYS SER ILE ASP GLY          
SEQRES   4 E  137  ASN ILE CYS ASP CYS SER GLY GLY SER LEU THR ASN CYS          
SEQRES   5 E  137  PRO PRO GLY THR LYS LEU ALA THR ALA SER 0AF VAL ALA          
SEQRES   6 E  137  SER CYS TYR ASN PRO THR ASP GLY GLN SER TYR LEU ILE          
SEQRES   7 E  137  ALA TYR ARG ASP CYS CYS GLY TYR ASN VAL SER GLY ARG          
SEQRES   8 E  137  CYS PRO CYS LEU ASN THR GLU GLY GLU LEU PRO VAL TYR          
SEQRES   9 E  137  ARG PRO GLU PHE ALA ASN ASP ILE ILE TRP CYS PHE GLY          
SEQRES  10 E  137  ALA GLU ASP ASP ALA MET THR TYR HIS CYS THR ILE SER          
SEQRES  11 E  137  PRO ILE VAL GLY LYS ALA SER                                  
SEQRES   1 F  385  ASP ALA PRO GLU ALA GLU THR GLN ALA GLN GLU THR GLN          
SEQRES   2 F  385  GLY GLN ALA ALA ALA ARG ALA ALA ALA ALA ASP LEU ALA          
SEQRES   3 F  385  ALA GLY GLN ASP ASP GLU PRO ARG ILE LEU GLU ALA PRO          
SEQRES   4 F  385  ALA PRO ASP ALA ARG ARG VAL TYR VAL ASN ASP PRO ALA          
SEQRES   5 F  385  HIS PHE ALA ALA VAL THR GLN GLN PHE VAL ILE ASP GLY          
SEQRES   6 F  385  GLU ALA GLY ARG VAL ILE GLY MET ILE ASP GLY GLY PHE          
SEQRES   7 F  385  LEU PRO ASN PRO VAL VAL ALA ASP ASP GLY SER PHE ILE          
SEQRES   8 F  385  ALA HIS ALA SER THR VAL PHE SER ARG ILE ALA ARG GLY          
SEQRES   9 F  385  GLU ARG THR ASP TYR VAL GLU VAL PHE ASP PRO VAL THR          
SEQRES  10 F  385  LEU LEU PRO THR ALA ASP ILE GLU LEU PRO ASP ALA PRO          
SEQRES  11 F  385  ARG PHE LEU VAL GLY THR TYR PRO TRP MET THR SER LEU          
SEQRES  12 F  385  THR PRO ASP GLY LYS THR LEU LEU PHE TYR GLN PHE SER          
SEQRES  13 F  385  PRO ALA PRO ALA VAL GLY VAL VAL ASP LEU GLU GLY LYS          
SEQRES  14 F  385  ALA PHE LYS ARG MET LEU ASP VAL PRO ASP CYS TYR HIS          
SEQRES  15 F  385  ILE PHE PRO THR ALA PRO ASP THR PHE PHE MET HIS CYS          
SEQRES  16 F  385  ARG ASP GLY SER LEU ALA LYS VAL ALA PHE GLY THR GLU          
SEQRES  17 F  385  GLY THR PRO GLU ILE THR HIS THR GLU VAL PHE HIS PRO          
SEQRES  18 F  385  GLU ASP GLU PHE LEU ILE ASN HIS PRO ALA TYR SER GLN          
SEQRES  19 F  385  LYS ALA GLY ARG LEU VAL TRP PRO THR TYR THR GLY LYS          
SEQRES  20 F  385  ILE HIS GLN ILE ASP LEU SER SER GLY ASP ALA LYS PHE          
SEQRES  21 F  385  LEU PRO ALA VAL GLU ALA LEU THR GLU ALA GLU ARG ALA          
SEQRES  22 F  385  ASP GLY TRP ARG PRO GLY GLY TRP GLN GLN VAL ALA TYR          
SEQRES  23 F  385  HIS ARG ALA LEU ASP ARG ILE TYR LEU LEU VAL ASP GLN          
SEQRES  24 F  385  ARG ASP GLU TRP ARG HIS LYS THR ALA SER ARG PHE VAL          
SEQRES  25 F  385  VAL VAL LEU ASP ALA LYS THR GLY GLU ARG LEU ALA LYS          
SEQRES  26 F  385  PHE GLU MET GLY HIS GLU ILE ASP SER ILE ASN VAL SER          
SEQRES  27 F  385  GLN ASP GLU LYS PRO LEU LEU TYR ALA LEU SER THR GLY          
SEQRES  28 F  385  ASP LYS THR LEU TYR ILE HIS ASP ALA GLU SER GLY GLU          
SEQRES  29 F  385  GLU LEU ARG SER VAL ASN GLN LEU GLY HIS GLY PRO GLN          
SEQRES  30 F  385  VAL ILE THR THR ALA ASP MET GLY                              
MODRES 4O1Q 0AF C   57  TRP  7-HYDROXY-L-TRYPTOPHAN                             
MODRES 4O1Q 0AF E   57  TRP  7-HYDROXY-L-TRYPTOPHAN                             
HET    0AF  C  57      15                                                       
HET    0AF  E  57      15                                                       
HET     CA  A 401       1                                                       
HET    HEC  A 402      43                                                       
HET    HEC  A 403      43                                                       
HET    EDO  A 404       4                                                       
HET    EDO  A 405       4                                                       
HET     CA  B 401       1                                                       
HET    HEC  B 402      43                                                       
HET    HEC  B 403      43                                                       
HET    EDO  B 404       4                                                       
HET    PO4  B 405       5                                                       
HET    PGE  C 201      10                                                       
HET    MES  D 401      12                                                       
HET    MES  F 401      12                                                       
HET     NA  F 402       1                                                       
HETNAM     0AF 7-HYDROXY-L-TRYPTOPHAN                                           
HETNAM      CA CALCIUM ION                                                      
HETNAM     HEC HEME C                                                           
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETNAM     PO4 PHOSPHATE ION                                                    
HETNAM     PGE TRIETHYLENE GLYCOL                                               
HETNAM     MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID                             
HETNAM      NA SODIUM ION                                                       
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   3  0AF    2(C11 H12 N2 O3)                                             
FORMUL   7   CA    2(CA 2+)                                                     
FORMUL   8  HEC    4(C34 H34 FE N4 O4)                                          
FORMUL  10  EDO    3(C2 H6 O2)                                                  
FORMUL  16  PO4    O4 P 3-                                                      
FORMUL  17  PGE    C6 H14 O4                                                    
FORMUL  18  MES    2(C6 H13 N O4 S)                                             
FORMUL  20   NA    NA 1+                                                        
FORMUL  21  HOH   *397(H2 O)                                                    
HELIX    1   1 ALA A    6  VAL A   19  1                                  14    
HELIX    2   2 ASP A   20  SER A   24  5                                   5    
HELIX    3   3 SER A   30  HIS A   35  1                                   6    
HELIX    4   4 ASP A   36  ALA A   40  5                                   5    
HELIX    5   5 TYR A   72  VAL A   76  5                                   5    
HELIX    6   6 ASP A   99  ASN A  110  1                                  12    
HELIX    7   7 ASP A  118  ASP A  129  1                                  12    
HELIX    8   8 ASP A  129  GLY A  141  1                                  13    
HELIX    9   9 GLY A  143  ASP A  146  5                                   4    
HELIX   10  10 ASP A  147  ALA A  164  1                                  18    
HELIX   11  11 SER A  173  ARG A  180  1                                   8    
HELIX   12  12 THR A  186  ILE A  197  1                                  12    
HELIX   13  13 ASN A  200  HIS A  205  1                                   6    
HELIX   14  14 ASN A  231  GLY A  239  1                                   9    
HELIX   15  15 HIS A  247  ARG A  252  5                                   6    
HELIX   16  16 ASP A  257  SER A  261  5                                   5    
HELIX   17  17 ASN A  271  THR A  275  5                                   5    
HELIX   18  18 ASP A  286  PHE A  293  1                                   8    
HELIX   19  19 TYR A  294  THR A  298  5                                   5    
HELIX   20  20 ARG A  301  ALA A  304  5                                   4    
HELIX   21  21 SER A  324  GLN A  329  1                                   6    
HELIX   22  22 ASP A  335  THR A  348  1                                  14    
HELIX   23  23 LEU A  349  THR A  350  5                                   2    
HELIX   24  24 ASP A  351  GLU A  355  5                                   5    
HELIX   25  25 ASP B    7  VAL B   19  1                                  13    
HELIX   26  26 ASP B   20  SER B   24  5                                   5    
HELIX   27  27 SER B   30  HIS B   35  1                                   6    
HELIX   28  28 ASP B   36  ALA B   40  5                                   5    
HELIX   29  29 TYR B   72  VAL B   76  5                                   5    
HELIX   30  30 ASP B   99  ASN B  110  1                                  12    
HELIX   31  31 ASP B  118  ASP B  128  1                                  11    
HELIX   32  32 ASP B  129  PHE B  140  1                                  12    
HELIX   33  33 GLY B  143  ASP B  146  5                                   4    
HELIX   34  34 ASP B  147  ALA B  164  1                                  18    
HELIX   35  35 SER B  173  GLY B  181  1                                   9    
HELIX   36  36 THR B  186  ILE B  197  1                                  12    
HELIX   37  37 ASN B  200  HIS B  205  1                                   6    
HELIX   38  38 ASN B  231  GLY B  239  1                                   9    
HELIX   39  39 HIS B  247  ARG B  252  5                                   6    
HELIX   40  40 ASP B  257  SER B  261  5                                   5    
HELIX   41  41 ASN B  271  THR B  275  5                                   5    
HELIX   42  42 ASP B  286  PHE B  293  1                                   8    
HELIX   43  43 TYR B  294  THR B  298  5                                   5    
HELIX   44  44 ARG B  301  ILE B  306  5                                   6    
HELIX   45  45 SER B  324  GLN B  329  1                                   6    
HELIX   46  46 ASP B  335  THR B  348  1                                  14    
HELIX   47  47 LEU B  349  THR B  350  5                                   2    
HELIX   48  48 ASP B  351  GLU B  355  5                                   5    
HELIX   49  49 TYR C   25  CYS C   29  5                                   5    
HELIX   50  50 CYS C   36  SER C   39  5                                   4    
HELIX   51  51 ARG C   99  ALA C  103  5                                   5    
HELIX   52  52 ALA C  112  ALA C  116  5                                   5    
HELIX   53  53 THR D   13  GLY D   29  1                                  17    
HELIX   54  54 PRO D   52  ALA D   56  5                                   5    
HELIX   55  55 TYR D  138  TRP D  140  5                                   3    
HELIX   56  56 THR D  269  ASP D  275  1                                   7    
HELIX   57  57 TYR E   25  CYS E   29  5                                   5    
HELIX   58  58 CYS E   36  GLY E   40  5                                   5    
HELIX   59  59 ARG E   99  ALA E  103  5                                   5    
HELIX   60  60 ALA E  112  ALA E  116  5                                   5    
HELIX   61  61 THR F   13  GLY F   29  1                                  17    
HELIX   62  62 TYR F  138  TRP F  140  5                                   3    
HELIX   63  63 THR F  269  ASP F  275  1                                   7    
SHEET    1   A 2 HIS A  80  ARG A  81  0                                        
SHEET    2   A 2 TYR A  87  LYS A  88 -1  O  LYS A  88   N  HIS A  80           
SHEET    1   B 2 TYR A 223  HIS A 224  0                                        
SHEET    2   B 2 PHE A 264  LYS A 265 -1  O  PHE A 264   N  HIS A 224           
SHEET    1   C 2 ILE A 306  ASN A 307  0                                        
SHEET    2   C 2 ALA A 312  PRO A 313 -1  O  ALA A 312   N  ASN A 307           
SHEET    1   D 2 HIS B  80  ARG B  81  0                                        
SHEET    2   D 2 TYR B  87  LYS B  88 -1  O  LYS B  88   N  HIS B  80           
SHEET    1   E 2 TYR B 223  HIS B 224  0                                        
SHEET    2   E 2 PHE B 264  LYS B 265 -1  O  PHE B 264   N  HIS B 224           
SHEET    1   F 2 ASP C  32  ASN C  34  0                                        
SHEET    2   F 2 PRO C  87  LEU C  89 -1  O  CYS C  88   N  GLY C  33           
SHEET    1   G 3 LYS C  51  LEU C  52  0                                        
SHEET    2   G 3 SER C  69  CYS C  78 -1  O  CYS C  78   N  LYS C  51           
SHEET    3   G 3 TYR C 119  ILE C 123 -1  O  CYS C 121   N  CYS C  77           
SHEET    1   H 3 0AF C  57  TYR C  62  0                                        
SHEET    2   H 3 SER C  69  CYS C  78 -1  O  ILE C  72   N  ALA C  59           
SHEET    3   H 3 ILE C 126  LYS C 129 -1  O  VAL C 127   N  LEU C  71           
SHEET    1   I 4 ARG D  70  GLY D  77  0                                        
SHEET    2   I 4 THR D  59  ASP D  65 -1  N  VAL D  63   O  GLY D  73           
SHEET    3   I 4 ARG D  46  ASP D  51 -1  N  VAL D  47   O  ILE D  64           
SHEET    4   I 4 VAL D 379  THR D 382 -1  O  THR D 381   N  TYR D  48           
SHEET    1   J 4 ASN D  82  VAL D  85  0                                        
SHEET    2   J 4 ILE D  92  PHE D  99 -1  O  ALA D  93   N  VAL D  84           
SHEET    3   J 4 ARG D 107  PHE D 114 -1  O  PHE D 114   N  ILE D  92           
SHEET    4   J 4 PRO D 121  LEU D 127 -1  O  LEU D 127   N  ASP D 109           
SHEET    1   K 4 THR D 142  LEU D 144  0                                        
SHEET    2   K 4 THR D 150  GLN D 155 -1  O  LEU D 152   N  SER D 143           
SHEET    3   K 4 ALA D 161  ASP D 166 -1  O  GLY D 163   N  PHE D 153           
SHEET    4   K 4 ALA D 171  ASP D 177 -1  O  ALA D 171   N  ASP D 166           
SHEET    1   L 4 CYS D 181  ALA D 188  0                                        
SHEET    2   L 4 THR D 191  CYS D 196 -1  O  HIS D 195   N  TYR D 182           
SHEET    3   L 4 LEU D 201  ALA D 205 -1  O  ALA D 202   N  MET D 194           
SHEET    4   L 4 GLU D 213  HIS D 216 -1  O  THR D 215   N  LYS D 203           
SHEET    1   M 4 ALA D 232  SER D 234  0                                        
SHEET    2   M 4 ARG D 239  PRO D 243 -1  O  VAL D 241   N  ALA D 232           
SHEET    3   M 4 LYS D 248  ASP D 253 -1  O  HIS D 250   N  TRP D 242           
SHEET    4   M 4 LYS D 260  PHE D 261 -1  O  LYS D 260   N  ASP D 253           
SHEET    1   N 4 ALA D 232  SER D 234  0                                        
SHEET    2   N 4 ARG D 239  PRO D 243 -1  O  VAL D 241   N  ALA D 232           
SHEET    3   N 4 LYS D 248  ASP D 253 -1  O  HIS D 250   N  TRP D 242           
SHEET    4   N 4 VAL D 265  GLU D 266 -1  O  VAL D 265   N  ILE D 249           
SHEET    1   O 3 TRP D 277  PRO D 279  0                                        
SHEET    2   O 3 ARG D 293  GLN D 300 -1  O  ASP D 299   N  ARG D 278           
SHEET    3   O 3 VAL D 285  HIS D 288 -1  N  ALA D 286   O  TYR D 295           
SHEET    1   P 4 TRP D 277  PRO D 279  0                                        
SHEET    2   P 4 ARG D 293  GLN D 300 -1  O  ASP D 299   N  ARG D 278           
SHEET    3   P 4 SER D 310  ASP D 317 -1  O  LEU D 316   N  ILE D 294           
SHEET    4   P 4 ARG D 323  ILE D 333 -1  O  ALA D 325   N  VAL D 315           
SHEET    1   Q 4 SER D 335  VAL D 338  0                                        
SHEET    2   Q 4 LEU D 345  SER D 350 -1  O  LEU D 349   N  SER D 335           
SHEET    3   Q 4 THR D 355  ASP D 360 -1  O  TYR D 357   N  ALA D 348           
SHEET    4   Q 4 GLU D 366  VAL D 370 -1  O  VAL D 370   N  LEU D 356           
SHEET    1   R 2 ASP E  32  ASN E  34  0                                        
SHEET    2   R 2 PRO E  87  LEU E  89 -1  O  CYS E  88   N  GLY E  33           
SHEET    1   S 3 LYS E  51  LEU E  52  0                                        
SHEET    2   S 3 SER E  69  CYS E  78 -1  O  CYS E  78   N  LYS E  51           
SHEET    3   S 3 TYR E 119  ILE E 123 -1  O  ILE E 123   N  ARG E  75           
SHEET    1   T 3 0AF E  57  TYR E  62  0                                        
SHEET    2   T 3 SER E  69  CYS E  78 -1  O  TYR E  70   N  CYS E  61           
SHEET    3   T 3 ILE E 126  LYS E 129 -1  O  VAL E 127   N  LEU E  71           
SHEET    1   U 4 ARG F  70  GLY F  77  0                                        
SHEET    2   U 4 THR F  59  ASP F  65 -1  N  THR F  59   O  GLY F  77           
SHEET    3   U 4 ARG F  46  ASP F  51 -1  N  VAL F  49   O  PHE F  62           
SHEET    4   U 4 VAL F 379  THR F 382 -1  O  VAL F 379   N  ASN F  50           
SHEET    1   V 3 ASN F  82  VAL F  85  0                                        
SHEET    2   V 3 ILE F  92  PHE F 114 -1  O  ALA F  93   N  VAL F  84           
SHEET    3   V 3 PRO F 121  LEU F 127 -1  O  LEU F 127   N  ASP F 109           
SHEET    1   W 4 THR F 142  LEU F 144  0                                        
SHEET    2   W 4 THR F 150  GLN F 155 -1  O  LEU F 152   N  SER F 143           
SHEET    3   W 4 ALA F 161  ASP F 166 -1  O  ALA F 161   N  GLN F 155           
SHEET    4   W 4 ALA F 171  ASP F 177 -1  O  ARG F 174   N  VAL F 164           
SHEET    1   X 4 CYS F 181  ALA F 188  0                                        
SHEET    2   X 4 THR F 191  CYS F 196 -1  O  HIS F 195   N  TYR F 182           
SHEET    3   X 4 LEU F 201  ALA F 205 -1  O  ALA F 202   N  MET F 194           
SHEET    4   X 4 GLU F 213  HIS F 216 -1  O  THR F 215   N  LYS F 203           
SHEET    1   Y 4 ALA F 232  SER F 234  0                                        
SHEET    2   Y 4 ARG F 239  PRO F 243 -1  O  VAL F 241   N  ALA F 232           
SHEET    3   Y 4 LYS F 248  ASP F 253 -1  O  HIS F 250   N  TRP F 242           
SHEET    4   Y 4 LYS F 260  PHE F 261 -1  O  LYS F 260   N  ASP F 253           
SHEET    1   Z 4 ALA F 232  SER F 234  0                                        
SHEET    2   Z 4 ARG F 239  PRO F 243 -1  O  VAL F 241   N  ALA F 232           
SHEET    3   Z 4 LYS F 248  ASP F 253 -1  O  HIS F 250   N  TRP F 242           
SHEET    4   Z 4 VAL F 265  GLU F 266 -1  O  VAL F 265   N  ILE F 249           
SHEET    1  AA 3 TRP F 277  PRO F 279  0                                        
SHEET    2  AA 3 ARG F 293  GLN F 300 -1  O  ASP F 299   N  ARG F 278           
SHEET    3  AA 3 VAL F 285  HIS F 288 -1  N  ALA F 286   O  TYR F 295           
SHEET    1  AB 4 TRP F 277  PRO F 279  0                                        
SHEET    2  AB 4 ARG F 293  GLN F 300 -1  O  ASP F 299   N  ARG F 278           
SHEET    3  AB 4 SER F 310  ASP F 317 -1  O  LEU F 316   N  ILE F 294           
SHEET    4  AB 4 ARG F 323  ILE F 333 -1  O  LEU F 324   N  VAL F 315           
SHEET    1  AC 4 SER F 335  VAL F 338  0                                        
SHEET    2  AC 4 LEU F 345  SER F 350 -1  O  TYR F 347   N  ASN F 337           
SHEET    3  AC 4 THR F 355  ASP F 360 -1  O  HIS F 359   N  LEU F 346           
SHEET    4  AC 4 GLU F 366  VAL F 370 -1  O  VAL F 370   N  LEU F 356           
SSBOND   1 CYS C   23    CYS C   88                          1555   1555  2.03  
SSBOND   2 CYS C   29    CYS C   61                          1555   1555  2.02  
SSBOND   3 CYS C   36    CYS C  121                          1555   1555  2.04  
SSBOND   4 CYS C   38    CYS C   86                          1555   1555  2.02  
SSBOND   5 CYS C   46    CYS C   77                          1555   1555  2.01  
SSBOND   6 CYS C   78    CYS C  109                          1555   1555  2.02  
SSBOND   7 CYS D  181    CYS D  196                          1555   1555  2.03  
SSBOND   8 CYS E   23    CYS E   88                          1555   1555  2.03  
SSBOND   9 CYS E   29    CYS E   61                          1555   1555  2.03  
SSBOND  10 CYS E   36    CYS E  121                          1555   1555  2.03  
SSBOND  11 CYS E   38    CYS E   86                          1555   1555  2.03  
SSBOND  12 CYS E   46    CYS E   77                          1555   1555  2.02  
SSBOND  13 CYS E   78    CYS E  109                          1555   1555  2.02  
SSBOND  14 CYS F  181    CYS F  196                          1555   1555  2.04  
LINK         SG  CYS A  31                 CAB HEC A 402     1555   1555  1.76  
LINK         SG  CYS A  34                 CAC HEC A 402     1555   1555  1.78  
LINK         SG  CYS A 201                 CAB HEC A 403     1555   1555  1.76  
LINK         SG  CYS A 204                 CAC HEC A 403     1555   1555  1.77  
LINK         SG  CYS B  31                 CAB HEC B 402     1555   1555  1.76  
LINK         SG  CYS B  34                 CAC HEC B 402     1555   1555  1.80  
LINK         SG  CYS B 201                 CAB HEC B 403     1555   1555  1.76  
LINK         SG  CYS B 204                 CAC HEC B 403     1555   1555  1.78  
LINK         C   SER C  56                 N   0AF C  57     1555   1555  1.33  
LINK         C   0AF C  57                 N   VAL C  58     1555   1555  1.33  
LINK         C   SER E  56                 N   0AF E  57     1555   1555  1.33  
LINK         C   0AF E  57                 N   VAL E  58     1555   1555  1.33  
LINK         NE2 HIS A  35                FE   HEC A 402     1555   1555  2.29  
LINK         OD1 ASN A  66                CA    CA A 401     1555   1555  2.51  
LINK         NE2 HIS A 205                FE   HEC A 403     1555   1555  2.37  
LINK         O   THR A 275                CA    CA A 401     1555   1555  2.27  
LINK         O   PRO A 277                CA    CA A 401     1555   1555  2.46  
LINK         OH  TYR A 294                FE   HEC A 403     1555   1555  1.86  
LINK        CA    CA A 401                 O   HOH A 534     1555   1555  2.41  
LINK        CA    CA A 401                 O   HOH A 550     1555   1555  2.12  
LINK         NE2 HIS B  35                FE   HEC B 402     1555   1555  2.24  
LINK         OD1 ASN B  66                CA    CA B 401     1555   1555  2.27  
LINK         NE2 HIS B 205                FE   HEC B 403     1555   1555  2.30  
LINK         O   THR B 275                CA    CA B 401     1555   1555  2.35  
LINK         O   PRO B 277                CA    CA B 401     1555   1555  2.33  
LINK         OH  TYR B 294                FE   HEC B 403     1555   1555  1.89  
LINK        CA    CA B 401                 O   HOH B 542     1555   1555  2.18  
LINK        CA    CA B 401                 O   HOH B 548     1555   1555  2.26  
LINK        CA    CA B 401                 O   HOH B 551     1555   1555  2.48  
LINK        CA    CA B 401                 O   HOH B 584     1555   1555  2.80  
LINK         O   ASP F 253                NA    NA F 402     1555   1555  2.82  
LINK         OD2 ASP F 253                NA    NA F 402     1555   1555  2.90  
LINK         OG  SER F 256                NA    NA F 402     1555   1555  2.59  
LINK         O   ASP F 258                NA    NA F 402     1555   1555  2.61  
CISPEP   1 GLY A  276    PRO A  277          0        -7.64                     
CISPEP   2 GLY B  276    PRO B  277          0        -5.90                     
CISPEP   3 SER D  157    PRO D  158          0        -0.85                     
CISPEP   4 SER F  157    PRO F  158          0        -4.61                     
SITE     1 AC1  5 ASN A  66  THR A 275  PRO A 277  HOH A 534                    
SITE     2 AC1  5 HOH A 550                                                     
SITE     1 AC2 26 GLN A  29  SER A  30  CYS A  31  CYS A  34                    
SITE     2 AC2 26 HIS A  35  VAL A  55  ARG A  65  ASN A  66                    
SITE     3 AC2 26 THR A  67  PRO A  68  LEU A  70  GLN A  91                    
SITE     4 AC2 26 PHE A  92  TRP A  93  ARG A  96  LEU A 100                    
SITE     5 AC2 26 ASN A 103  ALA A 104  PRO A 107  GLU A 113                    
SITE     6 AC2 26 MET A 114  LEU A 159  GLN A 163  LYS A 265                    
SITE     7 AC2 26 HOH A 535  HOH A 563                                          
SITE     1 AC3 20 TRP A  93  ASN A 200  CYS A 201  CYS A 204                    
SITE     2 AC3 20 HIS A 205  HIS A 224  LEU A 228  PHE A 264                    
SITE     3 AC3 20 LYS A 265  PRO A 267  LEU A 269  VAL A 272                    
SITE     4 AC3 20 TYR A 278  MET A 279  HIS A 280  LEU A 287                    
SITE     5 AC3 20 TYR A 294  GLU A 327  LEU A 334  HOH A 550                    
SITE     1 AC4  4 LYS A  48  GLN A  60  ALA A 237  HOH A 507                    
SITE     1 AC5  3 LYS A 296  SER A 299  ARG A 300                               
SITE     1 AC6  7 ASN B  66  THR B 275  PRO B 277  HOH B 542                    
SITE     2 AC6  7 HOH B 548  HOH B 551  HOH B 584                               
SITE     1 AC7 25 GLN B  29  SER B  30  CYS B  31  CYS B  34                    
SITE     2 AC7 25 HIS B  35  ARG B  65  ASN B  66  THR B  67                    
SITE     3 AC7 25 PRO B  68  LEU B  70  GLN B  91  PHE B  92                    
SITE     4 AC7 25 TRP B  93  ARG B  96  LEU B 100  ASN B 103                    
SITE     5 AC7 25 PRO B 107  GLU B 113  MET B 114  GLN B 163                    
SITE     6 AC7 25 LYS B 265  HOH B 573  HOH B 587  HOH B 588                    
SITE     7 AC7 25 HOH B 596                                                     
SITE     1 AC8 22 ASN B 200  CYS B 201  CYS B 204  HIS B 205                    
SITE     2 AC8 22 HIS B 224  LEU B 228  PHE B 264  VAL B 266                    
SITE     3 AC8 22 PRO B 267  TYR B 278  MET B 279  HIS B 280                    
SITE     4 AC8 22 LEU B 287  TYR B 294  SER B 324  GLU B 327                    
SITE     5 AC8 22 LEU B 334  HOH B 510  HOH B 548  HOH B 551                    
SITE     6 AC8 22 HOH B 590  HOH B 595                                          
SITE     1 AC9  3 LEU B  75  ALA B 164  ARG B 215                               
SITE     1 BC1  1 HOH B 577                                                     
SITE     1 BC2  4 SER C  60  GLU C  92  GLY C  93  HOH C 320                    
SITE     1 BC3  4 ALA A 138  ARG D  35  LEU D  37  GLU D  38                    
SITE     1 BC4  6 ALA B 138  LEU B 139  GLY B 141  ARG F  35                    
SITE     2 BC4  6 LEU F  37  GLU F  38                                          
SITE     1 BC5  3 ASP F 253  SER F 256  ASP F 258                               
CRYST1   55.530   83.520  107.780 109.94  91.54 105.78 P 1           2          
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      0.018008  0.005089  0.002496        0.00000                         
SCALE2      0.000000  0.012442  0.004834        0.00000                         
SCALE3      0.000000  0.000000  0.009957        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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