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Database: PDB
Entry: 3VLY
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Original site: 3VLY 
HEADER    OXIDOREDUCTASE                          05-DEC-11   3VLY              
TITLE     ASSIMILATORY NITRITE REDUCTASE (NII3) - N226K MUTANT - SO3 PARTIAL    
TITLE    2 COMPLEX FROM TOBACCO LEAF                                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: NITRITE REDUCTASE;                                         
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 19-580;                                       
COMPND   5 EC: 1.7.7.1;                                                         
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: NICOTIANA TABACUM;                              
SOURCE   3 ORGANISM_COMMON: TOBACCO;                                            
SOURCE   4 ORGANISM_TAXID: 4097;                                                
SOURCE   5 GENE: NII3;                                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)PLYSS;                            
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET16B                                    
KEYWDS    NII3 N226K MUTANT, SO3 PARTIAL COMPLEX, 3 ALPHA/BETA DOMAINS,         
KEYWDS   2 REDUCTASE, OXIDOREDUCTASE                                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.NAKANO,M.TAKAHASHI,A.SAKAMOTO,H.MORIKAWA,K.KATAYANAGI               
REVDAT   3   27-DEC-23 3VLY    1       COMPND FORMUL                            
REVDAT   2   08-NOV-23 3VLY    1       REMARK SEQADV LINK                       
REVDAT   1   26-SEP-12 3VLY    0                                                
JRNL        AUTH   S.NAKANO,M.TAKAHASHI,A.SAKAMOTO,H.MORIKAWA,K.KATAYANAGI      
JRNL        TITL   X-RAY CRYSTAL STRUCTURE OF A MUTANT ASSIMILATORY NITRITE     
JRNL        TITL 2 REDUCTASE THAT SHOWS SULFITE REDUCTASE-LIKE ACTIVITY         
JRNL        REF    CHEM.BIODIVERS.               V.   9  1989 2012              
JRNL        REFN                   ISSN 1612-1872                               
JRNL        PMID   22976986                                                     
JRNL        DOI    10.1002/CBDV.201100442                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.55 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC                                               
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.55                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 35.99                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 101113                         
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) : 0.164                           
REMARK   3   R VALUE            (WORKING SET) : 0.164                           
REMARK   3   FREE R VALUE                     : 0.176                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 5048                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.55                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.59                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 6933                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.0                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2200                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 358                          
REMARK   3   BIN FREE R VALUE                    : 0.2550                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4248                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 78                                      
REMARK   3   SOLVENT ATOMS            : 922                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 22.60                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 16.61                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.46000                                             
REMARK   3    B22 (A**2) : -0.46000                                             
REMARK   3    B33 (A**2) : 0.91000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.065         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.038         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.001         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.965                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.961                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4427 ; 0.009 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  6003 ; 1.267 ; 1.996       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   537 ; 5.999 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   204 ;32.011 ;24.167       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   790 ;12.032 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    37 ;12.980 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   651 ; 0.085 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3323 ; 0.005 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  2293 ; 0.205 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  3051 ; 0.304 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   751 ; 0.128 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):     4 ; 0.233 ; 0.200       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    39 ; 0.139 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    71 ; 0.179 ; 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):  2679 ; 0.525 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4344 ; 1.030 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1759 ; 1.837 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1647 ; 3.022 ; 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 : 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: NULL                                      
REMARK   4                                                                      
REMARK   4 3VLY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 20-DEC-11.                  
REMARK 100 THE DEPOSITION ID IS D_1000095210.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 07-JUN-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 95                                 
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : PHOTON FACTORY                     
REMARK 200  BEAMLINE                       : AR-NE3A                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : SI(111) DOUBLE-CRYSTAL             
REMARK 200                                   MONOCHROMATOR                      
REMARK 200  OPTICS                         : RH COATED COLLIMATING AND          
REMARK 200                                   FOCUSING SI MIRROR                 
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 270                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 101449                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.550                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 14.20                              
REMARK 200  R MERGE                    (I) : 0.10700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 6.3000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.55                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.61                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 13.70                              
REMARK 200  R MERGE FOR SHELL          (I) : 0.45700                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 5.150                              
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: 3B0G                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 53.58                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.65                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG4000, TRIS-HCL, MGCL2, MPD, NA2SO3,   
REMARK 280  PH 8.5, VAPOR DIFFUSION, TEMPERATURE 277K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 4 21 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   -Y+1/2,X+1/2,Z                                          
REMARK 290       4555   Y+1/2,-X+1/2,Z                                          
REMARK 290       5555   -X+1/2,Y+1/2,-Z                                         
REMARK 290       6555   X+1/2,-Y+1/2,-Z                                         
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z                                                
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       66.82850            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       66.82850            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       66.82850            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       66.82850            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       66.82850            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       66.82850            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       66.82850            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       66.82850            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  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: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A1114  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A1464  LIES ON A SPECIAL POSITION.                          
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A   -28                                                      
REMARK 465     GLY A   -27                                                      
REMARK 465     HIS A   -26                                                      
REMARK 465     HIS A   -25                                                      
REMARK 465     HIS A   -24                                                      
REMARK 465     HIS A   -23                                                      
REMARK 465     HIS A   -22                                                      
REMARK 465     HIS A   -21                                                      
REMARK 465     HIS A   -20                                                      
REMARK 465     HIS A   -19                                                      
REMARK 465     HIS A   -18                                                      
REMARK 465     HIS A   -17                                                      
REMARK 465     SER A   -16                                                      
REMARK 465     SER A   -15                                                      
REMARK 465     GLY A   -14                                                      
REMARK 465     HIS A   -13                                                      
REMARK 465     ILE A   -12                                                      
REMARK 465     GLU A   -11                                                      
REMARK 465     GLY A   -10                                                      
REMARK 465     ARG A    -9                                                      
REMARK 465     HIS A    -8                                                      
REMARK 465     MET A    -7                                                      
REMARK 465     PHE A    -6                                                      
REMARK 465     SER A    -5                                                      
REMARK 465     LYS A    -4                                                      
REMARK 465     ASN A    -3                                                      
REMARK 465     ALA A    -2                                                      
REMARK 465     VAL A    -1                                                      
REMARK 465     LYS A     0                                                      
REMARK 465     LEU A     1                                                      
REMARK 465     HIS A     2                                                      
REMARK 465     ALA A     3                                                      
REMARK 465     THR A     4                                                      
REMARK 465     PRO A     5                                                      
REMARK 465     PRO A     6                                                      
REMARK 465     SER A     7                                                      
REMARK 465     VAL A     8                                                      
REMARK 465     ALA A     9                                                      
REMARK 465     ALA A    10                                                      
REMARK 465     PRO A    11                                                      
REMARK 465     PRO A    12                                                      
REMARK 465     THR A    13                                                      
REMARK 465     GLY A    14                                                      
REMARK 465     ALA A    15                                                      
REMARK 465     PRO A    16                                                      
REMARK 465     GLU A    17                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH A  1133     O    HOH A  1894              1.77            
REMARK 500   OE1  GLU A   383     NH2  ARG A   386              2.05            
REMARK 500   O    HOH A  1040     O    HOH A  1927              2.16            
REMARK 500   O    HOH A  1191     O    HOH A  1344              2.16            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH A  1191     O    HOH A  1906     7555     2.13            
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    VAL A  88      -59.47   -130.70                                   
REMARK 500    GLN A 102       59.96   -151.20                                   
REMARK 500    CYS A 137     -178.38   -176.42                                   
REMARK 500    MET A 175     -139.76     51.76                                   
REMARK 500    ASN A 220       62.02   -117.54                                   
REMARK 500    ASN A 304      117.43    -37.25                                   
REMARK 500    GLN A 332       13.39     57.76                                   
REMARK 500    VAL A 373       28.84     41.91                                   
REMARK 500    ASP A 522       59.72    -93.79                                   
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                               K A 603   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ILE A 371   O                                                      
REMARK 620 2 GLU A 401   O   150.8                                              
REMARK 620 3 GLN A 402   O    77.2  74.6                                        
REMARK 620 4 ASN A 403   OD1  89.1  90.8  75.0                                  
REMARK 620 5 HOH A1013   O   105.6  75.5 105.8 165.2                            
REMARK 620 6 HOH A1027   O   131.1  77.4 141.4  79.4  92.0                      
REMARK 620 7 HOH A1042   O    78.1 126.1 150.8 119.8  66.5  67.7                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 A 602  FE4                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 440   SG                                                     
REMARK 620 2 SF4 A 602   S1  107.7                                              
REMARK 620 3 SF4 A 602   S2  114.6 110.5                                        
REMARK 620 4 SF4 A 602   S3  116.3 104.6 102.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 A 602  FE2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 446   SG                                                     
REMARK 620 2 SF4 A 602   S1  123.9                                              
REMARK 620 3 SF4 A 602   S3  112.5 103.7                                        
REMARK 620 4 SF4 A 602   S4  104.0 104.1 107.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 A 602  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 481   SG                                                     
REMARK 620 2 SF4 A 602   S2  118.3                                              
REMARK 620 3 SF4 A 602   S3  119.5 102.5                                        
REMARK 620 4 SF4 A 602   S4  102.9 104.6 107.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SRM A 601  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 485   SG                                                     
REMARK 620 2 SRM A 601   NA   91.5                                              
REMARK 620 3 SRM A 601   NB   93.5  90.9                                        
REMARK 620 4 SRM A 601   NC   88.3 179.5  88.7                                  
REMARK 620 5 SRM A 601   ND   84.0  89.2 177.6  91.2                            
REMARK 620 6 SO3 A 606   S   175.3  93.0  87.9  87.2  94.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 A 602  FE3                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 485   SG                                                     
REMARK 620 2 SF4 A 602   S1  118.2                                              
REMARK 620 3 SF4 A 602   S2  100.0 109.0                                        
REMARK 620 4 SF4 A 602   S4  119.8 103.7 105.0                                  
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 SRM A 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 A 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A 603                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 604                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 605                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO3 A 606                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3B0G   RELATED DB: PDB                                   
REMARK 900 ASSIMILATORY NITRITE REDUCTASE (NII3) FROM TOBBACO LEAF              
REMARK 900 RELATED ID: 3VLX   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3VLZ   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3VM0   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3VM1   RELATED DB: PDB                                   
DBREF  3VLY A   -6   555  UNP    Q76KB0   Q76KB0_TOBAC    19    580             
SEQADV 3VLY MET A  -28  UNP  Q76KB0              EXPRESSION TAG                 
SEQADV 3VLY GLY A  -27  UNP  Q76KB0              EXPRESSION TAG                 
SEQADV 3VLY HIS A  -26  UNP  Q76KB0              EXPRESSION TAG                 
SEQADV 3VLY HIS A  -25  UNP  Q76KB0              EXPRESSION TAG                 
SEQADV 3VLY HIS A  -24  UNP  Q76KB0              EXPRESSION TAG                 
SEQADV 3VLY HIS A  -23  UNP  Q76KB0              EXPRESSION TAG                 
SEQADV 3VLY HIS A  -22  UNP  Q76KB0              EXPRESSION TAG                 
SEQADV 3VLY HIS A  -21  UNP  Q76KB0              EXPRESSION TAG                 
SEQADV 3VLY HIS A  -20  UNP  Q76KB0              EXPRESSION TAG                 
SEQADV 3VLY HIS A  -19  UNP  Q76KB0              EXPRESSION TAG                 
SEQADV 3VLY HIS A  -18  UNP  Q76KB0              EXPRESSION TAG                 
SEQADV 3VLY HIS A  -17  UNP  Q76KB0              EXPRESSION TAG                 
SEQADV 3VLY SER A  -16  UNP  Q76KB0              EXPRESSION TAG                 
SEQADV 3VLY SER A  -15  UNP  Q76KB0              EXPRESSION TAG                 
SEQADV 3VLY GLY A  -14  UNP  Q76KB0              EXPRESSION TAG                 
SEQADV 3VLY HIS A  -13  UNP  Q76KB0              EXPRESSION TAG                 
SEQADV 3VLY ILE A  -12  UNP  Q76KB0              EXPRESSION TAG                 
SEQADV 3VLY GLU A  -11  UNP  Q76KB0              EXPRESSION TAG                 
SEQADV 3VLY GLY A  -10  UNP  Q76KB0              EXPRESSION TAG                 
SEQADV 3VLY ARG A   -9  UNP  Q76KB0              EXPRESSION TAG                 
SEQADV 3VLY HIS A   -8  UNP  Q76KB0              EXPRESSION TAG                 
SEQADV 3VLY MET A   -7  UNP  Q76KB0              EXPRESSION TAG                 
SEQADV 3VLY LYS A  226  UNP  Q76KB0    ASN   251 ENGINEERED MUTATION            
SEQADV 3VLY ARG A  290  UNP  Q76KB0    LYS   315 CONFLICT                       
SEQRES   1 A  584  MET GLY HIS HIS HIS HIS HIS HIS HIS HIS HIS HIS SER          
SEQRES   2 A  584  SER GLY HIS ILE GLU GLY ARG HIS MET PHE SER LYS ASN          
SEQRES   3 A  584  ALA VAL LYS LEU HIS ALA THR PRO PRO SER VAL ALA ALA          
SEQRES   4 A  584  PRO PRO THR GLY ALA PRO GLU VAL ALA ALA GLU ARG LEU          
SEQRES   5 A  584  GLU PRO ARG VAL GLU GLU LYS ASP GLY TYR TRP ILE LEU          
SEQRES   6 A  584  LYS GLU GLN PHE ARG LYS GLY ILE ASN PRO GLN GLU LYS          
SEQRES   7 A  584  VAL LYS ILE GLU LYS GLU PRO MET LYS LEU PHE MET GLU          
SEQRES   8 A  584  ASN GLY ILE GLU GLU LEU ALA LYS ILE PRO ILE GLU GLU          
SEQRES   9 A  584  ILE ASP GLN SER LYS LEU THR LYS ASP ASP ILE ASP VAL          
SEQRES  10 A  584  ARG LEU LYS TRP LEU GLY LEU PHE HIS ARG ARG LYS ASN          
SEQRES  11 A  584  GLN TYR GLY ARG PHE MET MET ARG LEU LYS LEU PRO ASN          
SEQRES  12 A  584  GLY VAL THR THR SER ALA GLN THR ARG TYR LEU ALA SER          
SEQRES  13 A  584  VAL ILE ARG LYS TYR GLY LYS GLU GLY CYS ALA ASP ILE          
SEQRES  14 A  584  THR THR ARG GLN ASN TRP GLN ILE ARG GLY VAL VAL LEU          
SEQRES  15 A  584  PRO ASP VAL PRO GLU ILE LEU LYS GLY LEU ALA GLU VAL          
SEQRES  16 A  584  GLY LEU THR SER LEU GLN SER GLY MET ASP ASN VAL ARG          
SEQRES  17 A  584  ASN PRO VAL GLY ASN PRO LEU ALA GLY ILE ASP PRO GLU          
SEQRES  18 A  584  GLU ILE VAL ASP THR ARG PRO TYR THR ASN LEU LEU SER          
SEQRES  19 A  584  GLN PHE ILE THR GLY ASN SER ARG GLY ASN PRO ALA VAL          
SEQRES  20 A  584  SER ASN LEU PRO ARG LYS TRP LYS PRO CYS VAL VAL GLY          
SEQRES  21 A  584  SER HIS ASP LEU TYR GLU HIS PRO HIS ILE ASN ASP LEU          
SEQRES  22 A  584  ALA TYR MET PRO ALA THR LYS ASP GLY ARG PHE GLY PHE          
SEQRES  23 A  584  ASN LEU LEU VAL GLY GLY PHE PHE SER ALA LYS ARG CYS          
SEQRES  24 A  584  ASP GLU ALA ILE PRO LEU ASP ALA TRP VAL PRO ALA ASP          
SEQRES  25 A  584  ASP VAL VAL PRO VAL CYS ARG ALA ILE LEU GLU ALA PHE          
SEQRES  26 A  584  ARG ASP LEU GLY PHE ARG GLY ASN ARG GLN LYS CYS ARG          
SEQRES  27 A  584  MET MET TRP LEU ILE ASP GLU LEU GLY VAL GLU GLY PHE          
SEQRES  28 A  584  ARG ALA GLU VAL GLU LYS ARG MET PRO GLN GLN GLN LEU          
SEQRES  29 A  584  GLU ARG ALA SER PRO GLU ASP LEU VAL GLN LYS GLN TRP          
SEQRES  30 A  584  GLU ARG ARG ASP TYR LEU GLY VAL HIS PRO GLN LYS GLN          
SEQRES  31 A  584  GLU GLY TYR SER PHE ILE GLY LEU HIS ILE PRO VAL GLY          
SEQRES  32 A  584  ARG VAL GLN ALA ASP ASP MET ASP GLU LEU ALA ARG LEU          
SEQRES  33 A  584  ALA ASP GLU TYR GLY SER GLY GLU ILE ARG LEU THR VAL          
SEQRES  34 A  584  GLU GLN ASN ILE ILE ILE PRO ASN ILE GLU THR SER LYS          
SEQRES  35 A  584  ILE GLU ALA LEU LEU LYS GLU PRO VAL LEU SER THR PHE          
SEQRES  36 A  584  SER PRO ASP PRO PRO ILE LEU MET LYS GLY LEU VAL ALA          
SEQRES  37 A  584  CYS THR GLY ASN GLN PHE CYS GLY GLN ALA ILE ILE GLU          
SEQRES  38 A  584  THR LYS ALA ARG SER LEU LYS ILE THR GLU GLU VAL GLN          
SEQRES  39 A  584  ARG GLN VAL SER LEU THR LYS PRO VAL ARG MET HIS TRP          
SEQRES  40 A  584  THR GLY CYS PRO ASN THR CYS ALA GLN VAL GLN VAL ALA          
SEQRES  41 A  584  ASP ILE GLY PHE MET GLY CYS LEU THR ARG ASP LYS ASN          
SEQRES  42 A  584  GLY LYS THR VAL GLU GLY ALA ASP VAL PHE LEU GLY GLY          
SEQRES  43 A  584  ARG ILE GLY SER ASP SER HIS LEU GLY GLU VAL TYR LYS          
SEQRES  44 A  584  LYS ALA VAL PRO CYS ASP ASP LEU VAL PRO LEU VAL VAL          
SEQRES  45 A  584  ASP LEU LEU VAL ASN ASN PHE GLY ALA VAL PRO ARG              
HET    SRM  A 601      63                                                       
HET    SF4  A 602       8                                                       
HET      K  A 603       1                                                       
HET     CL  A 604       1                                                       
HET     CL  A 605       1                                                       
HET    SO3  A 606       4                                                       
HETNAM     SRM SIROHEME                                                         
HETNAM     SF4 IRON/SULFUR CLUSTER                                              
HETNAM       K POTASSIUM ION                                                    
HETNAM      CL CHLORIDE ION                                                     
HETNAM     SO3 SULFITE ION                                                      
FORMUL   2  SRM    C42 H44 FE N4 O16                                            
FORMUL   3  SF4    FE4 S4                                                       
FORMUL   4    K    K 1+                                                         
FORMUL   5   CL    2(CL 1-)                                                     
FORMUL   7  SO3    O3 S 2-                                                      
FORMUL   8  HOH   *922(H2 O)                                                    
HELIX    1   1 ALA A   19  GLU A   24  5                                   6    
HELIX    2   2 GLU A   38  ARG A   41  5                                   4    
HELIX    3   3 ASN A   45  LYS A   54  1                                  10    
HELIX    4   4 MET A   57  GLU A   62  1                                   6    
HELIX    5   5 GLY A   64  ALA A   69  1                                   6    
HELIX    6   6 PRO A   72  ASP A   77  1                                   6    
HELIX    7   7 SER A   79  VAL A   88  1                                  10    
HELIX    8   8 ARG A   89  LEU A   93  5                                   5    
HELIX    9   9 LEU A  112  ASN A  114  5                                   3    
HELIX   10  10 SER A  119  TYR A  132  1                                  14    
HELIX   11  11 GLY A  133  GLY A  136  5                                   4    
HELIX   12  12 ASP A  155  VAL A  166  1                                  12    
HELIX   13  13 THR A  197  GLY A  210  1                                  14    
HELIX   14  14 ASN A  215  SER A  219  5                                   5    
HELIX   15  15 HIS A  238  ASN A  242  5                                   5    
HELIX   16  16 ASP A  284  GLY A  300  1                                  17    
HELIX   17  17 ASN A  304  CYS A  308  5                                   5    
HELIX   18  18 ARG A  309  ARG A  329  1                                  21    
HELIX   19  19 MET A  330  GLN A  334  5                                   5    
HELIX   20  20 ILE A  371  VAL A  373  5                                   3    
HELIX   21  21 GLN A  377  GLY A  392  1                                  16    
HELIX   22  22 LYS A  413  LYS A  419  1                                   7    
HELIX   23  23 GLU A  420  THR A  425  5                                   6    
HELIX   24  24 PRO A  431  GLY A  436  1                                   6    
HELIX   25  25 THR A  441  PHE A  445  5                                   5    
HELIX   26  26 THR A  453  GLN A  467  1                                  15    
HELIX   27  27 GLN A  487  ALA A  491  5                                   5    
HELIX   28  28 ASP A  537  PHE A  550  1                                  14    
SHEET    1   A 2 VAL A  27  LYS A  30  0                                        
SHEET    2   A 2 TYR A  33  LEU A  36 -1  O  TYR A  33   N  LYS A  30           
SHEET    1   B 5 LEU A  95  HIS A  97  0                                        
SHEET    2   B 5 ARG A 105  ARG A 109 -1  O  MET A 107   N  PHE A  96           
SHEET    3   B 5 TRP A 146  VAL A 152 -1  O  ILE A 148   N  MET A 108           
SHEET    4   B 5 CYS A 137  ILE A 140 -1  N  ASP A 139   O  GLN A 147           
SHEET    5   B 5 ARG A 375  VAL A 376 -1  O  VAL A 376   N  ALA A 138           
SHEET    1   C 5 VAL A 116  THR A 118  0                                        
SHEET    2   C 5 GLU A 395  LEU A 398 -1  O  ILE A 396   N  THR A 117           
SHEET    3   C 5 ILE A 404  GLU A 410 -1  O  ILE A 405   N  ARG A 397           
SHEET    4   C 5 TYR A 364  LEU A 369 -1  N  SER A 365   O  ILE A 409           
SHEET    5   C 5 GLY A 355  PRO A 358 -1  N  HIS A 357   O  PHE A 366           
SHEET    1   D 4 PRO A 227  VAL A 229  0                                        
SHEET    2   D 4 LEU A 244  LYS A 251  1  O  LEU A 244   N  CYS A 228           
SHEET    3   D 4 ARG A 254  VAL A 261 -1  O  ASN A 258   N  MET A 247           
SHEET    4   D 4 ILE A 274  PRO A 281 -1  O  ILE A 274   N  VAL A 261           
SHEET    1   E 5 VAL A 438  ALA A 439  0                                        
SHEET    2   E 5 MET A 476  THR A 479  1  O  TRP A 478   N  VAL A 438           
SHEET    3   E 5 ILE A 493  ARG A 501  1  O  PHE A 495   N  THR A 479           
SHEET    4   E 5 THR A 507  LEU A 515 -1  O  VAL A 508   N  THR A 500           
SHEET    5   E 5 GLU A 527  PRO A 534 -1  O  TYR A 529   N  VAL A 513           
SHEET    1   F 2 VAL A 468  SER A 469  0                                        
SHEET    2   F 2 VAL A 553  PRO A 554 -1  O  VAL A 553   N  SER A 469           
LINK         O   ILE A 371                 K     K A 603     1555   1555  2.58  
LINK         O   GLU A 401                 K     K A 603     1555   1555  2.86  
LINK         O   GLN A 402                 K     K A 603     1555   1555  2.85  
LINK         OD1 ASN A 403                 K     K A 603     1555   1555  2.57  
LINK         SG  CYS A 440                FE4  SF4 A 602     1555   1555  2.30  
LINK         SG  CYS A 446                FE2  SF4 A 602     1555   1555  2.29  
LINK         SG  CYS A 481                FE1  SF4 A 602     1555   1555  2.28  
LINK         SG  CYS A 485                FE   SRM A 601     1555   1555  2.39  
LINK         SG  CYS A 485                FE3  SF4 A 602     1555   1555  2.30  
LINK        FE   SRM A 601                 S   SO3 A 606     1555   1555  2.29  
LINK         K     K A 603                 O   HOH A1013     1555   1555  2.46  
LINK         K     K A 603                 O   HOH A1027     1555   1555  2.67  
LINK         K     K A 603                 O   HOH A1042     1555   1555  3.17  
SITE     1 AC1 45 PHE A  96  ARG A  98  ARG A 109  THR A 141                    
SITE     2 AC1 45 THR A 142  ARG A 143  ASN A 145  GLN A 147                    
SITE     3 AC1 45 ARG A 149  ARG A 223  LYS A 224  LYS A 226                    
SITE     4 AC1 45 PHE A 264  PHE A 265  SER A 266  ARG A 309                    
SITE     5 AC1 45 GLN A 402  CYS A 440  THR A 441  CYS A 446                    
SITE     6 AC1 45 GLN A 448  ASN A 483  THR A 484  CYS A 485                    
SITE     7 AC1 45 GLN A 487  SF4 A 602  SO3 A 606  HOH A1004                    
SITE     8 AC1 45 HOH A1005  HOH A1022  HOH A1039  HOH A1040                    
SITE     9 AC1 45 HOH A1054  HOH A1060  HOH A1065  HOH A1087                    
SITE    10 AC1 45 HOH A1133  HOH A1166  HOH A1188  HOH A1221                    
SITE    11 AC1 45 HOH A1285  HOH A1429  HOH A1471  HOH A1894                    
SITE    12 AC1 45 HOH A1927                                                     
SITE     1 AC2 10 CYS A 440  CYS A 446  ALA A 449  THR A 479                    
SITE     2 AC2 10 GLY A 480  CYS A 481  ASN A 483  THR A 484                    
SITE     3 AC2 10 CYS A 485  SRM A 601                                          
SITE     1 AC3  6 ILE A 371  GLU A 401  GLN A 402  ASN A 403                    
SITE     2 AC3  6 HOH A1013  HOH A1027                                          
SITE     1 AC4  5 PHE A  96  MET A 175  ARG A 179  HOH A1054                    
SITE     2 AC4  5 HOH A1285                                                     
SITE     1 AC5  3 ARG A  99  LYS A 100  HOH A1133                               
SITE     1 AC6  7 ARG A 109  ARG A 179  LYS A 224  LYS A 226                    
SITE     2 AC6  7 SRM A 601  HOH A1022  HOH A1054                               
CRYST1  133.657  133.657   77.823  90.00  90.00  90.00 P 4 21 2      8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.007482  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007482  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012850        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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