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Database: PDB
Entry: 3LC3
LinkDB: 3LC3
Original site: 3LC3 
HEADER    HYDROLASE/HYDROLASE INHIBITOR           09-JAN-10   3LC3              
TITLE     BENZOTHIOPHENE INHIBITORS OF FACTOR IXA                               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: COAGULATION FACTOR IX;                                     
COMPND   3 CHAIN: A, C;                                                         
COMPND   4 FRAGMENT: RESIDUES 227-461;                                          
COMPND   5 SYNONYM: CHRISTMAS FACTOR, PLASMA THROMBOPLASTIN COMPONENT,          
COMPND   6 PTC, COAGULATION FACTOR IXA LIGHT CHAIN, COAGULATION FACTOR          
COMPND   7 IXA HEAVY CHAIN;                                                     
COMPND   8 EC: 3.4.21.22;                                                       
COMPND   9 ENGINEERED: YES;                                                     
COMPND  10 MOL_ID: 2;                                                           
COMPND  11 MOLECULE: COAGULATION FACTOR IX;                                     
COMPND  12 CHAIN: B, D;                                                         
COMPND  13 FRAGMENT: RESIDUES 133-188;                                          
COMPND  14 SYNONYM: CHRISTMAS FACTOR, PLASMA THROMBOPLASTIN COMPONENT,          
COMPND  15 PTC, COAGULATION FACTOR IXA LIGHT CHAIN, COAGULATION FACTOR          
COMPND  16 IXA HEAVY CHAIN;                                                     
COMPND  17 EC: 3.4.21.22;                                                       
COMPND  18 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: F9;                                                            
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  10 ORGANISM_COMMON: HUMAN;                                              
SOURCE  11 ORGANISM_TAXID: 9606;                                                
SOURCE  12 GENE: F9;                                                            
SOURCE  13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    PROTEIN-INHIBITOR COMPLEX, PEPTIDASE S1, BLOOD COAGULATION,           
KEYWDS   2 CALCIUM, CLEAVAGE ON PAIR OF BASIC RESIDUES, DISEASE                 
KEYWDS   3 MUTATION, DISULFIDE BOND, EGF-LIKE DOMAIN, GAMMA-                    
KEYWDS   4 CARBOXYGLUTAMIC ACID, GLYCOPROTEIN, HEMOPHILIA, HYDROLASE,           
KEYWDS   5 HYDROXYLATION, PHARMACEUTICAL, PHOSPHOPROTEIN,                       
KEYWDS   6 POLYMORPHISM, PROTEASE, SECRETED, SERINE PROTEASE,                   
KEYWDS   7 SULFATION, ZYMOGEN, HYDROLASE-HYDROLASE INHIBITOR COMPLEX            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.WANG,R.BECK                                                         
REVDAT   2   02-MAR-10 3LC3    1       JRNL                                     
REVDAT   1   23-FEB-10 3LC3    0                                                
JRNL        AUTH   S.WANG,R.BECK,T.BLENCH,A.BURD,S.BUXTON,M.MALIC,              
JRNL        AUTH 2 T.AYELE,S.SHAIKH,S.CHAHWALA,C.CHANDER,R.HOLLAND,             
JRNL        AUTH 3 S.MERETTE,L.ZHAO,M.BLACKNEY,A.WATTS                          
JRNL        TITL   STUDIES OF BENZOTHIOPHENE TEMPLATE AS POTENT FACTOR          
JRNL        TITL 2 IXA (FIXA) INHIBITORS IN THROMBOSIS.                         
JRNL        REF    J.MED.CHEM.                   V.  53  1465 2010              
JRNL        REFN                   ISSN 0022-2623                               
JRNL        PMID   20121198                                                     
JRNL        DOI    10.1021/JM901475E                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0003                                      
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) : 1.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 67.42                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 41605                          
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) : 0.199                           
REMARK   3   R VALUE            (WORKING SET) : 0.197                           
REMARK   3   FREE R VALUE                     : 0.260                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1754                            
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) : 1.90                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.95                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3016                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 96.66                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2080                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 137                          
REMARK   3   BIN FREE R VALUE                    : 0.2730                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4548                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 90                                      
REMARK   3   SOLVENT ATOMS            : 420                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 27.40                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 31.42                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.47000                                             
REMARK   3    B22 (A**2) : 1.06000                                              
REMARK   3    B33 (A**2) : -0.59000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.02000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.185         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.176         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.117         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.844         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.945                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.905                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4756 ; 0.013 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  4172 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  6452 ; 1.481 ; 1.952       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  9714 ; 0.836 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   580 ; 6.940 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   208 ;35.509 ;24.231       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   788 ;15.960 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    24 ;14.439 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   690 ; 0.094 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  5306 ; 0.005 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   988 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1008 ; 0.209 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  4440 ; 0.187 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  2324 ; 0.181 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  2803 ; 0.086 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   351 ; 0.162 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):     1 ; 0.029 ; 0.200       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):     2 ; 0.067 ; 0.200       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    40 ; 0.272 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):   112 ; 0.176 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    19 ; 0.146 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):     8 ; 0.111 ; 0.200       
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):  2978 ; 0.996 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  1210 ; 0.203 ; 1.500       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4664 ; 1.598 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2120 ; 2.064 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1788 ; 3.007 ; 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: HYDROGENS HAVE BEEN ADDED IN THE          
REMARK   3  RIDING POSITIONS                                                    
REMARK   4                                                                      
REMARK   4 3LC3 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-JAN-10.                  
REMARK 100 THE RCSB ID CODE IS RCSB057093.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SRS                                
REMARK 200  BEAMLINE                       : PX9.6                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.03320                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MAR CCD 130 MM                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 43359                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 67.420                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
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  : 5.4000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.95                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.7                               
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         : 2.200                              
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: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 44.04                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
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       48.01750            
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                                                    
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: 1690 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13830 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -21.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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: 1720 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13930 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -21.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, 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 475                                                                      
REMARK 475 ZERO OCCUPANCY RESIDUES                                              
REMARK 475 THE FOLLOWING RESIDUES WERE MODELED WITH ZERO OCCUPANCY.             
REMARK 475 THE LOCATION AND PROPERTIES OF THESE RESIDUES MAY NOT                
REMARK 475 BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;                      
REMARK 475 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE)          
REMARK 475   M RES C SSEQI                                                      
REMARK 475     THR B  140                                                       
REMARK 475     SER B  141                                                       
REMARK 475     LYS B  142                                                       
REMARK 475     THR D  140                                                       
REMARK 475     SER D  141                                                       
REMARK 475     LYS D  142                                                       
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     LYS A   36   CD    CE    NZ                                      
REMARK 480     ARG A  150   CZ    NH1   NH2                                     
REMARK 480     TYR A  177   CD1   CD2   CE1   CE2   CZ    OH                    
REMARK 480     ASN A  178   CG    OD1   ND2                                     
REMARK 480     MET B   86   CG    SD    CE                                      
REMARK 480     LYS B   91   CD    CE    NZ                                      
REMARK 480     ARG B   94   CG    CD    NE    CZ    NH1   NH2                   
REMARK 480     LYS B  100   CG    CD    CE    NZ                                
REMARK 480     ASP B  104   CG    OD1   OD2                                     
REMARK 480     ASN B  105   CG    OD1   ND2                                     
REMARK 480     LYS B  106   CG    CD    CE    NZ                                
REMARK 480     VAL B  107   CG1   CG2                                           
REMARK 480     VAL B  108   CG1   CG2                                           
REMARK 480     GLU B  119   CG    CD    OE1   OE2                               
REMARK 480     GLU B  125   CG    CD    OE1   OE2                               
REMARK 480     LYS C   36   CD    CE    NZ                                      
REMARK 480     ARG C  150   CZ    NH1   NH2                                     
REMARK 480     TYR C  177   CD1   CD2   CE1   CE2   CZ    OH                    
REMARK 480     ASN C  178   CG    OD1   ND2                                     
REMARK 480     MET D   86   CG    SD    CE                                      
REMARK 480     LYS D   91   CD    CE    NZ                                      
REMARK 480     ARG D   94   CG    CD    NE    CZ    NH1   NH2                   
REMARK 480     LYS D  100   CG    CD    CE    NZ                                
REMARK 480     ASP D  104   CG    OD1   OD2                                     
REMARK 480     ASN D  105   CG    OD1   ND2                                     
REMARK 480     LYS D  106   CG    CD    CE    NZ                                
REMARK 480     VAL D  107   CG1   CG2                                           
REMARK 480     VAL D  108   CG1   CG2                                           
REMARK 480     GLU D  119   CG    CD    OE1   OE2                               
REMARK 480     GLU D  125   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   NZ   LYS C    23     O    GLN D   139              2.10            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ASP A  39   CB  -  CG  -  OD2 ANGL. DEV. =   6.4 DEGREES          
REMARK 500    ASP A 125   CB  -  CG  -  OD2 ANGL. DEV. =   6.1 DEGREES          
REMARK 500    ASP C  39   CB  -  CG  -  OD2 ANGL. DEV. =   5.6 DEGREES          
REMARK 500    ASP C 125   CB  -  CG  -  OD2 ANGL. DEV. =   8.3 DEGREES          
REMARK 500    ASP D 104   CB  -  CG  -  OD2 ANGL. DEV. =   5.4 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    LYS A  63       68.20      1.75                                   
REMARK 500    HIS A  71      -65.39   -137.28                                   
REMARK 500    LYS A 148       19.20     55.53                                   
REMARK 500    SER A 214      -72.92   -117.68                                   
REMARK 500    GLU A 217     -149.44    -99.03                                   
REMARK 500    GLN B  97      -85.35   -111.66                                   
REMARK 500    ASP B 104      -81.37     59.40                                   
REMARK 500    ASN B 105       73.64    -68.23                                   
REMARK 500    LYS B 106     -161.80    -77.31                                   
REMARK 500    VAL B 107      108.51     75.03                                   
REMARK 500    ASN B 120      -11.87    -48.92                                   
REMARK 500    SER B 141      -83.21   -107.05                                   
REMARK 500    HIS C  71      -62.14   -135.42                                   
REMARK 500    SER C 214      -70.61   -118.81                                   
REMARK 500    GLU C 217     -150.58   -101.76                                   
REMARK 500    LYS D  91       44.93     39.76                                   
REMARK 500    GLN D  97      -83.92   -109.55                                   
REMARK 500    ALA D 103       94.03    -52.60                                   
REMARK 500    ASP D 104      -51.01     71.78                                   
REMARK 500    LYS D 106     -172.38     43.23                                   
REMARK 500    VAL D 107       98.01     73.45                                   
REMARK 500    ASN D 120      -49.32    -28.88                                   
REMARK 500    LYS D 122      -51.63   -129.28                                   
REMARK 500    SER D 141      -94.52   -124.92                                   
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 246  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A  75   O                                                      
REMARK 620 2 ASN A  72   O    82.2                                              
REMARK 620 3 GLU A  70   OE1 154.6  86.9                                        
REMARK 620 4 GLU A  80   OE2  94.0 166.4 101.5                                  
REMARK 620 5 GLU A  77   OE1 122.7  90.3  80.1  80.7                            
REMARK 620 6 GLU A  77   OE2  72.5  84.2 129.2  82.3  50.2                      
REMARK 620 7 HOH A   6   O    82.0  99.3  77.3  93.0 154.8 153.5                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA C 246  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN C  72   O                                                      
REMARK 620 2 GLU C  75   O    80.7                                              
REMARK 620 3 GLU C  70   OE1  87.5 154.2                                        
REMARK 620 4 GLU C  80   OE2 170.4  97.0  98.2                                  
REMARK 620 5 GLU C  77   OE1  87.3 122.8  79.1  86.2                            
REMARK 620 6 GLU C  77   OE2  86.6  72.1 130.3  83.8  51.4                      
REMARK 620 7 HOH C 400   O    98.2  83.5  75.6  90.8 153.7 154.0                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IYX A 1                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IYX A 2                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 246                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IYX C 1                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IYX C 2                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 246                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3LC5   RELATED DB: PDB                                   
DBREF  3LC3 A   16   245  UNP    P00740   FA9_HUMAN      227    461             
DBREF  3LC3 B   87   142  UNP    P00740   FA9_HUMAN      133    188             
DBREF  3LC3 C   16   245  UNP    P00740   FA9_HUMAN      227    461             
DBREF  3LC3 D   87   142  UNP    P00740   FA9_HUMAN      133    188             
SEQADV 3LC3 MET B   86  UNP  P00740              INITIATING METHIONINE          
SEQADV 3LC3 MET D   86  UNP  P00740              INITIATING METHIONINE          
SEQRES   1 A  235  VAL VAL GLY GLY GLU ASP ALA LYS PRO GLY GLN PHE PRO          
SEQRES   2 A  235  TRP GLN VAL VAL LEU ASN GLY LYS VAL ASP ALA PHE CYS          
SEQRES   3 A  235  GLY GLY SER ILE VAL ASN GLU LYS TRP ILE VAL THR ALA          
SEQRES   4 A  235  ALA HIS CYS VAL GLU THR GLY VAL LYS ILE THR VAL VAL          
SEQRES   5 A  235  ALA GLY GLU HIS ASN ILE GLU GLU THR GLU HIS THR GLU          
SEQRES   6 A  235  GLN LYS ARG ASN VAL ILE ARG ILE ILE PRO HIS HIS ASN          
SEQRES   7 A  235  TYR ASN ALA ALA ILE ASN LYS TYR ASN HIS ASP ILE ALA          
SEQRES   8 A  235  LEU LEU GLU LEU ASP GLU PRO LEU VAL LEU ASN SER TYR          
SEQRES   9 A  235  VAL THR PRO ILE CYS ILE ALA ASP LYS GLU TYR THR ASN          
SEQRES  10 A  235  ILE PHE LEU LYS PHE GLY SER GLY TYR VAL SER GLY TRP          
SEQRES  11 A  235  GLY ARG VAL PHE HIS LYS GLY ARG SER ALA LEU VAL LEU          
SEQRES  12 A  235  GLN TYR LEU ARG VAL PRO LEU VAL ASP ARG ALA THR CYS          
SEQRES  13 A  235  LEU ARG SER THR LYS PHE THR ILE TYR ASN ASN MET PHE          
SEQRES  14 A  235  CYS ALA GLY PHE HIS GLU GLY GLY ARG ASP SER CYS GLN          
SEQRES  15 A  235  GLY ASP SER GLY GLY PRO HIS VAL THR GLU VAL GLU GLY          
SEQRES  16 A  235  THR SER PHE LEU THR GLY ILE ILE SER TRP GLY GLU GLU          
SEQRES  17 A  235  CYS ALA MET LYS GLY LYS TYR GLY ILE TYR THR LYS VAL          
SEQRES  18 A  235  SER ARG TYR VAL ASN TRP ILE LYS GLU LYS THR LYS LEU          
SEQRES  19 A  235  THR                                                          
SEQRES   1 B   57  MET THR CYS ASN ILE LYS ASN GLY ARG CYS GLU GLN PHE          
SEQRES   2 B   57  CYS LYS ASN SER ALA ASP ASN LYS VAL VAL CYS SER CYS          
SEQRES   3 B   57  THR GLU GLY TYR ARG LEU ALA GLU ASN GLN LYS SER CYS          
SEQRES   4 B   57  GLU PRO ALA VAL PRO PHE PRO CYS GLY ARG VAL SER VAL          
SEQRES   5 B   57  SER GLN THR SER LYS                                          
SEQRES   1 C  235  VAL VAL GLY GLY GLU ASP ALA LYS PRO GLY GLN PHE PRO          
SEQRES   2 C  235  TRP GLN VAL VAL LEU ASN GLY LYS VAL ASP ALA PHE CYS          
SEQRES   3 C  235  GLY GLY SER ILE VAL ASN GLU LYS TRP ILE VAL THR ALA          
SEQRES   4 C  235  ALA HIS CYS VAL GLU THR GLY VAL LYS ILE THR VAL VAL          
SEQRES   5 C  235  ALA GLY GLU HIS ASN ILE GLU GLU THR GLU HIS THR GLU          
SEQRES   6 C  235  GLN LYS ARG ASN VAL ILE ARG ILE ILE PRO HIS HIS ASN          
SEQRES   7 C  235  TYR ASN ALA ALA ILE ASN LYS TYR ASN HIS ASP ILE ALA          
SEQRES   8 C  235  LEU LEU GLU LEU ASP GLU PRO LEU VAL LEU ASN SER TYR          
SEQRES   9 C  235  VAL THR PRO ILE CYS ILE ALA ASP LYS GLU TYR THR ASN          
SEQRES  10 C  235  ILE PHE LEU LYS PHE GLY SER GLY TYR VAL SER GLY TRP          
SEQRES  11 C  235  GLY ARG VAL PHE HIS LYS GLY ARG SER ALA LEU VAL LEU          
SEQRES  12 C  235  GLN TYR LEU ARG VAL PRO LEU VAL ASP ARG ALA THR CYS          
SEQRES  13 C  235  LEU ARG SER THR LYS PHE THR ILE TYR ASN ASN MET PHE          
SEQRES  14 C  235  CYS ALA GLY PHE HIS GLU GLY GLY ARG ASP SER CYS GLN          
SEQRES  15 C  235  GLY ASP SER GLY GLY PRO HIS VAL THR GLU VAL GLU GLY          
SEQRES  16 C  235  THR SER PHE LEU THR GLY ILE ILE SER TRP GLY GLU GLU          
SEQRES  17 C  235  CYS ALA MET LYS GLY LYS TYR GLY ILE TYR THR LYS VAL          
SEQRES  18 C  235  SER ARG TYR VAL ASN TRP ILE LYS GLU LYS THR LYS LEU          
SEQRES  19 C  235  THR                                                          
SEQRES   1 D   57  MET THR CYS ASN ILE LYS ASN GLY ARG CYS GLU GLN PHE          
SEQRES   2 D   57  CYS LYS ASN SER ALA ASP ASN LYS VAL VAL CYS SER CYS          
SEQRES   3 D   57  THR GLU GLY TYR ARG LEU ALA GLU ASN GLN LYS SER CYS          
SEQRES   4 D   57  GLU PRO ALA VAL PRO PHE PRO CYS GLY ARG VAL SER VAL          
SEQRES   5 D   57  SER GLN THR SER LYS                                          
HET    IYX  A   1      22                                                       
HET    IYX  A   2      22                                                       
HET     CA  A 246       1                                                       
HET    IYX  C   1      22                                                       
HET    IYX  C   2      22                                                       
HET     CA  C 246       1                                                       
HETNAM     IYX 1-[5-(3,4-DIMETHOXYPHENYL)-1-BENZOTHIOPHEN-2-                    
HETNAM   2 IYX  YL]METHANEDIAMINE                                               
HETNAM      CA CALCIUM ION                                                      
FORMUL   5  IYX    4(C17 H18 N2 O2 S)                                           
FORMUL   7   CA    2(CA 2+)                                                     
FORMUL  11  HOH   *420(H2 O)                                                    
HELIX    1   1 ALA A   55  VAL A   59  5                                   5    
HELIX    2   2 ASP A  125  PHE A  133  1                                  11    
HELIX    3   3 ASP A  164  SER A  171  1                                   8    
HELIX    4   4 TYR A  234  THR A  242  1                                   9    
HELIX    5   5 ILE B   90  CYS B   95  5                                   6    
HELIX    6   6 ALA C   55  VAL C   59  5                                   5    
HELIX    7   7 ASP C  125  PHE C  133  1                                  11    
HELIX    8   8 ASP C  164  SER C  171  1                                   8    
HELIX    9   9 TYR C  234  THR C  242  1                                   9    
HELIX   10  10 ILE D   90  CYS D   95  5                                   6    
SHEET    1   A 8 GLU A  20  ASP A  21  0                                        
SHEET    2   A 8 GLN A 156  VAL A 163 -1  O  TYR A 157   N  GLU A  20           
SHEET    3   A 8 MET A 180  ALA A 183 -1  O  CYS A 182   N  VAL A 163           
SHEET    4   A 8 GLY A 226  LYS A 230 -1  O  TYR A 228   N  PHE A 181           
SHEET    5   A 8 THR A 206  TRP A 215 -1  N  TRP A 215   O  ILE A 227           
SHEET    6   A 8 PRO A 198  VAL A 203 -1  N  VAL A 203   O  THR A 206           
SHEET    7   A 8 SER A 135  GLY A 140 -1  N  TYR A 137   O  VAL A 200           
SHEET    8   A 8 GLN A 156  VAL A 163 -1  O  VAL A 160   N  GLY A 136           
SHEET    1   B 7 GLN A  30  ASN A  34  0                                        
SHEET    2   B 7 CYS A  42  ASN A  48 -1  O  CYS A  42   N  LEU A  33           
SHEET    3   B 7 TRP A  51  THR A  54 -1  O  VAL A  53   N  SER A  45           
SHEET    4   B 7 ALA A 104  LEU A 108 -1  O  LEU A 106   N  ILE A  52           
SHEET    5   B 7 GLN A  81  PRO A  90 -1  N  ARG A  87   O  GLU A 107           
SHEET    6   B 7 THR A  65  ALA A  68 -1  N  ALA A  68   O  GLN A  81           
SHEET    7   B 7 GLN A  30  ASN A  34 -1  N  ASN A  34   O  THR A  65           
SHEET    1   C 2 PHE B  98  LYS B 100  0                                        
SHEET    2   C 2 VAL B 108  SER B 110 -1  O  SER B 110   N  PHE B  98           
SHEET    1   D 2 TYR B 115  LEU B 117  0                                        
SHEET    2   D 2 CYS B 124  PRO B 126 -1  O  GLU B 125   N  ARG B 116           
SHEET    1   E 8 GLU C  20  ASP C  21  0                                        
SHEET    2   E 8 GLN C 156  VAL C 163 -1  O  TYR C 157   N  GLU C  20           
SHEET    3   E 8 MET C 180  ALA C 183 -1  O  CYS C 182   N  VAL C 163           
SHEET    4   E 8 GLY C 226  LYS C 230 -1  O  TYR C 228   N  PHE C 181           
SHEET    5   E 8 THR C 206  TRP C 215 -1  N  TRP C 215   O  ILE C 227           
SHEET    6   E 8 PRO C 198  VAL C 203 -1  N  VAL C 203   O  THR C 206           
SHEET    7   E 8 SER C 135  GLY C 140 -1  N  TYR C 137   O  VAL C 200           
SHEET    8   E 8 GLN C 156  VAL C 163 -1  O  VAL C 160   N  GLY C 136           
SHEET    1   F 7 GLN C  30  ASN C  34  0                                        
SHEET    2   F 7 CYS C  42  ASN C  48 -1  O  CYS C  42   N  LEU C  33           
SHEET    3   F 7 TRP C  51  THR C  54 -1  O  TRP C  51   N  VAL C  47           
SHEET    4   F 7 ALA C 104  LEU C 108 -1  O  ALA C 104   N  THR C  54           
SHEET    5   F 7 GLN C  81  PRO C  90 -1  N  ILE C  89   O  LEU C 105           
SHEET    6   F 7 THR C  65  ALA C  68 -1  N  VAL C  66   O  ARG C  83           
SHEET    7   F 7 GLN C  30  ASN C  34 -1  N  ASN C  34   O  THR C  65           
SHEET    1   G 2 PHE D  98  LYS D 100  0                                        
SHEET    2   G 2 VAL D 108  SER D 110 -1  O  SER D 110   N  PHE D  98           
SHEET    1   H 2 TYR D 115  LEU D 117  0                                        
SHEET    2   H 2 CYS D 124  PRO D 126 -1  O  GLU D 125   N  ARG D 116           
SSBOND   1 CYS A   42    CYS A   58                          1555   1555  2.05  
SSBOND   2 CYS A  122    CYS B  132                          1555   1555  2.06  
SSBOND   3 CYS A  168    CYS A  182                          1555   1555  1.94  
SSBOND   4 CYS A  191    CYS A  220                          1555   1555  2.05  
SSBOND   5 CYS B   88    CYS B   99                          1555   1555  2.03  
SSBOND   6 CYS B   95    CYS B  109                          1555   1555  2.03  
SSBOND   7 CYS B  111    CYS B  124                          1555   1555  2.06  
SSBOND   8 CYS C   42    CYS C   58                          1555   1555  2.02  
SSBOND   9 CYS C  122    CYS D  132                          1555   1555  2.04  
SSBOND  10 CYS C  168    CYS C  182                          1555   1555  1.95  
SSBOND  11 CYS C  191    CYS C  220                          1555   1555  2.07  
SSBOND  12 CYS D   88    CYS D   99                          1555   1555  2.02  
SSBOND  13 CYS D   95    CYS D  109                          1555   1555  2.05  
SSBOND  14 CYS D  111    CYS D  124                          1555   1555  2.06  
LINK         O   GLU A  75                CA    CA A 246     1555   1555  2.27  
LINK         O   ASN C  72                CA    CA C 246     1555   1555  2.28  
LINK         O   GLU C  75                CA    CA C 246     1555   1555  2.30  
LINK         OE1 GLU C  70                CA    CA C 246     1555   1555  2.30  
LINK         OE2 GLU C  80                CA    CA C 246     1555   1555  2.32  
LINK         O   ASN A  72                CA    CA A 246     1555   1555  2.33  
LINK         OE1 GLU A  70                CA    CA A 246     1555   1555  2.33  
LINK         OE2 GLU A  80                CA    CA A 246     1555   1555  2.39  
LINK         OE1 GLU C  77                CA    CA C 246     1555   1555  2.43  
LINK         OE1 GLU A  77                CA    CA A 246     1555   1555  2.45  
LINK         OE2 GLU C  77                CA    CA C 246     1555   1555  2.60  
LINK         OE2 GLU A  77                CA    CA A 246     1555   1555  2.74  
LINK        CA    CA A 246                 O   HOH A   6     1555   1555  2.34  
LINK        CA    CA C 246                 O   HOH C 400     1555   1555  2.38  
SITE     1 AC1 12 IYX A   2  TYR A  99  ASP A 189  SER A 190                    
SITE     2 AC1 12 CYS A 191  GLN A 192  SER A 195  GLY A 216                    
SITE     3 AC1 12 GLU A 217  CYS A 220  GLY A 226  HOH A 351                    
SITE     1 AC2 11 IYX A   1  ASN A  97  LYS A  98  TYR A  99                    
SITE     2 AC2 11 HIS A 147  PHE A 174  TRP A 215  GLY A 216                    
SITE     3 AC2 11 GLU A 217  GLU A 219  HOH C 346                               
SITE     1 AC3  6 HOH A   6  GLU A  70  ASN A  72  GLU A  75                    
SITE     2 AC3  6 GLU A  77  GLU A  80                                          
SITE     1 AC4 10 IYX C   2  TYR C  99  ASP C 189  SER C 190                    
SITE     2 AC4 10 GLN C 192  SER C 195  GLY C 216  GLU C 217                    
SITE     3 AC4 10 CYS C 220  GLY C 226                                          
SITE     1 AC5 13 IYX C   1  ASN C  97  LYS C  98  TYR C  99                    
SITE     2 AC5 13 HIS C 147  PHE C 174  TRP C 215  GLY C 216                    
SITE     3 AC5 13 GLU C 217  GLU C 219  HOH C 344  HOH C 405                    
SITE     4 AC5 13 HOH C 420                                                     
SITE     1 AC6  6 GLU C  70  ASN C  72  GLU C  75  GLU C  77                    
SITE     2 AC6  6 GLU C  80  HOH C 400                                          
CRYST1   66.922   96.035   44.391  90.00  89.93  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      0.014943 -0.000014 -0.000019        0.00000                         
SCALE2      0.000000  0.010413  0.000007        0.00000                         
SCALE3      0.000000  0.000000  0.022527        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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