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Database: PDB
Entry: 1H81
LinkDB: 1H81
Original site: 1H81 
HEADER    OXIDOREDUCTASE                          24-JAN-01   1H81              
TITLE     STRUCTURE OF POLYAMINE OXIDASE IN THE REDUCED STATE                   
CAVEAT     1H81    THR C 386 HAS WRONG CHIRALITY AT ATOM CB                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: POLYAMINE OXIDASE;                                         
COMPND   3 CHAIN: A, B, C;                                                      
COMPND   4 FRAGMENT: FAD-BINDING DOMAIN RESIDUES 29-500;                        
COMPND   5 EC: 1.5.3.11                                                         
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ZEA MAYS;                                       
SOURCE   3 ORGANISM_COMMON: MAIZE;                                              
SOURCE   4 ORGANISM_TAXID: 4577                                                 
KEYWDS    FLAVIN-DEPENDENT AMINE OXIDASE, OXIDOREDUCTASE                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.BINDA,A.CODA,R.ANGELINI,R.FEDERICO,P.ASCENZI,A.MATTEVI              
REVDAT   6   13-DEC-23 1H81    1       REMARK HETSYN LINK                       
REVDAT   5   29-JUL-20 1H81    1       CAVEAT COMPND REMARK HETNAM              
REVDAT   5 2                   1       LINK   SITE   ATOM                       
REVDAT   4   24-JUL-19 1H81    1       REMARK LINK                              
REVDAT   3   24-FEB-09 1H81    1       VERSN                                    
REVDAT   2   27-MAR-01 1H81    1       JRNL                                     
REVDAT   1   31-JAN-01 1H81    0                                                
JRNL        AUTH   C.BINDA,R.ANGELINI,R.FEDERICO,P.ASCENZI,A.MATTEVI            
JRNL        TITL   STRUCTURAL BASES FOR INHIBITOR BINDING AND CATALYSIS IN      
JRNL        TITL 2 POLYAMINE OXIDASE                                            
JRNL        REF    BIOCHEMISTRY                  V.  40  2766 2001              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   11258887                                                     
JRNL        DOI    10.1021/BI002751J                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : TNT 5D                                               
REMARK   3   AUTHORS     : TRONRUD,TEN EYCK,MATTHEWS                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 156392                         
REMARK   3                                                                      
REMARK   3  USING DATA ABOVE SIGMA CUTOFF.                                      
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.191                           
REMARK   3   R VALUE            (WORKING SET) : 0.191                           
REMARK   3   FREE R VALUE                     : 0.235                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 2.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
REMARK   3                                                                      
REMARK   3  USING ALL DATA, NO SIGMA CUTOFF.                                    
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : 0.1910                 
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : 0.1910                 
REMARK   3   FREE R VALUE                  (NO CUTOFF) : 0.235                  
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 2.00                   
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : NULL                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : 156392                 
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 11114                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 275                                     
REMARK   3   SOLVENT ATOMS            : 724                                     
REMARK   3                                                                      
REMARK   3  WILSON B VALUE (FROM FCALC, A**2) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.    RMS    WEIGHT  COUNT           
REMARK   3   BOND LENGTHS                 (A) : 0.009 ; NULL  ; NULL            
REMARK   3   BOND ANGLES            (DEGREES) : 2.200 ; NULL  ; NULL            
REMARK   3   TORSION ANGLES         (DEGREES) : NULL  ; NULL  ; NULL            
REMARK   3   PSEUDOROTATION ANGLES  (DEGREES) : NULL  ; NULL  ; NULL            
REMARK   3   TRIGONAL CARBON PLANES       (A) : 0.013 ; NULL  ; NULL            
REMARK   3   GENERAL PLANES               (A) : 0.015 ; NULL  ; NULL            
REMARK   3   ISOTROPIC THERMAL FACTORS (A**2) : NULL  ; NULL  ; NULL            
REMARK   3   NON-BONDED CONTACTS          (A) : NULL  ; NULL  ; NULL            
REMARK   3                                                                      
REMARK   3  INCORRECT CHIRAL-CENTERS (COUNT) : NULL                             
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : NULL                                                 
REMARK   3                                                                      
REMARK   3  RESTRAINT LIBRARIES.                                                
REMARK   3   STEREOCHEMISTRY : TNT PROTGEO                                      
REMARK   3   ISOTROPIC THERMAL FACTOR RESTRAINTS : NULL                         
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1H81 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 24-JAN-01.                  
REMARK 100 THE DEPOSITION ID IS D_1290005824.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 4.60                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : EMBL/DESY, HAMBURG                 
REMARK 200  BEAMLINE                       : X11                                
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                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 156868                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 3.600                              
REMARK 200  R MERGE                    (I) : 0.07000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.20                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.17600                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: CCP4                                                  
REMARK 200 STARTING MODEL: 1B37                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 70.06                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.11                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 4.60                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65 2 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+1/6                                            
REMARK 290       6555   X-Y,X,Z+5/6                                             
REMARK 290       7555   Y,X,-Z+2/3                                              
REMARK 290       8555   X-Y,-Y,-Z                                               
REMARK 290       9555   -X,-X+Y,-Z+1/3                                          
REMARK 290      10555   -Y,-X,-Z+1/6                                            
REMARK 290      11555   -X+Y,Y,-Z+1/2                                           
REMARK 290      12555   X,X-Y,-Z+5/6                                            
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      185.02000            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       92.51000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      138.76500            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       46.25500            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000      231.27500            
REMARK 290   SMTRY1   7 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000      185.02000            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   9 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   9  0.000000  0.000000 -1.000000       92.51000            
REMARK 290   SMTRY1  10  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  10 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000       46.25500            
REMARK 290   SMTRY1  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  11  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000      138.76500            
REMARK 290   SMTRY1  12  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  12  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000      231.27500            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 300 REMARK: IN THE CRYSTAL WHILE THE CHAIN C FORMS A                     
REMARK 300   HOMODIMERWITH A SYMMETRY RELATED MOLECULE. THE                     
REMARK 300  PROTEIN ISACTIVE AS A MONOMER.                                      
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: PQS                                                   
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, D, E                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, F                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2  0.500000 -0.866025  0.000000       90.88500            
REMARK 350   BIOMT2   2 -0.866025 -0.500000  0.000000      157.41744            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       46.25500            
REMARK 400                                                                      
REMARK 400 COMPOUND                                                             
REMARK 400 CATALYSES THE OXIDATION OF THE SECONDARY AMINO GROUP OF              
REMARK 400  POLYAMINES (SPERMINE, SPERMIDINE AND THEIR ACETYL DERIVATIVES)      
REMARK 400  THIS IS IMPORTANT FOR REGULATION OF POLYAMINE INTRACELLULAR         
REMARK 400  CONCENTRATION.                                                      
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     ALA A     1                                                      
REMARK 465     THR A     2                                                      
REMARK 465     VAL A     3                                                      
REMARK 465     GLY A     4                                                      
REMARK 465     LYS A   464                                                      
REMARK 465     TYR A   465                                                      
REMARK 465     HIS A   466                                                      
REMARK 465     VAL A   467                                                      
REMARK 465     GLN A   468                                                      
REMARK 465     GLY A   469                                                      
REMARK 465     LYS A   470                                                      
REMARK 465     TYR A   471                                                      
REMARK 465     ASP A   472                                                      
REMARK 465     ALA B     1                                                      
REMARK 465     THR B     2                                                      
REMARK 465     VAL B     3                                                      
REMARK 465     GLY B     4                                                      
REMARK 465     VAL B   467                                                      
REMARK 465     GLN B   468                                                      
REMARK 465     GLY B   469                                                      
REMARK 465     LYS B   470                                                      
REMARK 465     TYR B   471                                                      
REMARK 465     ASP B   472                                                      
REMARK 465     ALA C     1                                                      
REMARK 465     THR C     2                                                      
REMARK 465     VAL C     3                                                      
REMARK 465     GLY C     4                                                      
REMARK 465     VAL C   467                                                      
REMARK 465     GLN C   468                                                      
REMARK 465     GLY C   469                                                      
REMARK 465     LYS C   470                                                      
REMARK 465     TYR C   471                                                      
REMARK 465     ASP C   472                                                      
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     LYS A   68   CD   CE   NZ                                        
REMARK 480     LYS A   81   CE   NZ                                             
REMARK 480     LYS A   98   CE   NZ                                             
REMARK 480     LYS A  111   CG   CD   CE   NZ                                   
REMARK 480     LYS A  125   CD   CE   NZ                                        
REMARK 480     ARG A  135   CZ   NH1  NH2                                       
REMARK 480     LYS A  218   CD   CE   NZ                                        
REMARK 480     ASP A  221   CG   OD1  OD2                                       
REMARK 480     LYS A  222   CG   CD   CE   NZ                                   
REMARK 480     LYS A  225   CG   CD   CE   NZ                                   
REMARK 480     LYS A  279   CD   CE   NZ                                        
REMARK 480     LYS A  308   CD   CE   NZ                                        
REMARK 480     LYS A  314   CG   CD   CE   NZ                                   
REMARK 480     GLU A  363   CG   CD   OE1  OE2                                  
REMARK 480     GLN A  364   CG   CD   OE1  NE2                                  
REMARK 480     LYS A  380   CD   CE   NZ                                        
REMARK 480     ASP A  381   CG   OD1  OD2                                       
REMARK 480     LYS B   68   CD   CE   NZ                                        
REMARK 480     LYS B   81   CB   CG   CD   CE   NZ                              
REMARK 480     LYS B  111   CE   NZ                                             
REMARK 480     GLU B  121   CG   CD   OE1  OE2                                  
REMARK 480     GLN B  202   CG   CD   OE1  NE2                                  
REMARK 480     LYS B  218   CD   CE   NZ                                        
REMARK 480     LYS B  222   CB   CG   CD   CE   NZ                              
REMARK 480     LYS B  225   CE   NZ                                             
REMARK 480     LYS B  241   CE   NZ                                             
REMARK 480     LYS B  279   CD   CE   NZ                                        
REMARK 480     LYS B  281   CD   CE   NZ                                        
REMARK 480     LYS B  314   CG   CD   CE   NZ                                   
REMARK 480     GLU B  363   CD   OE1  OE2                                       
REMARK 480     GLN B  364   CD   OE1  NE2                                       
REMARK 480     LYS B  380   CD   CE   NZ                                        
REMARK 480     GLU B  434   OE1  OE2                                            
REMARK 480     LYS B  460   CD   CE   NZ                                        
REMARK 480     LYS B  461   CE   NZ                                             
REMARK 480     LYS B  464   CB   CG   CD   CE   NZ                              
REMARK 480     LYS C   81   CE   NZ                                             
REMARK 480     LYS C  111   CE   NZ                                             
REMARK 480     ARG C  135   CG   CD   NE   CZ   NH1  NH2                        
REMARK 480     LYS C  218   CG   CD   CE   NZ                                   
REMARK 480     ASP C  221   CG   OD1  OD2                                       
REMARK 480     LYS C  222   CB   CG   CD   CE   NZ                              
REMARK 480     LYS C  225   CG   CD   CE   NZ                                   
REMARK 480     LYS C  250   CE   NZ                                             
REMARK 480     ASP C  274   CB   CG   OD1  OD2                                  
REMARK 480     LYS C  314   CD   CE   NZ                                        
REMARK 480     GLU C  363   CG   CD   OE1  OE2                                  
REMARK 480     GLN C  364   CD   OE1  NE2                                       
REMARK 480     LYS C  380   CE   NZ                                             
REMARK 480     GLU C  414   CD   OE1  OE2                                       
REMARK 480     LYS C  464   CD   CE   NZ                                        
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  2015     O    HOH A  2050              1.82            
REMARK 500   O4   NAG F     2     O5   MAN F     3              1.88            
REMARK 500   O    HOH A  2016     O    HOH A  2052              1.91            
REMARK 500   O    HOH A  2003     O    HOH A  2009              2.07            
REMARK 500   OE1  GLN C   292     O    HOH C  2137              2.07            
REMARK 500   O    HOH C  2013     O    HOH C  2082              2.07            
REMARK 500   ND2  ASN B    77     O5   NAG E     1              2.10            
REMARK 500   OD1  ASP A   117     O    HOH A  2050              2.11            
REMARK 500   ND2  ASN A    77     O5   NAG D     1              2.13            
REMARK 500   O    HOH B  2221     O    HOH B  2225              2.16            
REMARK 500   ND2  ASN C    77     O5   NAG F     1              2.16            
REMARK 500   O    HOH C  2106     O    HOH C  2108              2.17            
REMARK 500   O3   NAG F     1     C2   FCA F     5              2.17            
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    VAL A  61   N   -  CA  -  C   ANGL. DEV. = -18.3 DEGREES          
REMARK 500    GLY A 101   N   -  CA  -  C   ANGL. DEV. =  17.9 DEGREES          
REMARK 500    ASP A 117   CB  -  CG  -  OD1 ANGL. DEV. =  -9.7 DEGREES          
REMARK 500    ASP A 136   CB  -  CG  -  OD2 ANGL. DEV. =  -5.5 DEGREES          
REMARK 500    ASP A 260   CB  -  CG  -  OD2 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    ARG A 326   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.0 DEGREES          
REMARK 500    ASP A 351   N   -  CA  -  CB  ANGL. DEV. = -10.9 DEGREES          
REMARK 500    ARG A 355   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES          
REMARK 500    ARG A 355   NE  -  CZ  -  NH2 ANGL. DEV. =  -6.3 DEGREES          
REMARK 500    ARG B  22   NE  -  CZ  -  NH1 ANGL. DEV. =   3.5 DEGREES          
REMARK 500    VAL B  61   N   -  CA  -  C   ANGL. DEV. = -16.7 DEGREES          
REMARK 500    ARG B 135   NE  -  CZ  -  NH1 ANGL. DEV. =  -4.6 DEGREES          
REMARK 500    GLU B 252   N   -  CA  -  CB  ANGL. DEV. = -11.9 DEGREES          
REMARK 500    ASP B 351   N   -  CA  -  CB  ANGL. DEV. = -11.2 DEGREES          
REMARK 500    ARG B 355   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.5 DEGREES          
REMARK 500    ARG C   6   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.1 DEGREES          
REMARK 500    ASP C 105   CB  -  CG  -  OD1 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    ARG C 112   NE  -  CZ  -  NH1 ANGL. DEV. =   4.1 DEGREES          
REMARK 500    LEU C 115   CB  -  CG  -  CD1 ANGL. DEV. = -11.2 DEGREES          
REMARK 500    ARG C 145   NE  -  CZ  -  NH1 ANGL. DEV. =   4.4 DEGREES          
REMARK 500    ARG C 145   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.1 DEGREES          
REMARK 500    ARG C 176   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.4 DEGREES          
REMARK 500    ARG C 230   NE  -  CZ  -  NH1 ANGL. DEV. =  -5.4 DEGREES          
REMARK 500    ARG C 307   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.7 DEGREES          
REMARK 500    ARG C 355   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.7 DEGREES          
REMARK 500    ARG C 397   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.0 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ALA A  12       40.21   -107.94                                   
REMARK 500    SER A  78      -62.75   -109.47                                   
REMARK 500    PHE A 167      -62.01   -124.78                                   
REMARK 500    THR A 183      -17.44   -142.36                                   
REMARK 500    TYR A 216       -9.99   -153.36                                   
REMARK 500    LYS A 222      -63.66    -97.49                                   
REMARK 500    ASN A 254        4.79     83.80                                   
REMARK 500    TYR A 329       51.05     34.40                                   
REMARK 500    PHE A 335       43.33   -107.33                                   
REMARK 500    ASP A 341       -1.33     74.67                                   
REMARK 500    ASP A 351     -120.90     47.70                                   
REMARK 500    PHE A 377       59.66   -114.56                                   
REMARK 500    ARG A 392       56.30   -113.75                                   
REMARK 500    TYR A 399      -46.96   -139.62                                   
REMARK 500    SER B  78      -56.45   -132.14                                   
REMARK 500    ASP B 100       40.87   -106.97                                   
REMARK 500    TYR B 216       -5.63   -147.98                                   
REMARK 500    TYR B 329       54.91     38.42                                   
REMARK 500    ASP B 351     -121.74     45.32                                   
REMARK 500    ARG B 392       62.04   -117.19                                   
REMARK 500    TYR B 399      -48.19   -136.02                                   
REMARK 500    ASN C  59      -18.68   -140.39                                   
REMARK 500    SER C  78      -51.83   -127.27                                   
REMARK 500    TYR C 216      -14.10   -143.34                                   
REMARK 500    LYS C 222      -76.22    -88.14                                   
REMARK 500    ASN C 254       -2.71     82.51                                   
REMARK 500    ASP C 351     -125.46     45.30                                   
REMARK 500    TYR C 399      -45.61   -135.50                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1B37   RELATED DB: PDB                                   
REMARK 900 A 30 ANGSTROM U-SHAPED CATALYTIC TUNNEL IN THE CRYSTAL STRUCTURE OF  
REMARK 900 POLYAMINE OXIDASE                                                    
REMARK 900 RELATED ID: 1B5Q   RELATED DB: PDB                                   
REMARK 900 A 30 ANGSTROM U-SHAPED CATALYTIC TUNNEL IN THE CRYSTAL STRUCTURE OF  
REMARK 900 POLYAMINE OXIDASE                                                    
REMARK 900 RELATED ID: 1H82   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF POLYAMINE OXIDASE IN COMPLEX WITH GUAZATINE             
REMARK 900 RELATED ID: 1H83   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF POLYAMINE OXIDASE IN COMPLEX WITH 1,8-DIAMINOOCTANE     
REMARK 900 RELATED ID: 1H84   RELATED DB: PDB                                   
REMARK 900 COVALENT ADDUCT BETWEEN POLYAMINE OXIDASE AND                        
REMARK 900 N1ETHYLN11((CYCLOHEPTYL)METHYL)4, 8DIAZAUNDECANE AT PH 4.6           
REMARK 900 RELATED ID: 1H86   RELATED DB: PDB                                   
REMARK 900 COVALENT ADDUCT BETWEEN POLYAMINE OXIDASE AND                        
REMARK 900 N1ETHYLN11((CYCLOHEPTYL)METHYL)4, 8DIAZAUNDECANE AT PH 7.0           
DBREF  1H81 A    1   472  UNP    O64411   PAO_MAIZE       29    500             
DBREF  1H81 B    1   472  UNP    O64411   PAO_MAIZE       29    500             
DBREF  1H81 C    1   472  UNP    O64411   PAO_MAIZE       29    500             
SEQRES   1 A  472  ALA THR VAL GLY PRO ARG VAL ILE VAL VAL GLY ALA GLY          
SEQRES   2 A  472  MET SER GLY ILE SER ALA ALA LYS ARG LEU SER GLU ALA          
SEQRES   3 A  472  GLY ILE THR ASP LEU LEU ILE LEU GLU ALA THR ASP HIS          
SEQRES   4 A  472  ILE GLY GLY ARG MET HIS LYS THR ASN PHE ALA GLY ILE          
SEQRES   5 A  472  ASN VAL GLU LEU GLY ALA ASN TRP VAL GLU GLY VAL ASN          
SEQRES   6 A  472  GLY GLY LYS MET ASN PRO ILE TRP PRO ILE VAL ASN SER          
SEQRES   7 A  472  THR LEU LYS LEU ARG ASN PHE ARG SER ASP PHE ASP TYR          
SEQRES   8 A  472  LEU ALA GLN ASN VAL TYR LYS GLU ASP GLY GLY VAL TYR          
SEQRES   9 A  472  ASP GLU ASP TYR VAL GLN LYS ARG ILE GLU LEU ALA ASP          
SEQRES  10 A  472  SER VAL GLU GLU MET GLY GLU LYS LEU SER ALA THR LEU          
SEQRES  11 A  472  HIS ALA SER GLY ARG ASP ASP MET SER ILE LEU ALA MET          
SEQRES  12 A  472  GLN ARG LEU ASN GLU HIS GLN PRO ASN GLY PRO ALA THR          
SEQRES  13 A  472  PRO VAL ASP MET VAL VAL ASP TYR TYR LYS PHE ASP TYR          
SEQRES  14 A  472  GLU PHE ALA GLU PRO PRO ARG VAL THR SER LEU GLN ASN          
SEQRES  15 A  472  THR VAL PRO LEU ALA THR PHE SER ASP PHE GLY ASP ASP          
SEQRES  16 A  472  VAL TYR PHE VAL ALA ASP GLN ARG GLY TYR GLU ALA VAL          
SEQRES  17 A  472  VAL TYR TYR LEU ALA GLY GLN TYR LEU LYS THR ASP ASP          
SEQRES  18 A  472  LYS SER GLY LYS ILE VAL ASP PRO ARG LEU GLN LEU ASN          
SEQRES  19 A  472  LYS VAL VAL ARG GLU ILE LYS TYR SER PRO GLY GLY VAL          
SEQRES  20 A  472  THR VAL LYS THR GLU ASP ASN SER VAL TYR SER ALA ASP          
SEQRES  21 A  472  TYR VAL MET VAL SER ALA SER LEU GLY VAL LEU GLN SER          
SEQRES  22 A  472  ASP LEU ILE GLN PHE LYS PRO LYS LEU PRO THR TRP LYS          
SEQRES  23 A  472  VAL ARG ALA ILE TYR GLN PHE ASP MET ALA VAL TYR THR          
SEQRES  24 A  472  LYS ILE PHE LEU LYS PHE PRO ARG LYS PHE TRP PRO GLU          
SEQRES  25 A  472  GLY LYS GLY ARG GLU PHE PHE LEU TYR ALA SER SER ARG          
SEQRES  26 A  472  ARG GLY TYR TYR GLY VAL TRP GLN GLU PHE GLU LYS GLN          
SEQRES  27 A  472  TYR PRO ASP ALA ASN VAL LEU LEU VAL THR VAL THR ASP          
SEQRES  28 A  472  GLU GLU SER ARG ARG ILE GLU GLN GLN SER ASP GLU GLN          
SEQRES  29 A  472  THR LYS ALA GLU ILE MET GLN VAL LEU ARG LYS MET PHE          
SEQRES  30 A  472  PRO GLY LYS ASP VAL PRO ASP ALA THR ASP ILE LEU VAL          
SEQRES  31 A  472  PRO ARG TRP TRP SER ASP ARG PHE TYR LYS GLY THR PHE          
SEQRES  32 A  472  SER ASN TRP PRO VAL GLY VAL ASN ARG TYR GLU TYR ASP          
SEQRES  33 A  472  GLN LEU ARG ALA PRO VAL GLY ARG VAL TYR PHE THR GLY          
SEQRES  34 A  472  GLU HIS THR SER GLU HIS TYR ASN GLY TYR VAL HIS GLY          
SEQRES  35 A  472  ALA TYR LEU SER GLY ILE ASP SER ALA GLU ILE LEU ILE          
SEQRES  36 A  472  ASN CYS ALA GLN LYS LYS MET CYS LYS TYR HIS VAL GLN          
SEQRES  37 A  472  GLY LYS TYR ASP                                              
SEQRES   1 B  472  ALA THR VAL GLY PRO ARG VAL ILE VAL VAL GLY ALA GLY          
SEQRES   2 B  472  MET SER GLY ILE SER ALA ALA LYS ARG LEU SER GLU ALA          
SEQRES   3 B  472  GLY ILE THR ASP LEU LEU ILE LEU GLU ALA THR ASP HIS          
SEQRES   4 B  472  ILE GLY GLY ARG MET HIS LYS THR ASN PHE ALA GLY ILE          
SEQRES   5 B  472  ASN VAL GLU LEU GLY ALA ASN TRP VAL GLU GLY VAL ASN          
SEQRES   6 B  472  GLY GLY LYS MET ASN PRO ILE TRP PRO ILE VAL ASN SER          
SEQRES   7 B  472  THR LEU LYS LEU ARG ASN PHE ARG SER ASP PHE ASP TYR          
SEQRES   8 B  472  LEU ALA GLN ASN VAL TYR LYS GLU ASP GLY GLY VAL TYR          
SEQRES   9 B  472  ASP GLU ASP TYR VAL GLN LYS ARG ILE GLU LEU ALA ASP          
SEQRES  10 B  472  SER VAL GLU GLU MET GLY GLU LYS LEU SER ALA THR LEU          
SEQRES  11 B  472  HIS ALA SER GLY ARG ASP ASP MET SER ILE LEU ALA MET          
SEQRES  12 B  472  GLN ARG LEU ASN GLU HIS GLN PRO ASN GLY PRO ALA THR          
SEQRES  13 B  472  PRO VAL ASP MET VAL VAL ASP TYR TYR LYS PHE ASP TYR          
SEQRES  14 B  472  GLU PHE ALA GLU PRO PRO ARG VAL THR SER LEU GLN ASN          
SEQRES  15 B  472  THR VAL PRO LEU ALA THR PHE SER ASP PHE GLY ASP ASP          
SEQRES  16 B  472  VAL TYR PHE VAL ALA ASP GLN ARG GLY TYR GLU ALA VAL          
SEQRES  17 B  472  VAL TYR TYR LEU ALA GLY GLN TYR LEU LYS THR ASP ASP          
SEQRES  18 B  472  LYS SER GLY LYS ILE VAL ASP PRO ARG LEU GLN LEU ASN          
SEQRES  19 B  472  LYS VAL VAL ARG GLU ILE LYS TYR SER PRO GLY GLY VAL          
SEQRES  20 B  472  THR VAL LYS THR GLU ASP ASN SER VAL TYR SER ALA ASP          
SEQRES  21 B  472  TYR VAL MET VAL SER ALA SER LEU GLY VAL LEU GLN SER          
SEQRES  22 B  472  ASP LEU ILE GLN PHE LYS PRO LYS LEU PRO THR TRP LYS          
SEQRES  23 B  472  VAL ARG ALA ILE TYR GLN PHE ASP MET ALA VAL TYR THR          
SEQRES  24 B  472  LYS ILE PHE LEU LYS PHE PRO ARG LYS PHE TRP PRO GLU          
SEQRES  25 B  472  GLY LYS GLY ARG GLU PHE PHE LEU TYR ALA SER SER ARG          
SEQRES  26 B  472  ARG GLY TYR TYR GLY VAL TRP GLN GLU PHE GLU LYS GLN          
SEQRES  27 B  472  TYR PRO ASP ALA ASN VAL LEU LEU VAL THR VAL THR ASP          
SEQRES  28 B  472  GLU GLU SER ARG ARG ILE GLU GLN GLN SER ASP GLU GLN          
SEQRES  29 B  472  THR LYS ALA GLU ILE MET GLN VAL LEU ARG LYS MET PHE          
SEQRES  30 B  472  PRO GLY LYS ASP VAL PRO ASP ALA THR ASP ILE LEU VAL          
SEQRES  31 B  472  PRO ARG TRP TRP SER ASP ARG PHE TYR LYS GLY THR PHE          
SEQRES  32 B  472  SER ASN TRP PRO VAL GLY VAL ASN ARG TYR GLU TYR ASP          
SEQRES  33 B  472  GLN LEU ARG ALA PRO VAL GLY ARG VAL TYR PHE THR GLY          
SEQRES  34 B  472  GLU HIS THR SER GLU HIS TYR ASN GLY TYR VAL HIS GLY          
SEQRES  35 B  472  ALA TYR LEU SER GLY ILE ASP SER ALA GLU ILE LEU ILE          
SEQRES  36 B  472  ASN CYS ALA GLN LYS LYS MET CYS LYS TYR HIS VAL GLN          
SEQRES  37 B  472  GLY LYS TYR ASP                                              
SEQRES   1 C  472  ALA THR VAL GLY PRO ARG VAL ILE VAL VAL GLY ALA GLY          
SEQRES   2 C  472  MET SER GLY ILE SER ALA ALA LYS ARG LEU SER GLU ALA          
SEQRES   3 C  472  GLY ILE THR ASP LEU LEU ILE LEU GLU ALA THR ASP HIS          
SEQRES   4 C  472  ILE GLY GLY ARG MET HIS LYS THR ASN PHE ALA GLY ILE          
SEQRES   5 C  472  ASN VAL GLU LEU GLY ALA ASN TRP VAL GLU GLY VAL ASN          
SEQRES   6 C  472  GLY GLY LYS MET ASN PRO ILE TRP PRO ILE VAL ASN SER          
SEQRES   7 C  472  THR LEU LYS LEU ARG ASN PHE ARG SER ASP PHE ASP TYR          
SEQRES   8 C  472  LEU ALA GLN ASN VAL TYR LYS GLU ASP GLY GLY VAL TYR          
SEQRES   9 C  472  ASP GLU ASP TYR VAL GLN LYS ARG ILE GLU LEU ALA ASP          
SEQRES  10 C  472  SER VAL GLU GLU MET GLY GLU LYS LEU SER ALA THR LEU          
SEQRES  11 C  472  HIS ALA SER GLY ARG ASP ASP MET SER ILE LEU ALA MET          
SEQRES  12 C  472  GLN ARG LEU ASN GLU HIS GLN PRO ASN GLY PRO ALA THR          
SEQRES  13 C  472  PRO VAL ASP MET VAL VAL ASP TYR TYR LYS PHE ASP TYR          
SEQRES  14 C  472  GLU PHE ALA GLU PRO PRO ARG VAL THR SER LEU GLN ASN          
SEQRES  15 C  472  THR VAL PRO LEU ALA THR PHE SER ASP PHE GLY ASP ASP          
SEQRES  16 C  472  VAL TYR PHE VAL ALA ASP GLN ARG GLY TYR GLU ALA VAL          
SEQRES  17 C  472  VAL TYR TYR LEU ALA GLY GLN TYR LEU LYS THR ASP ASP          
SEQRES  18 C  472  LYS SER GLY LYS ILE VAL ASP PRO ARG LEU GLN LEU ASN          
SEQRES  19 C  472  LYS VAL VAL ARG GLU ILE LYS TYR SER PRO GLY GLY VAL          
SEQRES  20 C  472  THR VAL LYS THR GLU ASP ASN SER VAL TYR SER ALA ASP          
SEQRES  21 C  472  TYR VAL MET VAL SER ALA SER LEU GLY VAL LEU GLN SER          
SEQRES  22 C  472  ASP LEU ILE GLN PHE LYS PRO LYS LEU PRO THR TRP LYS          
SEQRES  23 C  472  VAL ARG ALA ILE TYR GLN PHE ASP MET ALA VAL TYR THR          
SEQRES  24 C  472  LYS ILE PHE LEU LYS PHE PRO ARG LYS PHE TRP PRO GLU          
SEQRES  25 C  472  GLY LYS GLY ARG GLU PHE PHE LEU TYR ALA SER SER ARG          
SEQRES  26 C  472  ARG GLY TYR TYR GLY VAL TRP GLN GLU PHE GLU LYS GLN          
SEQRES  27 C  472  TYR PRO ASP ALA ASN VAL LEU LEU VAL THR VAL THR ASP          
SEQRES  28 C  472  GLU GLU SER ARG ARG ILE GLU GLN GLN SER ASP GLU GLN          
SEQRES  29 C  472  THR LYS ALA GLU ILE MET GLN VAL LEU ARG LYS MET PHE          
SEQRES  30 C  472  PRO GLY LYS ASP VAL PRO ASP ALA THR ASP ILE LEU VAL          
SEQRES  31 C  472  PRO ARG TRP TRP SER ASP ARG PHE TYR LYS GLY THR PHE          
SEQRES  32 C  472  SER ASN TRP PRO VAL GLY VAL ASN ARG TYR GLU TYR ASP          
SEQRES  33 C  472  GLN LEU ARG ALA PRO VAL GLY ARG VAL TYR PHE THR GLY          
SEQRES  34 C  472  GLU HIS THR SER GLU HIS TYR ASN GLY TYR VAL HIS GLY          
SEQRES  35 C  472  ALA TYR LEU SER GLY ILE ASP SER ALA GLU ILE LEU ILE          
SEQRES  36 C  472  ASN CYS ALA GLN LYS LYS MET CYS LYS TYR HIS VAL GLN          
SEQRES  37 C  472  GLY LYS TYR ASP                                              
MODRES 1H81 ASN A   77  ASN  GLYCOSYLATION SITE                                 
MODRES 1H81 ASN B   77  ASN  GLYCOSYLATION SITE                                 
MODRES 1H81 ASN C   77  ASN  GLYCOSYLATION SITE                                 
HET    NAG  D   1      14                                                       
HET    NAG  D   2      14                                                       
HET    NAG  E   1      14                                                       
HET    NAG  E   2      14                                                       
HET    NAG  F   1      14                                                       
HET    NAG  F   2      14                                                       
HET    MAN  F   3      11                                                       
HET    MAN  F   4      11                                                       
HET    FCA  F   5      10                                                       
HET    FAD  A 579      53                                                       
HET    FAD  B 579      53                                                       
HET    FAD  C 579      53                                                       
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
HETNAM     MAN ALPHA-D-MANNOPYRANOSE                                            
HETNAM     FCA ALPHA-D-FUCOPYRANOSE                                             
HETNAM     FAD FLAVIN-ADENINE DINUCLEOTIDE                                      
HETSYN     NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-           
HETSYN   2 NAG  D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-          
HETSYN   3 NAG  2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE                         
HETSYN     MAN ALPHA-D-MANNOSE; D-MANNOSE; MANNOSE                              
HETSYN     FCA ALPHA-D-FUCOSE; 6-DEOXY-ALPHA-D-GALACTOPYRANOSE; D-              
HETSYN   2 FCA  FUCOSE; FUCOSE                                                  
FORMUL   4  NAG    6(C8 H15 N O6)                                               
FORMUL   6  MAN    2(C6 H12 O6)                                                 
FORMUL   6  FCA    C6 H12 O5                                                    
FORMUL   7  FAD    3(C27 H33 N9 O15 P2)                                         
FORMUL  10  HOH   *724(H2 O)                                                    
HELIX    1   1 GLY A   13  ALA A   26  1                                  14    
HELIX    2   2 PRO A   71  SER A   78  1                                   8    
HELIX    3   3 TYR A   91  GLN A   94  5                                   4    
HELIX    4   4 ASP A  105  THR A  129  1                                  25    
HELIX    5   5 SER A  139  HIS A  149  1                                  11    
HELIX    6   6 THR A  156  PHE A  167  1                                  12    
HELIX    7   7 PHE A  167  ALA A  172  1                                   6    
HELIX    8   8 LEU A  186  GLY A  193  1                                   8    
HELIX    9   9 GLU A  206  GLN A  215  1                                  10    
HELIX   10  10 SER A  267  SER A  273  1                                   7    
HELIX   11  11 PRO A  283  PHE A  293  1                                  11    
HELIX   12  12 ASP A  351  GLN A  359  1                                   9    
HELIX   13  13 SER A  361  PHE A  377  1                                  17    
HELIX   14  14 ASN A  411  ALA A  420  1                                  10    
HELIX   15  15 GLY A  429  SER A  433  5                                   5    
HELIX   16  16 TYR A  439  GLN A  459  1                                  21    
HELIX   17  17 GLY B   13  ALA B   26  1                                  14    
HELIX   18  18 PRO B   71  SER B   78  1                                   8    
HELIX   19  19 TYR B   91  GLN B   94  5                                   4    
HELIX   20  20 ASP B  105  LEU B  130  1                                  26    
HELIX   21  21 SER B  139  HIS B  149  1                                  11    
HELIX   22  22 THR B  156  PHE B  167  1                                  12    
HELIX   23  23 PHE B  167  ALA B  172  1                                   6    
HELIX   24  24 SER B  179  VAL B  184  1                                   6    
HELIX   25  25 LEU B  186  GLY B  193  1                                   8    
HELIX   26  26 GLU B  206  GLN B  215  1                                  10    
HELIX   27  27 SER B  267  GLN B  272  1                                   6    
HELIX   28  28 PRO B  283  PHE B  293  1                                  11    
HELIX   29  29 ASP B  351  GLN B  359  1                                   9    
HELIX   30  30 SER B  361  PHE B  377  1                                  17    
HELIX   31  31 ASN B  411  ALA B  420  1                                  10    
HELIX   32  32 GLY B  429  SER B  433  5                                   5    
HELIX   33  33 TYR B  439  LYS B  461  1                                  23    
HELIX   34  34 GLY C   13  ALA C   26  1                                  14    
HELIX   35  35 PRO C   71  SER C   78  1                                   8    
HELIX   36  36 TYR C   91  GLN C   94  5                                   4    
HELIX   37  37 ASP C  105  LEU C  130  1                                  26    
HELIX   38  38 SER C  139  HIS C  149  1                                  11    
HELIX   39  39 THR C  156  PHE C  167  1                                  12    
HELIX   40  40 PHE C  167  ALA C  172  1                                   6    
HELIX   41  41 LEU C  186  GLY C  193  1                                   8    
HELIX   42  42 GLU C  206  GLY C  214  1                                   9    
HELIX   43  43 SER C  267  SER C  273  1                                   7    
HELIX   44  44 PRO C  283  PHE C  293  1                                  11    
HELIX   45  45 ASP C  351  GLN C  359  1                                   9    
HELIX   46  46 SER C  361  PHE C  377  1                                  17    
HELIX   47  47 ASN C  411  ALA C  420  1                                  10    
HELIX   48  48 GLY C  429  SER C  433  5                                   5    
HELIX   49  49 TYR C  439  LYS C  461  1                                  23    
SHEET    1  AA 5 LEU A 231  GLN A 232  0                                        
SHEET    2  AA 5 LEU A  31  LEU A  34  1  O  ILE A  33   N  GLN A 232           
SHEET    3  AA 5 VAL A   7  VAL A  10  1  O  VAL A   7   N  LEU A  32           
SHEET    4  AA 5 TYR A 261  VAL A 264  1  O  TYR A 261   N  ILE A   8           
SHEET    5  AA 5 VAL A 425  PHE A 427  1  O  TYR A 426   N  VAL A 264           
SHEET    1  AB 2 LYS A  46  PHE A  49  0                                        
SHEET    2  AB 2 ILE A  52  GLU A  55 -1  O  ILE A  52   N  PHE A  49           
SHEET    1  AC 3 TRP A  60  VAL A  64  0                                        
SHEET    2  AC 3 ASP A 195  VAL A 199 -1  O  ASP A 195   N  GLY A  63           
SHEET    3  AC 3 ASN A  84  ARG A  86 -1  O  PHE A  85   N  PHE A 198           
SHEET    1  AD 6 VAL A  96  LYS A  98  0                                        
SHEET    2  AD 6 PHE A 318  ALA A 322  1  O  LEU A 320   N  TYR A  97           
SHEET    3  AD 6 VAL A 331  GLU A 334 -1  O  TRP A 332   N  PHE A 319           
SHEET    4  AD 6 VAL A 344  THR A 350 -1  O  LEU A 346   N  GLN A 333           
SHEET    5  AD 6 TYR A 298  LYS A 304 -1  O  THR A 299   N  VAL A 349           
SHEET    6  AD 6 ASP A 387  LEU A 389 -1  O  ASP A 387   N  LYS A 304           
SHEET    1  AE 4 VAL A 256  ALA A 259  0                                        
SHEET    2  AE 4 VAL A 247  THR A 251 -1  O  VAL A 247   N  ALA A 259           
SHEET    3  AE 4 VAL A 237  TYR A 242 -1  N  ARG A 238   O  LYS A 250           
SHEET    4  AE 4 GLN A 277  LYS A 279  1  O  GLN A 277   N  ILE A 240           
SHEET    1  AF 2 ASP A 294  ALA A 296  0                                        
SHEET    2  AF 2 PHE A 403  ASN A 405 -1  O  PHE A 403   N  ALA A 296           
SHEET    1  BA 5 LEU B 231  GLN B 232  0                                        
SHEET    2  BA 5 ASP B  30  LEU B  34  1  O  ILE B  33   N  GLN B 232           
SHEET    3  BA 5 ARG B   6  VAL B  10  1  O  VAL B   7   N  LEU B  32           
SHEET    4  BA 5 TYR B 261  VAL B 264  1  O  TYR B 261   N  ILE B   8           
SHEET    5  BA 5 VAL B 425  PHE B 427  1  O  TYR B 426   N  VAL B 264           
SHEET    1  BB 2 LYS B  46  PHE B  49  0                                        
SHEET    2  BB 2 ILE B  52  GLU B  55 -1  O  ILE B  52   N  PHE B  49           
SHEET    1  BC 3 TRP B  60  VAL B  64  0                                        
SHEET    2  BC 3 ASP B 195  VAL B 199 -1  O  ASP B 195   N  GLY B  63           
SHEET    3  BC 3 ASN B  84  ARG B  86 -1  O  PHE B  85   N  PHE B 198           
SHEET    1  BD 6 VAL B  96  LYS B  98  0                                        
SHEET    2  BD 6 PHE B 318  ALA B 322  1  O  LEU B 320   N  TYR B  97           
SHEET    3  BD 6 VAL B 331  GLU B 334 -1  O  TRP B 332   N  PHE B 319           
SHEET    4  BD 6 VAL B 344  THR B 350 -1  O  LEU B 346   N  GLN B 333           
SHEET    5  BD 6 TYR B 298  LYS B 304 -1  O  THR B 299   N  VAL B 349           
SHEET    6  BD 6 ASP B 387  LEU B 389 -1  O  ASP B 387   N  LYS B 304           
SHEET    1  BE 4 VAL B 256  ALA B 259  0                                        
SHEET    2  BE 4 VAL B 247  THR B 251 -1  O  VAL B 247   N  ALA B 259           
SHEET    3  BE 4 VAL B 237  TYR B 242 -1  N  ARG B 238   O  LYS B 250           
SHEET    4  BE 4 GLN B 277  LYS B 279  1  O  GLN B 277   N  ILE B 240           
SHEET    1  BF 2 ASP B 294  ALA B 296  0                                        
SHEET    2  BF 2 PHE B 403  ASN B 405 -1  O  PHE B 403   N  ALA B 296           
SHEET    1  CA 5 LEU C 231  GLN C 232  0                                        
SHEET    2  CA 5 LEU C  31  LEU C  34  1  O  ILE C  33   N  GLN C 232           
SHEET    3  CA 5 VAL C   7  VAL C  10  1  O  VAL C   7   N  LEU C  32           
SHEET    4  CA 5 TYR C 261  VAL C 264  1  O  TYR C 261   N  ILE C   8           
SHEET    5  CA 5 VAL C 425  PHE C 427  1  O  TYR C 426   N  VAL C 264           
SHEET    1  CB 2 LYS C  46  PHE C  49  0                                        
SHEET    2  CB 2 ILE C  52  GLU C  55 -1  O  ILE C  52   N  PHE C  49           
SHEET    1  CC 3 TRP C  60  VAL C  64  0                                        
SHEET    2  CC 3 ASP C 195  VAL C 199 -1  O  ASP C 195   N  GLY C  63           
SHEET    3  CC 3 ASN C  84  ARG C  86 -1  O  PHE C  85   N  PHE C 198           
SHEET    1  CD 6 VAL C  96  LYS C  98  0                                        
SHEET    2  CD 6 PHE C 318  ALA C 322  1  O  LEU C 320   N  TYR C  97           
SHEET    3  CD 6 VAL C 331  GLU C 334 -1  O  TRP C 332   N  PHE C 319           
SHEET    4  CD 6 VAL C 344  THR C 350 -1  O  LEU C 346   N  GLN C 333           
SHEET    5  CD 6 TYR C 298  LYS C 304 -1  O  THR C 299   N  VAL C 349           
SHEET    6  CD 6 ASP C 387  LEU C 389 -1  O  ASP C 387   N  LYS C 304           
SHEET    1  CE 4 VAL C 256  ALA C 259  0                                        
SHEET    2  CE 4 GLY C 246  THR C 251 -1  O  VAL C 247   N  ALA C 259           
SHEET    3  CE 4 VAL C 237  SER C 243 -1  N  ARG C 238   O  LYS C 250           
SHEET    4  CE 4 GLN C 277  LYS C 279  1  O  GLN C 277   N  ILE C 240           
SHEET    1  CF 2 ASP C 294  ALA C 296  0                                        
SHEET    2  CF 2 PHE C 403  ASN C 405 -1  O  PHE C 403   N  ALA C 296           
SSBOND   1 CYS A  457    CYS A  463                          1555   1555  2.04  
SSBOND   2 CYS B  457    CYS B  463                          1555   1555  2.02  
SSBOND   3 CYS C  457    CYS C  463                          1555   1555  2.04  
LINK         ND2 ASN A  77                 C1  NAG D   1     1555   1555  1.40  
LINK         ND2 ASN B  77                 C1  NAG E   1     1555   1555  1.41  
LINK         ND2 ASN C  77                 C1  NAG F   1     1555   1555  1.42  
LINK         O4  NAG D   1                 C1  NAG D   2     1555   1555  1.81  
LINK         O4  NAG E   1                 C1  NAG E   2     1555   1555  1.79  
LINK         O4  NAG F   1                 C1  NAG F   2     1555   1555  1.70  
LINK         O3  NAG F   1                 C1  FCA F   5     1555   1555  1.31  
LINK         O4  NAG F   2                 C1  MAN F   3     1555   1555  1.09  
LINK         O6  MAN F   3                 C1  MAN F   4     1555   1555  1.38  
CISPEP   1 VAL A  184    PRO A  185          0        -2.52                     
CISPEP   2 LYS A  279    PRO A  280          0        -0.18                     
CISPEP   3 VAL B  184    PRO B  185          0        -0.85                     
CISPEP   4 LYS B  279    PRO B  280          0        -0.39                     
CISPEP   5 VAL C  184    PRO C  185          0        -4.26                     
CISPEP   6 LYS C  279    PRO C  280          0         2.44                     
CRYST1  181.770  181.770  277.530  90.00  90.00 120.00 P 65 2 2     36          
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      0.005501  0.003176  0.000000        0.00000                         
SCALE2      0.000000  0.006352  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003603        0.00000                         
MTRIX1   1  0.137894 -0.485816  0.863115       84.16400    1                    
MTRIX2   1  0.487082  0.792042  0.367994      -60.69300    1                    
MTRIX3   1 -0.862402  0.369664  0.345850      107.70600    1                    
MTRIX1   2 -0.387625 -0.912764  0.128873      189.07800    1                    
MTRIX2   2 -0.357429  0.019957 -0.933727      114.48400    1                    
MTRIX3   2  0.849701 -0.407999 -0.333984      -57.26700    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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