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Database: PDB
Entry: 3CNT
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Original site: 3CNT 
HEADER    OXIDOREDUCTASE                          26-MAR-08   3CNT              
TITLE     CRYSTAL STRUCTURE OF FMS1 IN COMPLEX WITH R-BZ-MESPERMIDINE           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: FMS1;                                                      
COMPND   3 CHAIN: B, A;                                                         
COMPND   4 EC: 1.5.3.11;                                                        
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;                       
SOURCE   3 ORGANISM_COMMON: BAKER'S YEAST;                                      
SOURCE   4 ORGANISM_TAXID: 4932;                                                
SOURCE   5 GENE: FMS1;                                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET28B                                    
KEYWDS    FMS1, POLYAMINE OXIDASE, N1-BENZOYL-1-METHYLSPERMIDINE, COMPLEX,      
KEYWDS   2 OXIDOREDUCTASE                                                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Q.HUANG,Q.HAO                                                         
REVDAT   3   30-AUG-23 3CNT    1       REMARK SEQADV                            
REVDAT   2   24-FEB-09 3CNT    1       VERSN                                    
REVDAT   1   22-APR-08 3CNT    0                                                
JRNL        AUTH   Q.HUANG,Q.HAO                                                
JRNL        TITL   CRYSTAL STRUCTURE OF FMS1 IN COMPLEX WITH R-BZ-MESPERMIDINE  
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS                                                  
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 91.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 31701                          
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 SET) : 0.223                           
REMARK   3   FREE R VALUE                     : 0.290                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 9.200                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3170                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.70                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.87                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 79.50                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3520                       
REMARK   3   BIN FREE R VALUE                    : 0.4050                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 453                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.019                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 7723                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 125                                     
REMARK   3   SOLVENT ATOMS            : 51                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 49.80                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 58.97                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.06800                                              
REMARK   3    B22 (A**2) : -4.56300                                             
REMARK   3    B33 (A**2) : 3.49500                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -21.84200                                            
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.36                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.55                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.008                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.342                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : 40.68                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : CNS_TOPPAR:PROTEIN_REP.PARAM                   
REMARK   3  PARAMETER FILE  2  : CNS_TOPPAR:WATER.PARAM                         
REMARK   3  PARAMETER FILE  3  : FADTMP.PARAM                                   
REMARK   3  PARAMETER FILE  4  : SUB7R.PARAM                                    
REMARK   3  PARAMETER FILE  5  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3  TOPOLOGY FILE  2   : NULL                                           
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3  TOPOLOGY FILE  4   : NULL                                           
REMARK   3  TOPOLOGY FILE  5   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3CNT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-APR-08.                  
REMARK 100 THE DEPOSITION ID IS D_1000046999.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 04-MAY-06                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : CHESS                              
REMARK 200  BEAMLINE                       : F2                                 
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9779                             
REMARK 200  MONOCHROMATOR                  : GRAPHITE                           
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 40569                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500                              
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     (%) : 93.2                               
REMARK 200  DATA REDUNDANCY                : 3.000                              
REMARK 200  R MERGE                    (I) : 0.06500                            
REMARK 200  R SYM                      (I) : 0.09100                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.54                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 51.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.52700                            
REMARK 200  R SYM FOR SHELL            (I) : 0.64200                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: CNS                                                   
REMARK 200 STARTING MODEL: 1YY5                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 54.51                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.70                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG4000, 0.2M LI2SO4, 0.1M TRIS      
REMARK 280  -HCL, PH8.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 295K        
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
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+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       80.92900            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       51.20650            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       80.92900            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       51.20650            
REMARK 290   SMTRY3   4  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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 5940 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 38470 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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 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 B     1                                                      
REMARK 465     ASN B     2                                                      
REMARK 465     THR B     3                                                      
REMARK 465     VAL B     4                                                      
REMARK 465     SER B     5                                                      
REMARK 465     PRO B     6                                                      
REMARK 465     ALA B     7                                                      
REMARK 465     GLY B   135                                                      
REMARK 465     VAL B   136                                                      
REMARK 465     SER B   137                                                      
REMARK 465     ASP B   138                                                      
REMARK 465     ASP B   344                                                      
REMARK 465     SER B   345                                                      
REMARK 465     GLN B   346                                                      
REMARK 465     LYS B   347                                                      
REMARK 465     HIS B   348                                                      
REMARK 465     HIS B   512                                                      
REMARK 465     HIS B   513                                                      
REMARK 465     HIS B   514                                                      
REMARK 465     HIS B   515                                                      
REMARK 465     HIS B   516                                                      
REMARK 465     MET A     1                                                      
REMARK 465     ASN A     2                                                      
REMARK 465     THR A     3                                                      
REMARK 465     VAL A     4                                                      
REMARK 465     ASP A   344                                                      
REMARK 465     SER A   345                                                      
REMARK 465     GLN A   346                                                      
REMARK 465     LYS A   347                                                      
REMARK 465     HIS A   348                                                      
REMARK 465     PRO A   420                                                      
REMARK 465     ILE A   421                                                      
REMARK 465     GLU A   422                                                      
REMARK 465     ASN A   423                                                      
REMARK 465     ILE A   424                                                      
REMARK 465     ALA A   425                                                      
REMARK 465     ASN A   426                                                      
REMARK 465     HIS A   514                                                      
REMARK 465     HIS A   515                                                      
REMARK 465     HIS A   516                                                      
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     LYS B   8    CG   CD   CE   NZ                                   
REMARK 470     ARG B  87    CB   CG   CD   NE   CZ   NH1  NH2                   
REMARK 470     LYS B 111    CG   CD   CE   NZ                                   
REMARK 470     GLU B 112    CG   CD   OE1  OE2                                  
REMARK 470     GLN B 132    CB   CG   CD   OE1  NE2                             
REMARK 470     LEU B 134    CB   CG   CD1  CD2                                  
REMARK 470     LYS B 185    CG   CD   CE   NZ                                   
REMARK 470     ASN B 200    CB   CG   OD1  ND2                                  
REMARK 470     GLN B 206    CG   CD   OE1  NE2                                  
REMARK 470     GLN B 214    CG   CD   OE1  NE2                                  
REMARK 470     LYS B 218    CG   CD   CE   NZ                                   
REMARK 470     ARG B 228    CB   CG   CD   NE   CZ   NH1  NH2                   
REMARK 470     GLU B 229    CB   CG   CD   OE1  OE2                             
REMARK 470     SER B 231    OG                                                  
REMARK 470     LYS B 232    CB   CG   CD   CE   NZ                              
REMARK 470     ASN B 233    CG   OD1  ND2                                       
REMARK 470     GLN B 263    CB   CG   CD   OE1  NE2                             
REMARK 470     PRO B 264    CB   CG   CD                                        
REMARK 470     GLU B 265    CB   CG   CD   OE1  OE2                             
REMARK 470     LYS B 266    CB   CG   CD   CE   NZ                              
REMARK 470     ALA B 285    CB                                                  
REMARK 470     LYS B 288    CG   CD   CE   NZ                                   
REMARK 470     ILE B 289    CB   CG1  CG2  CD1                                  
REMARK 470     HIS B 290    CB   CG   ND1  CD2  CE1  NE2                        
REMARK 470     PHE B 291    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     GLU B 331    CG   CD   OE1  OE2                                  
REMARK 470     LEU B 333    CG   CD1  CD2                                       
REMARK 470     ASP B 337    CB   CG   OD1  OD2                                  
REMARK 470     GLU B 341    CB   CG   CD   OE1  OE2                             
REMARK 470     ARG B 342    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B 343    CB   CG   CD   OE1  OE2                             
REMARK 470     THR B 349    OG1  CG2                                            
REMARK 470     SER B 350    OG                                                  
REMARK 470     ILE B 424    CB   CG1  CG2  CD1                                  
REMARK 470     ALA B 427    CB                                                  
REMARK 470     ASN B 428    CG   OD1  ND2                                       
REMARK 470     ALA B 449    CB                                                  
REMARK 470     VAL B 460    CG1  CG2                                            
REMARK 470     ASN B 468    CG   OD1  ND2                                       
REMARK 470     SER B 472    CB   OG                                             
REMARK 470     HIS B 511    CB   CG   ND1  CD2  CE1  NE2                        
REMARK 470     GLU A 112    CG   CD   OE1  OE2                                  
REMARK 470     ASN A 120    CG   OD1  ND2                                       
REMARK 470     HIS A 131    CG   ND1  CD2  CE1  NE2                             
REMARK 470     GLN A 132    CB   CG   CD   OE1  NE2                             
REMARK 470     GLN A 143    CG   CD   OE1  NE2                                  
REMARK 470     ASN A 200    CB   CG   OD1  ND2                                  
REMARK 470     LYS A 232    CB   CG   CD   CE   NZ                              
REMARK 470     LYS A 266    CG   CD   CE   NZ                                   
REMARK 470     ALA A 330    CB                                                  
REMARK 470     GLU A 331    CG   CD   OE1  OE2                                  
REMARK 470     LEU A 333    CG   CD1  CD2                                       
REMARK 470     ASP A 337    CG   OD1  OD2                                       
REMARK 470     SER A 338    CB   OG                                             
REMARK 470     GLU A 341    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 342    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 343    CG   CD   OE1  OE2                                  
REMARK 470     ALA A 427    CB                                                  
REMARK 470     ASN A 428    CB   CG   OD1  ND2                                  
REMARK 470     LYS A 429    CG   CD   CE   NZ                                   
REMARK 470     ASP A 458    CB   CG   OD1  OD2                                  
REMARK 470     GLU A 510    CB   CG   CD   OE1  OE2                             
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   NH2  ARG A   269     NH2  ARG A   269     2555     1.98            
REMARK 500   NE   ARG A   269     NE   ARG A   269     2555     2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    PRO B 420   C   -  N   -  CA  ANGL. DEV. =  11.1 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP B  34       72.70     41.76                                   
REMARK 500    VAL B  44     -146.79    -90.63                                   
REMARK 500    GLN B  55       28.98     34.77                                   
REMARK 500    SER B  64      -20.09   -155.95                                   
REMARK 500    THR B  69       12.07    -62.55                                   
REMARK 500    ASN B  72      101.47    -59.80                                   
REMARK 500    ASN B  84      -73.89    -59.83                                   
REMARK 500    VAL B 107       10.10   -140.63                                   
REMARK 500    GLN B 132       74.18     51.38                                   
REMARK 500    PHE B 189     -178.86    -68.70                                   
REMARK 500    ASN B 200      103.53     86.75                                   
REMARK 500    ASN B 215       15.91    -68.66                                   
REMARK 500    SER B 220       41.44     70.31                                   
REMARK 500    SER B 225      130.20   -173.56                                   
REMARK 500    SER B 231       58.35    -65.41                                   
REMARK 500    LYS B 232       27.12     39.03                                   
REMARK 500    GLU B 239      -66.38    -23.17                                   
REMARK 500    THR B 242      107.54    -21.25                                   
REMARK 500    LYS B 266       71.45    -57.14                                   
REMARK 500    ASN B 267      -34.80   -145.24                                   
REMARK 500    LEU B 268      121.66    -21.72                                   
REMARK 500    ARG B 269      140.71    -36.30                                   
REMARK 500    PRO B 277      174.75    -56.69                                   
REMARK 500    PHE B 286       27.25    -76.50                                   
REMARK 500    ILE B 289     -164.44     28.37                                   
REMARK 500    HIS B 290       16.72    139.05                                   
REMARK 500    GLU B 302      -71.16    -56.28                                   
REMARK 500    CYS B 305       67.15   -161.72                                   
REMARK 500    ASN B 308       31.92    -98.77                                   
REMARK 500    GLU B 341      135.06    141.58                                   
REMARK 500    ARG B 342     -135.56    179.59                                   
REMARK 500    SER B 350      110.27     86.67                                   
REMARK 500    CYS B 353       -9.64    -58.73                                   
REMARK 500    LEU B 363       -5.19    -58.98                                   
REMARK 500    ALA B 370       68.87    -65.42                                   
REMARK 500    SER B 411     -159.79   -148.10                                   
REMARK 500    PRO B 420      148.25    -35.15                                   
REMARK 500    ILE B 421       78.98   -154.48                                   
REMARK 500    GLU B 422      117.76    -36.96                                   
REMARK 500    ALA B 425      -19.16    -46.03                                   
REMARK 500    ASN B 426       41.07    -83.44                                   
REMARK 500    ALA B 427      -83.66    -55.10                                   
REMARK 500    LYS B 429      138.24    -34.61                                   
REMARK 500    ARG B 433      -63.95   -101.51                                   
REMARK 500    SER B 446      -66.03   -134.62                                   
REMARK 500    PRO B 455       95.50    -51.25                                   
REMARK 500    VAL B 460      -59.64   -155.49                                   
REMARK 500    ASP B 471     -157.28   -154.33                                   
REMARK 500    ALA B 486      134.36    -39.30                                   
REMARK 500    ALA A   7      126.21    -38.41                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      89 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD A 517                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD B 517                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SP9 B 518                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1YY5   RELATED DB: PDB                                   
REMARK 900 NATIVE FMS1                                                          
REMARK 900 RELATED ID: 1XPQ   RELATED DB: PDB                                   
REMARK 900 FMS1 IN COMPLEX WITH ITS NATIVE SUBSTRATE SPERMINE                   
REMARK 900 RELATED ID: 3CN8   RELATED DB: PDB                                   
REMARK 900 FMS1 IN COMPLEX WITH SPERMIDINE                                      
REMARK 900 RELATED ID: 3CND   RELATED DB: PDB                                   
REMARK 900 FMS1 IN COMPLEX WITH N1-ACSPERMINE                                   
REMARK 900 RELATED ID: 3CNP   RELATED DB: PDB                                   
REMARK 900 FMS1 IN COMPLEX WITH S-N1-ACMESPERMIDINE                             
REMARK 900 RELATED ID: 3CNS   RELATED DB: PDB                                   
REMARK 900 FMS1 IN COMPLEX WITH S-BZ-MESPERMIDINE                               
DBREF  3CNT A    1   508  UNP    P50264   FMS1_YEAST       1    508             
DBREF  3CNT B    1   508  UNP    P50264   FMS1_YEAST       1    508             
SEQADV 3CNT LEU B  509  UNP  P50264              EXPRESSION TAG                 
SEQADV 3CNT GLU B  510  UNP  P50264              EXPRESSION TAG                 
SEQADV 3CNT HIS B  511  UNP  P50264              EXPRESSION TAG                 
SEQADV 3CNT HIS B  512  UNP  P50264              EXPRESSION TAG                 
SEQADV 3CNT HIS B  513  UNP  P50264              EXPRESSION TAG                 
SEQADV 3CNT HIS B  514  UNP  P50264              EXPRESSION TAG                 
SEQADV 3CNT HIS B  515  UNP  P50264              EXPRESSION TAG                 
SEQADV 3CNT HIS B  516  UNP  P50264              EXPRESSION TAG                 
SEQADV 3CNT LEU A  509  UNP  P50264              EXPRESSION TAG                 
SEQADV 3CNT GLU A  510  UNP  P50264              EXPRESSION TAG                 
SEQADV 3CNT HIS A  511  UNP  P50264              EXPRESSION TAG                 
SEQADV 3CNT HIS A  512  UNP  P50264              EXPRESSION TAG                 
SEQADV 3CNT HIS A  513  UNP  P50264              EXPRESSION TAG                 
SEQADV 3CNT HIS A  514  UNP  P50264              EXPRESSION TAG                 
SEQADV 3CNT HIS A  515  UNP  P50264              EXPRESSION TAG                 
SEQADV 3CNT HIS A  516  UNP  P50264              EXPRESSION TAG                 
SEQRES   1 B  516  MET ASN THR VAL SER PRO ALA LYS LYS LYS VAL ILE ILE          
SEQRES   2 B  516  ILE GLY ALA GLY ILE ALA GLY LEU LYS ALA ALA SER THR          
SEQRES   3 B  516  LEU HIS GLN ASN GLY ILE GLN ASP CYS LEU VAL LEU GLU          
SEQRES   4 B  516  ALA ARG ASP ARG VAL GLY GLY ARG LEU GLN THR VAL THR          
SEQRES   5 B  516  GLY TYR GLN GLY ARG LYS TYR ASP ILE GLY ALA SER TRP          
SEQRES   6 B  516  HIS HIS ASP THR LEU THR ASN PRO LEU PHE LEU GLU GLU          
SEQRES   7 B  516  ALA GLN LEU SER LEU ASN ASP GLY ARG THR ARG PHE VAL          
SEQRES   8 B  516  PHE ASP ASP ASP ASN PHE ILE TYR ILE ASP GLU GLU ARG          
SEQRES   9 B  516  GLY ARG VAL ASP HIS ASP LYS GLU LEU LEU LEU GLU ILE          
SEQRES  10 B  516  VAL ASP ASN GLU MET SER LYS PHE ALA GLU LEU GLU PHE          
SEQRES  11 B  516  HIS GLN HIS LEU GLY VAL SER ASP CYS SER PHE PHE GLN          
SEQRES  12 B  516  LEU VAL MET LYS TYR LEU LEU GLN ARG ARG GLN PHE LEU          
SEQRES  13 B  516  THR ASN ASP GLN ILE ARG TYR LEU PRO GLN LEU CYS ARG          
SEQRES  14 B  516  TYR LEU GLU LEU TRP HIS GLY LEU ASP TRP LYS LEU LEU          
SEQRES  15 B  516  SER ALA LYS ASP THR TYR PHE GLY HIS GLN GLY ARG ASN          
SEQRES  16 B  516  ALA PHE ALA LEU ASN TYR ASP SER VAL VAL GLN ARG ILE          
SEQRES  17 B  516  ALA GLN SER PHE PRO GLN ASN TRP LEU LYS LEU SER CYS          
SEQRES  18 B  516  GLU VAL LYS SER ILE THR ARG GLU PRO SER LYS ASN VAL          
SEQRES  19 B  516  THR VAL ASN CYS GLU ASP GLY THR VAL TYR ASN ALA ASP          
SEQRES  20 B  516  TYR VAL ILE ILE THR VAL PRO GLN SER VAL LEU ASN LEU          
SEQRES  21 B  516  SER VAL GLN PRO GLU LYS ASN LEU ARG GLY ARG ILE GLU          
SEQRES  22 B  516  PHE GLN PRO PRO LEU LYS PRO VAL ILE GLN ASP ALA PHE          
SEQRES  23 B  516  ASP LYS ILE HIS PHE GLY ALA LEU GLY LYS VAL ILE PHE          
SEQRES  24 B  516  GLU PHE GLU GLU CYS CYS TRP SER ASN GLU SER SER LYS          
SEQRES  25 B  516  ILE VAL THR LEU ALA ASN SER THR ASN GLU PHE VAL GLU          
SEQRES  26 B  516  ILE VAL ARG ASN ALA GLU ASN LEU ASP GLU LEU ASP SER          
SEQRES  27 B  516  MET LEU GLU ARG GLU ASP SER GLN LYS HIS THR SER VAL          
SEQRES  28 B  516  THR CYS TRP SER GLN PRO LEU PHE PHE VAL ASN LEU SER          
SEQRES  29 B  516  LYS SER THR GLY VAL ALA SER PHE MET MET LEU MET GLN          
SEQRES  30 B  516  ALA PRO LEU THR ASN HIS ILE GLU SER ILE ARG GLU ASP          
SEQRES  31 B  516  LYS GLU ARG LEU PHE SER PHE PHE GLN PRO VAL LEU ASN          
SEQRES  32 B  516  LYS ILE MET LYS CYS LEU ASP SER GLU ASP VAL ILE ASP          
SEQRES  33 B  516  GLY MET ARG PRO ILE GLU ASN ILE ALA ASN ALA ASN LYS          
SEQRES  34 B  516  PRO VAL LEU ARG ASN ILE ILE VAL SER ASN TRP THR ARG          
SEQRES  35 B  516  ASP PRO TYR SER ARG GLY ALA TYR SER ALA CYS PHE PRO          
SEQRES  36 B  516  GLY ASP ASP PRO VAL ASP MET VAL VAL ALA MET SER ASN          
SEQRES  37 B  516  GLY GLN ASP SER ARG ILE ARG PHE ALA GLY GLU HIS THR          
SEQRES  38 B  516  ILE MET ASP GLY ALA GLY CYS ALA TYR GLY ALA TRP GLU          
SEQRES  39 B  516  SER GLY ARG ARG GLU ALA THR ARG ILE SER ASP LEU LEU          
SEQRES  40 B  516  LYS LEU GLU HIS HIS HIS HIS HIS HIS                          
SEQRES   1 A  516  MET ASN THR VAL SER PRO ALA LYS LYS LYS VAL ILE ILE          
SEQRES   2 A  516  ILE GLY ALA GLY ILE ALA GLY LEU LYS ALA ALA SER THR          
SEQRES   3 A  516  LEU HIS GLN ASN GLY ILE GLN ASP CYS LEU VAL LEU GLU          
SEQRES   4 A  516  ALA ARG ASP ARG VAL GLY GLY ARG LEU GLN THR VAL THR          
SEQRES   5 A  516  GLY TYR GLN GLY ARG LYS TYR ASP ILE GLY ALA SER TRP          
SEQRES   6 A  516  HIS HIS ASP THR LEU THR ASN PRO LEU PHE LEU GLU GLU          
SEQRES   7 A  516  ALA GLN LEU SER LEU ASN ASP GLY ARG THR ARG PHE VAL          
SEQRES   8 A  516  PHE ASP ASP ASP ASN PHE ILE TYR ILE ASP GLU GLU ARG          
SEQRES   9 A  516  GLY ARG VAL ASP HIS ASP LYS GLU LEU LEU LEU GLU ILE          
SEQRES  10 A  516  VAL ASP ASN GLU MET SER LYS PHE ALA GLU LEU GLU PHE          
SEQRES  11 A  516  HIS GLN HIS LEU GLY VAL SER ASP CYS SER PHE PHE GLN          
SEQRES  12 A  516  LEU VAL MET LYS TYR LEU LEU GLN ARG ARG GLN PHE LEU          
SEQRES  13 A  516  THR ASN ASP GLN ILE ARG TYR LEU PRO GLN LEU CYS ARG          
SEQRES  14 A  516  TYR LEU GLU LEU TRP HIS GLY LEU ASP TRP LYS LEU LEU          
SEQRES  15 A  516  SER ALA LYS ASP THR TYR PHE GLY HIS GLN GLY ARG ASN          
SEQRES  16 A  516  ALA PHE ALA LEU ASN TYR ASP SER VAL VAL GLN ARG ILE          
SEQRES  17 A  516  ALA GLN SER PHE PRO GLN ASN TRP LEU LYS LEU SER CYS          
SEQRES  18 A  516  GLU VAL LYS SER ILE THR ARG GLU PRO SER LYS ASN VAL          
SEQRES  19 A  516  THR VAL ASN CYS GLU ASP GLY THR VAL TYR ASN ALA ASP          
SEQRES  20 A  516  TYR VAL ILE ILE THR VAL PRO GLN SER VAL LEU ASN LEU          
SEQRES  21 A  516  SER VAL GLN PRO GLU LYS ASN LEU ARG GLY ARG ILE GLU          
SEQRES  22 A  516  PHE GLN PRO PRO LEU LYS PRO VAL ILE GLN ASP ALA PHE          
SEQRES  23 A  516  ASP LYS ILE HIS PHE GLY ALA LEU GLY LYS VAL ILE PHE          
SEQRES  24 A  516  GLU PHE GLU GLU CYS CYS TRP SER ASN GLU SER SER LYS          
SEQRES  25 A  516  ILE VAL THR LEU ALA ASN SER THR ASN GLU PHE VAL GLU          
SEQRES  26 A  516  ILE VAL ARG ASN ALA GLU ASN LEU ASP GLU LEU ASP SER          
SEQRES  27 A  516  MET LEU GLU ARG GLU ASP SER GLN LYS HIS THR SER VAL          
SEQRES  28 A  516  THR CYS TRP SER GLN PRO LEU PHE PHE VAL ASN LEU SER          
SEQRES  29 A  516  LYS SER THR GLY VAL ALA SER PHE MET MET LEU MET GLN          
SEQRES  30 A  516  ALA PRO LEU THR ASN HIS ILE GLU SER ILE ARG GLU ASP          
SEQRES  31 A  516  LYS GLU ARG LEU PHE SER PHE PHE GLN PRO VAL LEU ASN          
SEQRES  32 A  516  LYS ILE MET LYS CYS LEU ASP SER GLU ASP VAL ILE ASP          
SEQRES  33 A  516  GLY MET ARG PRO ILE GLU ASN ILE ALA ASN ALA ASN LYS          
SEQRES  34 A  516  PRO VAL LEU ARG ASN ILE ILE VAL SER ASN TRP THR ARG          
SEQRES  35 A  516  ASP PRO TYR SER ARG GLY ALA TYR SER ALA CYS PHE PRO          
SEQRES  36 A  516  GLY ASP ASP PRO VAL ASP MET VAL VAL ALA MET SER ASN          
SEQRES  37 A  516  GLY GLN ASP SER ARG ILE ARG PHE ALA GLY GLU HIS THR          
SEQRES  38 A  516  ILE MET ASP GLY ALA GLY CYS ALA TYR GLY ALA TRP GLU          
SEQRES  39 A  516  SER GLY ARG ARG GLU ALA THR ARG ILE SER ASP LEU LEU          
SEQRES  40 A  516  LYS LEU GLU HIS HIS HIS HIS HIS HIS                          
HET    FAD  B 517      53                                                       
HET    SP9  B 518      19                                                       
HET    FAD  A 517      53                                                       
HETNAM     FAD FLAVIN-ADENINE DINUCLEOTIDE                                      
HETNAM     SP9 N-{(1R)-3-[(4-AMINOBUTYL)AMINO]-1-                               
HETNAM   2 SP9  METHYLPROPYL}BENZAMIDE                                          
HETSYN     SP9 R-BZ-MESPERMIDINE                                                
FORMUL   3  FAD    2(C27 H33 N9 O15 P2)                                         
FORMUL   4  SP9    C15 H25 N3 O                                                 
FORMUL   6  HOH   *51(H2 O)                                                     
HELIX    1   1 GLY B   17  ASN B   30  1                                  14    
HELIX    2   2 TYR B   54  GLY B   56  5                                   3    
HELIX    3   3 ASN B   72  GLY B   86  1                                  15    
HELIX    4   4 LEU B  114  HIS B  131  1                                  18    
HELIX    5   5 SER B  140  ARG B  153  1                                  14    
HELIX    6   6 GLN B  154  LEU B  156  5                                   3    
HELIX    7   7 THR B  157  ARG B  169  1                                  13    
HELIX    8   8 LEU B  171  GLY B  176  1                                   6    
HELIX    9   9 SER B  183  TYR B  188  1                                   6    
HELIX   10  10 TYR B  201  SER B  211  1                                  11    
HELIX   11  11 PHE B  212  LEU B  217  5                                   6    
HELIX   12  12 PRO B  254  ASN B  259  1                                   6    
HELIX   13  13 LEU B  260  GLN B  263  5                                   4    
HELIX   14  14 LYS B  279  PHE B  286  1                                   8    
HELIX   15  15 THR B  320  ALA B  330  1                                  11    
HELIX   16  16 ASP B  334  MET B  339  1                                   6    
HELIX   17  17 LEU B  363  GLY B  368  1                                   6    
HELIX   18  18 PRO B  379  ILE B  387  1                                   9    
HELIX   19  19 ASP B  390  LEU B  409  1                                  20    
HELIX   20  20 VAL B  460  SER B  467  1                                   8    
HELIX   21  21 CYS B  488  GLU B  510  1                                  23    
HELIX   22  22 GLY A   17  ASN A   30  1                                  14    
HELIX   23  23 TYR A   54  GLY A   56  5                                   3    
HELIX   24  24 ASN A   72  GLY A   86  1                                  15    
HELIX   25  25 LEU A  114  PHE A  130  1                                  17    
HELIX   26  26 SER A  140  ARG A  152  1                                  13    
HELIX   27  27 ARG A  153  LEU A  156  5                                   4    
HELIX   28  28 THR A  157  ARG A  169  1                                  13    
HELIX   29  29 LEU A  171  GLY A  176  1                                   6    
HELIX   30  30 SER A  183  TYR A  188  1                                   6    
HELIX   31  31 TYR A  201  GLN A  210  1                                  10    
HELIX   32  32 PRO A  254  LEU A  260  1                                   7    
HELIX   33  33 SER A  261  GLN A  263  5                                   3    
HELIX   34  34 LYS A  279  ASP A  284  1                                   6    
HELIX   35  35 ALA A  285  ILE A  289  5                                   5    
HELIX   36  36 THR A  320  ALA A  330  1                                  11    
HELIX   37  37 ASN A  332  GLU A  341  1                                  10    
HELIX   38  38 LEU A  363  THR A  367  1                                   5    
HELIX   39  39 PRO A  379  ILE A  387  1                                   9    
HELIX   40  40 ASP A  390  LEU A  409  1                                  20    
HELIX   41  41 ASP A  458  GLY A  469  1                                  12    
HELIX   42  42 CYS A  488  LEU A  509  1                                  22    
HELIX   43  43 GLU A  510  HIS A  512  5                                   3    
SHEET    1   A 6 CYS B  35  LEU B  38  0                                        
SHEET    2   A 6 LYS B   9  ILE B  14  1  N  ILE B  13   O  LEU B  36           
SHEET    3   A 6 VAL B 243  ILE B 251  1  O  ILE B 250   N  ILE B  14           
SHEET    4   A 6 ASN B 233  CYS B 238 -1  N  VAL B 234   O  ALA B 246           
SHEET    5   A 6 VAL B 223  GLU B 229 -1  N  THR B 227   O  THR B 235           
SHEET    6   A 6 GLU B 273  GLN B 275  1  O  GLN B 275   N  ILE B 226           
SHEET    1   B 4 CYS B  35  LEU B  38  0                                        
SHEET    2   B 4 LYS B   9  ILE B  14  1  N  ILE B  13   O  LEU B  36           
SHEET    3   B 4 VAL B 243  ILE B 251  1  O  ILE B 250   N  ILE B  14           
SHEET    4   B 4 ILE B 474  PHE B 476  1  O  ARG B 475   N  ILE B 251           
SHEET    1   C 2 THR B  50  THR B  52  0                                        
SHEET    2   C 2 LYS B  58  ASP B  60 -1  O  TYR B  59   N  VAL B  51           
SHEET    1   D 3 TRP B  65  HIS B  66  0                                        
SHEET    2   D 3 ALA B 196  ALA B 198 -1  O  ALA B 196   N  HIS B  66           
SHEET    3   D 3 PHE B  90  VAL B  91 -1  N  VAL B  91   O  PHE B 197           
SHEET    1   E 8 GLY B 105  ARG B 106  0                                        
SHEET    2   E 8 ILE B  98  ASP B 101 -1  N  ASP B 101   O  GLY B 105           
SHEET    3   E 8 LYS B 312  LEU B 316  1  O  LEU B 316   N  ILE B 100           
SHEET    4   E 8 LEU B 358  ASN B 362 -1  O  PHE B 360   N  ILE B 313           
SHEET    5   E 8 SER B 371  MET B 376 -1  O  MET B 373   N  VAL B 361           
SHEET    6   E 8 GLY B 295  PHE B 301 -1  N  PHE B 299   O  PHE B 372           
SHEET    7   E 8 VAL B 431  VAL B 437 -1  O  ARG B 433   N  GLU B 300           
SHEET    8   E 8 ILE B 415  ASP B 416  1  N  ILE B 415   O  LEU B 432           
SHEET    1   F 7 LEU A 217  LYS A 218  0                                        
SHEET    2   F 7 LEU A  36  LEU A  38  1  N  VAL A  37   O  LYS A 218           
SHEET    3   F 7 ALA A   7  ILE A  14  1  N  ILE A  13   O  LEU A  36           
SHEET    4   F 7 VAL A 243  ILE A 251  1  O  ASN A 245   N  ALA A   7           
SHEET    5   F 7 ASN A 233  CYS A 238 -1  N  VAL A 234   O  ALA A 246           
SHEET    6   F 7 VAL A 223  GLU A 229 -1  N  GLU A 229   O  ASN A 233           
SHEET    7   F 7 GLU A 273  GLN A 275  1  O  GLN A 275   N  ARG A 228           
SHEET    1   G 5 LEU A 217  LYS A 218  0                                        
SHEET    2   G 5 LEU A  36  LEU A  38  1  N  VAL A  37   O  LYS A 218           
SHEET    3   G 5 ALA A   7  ILE A  14  1  N  ILE A  13   O  LEU A  36           
SHEET    4   G 5 VAL A 243  ILE A 251  1  O  ASN A 245   N  ALA A   7           
SHEET    5   G 5 ILE A 474  PHE A 476  1  O  ARG A 475   N  VAL A 249           
SHEET    1   H 2 THR A  50  THR A  52  0                                        
SHEET    2   H 2 LYS A  58  ASP A  60 -1  O  TYR A  59   N  VAL A  51           
SHEET    1   I 3 TRP A  65  HIS A  66  0                                        
SHEET    2   I 3 ALA A 196  ALA A 198 -1  O  ALA A 196   N  HIS A  66           
SHEET    3   I 3 PHE A  90  VAL A  91 -1  N  VAL A  91   O  PHE A 197           
SHEET    1   J 8 GLY A 105  ARG A 106  0                                        
SHEET    2   J 8 ILE A  98  ASP A 101 -1  N  ASP A 101   O  GLY A 105           
SHEET    3   J 8 LYS A 312  THR A 315  1  O  VAL A 314   N  ILE A  98           
SHEET    4   J 8 LEU A 358  ASN A 362 -1  O  PHE A 360   N  ILE A 313           
SHEET    5   J 8 SER A 371  MET A 376 -1  O  LEU A 375   N  PHE A 359           
SHEET    6   J 8 GLY A 295  PHE A 301 -1  N  PHE A 299   O  PHE A 372           
SHEET    7   J 8 VAL A 431  VAL A 437 -1  O  ILE A 436   N  ILE A 298           
SHEET    8   J 8 ILE A 415  ASP A 416  1  N  ILE A 415   O  LEU A 432           
SHEET    1   K 2 HIS A 290  GLY A 292  0                                        
SHEET    2   K 2 TYR A 450  ALA A 452 -1  O  TYR A 450   N  GLY A 292           
SSBOND   1 CYS B  221    CYS B  238                          1555   1555  2.03  
SSBOND   2 CYS A  221    CYS A  238                          1555   1555  2.04  
CISPEP   1 GLN B  275    PRO B  276          0         0.00                     
CISPEP   2 ALA B  378    PRO B  379          0         0.30                     
CISPEP   3 GLN A  275    PRO A  276          0        -0.42                     
CISPEP   4 ALA A  378    PRO A  379          0         0.42                     
SITE     1 AC1 30 GLY A  15  GLY A  17  ILE A  18  ALA A  19                    
SITE     2 AC1 30 GLU A  39  ALA A  40  ARG A  41  GLY A  45                    
SITE     3 AC1 30 GLY A  46  ARG A  47  GLY A  62  ALA A  63                    
SITE     4 AC1 30 SER A  64  TRP A  65  HIS A  67  CYS A 221                    
SITE     5 AC1 30 GLU A 222  THR A 252  PRO A 254  GLY A 270                    
SITE     6 AC1 30 LEU A 294  TRP A 440  ALA A 449  TYR A 450                    
SITE     7 AC1 30 GLY A 478  GLU A 479  GLY A 487  CYS A 488                    
SITE     8 AC1 30 ALA A 489  ALA A 492                                          
SITE     1 AC2 30 GLY B  15  GLY B  17  ILE B  18  ALA B  19                    
SITE     2 AC2 30 LEU B  38  GLU B  39  ALA B  40  ARG B  41                    
SITE     3 AC2 30 GLY B  46  ARG B  47  LEU B  48  GLY B  62                    
SITE     4 AC2 30 ALA B  63  SER B  64  TRP B  65  HIS B  67                    
SITE     5 AC2 30 CYS B 221  THR B 252  GLY B 270  LEU B 294                    
SITE     6 AC2 30 TRP B 440  TYR B 445  ALA B 449  TYR B 450                    
SITE     7 AC2 30 GLY B 478  GLU B 479  GLY B 487  CYS B 488                    
SITE     8 AC2 30 ALA B 489  ALA B 492                                          
SITE     1 AC3  9 TRP B  65  HIS B  67  LEU B 173  TRP B 174                    
SITE     2 AC3  9 PHE B 359  LEU B 375  TYR B 450  ALA B 486                    
SITE     3 AC3  9 CYS B 488                                                     
CRYST1  161.858  102.413   77.204  90.00  94.94  90.00 C 1 2 1       8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.006178  0.000000  0.000534        0.00000                         
SCALE2      0.000000  0.009764  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013001        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system