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Database: PDB
Entry: 3MYW
LinkDB: 3MYW
Original site: 3MYW 
HEADER    HYDROLASE/HYDROLASE INHIBITOR           11-MAY-10   3MYW              
TITLE     THE BOWMAN-BIRK TYPE INHIBITOR FROM MUNG BEAN IN TERNARY COMPLEX WITH 
TITLE    2 PORCINE TRYPSIN                                                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TRYPSIN;                                                   
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 EC: 3.4.21.4;                                                        
COMPND   5 MOL_ID: 2;                                                           
COMPND   6 MOLECULE: BOWMAN-BIRK TYPE TRYPSIN INHIBITOR;                        
COMPND   7 CHAIN: I                                                             
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SUS SCROFA;                                     
SOURCE   3 ORGANISM_COMMON: PIGS,SWINE,WILD BOAR;                               
SOURCE   4 ORGANISM_TAXID: 9823;                                                
SOURCE   5 MOL_ID: 2;                                                           
SOURCE   6 ORGANISM_SCIENTIFIC: VIGNA RADIATA VAR. RADIATA;                     
SOURCE   7 ORGANISM_COMMON: GOLDEN GRAM,GREEN GRAM;                             
SOURCE   8 ORGANISM_TAXID: 3916                                                 
KEYWDS    SERINE PROTEINASE, BOWMAN-BIRK-TYPE INHIBITOR, HYDROLASE-HYDROLASE    
KEYWDS   2 INHIBITOR COMPLEX                                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    R.A.ENGH,W.BODE,R.HUBER,G.LIN,C.CHI                                   
REVDAT   1   29-DEC-10 3MYW    0                                                
JRNL        AUTH   G.LIN,W.BODE,R.HUBER,C.CHI,R.A.ENGH                          
JRNL        TITL   THE 0.25-NM X-RAY STRUCTURE OF THE BOWMAN-BIRK-TYPE          
JRNL        TITL 2 INHIBITOR FROM MUNG BEAN IN TERNARY COMPLEX WITH PORCINE     
JRNL        TITL 3 TRYPSIN.                                                     
JRNL        REF    EUR.J.BIOCHEM.                V. 212   549 1993              
JRNL        REFN                   ISSN 0014-2956                               
JRNL        PMID   8444191                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR                                               
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 8.00                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 10516                          
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) : 0.179                           
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            : 3689                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 2                                       
REMARK   3   SOLVENT ATOMS            : 262                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
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) : NULL                            
REMARK   3   BOND ANGLES            (DEGREES) : NULL                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3MYW COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-JUL-10.                  
REMARK 100 THE RCSB ID CODE IS RCSB059167.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 16-JUL-90                          
REMARK 200  TEMPERATURE           (KELVIN) : 283                                
REMARK 200  PH                             : 5                                  
REMARK 200  NUMBER OF CRYSTALS USED        : 2                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU RU200                       
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54                               
REMARK 200  MONOCHROMATOR                  : GRAPHITE                           
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : AREA DETECTOR                      
REMARK 200  DETECTOR MANUFACTURER          : ENRAF-NONIUS FAST                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : PROTEIN                            
REMARK 200  DATA SCALING SOFTWARE          : PROTEIN                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 10516                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 8.000                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 77.5                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
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) : 2.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.61                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 35.0                               
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: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PROTEIN                                               
REMARK 200 STARTING MODEL: PDB ENTRY 3PDB                                       
REMARK 200                                                                      
REMARK 200 REMARK: THE AUTHORS ORIGINALLY SOLVED THIS STRUCTURE IN SPACE        
REMARK 200  GROUP P 31 2 1 RELYING ON THE INTERNAL SYMMETRY OF THE INHIBITOR.   
REMARK 200  IN ORDER TO PROCESS THIS ENTRY, THE SPACE GROUP SYMMETRY WAS        
REMARK 200  REDUCED TO P 31 AND THE OCCUPANCIES DOUBLED.                        
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 62.52                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.28                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.5M AMMONIUM SULFATE, 0.2M SODIUM       
REMARK 280  POTASSIUM PHOSPHATE, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE     
REMARK 280  293K                                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       53.33667            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      106.67333            
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: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3430 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 19450 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -34.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, I, 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 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     SER I     1                                                      
REMARK 465     HIS I     2                                                      
REMARK 465     ASP I     3                                                      
REMARK 465     GLU I     4                                                      
REMARK 465     PRO I     5                                                      
REMARK 465     SER I     6                                                      
REMARK 465     GLU I     7                                                      
REMARK 465     SER I     8                                                      
REMARK 465     SER I     9                                                      
REMARK 465     GLU I    10                                                      
REMARK 465     PRO I    11                                                      
REMARK 465     GLU I    67                                                      
REMARK 465     SER I    68                                                      
REMARK 465     MET I    69                                                      
REMARK 465     ASP I    70                                                      
REMARK 465     LYS I    71                                                      
REMARK 465     ASP I    72                                                      
REMARK 475                                                                      
REMARK 475 ZERO OCCUPANCY RESIDUES                                              
REMARK 475 THE FOLLOWING RESIDUES WERE MODELED WITH ZERO OCCUPANCY.             
REMARK 475 THE LOCATION AND PROPERTIES OF THESE RESIDUES MAY NOT                
REMARK 475 BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;                      
REMARK 475 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE)          
REMARK 475   M RES C SSEQI                                                      
REMARK 475     ILE A   63                                                       
REMARK 475     GLN A   64                                                       
REMARK 475     VAL A   65                                                       
REMARK 475     ARG A   66                                                       
REMARK 475     CYS I   12                                                       
REMARK 475     TYR I   63                                                       
REMARK 475     LYS I   64                                                       
REMARK 475     PRO I   65                                                       
REMARK 475     CYS I   66                                                       
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   C    LYS I    20     OG   SER B   195              1.71            
REMARK 500   O    LYS I    20     OG   SER B   195              2.08            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   OH   TYR A    59     O    HOH B   465     2665     2.09            
REMARK 500   O    HOH A   309     OH   TYR B    59     2775     2.13            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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  57   NE2   HIS A  57   CD2    -0.070                       
REMARK 500    HIS A  71   NE2   HIS A  71   CD2    -0.075                       
REMARK 500    VAL A 213   CA    VAL A 213   CB      0.136                       
REMARK 500    TRP A 237   CG    TRP A 237   CD2    -0.105                       
REMARK 500    ARG I  47   C     ARG I  47   O       0.155                       
REMARK 500    HIS B  57   NE2   HIS B  57   CD2    -0.068                       
REMARK 500    VAL B 213   CA    VAL B 213   CB      0.132                       
REMARK 500    TRP B 237   CG    TRP B 237   CD2    -0.106                       
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    TRP A  51   CD1 -  CG  -  CD2 ANGL. DEV. =   5.9 DEGREES          
REMARK 500    TRP A  51   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.0 DEGREES          
REMARK 500    ARG A 117   NE  -  CZ  -  NH2 ANGL. DEV. =   3.1 DEGREES          
REMARK 500    TRP A 141   CD1 -  CG  -  CD2 ANGL. DEV. =   7.3 DEGREES          
REMARK 500    TRP A 141   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.3 DEGREES          
REMARK 500    TRP A 215   CD1 -  CG  -  CD2 ANGL. DEV. =   6.5 DEGREES          
REMARK 500    TRP A 215   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.7 DEGREES          
REMARK 500    TRP A 237   CD1 -  CG  -  CD2 ANGL. DEV. =   7.5 DEGREES          
REMARK 500    TRP A 237   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.0 DEGREES          
REMARK 500    TRP B  51   CD1 -  CG  -  CD2 ANGL. DEV. =   5.8 DEGREES          
REMARK 500    TRP B  51   CE2 -  CD2 -  CG  ANGL. DEV. =  -4.9 DEGREES          
REMARK 500    ARG B 117   NE  -  CZ  -  NH2 ANGL. DEV. =   3.1 DEGREES          
REMARK 500    TRP B 141   CD1 -  CG  -  CD2 ANGL. DEV. =   7.3 DEGREES          
REMARK 500    TRP B 141   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.4 DEGREES          
REMARK 500    TRP B 215   CD1 -  CG  -  CD2 ANGL. DEV. =   6.7 DEGREES          
REMARK 500    TRP B 215   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.9 DEGREES          
REMARK 500    TRP B 237   CD1 -  CG  -  CD2 ANGL. DEV. =   7.5 DEGREES          
REMARK 500    TRP B 237   CE2 -  CD2 -  CG  ANGL. DEV. =  -4.9 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  23      141.87     76.42                                   
REMARK 500    SER A  54     -155.63   -138.03                                   
REMARK 500    ARG A  62      102.25     67.81                                   
REMARK 500    HIS A  71      -71.50   -138.45                                   
REMARK 500    LEU A  99       25.82     49.99                                   
REMARK 500    ASN A 115     -156.19   -142.45                                   
REMARK 500    ASN A 143      150.60    -41.81                                   
REMARK 500    ASN A 202       22.64     45.30                                   
REMARK 500    SER A 214      -75.00   -119.11                                   
REMARK 500    LYS I  20       69.97   -107.79                                   
REMARK 500    ASN I  34      -21.02     64.43                                   
REMARK 500    CYS I  36     -108.93   -109.51                                   
REMARK 500    CYS I  40      126.88    178.56                                   
REMARK 500    ARG I  47       63.66   -109.34                                   
REMARK 500    PHE I  61      166.28    144.96                                   
REMARK 500    TYR I  63      -83.37   -142.15                                   
REMARK 500    PRO I  65      100.69      0.94                                   
REMARK 500    ALA B  23      141.80     76.60                                   
REMARK 500    SER B  54     -155.73   -138.05                                   
REMARK 500    ARG B  62      102.01     67.77                                   
REMARK 500    HIS B  71      -73.33   -124.86                                   
REMARK 500    ASN B 115     -156.23   -142.46                                   
REMARK 500    ASN B 202       22.72     45.39                                   
REMARK 500    SER B 214      -75.84   -127.73                                   
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 LYS I   64     PRO I   65                   57.36                    
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    TYR B 172         0.07    SIDE CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY                                       
REMARK 500                                                                      
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY                       
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER                 
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;                     
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;                            
REMARK 500 I=INSERTION CODE).                                                   
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        ANGLE                                           
REMARK 500    LYS I  20        -22.86                                           
REMARK 500    ARG I  47        -29.95                                           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 299  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 VAL A  75   O                                                      
REMARK 620 2 ASN A  72   O    90.0                                              
REMARK 620 3 GLU A  70   OE1 157.2  88.8                                        
REMARK 620 4 GLU A  80   OE2  98.5 157.5  91.2                                  
REMARK 620 5 HOH A 425   O    93.8 107.8  65.1  92.5                            
REMARK 620 6 HOH A 428   O   129.0  92.5  73.8  66.0 133.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B 246  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 VAL B  75   O                                                      
REMARK 620 2 ASN B  72   O    90.1                                              
REMARK 620 3 GLU B  70   OE1 156.9  89.4                                        
REMARK 620 4 GLU B  80   OE2  97.8 158.0  91.1                                  
REMARK 620 5 HOH B 508   O    93.4 108.4  65.0  91.6                            
REMARK 620 6 HOH B 510   O   129.1  93.7  74.0  65.5 132.4                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 299                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 246                  
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 THE SEQUENCES IN THIS ENTRY REFLECT THE BELIEVED SEQUENCES AT THE    
REMARK 999 TIME THE WORK WAS PERFORMED.                                         
DBREF  3MYW A   16   245  UNP    P00761   TRYP_PIG         9    231             
DBREF  3MYW I    1    72  UNP    P01062   IBB_PHAAU        1     72             
DBREF  3MYW B   16   245  UNP    P00761   TRYP_PIG         9    231             
SEQADV 3MYW VAL A   27  UNP  P00761    ILE    20 VARIANT                        
SEQADV 3MYW ALA A  171  UNP  P00761    SER   159 SEE REMARK 999                 
SEQADV 3MYW LYS I   22  UNP  P01062    ILE    22 SEE REMARK 999                 
SEQADV 3MYW GLN I   25  UNP  P01062    GLU    25 SEE REMARK 999                 
SEQADV 3MYW VAL B   27  UNP  P00761    ILE    20 VARIANT                        
SEQADV 3MYW ALA B  171  UNP  P00761    SER   159 SEE REMARK 999                 
SEQRES   1 A  223  ILE VAL GLY GLY TYR THR CYS ALA ALA ASN SER VAL PRO          
SEQRES   2 A  223  TYR GLN VAL SER LEU ASN SER GLY SER HIS PHE CYS GLY          
SEQRES   3 A  223  GLY SER LEU ILE ASN SER GLN TRP VAL VAL SER ALA ALA          
SEQRES   4 A  223  HIS CYS TYR LYS SER ARG ILE GLN VAL ARG LEU GLY GLU          
SEQRES   5 A  223  HIS ASN ILE ASP VAL LEU GLU GLY ASN GLU GLN PHE ILE          
SEQRES   6 A  223  ASN ALA ALA LYS ILE ILE THR HIS PRO ASN PHE ASN GLY          
SEQRES   7 A  223  ASN THR LEU ASP ASN ASP ILE MET LEU ILE LYS LEU SER          
SEQRES   8 A  223  SER PRO ALA THR LEU ASN SER ARG VAL ALA THR VAL SER          
SEQRES   9 A  223  LEU PRO ARG SER CYS ALA ALA ALA GLY THR GLU CYS LEU          
SEQRES  10 A  223  ILE SER GLY TRP GLY ASN THR LYS SER SER GLY SER SER          
SEQRES  11 A  223  TYR PRO SER LEU LEU GLN CYS LEU LYS ALA PRO VAL LEU          
SEQRES  12 A  223  SER ASP SER SER CYS LYS SER ALA TYR PRO GLY GLN ILE          
SEQRES  13 A  223  THR GLY ASN MET ILE CYS VAL GLY PHE LEU GLU GLY GLY          
SEQRES  14 A  223  LYS ASP SER CYS GLN GLY ASP SER GLY GLY PRO VAL VAL          
SEQRES  15 A  223  CYS ASN GLY GLN LEU GLN GLY ILE VAL SER TRP GLY TYR          
SEQRES  16 A  223  GLY CYS ALA GLN LYS ASN LYS PRO GLY VAL TYR THR LYS          
SEQRES  17 A  223  VAL CYS ASN TYR VAL ASN TRP ILE GLN GLN THR ILE ALA          
SEQRES  18 A  223  ALA ASN                                                      
SEQRES   1 I   72  SER HIS ASP GLU PRO SER GLU SER SER GLU PRO CYS CYS          
SEQRES   2 I   72  ASP SER CYS ASP CYS THR LYS SER LYS PRO PRO GLN CYS          
SEQRES   3 I   72  HIS CYS ALA ASN ILE ARG LEU ASN SER CYS HIS SER ALA          
SEQRES   4 I   72  CYS LYS SER CYS ILE CYS THR ARG SER MET PRO GLY LYS          
SEQRES   5 I   72  CYS ARG CYS LEU ASP THR ASP ASP PHE CYS TYR LYS PRO          
SEQRES   6 I   72  CYS GLU SER MET ASP LYS ASP                                  
SEQRES   1 B  223  ILE VAL GLY GLY TYR THR CYS ALA ALA ASN SER VAL PRO          
SEQRES   2 B  223  TYR GLN VAL SER LEU ASN SER GLY SER HIS PHE CYS GLY          
SEQRES   3 B  223  GLY SER LEU ILE ASN SER GLN TRP VAL VAL SER ALA ALA          
SEQRES   4 B  223  HIS CYS TYR LYS SER ARG ILE GLN VAL ARG LEU GLY GLU          
SEQRES   5 B  223  HIS ASN ILE ASP VAL LEU GLU GLY ASN GLU GLN PHE ILE          
SEQRES   6 B  223  ASN ALA ALA LYS ILE ILE THR HIS PRO ASN PHE ASN GLY          
SEQRES   7 B  223  ASN THR LEU ASP ASN ASP ILE MET LEU ILE LYS LEU SER          
SEQRES   8 B  223  SER PRO ALA THR LEU ASN SER ARG VAL ALA THR VAL SER          
SEQRES   9 B  223  LEU PRO ARG SER CYS ALA ALA ALA GLY THR GLU CYS LEU          
SEQRES  10 B  223  ILE SER GLY TRP GLY ASN THR LYS SER SER GLY SER SER          
SEQRES  11 B  223  TYR PRO SER LEU LEU GLN CYS LEU LYS ALA PRO VAL LEU          
SEQRES  12 B  223  SER ASP SER SER CYS LYS SER ALA TYR PRO GLY GLN ILE          
SEQRES  13 B  223  THR GLY ASN MET ILE CYS VAL GLY PHE LEU GLU GLY GLY          
SEQRES  14 B  223  LYS ASP SER CYS GLN GLY ASP SER GLY GLY PRO VAL VAL          
SEQRES  15 B  223  CYS ASN GLY GLN LEU GLN GLY ILE VAL SER TRP GLY TYR          
SEQRES  16 B  223  GLY CYS ALA GLN LYS ASN LYS PRO GLY VAL TYR THR LYS          
SEQRES  17 B  223  VAL CYS ASN TYR VAL ASN TRP ILE GLN GLN THR ILE ALA          
SEQRES  18 B  223  ALA ASN                                                      
HET     CA  A 299       1                                                       
HET     CA  B 246       1                                                       
HETNAM      CA CALCIUM ION                                                      
FORMUL   4   CA    2(CA 2+)                                                     
FORMUL   6  HOH   *262(H2 O)                                                    
HELIX    1   1 ALA A   55  TYR A   59  5                                   5    
HELIX    2   2 SER A  164  TYR A  172  1                                   9    
HELIX    3   3 TYR A  234  ASN A  245  1                                  12    
HELIX    4   4 ALA B   55  TYR B   59  5                                   5    
HELIX    5   5 SER B  164  TYR B  172  1                                   9    
HELIX    6   6 TYR B  234  ASN B  245  1                                  12    
SHEET    1   A 7 TYR A  20  THR A  21  0                                        
SHEET    2   A 7 GLN A 156  PRO A 161 -1  O  CYS A 157   N  TYR A  20           
SHEET    3   A 7 GLU A 135  GLY A 140 -1  N  CYS A 136   O  ALA A 160           
SHEET    4   A 7 PRO A 198  CYS A 201 -1  O  VAL A 200   N  LEU A 137           
SHEET    5   A 7 GLN A 204  GLY A 216 -1  O  GLN A 204   N  CYS A 201           
SHEET    6   A 7 GLY A 226  LYS A 230 -1  O  THR A 229   N  ILE A 212           
SHEET    7   A 7 MET A 180  VAL A 183 -1  N  ILE A 181   O  TYR A 228           
SHEET    1   B 8 TYR A  20  THR A  21  0                                        
SHEET    2   B 8 GLN A 156  PRO A 161 -1  O  CYS A 157   N  TYR A  20           
SHEET    3   B 8 GLU A 135  GLY A 140 -1  N  CYS A 136   O  ALA A 160           
SHEET    4   B 8 PRO A 198  CYS A 201 -1  O  VAL A 200   N  LEU A 137           
SHEET    5   B 8 GLN A 204  GLY A 216 -1  O  GLN A 204   N  CYS A 201           
SHEET    6   B 8 CYS I  43  THR I  46 -1  O  CYS I  45   N  GLY A 216           
SHEET    7   B 8 LYS I  52  CYS I  55 -1  O  ARG I  54   N  ILE I  44           
SHEET    8   B 8 ARG I  32  LEU I  33 -1  N  ARG I  32   O  CYS I  53           
SHEET    1   C 7 GLN A  30  ASN A  34  0                                        
SHEET    2   C 7 HIS A  40  ASN A  48 -1  O  CYS A  42   N  LEU A  33           
SHEET    3   C 7 TRP A  51  SER A  54 -1  O  TRP A  51   N  ILE A  47           
SHEET    4   C 7 MET A 104  LEU A 108 -1  O  ILE A 106   N  VAL A  52           
SHEET    5   C 7 GLN A  81  THR A  90 -1  N  ALA A  86   O  LYS A 107           
SHEET    6   C 7 GLN A  64  LEU A  67 -1  N  LEU A  67   O  GLN A  81           
SHEET    7   C 7 GLN A  30  ASN A  34 -1  N  ASN A  34   O  GLN A  64           
SHEET    1   D 7 CYS I  26  CYS I  28  0                                        
SHEET    2   D 7 CYS I  16  THR I  19 -1  N  ASP I  17   O  HIS I  27           
SHEET    3   D 7 GLN B 204  GLY B 216 -1  O  GLY B 216   N  CYS I  18           
SHEET    4   D 7 PRO B 198  CYS B 201 -1  N  CYS B 201   O  GLN B 204           
SHEET    5   D 7 GLU B 135  GLY B 140 -1  N  LEU B 137   O  VAL B 200           
SHEET    6   D 7 GLN B 156  PRO B 161 -1  O  ALA B 160   N  CYS B 136           
SHEET    7   D 7 TYR B  20  THR B  21 -1  N  TYR B  20   O  CYS B 157           
SHEET    1   E 5 CYS I  26  CYS I  28  0                                        
SHEET    2   E 5 CYS I  16  THR I  19 -1  N  ASP I  17   O  HIS I  27           
SHEET    3   E 5 GLN B 204  GLY B 216 -1  O  GLY B 216   N  CYS I  18           
SHEET    4   E 5 GLY B 226  LYS B 230 -1  O  THR B 229   N  ILE B 212           
SHEET    5   E 5 MET B 180  VAL B 183 -1  N  ILE B 181   O  TYR B 228           
SHEET    1   F 7 GLN B  30  ASN B  34  0                                        
SHEET    2   F 7 HIS B  40  ASN B  48 -1  O  GLY B  44   N  VAL B  31           
SHEET    3   F 7 TRP B  51  SER B  54 -1  O  TRP B  51   N  ILE B  47           
SHEET    4   F 7 MET B 104  LEU B 108 -1  O  ILE B 106   N  VAL B  52           
SHEET    5   F 7 GLN B  81  THR B  90 -1  N  ALA B  86   O  LYS B 107           
SHEET    6   F 7 GLN B  64  LEU B  67 -1  N  LEU B  67   O  GLN B  81           
SHEET    7   F 7 GLN B  30  ASN B  34 -1  N  ASN B  34   O  GLN B  64           
SSBOND   1 CYS A   22    CYS A  157                          1555   1555  2.01  
SSBOND   2 CYS A   42    CYS A   58                          1555   1555  2.08  
SSBOND   3 CYS A  128    CYS A  232                          1555   1555  2.00  
SSBOND   4 CYS A  136    CYS A  201                          1555   1555  2.00  
SSBOND   5 CYS A  168    CYS A  182                          1555   1555  2.03  
SSBOND   6 CYS A  191    CYS A  220                          1555   1555  2.03  
SSBOND   7 CYS I   12    CYS I   66                          1555   1555  2.02  
SSBOND   8 CYS I   13    CYS I   28                          1555   1555  1.99  
SSBOND   9 CYS I   16    CYS I   62                          1555   1555  2.03  
SSBOND  10 CYS I   18    CYS I   26                          1555   1555  2.04  
SSBOND  11 CYS I   36    CYS I   43                          1555   1555  2.03  
SSBOND  12 CYS I   40    CYS I   55                          1555   1555  2.04  
SSBOND  13 CYS I   45    CYS I   53                          1555   1555  1.97  
SSBOND  14 CYS B   22    CYS B  157                          1555   1555  2.01  
SSBOND  15 CYS B   42    CYS B   58                          1555   1555  2.04  
SSBOND  16 CYS B  128    CYS B  232                          1555   1555  2.00  
SSBOND  17 CYS B  136    CYS B  201                          1555   1555  2.00  
SSBOND  18 CYS B  168    CYS B  182                          1555   1555  2.03  
SSBOND  19 CYS B  191    CYS B  220                          1555   1555  2.04  
LINK         O   VAL A  75                CA    CA A 299     1555   1555  2.30  
LINK         O   VAL B  75                CA    CA B 246     1555   1555  2.32  
LINK         O   ASN B  72                CA    CA B 246     1555   1555  2.33  
LINK         O   ASN A  72                CA    CA A 299     1555   1555  2.34  
LINK         OE1 GLU B  70                CA    CA B 246     1555   1555  2.65  
LINK         OE1 GLU A  70                CA    CA A 299     1555   1555  2.66  
LINK         OE2 GLU A  80                CA    CA A 299     1555   1555  2.67  
LINK         OE2 GLU B  80                CA    CA B 246     1555   1555  2.68  
LINK        CA    CA A 299                 O   HOH A 425     1555   1555  2.41  
LINK        CA    CA B 246                 O   HOH B 508     1555   1555  2.42  
LINK        CA    CA A 299                 O   HOH A 428     1555   1555  2.44  
LINK        CA    CA B 246                 O   HOH B 510     1555   1555  2.44  
CISPEP   1 LYS I   22    PRO I   23          0       -14.93                     
CISPEP   2 MET I   49    PRO I   50          0         7.02                     
SITE     1 AC1  6 GLU A  70  ASN A  72  VAL A  75  GLU A  80                    
SITE     2 AC1  6 HOH A 425  HOH A 428                                          
SITE     1 AC2  6 GLU B  70  ASN B  72  VAL B  75  GLU B  80                    
SITE     2 AC2  6 HOH B 508  HOH B 510                                          
CRYST1   62.460   62.460  160.010  90.00  90.00 120.00 P 31          6          
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      0.016010  0.009244  0.000000        0.00000                         
SCALE2      0.000000  0.018487  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006250        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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