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Database: PDB
Entry: 1BPL
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HEADER    GLYCOSYLTRANSFERASE                     13-JUL-95   1BPL              
TITLE     GLYCOSYLTRANSFERASE                                                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ALPHA-1,4-GLUCAN-4-GLUCANOHYDROLASE;                       
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: ALPHA-AMYLASE (BLA);                                        
COMPND   5 EC: 3.2.1.1;                                                         
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: ALPHA-1,4-GLUCAN-4-GLUCANOHYDROLASE;                       
COMPND   8 CHAIN: B;                                                            
COMPND   9 SYNONYM: ALPHA-AMYLASE (BLA);                                        
COMPND  10 EC: 3.2.1.1                                                          
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BACILLUS LICHENIFORMIS;                         
SOURCE   3 ORGANISM_TAXID: 1402;                                                
SOURCE   4 ATCC: 27811;                                                         
SOURCE   5 MOL_ID: 2;                                                           
SOURCE   6 ORGANISM_SCIENTIFIC: BACILLUS LICHENIFORMIS;                         
SOURCE   7 ORGANISM_TAXID: 1402;                                                
SOURCE   8 ATCC: 27811                                                          
KEYWDS    ALPHA-1,4-GLUCAN-4-GLUCANOHYDROLASE, ALPHA-AMYLASE                    
KEYWDS   2 GLYCOSYLTRANSFERASE                                                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.MACHIUS,G.WIEGAND,R.HUBER                                           
REVDAT   3   24-FEB-09 1BPL    1       VERSN                                    
REVDAT   2   01-APR-03 1BPL    1       JRNL                                     
REVDAT   1   17-AUG-96 1BPL    0                                                
JRNL        AUTH   M.MACHIUS,G.WIEGAND,R.HUBER                                  
JRNL        TITL   CRYSTAL STRUCTURE OF CALCIUM-DEPLETED BACILLUS               
JRNL        TITL 2 LICHENIFORMIS ALPHA-AMYLASE AT 2.2 A RESOLUTION.             
JRNL        REF    J.MOL.BIOL.                   V. 246   545 1995              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   7877175                                                      
JRNL        DOI    10.1006/JMBI.1994.0106                                       
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR 3.1                                           
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 8.00                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 89.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 28093                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.167                           
REMARK   3   FREE R VALUE                     : NULL                            
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4033                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 237                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 20.37                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.20                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.009                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.40                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 20.40                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.32                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: THE CALCIUM FREE FORM OF BLA IS           
REMARK   3  CLEAVED AFTER GLU 189 DUE TO TRACE AMOUNTS OF A GLU-C-              
REMARK   3  ENDOPEPTIDASE PRESENT IN THE PREPARATION. WITHOUT THIS              
REMARK   3  CLEAVAGE, BLA DID NOT CRYSTALLIZE UNDER THE CONDITIONS              
REMARK   3  APPLIED. DUE TO THIS CLEAVAGE, THE REGION BETWEEN TRP 182 AND       
REMARK   3  ASN 192 IS NOT VISIBLE IN THE ELECTRON DENSITY. IN ADDITION         
REMARK   3  THE FIRST TWO (N TERMINAL) RESIDUES ALA 1 AND ASN 2 AS WELL AS      
REMARK   3  THE C-TERMINAL ARG 483 ARE NOT VISIBLE. A RAMACHANDRAN PLOT         
REMARK   3  SHOWS THAT TYR 150, WHICH IS WELL DEFINED IN THE DENSITY, IS        
REMARK   3  IN THE DISALLOWED REGION. ARG 134 HAS BEEN MODELED AS LEU AS        
REMARK   3  THIS FITS BETTER INTO THE ELECTRON DENSITY.                         
REMARK   4                                                                      
REMARK   4 1BPL COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 09-SEP-94                          
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : 8.2                                
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : NULL                               
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : NULL                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 25.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
REMARK 200  DATA REDUNDANCY                : 1.900                              
REMARK 200  R MERGE                    (I) : 0.04500                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: X-PLOR 3.1                                            
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 56.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.78                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: MOLECULE: ALPHA-1,4-GLUCAN-4-            
REMARK 280  GLUCANOHYDROLASE FROM BACILLUS LICHENIFORMIS. VAPOR DIFFUSION,      
REMARK 280  ROOM TEMPERATURE PROTEIN SOLUTION: 15 MG/ML BLA IN 0.4 M            
REMARK 280  SODIUM CITRATE 2.5 MM EDTA, PH 8.2 RESERVOIR: 0.66 M SODIUM         
REMARK 280  CITRATE, 2.5 MM EDTA, PH 8.2 CALCIUM REMOVAL BY EDTA LEADS TO       
REMARK 280  A CLEAVAGE OF BLA AFTER GLU 189 DUE TO TRACE AMOUNTS OF A GLU-      
REMARK 280  C-ENDOPEPTIDASE PRESENT IN THE PREPARATION (SEE PAPER)., VAPOR      
REMARK 280  DIFFUSION                                                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y+1/2,X+1/2,Z+3/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+1/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+3/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+1/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z+1/2                                            
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        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       42.70000            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       59.90000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       59.90000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       64.05000            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       59.90000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       59.90000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       21.35000            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       59.90000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       59.90000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       64.05000            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       59.90000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       59.90000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       21.35000            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       42.70000            
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 5950 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 17820 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -30.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
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 400                                                                      
REMARK 400 COMPOUND                                                             
REMARK 400                                                                      
REMARK 400 THE CALCIUM FREE FORM OF BLA IS CLEAVED AFTER GLU 189 DUE            
REMARK 400 TO TRACE AMOUNTS OF A GLU-C-ENDOPEPTIDASE PRESENT IN THE             
REMARK 400 PREPARATION.  WITHOUT THIS CLEAVAGE, BLA DID NOT                     
REMARK 400 CRYSTALLIZE UNDER THE CONDITIONS APPLIED.  DUE TO THIS               
REMARK 400 CLEAVAGE, THE REGION BETWEEN TRP 182 AND ASN 192 IS NOT              
REMARK 400 VISIBLE IN THE ELECTRON DENSITY.  IN ADDITION THE FIRST              
REMARK 400 TWO (N TERMINAL) RESIDUES ALA 1 AND ASN 2 AS WELL AS THE             
REMARK 400 C-TERMINAL ARG 483 ARE NOT VISIBLE.  A RAMACHANDRAN PLOT             
REMARK 400 SHOWS THAT TYR 150, WHICH IS WELL DEFINED IN THE DENSITY,            
REMARK 400 IS IN THE DISALLOWED REGION.  ARG 134 HAS BEEN MODELED AS            
REMARK 400 LEU AS THIS FITS BETTER INTO THE ELECTRON DENSITY.                   
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     ALA A     1                                                      
REMARK 465     ASN A     2                                                      
REMARK 465     TRP A   182                                                      
REMARK 465     ASP A   183                                                      
REMARK 465     TRP A   184                                                      
REMARK 465     GLU A   185                                                      
REMARK 465     VAL A   186                                                      
REMARK 465     SER A   187                                                      
REMARK 465     ASN A   188                                                      
REMARK 465     GLU A   189                                                      
REMARK 465     ASN B   190                                                      
REMARK 465     GLY B   191                                                      
REMARK 465     ASN B   192                                                      
REMARK 465     ARG B   483                                                      
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     SER B  310   OG                                                  
REMARK 480     GLU B  465   CG    CD    OE1   OE2                               
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  10       53.19    -92.60                                   
REMARK 500    ALA A  58       86.33     46.33                                   
REMARK 500    LEU A  64       43.42    -88.88                                   
REMARK 500    ARG A 125       68.35    -64.86                                   
REMARK 500    ASN A 126      -45.68   -166.71                                   
REMARK 500    PHE A 143       70.76     53.70                                   
REMARK 500    TYR A 150      -30.41     75.29                                   
REMARK 500    LYS A 180       81.20     77.69                                   
REMARK 500    ASP B 266      118.52   -163.72                                   
REMARK 500    GLU B 336      120.91    -37.42                                   
REMARK 500    SER B 337       48.90   -169.66                                   
REMARK 500    PHE B 403       62.72   -100.49                                   
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 A1231        DISTANCE =  5.89 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: ACT                                                 
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: ACTIVE SITE CATALYTIC RESIDUES                     
DBREF  1BPL A    1   189  UNP    P06278   AMY_BACLI       30    218             
DBREF  1BPL B  190   483  UNP    P06278   AMY_BACLI      219    512             
SEQRES   1 A  189  ALA ASN LEU ASN GLY THR LEU MET GLN TYR PHE GLU TRP          
SEQRES   2 A  189  TYR MET PRO ASN ASP GLY GLN HIS TRP LYS ARG LEU GLN          
SEQRES   3 A  189  ASN ASP SER ALA TYR LEU ALA GLU HIS GLY ILE THR ALA          
SEQRES   4 A  189  VAL TRP ILE PRO PRO ALA TYR LYS GLY THR SER GLN ALA          
SEQRES   5 A  189  ASP VAL GLY TYR GLY ALA TYR ASP LEU TYR ASP LEU GLY          
SEQRES   6 A  189  GLU PHE HIS GLN LYS GLY THR VAL ARG THR LYS TYR GLY          
SEQRES   7 A  189  THR LYS GLY GLU LEU GLN SER ALA ILE LYS SER LEU HIS          
SEQRES   8 A  189  SER ARG ASP ILE ASN VAL TYR GLY ASP VAL VAL ILE ASN          
SEQRES   9 A  189  HIS LYS GLY GLY ALA ASP ALA THR GLU ASP VAL THR ALA          
SEQRES  10 A  189  VAL GLU VAL ASP PRO ALA ASP ARG ASN ARG VAL ILE SER          
SEQRES  11 A  189  GLY GLU HIS LEU ILE LYS ALA TRP THR HIS PHE HIS PHE          
SEQRES  12 A  189  PRO GLY ARG GLY SER THR TYR SER ASP PHE LYS TRP HIS          
SEQRES  13 A  189  TRP TYR HIS PHE ASP GLY THR ASP TRP ASP GLU SER ARG          
SEQRES  14 A  189  LYS LEU ASN ARG ILE TYR LYS PHE GLN GLY LYS ALA TRP          
SEQRES  15 A  189  ASP TRP GLU VAL SER ASN GLU                                  
SEQRES   1 B  294  ASN GLY ASN TYR ASP TYR LEU MET TYR ALA ASP ILE ASP          
SEQRES   2 B  294  TYR ASP HIS PRO ASP VAL ALA ALA GLU ILE LYS ARG TRP          
SEQRES   3 B  294  GLY THR TRP TYR ALA ASN GLU LEU GLN LEU ASP GLY PHE          
SEQRES   4 B  294  ARG LEU ASP ALA VAL LYS HIS ILE LYS PHE SER PHE LEU          
SEQRES   5 B  294  ARG ASP TRP VAL ASN HIS VAL ARG GLU LYS THR GLY LYS          
SEQRES   6 B  294  GLU MET PHE THR VAL ALA GLU TYR TRP GLN ASN ASP LEU          
SEQRES   7 B  294  GLY ALA LEU GLU ASN TYR LEU ASN LYS THR ASN PHE ASN          
SEQRES   8 B  294  HIS SER VAL PHE ASP VAL PRO LEU HIS TYR GLN PHE HIS          
SEQRES   9 B  294  ALA ALA SER THR GLN GLY GLY GLY TYR ASP MET ARG LYS          
SEQRES  10 B  294  LEU LEU ASN SER THR VAL VAL SER LYS HIS PRO LEU LYS          
SEQRES  11 B  294  ALA VAL THR PHE VAL ASP ASN HIS ASP THR GLN PRO GLY          
SEQRES  12 B  294  GLN SER LEU GLU SER THR VAL GLN THR TRP PHE LYS PRO          
SEQRES  13 B  294  LEU ALA TYR ALA PHE ILE LEU THR ARG GLU SER GLY TYR          
SEQRES  14 B  294  PRO GLN VAL PHE TYR GLY ASP MET TYR GLY THR LYS GLY          
SEQRES  15 B  294  ASP SER GLN ARG GLU ILE PRO ALA LEU LYS HIS LYS ILE          
SEQRES  16 B  294  GLU PRO ILE LEU LYS ALA ARG LYS GLN TYR ALA TYR GLY          
SEQRES  17 B  294  ALA GLN HIS ASP TYR PHE ASP HIS HIS ASP ILE VAL GLY          
SEQRES  18 B  294  TRP THR ARG GLU GLY ASP SER SER VAL ALA ASN SER GLY          
SEQRES  19 B  294  LEU ALA ALA LEU ILE THR ASP GLY PRO GLY GLY ALA LYS          
SEQRES  20 B  294  ARG MET TYR VAL GLY ARG GLN ASN ALA GLY GLU THR TRP          
SEQRES  21 B  294  HIS ASP ILE THR GLY ASN ARG SER GLU PRO VAL VAL ILE          
SEQRES  22 B  294  ASN SER GLU GLY TRP GLY GLU PHE HIS VAL ASN GLY GLY          
SEQRES  23 B  294  SER VAL SER ILE TYR VAL GLN ARG                              
FORMUL   3  HOH   *237(H2 O)                                                    
HELIX    1   1 HIS A   21  ASN A   27  1                                   7    
HELIX    2   2 SER A   29  GLU A   34  1                                   6    
HELIX    3   3 LYS A   80  ARG A   93  1                                  14    
HELIX    4   4 TRP A  157  HIS A  159  5                                   3    
HELIX    5   5 ASP B  194  MET B  197  5                                   4    
HELIX    6   6 PRO B  206  LEU B  223  1                                  18    
HELIX    7   7 VAL B  233  HIS B  235  5                                   3    
HELIX    8   8 PHE B  238  THR B  252  1                                  15    
HELIX    9   9 LEU B  267  LYS B  276  1                                  10    
HELIX   10  10 VAL B  286  THR B  297  1                                  12    
HELIX   11  11 MET B  304  LEU B  308  5                                   5    
HELIX   12  12 VAL B  312  LYS B  315  1                                   4    
HELIX   13  13 PRO B  317  LYS B  319  5                                   3    
HELIX   14  14 THR B  341  THR B  353  1                                  13    
HELIX   15  15 TYR B  363  TYR B  367  1                                   5    
HELIX   16  16 LYS B  381  GLN B  393  1                                  13    
HELIX   17  17 ARG B  442  ASN B  444  5                                   3    
SHEET    1   A 7 VAL B 321  PHE B 323  0                                        
SHEET    2   A 7 TYR B 358  PHE B 362  1  N  TYR B 358   O  THR B 322           
SHEET    3   A 7 LEU A   7  GLN A   9  1  N  LEU A   7   O  VAL B 361           
SHEET    4   A 7 ALA A  39  TRP A  41  1  N  ALA A  39   O  MET A   8           
SHEET    5   A 7 ASN A  96  VAL A 101  1  N  ASN A  96   O  VAL A  40           
SHEET    6   A 7 GLY B 227  LEU B 230  1  N  GLY B 227   O  GLY A  99           
SHEET    7   A 7 PHE B 257  ALA B 260  1  N  PHE B 257   O  PHE B 228           
SHEET    1   B 3 HIS A 133  ALA A 137  0                                        
SHEET    2   B 3 GLU A 113  GLU A 119 -1  N  ALA A 117   O  HIS A 133           
SHEET    3   B 3 TYR A 175  PHE A 177 -1  N  LYS A 176   O  VAL A 118           
SHEET    1   C 4 GLN B 399  TYR B 402  0                                        
SHEET    2   C 4 ILE B 408  ARG B 413 -1  N  THR B 412   O  HIS B 400           
SHEET    3   C 4 LEU B 424  THR B 429 -1  N  ILE B 428   O  VAL B 409           
SHEET    4   C 4 VAL B 477  TYR B 480 -1  N  TYR B 480   O  ALA B 425           
SHEET    1   D 2 GLY B 434  TYR B 439  0                                        
SHEET    2   D 2 TRP B 467  VAL B 472 -1  N  VAL B 472   O  GLY B 434           
SHEET    1   E 2 PHE A 160  THR A 163  0                                        
SHEET    2   E 2 ALA B 199  ILE B 201 -1  N  ASP B 200   O  ASP A 161           
SITE     1 ACT  3 ASP B 231  GLU B 261  ASP B 328                               
CRYST1  119.800  119.800   85.400  90.00  90.00  90.00 P 43 21 2     8          
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      0.008347  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008347  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011710        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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