GenomeNet

Database: PDB
Entry: 3NH3
LinkDB: 3NH3
Original site: 3NH3 
HEADER    OXIDOREDUCTASE                          14-JUN-10   3NH3              
TITLE     COMPLEX OF 6-HYDROXY-L-NICOTINE OXIDASE WITH FINAL KETONE PRODUCT     
TITLE    2 FORMED DURING CATALYTIC TURNOVER                                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: 6-HYDROXY-L-NICOTINE OXIDASE;                              
COMPND   3 CHAIN: X;                                                            
COMPND   4 EC: 1.5.3.5;                                                         
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ARTHROBACTER NICOTINOVORANS;                    
SOURCE   3 ORGANISM_TAXID: 29320;                                               
SOURCE   4 GENE: 6-HLNO;                                                        
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: JM105;                                     
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PTRC99A                                   
KEYWDS    ENANTHIOMERIC SUBSTRATE-INHIBITOR, FLAVOENZYMES, NICOTINE             
KEYWDS   2 DEGRADATION, OXIDOREDUCTASE                                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    G.S.KACHALOVA,H.D.BARTUNIK                                            
REVDAT   4   06-SEP-23 3NH3    1       REMARK SEQADV                            
REVDAT   3   08-NOV-17 3NH3    1       REMARK                                   
REVDAT   2   10-AUG-11 3NH3    1       JRNL   VERSN                             
REVDAT   1   23-MAR-11 3NH3    0                                                
JRNL        AUTH   G.S.KACHALOVA,G.P.BOURENKOV,T.MENGESDORF,S.SCHENK,H.R.MAUN,  
JRNL        AUTH 2 M.BURGHAMMER,C.RIEKEL,K.DECKER,H.D.BARTUNIK                  
JRNL        TITL   CRYSTAL STRUCTURE ANALYSIS OF FREE AND SUBSTRATE-BOUND       
JRNL        TITL 2 6-HYDROXY-L-NICOTINE OXIDASE FROM ARTHROBACTER               
JRNL        TITL 3 NICOTINOVORANS.                                              
JRNL        REF    J.MOL.BIOL.                   V. 396   785 2010              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   20006620                                                     
JRNL        DOI    10.1016/J.JMB.2009.12.009                                    
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   G.S.KACHALOVA,G.P.BOURENKOV,T.MENGESDORF,S.SCHENK,H.R.MAUN,  
REMARK   1  AUTH 2 M.BURGHAMMER,C.RIEKEL,K.DECKER,H.D.BARTUNIK                  
REMARK   1  TITL   CRYSTAL STRUCTURE ANALYSIS OF FREE AND SUBSTRATE-BOUND       
REMARK   1  TITL 2 6-HYDROXY-L-NICOTINE FROM ARTHROBACTER NICOTINOVORANS        
REMARK   1  REF    J.MOL.BIOL.                   V. 396   785 2010              
REMARK   1  REFN                   ISSN 0022-2836                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
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) : 2.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 12.22                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 41266                          
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) : 0.161                           
REMARK   3   R VALUE            (WORKING SET) : 0.159                           
REMARK   3   FREE R VALUE                     : 0.204                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2184                            
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) : 2.10                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.15                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2918                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.94                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2120                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 165                          
REMARK   3   BIN FREE R VALUE                    : 0.2610                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3270                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 123                                     
REMARK   3   SOLVENT ATOMS            : 393                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 31.40                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 31.53                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.133         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.087         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.264         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.969                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.954                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3526 ; 0.031 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4800 ; 2.369 ; 2.000       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   434 ; 6.630 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   156 ;40.207 ;23.462       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   536 ;16.248 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    26 ;19.739 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   522 ; 0.208 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2692 ; 0.014 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1710 ; 0.242 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  2375 ; 0.327 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   334 ; 0.218 ; 0.200       
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):    60 ; 0.392 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    39 ; 0.519 ; 0.200       
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):  2201 ; 1.846 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3407 ; 2.740 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1603 ; 4.484 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1388 ; 6.741 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3NH3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-JUN-10.                  
REMARK 100 THE DEPOSITION ID IS D_1000059820.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 17-MAR-03                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : MPG/DESY, HAMBURG                  
REMARK 200  BEAMLINE                       : BW6                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.05                               
REMARK 200  MONOCHROMATOR                  : GRAPHITE                           
REMARK 200  OPTICS                         : MIRROR                             
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MAR CCD 165 MM                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 43679                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 8.500                              
REMARK 200  R MERGE                    (I) : 0.11600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 20.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.14                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 8.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.70400                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.500                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: PDB CODE 3K7M                                        
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 67.85                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.83                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20MM SODIUM PHOSPHATE; 4M SODIUM         
REMARK 280  FORMIATE, PH 7.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 4 3 2                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X,Y,-Z                                                 
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   Z,X,Y                                                   
REMARK 290       6555   Z,-X,-Y                                                 
REMARK 290       7555   -Z,-X,Y                                                 
REMARK 290       8555   -Z,X,-Y                                                 
REMARK 290       9555   Y,Z,X                                                   
REMARK 290      10555   -Y,Z,-X                                                 
REMARK 290      11555   Y,-Z,-X                                                 
REMARK 290      12555   -Y,-Z,X                                                 
REMARK 290      13555   Y,X,-Z                                                  
REMARK 290      14555   -Y,-X,-Z                                                
REMARK 290      15555   Y,-X,Z                                                  
REMARK 290      16555   -Y,X,Z                                                  
REMARK 290      17555   X,Z,-Y                                                  
REMARK 290      18555   -X,Z,Y                                                  
REMARK 290      19555   -X,-Z,-Y                                                
REMARK 290      20555   X,-Z,Y                                                  
REMARK 290      21555   Z,Y,-X                                                  
REMARK 290      22555   Z,-Y,X                                                  
REMARK 290      23555   -Z,Y,X                                                  
REMARK 290      24555   -Z,-Y,-X                                                
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY2   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY1   6  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY2   6 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY1   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY2   7 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY2   8  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY1   9  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   9  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY3   9  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY1  10  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2  10  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY3  10 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY1  11  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2  11  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY3  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY1  12  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2  12  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY3  12  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY1  13  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2  13  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3  13  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1  14  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2  14 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3  14  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1  15  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2  15 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3  15  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1  16  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2  16  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3  16  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1  17  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  17  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY3  17  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY1  18 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  18  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY3  18  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY1  19 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  19  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY3  19  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY1  20  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  20  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY3  20  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY1  21  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY2  21  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  21 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY1  22  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY2  22  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  22  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY1  23  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY2  23  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  23  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY1  24  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY2  24  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  24 -1.000000  0.000000  0.000000        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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1230 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 32590 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: X                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      163.05100            
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 X   426                                                      
REMARK 465     HIS X   427                                                      
REMARK 465     HIS X   428                                                      
REMARK 465     HIS X   429                                                      
REMARK 465     HIS X   430                                                      
REMARK 465     HIS X   431                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     SER X 425    CB   OG                                             
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     SER X   12   CA   CB   OG                                        
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   CB   ALA X    82     O    HOH X   464              1.16            
REMARK 500   OE2  GLU X   300     C12  HNM X   436              2.11            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ALA X  58      -39.08   -146.90                                   
REMARK 500    ARG X  91       76.83   -116.54                                   
REMARK 500    HIS X 187       43.06    -93.51                                   
REMARK 500    TYR X 313      -60.74   -125.10                                   
REMARK 500    THR X 327     -150.79   -148.60                                   
REMARK 500    PHE X 367      -53.36   -144.22                                   
REMARK 500    PRO X 370     -137.94    -81.65                                   
REMARK 500    HIS X 383      -58.34   -144.80                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     GP7 X  435                                                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HNL X 433                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD X 434                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GP7 X 435                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HNM X 436                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3NGC   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3NHO   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3NK0   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3NK1   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3NK2   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3NN0   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3NN6   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3K7Q   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3K7M   RELATED DB: PDB                                   
DBREF  3NH3 X    1   425  UNP    Q93NH4   Q93NH4_ARTNI     1    425             
SEQADV 3NH3 HIS X  426  UNP  Q93NH4              EXPRESSION TAG                 
SEQADV 3NH3 HIS X  427  UNP  Q93NH4              EXPRESSION TAG                 
SEQADV 3NH3 HIS X  428  UNP  Q93NH4              EXPRESSION TAG                 
SEQADV 3NH3 HIS X  429  UNP  Q93NH4              EXPRESSION TAG                 
SEQADV 3NH3 HIS X  430  UNP  Q93NH4              EXPRESSION TAG                 
SEQADV 3NH3 HIS X  431  UNP  Q93NH4              EXPRESSION TAG                 
SEQRES   1 X  431  MET TYR ASP ALA ILE VAL VAL GLY GLY GLY PHE SER GLY          
SEQRES   2 X  431  LEU LYS ALA ALA ARG ASP LEU THR ASN ALA GLY LYS LYS          
SEQRES   3 X  431  VAL LEU LEU LEU GLU GLY GLY GLU ARG LEU GLY GLY ARG          
SEQRES   4 X  431  ALA TYR SER ARG GLU SER ARG ASN VAL PRO GLY LEU ARG          
SEQRES   5 X  431  VAL GLU ILE GLY GLY ALA TYR LEU HIS ARG LYS HIS HIS          
SEQRES   6 X  431  PRO ARG LEU ALA ALA GLU LEU ASP ARG TYR GLY ILE PRO          
SEQRES   7 X  431  THR ALA ALA ALA SER GLU PHE THR SER PHE ARG HIS ARG          
SEQRES   8 X  431  LEU GLY PRO THR ALA VAL ASP GLN ALA PHE PRO ILE PRO          
SEQRES   9 X  431  GLY SER GLU ALA VAL ALA VAL GLU ALA ALA THR TYR THR          
SEQRES  10 X  431  LEU LEU ARG ASP ALA HIS ARG ILE ASP LEU GLU LYS GLY          
SEQRES  11 X  431  LEU GLU ASN GLN ASP LEU GLU ASP LEU ASP ILE PRO LEU          
SEQRES  12 X  431  ASN GLU TYR VAL ASP LYS LEU ASP LEU PRO PRO VAL SER          
SEQRES  13 X  431  ARG GLN PHE LEU LEU ALA TRP ALA TRP ASN MET LEU GLY          
SEQRES  14 X  431  GLN PRO ALA ASP GLN ALA SER ALA LEU TRP MET LEU GLN          
SEQRES  15 X  431  LEU VAL ALA ALA HIS HIS TYR SER ILE LEU GLY VAL VAL          
SEQRES  16 X  431  LEU SER LEU ASP GLU VAL PHE SER ASN GLY SER ALA ASP          
SEQRES  17 X  431  LEU VAL ASP ALA MET SER GLN GLU ILE PRO GLU ILE ARG          
SEQRES  18 X  431  LEU GLN THR VAL VAL THR GLY ILE ASP GLN SER GLY ASP          
SEQRES  19 X  431  VAL VAL ASN VAL THR VAL LYS ASP GLY HIS ALA PHE GLN          
SEQRES  20 X  431  ALA HIS SER VAL ILE VAL ALA THR PRO MET ASN THR TRP          
SEQRES  21 X  431  ARG ARG ILE VAL PHE THR PRO ALA LEU PRO GLU ARG ARG          
SEQRES  22 X  431  ARG SER VAL ILE GLU GLU GLY HIS GLY GLY GLN GLY LEU          
SEQRES  23 X  431  LYS ILE LEU ILE HIS VAL ARG GLY ALA GLU ALA GLY ILE          
SEQRES  24 X  431  GLU CYS VAL GLY ASP GLY ILE PHE PRO THR LEU TYR ASP          
SEQRES  25 X  431  TYR CYS GLU VAL SER GLU SER GLU ARG LEU LEU VAL ALA          
SEQRES  26 X  431  PHE THR ASP SER GLY SER PHE ASP PRO THR ASP ILE GLY          
SEQRES  27 X  431  ALA VAL LYS ASP ALA VAL LEU TYR TYR LEU PRO GLU VAL          
SEQRES  28 X  431  GLU VAL LEU GLY ILE ASP TYR HIS ASP TRP ILE ALA ASP          
SEQRES  29 X  431  PRO LEU PHE GLU GLY PRO TRP VAL ALA PRO ARG VAL GLY          
SEQRES  30 X  431  GLN PHE SER ARG VAL HIS LYS GLU LEU GLY GLU PRO ALA          
SEQRES  31 X  431  GLY ARG ILE HIS PHE VAL GLY SER ASP VAL SER LEU GLU          
SEQRES  32 X  431  PHE PRO GLY TYR ILE GLU GLY ALA LEU GLU THR ALA GLU          
SEQRES  33 X  431  CYS ALA VAL ASN ALA ILE LEU HIS SER HIS HIS HIS HIS          
SEQRES  34 X  431  HIS HIS                                                      
HET    HNL  X 433      13                                                       
HET    FAD  X 434      53                                                       
HET    GP7  X 435      43                                                       
HET    HNM  X 436      28                                                       
HETNAM     HNL 5-[(2S)-1-METHYLPYRROLIDIN-2-YL]PYRIDIN-2-OL                     
HETNAM     FAD FLAVIN-ADENINE DINUCLEOTIDE                                      
HETNAM     GP7 (1R)-2-{[(S)-(2-AMINOETHOXY)(HYDROXY)PHOSPHORYL]OXY}-1-          
HETNAM   2 GP7  [(PENTADECANOYLOXY)METHYL]ETHYL (12E)-HEXADECA-9,12-            
HETNAM   3 GP7  DIENOATE                                                        
HETNAM     HNM 1-(6-HYDROXYPYRIDIN-3-YL)-4-(METHYLAMINO)BUTAN-1-ONE             
HETSYN     HNL 6-HYDROXY-L-NICOTINE                                             
HETSYN     GP7 1-PENTADECANOYL-2-HEXADECANOYL-SN-GLYCERO-3-                     
HETSYN   2 GP7  PHOSPHOETHANOLAMINE                                             
FORMUL   2  HNL    C10 H14 N2 O                                                 
FORMUL   3  FAD    C27 H33 N9 O15 P2                                            
FORMUL   4  GP7    C36 H68 N O8 P                                               
FORMUL   5  HNM    C10 H14 N2 O2                                                
FORMUL   6  HOH   *393(H2 O)                                                    
HELIX    1   1 GLY X   10  ALA X   23  1                                  14    
HELIX    2   2 HIS X   65  GLY X   76  1                                  12    
HELIX    3   3 PRO X  104  SER X  106  5                                   3    
HELIX    4   4 GLU X  107  HIS X  123  1                                  17    
HELIX    5   5 LEU X  136  ASP X  140  5                                   5    
HELIX    6   6 PRO X  142  ASP X  151  1                                  10    
HELIX    7   7 PRO X  153  GLY X  169  1                                  17    
HELIX    8   8 SER X  176  HIS X  187  1                                  12    
HELIX    9   9 SER X  190  SER X  197  1                                   8    
HELIX   10  10 GLY X  205  GLN X  215  1                                  11    
HELIX   11  11 PRO X  256  ILE X  263  5                                   8    
HELIX   12  12 PRO X  270  GLY X  280  1                                  11    
HELIX   13  13 ASP X  336  LEU X  348  1                                  13    
HELIX   14  14 GLY X  377  VAL X  382  1                                   6    
HELIX   15  15 LYS X  384  GLU X  388  5                                   5    
HELIX   16  16 GLY X  397  SER X  401  5                                   5    
HELIX   17  17 TYR X  407  HIS X  424  1                                  18    
SHEET    1   A 7 ILE X 220  ARG X 221  0                                        
SHEET    2   A 7 VAL X  27  LEU X  30  1  N  LEU X  29   O  ARG X 221           
SHEET    3   A 7 TYR X   2  VAL X   7  1  N  VAL X   6   O  LEU X  28           
SHEET    4   A 7 PHE X 246  VAL X 253  1  O  ILE X 252   N  VAL X   7           
SHEET    5   A 7 VAL X 236  VAL X 240 -1  N  VAL X 238   O  PHE X 246           
SHEET    6   A 7 VAL X 226  ASP X 230 -1  N  ASP X 230   O  ASN X 237           
SHEET    7   A 7 VAL X 264  THR X 266  1  O  VAL X 264   N  ILE X 229           
SHEET    1   B 5 ILE X 220  ARG X 221  0                                        
SHEET    2   B 5 VAL X  27  LEU X  30  1  N  LEU X  29   O  ARG X 221           
SHEET    3   B 5 TYR X   2  VAL X   7  1  N  VAL X   6   O  LEU X  28           
SHEET    4   B 5 PHE X 246  VAL X 253  1  O  ILE X 252   N  VAL X   7           
SHEET    5   B 5 ILE X 393  PHE X 395  1  O  HIS X 394   N  VAL X 253           
SHEET    1   C 2 SER X  42  GLU X  44  0                                        
SHEET    2   C 2 ARG X  52  GLU X  54 -1  O  VAL X  53   N  ARG X  43           
SHEET    1   D 3 TYR X  59  LEU X  60  0                                        
SHEET    2   D 3 GLU X 200  PHE X 202 -1  O  GLU X 200   N  LEU X  60           
SHEET    3   D 3 THR X  79  ALA X  80 -1  N  ALA X  80   O  VAL X 201           
SHEET    1   E 6 SER X  87  PHE X  88  0                                        
SHEET    2   E 6 ILE X 299  VAL X 302  1  O  GLU X 300   N  SER X  87           
SHEET    3   E 6 THR X 309  GLU X 315 -1  O  ASP X 312   N  ILE X 299           
SHEET    4   E 6 GLU X 320  ASP X 328 -1  O  LEU X 322   N  CYS X 314           
SHEET    5   E 6 GLY X 285  ARG X 293 -1  N  ILE X 290   O  LEU X 323           
SHEET    6   E 6 GLU X 352  ASP X 357 -1  O  LEU X 354   N  HIS X 291           
CISPEP   1 THR X  266    PRO X  267          0        -2.73                     
SITE     1 AC1 10 TYR X  59  ASN X 166  MET X 167  LEU X 198                    
SITE     2 AC1 10 TYR X 311  PHE X 326  TRP X 371  GLY X 406                    
SITE     3 AC1 10 TYR X 407  FAD X 434                                          
SITE     1 AC2 40 GLY X   8  GLY X   9  GLY X  10  PHE X  11                    
SITE     2 AC2 40 SER X  12  GLU X  31  GLY X  32  GLY X  37                    
SITE     3 AC2 40 GLY X  38  ARG X  39  ALA X  40  GLY X  56                    
SITE     4 AC2 40 GLY X  57  ALA X  58  TYR X  59  THR X 224                    
SITE     5 AC2 40 VAL X 226  ALA X 254  THR X 255  PRO X 256                    
SITE     6 AC2 40 TRP X 361  LEU X 366  PHE X 367  PRO X 370                    
SITE     7 AC2 40 TRP X 371  GLY X 397  SER X 398  GLY X 406                    
SITE     8 AC2 40 TYR X 407  ILE X 408  HNL X 433  HOH X 453                    
SITE     9 AC2 40 HOH X 469  HOH X 476  HOH X 505  HOH X 530                    
SITE    10 AC2 40 HOH X 674  HOH X 746  HOH X1008  HOH X1011                    
SITE     1 AC3  9 GLY X 105  THR X 115  PHE X 159  MET X 180                    
SITE     2 AC3  9 VAL X 195  HOH X 733  HOH X 741  HOH X1032                    
SITE     3 AC3  9 HOH X1044                                                     
SITE     1 AC4 11 TYR X  59  PHE X  85  TRP X 163  VAL X 195                    
SITE     2 AC4 11 LEU X 198  GLU X 300  TYR X 311  HOH X 660                    
SITE     3 AC4 11 HOH X 693  HOH X 918  HOH X1151                               
CRYST1  163.051  163.051  163.051  90.00  90.00  90.00 P 4 3 2      24          
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      0.006133  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006133  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006133        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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