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Database: PDB
Entry: 1JFH
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HEADER    HYDROLASE                               19-SEP-97   1JFH              
TITLE     STRUCTURE OF A PANCREATIC ALPHA-AMYLASE BOUND TO A                    
TITLE    2 SUBSTRATE ANALOGUE AT 2.03 ANGSTROM RESOLUTION                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ALPHA-AMYLASE;                                             
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: PPA;                                                        
COMPND   5 EC: 3.2.1.1;                                                         
COMPND   6 OTHER_DETAILS: COMPLEXED WITH METHYL 4,4'-DITHIO-ALPHA-              
COMPND   7 MALTOTRIOSIDE                                                        
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    HYDROLASE, O-GLYCOSYL, ALPHA-AMYLASE, METHYL 4,4'-DITHIO-             
KEYWDS   2 ALPHA-MALTOTRIOSIDE                                                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.QIAN,F.PAYAN                                                        
REVDAT   3   24-FEB-09 1JFH    1       VERSN                                    
REVDAT   2   13-JAN-99 1JFH    1       COMPND REMARK TITLE  SEQADV              
REVDAT   2 2                   1       HEADER MODRES SOURCE KEYWDS              
REVDAT   1   02-DEC-98 1JFH    0                                                
JRNL        AUTH   M.QIAN,S.SPINELLI,H.DRIGUEZ,F.PAYAN                          
JRNL        TITL   STRUCTURE OF A PANCREATIC ALPHA-AMYLASE BOUND TO A           
JRNL        TITL 2 SUBSTRATE ANALOGUE AT 2.03 A RESOLUTION.                     
JRNL        REF    PROTEIN SCI.                  V.   6  2285 1997              
JRNL        REFN                   ISSN 0961-8368                               
JRNL        PMID   9385631                                                      
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   C.GILLES,J.P.ASTIER,G.MARCHIS-MOUREN,C.CAMBILLAU,            
REMARK   1  AUTH 2 F.PAYAN                                                      
REMARK   1  TITL   CRYSTAL STRUCTURE OF PIG PANCREATIC ALPHA-AMYLASE            
REMARK   1  TITL 2 ISOENZYME II, IN COMPLEX WITH THE CARBOHYDRATE               
REMARK   1  TITL 3 INHIBITOR ACARBOSE                                           
REMARK   1  REF    EUR.J.BIOCHEM.                V. 238   561 1996              
REMARK   1  REFN                   ISSN 0014-2956                               
REMARK   1 REFERENCE 2                                                          
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                
REMARK   1  TITL 3 X-RAY 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 3                                                          
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                  
REMARK   1  TITL 4 REFINED TO 2.2-A RESOLUTION                                  
REMARK   1  REF    BIOCHEMISTRY                  V.  33  6284 1994              
REMARK   1  REFN                   ISSN 0006-2960                               
REMARK   1 REFERENCE 4                                                          
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.    2.03 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR 3.843                                         
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.03                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 35.00                          
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)   (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 33421                          
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) : 0.160                           
REMARK   3   FREE R VALUE                     : 0.185                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
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            : 3908                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 71                                      
REMARK   3   SOLVENT ATOMS            : 384                                     
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) : 0.20                            
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) : 0.010                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.40                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
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 1JFH 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 : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 33718                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : NULL                               
REMARK 200  RESOLUTION RANGE LOW       (A) : NULL                               
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.4                               
REMARK 200  DATA REDUNDANCY                : 9.500                              
REMARK 200  R MERGE                    (I) : 0.05700                            
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 3.843                                          
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 45.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.30                     
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       28.15000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       51.70000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       43.90000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       51.70000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       28.15000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       43.90000            
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: 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      -61.53   -140.97                                   
REMARK 500    MET A 102     -140.66   -113.27                                   
REMARK 500    ASP A 317       58.35   -115.32                                   
REMARK 500    SER A 414     -103.40   -133.61                                   
REMARK 500    PRO A 486       40.74    -75.96                                   
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 A 853        DISTANCE =  5.16 ANGSTROMS                       
REMARK 525    HOH A 888        DISTANCE =  6.61 ANGSTROMS                       
REMARK 525    HOH A 894        DISTANCE =  8.18 ANGSTROMS                       
REMARK 525    HOH A 897        DISTANCE =  7.25 ANGSTROMS                       
REMARK 525    HOH A 905        DISTANCE =  6.43 ANGSTROMS                       
REMARK 525    HOH A 920        DISTANCE =  6.78 ANGSTROMS                       
REMARK 525    HOH A 931        DISTANCE =  5.22 ANGSTROMS                       
REMARK 525    HOH A 937        DISTANCE =  5.58 ANGSTROMS                       
REMARK 525    HOH A 947        DISTANCE =  5.47 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 HIS A 201   O                                                      
REMARK 620 2 HOH A 520   O   123.0                                              
REMARK 620 3 ASN A 100   OD1  72.8  69.9                                        
REMARK 620 4 HOH A 539   O    83.8  63.2 100.7                                  
REMARK 620 5 ASP A 167   OD1 138.7  78.2  85.1 135.4                            
REMARK 620 6 HOH A 527   O    81.4 146.0 100.0 149.6  68.4                      
REMARK 620 7 ARG A 158   O    82.6 123.3 155.0  72.2 117.1  79.6                
REMARK 620 8 ASP A 167   OD2 159.6  73.4 127.2  95.0  50.8  89.9  77.7          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              HG A 499  HG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 103   SG                                                     
REMARK 620 2 CYS A 119   SG  168.2                                              
REMARK 620 N                    1                                               
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MA2 A 991                 
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MA3 A 992                 
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC A 993                 
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MA1 A 994                 
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC A 995                 
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MA1 A 996                 
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 498                  
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HG A 499                  
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 500                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1PPI   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OBTAINED AT ROOM TEMPERATURE WITH DIFFERENT                
REMARK 900 LIGANDS                                                              
DBREF  1JFH A    2   496  UNP    P00690   AMYP_PIG         2    496             
SEQADV 1JFH VAL A   49  UNP  P00690    ILE    49 CONFLICT                       
SEQADV 1JFH LYS A  243  UNP  P00690    GLN   243 CONFLICT                       
SEQADV 1JFH SER A  310  UNP  P00690    ALA   310 CONFLICT                       
SEQADV 1JFH ILE A  323  UNP  P00690    VAL   323 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 VAL 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 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  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 1JFH PCA A    1  GLU  PYROGLUTAMIC ACID                                  
HET    PCA  A   1       8                                                       
HET    MA2  A 991      12                                                       
HET    MA3  A 992      13                                                       
HET    GLC  A 993      11                                                       
HET    MA1  A 994      12                                                       
HET    GLC  A 995      11                                                       
HET    MA1  A 996      12                                                       
HET     CL  A 498       1                                                       
HET     HG  A 499       1                                                       
HET     CA  A 500       1                                                       
HETNAM     PCA PYROGLUTAMIC ACID                                                
HETNAM     MA2 4-S-METHYL-4-THIO-ALPHA-D-GLUCOPYRANOSE                          
HETNAM     MA3 O1-METHYL-4-DEOXY-4-THIO-ALPHA-D-GLUCOSE                         
HETNAM     GLC ALPHA-D-GLUCOSE                                                  
HETNAM     MA1 1,4-DITHIO-ALPHA-D-GLUCOPYRANOSE                                 
HETNAM      CL CHLORIDE ION                                                     
HETNAM      HG MERCURY (II) ION                                                 
HETNAM      CA CALCIUM ION                                                      
FORMUL   1  PCA    C5 H7 N O3                                                   
FORMUL   2  MA2    C7 H14 O5 S                                                  
FORMUL   3  MA3    C7 H14 O5 S                                                  
FORMUL   4  GLC    2(C6 H12 O6)                                                 
FORMUL   5  MA1    2(C6 H12 O4 S2)                                              
FORMUL   8   CL    CL 1-                                                        
FORMUL   9   HG    HG 2+                                                        
FORMUL  10   CA    CA 2+                                                        
FORMUL  11  HOH   *383(H2 O)                                                    
HELIX    1   1 TRP A   21  ARG A   30  1                                  10    
HELIX    2   2 TRP A   58  TYR A   62  5                                   5    
HELIX    3   3 GLU A   76  VAL A   89  1                                  14    
HELIX    4   4 PRO A  121  SER A  123  5                                   3    
HELIX    5   5 ALA A  133  ASP A  135  5                                   3    
HELIX    6   6 PRO A  154  ASP A  159  1                                   6    
HELIX    7   7 LEU A  162  GLY A  164  5                                   3    
HELIX    8   8 ASP A  173  ILE A  189  1                                  17    
HELIX    9   9 SER A  199  HIS A  201  5                                   3    
HELIX   10  10 PRO A  204  LYS A  213  1                                  10    
HELIX   11  11 SER A  244  TYR A  247  5                                   4    
HELIX   12  12 PHE A  256  VAL A  266  1                                  11    
HELIX   13  13 MET A  274  ASN A  279  5                                   6    
HELIX   14  14 GLU A  282  TRP A  284  5                                   3    
HELIX   15  15 SER A  289  ARG A  291  5                                   3    
HELIX   16  16 ASN A  301  ARG A  303  5                                   3    
HELIX   17  17 PHE A  315  ALA A  330  5                                  16    
HELIX   18  18 GLU A  385  ARG A  387  5                                   3    
HELIX   19  19 ARG A  389  VAL A  400  1                                  12    
HELIX   20  20 ALA A  492  SER A  494  5                                   3    
SHEET    1   A 6 THR A 336  SER A 340  0                                        
SHEET    2   A 6 SER A  12  LEU A  16  1  N  ILE A  13   O  THR A 336           
SHEET    3   A 6 GLY A  39  VAL A  42  1  N  GLY A  39   O  VAL A  14           
SHEET    4   A 6 ARG A  92  ALA A  97  1  N  ARG A  92   O  VAL A  40           
SHEET    5   A 6 GLY A 193  ILE A 196  1  N  GLY A 193   O  VAL A  95           
SHEET    6   A 6 PHE A 229  GLN A 232  1  N  PHE A 229   O  PHE A 194           
SHEET    1   B 3 GLN A 416  ARG A 421  0                                        
SHEET    2   B 3 GLY A 425  ASN A 430 -1  N  PHE A 429   O  VAL A 417           
SHEET    3   B 3 PHE A 487  HIS A 491 -1  N  ILE A 490   O  PHE A 426           
SHEET    1   C 2 LEU A 436  GLN A 441  0                                        
SHEET    2   C 2 THR A 474  ILE A 479 -1  N  ILE A 479   O  LEU A 436           
SHEET    1   D 2 GLY A 447  CYS A 450  0                                        
SHEET    2   D 2 LYS A 466  VAL A 469 -1  N  VAL A 469   O  GLY A 447           
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  2.03  
SSBOND   5 CYS A  450    CYS A  462                          1555   1555  2.03  
LINK         C   PCA A   1                 N   TYR A   2     1555   1555  1.33  
LINK        CA    CA A 500                 O   HIS A 201     1555   1555  2.39  
LINK         C1  MA2 A 991                 S4  MA3 A 992     1555   1555  1.82  
LINK        HG    HG A 499                 SG  CYS A 103     1555   1555  2.31  
LINK        HG    HG A 499                 SG  CYS A 119     1555   1555  2.40  
LINK        CA    CA A 500                 O   HOH A 520     1555   1555  2.64  
LINK        CA    CA A 500                 OD1 ASN A 100     1555   1555  2.40  
LINK        CA    CA A 500                 O   HOH A 539     1555   1555  2.54  
LINK        CA    CA A 500                 OD1 ASP A 167     1555   1555  2.57  
LINK        CA    CA A 500                 O   HOH A 527     1555   1555  2.61  
LINK        CA    CA A 500                 O   ARG A 158     1555   1555  2.41  
LINK        CA    CA A 500                 OD2 ASP A 167     1555   1555  2.54  
LINK         C1  GLC A 993                 S4  MA1 A 994     1555   1555  1.82  
LINK         C1  GLC A 995                 S4  MA1 A 996     1555   1555  1.84  
CISPEP   1 ASN A   53    PRO A   54          0        -0.05                     
CISPEP   2 VAL A  129    PRO A  130          0        -0.29                     
SITE     1 AC1  5 TRP A  59  GLN A  63  VAL A 163  HOH A 666                    
SITE     2 AC1  5 MA3 A 992                                                     
SITE     1 AC2  7 TRP A  59  GLN A  63  HIS A 305  HOH A 566                    
SITE     2 AC2  7 HOH A 970  MA2 A 991  GLC A 993                               
SITE     1 AC3 11 TYR A 151  LEU A 162  HIS A 201  GLU A 233                    
SITE     2 AC3 11 HOH A 748  HOH A 764  HOH A 950  HOH A 970                    
SITE     3 AC3 11 HOH A 986  MA3 A 992  MA1 A 994                               
SITE     1 AC4  5 LYS A 200  GLU A 240  GLY A 306  HOH A 964                    
SITE     2 AC4  5 GLC A 993                                                     
SITE     1 AC5  9 ASP A 375  THR A 376  ARG A 387  TRP A 388                    
SITE     2 AC5  9 ARG A 389  GLU A 390  HOH A 906  HOH A 925                    
SITE     3 AC5  9 MA1 A 996                                                     
SITE     1 AC6 10 TRP A 134  ALA A 318  LYS A 322  TRP A 388                    
SITE     2 AC6 10 GLU A 390  HOH A 661  HOH A 875  HOH A 885                    
SITE     3 AC6 10 HOH A 931  GLC A 995                                          
SITE     1 AC7  3 ARG A 195  ASN A 298  ARG A 337                               
SITE     1 AC8  4 CYS A 103  CYS A 119  PRO A 121  PHE A 126                    
SITE     1 AC9  7 ASN A 100  ARG A 158  ASP A 167  HIS A 201                    
SITE     2 AC9  7 HOH A 520  HOH A 527  HOH A 539                               
CRYST1   56.300   87.800  103.400  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      0.017762  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011390  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009671        0.00000                         
HETATM    1  N   PCA A   1      17.421  60.913  14.256  1.00 20.15           N  
HETATM    2  CA  PCA A   1      16.378  59.896  14.403  1.00 20.07           C  
HETATM    3  CB  PCA A   1      15.230  60.572  13.710  1.00 21.72           C  
HETATM    4  CG  PCA A   1      15.635  62.033  13.677  1.00 26.95           C  
HETATM    5  CD  PCA A   1      17.173  62.178  13.870  1.00 24.07           C  
HETATM    6  OE  PCA A   1      17.741  63.244  13.648  1.00 35.03           O  
HETATM    7  C   PCA A   1      16.840  58.593  13.743  1.00 15.22           C  
HETATM    8  O   PCA A   1      16.295  57.532  14.025  1.00 15.57           O  
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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