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Database: PDB
Entry: 3MPH
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Original site: 3MPH 
HEADER    OXIDOREDUCTASE                          27-APR-10   3MPH              
TITLE     THE STRUCTURE OF HUMAN DIAMINE OXIDASE COMPLEXED WITH AN INHIBITOR    
TITLE    2 AMINOGUANIDINE                                                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: AMILORIDE-SENSITIVE AMINE OXIDASE;                         
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: DIAMINE OXIDASE, DAO, AMILORIDE-BINDING PROTEIN, ABP,       
COMPND   5 HISTAMINASE, KIDNEY AMINE OXIDASE, KAO;                              
COMPND   6 EC: 1.4.3.22;                                                        
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 CELL_LINE: SCHNEIDER 2;                                              
SOURCE   6 GENE: ABP1;                                                          
SOURCE   7 EXPRESSION_SYSTEM: DROSOPHILA MELANOGASTER;                          
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7227;                                       
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PMTDAO                                    
KEYWDS    OXIDOREDUCTASE, COPPER AMINE OXIDASE, CAO, TOPAQUINONE, TPQ, DIAMINE  
KEYWDS   2 OXIDASE, DAO, HUMAN, AMINOGUANIDINE                                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.P.MCGRATH,J.M.GUSS                                                  
REVDAT   3   05-MAR-14 3MPH    1       JRNL                                     
REVDAT   2   18-APR-12 3MPH    1       SHEET  VERSN                             
REVDAT   1   08-SEP-10 3MPH    0                                                
JRNL        AUTH   A.P.MCGRATH,T.CARADOC-DAVIES,C.A.COLLYER,J.M.GUSS            
JRNL        TITL   CORRELATION OF ACTIVE SITE METAL CONTENT IN HUMAN DIAMINE    
JRNL        TITL 2 OXIDASE WITH TRIHYDROXYPHENYLALANINE QUINONE COFACTOR        
JRNL        TITL 3 BIOGENESIS                                                   
JRNL        REF    BIOCHEMISTRY                  V.  49  8316 2010              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   20722416                                                     
JRNL        DOI    10.1021/BI1010915                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.05 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0088                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.05                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 31.13                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 101159                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.179                           
REMARK   3   R VALUE            (WORKING SET) : 0.177                           
REMARK   3   FREE R VALUE                     : 0.215                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 5416                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.05                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.10                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 6417                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 84.86                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2770                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 353                          
REMARK   3   BIN FREE R VALUE                    : 0.3100                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 11408                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 185                                     
REMARK   3   SOLVENT ATOMS            : 997                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 18.60                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 14.10                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.12000                                              
REMARK   3    B22 (A**2) : -0.34000                                             
REMARK   3    B33 (A**2) : 0.22000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.160         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.106         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.969         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.946                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.918                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 12161 ; 0.009 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  8132 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 16684 ; 1.251 ; 1.953       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 19637 ; 0.798 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1472 ; 6.732 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   581 ;31.410 ;22.943       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1729 ;12.587 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    78 ;16.041 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1776 ; 0.072 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 13651 ; 0.005 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  2668 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  7218 ; 0.496 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  2862 ; 0.099 ; 1.500       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 11720 ; 0.928 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  4943 ; 1.396 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  4941 ; 2.253 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS U VALUES: REFINED INDIVIDUALLY                            
REMARK   4                                                                      
REMARK   4 3MPH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 13-MAY-10.                  
REMARK 100 THE RCSB ID CODE IS RCSB058836.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 25-NOV-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU RU200                       
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NI FILTER                          
REMARK 200  OPTICS                         : OSMIC MIRRORS                      
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MAR SCANNER 345 MM PLATE           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 106658                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.037                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 31.136                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.6                               
REMARK 200  DATA REDUNDANCY                : 4.300                              
REMARK 200  R MERGE                    (I) : 0.13500                            
REMARK 200  R SYM                      (I) : 0.13500                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.03                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.14                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 77.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.49000                            
REMARK 200  R SYM FOR SHELL            (I) : 0.49000                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.600                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: BY REFINEMENT                
REMARK 200 SOFTWARE USED: REFMAC 5.5.0088                                       
REMARK 200 STARTING MODEL: PDB ENTRY 3HI7                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 52.22                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.57                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M BIS-TRIS PROPANE, 20%(W/V) PEG      
REMARK 280  3350, 0.2M SODIUM SULFATE, PH 7.5, VAPOR DIFFUSION, HANGING DROP,   
REMARK 280  TEMPERATURE 298K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
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       46.34250            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       98.02550            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       47.30200            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       98.02550            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       46.34250            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       47.30200            
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: 17220 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 45990 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -89.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
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     ARG A    21                                                      
REMARK 465     SER A    22                                                      
REMARK 465     PRO A    23                                                      
REMARK 465     GLY A    24                                                      
REMARK 465     THR A    25                                                      
REMARK 465     LEU A    26                                                      
REMARK 465     PRO A    27                                                      
REMARK 465     PRO A   268                                                      
REMARK 465     GLY A   269                                                      
REMARK 465     GLY A   270                                                      
REMARK 465     LYS A   271                                                      
REMARK 465     GLY A   272                                                      
REMARK 465     HIS A   273                                                      
REMARK 465     ASP A   274                                                      
REMARK 465     SER A   275                                                      
REMARK 465     THR A   276                                                      
REMARK 465     GLU A   277                                                      
REMARK 465     ARG B    21                                                      
REMARK 465     SER B    22                                                      
REMARK 465     PRO B    23                                                      
REMARK 465     GLY B    24                                                      
REMARK 465     THR B    25                                                      
REMARK 465     LEU B    26                                                      
REMARK 465     PRO B    27                                                      
REMARK 465     GLU B   264                                                      
REMARK 465     ASP B   265                                                      
REMARK 465     PRO B   266                                                      
REMARK 465     LEU B   267                                                      
REMARK 465     PRO B   268                                                      
REMARK 465     GLY B   269                                                      
REMARK 465     GLY B   270                                                      
REMARK 465     LYS B   271                                                      
REMARK 465     GLY B   272                                                      
REMARK 465     HIS B   273                                                      
REMARK 465     ASP B   274                                                      
REMARK 465     SER B   275                                                      
REMARK 465     THR B   276                                                      
REMARK 465     GLU B   277                                                      
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     ARG A  28    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A  29    CG   CD   CE   NZ                                   
REMARK 470     GLN A  39    CG   CD   OE1  NE2                                  
REMARK 470     LYS A  52    CE   NZ                                             
REMARK 470     ARG A  55    CZ   NH1  NH2                                       
REMARK 470     LYS A  78    NZ                                                  
REMARK 470     ARG A  91    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN A 135    OE1  NE2                                            
REMARK 470     LYS A 241    CE   NZ                                             
REMARK 470     ARG A 251    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP A 259    CG   OD1  OD2                                       
REMARK 470     GLU A 264    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 278    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 526    CG   CD   CE   NZ                                   
REMARK 470     GLN A 533    CG   CD   OE1  NE2                                  
REMARK 470     ARG A 568    NE   CZ   NH1  NH2                                  
REMARK 470     LYS A 570    CG   CD   CE   NZ                                   
REMARK 470     ARG A 571    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 572    CG   CD   CE   NZ                                   
REMARK 470     LYS A 575    CD   CE   NZ                                        
REMARK 470     LYS A 590    CD   CE   NZ                                        
REMARK 470     ARG B  28    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B  29    CG   CD   CE   NZ                                   
REMARK 470     GLN B  39    CG   CD   OE1  NE2                                  
REMARK 470     LYS B  52    CG   CD   CE   NZ                                   
REMARK 470     ARG B  55    NH1  NH2                                            
REMARK 470     ARG B  91    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B 126    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     SER B 129    OG                                                  
REMARK 470     GLN B 164    CG   CD   OE1  NE2                                  
REMARK 470     GLU B 278    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 313    CG   CD   OE1  OE2                                  
REMARK 470     GLN B 533    CG   CD   OE1  NE2                                  
REMARK 470     LYS B 535    CD   CE   NZ                                        
REMARK 470     ARG B 546    NE   CZ   NH1  NH2                                  
REMARK 470     ARG B 568    CZ   NH1  NH2                                       
REMARK 470     LYS B 570    CG   CD   CE   NZ                                   
REMARK 470     ARG B 571    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 572    CG   CD   CE   NZ                                   
REMARK 470     LYS B 590    CE   NZ                                             
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    HIS A 178      -64.75   -136.97                                   
REMARK 500    ARG A 190       67.06   -117.97                                   
REMARK 500    ASN A 239       48.30     37.94                                   
REMARK 500    VAL A 381       42.50    -99.74                                   
REMARK 500    ILE A 389      -66.97   -123.17                                   
REMARK 500    LYS A 436       41.51   -142.56                                   
REMARK 500    TYR A 459      -83.20   -154.52                                   
REMARK 500    VAL A 604      -60.82    -98.41                                   
REMARK 500    GLN A 610     -107.24     43.63                                   
REMARK 500    THR B  62       46.29    -80.46                                   
REMARK 500    ASP B 105       64.41   -102.34                                   
REMARK 500    SER B 129       58.27     26.94                                   
REMARK 500    HIS B 178     -103.66     58.87                                   
REMARK 500    VAL B 381       47.57   -102.20                                   
REMARK 500    ILE B 389      -65.78   -106.50                                   
REMARK 500    TYR B 459      -81.33   -159.49                                   
REMARK 500    SER B 544       77.44   -162.23                                   
REMARK 500    GLN B 610     -110.33     39.80                                   
REMARK 500    ASN B 657       60.72     36.56                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU B 801  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B 512   NE2                                                    
REMARK 620 2 HIS B 675   ND1 137.0                                              
REMARK 620 3 HIS B 510   NE2  98.0  96.1                                        
REMARK 620 4 HOH B 986   O   109.4 110.6  91.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU A 801  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 510   NE2                                                    
REMARK 620 2 HIS A 675   ND1  97.5                                              
REMARK 620 3 HIS A 512   NE2 100.3 138.8                                        
REMARK 620 4 HOH A 985   O    94.9 114.1 101.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B 802  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 521   OD1                                                    
REMARK 620 2 ASP B 664   OD1  91.1                                              
REMARK 620 3 ASP B 519   OD1  89.5 102.5                                        
REMARK 620 4 LEU B 665   O   167.1 101.4  84.7                                  
REMARK 620 5 LEU B 520   O    78.6 156.0  99.1  90.9                            
REMARK 620 6 HOH B 893   O    86.2  86.3 170.4  97.8  71.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 802  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 664   OD1                                                    
REMARK 620 2 ASP A 519   OD1  99.2                                              
REMARK 620 3 LEU A 520   O   159.2 101.1                                        
REMARK 620 4 LEU A 665   O    98.2  83.9  88.5                                  
REMARK 620 5 ASP A 521   OD1  93.8  87.7  82.5 166.3                            
REMARK 620 6 HOH A  20   O    88.1 172.7  71.8  94.2  92.8                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B 803  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU B 658   OE1                                                    
REMARK 620 2 GLU B 562   OE1 105.0                                              
REMARK 620 3 PHE B 653   O   169.4  85.6                                        
REMARK 620 4 ASN B 656   OD1  85.1  81.5  95.6                                  
REMARK 620 5 GLU B 562   OE2  84.9  51.7 102.8 127.1                            
REMARK 620 6 HOH B1022   O    80.8 124.2  94.2 153.1  74.3                      
REMARK 620 7 HOH B   5   O    91.1 150.2  79.0  74.8 157.0  82.6                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 803  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 658   OE1                                                    
REMARK 620 2 PHE A 653   O   168.8                                              
REMARK 620 3 GLU A 562   OE2  94.4  95.0                                        
REMARK 620 4 GLU A 562   OE1 100.9  89.8  52.5                                  
REMARK 620 5 ASN A 656   OD1  85.2  93.4 130.2  78.6                            
REMARK 620 6 HOH A 758   O    80.1  95.8  77.8 130.3 149.5                      
REMARK 620 7 HOH A 814   O    88.2  80.7 152.8 153.2  77.0  76.0                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU A 801                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 802                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 803                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 1101                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 1102                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA A 1103                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 5381                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 5382                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 7451                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 7452                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU B 801                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 802                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 803                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 1101                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 1102                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 5381                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 5382                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 7451                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 7452                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3HI7   RELATED DB: PDB                                   
REMARK 900 THE CRYSTAL STRUCTURE OF HUMAN DIAMINE OXIDASE                       
REMARK 900 RELATED ID: 3HIG   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HUMAN DIAMINE OXIDASE IN COMPLEX WITH           
REMARK 900 THE INHIBITOR BERENIL                                                
REMARK 900 RELATED ID: 3HII   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HUMAN DIAMINE OXIDASE IN COMPLEX WITH           
REMARK 900 THE INHIBITOR PENTAMIDINE                                            
REMARK 900 RELATED ID: 3K5T   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HUMAN DIAMINE OXIDASE IN SPACE GROUP            
REMARK 900 C2221                                                                
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 REFER TO THE FOLLOWING PARTS OF UNP DATABASE P19801.                 
REMARK 999 NATURAL VARIANT FOR RESIDUE 645,                                     
REMARK 999 SEQUENCE CONFLICT OF EXPERIMENTAL INFO FOR RESIDUE 592.              
DBREF  3MPH A   21   751  UNP    P19801   ABP1_HUMAN      21    751             
DBREF  3MPH B   21   751  UNP    P19801   ABP1_HUMAN      21    751             
SEQADV 3MPH ARG A   21  UNP  P19801    PRO    21 ENGINEERED MUTATION            
SEQADV 3MPH SER A  592  UNP  P19801    THR   592 SEE REMARK 999                 
SEQADV 3MPH ASP A  645  UNP  P19801    HIS   645 SEE REMARK 999                 
SEQADV 3MPH ARG B   21  UNP  P19801    PRO    21 ENGINEERED MUTATION            
SEQADV 3MPH SER B  592  UNP  P19801    THR   592 SEE REMARK 999                 
SEQADV 3MPH ASP B  645  UNP  P19801    HIS   645 SEE REMARK 999                 
SEQRES   1 A  731  ARG SER PRO GLY THR LEU PRO ARG LYS ALA GLY VAL PHE          
SEQRES   2 A  731  SER ASP LEU SER ASN GLN GLU LEU LYS ALA VAL HIS SER          
SEQRES   3 A  731  PHE LEU TRP SER LYS LYS GLU LEU ARG LEU GLN PRO SER          
SEQRES   4 A  731  SER THR THR THR MET ALA LYS ASN THR VAL PHE LEU ILE          
SEQRES   5 A  731  GLU MET LEU LEU PRO LYS LYS TYR HIS VAL LEU ARG PHE          
SEQRES   6 A  731  LEU ASP LYS GLY GLU ARG HIS PRO VAL ARG GLU ALA ARG          
SEQRES   7 A  731  ALA VAL ILE PHE PHE GLY ASP GLN GLU HIS PRO ASN VAL          
SEQRES   8 A  731  THR GLU PHE ALA VAL GLY PRO LEU PRO GLY PRO CYS TYR          
SEQRES   9 A  731  MET ARG ALA LEU SER PRO ARG PRO GLY TYR GLN SER SER          
SEQRES  10 A  731  TRP ALA SER ARG PRO ILE SER THR ALA GLU TYR ALA LEU          
SEQRES  11 A  731  LEU TYR HIS THR LEU GLN GLU ALA THR LYS PRO LEU HIS          
SEQRES  12 A  731  GLN PHE PHE LEU ASN THR THR GLY PHE SER PHE GLN ASP          
SEQRES  13 A  731  CYS HIS ASP ARG CYS LEU ALA PHE THR ASP VAL ALA PRO          
SEQRES  14 A  731  ARG GLY VAL ALA SER GLY GLN ARG ARG SER TRP LEU ILE          
SEQRES  15 A  731  ILE GLN ARG TYR VAL GLU GLY TYR PHE LEU HIS PRO THR          
SEQRES  16 A  731  GLY LEU GLU LEU LEU VAL ASP HIS GLY SER THR ASP ALA          
SEQRES  17 A  731  GLY HIS TRP ALA VAL GLU GLN VAL TRP TYR ASN GLY LYS          
SEQRES  18 A  731  PHE TYR GLY SER PRO GLU GLU LEU ALA ARG LYS TYR ALA          
SEQRES  19 A  731  ASP GLY GLU VAL ASP VAL VAL VAL LEU GLU ASP PRO LEU          
SEQRES  20 A  731  PRO GLY GLY LYS GLY HIS ASP SER THR GLU GLU PRO PRO          
SEQRES  21 A  731  LEU PHE SER SER HIS LYS PRO ARG GLY ASP PHE PRO SER          
SEQRES  22 A  731  PRO ILE HIS VAL SER GLY PRO ARG LEU VAL GLN PRO HIS          
SEQRES  23 A  731  GLY PRO ARG PHE ARG LEU GLU GLY ASN ALA VAL LEU TYR          
SEQRES  24 A  731  GLY GLY TRP SER PHE ALA PHE ARG LEU ARG SER SER SER          
SEQRES  25 A  731  GLY LEU GLN VAL LEU ASN VAL HIS PHE GLY GLY GLU ARG          
SEQRES  26 A  731  ILE ALA TYR GLU VAL SER VAL GLN GLU ALA VAL ALA LEU          
SEQRES  27 A  731  TYR GLY GLY HIS THR PRO ALA GLY MET GLN THR LYS TYR          
SEQRES  28 A  731  LEU ASP VAL GLY TRP GLY LEU GLY SER VAL THR HIS GLU          
SEQRES  29 A  731  LEU ALA PRO GLY ILE ASP CYS PRO GLU THR ALA THR PHE          
SEQRES  30 A  731  LEU ASP THR PHE HIS TYR TYR ASP ALA ASP ASP PRO VAL          
SEQRES  31 A  731  HIS TYR PRO ARG ALA LEU CYS LEU PHE GLU MET PRO THR          
SEQRES  32 A  731  GLY VAL PRO LEU ARG ARG HIS PHE ASN SER ASN PHE LYS          
SEQRES  33 A  731  GLY GLY PHE ASN PHE TYR ALA GLY LEU LYS GLY GLN VAL          
SEQRES  34 A  731  LEU VAL LEU ARG THR THR SER THR VAL TYR ASN AGQ ASP          
SEQRES  35 A  731  TYR ILE TRP ASP PHE ILE PHE TYR PRO ASN GLY VAL MET          
SEQRES  36 A  731  GLU ALA LYS MET HIS ALA THR GLY TYR VAL HIS ALA THR          
SEQRES  37 A  731  PHE TYR THR PRO GLU GLY LEU ARG HIS GLY THR ARG LEU          
SEQRES  38 A  731  HIS THR HIS LEU ILE GLY ASN ILE HIS THR HIS LEU VAL          
SEQRES  39 A  731  HIS TYR ARG VAL ASP LEU ASP VAL ALA GLY THR LYS ASN          
SEQRES  40 A  731  SER PHE GLN THR LEU GLN MET LYS LEU GLU ASN ILE THR          
SEQRES  41 A  731  ASN PRO TRP SER PRO ARG HIS ARG VAL VAL GLN PRO THR          
SEQRES  42 A  731  LEU GLU GLN THR GLN TYR SER TRP GLU ARG GLN ALA ALA          
SEQRES  43 A  731  PHE ARG PHE LYS ARG LYS LEU PRO LYS TYR LEU LEU PHE          
SEQRES  44 A  731  THR SER PRO GLN GLU ASN PRO TRP GLY HIS LYS ARG SER          
SEQRES  45 A  731  TYR ARG LEU GLN ILE HIS SER MET ALA ASP GLN VAL LEU          
SEQRES  46 A  731  PRO PRO GLY TRP GLN GLU GLU GLN ALA ILE THR TRP ALA          
SEQRES  47 A  731  ARG TYR PRO LEU ALA VAL THR LYS TYR ARG GLU SER GLU          
SEQRES  48 A  731  LEU CYS SER SER SER ILE TYR HIS GLN ASN ASP PRO TRP          
SEQRES  49 A  731  ASP PRO PRO VAL VAL PHE GLU GLN PHE LEU HIS ASN ASN          
SEQRES  50 A  731  GLU ASN ILE GLU ASN GLU ASP LEU VAL ALA TRP VAL THR          
SEQRES  51 A  731  VAL GLY PHE LEU HIS ILE PRO HIS SER GLU ASP ILE PRO          
SEQRES  52 A  731  ASN THR ALA THR PRO GLY ASN SER VAL GLY PHE LEU LEU          
SEQRES  53 A  731  ARG PRO PHE ASN PHE PHE PRO GLU ASP PRO SER LEU ALA          
SEQRES  54 A  731  SER ARG ASP THR VAL ILE VAL TRP PRO ARG ASP ASN GLY          
SEQRES  55 A  731  PRO ASN TYR VAL GLN ARG TRP ILE PRO GLU ASP ARG ASP          
SEQRES  56 A  731  CYS SER MET PRO PRO PRO PHE SER TYR ASN GLY THR TYR          
SEQRES  57 A  731  ARG PRO VAL                                                  
SEQRES   1 B  731  ARG SER PRO GLY THR LEU PRO ARG LYS ALA GLY VAL PHE          
SEQRES   2 B  731  SER ASP LEU SER ASN GLN GLU LEU LYS ALA VAL HIS SER          
SEQRES   3 B  731  PHE LEU TRP SER LYS LYS GLU LEU ARG LEU GLN PRO SER          
SEQRES   4 B  731  SER THR THR THR MET ALA LYS ASN THR VAL PHE LEU ILE          
SEQRES   5 B  731  GLU MET LEU LEU PRO LYS LYS TYR HIS VAL LEU ARG PHE          
SEQRES   6 B  731  LEU ASP LYS GLY GLU ARG HIS PRO VAL ARG GLU ALA ARG          
SEQRES   7 B  731  ALA VAL ILE PHE PHE GLY ASP GLN GLU HIS PRO ASN VAL          
SEQRES   8 B  731  THR GLU PHE ALA VAL GLY PRO LEU PRO GLY PRO CYS TYR          
SEQRES   9 B  731  MET ARG ALA LEU SER PRO ARG PRO GLY TYR GLN SER SER          
SEQRES  10 B  731  TRP ALA SER ARG PRO ILE SER THR ALA GLU TYR ALA LEU          
SEQRES  11 B  731  LEU TYR HIS THR LEU GLN GLU ALA THR LYS PRO LEU HIS          
SEQRES  12 B  731  GLN PHE PHE LEU ASN THR THR GLY PHE SER PHE GLN ASP          
SEQRES  13 B  731  CYS HIS ASP ARG CYS LEU ALA PHE THR ASP VAL ALA PRO          
SEQRES  14 B  731  ARG GLY VAL ALA SER GLY GLN ARG ARG SER TRP LEU ILE          
SEQRES  15 B  731  ILE GLN ARG TYR VAL GLU GLY TYR PHE LEU HIS PRO THR          
SEQRES  16 B  731  GLY LEU GLU LEU LEU VAL ASP HIS GLY SER THR ASP ALA          
SEQRES  17 B  731  GLY HIS TRP ALA VAL GLU GLN VAL TRP TYR ASN GLY LYS          
SEQRES  18 B  731  PHE TYR GLY SER PRO GLU GLU LEU ALA ARG LYS TYR ALA          
SEQRES  19 B  731  ASP GLY GLU VAL ASP VAL VAL VAL LEU GLU ASP PRO LEU          
SEQRES  20 B  731  PRO GLY GLY LYS GLY HIS ASP SER THR GLU GLU PRO PRO          
SEQRES  21 B  731  LEU PHE SER SER HIS LYS PRO ARG GLY ASP PHE PRO SER          
SEQRES  22 B  731  PRO ILE HIS VAL SER GLY PRO ARG LEU VAL GLN PRO HIS          
SEQRES  23 B  731  GLY PRO ARG PHE ARG LEU GLU GLY ASN ALA VAL LEU TYR          
SEQRES  24 B  731  GLY GLY TRP SER PHE ALA PHE ARG LEU ARG SER SER SER          
SEQRES  25 B  731  GLY LEU GLN VAL LEU ASN VAL HIS PHE GLY GLY GLU ARG          
SEQRES  26 B  731  ILE ALA TYR GLU VAL SER VAL GLN GLU ALA VAL ALA LEU          
SEQRES  27 B  731  TYR GLY GLY HIS THR PRO ALA GLY MET GLN THR LYS TYR          
SEQRES  28 B  731  LEU ASP VAL GLY TRP GLY LEU GLY SER VAL THR HIS GLU          
SEQRES  29 B  731  LEU ALA PRO GLY ILE ASP CYS PRO GLU THR ALA THR PHE          
SEQRES  30 B  731  LEU ASP THR PHE HIS TYR TYR ASP ALA ASP ASP PRO VAL          
SEQRES  31 B  731  HIS TYR PRO ARG ALA LEU CYS LEU PHE GLU MET PRO THR          
SEQRES  32 B  731  GLY VAL PRO LEU ARG ARG HIS PHE ASN SER ASN PHE LYS          
SEQRES  33 B  731  GLY GLY PHE ASN PHE TYR ALA GLY LEU LYS GLY GLN VAL          
SEQRES  34 B  731  LEU VAL LEU ARG THR THR SER THR VAL TYR ASN AGQ ASP          
SEQRES  35 B  731  TYR ILE TRP ASP PHE ILE PHE TYR PRO ASN GLY VAL MET          
SEQRES  36 B  731  GLU ALA LYS MET HIS ALA THR GLY TYR VAL HIS ALA THR          
SEQRES  37 B  731  PHE TYR THR PRO GLU GLY LEU ARG HIS GLY THR ARG LEU          
SEQRES  38 B  731  HIS THR HIS LEU ILE GLY ASN ILE HIS THR HIS LEU VAL          
SEQRES  39 B  731  HIS TYR ARG VAL ASP LEU ASP VAL ALA GLY THR LYS ASN          
SEQRES  40 B  731  SER PHE GLN THR LEU GLN MET LYS LEU GLU ASN ILE THR          
SEQRES  41 B  731  ASN PRO TRP SER PRO ARG HIS ARG VAL VAL GLN PRO THR          
SEQRES  42 B  731  LEU GLU GLN THR GLN TYR SER TRP GLU ARG GLN ALA ALA          
SEQRES  43 B  731  PHE ARG PHE LYS ARG LYS LEU PRO LYS TYR LEU LEU PHE          
SEQRES  44 B  731  THR SER PRO GLN GLU ASN PRO TRP GLY HIS LYS ARG SER          
SEQRES  45 B  731  TYR ARG LEU GLN ILE HIS SER MET ALA ASP GLN VAL LEU          
SEQRES  46 B  731  PRO PRO GLY TRP GLN GLU GLU GLN ALA ILE THR TRP ALA          
SEQRES  47 B  731  ARG TYR PRO LEU ALA VAL THR LYS TYR ARG GLU SER GLU          
SEQRES  48 B  731  LEU CYS SER SER SER ILE TYR HIS GLN ASN ASP PRO TRP          
SEQRES  49 B  731  ASP PRO PRO VAL VAL PHE GLU GLN PHE LEU HIS ASN ASN          
SEQRES  50 B  731  GLU ASN ILE GLU ASN GLU ASP LEU VAL ALA TRP VAL THR          
SEQRES  51 B  731  VAL GLY PHE LEU HIS ILE PRO HIS SER GLU ASP ILE PRO          
SEQRES  52 B  731  ASN THR ALA THR PRO GLY ASN SER VAL GLY PHE LEU LEU          
SEQRES  53 B  731  ARG PRO PHE ASN PHE PHE PRO GLU ASP PRO SER LEU ALA          
SEQRES  54 B  731  SER ARG ASP THR VAL ILE VAL TRP PRO ARG ASP ASN GLY          
SEQRES  55 B  731  PRO ASN TYR VAL GLN ARG TRP ILE PRO GLU ASP ARG ASP          
SEQRES  56 B  731  CYS SER MET PRO PRO PRO PHE SER TYR ASN GLY THR TYR          
SEQRES  57 B  731  ARG PRO VAL                                                  
MODRES 3MPH ASN A  745  ASN  GLYCOSYLATION SITE                                 
MODRES 3MPH ASN B  538  ASN  GLYCOSYLATION SITE                                 
MODRES 3MPH ASN A  538  ASN  GLYCOSYLATION SITE                                 
MODRES 3MPH ASN B  745  ASN  GLYCOSYLATION SITE                                 
MODRES 3MPH ASN A  110  ASN  GLYCOSYLATION SITE                                 
MODRES 3MPH ASN B  110  ASN  GLYCOSYLATION SITE                                 
MODRES 3MPH AGQ A  461  TYR                                                     
MODRES 3MPH AGQ B  461  TYR                                                     
HET    AGQ  A 461      18                                                       
HET    AGQ  B 461      18                                                       
HET     CU  A 801       1                                                       
HET     CA  A 802       1                                                       
HET     CA  A 803       1                                                       
HET    NAG  A1101      14                                                       
HET    NAG  A1102      14                                                       
HET    BMA  A1103      11                                                       
HET    NAG  A5381      14                                                       
HET    NAG  A5382      14                                                       
HET    NAG  A7451      14                                                       
HET    NAG  A7452      14                                                       
HET     CU  B 801       1                                                       
HET     CA  B 802       1                                                       
HET     CA  B 803       1                                                       
HET    NAG  B1101      14                                                       
HET    NAG  B1102      14                                                       
HET    NAG  B5381      14                                                       
HET    NAG  B5382      14                                                       
HET    NAG  B7451      14                                                       
HET    NAG  B7452      14                                                       
HETNAM     AGQ 3-[(3E)-3-(CARBAMIMIDOYLHYDRAZONO)-4-HYDROXY-6-                  
HETNAM   2 AGQ  OXOCYCLOHEXA-1,4-DIEN-1-YL]-L-ALANINE                           
HETNAM      CU COPPER (II) ION                                                  
HETNAM      CA CALCIUM ION                                                      
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     BMA BETA-D-MANNOSE                                                   
FORMUL   1  AGQ    2(C10 H13 N5 O4)                                             
FORMUL   3   CU    2(CU 2+)                                                     
FORMUL   4   CA    4(CA 2+)                                                     
FORMUL   6  NAG    12(C8 H15 N O6)                                              
FORMUL   6  BMA    C6 H12 O6                                                    
FORMUL  15  HOH   *997(H2 O)                                                    
HELIX    1   1 ARG A   28  SER A   34  5                                   7    
HELIX    2   2 SER A   37  LYS A   51  1                                  15    
HELIX    3   3 LYS A   52  ARG A   55  5                                   4    
HELIX    4   4 LYS A   78  GLY A   89  1                                  12    
HELIX    5   5 SER A  136  ARG A  141  1                                   6    
HELIX    6   6 SER A  144  THR A  159  1                                  16    
HELIX    7   7 LEU A  162  GLY A  171  1                                  10    
HELIX    8   8 GLY A  209  LEU A  212  5                                   4    
HELIX    9   9 ASP A  227  TRP A  231  5                                   5    
HELIX   10  10 SER A  245  ASP A  255  1                                  11    
HELIX   11  11 THR A  363  THR A  369  1                                   7    
HELIX   12  12 VAL A  374  GLY A  377  5                                   4    
HELIX   13  13 THR A  491  ARG A  496  5                                   6    
HELIX   14  14 TRP A  561  ALA A  566  5                                   6    
HELIX   15  15 TRP A  609  TYR A  620  5                                  12    
HELIX   16  16 ARG A  628  LEU A  632  5                                   5    
HELIX   17  17 GLU A  651  ASN A  656  1                                   6    
HELIX   18  18 HIS A  678  ILE A  682  5                                   5    
HELIX   19  19 ASP A  705  SER A  710  5                                   6    
HELIX   20  20 LYS B   29  SER B   34  5                                   6    
HELIX   21  21 SER B   37  SER B   50  1                                  14    
HELIX   22  22 LYS B   51  ARG B   55  5                                   5    
HELIX   23  23 LYS B   78  LYS B   88  1                                  11    
HELIX   24  24 SER B  136  ARG B  141  1                                   6    
HELIX   25  25 SER B  144  THR B  159  1                                  16    
HELIX   26  26 LEU B  162  GLY B  171  1                                  10    
HELIX   27  27 GLY B  209  LEU B  212  5                                   4    
HELIX   28  28 ASP B  227  TRP B  231  5                                   5    
HELIX   29  29 SER B  245  ASP B  255  1                                  11    
HELIX   30  30 THR B  363  THR B  369  1                                   7    
HELIX   31  31 VAL B  374  GLY B  377  5                                   4    
HELIX   32  32 THR B  491  ARG B  496  5                                   6    
HELIX   33  33 TRP B  561  ALA B  566  5                                   6    
HELIX   34  34 TRP B  609  TYR B  620  5                                  12    
HELIX   35  35 ARG B  628  LEU B  632  5                                   5    
HELIX   36  36 VAL B  649  HIS B  655  5                                   7    
HELIX   37  37 HIS B  678  ILE B  682  5                                   5    
HELIX   38  38 ASP B  705  SER B  710  5                                   6    
SHEET    1   A20 TYR A 124  LEU A 128  0                                        
SHEET    2   A20 ASN A 110  GLY A 117 -1  N  ALA A 115   O  ARG A 126           
SHEET    3   A20 GLU A  96  PHE A 103 -1  N  ALA A  97   O  VAL A 116           
SHEET    4   A20 ASN A  67  LEU A  75 -1  N  GLU A  73   O  ARG A  98           
SHEET    5   A20 THR A 396  TYR A 404 -1  O  TYR A 403   N  ILE A  72           
SHEET    6   A20 VAL A 410  PRO A 422 -1  O  TYR A 412   N  THR A 400           
SHEET    7   A20 GLN A 448  THR A 457 -1  O  VAL A 451   N  PHE A 419           
SHEET    8   A20 AGQ A 461  PHE A 469 -1  O  PHE A 469   N  LEU A 450           
SHEET    9   A20 MET A 475  GLY A 483 -1  O  GLU A 476   N  ILE A 468           
SHEET   10   A20 SER A 691  PHE A 699 -1  O  LEU A 696   N  MET A 475           
SHEET   11   A20 LYS A 590  HIS A 598 -1  N  SER A 592   O  PHE A 699           
SHEET   12   A20 TYR A 576  GLU A 584 -1  N  GLN A 583   O  ARG A 591           
SHEET   13   A20 LYS A 526  THR A 540 -1  N  GLN A 530   O  LEU A 578           
SHEET   14   A20 GLU A 663  HIS A 675 -1  O  GLU A 663   N  ASN A 527           
SHEET   15   A20 HIS A 510  LEU A 520 -1  N  HIS A 510   O  HIS A 675           
SHEET   16   A20 GLU A 344  TYR A 359 -1  N  VAL A 356   O  LEU A 513           
SHEET   17   A20 GLY A 333  PHE A 341 -1  N  VAL A 339   O  ILE A 346           
SHEET   18   A20 TRP A 322  ARG A 329 -1  N  ALA A 325   O  LEU A 337           
SHEET   19   A20 ALA A 316  TYR A 319 -1  N  VAL A 317   O  PHE A 324           
SHEET   20   A20 ARG A 311  GLU A 313 -1  N  ARG A 311   O  LEU A 318           
SHEET    1   B 4 ARG A 548  GLN A 558  0                                        
SHEET    2   B 4 LYS A 526  THR A 540 -1  N  GLN A 533   O  GLU A 555           
SHEET    3   B 4 GLU A 663  HIS A 675 -1  O  GLU A 663   N  ASN A 527           
SHEET    4   B 4 LEU A 622  LYS A 626 -1  N  ALA A 623   O  TRP A 668           
SHEET    1   C 5 LYS A 370  LEU A 372  0                                        
SHEET    2   C 5 GLU A 344  TYR A 359 -1  N  ALA A 357   O  TYR A 371           
SHEET    3   C 5 HIS A 510  LEU A 520 -1  O  LEU A 513   N  VAL A 356           
SHEET    4   C 5 GLU A 663  HIS A 675 -1  O  HIS A 675   N  HIS A 510           
SHEET    5   C 5 LEU A 622  LYS A 626 -1  N  ALA A 623   O  TRP A 668           
SHEET    1   D 5 LEU A 182  ASP A 186  0                                        
SHEET    2   D 5 ARG A 198  ARG A 205 -1  O  GLN A 204   N  ALA A 183           
SHEET    3   D 5 PRO A 214  ASP A 222 -1  O  VAL A 221   N  SER A 199           
SHEET    4   D 5 ALA A 232  TYR A 238 -1  O  TRP A 237   N  GLU A 218           
SHEET    5   D 5 LYS A 241  PHE A 242 -1  O  LYS A 241   N  TYR A 238           
SHEET    1   E 2 ARG A 301  VAL A 303  0                                        
SHEET    2   E 2 ARG B 301  VAL B 303 -1  O  VAL B 303   N  ARG A 301           
SHEET    1   F 4 ARG A 428  SER A 433  0                                        
SHEET    2   F 4 PHE A 439  LEU A 445 -1  O  ASN A 440   N  ASN A 432           
SHEET    3   F 4 VAL A 714  TRP A 717 -1  O  VAL A 714   N  GLY A 444           
SHEET    4   F 4 TYR A 725  GLN A 727 -1  O  GLN A 727   N  ILE A 715           
SHEET    1   G 3 ALA A 487  PHE A 489  0                                        
SHEET    2   G 3 LEU A 505  ASN A 508 -1  O  ILE A 506   N  THR A 488           
SHEET    3   G 3 GLY A 498  HIS A 502 -1  N  THR A 499   O  GLY A 507           
SHEET    1   H14 TYR B 124  ALA B 127  0                                        
SHEET    2   H14 ASN B 110  GLY B 117 -1  N  ALA B 115   O  ARG B 126           
SHEET    3   H14 GLU B  96  PHE B 103 -1  N  ALA B  97   O  VAL B 116           
SHEET    4   H14 ASN B  67  LEU B  75 -1  N  GLU B  73   O  ARG B  98           
SHEET    5   H14 THR B 396  TYR B 404 -1  O  TYR B 403   N  ILE B  72           
SHEET    6   H14 VAL B 410  PRO B 422 -1  O  TYR B 412   N  THR B 400           
SHEET    7   H14 GLN B 448  THR B 457 -1  O  ARG B 453   N  CYS B 417           
SHEET    8   H14 AGQ B 461  PHE B 469 -1  O  PHE B 469   N  LEU B 450           
SHEET    9   H14 MET B 475  GLY B 483 -1  O  LYS B 478   N  ASP B 466           
SHEET   10   H14 SER B 691  PHE B 699 -1  O  LEU B 696   N  MET B 475           
SHEET   11   H14 LYS B 590  HIS B 598 -1  N  ARG B 594   O  ARG B 697           
SHEET   12   H14 TYR B 576  GLU B 584 -1  N  SER B 581   O  ARG B 591           
SHEET   13   H14 SER B 528  THR B 540 -1  N  GLN B 530   O  LEU B 578           
SHEET   14   H14 ARG B 548  GLN B 558 -1  O  VAL B 549   N  ILE B 539           
SHEET    1   I 5 LEU B 182  ASP B 186  0                                        
SHEET    2   I 5 ARG B 198  ARG B 205 -1  O  ILE B 202   N  THR B 185           
SHEET    3   I 5 PRO B 214  ASP B 222 -1  O  LEU B 219   N  LEU B 201           
SHEET    4   I 5 ALA B 232  TYR B 238 -1  O  TRP B 237   N  GLU B 218           
SHEET    5   I 5 LYS B 241  PHE B 242 -1  O  LYS B 241   N  TYR B 238           
SHEET    1   J 6 ARG B 311  GLU B 313  0                                        
SHEET    2   J 6 ALA B 316  TYR B 319 -1  O  LEU B 318   N  ARG B 311           
SHEET    3   J 6 TRP B 322  ARG B 329 -1  O  PHE B 324   N  VAL B 317           
SHEET    4   J 6 GLY B 333  PHE B 341 -1  O  LEU B 337   N  ALA B 325           
SHEET    5   J 6 GLU B 344  TYR B 359 -1  O  ILE B 346   N  VAL B 339           
SHEET    6   J 6 LYS B 370  LEU B 372 -1  O  TYR B 371   N  ALA B 357           
SHEET    1   K 8 ARG B 311  GLU B 313  0                                        
SHEET    2   K 8 ALA B 316  TYR B 319 -1  O  LEU B 318   N  ARG B 311           
SHEET    3   K 8 TRP B 322  ARG B 329 -1  O  PHE B 324   N  VAL B 317           
SHEET    4   K 8 GLY B 333  PHE B 341 -1  O  LEU B 337   N  ALA B 325           
SHEET    5   K 8 GLU B 344  TYR B 359 -1  O  ILE B 346   N  VAL B 339           
SHEET    6   K 8 HIS B 510  LEU B 520 -1  O  LEU B 513   N  VAL B 356           
SHEET    7   K 8 LEU B 665  HIS B 675 -1  O  ALA B 667   N  VAL B 518           
SHEET    8   K 8 LEU B 622  LYS B 626 -1  N  THR B 625   O  VAL B 666           
SHEET    1   L 4 ARG B 428  SER B 433  0                                        
SHEET    2   L 4 PHE B 439  LEU B 445 -1  O  ASN B 440   N  ASN B 432           
SHEET    3   L 4 VAL B 714  TRP B 717 -1  O  VAL B 716   N  TYR B 442           
SHEET    4   L 4 TYR B 725  ARG B 728 -1  O  GLN B 727   N  ILE B 715           
SHEET    1   M 3 ALA B 487  PHE B 489  0                                        
SHEET    2   M 3 LEU B 505  ASN B 508 -1  O  ILE B 506   N  THR B 488           
SHEET    3   M 3 GLY B 498  HIS B 502 -1  N  THR B 499   O  GLY B 507           
SSBOND   1 CYS A  177    CYS A  181                          1555   1555  2.06  
SSBOND   2 CYS A  391    CYS A  417                          1555   1555  2.04  
SSBOND   3 CYS A  736    CYS B  736                          1555   1555  2.05  
SSBOND   4 CYS B  177    CYS B  181                          1555   1555  2.05  
SSBOND   5 CYS B  391    CYS B  417                          1555   1555  2.05  
LINK         C   ASN A 460                 N   AGQ A 461     1555   1555  1.34  
LINK         C   AGQ A 461                 N   ASP A 462     1555   1555  1.33  
LINK         C   ASN B 460                 N   AGQ B 461     1555   1555  1.34  
LINK         C   AGQ B 461                 N   ASP B 462     1555   1555  1.32  
LINK         ND2 ASN A 745                 C1  NAG A7451     1555   1555  1.42  
LINK         O4  NAG A7451                 C1  NAG A7452     1555   1555  1.43  
LINK         ND2 ASN B 538                 C1  NAG B5381     1555   1555  1.43  
LINK         O4  NAG B1101                 C1  NAG B1102     1555   1555  1.43  
LINK         O4  NAG A1101                 C1  NAG A1102     1555   1555  1.44  
LINK         O4  NAG B5381                 C1  NAG B5382     1555   1555  1.44  
LINK         ND2 ASN A 538                 C1  NAG A5381     1555   1555  1.44  
LINK         ND2 ASN B 745                 C1  NAG B7451     1555   1555  1.44  
LINK         O4  NAG B7451                 C1  NAG B7452     1555   1555  1.44  
LINK         ND2 ASN A 110                 C1  NAG A1101     1555   1555  1.44  
LINK         O4  NAG A5381                 C1  NAG A5382     1555   1555  1.45  
LINK         ND2 ASN B 110                 C1  NAG B1101     1555   1555  1.45  
LINK         O4  NAG A1102                 C1  BMA A1103     1555   1555  1.46  
LINK         NE2 HIS B 512                CU    CU B 801     1555   1555  1.98  
LINK         ND1 HIS B 675                CU    CU B 801     1555   1555  2.02  
LINK         NE2 HIS B 510                CU    CU B 801     1555   1555  2.03  
LINK         NE2 HIS A 510                CU    CU A 801     1555   1555  2.03  
LINK         ND1 HIS A 675                CU    CU A 801     1555   1555  2.04  
LINK         NE2 HIS A 512                CU    CU A 801     1555   1555  2.07  
LINK         OD1 ASP B 521                CA    CA B 802     1555   1555  2.13  
LINK         OD1 ASP B 664                CA    CA B 802     1555   1555  2.22  
LINK         OD1 ASP A 664                CA    CA A 802     1555   1555  2.27  
LINK         OD1 ASP B 519                CA    CA B 802     1555   1555  2.29  
LINK         OE1 GLU B 658                CA    CA B 803     1555   1555  2.29  
LINK         OD1 ASP A 519                CA    CA A 802     1555   1555  2.30  
LINK         O   LEU A 520                CA    CA A 802     1555   1555  2.31  
LINK         O   LEU A 665                CA    CA A 802     1555   1555  2.31  
LINK         OE1 GLU A 658                CA    CA A 803     1555   1555  2.32  
LINK         OD1 ASP A 521                CA    CA A 802     1555   1555  2.32  
LINK         O   LEU B 665                CA    CA B 802     1555   1555  2.33  
LINK         O   PHE A 653                CA    CA A 803     1555   1555  2.34  
LINK         OE1 GLU B 562                CA    CA B 803     1555   1555  2.34  
LINK         O   PHE B 653                CA    CA B 803     1555   1555  2.35  
LINK         O   LEU B 520                CA    CA B 802     1555   1555  2.41  
LINK         OE2 GLU A 562                CA    CA A 803     1555   1555  2.42  
LINK         OD1 ASN B 656                CA    CA B 803     1555   1555  2.43  
LINK         OE1 GLU A 562                CA    CA A 803     1555   1555  2.50  
LINK         OD1 ASN A 656                CA    CA A 803     1555   1555  2.51  
LINK         OE2 GLU B 562                CA    CA B 803     1555   1555  2.61  
LINK        CU    CU B 801                 O   HOH B 986     1555   1555  2.19  
LINK        CA    CA B 803                 O   HOH B1022     1555   1555  2.29  
LINK        CU    CU A 801                 O   HOH A 985     1555   1555  2.31  
LINK        CA    CA A 803                 O   HOH A 758     1555   1555  2.34  
LINK        CA    CA A 803                 O   HOH A 814     1555   1555  2.39  
LINK        CA    CA B 802                 O   HOH B 893     1555   1555  2.44  
LINK        CA    CA A 802                 O   HOH A  20     1555   1555  2.44  
LINK        CA    CA B 803                 O   HOH B   5     1555   1555  2.46  
CISPEP   1 GLY A  117    PRO A  118          0        -7.32                     
CISPEP   2 LEU A  119    PRO A  120          0         0.58                     
CISPEP   3 ALA A  188    PRO A  189          0         3.49                     
CISPEP   4 ILE A  682    PRO A  683          0         3.23                     
CISPEP   5 GLY B  117    PRO B  118          0        -2.48                     
CISPEP   6 LEU B  119    PRO B  120          0        -1.39                     
CISPEP   7 ALA B  188    PRO B  189          0         3.90                     
CISPEP   8 ILE B  682    PRO B  683          0         1.33                     
SITE     1 AC1  4 HIS A 510  HIS A 512  HIS A 675  HOH A 985                    
SITE     1 AC2  6 HOH A  20  ASP A 519  LEU A 520  ASP A 521                    
SITE     2 AC2  6 ASP A 664  LEU A 665                                          
SITE     1 AC3  6 GLU A 562  PHE A 653  ASN A 656  GLU A 658                    
SITE     2 AC3  6 HOH A 758  HOH A 814                                          
SITE     1 AC4  4 GLN A 106  ASN A 110  THR A 112  NAG A1102                    
SITE     1 AC5  4 LEU A  54  ARG A 719  NAG A1101  BMA A1103                    
SITE     1 AC6  4 GLY A 722  PRO A 723  HOH A 881  NAG A1102                    
SITE     1 AC7  4 ASN A 538  ARG A 548  NAG A5382  TRP B 609                    
SITE     1 AC8  1 NAG A5381                                                     
SITE     1 AC9  4 ASN A 745  HOH A 884  NAG A7452  ASN B 724                    
SITE     1 BC1  1 NAG A7451                                                     
SITE     1 BC2  4 HIS B 510  HIS B 512  HIS B 675  HOH B 986                    
SITE     1 BC3  6 ASP B 519  LEU B 520  ASP B 521  ASP B 664                    
SITE     2 BC3  6 LEU B 665  HOH B 893                                          
SITE     1 BC4  6 HOH B   5  GLU B 562  PHE B 653  ASN B 656                    
SITE     2 BC4  6 GLU B 658  HOH B1022                                          
SITE     1 BC5  6 PHE B 103  GLN B 106  ASN B 110  THR B 112                    
SITE     2 BC5  6 GLU B 257  NAG B1102                                          
SITE     1 BC6  2 LEU B  54  NAG B1101                                          
SITE     1 BC7  5 ASN B 538  ARG B 548  HOH B 829  HOH B1146                    
SITE     2 BC7  5 NAG B5382                                                     
SITE     1 BC8  2 HOH B 829  NAG B5381                                          
SITE     1 BC9  4 ASN A 724  ASN B 745  HOH B1075  NAG B7452                    
SITE     1 CC1  1 NAG B7451                                                     
CRYST1   92.685   94.604  196.051  90.00  90.00  90.00 P 21 21 21    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      0.010789  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010570  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005101        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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