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Database: PDB
Entry: 3L2L
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HEADER    HYDROLASE                               15-DEC-09   3L2L              
TITLE     X-RAY CRYSTALLOGRAPHIC ANALYSIS OF PIG PANCREATIC ALPHA-AMYLASE WITH  
TITLE    2 LIMIT DEXTRIN AND OLIGOSACCHARIDE                                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PANCREATIC ALPHA-AMYLASE;                                  
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: RESIDUES 16-511;                                           
COMPND   5 SYNONYM: PA, 1,4-ALPHA-D-GLUCAN GLUCANOHYDROLASE;                    
COMPND   6 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 OTHER_DETAILS: PANCREAS                                              
KEYWDS    CATALYTIC DOMAIN, CARBOHYDRATE BINDING MODULE, OLIGOSACCHARIDE, LIMIT 
KEYWDS   2 DEXTRIN, GLUCOSE, CARBOHYDRATE METABOLISM, GLYCOPROTEIN,             
KEYWDS   3 GLYCOSIDASE, METAL-BINDING, PYRROLIDONE CARBOXYLIC ACID, SECRETED,   
KEYWDS   4 HYDROLASE                                                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.B.LARSON,J.S.DAY,A.MCPHERSON                                        
REVDAT   3   13-JUL-11 3L2L    1       VERSN                                    
REVDAT   2   21-APR-10 3L2L    1       JRNL                                     
REVDAT   1   14-APR-10 3L2L    0                                                
JRNL        AUTH   S.B.LARSON,J.S.DAY,A.MCPHERSON                               
JRNL        TITL   X-RAY CRYSTALLOGRAPHIC ANALYSES OF PIG PANCREATIC            
JRNL        TITL 2 ALPHA-AMYLASE WITH LIMIT DEXTRIN, OLIGOSACCHARIDE, AND       
JRNL        TITL 3 ALPHA-CYCLODEXTRIN.                                          
JRNL        REF    BIOCHEMISTRY                  V.  49  3101 2010              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   20222716                                                     
JRNL        DOI    10.1021/BI902183W                                            
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   S.B.LARSON,A.GREENWOOD,D.CASCIO,J.DAY,A.MCPHERSON            
REMARK   1  TITL   REFINED MOLECULAR STRUCTURE OF PIG PANCREATIC ALPHA-AMYLASE  
REMARK   1  TITL 2 AT 2.1 A RESOLUTION                                          
REMARK   1  REF    J.MOL.BIOL.                   V. 235  1560 1994              
REMARK   1  REFN                   ISSN 0022-2836                               
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   A.MCPHERSON,A.RICH                                           
REMARK   1  TITL   X-RAY CRYSTALLOGRAPHIC ANALYSIS OF SWINE PANCREAS            
REMARK   1  TITL 2 ALPHA-AMYLASE                                                
REMARK   1  REF    BIOCHIM.BIOPHYS.ACTA          V. 285   493 1972              
REMARK   1  REFN                   ISSN 0006-3002                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.11 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0089                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.11                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 14.01                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 84.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 47147                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.119                           
REMARK   3   R VALUE            (WORKING SET) : 0.115                           
REMARK   3   FREE R VALUE                     : 0.157                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.100                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 4749                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.11                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.16                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 438                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 12.22                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2230                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 55                           
REMARK   3   BIN FREE R VALUE                    : 0.3140                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3909                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 126                                     
REMARK   3   SOLVENT ATOMS            : 584                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : 23.25                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 19.70                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.36000                                              
REMARK   3    B22 (A**2) : -1.27000                                             
REMARK   3    B33 (A**2) : -0.09000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.126         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.125         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.076         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.718         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.978                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.962                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4593 ; 0.013 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  4197 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  6337 ; 1.487 ; 1.948       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  9517 ; 0.813 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   597 ; 6.044 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   231 ;35.877 ;24.113       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   708 ;14.545 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    31 ;19.778 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   672 ; 0.112 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  5308 ; 0.007 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  1149 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   942 ; 0.217 ; 0.300       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  4191 ; 0.187 ; 0.300       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  2259 ; 0.191 ; 0.500       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  2710 ; 0.094 ; 0.500       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   693 ; 0.210 ; 0.500       
REMARK   3   H-BOND (X...Y) OTHERS             (A):   523 ; 0.189 ; 0.500       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):     2 ; 0.070 ; 0.500       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):     8 ; 0.143 ; 0.300       
REMARK   3   SYMMETRY VDW OTHERS               (A):    48 ; 0.176 ; 0.300       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    30 ; 0.183 ; 0.500       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):     9 ; 0.159 ; 0.500       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  2699 ; 2.322 ; 4.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  1107 ; 0.595 ; 4.000       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4405 ; 3.372 ; 8.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1894 ; 4.199 ; 8.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1910 ; 5.443 ;10.000       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 14                                         
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     1        A    99                          
REMARK   3    RESIDUE RANGE :   A   169        A   403                          
REMARK   3    ORIGIN FOR THE GROUP (A):  38.8690  33.4020  44.6410              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0003 T22:   0.0067                                     
REMARK   3      T33:   0.0022 T12:   0.0010                                     
REMARK   3      T13:  -0.0001 T23:   0.0010                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6708 L22:   1.2826                                     
REMARK   3      L33:   0.7013 L12:   0.1325                                     
REMARK   3      L13:   0.0256 L23:   0.1581                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0097 S12:   0.0089 S13:  -0.0117                       
REMARK   3      S21:   0.0008 S22:  -0.0106 S23:  -0.0505                       
REMARK   3      S31:  -0.0037 S32:   0.0104 S33:   0.0010                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   100        A   168                          
REMARK   3    ORIGIN FOR THE GROUP (A):  35.0470  49.8490  62.0530              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0721 T22:   0.0473                                     
REMARK   3      T33:   0.0180 T12:   0.0042                                     
REMARK   3      T13:  -0.0049 T23:  -0.0121                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.6942 L22:   1.2806                                     
REMARK   3      L33:   1.1122 L12:   0.9278                                     
REMARK   3      L13:  -0.3768 L23:   0.0953                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0850 S12:  -0.2797 S13:   0.1308                       
REMARK   3      S21:   0.1699 S22:  -0.0458 S23:   0.0398                       
REMARK   3      S31:  -0.0847 S32:  -0.0160 S33:  -0.0393                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   404        A   496                          
REMARK   3    ORIGIN FOR THE GROUP (A):  32.4380   9.0210  28.8980              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0107 T22:   0.0110                                     
REMARK   3      T33:   0.0170 T12:   0.0052                                     
REMARK   3      T13:  -0.0017 T23:  -0.0126                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6513 L22:   1.8641                                     
REMARK   3      L33:   2.3054 L12:   0.0461                                     
REMARK   3      L13:  -0.3235 L23:   0.0102                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0207 S12:   0.0523 S13:  -0.0932                       
REMARK   3      S21:  -0.0790 S22:  -0.0054 S23:  -0.0292                       
REMARK   3      S31:   0.1056 S32:   0.0275 S33:   0.0261                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   601        A   601                          
REMARK   3    ORIGIN FOR THE GROUP (A):  47.4650  29.8860  71.0930              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0617 T22:   0.1799                                     
REMARK   3      T33:   0.1959 T12:  -0.0489                                     
REMARK   3      T13:   0.0092 T23:   0.1047                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  10.8944 L22:  65.6258                                     
REMARK   3      L33:   0.3561 L12:   7.8608                                     
REMARK   3      L13:   1.5422 L23:   0.0041                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1424 S12:   0.3525 S13:   0.3914                       
REMARK   3      S21:   0.5451 S22:  -0.1157 S23:  -0.0860                       
REMARK   3      S31:  -0.0493 S32:   0.1746 S33:   0.2581                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   602        A   602                          
REMARK   3    ORIGIN FOR THE GROUP (A):  50.6260  33.7470  72.2300              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2418 T22:   0.4034                                     
REMARK   3      T33:   0.3828 T12:  -0.1134                                     
REMARK   3      T13:  -0.0560 T23:   0.0562                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.5020 L22:  17.6753                                     
REMARK   3      L33:   0.1577 L12:  -9.8564                                     
REMARK   3      L13:   0.9077 L23:  -1.6140                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1037 S12:  -0.0516 S13:  -0.6245                       
REMARK   3      S21:  -0.1657 S22:   0.0451 S23:   1.0500                       
REMARK   3      S31:   0.0345 S32:  -0.0369 S33:  -0.1488                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   603        A   603                          
REMARK   3    ORIGIN FOR THE GROUP (A):  51.3680  38.9880  73.1750              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1311 T22:   0.0503                                     
REMARK   3      T33:   0.0573 T12:  -0.0085                                     
REMARK   3      T13:   0.0268 T23:   0.0051                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  16.6733 L22:   0.3362                                     
REMARK   3      L33:   1.0692 L12:  -2.3677                                     
REMARK   3      L13:   4.2221 L23:  -0.5996                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0374 S12:  -0.0981 S13:   0.0884                       
REMARK   3      S21:   0.0052 S22:   0.0142 S23:  -0.0124                       
REMARK   3      S31:  -0.0082 S32:  -0.0251 S33:   0.0233                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   604        A   604                          
REMARK   3    ORIGIN FOR THE GROUP (A):  48.0030  42.8810  72.9330              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1971 T22:   0.3942                                     
REMARK   3      T33:   0.2879 T12:   0.1550                                     
REMARK   3      T13:   0.0143 T23:   0.0404                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  17.5005 L22:  13.0692                                     
REMARK   3      L33:  24.1837 L12:  15.1231                                     
REMARK   3      L13:  20.5723 L23:  17.7778                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0785 S12:  -0.7603 S13:   0.6253                       
REMARK   3      S21:  -0.0729 S22:  -0.6672 S23:   0.5459                       
REMARK   3      S31:  -0.0903 S32:  -0.8912 S33:   0.7456                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   701        A   701                          
REMARK   3    ORIGIN FOR THE GROUP (A):  32.7310  42.2410  70.0000              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6617 T22:   1.9174                                     
REMARK   3      T33:   0.7859 T12:   0.1492                                     
REMARK   3      T13:  -0.2509 T23:   0.3966                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0004 L22:   0.0002                                     
REMARK   3      L33:   0.0020 L12:   0.0002                                     
REMARK   3      L13:   0.0007 L23:   0.0006                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0006 S12:  -0.0101 S13:   0.0124                       
REMARK   3      S21:   0.0079 S22:  -0.0048 S23:   0.0023                       
REMARK   3      S31:   0.0134 S32:  -0.0397 S33:   0.0054                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   702        A   702                          
REMARK   3    ORIGIN FOR THE GROUP (A):  36.2530  38.9420  68.6760              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1249 T22:   0.0828                                     
REMARK   3      T33:   0.1353 T12:  -0.0400                                     
REMARK   3      T13:   0.0236 T23:  -0.0317                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0281 L22:   0.3178                                     
REMARK   3      L33:  41.5545 L12:   0.0840                                     
REMARK   3      L13:  -0.8230 L23:  -3.5372                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0196 S12:   0.0302 S13:  -0.0098                       
REMARK   3      S21:   0.0147 S22:   0.0503 S23:  -0.0093                       
REMARK   3      S31:  -0.6131 S32:  -0.2245 S33:  -0.0308                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   703        A   703                          
REMARK   3    ORIGIN FOR THE GROUP (A):  38.9690  37.5810  64.7540              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1181 T22:   0.0743                                     
REMARK   3      T33:   0.0749 T12:  -0.0034                                     
REMARK   3      T13:   0.0316 T23:  -0.0104                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  31.4752 L22:   0.3339                                     
REMARK   3      L33:   3.2985 L12:  -3.2410                                     
REMARK   3      L13:   8.8442 L23:  -0.9226                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0066 S12:  -0.3667 S13:   0.1215                       
REMARK   3      S21:  -0.0021 S22:   0.0350 S23:  -0.0104                       
REMARK   3      S31:   0.1828 S32:   0.0514 S33:  -0.0416                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   704        A   704                          
REMARK   3    ORIGIN FOR THE GROUP (A):  38.3890  36.8360  59.8110              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1003 T22:   0.0600                                     
REMARK   3      T33:   0.0596 T12:  -0.0090                                     
REMARK   3      T13:  -0.0105 T23:  -0.0007                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  41.7595 L22:   0.0542                                     
REMARK   3      L33:   0.0634 L12:   1.5043                                     
REMARK   3      L13:  -1.6265 L23:  -0.0586                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0114 S12:   0.3045 S13:   0.0249                       
REMARK   3      S21:  -0.0003 S22:   0.0122 S23:   0.0012                       
REMARK   3      S31:   0.0019 S32:  -0.0115 S33:  -0.0008                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   705        A   705                          
REMARK   3    ORIGIN FOR THE GROUP (A):  34.7480  37.5510  56.1690              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1025 T22:   0.0886                                     
REMARK   3      T33:   0.2057 T12:  -0.0367                                     
REMARK   3      T13:  -0.1310 T23:   0.0386                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  10.4216 L22:   3.2509                                     
REMARK   3      L33:  28.1879 L12:   0.0000                                     
REMARK   3      L13:   9.5727 L23:   0.0000                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0583 S12:  -0.1827 S13:   0.0197                       
REMARK   3      S21:   0.0338 S22:   0.1012 S23:  -0.0124                       
REMARK   3      S31:   0.1036 S32:   0.2982 S33:  -0.0430                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   706        A   706                          
REMARK   3    ORIGIN FOR THE GROUP (A):  41.8110  41.2260  67.4590              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2107 T22:   0.1197                                     
REMARK   3      T33:   0.0388 T12:   0.0463                                     
REMARK   3      T13:  -0.0411 T23:  -0.0220                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  41.3493 L22:   4.0134                                     
REMARK   3      L33:   1.8216 L12:  12.8821                                     
REMARK   3      L13:  -8.6785 L23:  -2.7038                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0232 S12:   0.1274 S13:   0.3002                       
REMARK   3      S21:   0.0079 S22:   0.0399 S23:   0.0934                       
REMARK   3      S31:  -0.0045 S32:  -0.0293 S33:  -0.0632                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   801        A   801                          
REMARK   3    ORIGIN FOR THE GROUP (A):  21.6310  53.1520  52.4440              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2093 T22:   0.1929                                     
REMARK   3      T33:   0.1240 T12:  -0.1547                                     
REMARK   3      T13:  -0.0747 T23:   0.0545                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7935 L22:  17.7789                                     
REMARK   3      L33:   0.3508 L12:  -5.3308                                     
REMARK   3      L13:   0.5762 L23:  -2.2787                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1861 S12:   0.0952 S13:   0.1081                       
REMARK   3      S21:  -0.0033 S22:   0.2427 S23:  -0.0064                       
REMARK   3      S31:   0.1034 S32:  -0.1238 S33:  -0.0566                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 3L2L COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-JAN-10.                  
REMARK 100 THE RCSB ID CODE IS RCSB056753.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 02-SEP-92                          
REMARK 200  TEMPERATURE           (KELVIN) : 298                                
REMARK 200  PH                             : 6.75                               
REMARK 200  NUMBER OF CRYSTALS USED        : 9                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU RU200                       
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : SUPPER GRAPHITE                    
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : AREA DETECTOR                      
REMARK 200  DETECTOR MANUFACTURER          : SDMS                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : SDMS DETECTOR SYSTEM               
REMARK 200  DATA SCALING SOFTWARE          : SDMS DETECTOR SYSTEM               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 47147                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.110                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 14.010                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 82.6                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.05200                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.9300                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.11                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.22                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 28.8                               
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         : 3.910                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MIR                          
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 71.67                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.34                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.010 M CACODYLATE, 0.002 M CALCIUM      
REMARK 280  CHLORIDE, PH 6.75, EVAPORATION, TEMPERATURE 298K                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       35.29500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       59.39000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       57.41000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       59.39000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       35.29500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       57.41000            
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
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: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500  HH22  ARG A   424     O    HOH A   711              1.48            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG A 195   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 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      -57.98   -138.74                                   
REMARK 500    MET A 102     -147.46   -107.58                                   
REMARK 500    VAL A 163       45.73     35.33                                   
REMARK 500    ASP A 317       49.49   -106.37                                   
REMARK 500    SER A 414     -102.47   -137.77                                   
REMARK 500    ASP A 433       30.43    -90.96                                   
REMARK 500    ASN A 460       47.32   -104.68                                   
REMARK 500    PRO A 486       40.53    -83.87                                   
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 A1038        DISTANCE =  5.29 ANGSTROMS                       
REMARK 525    HOH A1050        DISTANCE =  6.36 ANGSTROMS                       
REMARK 525    HOH A1085        DISTANCE =  5.28 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 501  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ARG A 158   O                                                      
REMARK 620 2 ASN A 100   OD1 155.2                                              
REMARK 620 3 HIS A 201   O    78.6  76.6                                        
REMARK 620 4 HOH A 767   O    76.2 101.8  80.9                                  
REMARK 620 5 ASP A 167   OD2  80.1 124.7 158.4  90.7                            
REMARK 620 6 HOH A 760   O   123.8  70.4 124.5 148.1  71.3                      
REMARK 620 7 ASP A 167   OD1 119.0  81.9 138.6  69.3  52.6  78.8                
REMARK 620 8 HOH A 852   O    75.3 100.7  85.9 150.4  92.1  59.1 133.1          
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 604                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC A 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC A 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC A 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC A 705                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC A 704                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC A 703                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC A 702                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC A 701                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC A 706                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC A 801                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 501                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 502                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3L2M   RELATED DB: PDB                                   
REMARK 900 X-RAY CRYSTALLOGRAPHIC ANALYSIS OF PIG PANCREATIC ALPHA-             
REMARK 900 AMYLASE WITH ALPHA-CYCLODEXTRIN                                      
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 THE RESIDUE AT POSITION 426 IS A VARIANT AS LISTED IN UNP ENTRY      
REMARK 999 P00690. PCA IS A POST-TRANSLATIONAL MODIFICATION.                    
DBREF  3L2L A    1   496  UNP    P00690   AMYP_PIG        16    511             
SEQADV 3L2L PCA A    1  UNP  P00690    GLN    16 SEE REMARK 999                 
SEQADV 3L2L ASP A  411  UNP  P00690    ALA   426 SEE REMARK 999                 
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 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  GLN 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 GLN          
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 3L2L PCA A    1  GLU  PYROGLUTAMIC ACID                                  
HET    PCA  A   1      13                                                       
HET    GLC  A 604      23                                                       
HET    GLC  A 603      21                                                       
HET    GLC  A 602      21                                                       
HET    GLC  A 601      21                                                       
HET    GLC  A 705      23                                                       
HET    GLC  A 704      21                                                       
HET    GLC  A 703      20                                                       
HET    GLC  A 702      21                                                       
HET    GLC  A 701      21                                                       
HET    GLC  A 706      21                                                       
HET    GLC  A 801      24                                                       
HET     CA  A 501       1                                                       
HET     CL  A 502       1                                                       
HETNAM     PCA PYROGLUTAMIC ACID                                                
HETNAM     GLC ALPHA-D-GLUCOSE                                                  
HETNAM      CA CALCIUM ION                                                      
HETNAM      CL CHLORIDE ION                                                     
FORMUL   1  PCA    C5 H7 N O3                                                   
FORMUL   2  GLC    11(C6 H12 O6)                                                
FORMUL   5   CA    CA 2+                                                        
FORMUL   6   CL    CL 1-                                                        
FORMUL   7  HOH   *584(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 GLN A  161  VAL A  163  5                                   3    
HELIX    8   8 LYS A  172  GLY A  190  1                                  19    
HELIX    9   9 ALA A  198  MET A  202  5                                   5    
HELIX   10  10 TRP A  203  ASP A  212  1                                  10    
HELIX   11  11 GLN A  243  PHE A  248  5                                   6    
HELIX   12  12 PHE A  256  ARG A  267  1                                  12    
HELIX   13  13 LYS A  273  TRP A  280  5                                   8    
HELIX   14  14 GLY A  281  GLY A  285  5                                   5    
HELIX   15  15 PRO A  288  ASP A  290  5                                   3    
HELIX   16  16 ASP A  300  GLY A  304  5                                   5    
HELIX   17  17 GLY A  308  ILE A  312  5                                   5    
HELIX   18  18 THR A  314  TRP A  316  5                                   3    
HELIX   19  19 ASP A  317  HIS A  331  1                                  15    
HELIX   20  20 CYS A  384  ARG A  387  5                                   4    
HELIX   21  21 TRP A  388  ASP A  402  1                                  15    
HELIX   22  22 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 231   N  ILE A 196           
SHEET    6   A 9 ARG A 252  THR A 254  1  O  ARG A 252   N  ILE A 230           
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  MET A 102           
SHEET    1   C 2 ASN A 362  ASN A 363  0                                        
SHEET    2   C 2 VAL A 366  ILE A 367 -1  O  VAL A 366   N  ASN A 363           
SHEET    1   D 4 PHE A 406  ASP A 411  0                                        
SHEET    2   D 4 GLN A 416  ARG A 421 -1  O  GLY A 420   N  ALA A 407           
SHEET    3   D 4 GLY A 425  ASN A 430 -1  O  PHE A 429   N  VAL A 417           
SHEET    4   D 4 PHE A 487  HIS A 491 -1  O  ILE A 490   N  PHE A 426           
SHEET    1   E 2 LEU A 436  GLN A 441  0                                        
SHEET    2   E 2 THR A 474  ILE A 479 -1  O  ALA A 475   N  LEU A 440           
SHEET    1   F 2 GLY A 447  CYS A 450  0                                        
SHEET    2   F 2 LYS A 466  VAL A 469 -1  O  VAL A 469   N  GLY A 447           
SHEET    1   G 2 LYS A 457  VAL A 458  0                                        
SHEET    2   G 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  2.02  
SSBOND   2 CYS A   70    CYS A  115                          1555   1555  2.04  
SSBOND   3 CYS A  141    CYS A  160                          1555   1555  2.04  
SSBOND   4 CYS A  378    CYS A  384                          1555   1555  2.04  
SSBOND   5 CYS A  450    CYS A  462                          1555   1555  2.03  
LINK         C   PCA A   1                 N   TYR A   2     1555   1555  1.34  
LINK         O4 AGLC A 704                 C1 AGLC A 703     1555   1555  1.43  
LINK         O4 AGLC A 703                 C1 AGLC A 702     1555   1555  1.44  
LINK         O6 AGLC A 703                 C1 AGLC A 706     1555   1555  1.44  
LINK         O4 AGLC A 705                 C1 AGLC A 704     1555   1555  1.45  
LINK         O4 AGLC A 604                 C1 AGLC A 603     1555   1555  1.45  
LINK         O4 AGLC A 702                 C1 AGLC A 701     1555   1555  1.45  
LINK         O4 AGLC A 603                 C1 AGLC A 602     1555   1555  1.46  
LINK         O4 AGLC A 602                 C1 AGLC A 601     1555   1555  1.48  
LINK         O   ARG A 158                CA    CA A 501     1555   1555  2.32  
LINK         OD1 ASN A 100                CA    CA A 501     1555   1555  2.40  
LINK         O   HIS A 201                CA    CA A 501     1555   1555  2.42  
LINK        CA    CA A 501                 O   HOH A 767     1555   1555  2.42  
LINK         OD2 ASP A 167                CA    CA A 501     1555   1555  2.45  
LINK        CA    CA A 501                 O   HOH A 760     1555   1555  2.47  
LINK         OD1 ASP A 167                CA    CA A 501     1555   1555  2.52  
LINK        CA    CA A 501                 O   HOH A 852     1555   1555  2.54  
CISPEP   1 ASN A   53    PRO A   54          0        -5.34                     
CISPEP   2 VAL A  129    PRO A  130          0        -5.00                     
SITE     1 AC1  5 ALA A 108  HOH A 569  HOH A 570  GLC A 603                    
SITE     2 AC1  5 HOH A 606                                                     
SITE     1 AC2  7 THR A  52  ASN A  53  GLU A 272  ASN A 279                    
SITE     2 AC2  7 GLC A 602  GLC A 604  HOH A 696                               
SITE     1 AC3 11 THR A  52  ASN A  53  LYS A 261  TRP A 284                    
SITE     2 AC3 11 GLY A 285  HOH A 573  HOH A 574  GLC A 601                    
SITE     3 AC3 11 GLC A 603  HOH A 979  HOH A 998                               
SITE     1 AC4  9 ASN A  53  PRO A  54  HOH A 530  HOH A 571                    
SITE     2 AC4  9 HOH A 572  GLC A 602  HOH A 979  HOH A1034                    
SITE     3 AC4  9 HOH A1035                                                     
SITE     1 AC5 12 TYR A  62  HIS A 101  ASP A 197  ALA A 198                    
SITE     2 AC5 12 GLU A 233  ILE A 235  ASP A 300  HOH A 552                    
SITE     3 AC5 12 HOH A 582  HOH A 583  HOH A 584  GLC A 704                    
SITE     1 AC6 10 TRP A  58  TRP A  59  TYR A  62  GLN A  63                    
SITE     2 AC6 10 ASP A 300  HOH A 582  HOH A 584  GLC A 703                    
SITE     3 AC6 10 GLC A 705  HOH A1023                                          
SITE     1 AC7  5 GLN A  63  VAL A 163  GLC A 702  GLC A 704                    
SITE     2 AC7  5 GLC A 706                                                     
SITE     1 AC8  3 HOH A 578  GLC A 701  GLC A 703                               
SITE     1 AC9  8 GLY A 147  HOH A 550  HOH A 551  HOH A 575                    
SITE     2 AC9  8 HOH A 576  HOH A 577  HOH A 622  GLC A 702                    
SITE     1 BC1 11 TRP A  59  GLN A  63  GLY A 104  SER A 105                    
SITE     2 BC1 11 GLY A 106  ALA A 107  HOH A 579  HOH A 580                    
SITE     3 BC1 11 HOH A 581  HOH A 679  GLC A 703                               
SITE     1 BC2  8 LYS A 140  GLU A 171  TRP A 203  ASP A 206                    
SITE     2 BC2  8 HOH A 778  HOH A 805  HOH A 949  HOH A1093                    
SITE     1 BC3  7 ASN A 100  ARG A 158  ASP A 167  HIS A 201                    
SITE     2 BC3  7 HOH A 760  HOH A 767  HOH A 852                               
SITE     1 BC4  3 ARG A 195  ASN A 298  ARG A 337                               
CRYST1   70.590  114.820  118.780  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      0.014166  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008709  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008419        0.00000                         
HETATM    1  N   PCA A   1      29.919  44.461  34.158  1.00 26.34           N  
HETATM    2  CA  PCA A   1      29.952  44.044  35.543  1.00 26.37           C  
HETATM    3  CB  PCA A   1      28.861  44.738  36.402  1.00 28.47           C  
HETATM    4  CG  PCA A   1      28.015  45.512  35.417  1.00 31.89           C  
HETATM    5  CD  PCA A   1      28.841  45.415  34.153  1.00 29.27           C  
HETATM    6  OE  PCA A   1      28.651  46.109  33.182  1.00 43.41           O  
HETATM    7  C   PCA A   1      29.824  42.525  35.552  1.00 22.76           C  
HETATM    8  O   PCA A   1      30.492  41.873  36.356  1.00 20.19           O  
HETATM    9  HA  PCA A   1      30.828  44.270  35.917  1.00 26.72           H  
HETATM   10  HB2 PCA A   1      28.309  44.059  36.842  1.00 28.33           H  
HETATM   11  HB3 PCA A   1      29.289  45.276  37.101  1.00 27.64           H  
HETATM   12  HG2 PCA A   1      27.161  45.049  35.285  1.00 30.25           H  
HETATM   13  HG3 PCA A   1      27.822  46.402  35.779  1.00 30.47           H  
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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