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Database: PDB
Entry: 2DDF
LinkDB: 2DDF
Original site: 2DDF 
HEADER    HYDROLASE                               28-JAN-06   2DDF              
TITLE     CRYSTAL STRUCTURE OF TACE IN COMPLEX WITH TAPI-2                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ADAM 17;                                                   
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: A DISINTEGRIN AND METALLOPROTEINASE DOMAIN 17, TNF-ALPHA-   
COMPND   5 CONVERTING ENZYME, TNF-ALPHA CONVERTASE, SNAKE VENOM-LIKE PROTEASE,  
COMPND   6 CD156B ANTIGEN;                                                      
COMPND   7 EC: 3.4.24.86;                                                       
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: ADAM17, CSVP, TACE;                                            
SOURCE   6 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;                                  
SOURCE   7 EXPRESSION_SYSTEM_COMMON: CABBAGE LOOPER;                            
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7111                                        
KEYWDS    TACE ADAM17 ZN-ENDOPEPTIDASE, HYDROLASE                               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    P.ORTH                                                                
REVDAT   4   05-OCT-11 2DDF    1       LINK                                     
REVDAT   3   13-JUL-11 2DDF    1       VERSN                                    
REVDAT   2   24-FEB-09 2DDF    1       VERSN                                    
REVDAT   1   14-MAR-06 2DDF    0                                                
JRNL        AUTH   R.N.INGRAM,P.ORTH,C.L.STRICKLAND,H.V.LE,V.MADISON,B.M.BEYER  
JRNL        TITL   STABILIZATION OF THE AUTOPROTEOLYSIS OF TNF-ALPHA CONVERTING 
JRNL        TITL 2 ENZYME (TACE) RESULTS IN A NOVEL CRYSTAL FORM SUITABLE FOR   
JRNL        TITL 3 STRUCTURE-BASED DRUG DESIGN STUDIES.                         
JRNL        REF    PROTEIN ENG.DES.SEL.          V.  19   155 2006              
JRNL        REFN                   ISSN 1741-0126                               
JRNL        PMID   16459338                                                     
JRNL        DOI    10.1093/PROTEIN/GZJ014                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0005                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 63552                          
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) : 0.204                           
REMARK   3   R VALUE            (WORKING SET) : 0.204                           
REMARK   3   FREE R VALUE                     : 0.230                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 2.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1259                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.70                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.74                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 4409                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 95.84                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2660                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 108                          
REMARK   3   BIN FREE R VALUE                    : 0.2900                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3892                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 95                                      
REMARK   3   SOLVENT ATOMS            : 333                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 37.00                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.14000                                              
REMARK   3    B22 (A**2) : -0.40000                                             
REMARK   3    B33 (A**2) : -0.74000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.109         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.104         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.070         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.077         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.952                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.942                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4077 ; 0.013 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5522 ; 1.340 ; 1.966       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   504 ; 6.070 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   185 ;34.002 ;25.081       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   635 ;11.987 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    11 ;13.083 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   589 ; 0.093 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3144 ; 0.006 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1936 ; 0.201 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  2838 ; 0.308 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   310 ; 0.143 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):     5 ; 0.095 ; 0.200       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    69 ; 0.206 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    29 ; 0.136 ; 0.200       
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):  2587 ; 1.072 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3995 ; 1.616 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1711 ; 2.418 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1527 ; 3.430 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2DDF COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-FEB-06.                  
REMARK 100 THE RCSB ID CODE IS RCSB025284.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-NOV-05                          
REMARK 200  TEMPERATURE           (KELVIN) : 95                                 
REMARK 200  PH                             : 5.6                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU FR-E                        
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 63496                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.2                               
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) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: 1BKC                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 50.97                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.51                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 15% PEG 6K, 10% 2-PROPANOL, 100 MM       
REMARK 280  SODIUM CITRATE BUFFER , PH 5.6, VAPOR DIFFUSION, HANGING DROP,      
REMARK 280  TEMPERATURE 295K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       37.19700            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       51.85650            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       37.81950            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       51.85650            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       37.19700            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       37.81950            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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     ARG A   357                                                      
REMARK 465     ALA A   358                                                      
REMARK 465     ASN A   359                                                      
REMARK 465     SER A   360                                                      
REMARK 465     PRO B   218                                                      
REMARK 465     ASP B   219                                                      
REMARK 465     SER B   474                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ARG A 241    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 302    CG   CD   CE   NZ                                   
REMARK 470     LYS A 309    CG   CD   CE   NZ                                   
REMARK 470     HIS A 361    CG   ND1  CD2  CE1  NE2                             
REMARK 470     GLU A 427    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 445    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 448    CG   CD   CE   NZ                                   
REMARK 470     LYS A 460    CG   CD   CE   NZ                                   
REMARK 470     GLU A 463    CG   CD   OE1  OE2                                  
REMARK 470     SER A 464    OG                                                  
REMARK 470     PRO B 220    CB   CG   CD                                        
REMARK 470     LYS B 222    CG   CD   CE   NZ                                   
REMARK 470     ARG B 237    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B 241    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B 283    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B 290    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 302    CG   CD   CE   NZ                                   
REMARK 470     ASN B 306    CG   OD1  ND2                                       
REMARK 470     GLU B 307    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 309    CG   CD   CE   NZ                                   
REMARK 470     GLU B 327    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 328    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 331    CG   CD   CE   NZ                                   
REMARK 470     LYS B 367    CG   CD   CE   NZ                                   
REMARK 470     LYS B 392    CG   CD   CE   NZ                                   
REMARK 470     GLU B 427    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 445    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 460    CG   CD   CE   NZ                                   
REMARK 470     GLU B 463    CG   CD   OE1  OE2                                  
REMARK 470     GLN B 467    CG   CD   OE1  NE2                                  
REMARK 470     GLU B 472    CG   CD   OE1  OE2                                  
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   O    HOH B   533     O    HOH B   601              2.17            
REMARK 500   OE2  GLU A   290     O    HOH A   614              2.18            
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    LYS A 222       57.19   -141.03                                   
REMARK 500    ASN A 269       37.80     73.57                                   
REMARK 500    ALA A 270     -118.87   -150.30                                   
REMARK 500    CYS A 365      125.77     73.83                                   
REMARK 500    ASN A 381       57.94    -96.13                                   
REMARK 500    ALA B 270     -110.90   -133.25                                   
REMARK 500    SER B 360     -154.94    -99.60                                   
REMARK 500    CYS B 365      119.15     84.57                                   
REMARK 500    CYS B 469       -4.01   -144.77                                   
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 THR A  461     ILE A  462                 -148.33                    
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                              ZN A   1  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 405   NE2                                                    
REMARK 620 2 HIS A 409   NE2  96.5                                              
REMARK 620 3 HIS A 415   NE2 102.6  97.2                                        
REMARK 620 4 INN A   3   O    97.6 163.4  88.3                                  
REMARK 620 5 INN A   3   O4   93.3  90.1 161.6  80.4                            
REMARK 620 6 HOH A 661   O   174.1  85.5  82.6  79.7  81.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B   4  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B 405   NE2                                                    
REMARK 620 2 HIS B 409   NE2  96.3                                              
REMARK 620 3 HIS B 415   NE2 101.0  94.6                                        
REMARK 620 4 INN B   2   O    99.4 162.1  90.7                                  
REMARK 620 5 INN B   2   O4   97.3  89.8 160.6  79.9                            
REMARK 620 6 HOH B 642   O   170.6  80.3  88.1  82.8  74.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 475  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 342   OD1                                                    
REMARK 620 2 PHE A 343   O   109.1                                              
REMARK 620 3 ASN A 389   OD1 101.3 145.2                                        
REMARK 620 4 HOH A 660   O    86.9  83.7  81.6                                  
REMARK 620 5 HOH A 659   O    97.4 104.8  87.1 168.5                            
REMARK 620 6 PHE A 343   N    84.0  57.2 144.9 133.5  57.8                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 630                                                                      
REMARK 630 MOLECULE TYPE: NULL                                                  
REMARK 630 MOLECULE NAME: N-{(2R)-2-[2-(HYDROXYAMINO)-2-OXOETHYL]-4-            
REMARK 630 METHYLPENTANOYL}-3-METHYL-L-VALYL-N-(2-AMINOETHYL)-L-ALANINAMIDE     
REMARK 630 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 630  SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                           
REMARK 630                                                                      
REMARK 630   M RES C SSSEQI                                                     
REMARK 630     INN B     2                                                      
REMARK 630     INN A     3                                                      
REMARK 630 SOURCE: NULL                                                         
REMARK 630 TAXONOMY: NULL                                                       
REMARK 630 SUBCOMP:    2HM TBG ALA EDN                                          
REMARK 630 DETAILS: NULL                                                        
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 1                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 4                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 475                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE INN B 2                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE INN A 3                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IMD B 475                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CIT B 500                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IPA B 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IPA A 476                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IPA B 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IPA B 503                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1BKC   RELATED DB: PDB                                   
DBREF  2DDF A  218   474  UNP    P78536   ADA17_HUMAN    218    474             
DBREF  2DDF B  218   474  UNP    P78536   ADA17_HUMAN    218    474             
SEQADV 2DDF ALA A  266  UNP  P78536    SER   266 ENGINEERED                     
SEQADV 2DDF GLY A  353  UNP  P78536    VAL   353 ENGINEERED                     
SEQADV 2DDF GLN A  452  UNP  P78536    ASN   452 ENGINEERED                     
SEQADV 2DDF ALA B  266  UNP  P78536    SER   266 ENGINEERED                     
SEQADV 2DDF GLY B  353  UNP  P78536    VAL   353 ENGINEERED                     
SEQADV 2DDF GLN B  452  UNP  P78536    ASN   452 ENGINEERED                     
SEQRES   1 A  257  PRO ASP PRO MET LYS ASN THR CYS LYS LEU LEU VAL VAL          
SEQRES   2 A  257  ALA ASP HIS ARG PHE TYR ARG TYR MET GLY ARG GLY GLU          
SEQRES   3 A  257  GLU SER THR THR THR ASN TYR LEU ILE GLU LEU ILE ASP          
SEQRES   4 A  257  ARG VAL ASP ASP ILE TYR ARG ASN THR ALA TRP ASP ASN          
SEQRES   5 A  257  ALA GLY PHE LYS GLY TYR GLY ILE GLN ILE GLU GLN ILE          
SEQRES   6 A  257  ARG ILE LEU LYS SER PRO GLN GLU VAL LYS PRO GLY GLU          
SEQRES   7 A  257  LYS HIS TYR ASN MET ALA LYS SER TYR PRO ASN GLU GLU          
SEQRES   8 A  257  LYS ASP ALA TRP ASP VAL LYS MET LEU LEU GLU GLN PHE          
SEQRES   9 A  257  SER PHE ASP ILE ALA GLU GLU ALA SER LYS VAL CYS LEU          
SEQRES  10 A  257  ALA HIS LEU PHE THR TYR GLN ASP PHE ASP MET GLY THR          
SEQRES  11 A  257  LEU GLY LEU ALA TYR GLY GLY SER PRO ARG ALA ASN SER          
SEQRES  12 A  257  HIS GLY GLY VAL CYS PRO LYS ALA TYR TYR SER PRO VAL          
SEQRES  13 A  257  GLY LYS LYS ASN ILE TYR LEU ASN SER GLY LEU THR SER          
SEQRES  14 A  257  THR LYS ASN TYR GLY LYS THR ILE LEU THR LYS GLU ALA          
SEQRES  15 A  257  ASP LEU VAL THR THR HIS GLU LEU GLY HIS ASN PHE GLY          
SEQRES  16 A  257  ALA GLU HIS ASP PRO ASP GLY LEU ALA GLU CYS ALA PRO          
SEQRES  17 A  257  ASN GLU ASP GLN GLY GLY LYS TYR VAL MET TYR PRO ILE          
SEQRES  18 A  257  ALA VAL SER GLY ASP HIS GLU ASN ASN LYS MET PHE SER          
SEQRES  19 A  257  GLN CYS SER LYS GLN SER ILE TYR LYS THR ILE GLU SER          
SEQRES  20 A  257  LYS ALA GLN GLU CYS PHE GLN GLU ARG SER                      
SEQRES   1 B  257  PRO ASP PRO MET LYS ASN THR CYS LYS LEU LEU VAL VAL          
SEQRES   2 B  257  ALA ASP HIS ARG PHE TYR ARG TYR MET GLY ARG GLY GLU          
SEQRES   3 B  257  GLU SER THR THR THR ASN TYR LEU ILE GLU LEU ILE ASP          
SEQRES   4 B  257  ARG VAL ASP ASP ILE TYR ARG ASN THR ALA TRP ASP ASN          
SEQRES   5 B  257  ALA GLY PHE LYS GLY TYR GLY ILE GLN ILE GLU GLN ILE          
SEQRES   6 B  257  ARG ILE LEU LYS SER PRO GLN GLU VAL LYS PRO GLY GLU          
SEQRES   7 B  257  LYS HIS TYR ASN MET ALA LYS SER TYR PRO ASN GLU GLU          
SEQRES   8 B  257  LYS ASP ALA TRP ASP VAL LYS MET LEU LEU GLU GLN PHE          
SEQRES   9 B  257  SER PHE ASP ILE ALA GLU GLU ALA SER LYS VAL CYS LEU          
SEQRES  10 B  257  ALA HIS LEU PHE THR TYR GLN ASP PHE ASP MET GLY THR          
SEQRES  11 B  257  LEU GLY LEU ALA TYR GLY GLY SER PRO ARG ALA ASN SER          
SEQRES  12 B  257  HIS GLY GLY VAL CYS PRO LYS ALA TYR TYR SER PRO VAL          
SEQRES  13 B  257  GLY LYS LYS ASN ILE TYR LEU ASN SER GLY LEU THR SER          
SEQRES  14 B  257  THR LYS ASN TYR GLY LYS THR ILE LEU THR LYS GLU ALA          
SEQRES  15 B  257  ASP LEU VAL THR THR HIS GLU LEU GLY HIS ASN PHE GLY          
SEQRES  16 B  257  ALA GLU HIS ASP PRO ASP GLY LEU ALA GLU CYS ALA PRO          
SEQRES  17 B  257  ASN GLU ASP GLN GLY GLY LYS TYR VAL MET TYR PRO ILE          
SEQRES  18 B  257  ALA VAL SER GLY ASP HIS GLU ASN ASN LYS MET PHE SER          
SEQRES  19 B  257  GLN CYS SER LYS GLN SER ILE TYR LYS THR ILE GLU SER          
SEQRES  20 B  257  LYS ALA GLN GLU CYS PHE GLN GLU ARG SER                      
HET     ZN  A   1       1                                                       
HET     ZN  B   4       1                                                       
HET     CA  A 475       1                                                       
HET    INN  B   2      29                                                       
HET    INN  A   3      29                                                       
HET    IMD  B 475       5                                                       
HET    CIT  B 500      13                                                       
HET    IPA  B 501       4                                                       
HET    IPA  A 476       4                                                       
HET    IPA  B 502       4                                                       
HET    IPA  B 503       4                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM      CA CALCIUM ION                                                      
HETNAM     INN N-{(2R)-2-[2-(HYDROXYAMINO)-2-OXOETHYL]-4-                       
HETNAM   2 INN  METHYLPENTANOYL}-3-METHYL-L-VALYL-N-(2-AMINOETHYL)-L-           
HETNAM   3 INN  ALANINAMIDE                                                     
HETNAM     IMD IMIDAZOLE                                                        
HETNAM     CIT CITRIC ACID                                                      
HETNAM     IPA ISOPROPYL ALCOHOL                                                
HETSYN     IPA 2-PROPANOL                                                       
FORMUL   3   ZN    2(ZN 2+)                                                     
FORMUL   5   CA    CA 2+                                                        
FORMUL   6  INN    2(C19 H37 N5 O5)                                             
FORMUL   8  IMD    C3 H5 N2 1+                                                  
FORMUL   9  CIT    C6 H8 O7                                                     
FORMUL  10  IPA    4(C3 H8 O)                                                   
FORMUL  14  HOH   *333(H2 O)                                                    
HELIX    1   1 ASP A  232  MET A  239  1                                   8    
HELIX    2   2 GLU A  243  ASN A  264  1                                  22    
HELIX    3   3 ASP A  313  ILE A  325  1                                  13    
HELIX    4   4 ILE A  325  SER A  330  1                                   6    
HELIX    5   5 PHE A  343  THR A  347  5                                   5    
HELIX    6   6 LEU A  395  PHE A  411  1                                  17    
HELIX    7   7 ASN A  426  GLY A  430  5                                   5    
HELIX    8   8 SER A  451  PHE A  470  1                                  20    
HELIX    9   9 ASP B  232  MET B  239  1                                   8    
HELIX   10  10 GLU B  243  ASN B  264  1                                  22    
HELIX   11  11 ASP B  313  ILE B  325  1                                  13    
HELIX   12  12 ILE B  325  SER B  330  1                                   6    
HELIX   13  13 PHE B  343  THR B  347  5                                   5    
HELIX   14  14 LEU B  395  PHE B  411  1                                  17    
HELIX   15  15 ASN B  426  GLY B  430  5                                   5    
HELIX   16  16 HIS B  444  MET B  449  5                                   6    
HELIX   17  17 SER B  451  PHE B  470  1                                  20    
SHEET    1   A 5 GLY A 276  ILE A 284  0                                        
SHEET    2   A 5 THR A 224  ALA A 231  1  N  LEU A 227   O  GLU A 280           
SHEET    3   A 5 LEU A 334  THR A 339  1  O  PHE A 338   N  VAL A 230           
SHEET    4   A 5 SER A 382  SER A 386  1  O  THR A 385   N  THR A 339           
SHEET    5   A 5 GLY A 349  ALA A 351 -1  N  LEU A 350   O  LEU A 384           
SHEET    1   B 2 ALA A 368  SER A 371  0                                        
SHEET    2   B 2 LYS A 376  TYR A 379 -1  O  ILE A 378   N  TYR A 369           
SHEET    1   C 2 LYS A 388  ASN A 389  0                                        
SHEET    2   C 2 LYS A 392  THR A 393 -1  O  LYS A 392   N  ASN A 389           
SHEET    1   D 5 GLY B 276  ILE B 284  0                                        
SHEET    2   D 5 THR B 224  ALA B 231  1  N  LEU B 227   O  GLU B 280           
SHEET    3   D 5 LEU B 334  THR B 339  1  O  PHE B 338   N  VAL B 230           
SHEET    4   D 5 SER B 382  SER B 386  1  O  THR B 385   N  LEU B 337           
SHEET    5   D 5 GLY B 349  ALA B 351 -1  N  LEU B 350   O  LEU B 384           
SHEET    1   E 2 ALA B 368  SER B 371  0                                        
SHEET    2   E 2 LYS B 376  TYR B 379 -1  O  ILE B 378   N  TYR B 369           
SHEET    1   F 2 LYS B 388  ASN B 389  0                                        
SHEET    2   F 2 LYS B 392  THR B 393 -1  O  LYS B 392   N  ASN B 389           
SSBOND   1 CYS A  225    CYS A  333                          1555   1555  2.08  
SSBOND   2 CYS A  365    CYS A  469                          1555   1555  2.01  
SSBOND   3 CYS A  423    CYS A  453                          1555   1555  2.03  
SSBOND   4 CYS B  225    CYS B  333                          1555   1555  2.08  
SSBOND   5 CYS B  365    CYS B  469                          1555   1555  2.03  
SSBOND   6 CYS B  423    CYS B  453                          1555   1555  2.06  
LINK        ZN    ZN A   1                 NE2 HIS A 405     1555   1555  2.07  
LINK        ZN    ZN A   1                 NE2 HIS A 409     1555   1555  2.09  
LINK        ZN    ZN A   1                 NE2 HIS A 415     1555   1555  2.05  
LINK        ZN    ZN A   1                 O   INN A   3     1555   1555  2.06  
LINK        ZN    ZN A   1                 O4  INN A   3     1555   1555  2.18  
LINK        ZN    ZN B   4                 NE2 HIS B 405     1555   1555  2.14  
LINK        ZN    ZN B   4                 NE2 HIS B 409     1555   1555  2.12  
LINK        ZN    ZN B   4                 NE2 HIS B 415     1555   1555  2.06  
LINK        ZN    ZN B   4                 O   INN B   2     1555   1555  2.08  
LINK        ZN    ZN B   4                 O4  INN B   2     1555   1555  2.06  
LINK         OD1 ASP A 342                CA    CA A 475     1555   1555  2.28  
LINK         O   PHE A 343                CA    CA A 475     1555   1555  2.31  
LINK         OD1 ASN A 389                CA    CA A 475     1555   1555  2.31  
LINK        CA    CA A 475                 O   HOH A 660     1555   1555  2.39  
LINK        CA    CA A 475                 O   HOH A 659     1555   1555  2.43  
LINK        ZN    ZN A   1                 O   HOH A 661     1555   1555  2.48  
LINK        CA    CA A 475                 N   PHE A 343     1555   1555  3.29  
LINK        ZN    ZN B   4                 O   HOH B 642     1555   1555  2.47  
CISPEP   1 TYR A  304    PRO A  305          0         8.64                     
CISPEP   2 TYR B  304    PRO B  305          0         8.52                     
CISPEP   3 SER B  355    PRO B  356          0         4.67                     
SITE     1 AC1  5 INN A   3  HIS A 405  HIS A 409  HIS A 415                    
SITE     2 AC1  5 HOH A 661                                                     
SITE     1 AC2  5 INN B   2  HIS B 405  HIS B 409  HIS B 415                    
SITE     2 AC2  5 HOH B 642                                                     
SITE     1 AC3  5 ASP A 342  PHE A 343  ASN A 389  HOH A 659                    
SITE     2 AC3  5 HOH A 660                                                     
SITE     1 AC4 17  ZN B   4  MET B 345  GLY B 346  THR B 347                    
SITE     2 AC4 17 LEU B 348  GLY B 349  ASN B 389  HIS B 405                    
SITE     3 AC4 17 GLU B 406  HIS B 409  HIS B 415  PRO B 437                    
SITE     4 AC4 17 ILE B 438  ALA B 439  HOH B 630  HOH B 642                    
SITE     5 AC4 17 HOH B 645                                                     
SITE     1 AC5 22  ZN A   1  GLU A 327  SER A 330  MET A 345                    
SITE     2 AC5 22 GLY A 346  THR A 347  LEU A 348  GLY A 349                    
SITE     3 AC5 22 ASN A 389  TYR A 390  HIS A 405  GLU A 406                    
SITE     4 AC5 22 HIS A 409  HIS A 415  PRO A 437  ILE A 438                    
SITE     5 AC5 22 ALA A 439  HOH A 642  HOH A 661  HOH A 662                    
SITE     6 AC5 22 HOH A 663  HOH A 665                                          
SITE     1 AC6  5 ARG B 357  ALA B 358  ASN B 359  CIT B 500                    
SITE     2 AC6  5 HOH B 589                                                     
SITE     1 AC7 10 PRO A 356  HIS A 415  PRO A 437  ARG B 357                    
SITE     2 AC7 10 ASN B 359  SER B 360  HIS B 361  IMD B 475                    
SITE     3 AC7 10 HOH B 631  HOH B 643                                          
SITE     1 AC8  2 GLU A 280  LEU B 420                                          
SITE     1 AC9  5 LEU A 285  LYS A 286  SER A 287  PRO A 288                    
SITE     2 AC9  5 GLN A 289                                                     
SITE     1 BC1  2 LYS B 286  SER B 287                                          
SITE     1 BC2  3 ILE B 279  GLU B 280  HOH B 646                               
CRYST1   74.394   75.639  103.713  90.00  90.00  90.00 P 21 21 21    8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.013442  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.013221  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009642        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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