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Database: PDB
Entry: 1OSE
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Original site: 1OSE 
HEADER    HYDROLASE                               20-MAR-96   1OSE              
TITLE     PORCINE PANCREATIC ALPHA-AMYLASE COMPLEXED WITH ACARBOSE              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PORCINE ALPHA-AMYLASE;                                     
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: PPA;                                                        
COMPND   5 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 ORGAN: PANCREAS                                                      
KEYWDS    ALPHA-AMYLASE, ACARBOSE, HYDROLASE (O-GLYCOSYL), HYDROLASE            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.GILLES,F.PAYAN                                                      
REVDAT   3   25-AUG-09 1OSE    1       HET    HETATM HETNAM                     
REVDAT   2   24-FEB-09 1OSE    1       VERSN                                    
REVDAT   1   01-APR-97 1OSE    0                                                
JRNL        AUTH   C.GILLES,J.P.ASTIER,G.MARCHIS-MOUREN,C.CAMBILLAU,            
JRNL        AUTH 2 F.PAYAN                                                      
JRNL        TITL   CRYSTAL STRUCTURE OF PIG PANCREATIC ALPHA-AMYLASE            
JRNL        TITL 2 ISOENZYME II, IN COMPLEX WITH THE CARBOHYDRATE               
JRNL        TITL 3 INHIBITOR ACARBOSE.                                          
JRNL        REF    EUR.J.BIOCHEM.                V. 238   561 1996              
JRNL        REFN                   ISSN 0014-2956                               
JRNL        PMID   8681972                                                      
JRNL        DOI    10.1111/J.1432-1033.1996.0561Z.X                             
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   M.QIAN,R.HASER,F.PAYAN                                       
REMARK   1  TITL   CARBOHYDRATE BINDING SITES IN A PANCREATIC                   
REMARK   1  TITL 2 ALPHA-AMYLASE-SUBSTRATE COMPLEX, DERIVED FROM X-RAY          
REMARK   1  TITL 3 STRUCTURE ANALYSIS AT 2.1 A RESOLUTION                       
REMARK   1  REF    PROTEIN SCI.                  V.   4   747 1995              
REMARK   1  REFN                   ISSN 0961-8368                               
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.              
REMARK   1  TITL 2 STRUCTURE OF THE COMPLEX OF A PANCREATIC                     
REMARK   1  TITL 3 ALPHA-AMYLASE WITH A CARBOHYDRATE INHIBITOR REFINED          
REMARK   1  TITL 4 TO 2.2-A RESOLUTION                                          
REMARK   1  REF    BIOCHEMISTRY                  V.  33  6284 1994              
REMARK   1  REFN                   ISSN 0006-2960                               
REMARK   1 REFERENCE 3                                                          
REMARK   1  AUTH   M.QIAN,R.HASER,F.PAYAN                                       
REMARK   1  TITL   STRUCTURE AND MOLECULAR MODEL REFINEMENT OF PIG              
REMARK   1  TITL 2 PANCREATIC ALPHA-AMYLASE AT 2.1 A RESOLUTION                 
REMARK   1  REF    J.MOL.BIOL.                   V. 231   785 1993              
REMARK   1  REFN                   ISSN 0022-2836                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR 3.1                                           
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 8.00                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 90.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 37212                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.176                           
REMARK   3   FREE R VALUE                     : 0.222                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.000                          
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3907                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 79                                      
REMARK   3   SOLVENT ATOMS            : 403                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.18                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.024                           
REMARK   3   BOND ANGLES            (DEGREES) : 2.29                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 24.79                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.53                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1OSE COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : NULL                               
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MAR SCANNER 180 MM PLATE           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 41389                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.7                               
REMARK 200  DATA REDUNDANCY                : 3.100                              
REMARK 200  R MERGE                    (I) : 0.15700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: X-PLOR 3.1                                            
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 72.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.33                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
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       35.30000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       59.25000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       57.35000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       59.25000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       35.30000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       57.35000            
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    VAL A 323   CA  -  CB  -  CG2 ANGL. DEV. =  21.4 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      -60.30   -135.34                                   
REMARK 500    SER A  55       99.47    -61.33                                   
REMARK 500    SER A  66     -177.62   -171.93                                   
REMARK 500    MET A 102     -151.84   -113.58                                   
REMARK 500    ASP A 317       57.90   -110.18                                   
REMARK 500    SER A 414     -105.72   -137.79                                   
REMARK 500    PRO A 486       35.74    -70.60                                   
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 A1120        DISTANCE =  5.04 ANGSTROMS                       
REMARK 525    HOH A1240A       DISTANCE =  6.01 ANGSTROMS                       
REMARK 525    HOH A1374B       DISTANCE =  5.44 ANGSTROMS                       
REMARK 525    HOH A1380B       DISTANCE =  5.58 ANGSTROMS                       
REMARK 525    HOH A1382B       DISTANCE =  7.11 ANGSTROMS                       
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   156.5                                              
REMARK 620 3 ASP A 167   OD2 127.1  76.4                                        
REMARK 620 4 HIS A 201   O    73.8  82.7 158.8                                  
REMARK 620 5 HOH A1035   O   104.1  70.3  95.2  80.2                            
REMARK 620 6 HOH A1023   O   105.0  74.0  84.9  86.6 143.1                      
REMARK 620 7 HOH A1016   O    70.4 124.8  71.6 124.5  69.3 142.9                
REMARK 620 8 ASP A 167   OD1  82.7 117.3  52.4 140.0 137.7  68.6  74.3          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AS1                                                 
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: ACTIVE SITE, SUGAR BINDING SITE.                   
REMARK 800 SITE_IDENTIFIER: AS2                                                 
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: ACTIVE SITE, SUGAR BINDING SITE.                   
REMARK 800 SITE_IDENTIFIER: AS3                                                 
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: ACTIVE SITE, SUGAR BINDING SITE.                   
REMARK 800 SITE_IDENTIFIER: AS4                                                 
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: ACTIVE SITE, SUGAR BINDING SITE.                   
REMARK 800 SITE_IDENTIFIER: AS5                                                 
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: ACTIVE SITE, SUGAR BINDING SITE.                   
REMARK 800 SITE_IDENTIFIER: CAL                                                 
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: CALCIUM BINDING SITE.                              
REMARK 800 SITE_IDENTIFIER: CLO                                                 
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: CHLORIDE BINDING SITE. THERE ARE SIX BOUND         
REMARK 800  SUGAR RINGS. SITE *CAL* CONTAINS 3 WATERS. SITE *CLO* CONTAINS      
REMARK 800  1 WATER.                                                            
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AC1 A 990                 
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC A 991                 
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AC1 A 992                 
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BGC A 993                 
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BGC A 996                 
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 498                  
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 500                  
DBREF  1OSE A    2   496  UNP    P00690   AMYP_PIG         2    496             
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 SER 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 GLN 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 ALA SER ILE          
SEQRES  25 A  496  LEU THR PHE TRP ASP ALA ARG LEU TYR LYS VAL 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  GLU 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 1OSE PCA A    1  GLU  PYROGLUTAMIC ACID                                  
HET    PCA  A   1       8                                                       
HET    AC1  A 990      21                                                       
HET    GLC  A 991      11                                                       
HET    AC1  A 992      21                                                       
HET    BGC  A 993      12                                                       
HET    BGC  A 996      12                                                       
HET     CL  A 498       1                                                       
HET     CA  A 500       1                                                       
HETNAM     PCA PYROGLUTAMIC ACID                                                
HETNAM     AC1 6-METHYL-5-(4,5,6-TRIHYDROXY-3-HYDROXYMETHYL-CYCLOHEX-           
HETNAM   2 AC1  2-ENYLAMINO)-TETRAHYDRO-PYRAN-2,3,4-TRIOL                       
HETNAM     GLC ALPHA-D-GLUCOSE                                                  
HETNAM     BGC BETA-D-GLUCOSE                                                   
HETNAM      CL CHLORIDE ION                                                     
HETNAM      CA CALCIUM ION                                                      
HETSYN     AC1 N-[4-HYDROXYMETHYL-CYCLOHEXAN-6-YL-1,2,3-TRIOL]-4,6-             
HETSYN   2 AC1  DIDEOXY-4-AMINOGLUCOPYRANOSIDE                                  
FORMUL   1  PCA    C5 H7 N O3                                                   
FORMUL   2  AC1    2(C13 H23 N O8)                                              
FORMUL   2  GLC    C6 H12 O6                                                    
FORMUL   2  BGC    2(C6 H12 O6)                                                 
FORMUL   4   CL    CL 1-                                                        
FORMUL   5   CA    CA 2+                                                        
FORMUL   6  HOH   *403(H2 O)                                                    
HELIX    1 A1A ARG A   20  ARG A   30  1                                  11    
HELIX    2 A1B TYR A   31  GLY A   36  1                                   6    
HELIX    3  H1 PRO A   57  GLN A   63  13 CONSECUTIVE BETA TURNS           7    
HELIX    4  A2 ASN A   75  ARG A   92  1                                  18    
HELIX    5  H2 ASN A  120  ARG A  124  12 CONSECUTIVE BETA TURNS           5    
HELIX    6  A3 LYS A  172  GLY A  190  1                                  19    
HELIX    7  A4 TRP A  203  ASP A  212  1                                  10    
HELIX    8  A5 SER A  244  ASN A  250  5                                   7    
HELIX    9 A6A PHE A  256  LYS A  268  1                                  13    
HELIX   10 A6B LYS A  273  TRP A  280  52 CONSECUTIVE BETA TURNS           8    
HELIX   11  H3 GLY A  281  GLY A  285  52 CONSECUTIVE BETA TURNS           5    
HELIX   12  H4 PRO A  288  ALA A  292  52 CONSECUTIVE BETA TURNS           5    
HELIX   13  H5 ASP A  300  GLY A  304  52 CONSECUTIVE BETA TURNS           5    
HELIX   14  A7 ASP A  317  HIS A  331  1                                  15    
HELIX   15  H6 CYS A  384  TRP A  388  52 CONSECUTIVE BETA TURNS           5    
HELIX   16  A8 TRP A  388  ASP A  402  1                                  15    
HELIX   17  B1 ASP A  153  ASP A  159  1                                   7    
SHEET    1  A1 8 SER A  12  LEU A  16  0                                        
SHEET    2  A1 8 GLY A  38  VAL A  42  1  N  GLY A  38   O  SER A  12           
SHEET    3  A1 8 ARG A  92  ALA A  97  1  N  ARG A  92   O  GLY A  38           
SHEET    4  A1 8 ALA A 192  ASP A 197  1  N  ALA A 192   O  ILE A  93           
SHEET    5  A1 8 PHE A 229  GLU A 233  1  N  PHE A 229   O  ALA A 192           
SHEET    6  A1 8 ARG A 252  GLU A 255  1  N  ARG A 252   O  ILE A 230           
SHEET    7  A1 8 ARG A 291  VAL A 294  1  O  ARG A 291   N  VAL A 253           
SHEET    8  A1 8 PHE A 335  SER A 340  1  N  PHE A 335   O  ALA A 292           
SHEET    1  A2 4 SER A  73  GLU A  76  0                                        
SHEET    2  A2 4 LEU A  69  THR A  71 -1  O  CYS A  70   N  SER A  73           
SHEET    3  A2 4 PRO A  45  VAL A  50  1  O  PRO A  45   N  CYS A  70           
SHEET    4  A2 4 GLY A 110  THR A 114 -1  N  THR A 114   O  ASN A  48           
SHEET    1  A3 2 ASN A 347  VAL A 349  0                                        
SHEET    2  A3 2 GLU A 352  VAL A 354 -1  N  VAL A 354   O  ASN A 347           
SHEET    1  A4 2 THR A 371  ASN A 373  0                                        
SHEET    2  A4 2 THR A 376  GLY A 379 -1  N  GLY A 379   O  THR A 371           
SHEET    1  B1 4 GLY A 110  THR A 114  0                                        
SHEET    2  B1 4 CYS A 119  PRO A 121 -1  O  CYS A 119   N  GLY A 110           
SHEET    3  B1 4 ARG A 124  PRO A 127 -1  N  ARG A 124   O  PRO A 121           
SHEET    4  B1 4 TYR A 131  ALA A 133 -1  N  ALA A 133   O  ARG A 124           
SHEET    1  B2 3 ASN A 100  SER A 105  0                                        
SHEET    2  B2 3 GLY A 164  ALA A 169 -1  N  LEU A 168   O  ASN A 100           
SHEET    3  B2 3 ASP A 135  ASN A 137 -1  O  ASP A 135   N  ALA A 169           
SHEET    1  B3 3 GLY A 146  ILE A 148  0                                        
SHEET    2  B3 3 GLN A 161  LEU A 162  1  N  GLN A 161   O  GLY A 146           
SHEET    3  B3 3 GLY A 164  ALA A 169  1  N  LEU A 165   O  LEU A 162           
SHEET    1  C1 4 PRO A 405  ASN A 412  0                                        
SHEET    2  C1 4 ASN A 415  GLY A 422 -1  O  GLN A 416   N  ASN A 412           
SHEET    3  C1 4 ARG A 424  ASN A 431 -1  N  ASN A 431   O  ASN A 415           
SHEET    4  C1 4 PRO A 486  ALA A 492 -1  O  PRO A 486   N  ASN A 430           
SHEET    1  C2 4 LEU A 436  THR A 442  0                                        
SHEET    2  C2 4 GLY A 473  ILE A 479 -1  O  GLY A 473   N  THR A 442           
SHEET    3  C2 4 ILE A 465  SER A 470 -1  O  SER A 470   N  GLY A 473           
SHEET    4  C2 4 GLY A 447  ASP A 451 -1  N  GLY A 447   O  VAL A 469           
SHEET    1  C3 2 ASP A 456  VAL A 458  0                                        
SHEET    2  C3 2 SER A 461  THR A 463 -1  N  THR A 463   O  ASP A 456           
SSBOND   1 CYS A   28    CYS A   86                          1555   1555  2.03  
SSBOND   2 CYS A   70    CYS A  115                          1555   1555  2.03  
SSBOND   3 CYS A  141    CYS A  160                          1555   1555  2.03  
SSBOND   4 CYS A  378    CYS A  384                          1555   1555  2.02  
SSBOND   5 CYS A  450    CYS A  462                          1555   1555  2.02  
LINK         C   PCA A   1                 N   TYR A   2     1555   1555  1.33  
LINK        CA    CA A 500                 OD1 ASN A 100     1555   1555  2.20  
LINK        CA    CA A 500                 O   ARG A 158     1555   1555  2.40  
LINK        CA    CA A 500                 OD2 ASP A 167     1555   1555  2.39  
LINK        CA    CA A 500                 O   HIS A 201     1555   1555  2.32  
LINK         C1  AC1 A 990                 O4  GLC A 991     1555   1555  1.40  
LINK         C1  GLC A 991                 O4  AC1 A 992     1555   1555  1.40  
LINK        CA    CA A 500                 O   HOH A1035     1555   1555  2.29  
LINK        CA    CA A 500                 O   HOH A1023     1555   1555  2.25  
LINK        CA    CA A 500                 O   HOH A1016     1555   1555  2.34  
LINK        CA    CA A 500                 OD1 ASP A 167     1555   1555  2.54  
LINK         C1  AC1 A 992                 O4  BGC A 993     1555   1555  1.40  
CISPEP   1 ASN A   53    PRO A   54          0        -0.17                     
CISPEP   2 VAL A  129    PRO A  130          0         0.33                     
SITE     1 AS1  3 VAL A 163  GLN A  63  LEU A 165                               
SITE     1 AS2  3 HIS A 305  GLN A  63  TRP A  59                               
SITE     1 AS3  4 ASP A 300  HIS A 299  ASP A 197  HIS A 101                    
SITE     1 AS4  3 HIS A 201  GLU A 233  ASP A 300                               
SITE     1 AS5  2 GLU A 240  LYS A 200                                          
SITE     1 CAL  4 ASN A 100  ARG A 158  ASP A 167  HIS A 201                    
SITE     1 CLO  3 ARG A 195  ASN A 298  ARG A 337                               
SITE     1 AC1  9 GLN A  63  SER A 105  GLY A 106  VAL A 163                    
SITE     2 AC1  9 GLY A 164  LEU A 165  GLC A 991  HOH A1239A                   
SITE     3 AC1  9 HOH A1350B                                                    
SITE     1 AC2  7 TRP A  59  TYR A  62  GLN A  63  VAL A 163                    
SITE     2 AC2  7 HIS A 305  AC1 A 990  AC1 A 992                               
SITE     1 AC3 12 TRP A  58  TYR A  62  HIS A 101  LEU A 162                    
SITE     2 AC3 12 ASP A 197  ALA A 198  HIS A 201  GLU A 233                    
SITE     3 AC3 12 HIS A 299  ASP A 300  GLC A 991  HOH A1238A                   
SITE     1 AC4  8 TYR A 151  LYS A 200  ILE A 235  GLU A 240                    
SITE     2 AC4  8 GLY A 306  AC1 A 992  HOH A1189  HOH A1233A                   
SITE     1 AC5  8 THR A  52  GLU A 272  TYR A 276  ASN A 279                    
SITE     2 AC5  8 TRP A 284  HOH A1289B HOH A1365B HOH A1367B                   
SITE     1 AC6  3 ARG A 195  ASN A 298  ARG A 337                               
SITE     1 AC7  7 ASN A 100  ARG A 158  ASP A 167  HIS A 201                    
SITE     2 AC7  7 HOH A1016  HOH A1023  HOH A1035                               
CRYST1   70.600  114.700  118.500  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      0.014164  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008718  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008439        0.00000                         
HETATM    1  N   PCA A   1      41.002  44.319  25.144  1.00 25.94           N  
HETATM    2  CA  PCA A   1      40.524  43.817  23.853  1.00 22.58           C  
HETATM    3  CB  PCA A   1      41.438  44.552  22.917  1.00 23.48           C  
HETATM    4  CG  PCA A   1      42.055  45.646  23.764  1.00 26.62           C  
HETATM    5  CD  PCA A   1      41.855  45.340  25.273  1.00 27.53           C  
HETATM    6  OE  PCA A   1      42.446  45.997  26.129  1.00 38.77           O  
HETATM    7  C   PCA A   1      40.691  42.298  23.828  1.00 19.43           C  
HETATM    8  O   PCA A   1      40.068  41.626  23.010  1.00 20.05           O  
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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