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Database: PDB
Entry: 3L2M
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HEADER    HYDROLASE                               15-DEC-09   3L2M              
TITLE     X-RAY CRYSTALLOGRAPHIC ANALYSIS OF PIG PANCREATIC ALPHA-AMYLASE WITH  
TITLE    2 ALPHA-CYCLODEXTRIN                                                   
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, ALPHA-CYCLODEXTRIN,    
KEYWDS   2 CARBOHYDRATE METABOLISM, GLYCOPROTEIN, GLYCOSIDASE, METAL-BINDING,   
KEYWDS   3 PYRROLIDONE CARBOXYLIC ACID, SECRETED, HYDROLASE                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.B.LARSON,J.S.DAY,A.MCPHERSON                                        
REVDAT   3   13-JUL-11 3L2M    1       VERSN                                    
REVDAT   2   21-APR-10 3L2M    1       JRNL                                     
REVDAT   1   14-APR-10 3L2M    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.    1.97 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) : 1.97                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.30                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 89.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 55805                          
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) : 0.130                           
REMARK   3   R VALUE            (WORKING SET) : 0.127                           
REMARK   3   FREE R VALUE                     : 0.160                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.100                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 6279                            
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) : 1.97                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.02                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1115                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 23.96                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2400                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 103                          
REMARK   3   BIN FREE R VALUE                    : 0.2790                       
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          : 200                                     
REMARK   3   SOLVENT ATOMS            : 592                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : 22.00                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 18.81                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.49000                                              
REMARK   3    B22 (A**2) : -0.48000                                             
REMARK   3    B33 (A**2) : 0.00000                                              
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): 0.101         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.102         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.064         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.189         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.972                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.955                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4613 ; 0.012 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  4234 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  6371 ; 1.387 ; 1.973       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  9569 ; 0.712 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   587 ; 5.890 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   222 ;35.692 ;23.964       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   702 ;13.896 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    31 ;18.079 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   702 ; 0.087 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  5208 ; 0.006 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  1127 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   878 ; 0.208 ; 0.300       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  4002 ; 0.183 ; 0.300       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  2268 ; 0.187 ; 0.500       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  2666 ; 0.091 ; 0.500       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   673 ; 0.204 ; 0.500       
REMARK   3   H-BOND (X...Y) OTHERS             (A):   507 ; 0.180 ; 0.500       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):     2 ; 0.016 ; 0.500       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):     9 ; 0.131 ; 0.300       
REMARK   3   SYMMETRY VDW OTHERS               (A):    34 ; 0.221 ; 0.300       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    33 ; 0.199 ; 0.500       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):    10 ; 0.192 ; 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):  2671 ; 2.148 ; 4.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  1097 ; 0.551 ; 4.000       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4352 ; 3.128 ; 8.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1942 ; 3.789 ; 8.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1995 ; 4.917 ;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  : 21                                         
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):  38.9310  33.3860  44.7090              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0006 T22:   0.0188                                     
REMARK   3      T33:   0.0031 T12:   0.0021                                     
REMARK   3      T13:   0.0001 T23:   0.0026                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8350 L22:   1.7747                                     
REMARK   3      L33:   0.8629 L12:   0.1880                                     
REMARK   3      L13:   0.0898 L23:   0.1977                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0143 S12:  -0.0026 S13:  -0.0140                       
REMARK   3      S21:  -0.0034 S22:  -0.0153 S23:  -0.0699                       
REMARK   3      S31:  -0.0073 S32:   0.0197 S33:   0.0011                       
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):  35.0740  49.8070  62.1280              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0975 T22:   0.0623                                     
REMARK   3      T33:   0.0144 T12:  -0.0004                                     
REMARK   3      T13:  -0.0053 T23:  -0.0163                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.1550 L22:   1.7747                                     
REMARK   3      L33:   1.4466 L12:   0.9228                                     
REMARK   3      L13:  -0.4700 L23:   0.1809                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1441 S12:  -0.4025 S13:   0.1741                       
REMARK   3      S21:   0.2686 S22:  -0.0905 S23:   0.0382                       
REMARK   3      S31:  -0.1302 S32:  -0.0224 S33:  -0.0536                       
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):  32.5110   9.0980  28.8900              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0252 T22:   0.0174                                     
REMARK   3      T33:   0.0213 T12:   0.0054                                     
REMARK   3      T13:   0.0018 T23:  -0.0181                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4994 L22:   2.3840                                     
REMARK   3      L33:   3.1792 L12:   0.1172                                     
REMARK   3      L13:  -0.4477 L23:   0.1431                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0087 S12:   0.1004 S13:  -0.1004                       
REMARK   3      S21:  -0.1249 S22:   0.0105 S23:  -0.0574                       
REMARK   3      S31:   0.1369 S32:   0.0360 S33:  -0.0019                       
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):  51.5940  39.1790  73.0900              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1321 T22:   0.0940                                     
REMARK   3      T33:   0.0856 T12:   0.0115                                     
REMARK   3      T13:   0.0083 T23:   0.0007                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  13.4249 L22:   0.3327                                     
REMARK   3      L33:   1.4847 L12:  -2.1124                                     
REMARK   3      L13:   4.4645 L23:  -0.7024                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0772 S12:  -0.0514 S13:   0.2232                       
REMARK   3      S21:   0.0101 S22:   0.0031 S23:  -0.0356                       
REMARK   3      S31:  -0.0240 S32:  -0.0191 S33:   0.0740                       
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):  48.2690  42.5720  72.4600              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1232 T22:   0.1786                                     
REMARK   3      T33:   0.0924 T12:   0.0480                                     
REMARK   3      T13:   0.0271 T23:   0.0305                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  14.4903 L22:  17.3134                                     
REMARK   3      L33:   4.1381 L12:   9.5915                                     
REMARK   3      L13:   5.6880 L23:   8.3356                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0925 S12:  -0.0313 S13:  -0.1038                       
REMARK   3      S21:   0.0312 S22:  -0.2250 S23:   0.3434                       
REMARK   3      S31:   0.0241 S32:  -0.0950 S33:   0.1325                       
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):  43.6480  41.5040  71.4050              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1049 T22:   0.1771                                     
REMARK   3      T33:   0.1324 T12:  -0.0190                                     
REMARK   3      T13:  -0.0029 T23:  -0.0149                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.5206 L22:  30.2411                                     
REMARK   3      L33:  14.8188 L12:  -8.3057                                     
REMARK   3      L13:  -0.0592 L23:   6.7140                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1006 S12:  -0.0301 S13:   0.0256                       
REMARK   3      S21:   0.2060 S22:  -0.0440 S23:   0.0035                       
REMARK   3      S31:  -0.2935 S32:  -0.3220 S33:   0.1445                       
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):  42.2980  37.1280  71.0370              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1329 T22:   0.1842                                     
REMARK   3      T33:   0.1540 T12:  -0.0034                                     
REMARK   3      T13:  -0.0002 T23:  -0.0394                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  16.6495 L22:   4.6282                                     
REMARK   3      L33:   0.3205 L12:  -8.7780                                     
REMARK   3      L13:  -2.3074 L23:   1.2162                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0639 S12:   0.2091 S13:  -0.2470                       
REMARK   3      S21:  -0.0329 S22:  -0.1043 S23:   0.1313                       
REMARK   3      S31:  -0.0102 S32:  -0.0398 S33:   0.0403                       
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   605        A   605                          
REMARK   3    ORIGIN FOR THE GROUP (A):  45.6240  33.1180  71.9170              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1048 T22:   0.1416                                     
REMARK   3      T33:   0.1314 T12:   0.0078                                     
REMARK   3      T13:   0.0023 T23:   0.0161                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   9.5140 L22:  26.7351                                     
REMARK   3      L33:   4.5194 L12:  15.1784                                     
REMARK   3      L13:   1.5142 L23:   5.6974                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1346 S12:  -0.0478 S13:   0.1167                       
REMARK   3      S21:   0.0154 S22:  -0.0699 S23:   0.3470                       
REMARK   3      S31:   0.2749 S32:  -0.0032 S33:   0.2044                       
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   606        A   606                          
REMARK   3    ORIGIN FOR THE GROUP (A):  50.1230  34.2260  72.9240              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0711 T22:   0.1303                                     
REMARK   3      T33:   0.1079 T12:  -0.0202                                     
REMARK   3      T13:  -0.0026 T23:  -0.0145                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5975 L22:  26.5439                                     
REMARK   3      L33:  21.9417 L12:  -6.4172                                     
REMARK   3      L13:   0.0000 L23:   0.0000                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0687 S12:   0.0051 S13:  -0.0581                       
REMARK   3      S21:  -0.2750 S22:  -0.0698 S23:   0.2806                       
REMARK   3      S31:   0.2261 S32:  -0.1280 S33:   0.0012                       
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   701        A   701                          
REMARK   3    ORIGIN FOR THE GROUP (A):  39.0850  37.0420  64.2920              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2816 T22:   0.1343                                     
REMARK   3      T33:   0.1517 T12:  -0.0079                                     
REMARK   3      T13:   0.0417 T23:  -0.0284                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  39.5054 L22:   0.0001                                     
REMARK   3      L33:  10.2950 L12:  -0.0265                                     
REMARK   3      L13:  20.1669 L23:  -0.0135                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1399 S12:  -0.3446 S13:   0.2656                       
REMARK   3      S21:   0.0032 S22:   0.0022 S23:  -0.0012                       
REMARK   3      S31:  -0.0703 S32:  -0.1739 S33:   0.1377                       
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   702        A   702                          
REMARK   3    ORIGIN FOR THE GROUP (A):  37.1660  35.1620  59.8190              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2857 T22:   0.1603                                     
REMARK   3      T33:   0.2374 T12:  -0.0043                                     
REMARK   3      T13:  -0.0637 T23:   0.0169                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  32.1507 L22:   0.2808                                     
REMARK   3      L33:  20.0226 L12:   0.0000                                     
REMARK   3      L13:   2.3708 L23:   0.0000                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1663 S12:  -0.1439 S13:  -0.2042                       
REMARK   3      S21:   0.0170 S22:   0.0157 S23:   0.0180                       
REMARK   3      S31:   0.1077 S32:   0.1051 S33:   0.1505                       
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   703        A   703                          
REMARK   3    ORIGIN FOR THE GROUP (A):  32.4600  35.0700  59.8750              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1655 T22:   0.1445                                     
REMARK   3      T33:   0.2598 T12:   0.0130                                     
REMARK   3      T13:   0.0450 T23:   0.0344                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5330 L22:   6.6498                                     
REMARK   3      L33:  46.1880 L12:   1.8822                                     
REMARK   3      L13:   4.9604 L23:  17.5254                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0087 S12:   0.0517 S13:  -0.0245                       
REMARK   3      S21:   0.0096 S22:   0.1804 S23:  -0.0747                       
REMARK   3      S31:   0.0305 S32:   0.4743 S33:  -0.1891                       
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   704        A   704                          
REMARK   3    ORIGIN FOR THE GROUP (A):  29.7470  36.0240  64.1050              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2673 T22:   0.1372                                     
REMARK   3      T33:   0.1372 T12:   0.0089                                     
REMARK   3      T13:   0.0299 T23:   0.0140                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  23.1035 L22:   0.2050                                     
REMARK   3      L33:   4.4811 L12:   2.1751                                     
REMARK   3      L13:  10.1743 L23:   0.9580                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0834 S12:   0.4098 S13:  -0.2888                       
REMARK   3      S21:   0.0098 S22:   0.0429 S23:  -0.0281                       
REMARK   3      S31:   0.0485 S32:   0.1816 S33:  -0.1264                       
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   705        A   705                          
REMARK   3    ORIGIN FOR THE GROUP (A):  31.6170  37.3200  68.3000              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2353 T22:   0.1142                                     
REMARK   3      T33:   0.2278 T12:  -0.0212                                     
REMARK   3      T13:  -0.1090 T23:   0.0094                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  37.0412 L22:   1.8099                                     
REMARK   3      L33:  22.3709 L12:   0.0000                                     
REMARK   3      L13:   6.3629 L23:   0.0000                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0313 S12:  -0.1018 S13:   0.0721                       
REMARK   3      S21:  -0.0110 S22:   0.0237 S23:  -0.0154                       
REMARK   3      S31:  -0.0237 S32:   0.0779 S33:  -0.0549                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 15                                                     
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):  36.5980  38.1380  68.5700              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1352 T22:   0.1804                                     
REMARK   3      T33:   0.2634 T12:   0.0178                                     
REMARK   3      T13:   0.0445 T23:   0.0258                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7482 L22:   2.6166                                     
REMARK   3      L33:  25.7302 L12:   1.3991                                     
REMARK   3      L13:   4.3872 L23:   8.2050                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0607 S12:  -0.0777 S13:   0.0120                       
REMARK   3      S21:   0.1070 S22:  -0.1479 S23:   0.0276                       
REMARK   3      S31:   0.3432 S32:  -0.4737 S33:   0.0871                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 16                                                     
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):  40.0550  66.8410  64.0170              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2345 T22:   0.3217                                     
REMARK   3      T33:   0.3201 T12:  -0.0438                                     
REMARK   3      T13:   0.0614 T23:  -0.0610                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  27.6998 L22:   7.9803                                     
REMARK   3      L33:   0.1246 L12:   0.0000                                     
REMARK   3      L13:   0.0011 L23:  -0.0018                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1279 S12:   0.3130 S13:   0.1873                       
REMARK   3      S21:   0.0736 S22:  -0.0458 S23:  -0.1254                       
REMARK   3      S31:  -0.0669 S32:   0.0419 S33:   0.1737                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 17                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   802        A   802                          
REMARK   3    ORIGIN FOR THE GROUP (A):  36.3400  69.8750  63.5330              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1613 T22:   0.1935                                     
REMARK   3      T33:   0.2345 T12:   0.0364                                     
REMARK   3      T13:   0.0011 T23:   0.0707                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.5677 L22:  11.1202                                     
REMARK   3      L33:  26.2104 L12:   5.3433                                     
REMARK   3      L13:   8.2033 L23:  17.0723                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0001 S12:   0.1029 S13:  -0.0724                       
REMARK   3      S21:  -0.0023 S22:   0.2122 S23:  -0.1407                       
REMARK   3      S31:  -0.0052 S32:   0.3244 S33:  -0.2120                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 18                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   803        A   803                          
REMARK   3    ORIGIN FOR THE GROUP (A):  33.0210  69.4850  59.4350              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1374 T22:   0.1587                                     
REMARK   3      T33:   0.1366 T12:  -0.0033                                     
REMARK   3      T13:   0.0062 T23:   0.0017                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  25.9793 L22:  52.1359                                     
REMARK   3      L33:  53.1797 L12:   0.0000                                     
REMARK   3      L13:   0.0000 L23:   0.0000                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4829 S12:   0.6259 S13:   0.5448                       
REMARK   3      S21:   0.1780 S22:   0.1689 S23:  -0.5684                       
REMARK   3      S31:   0.2388 S32:  -0.6138 S33:   0.3140                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 19                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   804        A   804                          
REMARK   3    ORIGIN FOR THE GROUP (A):  34.7350  65.7570  56.3660              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2336 T22:   0.1592                                     
REMARK   3      T33:   0.1868 T12:   0.0155                                     
REMARK   3      T13:   0.0571 T23:  -0.0191                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  42.1025 L22:   0.6003                                     
REMARK   3      L33:   6.0870 L12:  -5.0266                                     
REMARK   3      L13:  16.0084 L23:  -1.9111                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0682 S12:  -0.0331 S13:   0.1688                       
REMARK   3      S21:   0.0039 S22:   0.0038 S23:  -0.0185                       
REMARK   3      S31:  -0.0317 S32:  -0.0167 S33:   0.0643                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 20                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   805        A   805                          
REMARK   3    ORIGIN FOR THE GROUP (A):  39.4760  63.9520  56.2990              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1174 T22:   0.1995                                     
REMARK   3      T33:   0.2180 T12:   0.0029                                     
REMARK   3      T13:   0.0086 T23:   0.0388                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0261 L22:  43.0648                                     
REMARK   3      L33:  13.2960 L12:   1.0459                                     
REMARK   3      L13:   0.5815 L23:  23.9271                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0013 S12:   0.0071 S13:  -0.0047                       
REMARK   3      S21:   0.0856 S22:  -0.0274 S23:   0.0484                       
REMARK   3      S31:   0.0328 S32:  -0.0175 S33:   0.0287                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 21                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   806        A   806                          
REMARK   3    ORIGIN FOR THE GROUP (A):  42.6080  65.5190  59.6510              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3064 T22:   0.1688                                     
REMARK   3      T33:   0.2006 T12:  -0.0287                                     
REMARK   3      T13:   0.0149 T23:  -0.0234                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  43.1989 L22:  27.0931                                     
REMARK   3      L33:   0.1641 L12:  -0.6859                                     
REMARK   3      L13:  -0.0021 L23:   0.0007                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4950 S12:  -0.0260 S13:  -0.5081                       
REMARK   3      S21:   0.0169 S22:   0.3641 S23:   0.3170                       
REMARK   3      S31:   0.1812 S32:  -0.0550 S33:   0.1310                       
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 3L2M 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 RCSB056754.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 17-JUN-93                          
REMARK 200  TEMPERATURE           (KELVIN) : 298                                
REMARK 200  PH                             : 6.75                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU RU200                       
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : 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   : 62592                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.970                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 29.300                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 84.6                               
REMARK 200  DATA REDUNDANCY                : 4.840                              
REMARK 200  R MERGE                    (I) : 0.06800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 19.8300                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.97                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.07                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 36.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.61                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.17800                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.070                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: DIRECT PLACEMENT OF MODEL IN UNIT CELL                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 71.72                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.35                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.010 M CACODYLATE, 0.002 M CALCIUM      
REMARK 280  CHLORIDE, SOAKING OF ALPHA-CYCLODEXTRIN, PH 6.75, EVAPORATION,      
REMARK 280  TEMPERATURE 298K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       35.32500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       59.42500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       57.44000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       59.42500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       35.32500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       57.44000            
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   O3   GLC A   704     O2   GLC A   703              2.08            
REMARK 500   OG   SER A   470     OD1  ASP A   472              2.17            
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      -58.58   -142.33                                   
REMARK 500    MET A 102     -146.69   -104.07                                   
REMARK 500    VAL A 163       47.14     37.40                                   
REMARK 500    ASP A 317       54.93   -106.78                                   
REMARK 500    SER A 414     -101.41   -139.34                                   
REMARK 500    ASP A 433       31.45    -86.81                                   
REMARK 500    PRO A 486       43.25    -81.54                                   
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 549        DISTANCE =  5.19 ANGSTROMS                       
REMARK 525    HOH A 610        DISTANCE =  6.87 ANGSTROMS                       
REMARK 525    HOH A 625        DISTANCE =  5.25 ANGSTROMS                       
REMARK 525    HOH A 739        DISTANCE =  5.23 ANGSTROMS                       
REMARK 525    HOH A1098        DISTANCE =  5.14 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 156.5                                              
REMARK 620 3 HOH A 771   O    76.9 103.8                                        
REMARK 620 4 HIS A 201   O    81.2  75.7  82.5                                  
REMARK 620 5 ASP A 167   OD1 119.5  82.3  73.2 142.1                            
REMARK 620 6 ASP A 167   OD2  76.9 126.3  90.2 158.0  52.3                      
REMARK 620 7 HOH A 861   O    73.0  99.1 147.6  81.3 133.1  94.4                
REMARK 620 8 HOH A 764   O   123.6  66.7 149.9 119.7  77.1  75.5  61.3          
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 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC A 606                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC A 605                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC A 604                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC A 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC A 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC A 706                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC A 705                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC A 704                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC A 703                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC A 702                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC A 701                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC A 803                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC A 802                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC A 801                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC A 806                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC A 805                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC A 804                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 501                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
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: 3L2L   RELATED DB: PDB                                   
REMARK 900 X-RAY CRYSTALLOGRAPHIC ANALYSIS OF PIG PANCREATIC ALPHA-             
REMARK 900 AMYLASE WITH LIMIT DEXTRIN AND OLIGOSACCHARIDE                       
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  3L2M A    1   496  UNP    P00690   AMYP_PIG        16    511             
SEQADV 3L2M PCA A    1  UNP  P00690    GLN    16 SEE REMARK 999                 
SEQADV 3L2M 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 3L2M PCA A    1  GLU  PYROGLUTAMIC ACID                                  
HET    PCA  A   1      13                                                       
HET    GLC  A 601      21                                                       
HET    GLC  A 606      21                                                       
HET    GLC  A 605      21                                                       
HET    GLC  A 604      21                                                       
HET    GLC  A 603      21                                                       
HET    GLC  A 602      21                                                       
HET    GLC  A 706      21                                                       
HET    GLC  A 705      21                                                       
HET    GLC  A 704      21                                                       
HET    GLC  A 703      21                                                       
HET    GLC  A 702      21                                                       
HET    GLC  A 701      21                                                       
HET    GLC  A 803      21                                                       
HET    GLC  A 802      21                                                       
HET    GLC  A 801      21                                                       
HET    GLC  A 806      21                                                       
HET    GLC  A 805      21                                                       
HET    GLC  A 804      21                                                       
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    18(C6 H12 O6)                                                
FORMUL   5   CA    CA 2+                                                        
FORMUL   6   CL    CL 1-                                                        
FORMUL   7  HOH   *592(H2 O)                                                    
HELIX    1   1 ARG A   20  TYR A   31  1                                  12    
HELIX    2   2 PRO A   57  GLN A   63  5                                   7    
HELIX    3   3 ASN A   75  VAL A   89  1                                  15    
HELIX    4   4 ASN A  120  ARG A  124  5                                   5    
HELIX    5   5 SER A  132  PHE A  136  5                                   5    
HELIX    6   6 ASP A  153  CYS A  160  1                                   8    
HELIX    7   7 LYS A  172  GLY A  190  1                                  19    
HELIX    8   8 ALA A  198  MET A  202  5                                   5    
HELIX    9   9 TRP A  203  ASP A  212  1                                  10    
HELIX   10  10 GLN A  243  PHE A  248  5                                   6    
HELIX   11  11 PHE A  256  ARG A  267  1                                  12    
HELIX   12  12 LYS A  273  TRP A  280  5                                   8    
HELIX   13  13 GLY A  281  GLY A  285  5                                   5    
HELIX   14  14 PRO A  288  ASP A  290  5                                   3    
HELIX   15  15 ASP A  300  GLY A  304  5                                   5    
HELIX   16  16 GLY A  308  ILE A  312  5                                   5    
HELIX   17  17 THR A  314  TRP A  316  5                                   3    
HELIX   18  18 ASP A  317  HIS A  331  1                                  15    
HELIX   19  19 CYS A  384  ARG A  387  5                                   4    
HELIX   20  20 TRP A  388  ASP A  402  1                                  15    
HELIX   21  21 GLU A  493  LYS A  495  5                                   3    
SHEET    1   A 9 SER A  12  LEU A  16  0                                        
SHEET    2   A 9 GLY A  39  VAL A  42  1  O  GLN A  41   N  VAL A  14           
SHEET    3   A 9 ARG A  92  ALA A  97  1  O  TYR A  94   N  VAL A  40           
SHEET    4   A 9 GLY A 193  ILE A 196  1  O  ARG A 195   N  ALA A  97           
SHEET    5   A 9 PHE A 229  GLN A 232  1  O  PHE A 231   N  ILE A 196           
SHEET    6   A 9 ARG A 252  THR A 254  1  O  ARG A 252   N  GLN A 232           
SHEET    7   A 9 ALA A 292  VAL A 294  1  O  LEU A 293   N  VAL A 253           
SHEET    8   A 9 PHE A 335  SER A 340  1  O  PHE A 335   N  VAL A 294           
SHEET    9   A 9 SER A  12  LEU A  16  1  N  ILE A  13   O  VAL A 338           
SHEET    1   B 2 HIS A 101  GLY A 104  0                                        
SHEET    2   B 2 LEU A 165  ASP A 167 -1  O  LEU A 166   N  CYS A 103           
SHEET    1   C 2 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 488   N  VAL A 428           
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  2.03  
SSBOND   2 CYS A   70    CYS A  115                          1555   1555  2.04  
SSBOND   3 CYS A  141    CYS A  160                          1555   1555  2.08  
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  1.34  
LINK         O4  GLC A 601                 C1  GLC A 606     1555   1555  1.44  
LINK         O4  GLC A 702                 C1  GLC A 701     1555   1555  1.44  
LINK         O4  GLC A 606                 C1  GLC A 605     1555   1555  1.44  
LINK         O4  GLC A 805                 C1  GLC A 804     1555   1555  1.44  
LINK         O4  GLC A 603                 C1  GLC A 602     1555   1555  1.45  
LINK         C1  GLC A 601                 O4  GLC A 602     1555   1555  1.45  
LINK         O4  GLC A 806                 C1  GLC A 805     1555   1555  1.45  
LINK         O4  GLC A 802                 C1  GLC A 801     1555   1555  1.45  
LINK         O4  GLC A 605                 C1  GLC A 604     1555   1555  1.45  
LINK         O4  GLC A 705                 C1  GLC A 704     1555   1555  1.45  
LINK         O4  GLC A 801                 C1  GLC A 806     1555   1555  1.45  
LINK         C1  GLC A 803                 O4  GLC A 804     1555   1555  1.45  
LINK         O4  GLC A 704                 C1  GLC A 703     1555   1555  1.45  
LINK         O4  GLC A 604                 C1  GLC A 603     1555   1555  1.45  
LINK         O4  GLC A 703                 C1  GLC A 702     1555   1555  1.45  
LINK         C1  GLC A 706                 O4  GLC A 701     1555   1555  1.45  
LINK         O4  GLC A 803                 C1  GLC A 802     1555   1555  1.45  
LINK         O4  GLC A 706                 C1  GLC A 705     1555   1555  1.46  
LINK         O   ARG A 158                CA    CA A 501     1555   1555  2.40  
LINK         OD1 ASN A 100                CA    CA A 501     1555   1555  2.41  
LINK        CA    CA A 501                 O   HOH A 771     1555   1555  2.42  
LINK         O   HIS A 201                CA    CA A 501     1555   1555  2.43  
LINK         OD1 ASP A 167                CA    CA A 501     1555   1555  2.45  
LINK         OD2 ASP A 167                CA    CA A 501     1555   1555  2.52  
LINK        CA    CA A 501                 O   HOH A 861     1555   1555  2.53  
LINK        CA    CA A 501                 O   HOH A 764     1555   1555  2.58  
CISPEP   1 ASN A   53    PRO A   54          0         0.17                     
CISPEP   2 VAL A  129    PRO A  130          0         0.34                     
SITE     1 AC1  7 THR A  52  GLU A 272  ASN A 279  TRP A 284                    
SITE     2 AC1  7 GLC A 602  GLC A 606  HOH A 712                               
SITE     1 AC2  8 THR A  52  ASN A  53  LYS A 261  GLY A 283                    
SITE     2 AC2  8 TRP A 284  GLC A 601  GLC A 605  HOH A 723                    
SITE     1 AC3  6 PRO A  54  GLC A 604  GLC A 606  HOH A1030                    
SITE     2 AC3  6 HOH A1031  HOH A1032                                          
SITE     1 AC4  4 ASN A  53  GLC A 603  GLC A 605  HOH A1028                    
SITE     1 AC5  8 ASN A  53  GLY A 106  HOH A 500  HOH A 526                    
SITE     2 AC5  8 GLC A 602  GLC A 604  HOH A 635  HOH A 965                    
SITE     1 AC6  5 ASN A  53  ALA A 108  GLC A 601  GLC A 603                    
SITE     2 AC6  5 HOH A1029                                                     
SITE     1 AC7  2 GLC A 701  GLC A 705                                          
SITE     1 AC8  3 GLC A 704  GLC A 706  HOH A1004                               
SITE     1 AC9  4 TYR A 151  VAL A 163  GLC A 703  GLC A 705                    
SITE     1 BC1  5 LEU A 162  GLC A 702  GLC A 704  HOH A1035                    
SITE     2 BC1  5 HOH A1044                                                     
SITE     1 BC2  7 TRP A  59  ASP A 300  HIS A 305  GLC A 701                    
SITE     2 BC2  7 GLC A 703  HOH A1034  HOH A1035                               
SITE     1 BC3  5 TRP A  59  GLN A  63  VAL A 163  GLC A 702                    
SITE     2 BC3  5 GLC A 706                                                     
SITE     1 BC4  3 TRP A 134  GLC A 802  GLC A 804                               
SITE     1 BC5  3 TRP A 134  GLC A 801  GLC A 803                               
SITE     1 BC6  3 SER A 132  GLC A 802  GLC A 806                               
SITE     1 BC7  4 PRO A 130  SER A 132  GLC A 801  GLC A 805                    
SITE     1 BC8  9 PRO A 130  TYR A 131  SER A 132  TRP A 134                    
SITE     2 BC8  9 ASP A 135  TYR A 174  GLC A 804  GLC A 806                    
SITE     3 BC8  9 HOH A1070                                                     
SITE     1 BC9  4 TRP A 134  LYS A 172  GLC A 803  GLC A 805                    
SITE     1 CC1  7 ASN A 100  ARG A 158  ASP A 167  HIS A 201                    
SITE     2 CC1  7 HOH A 764  HOH A 771  HOH A 861                               
SITE     1 CC2  3 ARG A 195  ASN A 298  ARG A 337                               
CRYST1   70.650  114.880  118.850  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      0.014154  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008705  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008414        0.00000                         
HETATM    1  N   PCA A   1      29.989  44.606  34.072  1.00 20.01           N  
HETATM    2  CA  PCA A   1      30.056  44.144  35.467  1.00 21.47           C  
HETATM    3  CB  PCA A   1      28.965  44.813  36.309  1.00 23.02           C  
HETATM    4  CG  PCA A   1      28.117  45.616  35.359  1.00 27.56           C  
HETATM    5  CD  PCA A   1      28.909  45.548  34.082  1.00 25.13           C  
HETATM    6  OE  PCA A   1      28.653  46.247  33.113  1.00 39.42           O  
HETATM    7  C   PCA A   1      29.889  42.629  35.559  1.00 16.22           C  
HETATM    8  O   PCA A   1      30.412  42.021  36.478  1.00 20.14           O  
HETATM    9  HA  PCA A   1      30.927  44.393  35.838  1.00 21.48           H  
HETATM   10  HB2 PCA A   1      28.413  44.127  36.738  1.00 23.33           H  
HETATM   11  HB3 PCA A   1      29.382  45.350  37.015  1.00 22.51           H  
HETATM   12  HG2 PCA A   1      27.254  45.168  35.233  1.00 25.64           H  
HETATM   13  HG3 PCA A   1      27.943  46.501  35.744  1.00 25.75           H  
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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