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Database: PDB
Entry: 5BN7
LinkDB: 5BN7
Original site: 5BN7 
HEADER    HYDROLASE                               25-MAY-15   5BN7              
TITLE     CRYSTAL STRUCTURE OF MALTODEXTRIN GLUCOSIDASE FROM E.COLI AT 3.7 A    
TITLE    2 RESOLUTION                                                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MALTODEXTRIN GLUCOSIDASE;                                  
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: ALPHA-GLUCOSIDASE;                                          
COMPND   5 EC: 3.2.1.20;                                                        
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI (STRAIN K12);                  
SOURCE   3 ORGANISM_TAXID: 83333;                                               
SOURCE   4 STRAIN: K12;                                                         
SOURCE   5 GENE: MALZ, B0403, JW0393;                                           
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID                               
KEYWDS    HYDROLASE, GLUCOSIDASE                                                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    P.K.SHUKLA,A.PASTOR,A.K.SINGH,S.SHARMA,T.P.SINGH,T.K.CHAUDHURI        
REVDAT   2   13-JUL-16 5BN7    1       JRNL                                     
REVDAT   1   12-AUG-15 5BN7    0                                                
JRNL        AUTH   A.PASTOR,A.K.SINGH,P.K.SHUKLA,M.J.EQUBAL,S.T.MALIK,          
JRNL        AUTH 2 T.P.SINGH,T.K.CHAUDHURI                                      
JRNL        TITL   ROLE OF N-TERMINAL REGION OF ESCHERICHIA COLI MALTODEXTRIN   
JRNL        TITL 2 GLUCOSIDASE IN FOLDING AND FUNCTION OF THE PROTEIN           
JRNL        REF    BIOCHIM.BIOPHYS.ACTA          V.1864  1138 2016              
JRNL        REFN                   ISSN 0006-3002                               
JRNL        PMID   27317979                                                     
JRNL        DOI    10.1016/J.BBAPAP.2016.06.008                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.6.0117                                      
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) : 3.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 110.61                         
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 70.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 6156                           
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) : 0.330                           
REMARK   3   R VALUE            (WORKING SET) : 0.330                           
REMARK   3   FREE R VALUE                     : 0.344                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.600                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 300                             
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) : 3.70                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.79                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 462                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 70.47                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3330                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 20                           
REMARK   3   BIN FREE R VALUE                    : 0.4430                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3618                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 88.00                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 131.0                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 5.04000                                              
REMARK   3    B22 (A**2) : 5.04000                                              
REMARK   3    B33 (A**2) : -10.08000                                            
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): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.235         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): NULL          
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL          
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.861                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.845                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3720 ; 0.015 ; 0.020       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5059 ; 2.425 ; 1.927       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   450 ;11.001 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   197 ;35.129 ;23.756       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   570 ;22.310 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    27 ;21.883 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   522 ; 0.155 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2952 ; 0.016 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
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):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
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  TWIN DETAILS                                                        
REMARK   3   NUMBER OF TWIN DOMAINS  : 2                                        
REMARK   3      TWIN DOMAIN   : 1                                               
REMARK   3      TWIN OPERATOR : H, K, L                                         
REMARK   3      TWIN FRACTION : 0.525                                           
REMARK   3      TWIN DOMAIN   : 2                                               
REMARK   3      TWIN OPERATOR : K, H, -L                                        
REMARK   3      TWIN FRACTION : 0.475                                           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN USED IF PRESENT IN    
REMARK   3  THE INPUT                                                           
REMARK   4                                                                      
REMARK   4 5BN7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-JUN-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000210216.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 18-FEB-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 77                                 
REMARK 200  PH                             : 4.6                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : BM14                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97625                            
REMARK 200  MONOCHROMATOR                  : GRAPHITE                           
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : IMOSFLM                            
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 6156                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 110.610                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 70.4                               
REMARK 200  DATA REDUNDANCY                : 4.000                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.09700                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 2.5000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.79                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 73.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.72000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 0.120                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: 1JI1                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 59.53                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.01                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.5 M AMMONIUM ACETATE, 0.1 M SODIUM     
REMARK 280  ACETATE, PH 4.6, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 4                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -Y,X,Z                                                  
REMARK 290       4555   Y,-X,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        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     MET A    -1                                                      
REMARK 465     GLY A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     LEU A     2                                                      
REMARK 465     ASN A     3                                                      
REMARK 465     ALA A     4                                                      
REMARK 465     TRP A     5                                                      
REMARK 465     HIS A     6                                                      
REMARK 465     LEU A     7                                                      
REMARK 465     PRO A     8                                                      
REMARK 465     VAL A     9                                                      
REMARK 465     PRO A    10                                                      
REMARK 465     PRO A    11                                                      
REMARK 465     PHE A    12                                                      
REMARK 465     VAL A    13                                                      
REMARK 465     LYS A    14                                                      
REMARK 465     GLN A    15                                                      
REMARK 465     SER A    16                                                      
REMARK 465     LYS A    17                                                      
REMARK 465     ASP A    18                                                      
REMARK 465     GLN A    19                                                      
REMARK 465     LEU A    20                                                      
REMARK 465     LEU A    21                                                      
REMARK 465     ILE A    22                                                      
REMARK 465     THR A    23                                                      
REMARK 465     LEU A    24                                                      
REMARK 465     TRP A    25                                                      
REMARK 465     LEU A    26                                                      
REMARK 465     THR A    27                                                      
REMARK 465     GLY A    28                                                      
REMARK 465     GLU A    29                                                      
REMARK 465     ASP A    30                                                      
REMARK 465     PRO A    31                                                      
REMARK 465     PRO A    32                                                      
REMARK 465     GLN A    33                                                      
REMARK 465     ARG A    34                                                      
REMARK 465     ILE A    35                                                      
REMARK 465     MET A    36                                                      
REMARK 465     LEU A    37                                                      
REMARK 465     ARG A    38                                                      
REMARK 465     THR A    39                                                      
REMARK 465     GLU A    40                                                      
REMARK 465     HIS A    41                                                      
REMARK 465     ASP A    42                                                      
REMARK 465     ASN A    43                                                      
REMARK 465     GLU A    44                                                      
REMARK 465     GLU A    45                                                      
REMARK 465     MET A    46                                                      
REMARK 465     SER A    47                                                      
REMARK 465     VAL A    48                                                      
REMARK 465     PRO A    49                                                      
REMARK 465     MET A    50                                                      
REMARK 465     HIS A    51                                                      
REMARK 465     LYS A    52                                                      
REMARK 465     GLN A    53                                                      
REMARK 465     ARG A    54                                                      
REMARK 465     SER A    55                                                      
REMARK 465     GLN A    56                                                      
REMARK 465     PRO A    57                                                      
REMARK 465     GLN A    58                                                      
REMARK 465     PRO A    59                                                      
REMARK 465     GLY A    60                                                      
REMARK 465     VAL A    61                                                      
REMARK 465     THR A    62                                                      
REMARK 465     ALA A    63                                                      
REMARK 465     TRP A    64                                                      
REMARK 465     ARG A    65                                                      
REMARK 465     ALA A    66                                                      
REMARK 465     ALA A    67                                                      
REMARK 465     ILE A    68                                                      
REMARK 465     ASP A    69                                                      
REMARK 465     LEU A    70                                                      
REMARK 465     SER A    71                                                      
REMARK 465     SER A    72                                                      
REMARK 465     GLY A    73                                                      
REMARK 465     GLN A    74                                                      
REMARK 465     PRO A    75                                                      
REMARK 465     ARG A    76                                                      
REMARK 465     ARG A    77                                                      
REMARK 465     ARG A    78                                                      
REMARK 465     TYR A    79                                                      
REMARK 465     SER A    80                                                      
REMARK 465     PHE A    81                                                      
REMARK 465     LYS A    82                                                      
REMARK 465     LEU A    83                                                      
REMARK 465     LEU A    84                                                      
REMARK 465     TRP A    85                                                      
REMARK 465     HIS A    86                                                      
REMARK 465     ASP A    87                                                      
REMARK 465     ARG A    88                                                      
REMARK 465     GLN A    89                                                      
REMARK 465     ARG A    90                                                      
REMARK 465     TRP A    91                                                      
REMARK 465     PHE A    92                                                      
REMARK 465     THR A    93                                                      
REMARK 465     PRO A    94                                                      
REMARK 465     GLN A    95                                                      
REMARK 465     GLY A    96                                                      
REMARK 465     PHE A    97                                                      
REMARK 465     SER A    98                                                      
REMARK 465     ARG A    99                                                      
REMARK 465     MET A   100                                                      
REMARK 465     PRO A   101                                                      
REMARK 465     PRO A   102                                                      
REMARK 465     ALA A   103                                                      
REMARK 465     ARG A   104                                                      
REMARK 465     LEU A   105                                                      
REMARK 465     GLU A   106                                                      
REMARK 465     GLN A   107                                                      
REMARK 465     PHE A   108                                                      
REMARK 465     ALA A   109                                                      
REMARK 465     VAL A   110                                                      
REMARK 465     ASP A   111                                                      
REMARK 465     VAL A   112                                                      
REMARK 465     PRO A   113                                                      
REMARK 465     ASP A   114                                                      
REMARK 465     ILE A   115                                                      
REMARK 465     GLY A   116                                                      
REMARK 465     PRO A   117                                                      
REMARK 465     GLN A   118                                                      
REMARK 465     TRP A   119                                                      
REMARK 465     ALA A   120                                                      
REMARK 465     ALA A   121                                                      
REMARK 465     ASP A   122                                                      
REMARK 465     GLN A   123                                                      
REMARK 465     ILE A   124                                                      
REMARK 465     PHE A   125                                                      
REMARK 465     TYR A   126                                                      
REMARK 465     GLN A   127                                                      
REMARK 465     ILE A   128                                                      
REMARK 465     PHE A   129                                                      
REMARK 465     PRO A   130                                                      
REMARK 465     GLN A   238                                                      
REMARK 465     LEU A   239                                                      
REMARK 465     GLY A   240                                                      
REMARK 465     MET A   241                                                      
REMARK 465     ARG A   242                                                      
REMARK 465     GLN A   419                                                      
REMARK 465     THR A   420                                                      
REMARK 465     CYS A   421                                                      
REMARK 465     MET A   422                                                      
REMARK 465     ALA A   423                                                      
REMARK 465     TRP A   424                                                      
REMARK 465     MET A   425                                                      
REMARK 465     ASP A   426                                                      
REMARK 465     ASN A   427                                                      
REMARK 465     TYR A   428                                                      
REMARK 465     ARG A   429                                                      
REMARK 465     ALA A   430                                                      
REMARK 465     VAL A   601                                                      
REMARK 465     TRP A   602                                                      
REMARK 465     MET A   603                                                      
REMARK 465     ASN A   604                                                      
REMARK 465     GLY A   605                                                      
REMARK 465     SER A   606                                                      
REMARK 465     ARG A   607                                                      
REMARK 465     SER A   608                                                      
REMARK 465     HIS A   609                                                      
REMARK 465     HIS A   610                                                      
REMARK 465     HIS A   611                                                      
REMARK 465     HIS A   612                                                      
REMARK 465     HIS A   613                                                      
REMARK 465     HIS A   614                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    HIS A 149   CG    HIS A 149   CD2     0.059                       
REMARK 500    GLY A 342   N     GLY A 342   CA     -0.090                       
REMARK 500    TRP A 401   CE2   TRP A 401   CD2     0.073                       
REMARK 500    TRP A 401   C     TRP A 401   O      -0.175                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    GLU A 184   CB  -  CA  -  C   ANGL. DEV. = -12.6 DEGREES          
REMARK 500    LYS A 185   CB  -  CA  -  C   ANGL. DEV. = -22.2 DEGREES          
REMARK 500    LEU A 290   N   -  CA  -  C   ANGL. DEV. =  17.1 DEGREES          
REMARK 500    LEU A 341   CA  -  C   -  N   ANGL. DEV. = -23.5 DEGREES          
REMARK 500    LEU A 341   O   -  C   -  N   ANGL. DEV. =  12.2 DEGREES          
REMARK 500    ALA A 378   CB  -  CA  -  C   ANGL. DEV. = -15.1 DEGREES          
REMARK 500    GLU A 387   CB  -  CA  -  C   ANGL. DEV. =  16.5 DEGREES          
REMARK 500    PRO A 413   C   -  N   -  CA  ANGL. DEV. =  11.0 DEGREES          
REMARK 500    MET A 440   CB  -  CA  -  C   ANGL. DEV. = -14.9 DEGREES          
REMARK 500    ASN A 442   CB  -  CA  -  C   ANGL. DEV. = -17.2 DEGREES          
REMARK 500    LEU A 463   CB  -  CA  -  C   ANGL. DEV. = -14.3 DEGREES          
REMARK 500    TRP A 501   CB  -  CA  -  C   ANGL. DEV. =  17.9 DEGREES          
REMARK 500    LYS A 522   CB  -  CA  -  C   ANGL. DEV. = -12.4 DEGREES          
REMARK 500    LEU A 592   N   -  CA  -  CB  ANGL. DEV. =  16.9 DEGREES          
REMARK 500    PRO A 595   C   -  N   -  CD  ANGL. DEV. = -21.8 DEGREES          
REMARK 500    ALA A 596   N   -  CA  -  CB  ANGL. DEV. =  -9.4 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ALA A 134      141.92   -170.78                                   
REMARK 500    HIS A 145        7.78     83.09                                   
REMARK 500    TYR A 147     -168.45   -168.82                                   
REMARK 500    ALA A 169      139.16    -34.85                                   
REMARK 500    THR A 173     -108.67   -156.69                                   
REMARK 500    PHE A 174       73.34     71.72                                   
REMARK 500    TYR A 175      -83.98   -109.61                                   
REMARK 500    LYS A 210       38.30     74.11                                   
REMARK 500    GLU A 214      -65.20   -107.95                                   
REMARK 500    TYR A 216      -71.06    -96.24                                   
REMARK 500    HIS A 256      154.98    -47.78                                   
REMARK 500    TRP A 258      -42.10   -130.58                                   
REMARK 500    HIS A 262       -4.43     83.98                                   
REMARK 500    PRO A 273       57.52   -100.77                                   
REMARK 500    GLU A 274       88.01   -165.12                                   
REMARK 500    PHE A 283     -126.27     53.80                                   
REMARK 500    ALA A 289     -151.61   -174.77                                   
REMARK 500    ASP A 291      -71.37    -56.37                                   
REMARK 500    SER A 307      -79.20   -134.47                                   
REMARK 500    VAL A 309       12.15     82.58                                   
REMARK 500    ILE A 312      -65.41    -95.37                                   
REMARK 500    TYR A 313      -55.70   -123.27                                   
REMARK 500    SER A 318      140.80    -38.58                                   
REMARK 500    TRP A 328      -13.96    171.33                                   
REMARK 500    ASN A 329      134.73    -37.27                                   
REMARK 500    HIS A 339       -9.88    -54.49                                   
REMARK 500    LEU A 341      161.20    -35.64                                   
REMARK 500    ALA A 344       22.08     82.74                                   
REMARK 500    ASP A 377      133.29    -39.57                                   
REMARK 500    ARG A 379      -54.66   -176.74                                   
REMARK 500    GLN A 383       11.70   -154.25                                   
REMARK 500    ALA A 384      -50.85     67.96                                   
REMARK 500    PRO A 399      -71.35    -59.72                                   
REMARK 500    LEU A 404      -50.27   -125.03                                   
REMARK 500    ASN A 406        2.94     54.69                                   
REMARK 500    THR A 407     -173.15   -178.26                                   
REMARK 500    TYR A 411       32.61     86.13                                   
REMARK 500    PRO A 413      141.28    -33.37                                   
REMARK 500    LEU A 444      -79.27   -113.88                                   
REMARK 500    LYS A 490      -70.99    -56.57                                   
REMARK 500    PRO A 493       35.84    -89.37                                   
REMARK 500    PRO A 498      142.42    -39.13                                   
REMARK 500    PRO A 500     -153.62    -92.06                                   
REMARK 500    TRP A 501      -61.24   -137.46                                   
REMARK 500    GLN A 506        0.53     85.65                                   
REMARK 500    THR A 508      104.44    -55.56                                   
REMARK 500    ALA A 509       -8.70    -59.47                                   
REMARK 500    LEU A 513      -84.59   -122.21                                   
REMARK 500    ARG A 528      -72.55   -120.36                                   
REMARK 500    CYS A 532      108.81     79.39                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      57 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 GLY A  171     SER A  172                  143.26                    
REMARK 500 LYS A  204     ALA A  205                  149.80                    
REMARK 500 PHE A  259     ASP A  260                  143.29                    
REMARK 500 PHE A  283     SER A  284                  -99.26                    
REMARK 500 SER A  284     ASP A  285                  144.96                    
REMARK 500 TRP A  501     GLN A  502                 -142.60                    
REMARK 500 GLN A  506     ASP A  507                  149.78                    
REMARK 500 LYS A  522     LYS A  523                  149.21                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    ARG A 451         0.08    SIDE CHAIN                              
REMARK 500    ARG A 546         0.26    SIDE CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1JI1   RELATED DB: PDB                                   
REMARK 900 MODEL PDB                                                            
DBREF  5BN7 A    1   604  UNP    P21517   MALZ_ECOLI       1    604             
SEQADV 5BN7 MET A   -1  UNP  P21517              EXPRESSION TAG                 
SEQADV 5BN7 GLY A    0  UNP  P21517              EXPRESSION TAG                 
SEQADV 5BN7 GLY A  605  UNP  P21517              EXPRESSION TAG                 
SEQADV 5BN7 SER A  606  UNP  P21517              EXPRESSION TAG                 
SEQADV 5BN7 ARG A  607  UNP  P21517              EXPRESSION TAG                 
SEQADV 5BN7 SER A  608  UNP  P21517              EXPRESSION TAG                 
SEQADV 5BN7 HIS A  609  UNP  P21517              EXPRESSION TAG                 
SEQADV 5BN7 HIS A  610  UNP  P21517              EXPRESSION TAG                 
SEQADV 5BN7 HIS A  611  UNP  P21517              EXPRESSION TAG                 
SEQADV 5BN7 HIS A  612  UNP  P21517              EXPRESSION TAG                 
SEQADV 5BN7 HIS A  613  UNP  P21517              EXPRESSION TAG                 
SEQADV 5BN7 HIS A  614  UNP  P21517              EXPRESSION TAG                 
SEQRES   1 A  616  MET GLY MET LEU ASN ALA TRP HIS LEU PRO VAL PRO PRO          
SEQRES   2 A  616  PHE VAL LYS GLN SER LYS ASP GLN LEU LEU ILE THR LEU          
SEQRES   3 A  616  TRP LEU THR GLY GLU ASP PRO PRO GLN ARG ILE MET LEU          
SEQRES   4 A  616  ARG THR GLU HIS ASP ASN GLU GLU MET SER VAL PRO MET          
SEQRES   5 A  616  HIS LYS GLN ARG SER GLN PRO GLN PRO GLY VAL THR ALA          
SEQRES   6 A  616  TRP ARG ALA ALA ILE ASP LEU SER SER GLY GLN PRO ARG          
SEQRES   7 A  616  ARG ARG TYR SER PHE LYS LEU LEU TRP HIS ASP ARG GLN          
SEQRES   8 A  616  ARG TRP PHE THR PRO GLN GLY PHE SER ARG MET PRO PRO          
SEQRES   9 A  616  ALA ARG LEU GLU GLN PHE ALA VAL ASP VAL PRO ASP ILE          
SEQRES  10 A  616  GLY PRO GLN TRP ALA ALA ASP GLN ILE PHE TYR GLN ILE          
SEQRES  11 A  616  PHE PRO ASP ARG PHE ALA ARG SER LEU PRO ARG GLU ALA          
SEQRES  12 A  616  GLU GLN ASP HIS VAL TYR TYR HIS HIS ALA ALA GLY GLN          
SEQRES  13 A  616  GLU ILE ILE LEU ARG ASP TRP ASP GLU PRO VAL THR ALA          
SEQRES  14 A  616  GLN ALA GLY GLY SER THR PHE TYR GLY GLY ASP LEU ASP          
SEQRES  15 A  616  GLY ILE SER GLU LYS LEU PRO TYR LEU LYS LYS LEU GLY          
SEQRES  16 A  616  VAL THR ALA LEU TYR LEU ASN PRO VAL PHE LYS ALA PRO          
SEQRES  17 A  616  SER VAL HIS LYS TYR ASP THR GLU ASP TYR ARG HIS VAL          
SEQRES  18 A  616  ASP PRO GLN PHE GLY GLY ASP GLY ALA LEU LEU ARG LEU          
SEQRES  19 A  616  ARG HIS ASN THR GLN GLN LEU GLY MET ARG LEU VAL LEU          
SEQRES  20 A  616  ASP GLY VAL PHE ASN HIS SER GLY ASP SER HIS ALA TRP          
SEQRES  21 A  616  PHE ASP ARG HIS ASN ARG GLY THR GLY GLY ALA CYS HIS          
SEQRES  22 A  616  ASN PRO GLU SER PRO TRP ARG ASP TRP TYR SER PHE SER          
SEQRES  23 A  616  ASP ASP GLY THR ALA LEU ASP TRP LEU GLY TYR ALA SER          
SEQRES  24 A  616  LEU PRO LYS LEU ASP TYR GLN SER GLU SER LEU VAL ASN          
SEQRES  25 A  616  GLU ILE TYR ARG GLY GLU ASP SER ILE VAL ARG HIS TRP          
SEQRES  26 A  616  LEU LYS ALA PRO TRP ASN MET ASP GLY TRP ARG LEU ASP          
SEQRES  27 A  616  VAL VAL HIS MET LEU GLY GLU ALA GLY GLY ALA ARG ASN          
SEQRES  28 A  616  ASN MET GLN HIS VAL ALA GLY ILE THR GLU ALA ALA LYS          
SEQRES  29 A  616  GLU THR GLN PRO GLU ALA TYR ILE VAL GLY GLU HIS PHE          
SEQRES  30 A  616  GLY ASP ALA ARG GLN TRP LEU GLN ALA ASP VAL GLU ASP          
SEQRES  31 A  616  ALA ALA MET ASN TYR ARG GLY PHE THR PHE PRO LEU TRP          
SEQRES  32 A  616  GLY PHE LEU ALA ASN THR ASP ILE SER TYR ASP PRO GLN          
SEQRES  33 A  616  GLN ILE ASP ALA GLN THR CYS MET ALA TRP MET ASP ASN          
SEQRES  34 A  616  TYR ARG ALA GLY LEU SER HIS GLN GLN GLN LEU ARG MET          
SEQRES  35 A  616  PHE ASN GLN LEU ASP SER HIS ASP THR ALA ARG PHE LYS          
SEQRES  36 A  616  THR LEU LEU GLY ARG ASP ILE ALA ARG LEU PRO LEU ALA          
SEQRES  37 A  616  VAL VAL TRP LEU PHE THR TRP PRO GLY VAL PRO CYS ILE          
SEQRES  38 A  616  TYR TYR GLY ASP GLU VAL GLY LEU ASP GLY LYS ASN ASP          
SEQRES  39 A  616  PRO PHE CYS ARG LYS PRO PHE PRO TRP GLN VAL GLU LYS          
SEQRES  40 A  616  GLN ASP THR ALA LEU PHE ALA LEU TYR GLN ARG MET ILE          
SEQRES  41 A  616  ALA LEU ARG LYS LYS SER GLN ALA LEU ARG HIS GLY GLY          
SEQRES  42 A  616  CYS GLN VAL LEU TYR ALA GLU ASP ASN VAL VAL VAL PHE          
SEQRES  43 A  616  VAL ARG VAL LEU ASN GLN GLN ARG VAL LEU VAL ALA ILE          
SEQRES  44 A  616  ASN ARG GLY GLU ALA CYS GLU VAL VAL LEU PRO ALA SER          
SEQRES  45 A  616  PRO PHE LEU ASN ALA VAL GLN TRP GLN CYS LYS GLU GLY          
SEQRES  46 A  616  HIS GLY GLN LEU THR ASP GLY ILE LEU ALA LEU PRO ALA          
SEQRES  47 A  616  ILE SER ALA THR VAL TRP MET ASN GLY SER ARG SER HIS          
SEQRES  48 A  616  HIS HIS HIS HIS HIS                                          
HELIX    1 AA1 LEU A  179  GLU A  184  1                                   6    
HELIX    2 AA2 ARG A  231  THR A  236  1                                   6    
HELIX    3 AA3 ALA A  347  GLN A  365  1                                  19    
HELIX    4 AA4 PRO A  399  LEU A  404  5                                   6    
HELIX    5 AA5 SER A  433  LEU A  438  1                                   6    
HELIX    6 AA6 ARG A  451  LEU A  456  1                                   6    
HELIX    7 AA7 ALA A  461  TRP A  469  1                                   9    
HELIX    8 AA8 LEU A  513  ARG A  521  1                                   9    
SHEET    1 AA1 2 PHE A 441  ASN A 442  0                                        
SHEET    2 AA1 2 VAL A 476  PRO A 477  1  O  VAL A 476   N  ASN A 442           
SHEET    1 AA2 2 ALA A 537  GLU A 538  0                                        
SHEET    2 AA2 2 VAL A 541  VAL A 542 -1  O  VAL A 541   N  GLU A 538           
SHEET    1 AA3 2 CYS A 580  LYS A 581  0                                        
SHEET    2 AA3 2 GLN A 586  LEU A 587 -1  O  GLN A 586   N  LYS A 581           
CISPEP   1 ALA A  151    ALA A  152          0        -6.87                     
CISPEP   2 ALA A  152    GLY A  153          0        -5.75                     
CISPEP   3 SER A  172    THR A  173          0         0.81                     
CISPEP   4 LYS A  191    LEU A  192          0         6.41                     
CISPEP   5 SER A  305    GLU A  306          0         1.58                     
CISPEP   6 ALA A  326    PRO A  327          0       -10.65                     
CISPEP   7 ASP A  492    PRO A  493          0        -2.35                     
CISPEP   8 HIS A  584    GLY A  585          0        -3.46                     
CRYST1  110.590  110.590   69.540  90.00  90.00  90.00 P 4           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      0.009042  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009042  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.014380        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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