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Database: PDB
Entry: 2EC9
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HEADER    BLOOD CLOTTING                          13-FEB-07   2EC9              
TITLE     CRYSTAL STRUCTURE ANALYSIS OF HUMAN FACTOR VIIA , SOULUBLE TISSUE     
TITLE    2 FACTOR COMPLEXED WITH BCX-3607                                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: COAGULATION FACTOR VII;                                    
COMPND   3 CHAIN: L;                                                            
COMPND   4 FRAGMENT: RESIDUES 1-142;                                            
COMPND   5 SYNONYM: SERUM PROTHROMBIN CONVERSION ACCELERATOR, SPCA,             
COMPND   6 PROCONVERTIN, EPTACOG ALFA;                                          
COMPND   7 EC: 3.4.21.21;                                                       
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MOL_ID: 2;                                                           
COMPND  10 MOLECULE: COAGULATION FACTOR VII;                                    
COMPND  11 CHAIN: H;                                                            
COMPND  12 FRAGMENT: RESIDUES 16-257;                                           
COMPND  13 SYNONYM: SERUM PROTHROMBIN CONVERSION ACCELERATOR, SPCA,             
COMPND  14 PROCONVERTIN, EPTACOG ALFA;                                          
COMPND  15 EC: 3.4.21.21;                                                       
COMPND  16 ENGINEERED: YES;                                                     
COMPND  17 MOL_ID: 3;                                                           
COMPND  18 MOLECULE: TISSUE FACTOR;                                             
COMPND  19 CHAIN: T;                                                            
COMPND  20 FRAGMENT: RESIDUES 38-112;                                           
COMPND  21 SYNONYM: TF, COAGULATION FACTOR III, THROMBOPLASTIN, CD142 ANTIGEN;  
COMPND  22 ENGINEERED: YES;                                                     
COMPND  23 MOL_ID: 4;                                                           
COMPND  24 MOLECULE: TISSUE FACTOR;                                             
COMPND  25 CHAIN: U;                                                            
COMPND  26 FRAGMENT: RESIDUES 91-210;                                           
COMPND  27 SYNONYM: TF, COAGULATION FACTOR III, THROMBOPLASTIN, CD142 ANTIGEN;  
COMPND  28 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BHK;                                       
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  10 ORGANISM_COMMON: HUMAN;                                              
SOURCE  11 ORGANISM_TAXID: 9606;                                                
SOURCE  12 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  13 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  14 EXPRESSION_SYSTEM_STRAIN: BHK;                                       
SOURCE  15 MOL_ID: 3;                                                           
SOURCE  16 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  17 ORGANISM_COMMON: HUMAN;                                              
SOURCE  18 ORGANISM_TAXID: 9606;                                                
SOURCE  19 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  20 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  21 EXPRESSION_SYSTEM_STRAIN: BHK;                                       
SOURCE  22 MOL_ID: 4;                                                           
SOURCE  23 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  24 ORGANISM_COMMON: HUMAN;                                              
SOURCE  25 ORGANISM_TAXID: 9606;                                                
SOURCE  26 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  27 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  28 EXPRESSION_SYSTEM_STRAIN: BHK                                        
KEYWDS    PROTEIN-COFACTOR COMPLEX, FVIIA AND SOULUBLE TISSUE FACTOR,           
KEYWDS   2 INHIBITOR, BLOOD CLOTTING                                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.RAMAN,B.YARLAGADDA                                                  
REVDAT   4   05-SEP-12 2EC9    1       JRNL                                     
REVDAT   3   13-JUL-11 2EC9    1       VERSN                                    
REVDAT   2   24-FEB-09 2EC9    1       VERSN                                    
REVDAT   1   19-FEB-08 2EC9    0                                                
JRNL        AUTH   R.KRISHNAN,P.L.KOTIAN,P.CHAND,S.BANTIA,S.ROWLAND,Y.S.BABU    
JRNL        TITL   PROBING THE S2 SITE OF FACTOR VIIA TO GENERATE POTENT AND    
JRNL        TITL 2 SELECTIVE INHIBITORS: THE STRUCTURE OF BCX-3607 IN COMPLEX   
JRNL        TITL 3 WITH TISSUE FACTOR-FACTOR VIIA.                              
JRNL        REF    ACTA CRYSTALLOGR.,SECT.D      V.  63   689 2007              
JRNL        REFN                   ISSN 0907-4449                               
JRNL        PMID   17505107                                                     
JRNL        DOI    10.1107/S0907444907014187                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNX                                                  
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 25.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 3.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 42984                          
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) : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.242                           
REMARK   3   FREE R VALUE                     : 0.282                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 4824                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT/AGREEMENT OF MODEL WITH ALL DATA.                               
REMARK   3   R VALUE     (WORKING + TEST SET, NO CUTOFF) : NULL                 
REMARK   3   R VALUE            (WORKING SET, NO CUTOFF) : NULL                 
REMARK   3   FREE R VALUE                    (NO CUTOFF) : NULL                 
REMARK   3   FREE R VALUE TEST SET SIZE   (%, NO CUTOFF) : NULL                 
REMARK   3   FREE R VALUE TEST SET COUNT     (NO CUTOFF) : NULL                 
REMARK   3   ESTIMATED ERROR OF FREE R VALUE (NO CUTOFF) : NULL                 
REMARK   3   TOTAL NUMBER OF REFLECTIONS     (NO CUTOFF) : 48596                
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4663                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 65                                      
REMARK   3   SOLVENT ATOMS            : 224                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 39.00                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.006                           
REMARK   3   BOND ANGLES            (DEGREES) : NULL                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.83                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : ISOTROPIC                                 
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : NULL                                                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2EC9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 27-FEB-07.                  
REMARK 100 THE RCSB ID CODE IS RCSB026490.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 12-SEP-04                          
REMARK 200  TEMPERATURE           (KELVIN) : 98                                 
REMARK 200  PH                             : 6.5                                
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 RU200                       
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : OSMIC MIRRORS                      
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : D*TREK                             
REMARK 200  DATA SCALING SOFTWARE          : CRYSTALCLEAR                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 47808                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 25.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.500                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 88.0                               
REMARK 200  DATA REDUNDANCY                : 4.200                              
REMARK 200  R MERGE                    (I) : 0.07900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.9000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.07                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.20                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.35700                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.200                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: CNX                                                   
REMARK 200 STARTING MODEL: 1DAN                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 53.74                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.66                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 14% (W/V)PEG 4K, 0.1M MGCL2, 0.1M ADA    
REMARK 280  BUFFER, PH 6.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       34.89000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       62.67500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       40.70500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       62.67500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       34.89000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       40.70500            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA,PQS                                              
REMARK 350 TOTAL BURIED SURFACE AREA: 10500 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 27200 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -115.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: L, H, T, U                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     LYS U   159                                                      
REMARK 465     SER U   160                                                      
REMARK 465     SER U   161                                                      
REMARK 465     SER U   162                                                      
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   NH1  ARG L   113     OE2  GLU H   125              2.15            
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    HIS H 199   N   -  CA  -  C   ANGL. DEV. = -20.2 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    PHE L   4      118.00      5.90                                   
REMARK 500    LEU L   5      -19.12    101.92                                   
REMARK 500    SER L  12      111.48   -165.00                                   
REMARK 500    ARG L  15     -100.55    -62.18                                   
REMARK 500    CGU L  16      -99.79     63.54                                   
REMARK 500    LYS L  18      -84.27    -73.83                                   
REMARK 500    CGU L  19     -120.01     29.97                                   
REMARK 500    ARG L  28      -92.87    -43.11                                   
REMARK 500    CGU L  29       -3.75     46.50                                   
REMARK 500    ILE L  30      -42.92   -155.74                                   
REMARK 500    LYS L  32      -60.00     76.39                                   
REMARK 500    ALA L  34      -89.19    -66.81                                   
REMARK 500    CGU L  35      -90.85     33.76                                   
REMARK 500    GLN L  49       -7.41    -57.45                                   
REMARK 500    SER L  53       66.49     34.48                                   
REMARK 500    GLN L 100      -94.02   -121.57                                   
REMARK 500    ILE L 140       -5.83    -59.44                                   
REMARK 500    SER H  54     -159.69   -140.82                                   
REMARK 500    ASN H  60D      79.48   -102.05                                   
REMARK 500    HIS H  71      -59.89   -146.82                                   
REMARK 500    THR H 129C     -58.97   -121.21                                   
REMARK 500    ASP H 146      -52.98    -27.08                                   
REMARK 500    ASP H 170G      53.28   -110.24                                   
REMARK 500    PHE T  19       -6.11     77.77                                   
REMARK 500    ASP T  66       91.33   -169.37                                   
REMARK 500    ARG U 136       76.96   -118.76                                   
REMARK 500    ASN U 137       73.59     62.27                                   
REMARK 500    ASN U 138       70.20     61.32                                   
REMARK 500    THR U 139      128.32    164.42                                   
REMARK 500    THR U 172     -150.36   -119.13                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 ARG L   15     CGU L   16                  107.40                    
REMARK 500 LYS L   18     CGU L   19                  119.72                    
REMARK 500 ARG L   28     CGU L   29                   86.39                    
REMARK 500 ALA L   34     CGU L   35                  126.53                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY                                       
REMARK 500                                                                      
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY                       
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER                 
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;                     
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;                            
REMARK 500 I=INSERTION CODE).                                                   
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        ANGLE                                           
REMARK 500    LEU L   5        -16.46                                           
REMARK 500    LEU L  13        -13.06                                           
REMARK 500    ARG L  15         19.10                                           
REMARK 500    ARG L  28         12.94                                           
REMARK 500    ALA L  34         10.76                                           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    CGU L  16       -29.0      L          D   WRONG HAND              
REMARK 500    CGU L  19       -29.0      L          D   WRONG HAND              
REMARK 500    CGU L  29       -30.1      L          D   WRONG HAND              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH H1042        DISTANCE =  8.38 ANGSTROMS                       
REMARK 525    HOH L1071        DISTANCE =  5.65 ANGSTROMS                       
REMARK 525    HOH L1088        DISTANCE =  5.56 ANGSTROMS                       
REMARK 525    HOH U 221        DISTANCE =  6.51 ANGSTROMS                       
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     FUC L 1060                                                       
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 L1007  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CGU L  14  OE11                                                    
REMARK 620 2 CGU L  14  OE12  46.4                                              
REMARK 620 3 CGU L  14  OE22  60.1  78.1                                        
REMARK 620 4 CGU L  19  OE21  89.0  54.5  67.4                                  
REMARK 620 5 CGU L  19  OE11 151.2 127.4  91.7  73.8                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA L1005  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CGU L  16  OE11                                                    
REMARK 620 2 CGU L  16  OE22  89.8                                              
REMARK 620 3 CGU L  26  OE11 142.3  60.5                                        
REMARK 620 4 CGU L  26  OE21  86.0  72.7  64.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA L1002  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP L  46   OD2                                                    
REMARK 620 2 GLY L  47   O   114.2                                              
REMARK 620 3 GLN L  49   OE1  89.1  75.6                                        
REMARK 620 4 ASP L  63   OD2 161.6  83.9  92.2                                  
REMARK 620 5 GLN L  64   O    77.3 142.4  68.6  86.1                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA H1001  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU H  70   OE1                                                    
REMARK 620 2 GLU H  70   OE2  46.2                                              
REMARK 620 3 GLU H  75   O    91.8 138.0                                        
REMARK 620 4 HIS H  76   ND1 143.1 122.5  90.6                                  
REMARK 620 5 GLU H  80   OE2  66.3  93.4  64.2  81.9                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA L1009  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH L1077   O                                                      
REMARK 620 2 CGU L  29  OE11 114.1                                              
REMARK 620 N                    1                                               
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ASO L 1052                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FUC L 1060                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA L 1002                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA L 1003                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA L 1004                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA L 1005                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA L 1006                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA L 1007                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA L 1008                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA L 1009                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA H 1001                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 24X H 999                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1DAN   RELATED DB: PDB                                   
DBREF  2EC9 L    1   142  UNP    P08709   FA7_HUMAN       61    202             
DBREF  2EC9 H   16   257  UNP    P08709   FA7_HUMAN      213    466             
DBREF  2EC9 T    6    80  UNP    P13726   TF_HUMAN        38    112             
DBREF  2EC9 U   91   210  UNP    P13726   TF_HUMAN       123    242             
SEQRES   1 L  142  ALA ASN ALA PHE LEU CGU CGU LEU ARG PRO GLY SER LEU          
SEQRES   2 L  142  CGU ARG CGU CYS LYS CGU CGU GLN CYS SER PHE CGU CGU          
SEQRES   3 L  142  ALA ARG CGU ILE PHE LYS ASP ALA CGU ARG THR LYS LEU          
SEQRES   4 L  142  PHE TRP ILE SER TYR SER ASP GLY ASP GLN CYS ALA SER          
SEQRES   5 L  142  SER PRO CYS GLN ASN GLY GLY SER CYS LYS ASP GLN LEU          
SEQRES   6 L  142  GLN SER TYR ILE CYS PHE CYS LEU PRO ALA PHE GLU GLY          
SEQRES   7 L  142  ARG ASN CYS GLU THR HIS LYS ASP ASP GLN LEU ILE CYS          
SEQRES   8 L  142  VAL ASN GLU ASN GLY GLY CYS GLU GLN TYR CYS SER ASP          
SEQRES   9 L  142  HIS THR GLY THR LYS ARG SER CYS ARG CYS HIS GLU GLY          
SEQRES  10 L  142  TYR SER LEU LEU ALA ASP GLY VAL SER CYS THR PRO THR          
SEQRES  11 L  142  VAL GLU TYR PRO CYS GLY LYS ILE PRO ILE LEU GLU              
SEQRES   1 H  254  ILE VAL GLY GLY LYS VAL CYS PRO LYS GLY GLU CYS PRO          
SEQRES   2 H  254  TRP GLN VAL LEU LEU LEU VAL ASN GLY ALA GLN LEU CYS          
SEQRES   3 H  254  GLY GLY THR LEU ILE ASN THR ILE TRP VAL VAL SER ALA          
SEQRES   4 H  254  ALA HIS CYS PHE ASP LYS ILE LYS ASN TRP ARG ASN LEU          
SEQRES   5 H  254  ILE ALA VAL LEU GLY GLU HIS ASP LEU SER GLU HIS ASP          
SEQRES   6 H  254  GLY ASP GLU GLN SER ARG ARG VAL ALA GLN VAL ILE ILE          
SEQRES   7 H  254  PRO SER THR TYR VAL PRO GLY THR THR ASN HIS ASP ILE          
SEQRES   8 H  254  ALA LEU LEU ARG LEU HIS GLN PRO VAL VAL LEU THR ASP          
SEQRES   9 H  254  HIS VAL VAL PRO LEU CYS LEU PRO GLU ARG THR PHE SER          
SEQRES  10 H  254  GLU ARG THR LEU ALA PHE VAL ARG PHE SER LEU VAL SER          
SEQRES  11 H  254  GLY TRP GLY GLN LEU LEU ASP ARG GLY ALA THR ALA LEU          
SEQRES  12 H  254  GLU LEU MET VAL LEU ASN VAL PRO ARG LEU MET THR GLN          
SEQRES  13 H  254  ASP CYS LEU GLN GLN SER ARG LYS VAL GLY ASP SER PRO          
SEQRES  14 H  254  ASN ILE THR GLU TYR MET PHE CYS ALA GLY TYR SER ASP          
SEQRES  15 H  254  GLY SER LYS ASP SER CYS LYS GLY ASP SER GLY GLY PRO          
SEQRES  16 H  254  HIS ALA THR HIS TYR ARG GLY THR TRP TYR LEU THR GLY          
SEQRES  17 H  254  ILE VAL SER TRP GLY GLN GLY CYS ALA THR VAL GLY HIS          
SEQRES  18 H  254  PHE GLY VAL TYR THR ARG VAL SER GLN TYR ILE GLU TRP          
SEQRES  19 H  254  LEU GLN LYS LEU MET ARG SER GLU PRO ARG PRO GLY VAL          
SEQRES  20 H  254  LEU LEU ARG ALA PRO PHE PRO                                  
SEQRES   1 T   75  THR VAL ALA ALA TYR ASN LEU THR TRP LYS SER THR ASN          
SEQRES   2 T   75  PHE LYS THR ILE LEU GLU TRP GLU PRO LYS PRO VAL ASN          
SEQRES   3 T   75  GLN VAL TYR THR VAL GLN ILE SER THR LYS SER GLY ASP          
SEQRES   4 T   75  TRP LYS SER LYS CYS PHE TYR THR THR ASP THR GLU CYS          
SEQRES   5 T   75  ASP LEU THR ASP GLU ILE VAL LYS ASP VAL LYS GLN THR          
SEQRES   6 T   75  TYR LEU ALA ARG VAL PHE SER TYR PRO ALA                      
SEQRES   1 U  120  GLU PRO LEU TYR GLU ASN SER PRO GLU PHE THR PRO TYR          
SEQRES   2 U  120  LEU GLU THR ASN LEU GLY GLN PRO THR ILE GLN SER PHE          
SEQRES   3 U  120  GLU GLN VAL GLY THR LYS VAL ASN VAL THR VAL GLU ASP          
SEQRES   4 U  120  GLU ARG THR LEU VAL ARG ARG ASN ASN THR PHE LEU SER          
SEQRES   5 U  120  LEU ARG ASP VAL PHE GLY LYS ASP LEU ILE TYR THR LEU          
SEQRES   6 U  120  TYR TYR TRP LYS SER SER SER SER GLY LYS LYS THR ALA          
SEQRES   7 U  120  LYS THR ASN THR ASN GLU PHE LEU ILE ASP VAL ASP LYS          
SEQRES   8 U  120  GLY GLU ASN TYR CYS PHE SER VAL GLN ALA VAL ILE PRO          
SEQRES   9 U  120  SER ARG THR VAL ASN ARG LYS SER THR ASP SER PRO VAL          
SEQRES  10 U  120  GLU CYS MET                                                  
MODRES 2EC9 CGU L    6  GLU  GAMMA-CARBOXY-GLUTAMIC ACID                        
MODRES 2EC9 CGU L    7  GLU  GAMMA-CARBOXY-GLUTAMIC ACID                        
MODRES 2EC9 CGU L   14  GLU  GAMMA-CARBOXY-GLUTAMIC ACID                        
MODRES 2EC9 CGU L   16  GLU  GAMMA-CARBOXY-GLUTAMIC ACID                        
MODRES 2EC9 CGU L   19  GLU  GAMMA-CARBOXY-GLUTAMIC ACID                        
MODRES 2EC9 CGU L   20  GLU  GAMMA-CARBOXY-GLUTAMIC ACID                        
MODRES 2EC9 CGU L   25  GLU  GAMMA-CARBOXY-GLUTAMIC ACID                        
MODRES 2EC9 CGU L   26  GLU  GAMMA-CARBOXY-GLUTAMIC ACID                        
MODRES 2EC9 CGU L   29  GLU  GAMMA-CARBOXY-GLUTAMIC ACID                        
MODRES 2EC9 CGU L   35  GLU  GAMMA-CARBOXY-GLUTAMIC ACID                        
HET    CGU  L   6      12                                                       
HET    CGU  L   7      12                                                       
HET    CGU  L  14      12                                                       
HET    CGU  L  16      12                                                       
HET    CGU  L  19      12                                                       
HET    CGU  L  20      12                                                       
HET    CGU  L  25      12                                                       
HET    CGU  L  26      12                                                       
HET    CGU  L  29      12                                                       
HET    CGU  L  35      12                                                       
HET    ASO  L1052      11                                                       
HET    FUC  L1060      10                                                       
HET     CA  L1002       1                                                       
HET     CA  L1003       1                                                       
HET     CA  L1004       1                                                       
HET     CA  L1005       1                                                       
HET     CA  L1006       1                                                       
HET     CA  L1007       1                                                       
HET     CA  L1008       1                                                       
HET     CA  L1009       1                                                       
HET     CA  H1001       1                                                       
HET    24X  H 999      35                                                       
HETNAM     CGU GAMMA-CARBOXY-GLUTAMIC ACID                                      
HETNAM     ASO 1,5-ANHYDROSORBITOL                                              
HETNAM     FUC ALPHA-L-FUCOSE                                                   
HETNAM      CA CALCIUM ION                                                      
HETNAM     24X 2'-((5-CARBAMIMIDOYLPYRIDIN-2-YLAMINO)METHYL)-4-                 
HETNAM   2 24X  (ISOBUTYLCARBAMOYL)-4'-VINYLBIPHENYL-2-CARBOXYLIC ACID          
FORMUL   1  CGU    10(C6 H9 N O6)                                               
FORMUL   5  ASO    C6 H12 O5                                                    
FORMUL   6  FUC    C6 H12 O5                                                    
FORMUL   7   CA    9(CA 2+)                                                     
FORMUL  16  24X    C27 H29 N5 O3                                                
FORMUL  17  HOH   *224(H2 O)                                                    
HELIX    1   1 SER L   12  CYS L   17  1                                   6    
HELIX    2   2 SER L   23  LYS L   32  1                                  10    
HELIX    3   3 ASP L   33  SER L   45  1                                  13    
HELIX    4   4 ASP L   86  GLN L   88  5                                   3    
HELIX    5   5 ASN L   93  CYS L   98  5                                   6    
HELIX    6   6 ALA H   55  ASP H   60  5                                   6    
HELIX    7   7 GLU H  125  THR H  129C 1                                   8    
HELIX    8   8 LEU H  129D VAL H  129G 5                                   4    
HELIX    9   9 MET H  164  SER H  170B 1                                   9    
HELIX   10  10 TYR H  234  ARG H  243  1                                  10    
HELIX   11  11 LEU T   59  VAL T   64  1                                   6    
HELIX   12  12 THR U  101  THR U  106  1                                   6    
HELIX   13  13 LEU U  143  GLY U  148  1                                   6    
HELIX   14  14 LYS U  149  LEU U  151  5                                   3    
SHEET    1   A 2 SER L  60  GLN L  64  0                                        
SHEET    2   A 2 SER L  67  PHE L  71 -1  O  PHE L  71   N  SER L  60           
SHEET    1   B 2 PHE L  76  GLU L  77  0                                        
SHEET    2   B 2 THR L  83  HIS L  84 -1  O  THR L  83   N  GLU L  77           
SHEET    1   C 2 TYR L 101  SER L 103  0                                        
SHEET    2   C 2 SER L 111  ARG L 113 -1  O  SER L 111   N  SER L 103           
SHEET    1   D 2 TYR L 118  LEU L 120  0                                        
SHEET    2   D 2 CYS L 127  PRO L 129 -1  O  THR L 128   N  SER L 119           
SHEET    1   E 8 LYS H  20  VAL H  21  0                                        
SHEET    2   E 8 MET H 156  LEU H 163 -1  O  VAL H 157   N  LYS H  20           
SHEET    3   E 8 MET H 180  ALA H 183 -1  O  CYS H 182   N  LEU H 163           
SHEET    4   E 8 GLY H 226  ARG H 230 -1  O  TYR H 228   N  PHE H 181           
SHEET    5   E 8 THR H 206  TRP H 215 -1  N  TRP H 215   O  VAL H 227           
SHEET    6   E 8 PRO H 198  TYR H 203 -1  N  THR H 201   O  TYR H 208           
SHEET    7   E 8 PHE H 135  GLY H 140 -1  N  LEU H 137   O  ALA H 200           
SHEET    8   E 8 MET H 156  LEU H 163 -1  O  VAL H 160   N  SER H 136           
SHEET    1   F 8 LEU H 251  ALA H 254  0                                        
SHEET    2   F 8 GLN H  81  PRO H  91  1  N  VAL H  88   O  LEU H 252           
SHEET    3   F 8 ALA H 104  LEU H 108 -1  O  LEU H 105   N  ILE H  89           
SHEET    4   F 8 TRP H  51  SER H  54 -1  N  VAL H  52   O  LEU H 106           
SHEET    5   F 8 ALA H  39  LEU H  46 -1  N  THR H  45   O  VAL H  53           
SHEET    6   F 8 GLN H  30  VAL H  35 -1  N  LEU H  33   O  LEU H  41           
SHEET    7   F 8 LEU H  64  LEU H  68 -1  O  ILE H  65   N  LEU H  34           
SHEET    8   F 8 GLN H  81  PRO H  91 -1  O  GLN H  81   N  LEU H  68           
SHEET    1   G 3 TYR T  10  THR T  17  0                                        
SHEET    2   G 3 LYS T  20  GLU T  26 -1  O  ILE T  22   N  LYS T  15           
SHEET    3   G 3 GLU T  56  ASP T  58 -1  O  CYS T  57   N  LEU T  23           
SHEET    1   H 4 LYS T  46  THR T  52  0                                        
SHEET    2   H 4 GLN T  32  THR T  40 -1  N  VAL T  36   O  LYS T  48           
SHEET    3   H 4 TYR T  71  PRO T  79 -1  O  TYR T  78   N  VAL T  33           
SHEET    4   H 4 LEU U  93  ASN U  96 -1  O  LEU U  93   N  SER T  77           
SHEET    1   I 3 ILE U 113  VAL U 119  0                                        
SHEET    2   I 3 LYS U 122  VAL U 127 -1  O  LYS U 122   N  VAL U 119           
SHEET    3   I 3 GLU U 174  ASP U 178 -1  O  PHE U 175   N  VAL U 125           
SHEET    1   J 2 ARG U 131  ARG U 135  0                                        
SHEET    2   J 2 PHE U 140  SER U 142 -1  O  LEU U 141   N  THR U 132           
SHEET    1   K 4 LYS U 166  THR U 170  0                                        
SHEET    2   K 4 ILE U 152  TRP U 158 -1  N  LEU U 155   O  ALA U 168           
SHEET    3   K 4 CYS U 186  VAL U 192 -1  O  SER U 188   N  TYR U 156           
SHEET    4   K 4 GLU U 208  CYS U 209 -1  O  GLU U 208   N  PHE U 187           
SSBOND   1 CYS L   17    CYS L   22                          1555   1555  2.03  
SSBOND   2 CYS L   50    CYS L   61                          1555   1555  2.03  
SSBOND   3 CYS L   55    CYS L   70                          1555   1555  2.03  
SSBOND   4 CYS L   72    CYS L   81                          1555   1555  2.03  
SSBOND   5 CYS L   91    CYS L  102                          1555   1555  2.03  
SSBOND   6 CYS L   98    CYS L  112                          1555   1555  2.04  
SSBOND   7 CYS L  114    CYS L  127                          1555   1555  2.03  
SSBOND   8 CYS L  135    CYS H  122                          1555   1555  2.03  
SSBOND   9 CYS H   22    CYS H   27                          1555   1555  2.04  
SSBOND  10 CYS H   42    CYS H   58                          1555   1555  2.03  
SSBOND  11 CYS H  168    CYS H  182                          1555   1555  2.02  
SSBOND  12 CYS H  191    CYS H  220                          1555   1555  2.03  
SSBOND  13 CYS T   49    CYS T   57                          1555   1555  2.03  
SSBOND  14 CYS U  186    CYS U  209                          1555   1555  2.03  
LINK         O   ARG L   9                CA    CA L1004     1555   1555  2.87  
LINK        OE11 CGU L  14                CA    CA L1007     1555   1555  2.94  
LINK        OE12 CGU L  14                CA    CA L1007     1555   1555  2.73  
LINK        OE22 CGU L  14                CA    CA L1007     1555   1555  2.84  
LINK        OE11 CGU L  16                CA    CA L1005     1555   1555  2.59  
LINK        OE22 CGU L  16                CA    CA L1005     1555   1555  2.68  
LINK        OE21 CGU L  19                CA    CA L1007     1555   1555  2.98  
LINK        OE22 CGU L  19                CA    CA L1008     1555   1555  2.71  
LINK        OE11 CGU L  26                CA    CA L1005     1555   1555  2.68  
LINK        OE21 CGU L  26                CA    CA L1005     1555   1555  2.75  
LINK         OD2 ASP L  46                CA    CA L1002     1555   1555  2.42  
LINK         O   GLY L  47                CA    CA L1002     1555   1555  2.37  
LINK         OE1 GLN L  49                CA    CA L1002     1555   1555  2.87  
LINK         OD2 ASP L  63                CA    CA L1002     1555   1555  2.49  
LINK         O   GLN L  64                CA    CA L1002     1555   1555  2.65  
LINK         OE1 GLU H  70                CA    CA H1001     1555   1555  2.95  
LINK         OE2 GLU H  70                CA    CA H1001     1555   1555  2.60  
LINK         O   GLU H  75                CA    CA H1001     1555   1555  2.90  
LINK         ND1 HIS H  76                CA    CA H1001     1555   1555  2.99  
LINK        CA    CA L1009                 O   HOH L1077     1555   1555  2.82  
LINK         C   LEU L   5                 N   CGU L   6     1555   1555  1.38  
LINK         C   CGU L   6                 N   CGU L   7     1555   1555  1.37  
LINK         C   CGU L   7                 N   LEU L   8     1555   1555  1.40  
LINK         C   LEU L  13                 N   CGU L  14     1555   1555  1.39  
LINK         C   CGU L  14                 N   ARG L  15     1555   1555  1.38  
LINK         C   ARG L  15                 N   CGU L  16     1555   1555  1.39  
LINK         C   CGU L  16                 N   CYS L  17     1555   1555  1.37  
LINK         C   LYS L  18                 N   CGU L  19     1555   1555  1.40  
LINK         C   CGU L  19                 N   CGU L  20     1555   1555  1.36  
LINK         C   CGU L  20                 N   GLN L  21     1555   1555  1.39  
LINK         C   PHE L  24                 N   CGU L  25     1555   1555  1.41  
LINK         C   CGU L  25                 N   CGU L  26     1555   1555  1.35  
LINK         C   CGU L  26                 N   ALA L  27     1555   1555  1.38  
LINK         C   ARG L  28                 N   CGU L  29     1555   1555  1.41  
LINK         C   CGU L  29                 N   ILE L  30     1555   1555  1.41  
LINK         C   ALA L  34                 N   CGU L  35     1555   1555  1.39  
LINK         C   CGU L  35                 N   ARG L  36     1555   1555  1.39  
LINK         OE2 GLU H  80                CA    CA H1001     1555   1555  3.00  
LINK        OE11 CGU L  29                CA    CA L1009     1555   1555  3.15  
LINK        OE11 CGU L  19                CA    CA L1007     1555   1555  3.20  
CISPEP   1 PHE H  256    PRO H  257          0         0.03                     
CISPEP   2 GLU T   26    PRO T   27          0         0.04                     
SITE     1 AC1  4 GLN L  49  SER L  52  PRO L  54  TYR L  68                    
SITE     1 AC2  5 GLY L  58  SER L  60  PHE L  71  LEU L  73                    
SITE     2 AC2  5 ARG U 131                                                     
SITE     1 AC3  5 ASP L  46  GLY L  47  GLN L  49  ASP L  63                    
SITE     2 AC3  5 GLN L  64                                                     
SITE     1 AC4  2 CGU L   7  CGU L  26                                          
SITE     1 AC6  3 CGU L   6  ARG L   9  CGU L  16                               
SITE     1 AC7  3 ASN L   2  CGU L  16  CGU L  26                               
SITE     1 AD1  1 CGU L   6                                                     
SITE     1 AD2  2 CGU L  14  CGU L  19                                          
SITE     1 AD3  2 CGU L  19  CGU L  20                                          
SITE     1 BC1  3 CGU L  29  HOH L1077  HOH T  93                               
SITE     1 BC2  5 GLU H  70  ASP H  72  GLU H  75  HIS H  76                    
SITE     2 BC2  5 GLU H  80                                                     
SITE     1 BC3 14 HIS H  57  ASP H 102  GLN H 143  ASP H 189                    
SITE     2 BC3 14 SER H 190  LYS H 192  GLY H 193  SER H 195                    
SITE     3 BC3 14 VAL H 213  SER H 214  TRP H 215  GLY H 216                    
SITE     4 BC3 14 GLY H 219  GLY H 226                                          
CRYST1   69.780   81.410  125.350  90.00  90.00  90.00 P 21 21 21    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      0.014331  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.012284  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007978        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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