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Database: PDB
Entry: 1HX0
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HEADER    HYDROLASE                               11-JAN-01   1HX0              
TITLE     STRUCTURE OF PIG PANCREATIC ALPHA-AMYLASE COMPLEXED WITH THE          
TITLE    2 "TRUNCATE" ACARBOSE MOLECULE (PSEUDOTRISACCHARIDE)                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ALPHA AMYLASE (PPA);                                       
COMPND   3 CHAIN: A;                                                            
COMPND   4 EC: 3.2.1.1                                                          
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SUS SCROFA;                                     
SOURCE   3 ORGANISM_COMMON: PIG;                                                
SOURCE   4 ORGANISM_TAXID: 9823;                                                
SOURCE   5 TISSUE: PANCREAS                                                     
KEYWDS    ALPHA-AMYLASE, INHIBITOR, CARBOHYDRATE, PANCREAS, HYDROLASE           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.QIAN,F.PAYAN                                                        
REVDAT   5   13-JUL-11 1HX0    1       VERSN                                    
REVDAT   4   04-AUG-09 1HX0    1       HETATM HETNAM REMARK                     
REVDAT   3   24-FEB-09 1HX0    1       VERSN                                    
REVDAT   2   31-DEC-02 1HX0    1       REMARK                                   
REVDAT   1   08-AUG-01 1HX0    0                                                
JRNL        AUTH   M.QIAN,V.NAHOUM,J.BONICEL,H.BISCHOFF,B.HENRISSAT,F.PAYAN     
JRNL        TITL   ENZYME-CATALYZED CONDENSATION REACTION IN A MAMMALIAN        
JRNL        TITL 2 ALPHA-AMYLASE. HIGH-RESOLUTION STRUCTURAL ANALYSIS OF AN     
JRNL        TITL 3 ENZYME-INHIBITOR COMPLEX                                     
JRNL        REF    BIOCHEMISTRY                  V.  40  7700 2001              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   11412124                                                     
JRNL        DOI    10.1021/BI0102050                                            
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   C.GILLES,J.P.ASTIER,G.MARCHIS-MOUREN,C.CAMBILLAU,F.PAYAN     
REMARK   1  TITL   CRYSTAL STRUCTURE OF PIG PANCREATIC ALPHA-AMYLASE ISOENZYME  
REMARK   1  TITL 2 II, IN COMPLEX WITH THE CARBOHYDRATE INHIBITOR ACARBOSE      
REMARK   1  REF    EUR.J.BIOCHEM.                V. 238   561 1996              
REMARK   1  REFN                   ISSN 0014-2956                               
REMARK   1  PMID   8681972                                                      
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   M.QIAN,R.HASER,G.BUISSON,E.DUEE,F.PAYAN                      
REMARK   1  TITL   THE ACTIVE CENTER OF A MAMMALIAN ALPHA-AMYLASE. STRUCTURE OF 
REMARK   1  TITL 2 THE COMPLEX OF A PANCREATIC ALPHA-AMYLASE WITH A             
REMARK   1  TITL 3 CARBOHYDRATE INHIBITOR REFINED TO 2.2-A RESOLUTION           
REMARK   1  REF    BIOCHEMISTRY                  V.  33  6284 1994              
REMARK   1  REFN                   ISSN 0006-2960                               
REMARK   1  PMID   8193143                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.38 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : SHELXL-97                                            
REMARK   3   AUTHORS     : G.M.SHELDRICK                                        
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.38                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 35.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 1.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.0                           
REMARK   3   CROSS-VALIDATION METHOD           : THROUGHOUT FREE R              
REMARK   3   FREE R VALUE TEST SET SELECTION   : RANDOM                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (NO CUTOFF).                         
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : 0.108                  
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : 0.108                  
REMARK   3   FREE R VALUE                  (NO CUTOFF) : 0.130                  
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : 2938                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : 184003                 
REMARK   3                                                                      
REMARK   3  FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).                     
REMARK   3   R VALUE   (WORKING + TEST SET, F>4SIG(F)) : NULL                   
REMARK   3   R VALUE          (WORKING SET, F>4SIG(F)) : NULL                   
REMARK   3   FREE R VALUE                  (F>4SIG(F)) : NULL                   
REMARK   3   FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : NULL                   
REMARK   3   FREE R VALUE TEST SET COUNT   (F>4SIG(F)) : NULL                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (F>4SIG(F)) : NULL                   
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS      : 3911                                          
REMARK   3   NUCLEIC ACID ATOMS : 0                                             
REMARK   3   HETEROGEN ATOMS    : 152                                           
REMARK   3   SOLVENT ATOMS      : 921                                           
REMARK   3                                                                      
REMARK   3  MODEL REFINEMENT.                                                   
REMARK   3   OCCUPANCY SUM OF NON-HYDROGEN ATOMS      : NULL                    
REMARK   3   OCCUPANCY SUM OF HYDROGEN ATOMS          : NULL                    
REMARK   3   NUMBER OF DISCRETELY DISORDERED RESIDUES : NULL                    
REMARK   3   NUMBER OF LEAST-SQUARES PARAMETERS       : NULL                    
REMARK   3   NUMBER OF RESTRAINTS                     : NULL                    
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.                        
REMARK   3   BOND LENGTHS                         (A) : NULL                    
REMARK   3   ANGLE DISTANCES                      (A) : NULL                    
REMARK   3   SIMILAR DISTANCES (NO TARGET VALUES) (A) : NULL                    
REMARK   3   DISTANCES FROM RESTRAINT PLANES      (A) : NULL                    
REMARK   3   ZERO CHIRAL VOLUMES               (A**3) : NULL                    
REMARK   3   NON-ZERO CHIRAL VOLUMES           (A**3) : NULL                    
REMARK   3   ANTI-BUMPING DISTANCE RESTRAINTS     (A) : NULL                    
REMARK   3   RIGID-BOND ADP COMPONENTS         (A**2) : NULL                    
REMARK   3   SIMILAR ADP COMPONENTS            (A**2) : NULL                    
REMARK   3   APPROXIMATELY ISOTROPIC ADPS      (A**2) : NULL                    
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED: NULL                                                  
REMARK   3                                                                      
REMARK   3  STEREOCHEMISTRY TARGET VALUES : ENGH & HUBER                        
REMARK   3   SPECIAL CASE: NULL                                                 
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1HX0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 17-JAN-01.                  
REMARK 100 THE RCSB ID CODE IS RCSB012644.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 20-NOV-99                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID14-2                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.933                              
REMARK 200  MONOCHROMATOR                  : BOUBLE-DIAMOND CRYSTAL (111)       
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 184003                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.380                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 35.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.0                               
REMARK 200  DATA REDUNDANCY                : 2.800                              
REMARK 200  R MERGE                    (I) : 0.06700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 13.1000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.38                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.42                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.58100                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.930                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: PDB ENTRY 1PPI                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 70.38                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.15                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: CACL2, PH 8.5, BATCH, TEMPERATURE 277K   
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       34.64000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       58.58000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       56.77500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       58.58000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       34.64000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       56.77500            
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: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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    ARG A  20   CD  -  NE  -  CZ  ANGL. DEV. =  11.0 DEGREES          
REMARK 500    CYS A  70   CA  -  CB  -  SG  ANGL. DEV. =   8.1 DEGREES          
REMARK 500    ARG A  80   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.5 DEGREES          
REMARK 500    ARG A  92   NE  -  CZ  -  NH1 ANGL. DEV. =  -5.8 DEGREES          
REMARK 500    HIS A 101   CG  -  ND1 -  CE1 ANGL. DEV. =  13.2 DEGREES          
REMARK 500    HIS A 101   ND1 -  CE1 -  NE2 ANGL. DEV. =  -9.9 DEGREES          
REMARK 500    ARG A 124   CD  -  NE  -  CZ  ANGL. DEV. =  24.3 DEGREES          
REMARK 500    ARG A 124   NE  -  CZ  -  NH1 ANGL. DEV. =   6.6 DEGREES          
REMARK 500    ARG A 158   NE  -  CZ  -  NH1 ANGL. DEV. =   4.9 DEGREES          
REMARK 500    ARG A 158   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.2 DEGREES          
REMARK 500    ARG A 227   NE  -  CZ  -  NH1 ANGL. DEV. =  -4.1 DEGREES          
REMARK 500    ARG A 227   NE  -  CZ  -  NH2 ANGL. DEV. =   3.3 DEGREES          
REMARK 500    GLU A 240   OE1 -  CD  -  OE2 ANGL. DEV. = -16.3 DEGREES          
REMARK 500    ARG A 252   NE  -  CZ  -  NH2 ANGL. DEV. =   3.9 DEGREES          
REMARK 500    ARG A 291   NE  -  CZ  -  NH2 ANGL. DEV. =   3.3 DEGREES          
REMARK 500    ASP A 317   CB  -  CG  -  OD2 ANGL. DEV. =  -7.6 DEGREES          
REMARK 500    HIS A 331   CG  -  ND1 -  CE1 ANGL. DEV. =   7.9 DEGREES          
REMARK 500    HIS A 331   ND1 -  CE1 -  NE2 ANGL. DEV. =  -7.2 DEGREES          
REMARK 500    PRO A 332   O   -  C   -  N   ANGL. DEV. = -11.2 DEGREES          
REMARK 500    ARG A 346   NE  -  CZ  -  NH1 ANGL. DEV. =   4.3 DEGREES          
REMARK 500    ARG A 389   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.7 DEGREES          
REMARK 500    ARG A 389   NE  -  CZ  -  NH2 ANGL. DEV. =   4.0 DEGREES          
REMARK 500    ARG A 392   NE  -  CZ  -  NH1 ANGL. DEV. =  -4.1 DEGREES          
REMARK 500    ASN A 460   C   -  N   -  CA  ANGL. DEV. =  19.2 DEGREES          
REMARK 500    HIS A 491   CG  -  ND1 -  CE1 ANGL. DEV. =   9.5 DEGREES          
REMARK 500    HIS A 491   ND1 -  CE1 -  NE2 ANGL. DEV. =  -7.7 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    TYR A  31      -60.20   -143.55                                   
REMARK 500    MET A 102     -148.07   -104.81                                   
REMARK 500    VAL A 163       47.71     37.73                                   
REMARK 500    ASP A 317       57.92   -108.67                                   
REMARK 500    THR A 376        1.51     80.77                                   
REMARK 500    SER A 414     -106.88   -135.88                                   
REMARK 500    ASP A 433       35.35    -87.31                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A6186        DISTANCE =  6.07 ANGSTROMS                       
REMARK 525    HOH A6341        DISTANCE =  5.58 ANGSTROMS                       
REMARK 525    HOH A6488        DISTANCE =  5.55 ANGSTROMS                       
REMARK 525    HOH A6499        DISTANCE =  5.87 ANGSTROMS                       
REMARK 525    HOH A6626        DISTANCE =  5.12 ANGSTROMS                       
REMARK 525    HOH A6701        DISTANCE =  5.67 ANGSTROMS                       
REMARK 525    HOH A6739        DISTANCE =  6.10 ANGSTROMS                       
REMARK 525    HOH A6760        DISTANCE =  5.25 ANGSTROMS                       
REMARK 525    HOH A6771        DISTANCE =  6.32 ANGSTROMS                       
REMARK 525    HOH A6804        DISTANCE =  5.30 ANGSTROMS                       
REMARK 525    HOH A6813        DISTANCE =  6.23 ANGSTROMS                       
REMARK 525    HOH A6829        DISTANCE =  6.29 ANGSTROMS                       
REMARK 525    HOH A6833        DISTANCE =  6.23 ANGSTROMS                       
REMARK 525    HOH A6882        DISTANCE =  5.29 ANGSTROMS                       
REMARK 525    HOH A6890        DISTANCE =  5.31 ANGSTROMS                       
REMARK 525    HOH A6915        DISTANCE =  6.01 ANGSTROMS                       
REMARK 525    HOH A6949        DISTANCE =  5.45 ANGSTROMS                       
REMARK 525    HOH A6954        DISTANCE =  5.19 ANGSTROMS                       
REMARK 525    HOH A6966        DISTANCE =  7.20 ANGSTROMS                       
REMARK 525    HOH A6968        DISTANCE =  5.44 ANGSTROMS                       
REMARK 525    HOH A6991        DISTANCE =  6.17 ANGSTROMS                       
REMARK 600                                                                      
REMARK 600 HETEROGEN                                                            
REMARK 600 RESIDUE GLC 1993 AND GBC 2993 ARE IN ALTERNATE CONFORMATIONS OF      
REMARK 600 EACH OTHER.                                                          
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                              CA A 500  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN A 100   OD1                                                    
REMARK 620 2 ARG A 158   O   155.5                                              
REMARK 620 3 ASP A 167   OD1  80.9 120.7                                        
REMARK 620 4 ASP A 167   OD2 127.6  76.9  52.7                                  
REMARK 620 5 HIS A 201   O    75.7  80.0 140.8 156.2                            
REMARK 620 6 HOH A6017   O    70.8 122.5  76.4  75.4 122.8                      
REMARK 620 7 HOH A6031   O   102.0  72.1 134.2  96.1  81.8  62.3                
REMARK 620 8 HOH A6023   O   101.0  77.8  71.3  87.0  82.8 147.7 148.1          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC A 1991                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AC1 A 1990                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AC1 A 1992                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC A 1993                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BGC A 2993                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAL A 1994                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 498                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 499                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 501                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 502                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 500                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 5000                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 5001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 5002                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 5003                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 5004                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 5005                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 5006                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 5007                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 5008                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 5010                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 5013                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 5014                
DBREF  1HX0 A    1   496  UNP    P00690   AMYP_PIG        16    511             
SEQADV 1HX0 PCA A    1  UNP  P00690    GLN    16 ENGINEERED                     
SEQADV 1HX0 ASN A  123  UNP  P00690    SER   138 CONFLICT                       
SEQADV 1HX0 LYS A  243  UNP  P00690    GLN   258 CONFLICT                       
SEQADV 1HX0 SER A  310  UNP  P00690    ALA   325 CONFLICT                       
SEQADV 1HX0 ILE A  323  UNP  P00690    VAL   338 CONFLICT                       
SEQADV 1HX0 GLN A  404  UNP  P00690    GLU   419 CONFLICT                       
SEQRES   1 A  496  PCA TYR ALA PRO GLN THR GLN SER GLY ARG THR SER ILE          
SEQRES   2 A  496  VAL HIS LEU PHE GLU TRP ARG TRP VAL ASP ILE ALA LEU          
SEQRES   3 A  496  GLU CYS GLU ARG TYR LEU GLY PRO LYS GLY PHE GLY GLY          
SEQRES   4 A  496  VAL GLN VAL SER PRO PRO ASN GLU ASN ILE VAL VAL THR          
SEQRES   5 A  496  ASN PRO SER ARG PRO TRP TRP GLU ARG TYR GLN PRO VAL          
SEQRES   6 A  496  SER TYR LYS LEU CYS THR ARG SER GLY ASN GLU ASN GLU          
SEQRES   7 A  496  PHE ARG ASP MET VAL THR ARG CYS ASN ASN VAL GLY VAL          
SEQRES   8 A  496  ARG ILE TYR VAL ASP ALA VAL ILE ASN HIS MET CYS GLY          
SEQRES   9 A  496  SER GLY ALA ALA ALA GLY THR GLY THR THR CYS GLY SER          
SEQRES  10 A  496  TYR CYS ASN PRO GLY ASN ARG GLU PHE PRO ALA VAL PRO          
SEQRES  11 A  496  TYR SER ALA TRP ASP PHE ASN ASP GLY LYS CYS LYS THR          
SEQRES  12 A  496  ALA SER GLY GLY ILE GLU SER TYR ASN ASP PRO TYR GLN          
SEQRES  13 A  496  VAL ARG ASP CYS GLN LEU VAL GLY LEU LEU ASP LEU ALA          
SEQRES  14 A  496  LEU GLU LYS ASP TYR VAL ARG SER MET ILE ALA ASP TYR          
SEQRES  15 A  496  LEU ASN LYS LEU ILE ASP ILE GLY VAL ALA GLY PHE ARG          
SEQRES  16 A  496  ILE ASP ALA SER LYS HIS MET TRP PRO GLY ASP ILE LYS          
SEQRES  17 A  496  ALA VAL LEU ASP LYS LEU HIS ASN LEU ASN THR ASN TRP          
SEQRES  18 A  496  PHE PRO ALA GLY SER ARG PRO PHE ILE PHE GLN GLU VAL          
SEQRES  19 A  496  ILE ASP LEU GLY GLY GLU ALA ILE LYS SER SER GLU TYR          
SEQRES  20 A  496  PHE GLY ASN GLY ARG VAL THR GLU PHE LYS TYR GLY ALA          
SEQRES  21 A  496  LYS LEU GLY THR VAL VAL ARG LYS TRP SER GLY GLU LYS          
SEQRES  22 A  496  MET SER TYR LEU LYS ASN TRP GLY GLU GLY TRP GLY PHE          
SEQRES  23 A  496  MET PRO SER ASP ARG ALA LEU VAL PHE VAL ASP ASN HIS          
SEQRES  24 A  496  ASP ASN GLN ARG GLY HIS GLY ALA GLY GLY SER SER ILE          
SEQRES  25 A  496  LEU THR PHE TRP ASP ALA ARG LEU TYR LYS ILE ALA VAL          
SEQRES  26 A  496  GLY PHE MET LEU ALA HIS PRO TYR GLY PHE THR ARG VAL          
SEQRES  27 A  496  MET SER SER TYR ARG TRP ALA ARG ASN PHE VAL ASN GLY          
SEQRES  28 A  496  GLU ASP VAL ASN ASP TRP ILE GLY PRO PRO ASN ASN ASN          
SEQRES  29 A  496  GLY VAL ILE LYS GLU VAL THR ILE ASN ALA ASP THR THR          
SEQRES  30 A  496  CYS GLY ASN ASP TRP VAL CYS GLU HIS ARG TRP ARG GLU          
SEQRES  31 A  496  ILE ARG ASN MET VAL TRP PHE ARG ASN VAL VAL ASP GLY          
SEQRES  32 A  496  GLN PRO PHE ALA ASN TRP TRP ASP ASN GLY SER ASN GLN          
SEQRES  33 A  496  VAL ALA PHE GLY ARG GLY ASN ARG GLY PHE ILE VAL PHE          
SEQRES  34 A  496  ASN ASN ASP ASP TRP GLN LEU SER SER THR LEU GLN THR          
SEQRES  35 A  496  GLY LEU PRO GLY GLY THR TYR CYS ASP VAL ILE SER GLY          
SEQRES  36 A  496  ASP LYS VAL GLY ASN SER CYS THR GLY ILE LYS VAL TYR          
SEQRES  37 A  496  VAL SER SER ASP GLY THR ALA GLN PHE SER ILE SER ASN          
SEQRES  38 A  496  SER ALA GLU ASP PRO PHE ILE ALA ILE HIS ALA GLU SER          
SEQRES  39 A  496  LYS LEU                                                      
MODRES 1HX0 PCA A    1  GLU  PYROGLUTAMIC ACID                                  
HET    PCA  A   1       8                                                       
HET    GLC  A1991      11                                                       
HET    AC1  A1990      21                                                       
HET    AC1  A1992      21                                                       
HET    GLC  A1993      12                                                       
HET    BGC  A2993      12                                                       
HET    MAL  A1994      22                                                       
HET     CL  A 498       1                                                       
HET     CL  A 499       1                                                       
HET     CL  A 501       1                                                       
HET     CL  A 502       1                                                       
HET     CA  A 500       1                                                       
HET    EDO  A5000       4                                                       
HET    EDO  A5001       4                                                       
HET    EDO  A5002       8                                                       
HET    EDO  A5003       4                                                       
HET    EDO  A5004       4                                                       
HET    EDO  A5005       4                                                       
HET    EDO  A5006       4                                                       
HET    EDO  A5007       4                                                       
HET    EDO  A5008       4                                                       
HET    EDO  A5010       4                                                       
HET    EDO  A5013       4                                                       
HET    EDO  A5014       4                                                       
HETNAM     PCA PYROGLUTAMIC ACID                                                
HETNAM     GLC ALPHA-D-GLUCOSE                                                  
HETNAM     AC1 6-METHYL-5-(4,5,6-TRIHYDROXY-3-HYDROXYMETHYL-CYCLOHEX-           
HETNAM   2 AC1  2-ENYLAMINO)-TETRAHYDRO-PYRAN-2,3,4-TRIOL                       
HETNAM     BGC BETA-D-GLUCOSE                                                   
HETNAM     MAL MALTOSE                                                          
HETNAM      CL CHLORIDE ION                                                     
HETNAM      CA CALCIUM ION                                                      
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETSYN     AC1 N-[4-HYDROXYMETHYL-CYCLOHEXAN-6-YL-1,2,3-TRIOL]-4,6-             
HETSYN   2 AC1  DIDEOXY-4-AMINOGLUCOPYRANOSIDE                                  
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   1  PCA    C5 H7 N O3                                                   
FORMUL   2  GLC    2(C6 H12 O6)                                                 
FORMUL   2  AC1    2(C13 H23 N O8)                                              
FORMUL   2  BGC    C6 H12 O6                                                    
FORMUL   3  MAL    C12 H22 O11                                                  
FORMUL   4   CL    4(CL 1-)                                                     
FORMUL   8   CA    CA 2+                                                        
FORMUL   9  EDO    12(C2 H6 O2)                                                 
FORMUL  21  HOH   *921(H2 O)                                                    
HELIX    1   1 ARG A   20  TYR A   31  1                                  12    
HELIX    2   2 PRO A   57  GLN A   63  5                                   7    
HELIX    3   3 ASN A   75  VAL A   89  1                                  15    
HELIX    4   4 ASN A  120  ARG A  124  5                                   5    
HELIX    5   5 SER A  132  PHE A  136  5                                   5    
HELIX    6   6 ASP A  153  CYS A  160  1                                   8    
HELIX    7   7 LYS A  172  GLY A  190  1                                  19    
HELIX    8   8 ALA A  198  MET A  202  5                                   5    
HELIX    9   9 TRP A  203  ASP A  212  1                                  10    
HELIX   10  10 LYS A  243  PHE A  248  5                                   6    
HELIX   11  11 PHE A  256  ARG A  267  1                                  12    
HELIX   12  12 LYS A  273  TRP A  280  5                                   8    
HELIX   13  13 GLY A  281  GLY A  285  5                                   5    
HELIX   14  14 PRO A  288  ASP A  290  5                                   3    
HELIX   15  15 ASP A  300  GLY A  304  5                                   5    
HELIX   16  16 GLY A  308  ILE A  312  5                                   5    
HELIX   17  17 THR A  314  TRP A  316  5                                   3    
HELIX   18  18 ASP A  317  HIS A  331  1                                  15    
HELIX   19  19 CYS A  384  ARG A  387  5                                   4    
HELIX   20  20 TRP A  388  VAL A  401  1                                  14    
HELIX   21  21 GLU A  493  LYS A  495  5                                   3    
SHEET    1   A 9 SER A  12  LEU A  16  0                                        
SHEET    2   A 9 GLY A  39  VAL A  42  1  O  GLN A  41   N  VAL A  14           
SHEET    3   A 9 ARG A  92  ALA A  97  1  O  TYR A  94   N  VAL A  40           
SHEET    4   A 9 GLY A 193  ILE A 196  1  O  ARG A 195   N  ALA A  97           
SHEET    5   A 9 PHE A 229  GLN A 232  1  O  PHE A 229   N  PHE A 194           
SHEET    6   A 9 ARG A 252  THR A 254  1  O  THR A 254   N  GLN A 232           
SHEET    7   A 9 ALA A 292  VAL A 294  1  O  LEU A 293   N  VAL A 253           
SHEET    8   A 9 PHE A 335  SER A 340  1  O  PHE A 335   N  VAL A 294           
SHEET    9   A 9 SER A  12  LEU A  16  1  N  ILE A  13   O  VAL A 338           
SHEET    1   B 2 HIS A 101  GLY A 104  0                                        
SHEET    2   B 2 LEU A 165  ASP A 167 -1  O  LEU A 166   N  CYS A 103           
SHEET    1   C 2 PHE A 348  VAL A 349  0                                        
SHEET    2   C 2 GLU A 352  ASP A 353 -1  O  GLU A 352   N  VAL A 349           
SHEET    1   D 2 ASN A 362  ASN A 363  0                                        
SHEET    2   D 2 VAL A 366  ILE A 367 -1  O  VAL A 366   N  ASN A 363           
SHEET    1   E 4 PHE A 406  ASP A 411  0                                        
SHEET    2   E 4 GLN A 416  ARG A 421 -1  O  GLY A 420   N  ALA A 407           
SHEET    3   E 4 GLY A 425  ASN A 430 -1  O  PHE A 429   N  VAL A 417           
SHEET    4   E 4 PHE A 487  HIS A 491 -1  O  ILE A 490   N  PHE A 426           
SHEET    1   F 2 LEU A 436  GLN A 441  0                                        
SHEET    2   F 2 THR A 474  ILE A 479 -1  O  ALA A 475   N  LEU A 440           
SHEET    1   G 2 GLY A 447  CYS A 450  0                                        
SHEET    2   G 2 LYS A 466  VAL A 469 -1  O  VAL A 469   N  GLY A 447           
SHEET    1   H 2 LYS A 457  VAL A 458  0                                        
SHEET    2   H 2 SER A 461  CYS A 462 -1  O  SER A 461   N  VAL A 458           
SSBOND   1 CYS A   28    CYS A   86                          1555   1555  2.16  
SSBOND   2 CYS A   70    CYS A  115                          1555   1555  2.03  
SSBOND   3 CYS A  141    CYS A  160                          1555   1555  2.11  
SSBOND   4 CYS A  378    CYS A  384                          1555   1555  2.10  
SSBOND   5 CYS A  450    CYS A  462                          1555   1555  2.00  
LINK         C   PCA A   1                 N   TYR A   2     1555   1555  1.33  
LINK         OD1 ASN A 100                CA    CA A 500     1555   1555  2.35  
LINK         O   ARG A 158                CA    CA A 500     1555   1555  2.37  
LINK         OD1 ASP A 167                CA    CA A 500     1555   1555  2.56  
LINK         OD2 ASP A 167                CA    CA A 500     1555   1555  2.48  
LINK         O   HIS A 201                CA    CA A 500     1555   1555  2.39  
LINK         C1  GLC A1991                 O4  AC1 A1992     1555   1555  1.39  
LINK         O4  GLC A1991                 C1  AC1 A1990     1555   1555  1.42  
LINK         C1  AC1 A1992                 O4 AGLC A1993     1555   1555  1.40  
LINK         C1  AC1 A1992                 O4 BBGC A2993     1555   1555  1.40  
LINK        CA    CA A 500                 O   HOH A6017     1555   1555  2.51  
LINK        CA    CA A 500                 O   HOH A6031     1555   1555  2.54  
LINK        CA    CA A 500                 O   HOH A6023     1555   1555  2.46  
LINK         C1' MAL A1994                 O2  EDO A5013     1555   1555  1.40  
CISPEP   1 ASN A   53    PRO A   54          0        -0.80                     
CISPEP   2 VAL A  129    PRO A  130          0        -5.34                     
SITE     1 AC1  6 TRP A  59  TYR A  62  GLN A  63  HIS A 305                    
SITE     2 AC1  6 AC1 A1990  AC1 A1992                                          
SITE     1 AC2 11 TRP A  59  GLN A  63  GLY A 104  SER A 105                    
SITE     2 AC2 11 GLY A 106  VAL A 163  GLY A 164  GLC A1991                    
SITE     3 AC2 11 HOH A6307  HOH A6608  HOH A6864                               
SITE     1 AC3 15 TRP A  58  TYR A  62  HIS A 101  ARG A 195                    
SITE     2 AC3 15 ASP A 197  ALA A 198  HIS A 201  GLU A 233                    
SITE     3 AC3 15 HIS A 299  ASP A 300  GLC A1991  GLC A1993                    
SITE     4 AC3 15 BGC A2993  HOH A6570  HOH A6610                               
SITE     1 AC4  8 TYR A 151  LYS A 200  ILE A 235  GLU A 240                    
SITE     2 AC4  8 ALA A 307  AC1 A1992  HOH A6380  HOH A6538                    
SITE     1 AC5  9 TYR A 151  LYS A 200  ILE A 235  GLU A 240                    
SITE     2 AC5  9 GLY A 306  AC1 A1992  HOH A6283  HOH A6378                    
SITE     3 AC5  9 HOH A6380                                                     
SITE     1 AC6 14 THR A  52  ASN A  53  SER A  55  LYS A 261                    
SITE     2 AC6 14 GLU A 272  TYR A 276  ASN A 279  TRP A 284                    
SITE     3 AC6 14 EDO A5013  HOH A6411  HOH A6462  HOH A6662                    
SITE     4 AC6 14 HOH A6684  HOH A6961                                          
SITE     1 AC7  3 ARG A 195  ASN A 298  ARG A 337                               
SITE     1 AC8  2 PRO A 204  GLY A 205                                          
SITE     1 AC9  6 ASN A 137  LYS A 140  ALA A 169  LEU A 170                    
SITE     2 AC9  6 GLU A 171  HOH A6720                                          
SITE     1 BC1  5 ASN A 216  GLY A 225  SER A 437  SER A 478                    
SITE     2 BC1  5 HOH A6309                                                     
SITE     1 BC2  7 ASN A 100  ARG A 158  ASP A 167  HIS A 201                    
SITE     2 BC2  7 HOH A6017  HOH A6023  HOH A6031                               
SITE     1 BC3  5 ARG A  30  THR A 376  ARG A 387  HOH A6157                    
SITE     2 BC3  5 HOH A6294                                                     
SITE     1 BC4  7 LYS A 466  VAL A 467  GLN A 476  PHE A 477                    
SITE     2 BC4  7 SER A 478  EDO A5004  HOH A6367                               
SITE     1 BC5 10 ILE A  49  VAL A  50  ALA A 108  ALA A 109                    
SITE     2 BC5 10 GLY A 110  THR A 111  GLY A 112  HOH A6269                    
SITE     3 BC5 10 HOH A6548  HOH A6557                                          
SITE     1 BC6  4 LYS A 322  TRP A 388  GLU A 390  HOH A6340                    
SITE     1 BC7  9 LYS A 213  LEU A 214  HIS A 215  LYS A 466                    
SITE     2 BC7  9 VAL A 467  TYR A 468  EDO A5001  HOH A6291                    
SITE     3 BC7  9 HOH A6367                                                     
SITE     1 BC8  7 ASN A 301  GLN A 302  SER A 310  ILE A 312                    
SITE     2 BC8  7 HOH A6688  HOH A6689  HOH A6724                               
SITE     1 BC9  5 ARG A 319  LYS A 322  GLU A 484  ASP A 485                    
SITE     2 BC9  5 HOH A6770                                                     
SITE     1 CC1  9 ARG A 343  ILE A 358  GLY A 359  PRO A 360                    
SITE     2 CC1  9 PRO A 361  ASP A 381  HOH A6165  HOH A6317                    
SITE     3 CC1  9 HOH A6591                                                     
SITE     1 CC2  5 ARG A  20  SER A  73  HOH A6233  HOH A6713                    
SITE     2 CC2  5 HOH A6753                                                     
SITE     1 CC3  6 PCA A   1  LEU A 211  ARG A 227  PRO A 228                    
SITE     2 CC3  6 ILE A 230  HOH A6935                                          
SITE     1 CC4  7 TYR A 276  MAL A1994  HOH A6362  HOH A6462                    
SITE     2 CC4  7 HOH A6616  HOH A6684  HOH A6685                               
SITE     1 CC5  7 ASN A 218  SER A 437  SER A 438  THR A 439                    
SITE     2 CC5  7 GLN A 476  HOH A6077  HOH A6113                               
CRYST1   69.280  113.550  117.160  90.00  90.00  90.00 P 21 21 21    4          
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      0.014434  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008807  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008535        0.00000                         
HETATM    1  N   PCA A   1      40.550  12.086  33.635  1.00 18.28           N  
ANISOU    1  N   PCA A   1     2989   1962   1995    101    259   -286       N  
HETATM    2  CA  PCA A   1      39.897  12.709  34.799  1.00 15.75           C  
ANISOU    2  CA  PCA A   1     2591   1593   1801    177    275    163       C  
HETATM    3  CB  PCA A   1      40.621  12.117  36.006  1.00 15.84           C  
ANISOU    3  CB  PCA A   1     2483   1540   1996    258    -54   -132       C  
HETATM    4  CG  PCA A   1      41.991  11.795  35.479  1.00 20.37           C  
ANISOU    4  CG  PCA A   1     2667   2591   2481    465    202     75       C  
HETATM    5  CD  PCA A   1      41.836  11.545  34.022  1.00 22.42           C  
ANISOU    5  CD  PCA A   1     3297   2618   2603    833    389   -551       C  
HETATM    6  OE  PCA A   1      42.580  11.024  33.224  1.00 26.55           O  
ANISOU    6  OE  PCA A   1     4043   2787   3258   1051    957   -496       O  
HETATM    7  C   PCA A   1      40.069  14.228  34.831  1.00 14.33           C  
ANISOU    7  C   PCA A   1     2129   1694   1623    213    120     42       C  
HETATM    8  O   PCA A   1      39.454  14.866  35.679  1.00 15.27           O  
ANISOU    8  O   PCA A   1     2318   1779   1706    116    359    -28       O  
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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