GenomeNet

Database: PDB
Entry: 1XKB
LinkDB: 1XKB
Original site: 1XKB 
HEADER    BLOOD COAGULATION FACTOR                19-MAR-98   1XKB              
TITLE     FACTOR XA COMPLEXED WITH A SYNTHETIC INHIBITOR FX-2212A,(2S)-(3'-     
TITLE    2 AMIDINO-3-BIPHENYLYL)-5-(4-PYRIDYLAMINO)PENTANOIC ACID               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: BLOOD COAGULATION FACTOR XA;                               
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: PROTEOLYTIC CLEAVAGE PRODUCT, GLA DOMAIN;                  
COMPND   5 SYNONYM: STUART FACTOR;                                              
COMPND   6 EC: 3.4.21.6;                                                        
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: BLOOD COAGULATION FACTOR XA;                               
COMPND   9 CHAIN: C, D;                                                         
COMPND  10 FRAGMENT: PROTEOLYTIC CLEAVAGE PRODUCT, GLA DOMAIN;                  
COMPND  11 SYNONYM: STUART FACTOR;                                              
COMPND  12 EC: 3.4.21.6                                                         
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 TISSUE: BLOOD;                                                       
SOURCE   6 MOL_ID: 2;                                                           
SOURCE   7 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   8 ORGANISM_COMMON: HUMAN;                                              
SOURCE   9 ORGANISM_TAXID: 9606;                                                
SOURCE  10 TISSUE: BLOOD                                                        
KEYWDS    BLOOD COAGULATION FACTOR, SERINE PROTEINASE, EPIDERMAL GROWTH FACTOR  
KEYWDS   2 LIKE DOMAIN                                                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.KAMATA,S.H.KIM                                                      
REVDAT   3   20-JUN-12 1XKB    1       HETNAM VERSN                             
REVDAT   2   24-FEB-09 1XKB    1       VERSN                                    
REVDAT   1   23-MAR-99 1XKB    0                                                
JRNL        AUTH   K.KAMATA,H.KAWAMOTO,T.HONMA,T.IWAMA,S.H.KIM                  
JRNL        TITL   STRUCTURAL BASIS FOR CHEMICAL INHIBITION OF HUMAN BLOOD      
JRNL        TITL 2 COAGULATION FACTOR XA.                                       
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V.  95  6630 1998              
JRNL        REFN                   ISSN 0027-8424                               
JRNL        PMID   9618463                                                      
JRNL        DOI    10.1073/PNAS.95.12.6630                                      
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   H.BRANDSTETTER,A.KUHNE,W.BODE,R.HUBER,W.VON DER SAAL,        
REMARK   1  AUTH 2 K.WIRTHENSOHN,R.A.ENGH                                       
REMARK   1  TITL   X-RAY STRUCTURE OF ACTIVE SITE-INHIBITED CLOTTING FACTOR XA. 
REMARK   1  TITL 2 IMPLICATIONS FOR DRUG DESIGN AND SUBSTRATE RECOGNITION       
REMARK   1  REF    J.BIOL.CHEM.                  V. 271 29988 1996              
REMARK   1  REFN                   ISSN 0021-9258                               
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   K.PADMANABHAN,K.P.PADMANABHAN,A.TULINSKY,C.H.PARK,W.BODE,    
REMARK   1  AUTH 2 R.HUBER,D.T.BLANKENSHIP,A.D.CARDIN,W.KISIEL                  
REMARK   1  TITL   STRUCTURE OF HUMAN DES(1-45) FACTOR XA AT 2.2 A RESOLUTION   
REMARK   1  REF    J.MOL.BIOL.                   V. 232   947 1993              
REMARK   1  REFN                   ISSN 0022-2836                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR 3.8                                           
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 8.00                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 1000000.000                    
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0010                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 86.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 24386                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RAMDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.206                           
REMARK   3   FREE R VALUE                     : 0.294                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 8.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1916                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.007                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 8                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.40                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.51                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 47.10                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 1528                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3540                       
REMARK   3   BIN FREE R VALUE                    : 0.4180                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 3.90                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 137                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.036                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5073                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 61                                      
REMARK   3   SOLVENT ATOMS            : 299                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 46.00                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 24.10                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.30                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.35                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.44                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.37                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.008                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.30                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 28.20                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.64                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.760 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 2.110 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 2.380 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 3.190 ; 2.500                
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  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : NULL                                           
REMARK   3  PARAMETER FILE  3  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : TOPHCSDX.PRO                                   
REMARK   3  TOPOLOGY FILE  2   : TOPH19.SOL                                     
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1XKB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 24-OCT-96                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.0                                
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 RUH2R                       
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NI FILTER                          
REMARK 200  OPTICS                         : YALE MIRRORS                       
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU                             
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 26594                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 91.2                               
REMARK 200  DATA REDUNDANCY                : 2.700                              
REMARK 200  R MERGE                    (I) : 0.05700                            
REMARK 200  R SYM                      (I) : 0.05700                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 17.7000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.53                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 58.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.10                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.25200                            
REMARK 200  R SYM FOR SHELL            (I) : 0.25200                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.100                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: X-PLOR 3.8                                            
REMARK 200 STARTING MODEL: PDB ENTRY 1HCG                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 60.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.50                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 6.0                                   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,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        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       52.61000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4                                              
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2700 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 15910 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -27.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C                                  
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2640 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 16160 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -20.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D                                  
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: 3                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 7580 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 29820 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -49.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C                                  
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 APPLY THE FOLLOWING TO CHAINS: B, D                                  
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000       43.61426            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000      -52.61000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       61.51835            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 7300 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 30110 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -50.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C                                  
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 APPLY THE FOLLOWING TO CHAINS: B, D                                  
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000      -52.61000            
REMARK 350   BIOMT3   2  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     LYS A    45                                                      
REMARK 465     ASP A    46                                                      
REMARK 465     GLY A    47                                                      
REMARK 465     ARG A   139                                                      
REMARK 465     LYS B    45                                                      
REMARK 465     ASP B    46                                                      
REMARK 465     GLY B    47                                                      
REMARK 465     ASP B    48                                                      
REMARK 465     GLN B    49                                                      
REMARK 465     ARG D   245                                                      
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    LEU C 158   CA  -  CB  -  CG  ANGL. DEV. =  14.5 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    GLN A  98     -112.39   -127.04                                   
REMARK 500    GLN A 104       39.76     81.29                                   
REMARK 500    ARG A 113      150.56    -49.34                                   
REMARK 500    LYS A 122      -58.51   -123.87                                   
REMARK 500    TYR A 130       78.46   -116.73                                   
REMARK 500    ASN C  35     -165.98    -79.24                                   
REMARK 500    ALA C  61A     132.91   -170.50                                   
REMARK 500    ASN C  92       -7.76    -53.28                                   
REMARK 500    ASN C 117        2.25     82.21                                   
REMARK 500    GLN C 187       52.89    -66.51                                   
REMARK 500    ASP C 189     -179.05    177.24                                   
REMARK 500    SER C 214      -67.51    -93.75                                   
REMARK 500    LYS C 230       97.60    -59.75                                   
REMARK 500    LYS C 243       49.65   -106.89                                   
REMARK 500    PRO B  54       45.11    -87.33                                   
REMARK 500    ASN B  57       51.56     36.81                                   
REMARK 500    GLN B  58       82.40     47.48                                   
REMARK 500    BHD B  63     -152.16   -122.83                                   
REMARK 500    LEU B  73     -159.39    -77.57                                   
REMARK 500    ASP B  95        0.91     86.85                                   
REMARK 500    GLN B  98     -107.30   -129.08                                   
REMARK 500    THR B 136       31.76    -75.57                                   
REMARK 500    GLU B 138        4.81   -160.25                                   
REMARK 500    GLN D  20      157.58    175.77                                   
REMARK 500    ASN D  35     -163.60    -69.74                                   
REMARK 500    SER D  48     -176.24   -172.28                                   
REMARK 500    ALA D  61A     117.78   -166.98                                   
REMARK 500    ARG D 125      -75.96    -43.63                                   
REMARK 500    LEU D 131A     -61.74   -103.32                                   
REMARK 500    ASP D 205       -5.66     77.87                                   
REMARK 500    SER D 214      -69.16   -101.44                                   
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 501  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 BHD A  63   OD1                                                    
REMARK 620 2 BHD A  63   OD2  40.9                                              
REMARK 620 3 GLY A  64   O    50.0  68.6                                        
REMARK 620 4 GLN A  49   OE1  73.3  98.1 107.5                                  
REMARK 620 5 LEU A  65   O   103.9 114.6  54.4 125.7                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA C 503  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU C  76   OE1                                                    
REMARK 620 2 GLU C  80   OE2  74.3                                              
REMARK 620 3 ASN C  72   O   119.7 143.3                                        
REMARK 620 4 GLN C  75   O    84.5 150.9  65.1                                  
REMARK 620 5 GLU C  77   OE1 109.4  85.5 116.2  82.9                            
REMARK 620 6 GLU C  77   OE2 149.2 107.5  77.9  80.9  42.0                      
REMARK 620 7 GLU C  80   OE1  79.1  42.4 160.3 114.6  46.7  82.7                
REMARK 620 8 ASP C  70   OD1 119.8  56.0  90.1 152.5  99.0  82.5  84.6          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA D 502  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP D  70   OD1                                                    
REMARK 620 2 ASN D  72   O    77.2                                              
REMARK 620 3 GLU D  77   OE2  82.5 118.9                                        
REMARK 620 4 GLU D  80   OE1  72.4 133.7  91.0                                  
REMARK 620 5 GLN D  75   O   141.5  68.0 128.6 121.6                            
REMARK 620 N                    1     2     3     4                             
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 501                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA D 502                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 503                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 4PP C 998                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 4PP D 999                 
DBREF  1XKB A   45   139  UNP    P00742   FA10_HUMAN      85    179             
DBREF  1XKB C   16   245  UNP    P00742   FA10_HUMAN     235    469             
DBREF  1XKB B   45   139  UNP    P00742   FA10_HUMAN      85    179             
DBREF  1XKB D   16   245  UNP    P00742   FA10_HUMAN     235    469             
SEQADV 1XKB BHD A   63  UNP  P00742    ASP   103 MODIFIED RESIDUE               
SEQADV 1XKB BHD B   63  UNP  P00742    ASP   103 MODIFIED RESIDUE               
SEQRES   1 A   95  LYS ASP GLY ASP GLN CYS GLU THR SER PRO CYS GLN ASN          
SEQRES   2 A   95  GLN GLY LYS CYS LYS BHD GLY LEU GLY GLU TYR THR CYS          
SEQRES   3 A   95  THR CYS LEU GLU GLY PHE GLU GLY LYS ASN CYS GLU LEU          
SEQRES   4 A   95  PHE THR ARG LYS LEU CYS SER LEU ASP ASN GLY ASP CYS          
SEQRES   5 A   95  ASP GLN PHE CYS HIS GLU GLU GLN ASN SER VAL VAL CYS          
SEQRES   6 A   95  SER CYS ALA ARG GLY TYR THR LEU ALA ASP ASN GLY LYS          
SEQRES   7 A   95  ALA CYS ILE PRO THR GLY PRO TYR PRO CYS GLY LYS GLN          
SEQRES   8 A   95  THR LEU GLU ARG                                              
SEQRES   1 C  235  ILE VAL GLY GLY GLN GLU CYS LYS ASP GLY GLU CYS PRO          
SEQRES   2 C  235  TRP GLN ALA LEU LEU ILE ASN GLU GLU ASN GLU GLY PHE          
SEQRES   3 C  235  CYS GLY GLY THR ILE LEU SER GLU PHE TYR ILE LEU THR          
SEQRES   4 C  235  ALA ALA HIS CYS LEU TYR GLN ALA LYS ARG PHE LYS VAL          
SEQRES   5 C  235  ARG VAL GLY ASP ARG ASN THR GLU GLN GLU GLU GLY GLY          
SEQRES   6 C  235  GLU ALA VAL HIS GLU VAL GLU VAL VAL ILE LYS HIS ASN          
SEQRES   7 C  235  ARG PHE THR LYS GLU THR TYR ASP PHE ASP ILE ALA VAL          
SEQRES   8 C  235  LEU ARG LEU LYS THR PRO ILE THR PHE ARG MET ASN VAL          
SEQRES   9 C  235  ALA PRO ALA CYS LEU PRO GLU ARG ASP TRP ALA GLU SER          
SEQRES  10 C  235  THR LEU MET THR GLN LYS THR GLY ILE VAL SER GLY PHE          
SEQRES  11 C  235  GLY ARG THR HIS GLU LYS GLY ARG GLN SER THR ARG LEU          
SEQRES  12 C  235  LYS MET LEU GLU VAL PRO TYR VAL ASP ARG ASN SER CYS          
SEQRES  13 C  235  LYS LEU SER SER SER PHE ILE ILE THR GLN ASN MET PHE          
SEQRES  14 C  235  CYS ALA GLY TYR ASP THR LYS GLN GLU ASP ALA CYS GLN          
SEQRES  15 C  235  GLY ASP SER GLY GLY PRO HIS VAL THR ARG PHE LYS ASP          
SEQRES  16 C  235  THR TYR PHE VAL THR GLY ILE VAL SER TRP GLY GLU GLY          
SEQRES  17 C  235  CYS ALA ARG LYS GLY LYS TYR GLY ILE TYR THR LYS VAL          
SEQRES  18 C  235  THR ALA PHE LEU LYS TRP ILE ASP ARG SER MET LYS THR          
SEQRES  19 C  235  ARG                                                          
SEQRES   1 B   95  LYS ASP GLY ASP GLN CYS GLU THR SER PRO CYS GLN ASN          
SEQRES   2 B   95  GLN GLY LYS CYS LYS BHD GLY LEU GLY GLU TYR THR CYS          
SEQRES   3 B   95  THR CYS LEU GLU GLY PHE GLU GLY LYS ASN CYS GLU LEU          
SEQRES   4 B   95  PHE THR ARG LYS LEU CYS SER LEU ASP ASN GLY ASP CYS          
SEQRES   5 B   95  ASP GLN PHE CYS HIS GLU GLU GLN ASN SER VAL VAL CYS          
SEQRES   6 B   95  SER CYS ALA ARG GLY TYR THR LEU ALA ASP ASN GLY LYS          
SEQRES   7 B   95  ALA CYS ILE PRO THR GLY PRO TYR PRO CYS GLY LYS GLN          
SEQRES   8 B   95  THR LEU GLU ARG                                              
SEQRES   1 D  235  ILE VAL GLY GLY GLN GLU CYS LYS ASP GLY GLU CYS PRO          
SEQRES   2 D  235  TRP GLN ALA LEU LEU ILE ASN GLU GLU ASN GLU GLY PHE          
SEQRES   3 D  235  CYS GLY GLY THR ILE LEU SER GLU PHE TYR ILE LEU THR          
SEQRES   4 D  235  ALA ALA HIS CYS LEU TYR GLN ALA LYS ARG PHE LYS VAL          
SEQRES   5 D  235  ARG VAL GLY ASP ARG ASN THR GLU GLN GLU GLU GLY GLY          
SEQRES   6 D  235  GLU ALA VAL HIS GLU VAL GLU VAL VAL ILE LYS HIS ASN          
SEQRES   7 D  235  ARG PHE THR LYS GLU THR TYR ASP PHE ASP ILE ALA VAL          
SEQRES   8 D  235  LEU ARG LEU LYS THR PRO ILE THR PHE ARG MET ASN VAL          
SEQRES   9 D  235  ALA PRO ALA CYS LEU PRO GLU ARG ASP TRP ALA GLU SER          
SEQRES  10 D  235  THR LEU MET THR GLN LYS THR GLY ILE VAL SER GLY PHE          
SEQRES  11 D  235  GLY ARG THR HIS GLU LYS GLY ARG GLN SER THR ARG LEU          
SEQRES  12 D  235  LYS MET LEU GLU VAL PRO TYR VAL ASP ARG ASN SER CYS          
SEQRES  13 D  235  LYS LEU SER SER SER PHE ILE ILE THR GLN ASN MET PHE          
SEQRES  14 D  235  CYS ALA GLY TYR ASP THR LYS GLN GLU ASP ALA CYS GLN          
SEQRES  15 D  235  GLY ASP SER GLY GLY PRO HIS VAL THR ARG PHE LYS ASP          
SEQRES  16 D  235  THR TYR PHE VAL THR GLY ILE VAL SER TRP GLY GLU GLY          
SEQRES  17 D  235  CYS ALA ARG LYS GLY LYS TYR GLY ILE TYR THR LYS VAL          
SEQRES  18 D  235  THR ALA PHE LEU LYS TRP ILE ASP ARG SER MET LYS THR          
SEQRES  19 D  235  ARG                                                          
MODRES 1XKB BHD A   63  ASP  (3S)-3-HYDROXY-L-ASPARTIC ACID                     
MODRES 1XKB BHD B   63  ASP  (3S)-3-HYDROXY-L-ASPARTIC ACID                     
HET    BHD  A  63       9                                                       
HET    BHD  B  63       9                                                       
HET     CA  A 501       1                                                       
HET     CA  D 502       1                                                       
HET     CA  C 503       1                                                       
HET    4PP  C 998      29                                                       
HET    4PP  D 999      29                                                       
HETNAM     BHD (3S)-3-HYDROXY-L-ASPARTIC ACID                                   
HETNAM      CA CALCIUM ION                                                      
HETNAM     4PP (2S)-(3'-AMIDINO-3-BIPHENYL)-5-(4-PYRIDYLAMINO)                  
HETNAM   2 4PP  PENTANOIC ACID                                                  
HETSYN     BHD BETA-HYDROXYASPARTIC ACID                                        
FORMUL   1  BHD    2(C4 H7 N O5)                                                
FORMUL   5   CA    3(CA 2+)                                                     
FORMUL   8  4PP    2(C23 H24 N4 O2)                                             
FORMUL  10  HOH   *299(H2 O)                                                    
HELIX    1   1 ASP A   92  ASP A   95  5                                   4    
HELIX    2   2 ALA C   56  TYR C   60  5                                   5    
HELIX    3   3 ARG C  125  THR C  131  1                                   7    
HELIX    4   4 ARG C  165  SER C  171  1                                   7    
HELIX    5   5 VAL C  231  ALA C  233  5                                   3    
HELIX    6   6 LEU C  235  SER C  241  1                                   7    
HELIX    7   7 ASP B   92  ASP B   95  5                                   4    
HELIX    8   8 ALA D   56  TYR D   60  5                                   5    
HELIX    9   9 ARG D  125  THR D  131  1                                   7    
HELIX   10  10 ARG D  165  SER D  171  1                                   7    
HELIX   11  11 VAL D  231  ALA D  233  5                                   3    
HELIX   12  12 LEU D  235  SER D  241  1                                   7    
SHEET    1   A 2 PHE A  99  GLU A 102  0                                        
SHEET    2   A 2 VAL A 107  SER A 110 -1  N  SER A 110   O  PHE A  99           
SHEET    1   B 2 TYR A 115  LEU A 117  0                                        
SHEET    2   B 2 CYS A 124  PRO A 126 -1  N  ILE A 125   O  THR A 116           
SHEET    1   C 4 ALA C  81  GLU C  84  0                                        
SHEET    2   C 4 LYS C  65  VAL C  68 -1  N  VAL C  68   O  ALA C  81           
SHEET    3   C 4 GLN C  30  ILE C  34 -1  N  ILE C  34   O  LYS C  65           
SHEET    4   C 4 GLY C  40  THR C  45 -1  N  GLY C  44   O  ALA C  31           
SHEET    1   D 3 TYR C  51  THR C  54  0                                        
SHEET    2   D 3 ALA C 104  LEU C 108 -1  N  LEU C 106   O  ILE C  52           
SHEET    3   D 3 VAL C  85  LYS C  90 -1  N  ILE C  89   O  VAL C 105           
SHEET    1   E 2 THR C 135  GLY C 140  0                                        
SHEET    2   E 2 LYS C 156  PRO C 161 -1  N  VAL C 160   O  GLY C 136           
SHEET    1   F 4 MET C 180  ALA C 183  0                                        
SHEET    2   F 4 GLY C 226  LYS C 230 -1  N  TYR C 228   O  PHE C 181           
SHEET    3   F 4 THR C 206  GLY C 216 -1  N  TRP C 215   O  ILE C 227           
SHEET    4   F 4 PRO C 198  PHE C 203 -1  N  PHE C 203   O  THR C 206           
SHEET    1   G 2 PHE B  99  GLU B 103  0                                        
SHEET    2   G 2 SER B 106  SER B 110 -1  N  SER B 110   O  PHE B  99           
SHEET    1   H 2 TYR B 115  LEU B 117  0                                        
SHEET    2   H 2 CYS B 124  PRO B 126 -1  N  ILE B 125   O  THR B 116           
SHEET    1   I 4 ALA D  81  HIS D  83  0                                        
SHEET    2   I 4 LYS D  65  VAL D  68 -1  N  VAL D  68   O  ALA D  81           
SHEET    3   I 4 GLN D  30  ILE D  34 -1  N  ILE D  34   O  LYS D  65           
SHEET    4   I 4 GLY D  40  THR D  45 -1  N  GLY D  44   O  ALA D  31           
SHEET    1   J 3 TYR D  51  THR D  54  0                                        
SHEET    2   J 3 ALA D 104  LEU D 108 -1  N  LEU D 106   O  ILE D  52           
SHEET    3   J 3 VAL D  85  LYS D  90 -1  N  ILE D  89   O  VAL D 105           
SHEET    1   K 2 THR D 135  GLY D 140  0                                        
SHEET    2   K 2 LYS D 156  PRO D 161 -1  N  VAL D 160   O  GLY D 136           
SHEET    1   L 4 MET D 180  ALA D 183  0                                        
SHEET    2   L 4 GLY D 226  LYS D 230 -1  N  TYR D 228   O  PHE D 181           
SHEET    3   L 4 THR D 206  GLY D 216 -1  N  TRP D 215   O  ILE D 227           
SHEET    4   L 4 PRO D 198  PHE D 203 -1  N  PHE D 203   O  THR D 206           
SSBOND   1 CYS A   50    CYS A   61                          1555   1555  2.04  
SSBOND   2 CYS A   55    CYS A   70                          1555   1555  2.03  
SSBOND   3 CYS A   72    CYS A   81                          1555   1555  2.02  
SSBOND   4 CYS A   89    CYS A  100                          1555   1555  2.04  
SSBOND   5 CYS A   96    CYS A  109                          1555   1555  2.03  
SSBOND   6 CYS A  111    CYS A  124                          1555   1555  2.03  
SSBOND   7 CYS A  132    CYS C  122                          1555   1555  2.03  
SSBOND   8 CYS C   22    CYS C   27                          1555   1555  2.03  
SSBOND   9 CYS C   42    CYS C   58                          1555   1555  2.02  
SSBOND  10 CYS C  168    CYS C  182                          1555   1555  2.02  
SSBOND  11 CYS C  191    CYS C  220                          1555   1555  2.03  
SSBOND  12 CYS B   50    CYS B   61                          1555   1555  2.05  
SSBOND  13 CYS B   55    CYS B   70                          1555   1555  2.03  
SSBOND  14 CYS B   72    CYS B   81                          1555   1555  2.03  
SSBOND  15 CYS B   89    CYS B  100                          1555   1555  2.03  
SSBOND  16 CYS B   96    CYS B  109                          1555   1555  2.03  
SSBOND  17 CYS B  111    CYS B  124                          1555   1555  2.03  
SSBOND  18 CYS B  132    CYS D  122                          1555   1555  2.03  
SSBOND  19 CYS D   22    CYS D   27                          1555   1555  2.03  
SSBOND  20 CYS D   42    CYS D   58                          1555   1555  2.02  
SSBOND  21 CYS D  168    CYS D  182                          1555   1555  2.03  
SSBOND  22 CYS D  191    CYS D  220                          1555   1555  2.03  
LINK         N   BHD A  63                 C   LYS A  62     1555   1555  1.33  
LINK         C   BHD A  63                 N   GLY A  64     1555   1555  1.31  
LINK         N   BHD B  63                 C   LYS B  62     1555   1555  1.33  
LINK         C   BHD B  63                 N   GLY B  64     1555   1555  1.31  
LINK        CA    CA A 501                 OD1 BHD A  63     1555   1555  2.98  
LINK        CA    CA A 501                 OD2 BHD A  63     1555   1555  3.27  
LINK        CA    CA A 501                 O   GLY A  64     1555   1555  3.26  
LINK        CA    CA A 501                 OE1 GLN A  49     1555   1555  2.89  
LINK        CA    CA A 501                 O   LEU A  65     1555   1555  2.83  
LINK        CA    CA C 503                 OE1 GLU C  76     1555   1555  3.15  
LINK        CA    CA C 503                 OE2 GLU C  80     1555   1555  2.85  
LINK        CA    CA C 503                 O   ASN C  72     1555   1555  2.61  
LINK        CA    CA C 503                 O   GLN C  75     1555   1555  2.89  
LINK        CA    CA C 503                 OE1 GLU C  77     1555   1555  3.18  
LINK        CA    CA C 503                 OE2 GLU C  77     1555   1555  2.85  
LINK        CA    CA C 503                 OE1 GLU C  80     1555   1555  3.17  
LINK        CA    CA C 503                 OD1 ASP C  70     1555   1555  2.53  
LINK        CA    CA D 502                 OD1 ASP D  70     1555   1555  2.62  
LINK        CA    CA D 502                 O   ASN D  72     1555   1555  2.93  
LINK        CA    CA D 502                 OE2 GLU D  77     1555   1555  2.97  
LINK        CA    CA D 502                 OE1 GLU D  80     1555   1555  2.65  
LINK        CA    CA D 502                 O   GLN D  75     1555   1555  2.55  
SITE     1 AC1  5 GLN A  49  BHD A  63  GLY A  64  LEU A  65                    
SITE     2 AC1  5 GLY A  66                                                     
SITE     1 AC2  5 ASP D  70  ASN D  72  GLN D  75  GLU D  77                    
SITE     2 AC2  5 GLU D  80                                                     
SITE     1 AC3  6 ASP C  70  ASN C  72  GLN C  75  GLU C  76                    
SITE     2 AC3  6 GLU C  77  GLU C  80                                          
SITE     1 AC4 17 GLU C  97  THR C  98  TYR C  99  PHE C 174                    
SITE     2 AC4 17 ASP C 189  ALA C 190  CYS C 191  GLN C 192                    
SITE     3 AC4 17 SER C 195  VAL C 213  GLY C 216  GLY C 218                    
SITE     4 AC4 17 GLY C 226  HOH C 558  HOH C 561  HOH C 790                    
SITE     5 AC4 17 HOH C 794                                                     
SITE     1 AC5 18 GLU D  97  THR D  98  TYR D  99  PHE D 174                    
SITE     2 AC5 18 ASP D 189  ALA D 190  CYS D 191  GLN D 192                    
SITE     3 AC5 18 SER D 195  VAL D 213  TRP D 215  GLY D 216                    
SITE     4 AC5 18 GLY D 218  GLY D 226  HOH D 647  HOH D 650                    
SITE     5 AC5 18 HOH D 670  HOH D 672                                          
CRYST1   58.270  105.220   63.240  90.00 103.40  90.00 P 1 21 1      4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.017161  0.000000  0.004088        0.00000                         
SCALE2      0.000000  0.009504  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.016255        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system