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Database: PDB
Entry: 3HPT
LinkDB: 3HPT
Original site: 3HPT 
HEADER    HYDROLASE, BLOOD CLOTTING               04-JUN-09   3HPT              
TITLE     CRYSTAL STRUCTURE OF HUMAN FXA IN COMPLEX WITH (S)-2-CYANO-1-(2-      
TITLE    2 METHYLBENZOFURAN-5-YL)-3-(2-OXO-1-(2-OXO-2-(PYRROLIDIN-1-YL)ETHYL)   
TITLE    3 AZEPAN-3-YL)GUANIDINE                                                
CAVEAT     3HPT    THIS ENTRY HAS BEEN RELEASED WITHOUT DEPOSITOR'S CHECKING    
CAVEAT   2 3HPT    AND CORRECTIONS, ONLY WITH NECESSARY PDB STAFF               
CAVEAT   3 3HPT    INTERVENTION. THE FOLLOWING RESIDUES IN COORDINATES ARE NOT  
CAVEAT   4 3HPT    PROPERLY LINKED: (B HIS 145) AND (B GLU 147) WITH C-N BOND   
CAVEAT   5 3HPT    DISTANCE 1.92 A, (B GLY 218) AND (B CYS 220) WITH C-N BOND   
CAVEAT   6 3HPT    DISTANCE 1.90 A, (D HIS 145) AND (D GLU 147) WITH C-N BOND   
CAVEAT   7 3HPT    DISTANCE 2.42 A, (D GLY 218) AND (D CYS 220) WITH C-N BOND   
CAVEAT   8 3HPT    DISTANCE 1.97 A.                                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: COAGULATION FACTOR X;                                      
COMPND   3 CHAIN: A, C;                                                         
COMPND   4 FRAGMENT: FACTOR X LIGHT CHAIN: UNP RESIDUES 85-178;                 
COMPND   5 SYNONYM: STUART FACTOR, STUART-PROWER FACTOR, FACTOR X LIGHT CHAIN;  
COMPND   6 EC: 3.4.21.6;                                                        
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: COAGULATION FACTOR X;                                      
COMPND   9 CHAIN: B, D;                                                         
COMPND  10 FRAGMENT: ACTIVATED FACTOR XA HEAVY CHAIN: UNP RESIDUES 235-472;     
COMPND  11 SYNONYM: STUART FACTOR, STUART-PROWER FACTOR, ACTIVATED FACTOR XA    
COMPND  12 HEAVY CHAIN;                                                         
COMPND  13 EC: 3.4.21.6                                                         
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 TISSUE: BLOOD;                                                       
SOURCE   6 MOL_ID: 2;                                                           
SOURCE   7 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   8 ORGANISM_COMMON: HUMAN;                                              
SOURCE   9 ORGANISM_TAXID: 9606;                                                
SOURCE  10 TISSUE: BLOOD                                                        
KEYWDS    SERINE PROTEASE, HYDROLASE, EPIDERMAL GROWTH FACTOR LIKE DOMAIN,      
KEYWDS   2 BLOOD COAGULATION FACTOR, CLEAVAGE ON PAIR OF BASIC RESIDUES, EGF-   
KEYWDS   3 LIKE DOMAIN, GAMMA-CARBOXYGLUTAMIC ACID, GLYCOPROTEIN,               
KEYWDS   4 HYDROXYLATION, ZYMOGEN, BLOOD CLOTTING, BLOOD COAGULATION, DISULFIDE 
KEYWDS   5 BOND, PROTEASE, SECRETED                                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    H.E.KLEI,K.GHOSH,A.RUSHITH,K.KISH                                     
REVDAT   3   01-NOV-17 3HPT    1       REMARK                                   
REVDAT   2   13-JUL-11 3HPT    1       VERSN                                    
REVDAT   1   17-NOV-09 3HPT    0                                                
JRNL        AUTH   Y.SHI,J.ZHANG,M.SHI,S.P.O'CONNOR,S.N.BISAHA,C.LI,D.SITKOFF,  
JRNL        AUTH 2 A.T.PUDZIANOWSKI,S.CHONG,H.E.KLEI,K.KISH,J.YANCHUNAS,        
JRNL        AUTH 3 E.C.LIU,K.S.HARTL,S.M.SEILER,T.E.STEINBACHER,W.A.SCHUMACHER, 
JRNL        AUTH 4 K.S.ATWAL,P.D.STEIN                                          
JRNL        TITL   CYANOGUANIDINE-BASED LACTAM DERIVATIVES AS A NOVEL CLASS OF  
JRNL        TITL 2 ORALLY BIOAVAILABLE FACTOR XA INHIBITORS.                    
JRNL        REF    BIOORG.MED.CHEM.LETT.         V.  19  4034 2009              
JRNL        REFN                   ISSN 0960-894X                               
JRNL        PMID   19541481                                                     
JRNL        DOI    10.1016/J.BMCL.2009.06.014                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.19 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
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) : 2.19                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 33872                          
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) : 0.179                           
REMARK   3   R VALUE            (WORKING SET) : 0.176                           
REMARK   3   FREE R VALUE                     : 0.239                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1781                            
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) : 2.19                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.24                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2393                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 94.08                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2100                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 102                          
REMARK   3   BIN FREE R VALUE                    : 0.2800                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4915                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 162                                     
REMARK   3   SOLVENT ATOMS            : 554                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 33.61                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.78000                                              
REMARK   3    B22 (A**2) : -0.05000                                             
REMARK   3    B33 (A**2) : -0.98000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.59000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.280         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.218         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.147         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.665         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.958                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.922                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  5236 ; 0.009 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  7070 ; 1.326 ; 1.975       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   647 ; 5.831 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   232 ;36.078 ;24.267       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   842 ;15.079 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    30 ;19.278 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   750 ; 0.080 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3974 ; 0.004 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  2444 ; 0.205 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  3533 ; 0.300 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   561 ; 0.149 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):    10 ; 0.121 ; 0.200       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    71 ; 0.183 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    38 ; 0.157 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  3223 ; 0.662 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  5131 ; 1.236 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2093 ; 1.541 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1931 ; 2.544 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
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 : 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 RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 3HPT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-JUN-09.                  
REMARK 100 THE DEPOSITION ID IS D_1000053433.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 07-JAN-99                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU RU200                       
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54178                            
REMARK 200  MONOCHROMATOR                  : YALE/MSC                           
REMARK 200  OPTICS                         : OSMIC MIRRORS                      
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IIC                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 35677                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.190                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 4.300                              
REMARK 200  R MERGE                    (I) : 0.08500                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 14.8000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.19                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.28                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.43800                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.600                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 47.97                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.36                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 15-22% W/V PEG MME 5000, 0.01 M          
REMARK 280  CALCIUM ACETATE, 0.35 M SODIUM ACETATE, 0.1 M LITHIUM SULFATE,      
REMARK 280  0.1 M MES, PH 6.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE       
REMARK 280  298K                                                                
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       39.33000            
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 300 REMARK: THE BIOLOGICAL UNIT CONSISTS OF ONE LIGHT CHAIN (EGF-LIKE    
REMARK 300 DOMAIN) AND ONE HEAVY CHAIN (CATALYTIC DOMAIN). THE ASYMMETRIC UNIT  
REMARK 300 CONTAINS TWO BIOLOGICAL UNITS (CHAINS A,B AND CHAINS C,D). CHAINS A  
REMARK 300 AND C ARE EGF-LIKE DOMAINS. CHAINS B AND D ARE CATALYTIC DOMAINS.    
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: 1740 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 15780 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -8.1 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: 1590 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 15840 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.4 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 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     LYS A    85                                                      
REMARK 465     ASP A    86                                                      
REMARK 465     GLY A    87                                                      
REMARK 465     ASP A    88                                                      
REMARK 465     GLN A    89                                                      
REMARK 465     GLU A    91                                                      
REMARK 465     THR A    92                                                      
REMARK 465     GLY A   104                                                      
REMARK 465     LEU A   105                                                      
REMARK 465     GLY A   106                                                      
REMARK 465     LYS C    85                                                      
REMARK 465     ASP C    86                                                      
REMARK 465     GLY C    87                                                      
REMARK 465     ASP C    88                                                      
REMARK 465     THR C    92                                                      
REMARK 465     LEU C   105                                                      
REMARK 465     GLY C   106                                                      
REMARK 465     LYS D   148                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     CYS A  90    O                                                   
REMARK 470     LYS A 100    CG   CD   CE   NZ                                   
REMARK 470     LYS A 102    CG   CD   CE   NZ                                   
REMARK 470     GLU A 114    CG   CD   OE1  OE2                                  
REMARK 470     GLN A 144    CG   CD   OE1  NE2                                  
REMARK 470     LYS B  62    CG   CD   CE   NZ                                   
REMARK 470     GLU B  74    CG   CD   OE1  OE2                                  
REMARK 470     GLN B  75    CG   CD   OE1  NE2                                  
REMARK 470     GLU B  76    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 134    CE   NZ                                             
REMARK 470     LYS B 148    CG   CD   CE   NZ                                   
REMARK 470     ARG B 150    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B 154    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU B 170    CD1                                                 
REMARK 470     GLN C  89    N    CB   CG   CD   OE1  NE2                        
REMARK 470     GLU C  91    CA   C    O    CB   CG   CD   OE1                   
REMARK 470     GLU C  91    OE2                                                 
REMARK 470     GLN C  98    CG   CD   OE1  NE2                                  
REMARK 470     LYS C 100    CG   CD   CE   NZ                                   
REMARK 470     LYS C 102    CG   CD   CE   NZ                                   
REMARK 470     GLU C 107    CG   CD   OE1  OE2                                  
REMARK 470     LYS C 119    CG   CD   CE   NZ                                   
REMARK 470     ARG C 126    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN C 144    CG   CD   OE1  NE2                                  
REMARK 470     ASN C 145    CG   OD1  ND2                                       
REMARK 470     ARG C 153    NE   CZ   NH1  NH2                                  
REMARK 470     LYS D  23    CD   CE   NZ                                        
REMARK 470     LYS D  62    CG   CD   CE   NZ                                   
REMARK 470     GLN D  75    CG   CD   OE1  NE2                                  
REMARK 470     GLU D  77    CG   CD   OE1  OE2                                  
REMARK 470     ARG D 143    CZ   NH1  NH2                                       
REMARK 470     ARG D 150    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG D 154    CZ   NH1  NH2                                       
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    GLN A 138     -105.98   -128.05                                   
REMARK 500    ARG B 245     -155.32     57.97                                   
REMARK 500    GLN C 138     -105.22   -126.71                                   
REMARK 500    LYS C 162      -54.71   -127.20                                   
REMARK 500    ARG D 245     -148.53     53.84                                   
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 B 249  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B  70   OD1                                                    
REMARK 620 2 ASN B  72   O    73.4                                              
REMARK 620 3 GLN B  75   O   150.3  79.6                                        
REMARK 620 4 GLU B  80   OE2  99.6 133.7  90.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA B   3  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 TYR B 185   O                                                      
REMARK 620 2 ASP B 185A  O    79.4                                              
REMARK 620 3 ARG B 222   O   164.0  84.6                                        
REMARK 620 4 LYS B 224   O    91.2 116.7  95.8                                  
REMARK 620 5 HOH B 317   O    94.2  79.6  83.0 163.6                            
REMARK 620 6 HOH B 323   O    98.7 177.9  97.4  63.9  99.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA D 249  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP D  70   OD1                                                    
REMARK 620 2 ASN D  72   O    80.7                                              
REMARK 620 3 GLN D  75   O   140.8  63.2                                        
REMARK 620 4 GLU D  80   OE2 107.5 149.5  97.5                                  
REMARK 620 5 HOH D 491   O    99.4 100.3 101.5 107.0                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA D   4  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 TYR D 185   O                                                      
REMARK 620 2 ASP D 185A  O    74.4                                              
REMARK 620 3 ARG D 222   O   159.4  87.9                                        
REMARK 620 4 LYS D 224   O    91.3 112.1  85.7                                  
REMARK 620 5 HOH D 342   O    96.8  78.6  89.6 168.1                            
REMARK 620 6 HOH D 330   O    94.2 167.8 102.5  63.0 107.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 7                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 21                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE YET B 1                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 249                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 3                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 8                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MES B 9                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT B 11                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT B 14                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT B 250                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS B 251                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT B 252                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE YET D 2                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA D 249                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA D 4                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 5                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 6                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MES D 10                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT D 12                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT D 13                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT D 15                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS D 250                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT D 251                 
DBREF  3HPT A   85   178  UNP    P00742   FA10_HUMAN      85    178             
DBREF  3HPT B   16   248  UNP    P00742   FA10_HUMAN     235    472             
DBREF  3HPT C   85   178  UNP    P00742   FA10_HUMAN      85    178             
DBREF  3HPT D   16   248  UNP    P00742   FA10_HUMAN     235    472             
SEQRES   1 A   94  LYS ASP GLY ASP GLN CYS GLU THR SER PRO CYS GLN ASN          
SEQRES   2 A   94  GLN GLY LYS CYS LYS ASP GLY LEU GLY GLU TYR THR CYS          
SEQRES   3 A   94  THR CYS LEU GLU GLY PHE GLU GLY LYS ASN CYS GLU LEU          
SEQRES   4 A   94  PHE THR ARG LYS LEU CYS SER LEU ASP ASN GLY ASP CYS          
SEQRES   5 A   94  ASP GLN PHE CYS HIS GLU GLU GLN ASN SER VAL VAL CYS          
SEQRES   6 A   94  SER CYS ALA ARG GLY TYR THR LEU ALA ASP ASN GLY LYS          
SEQRES   7 A   94  ALA CYS ILE PRO THR GLY PRO TYR PRO CYS GLY LYS GLN          
SEQRES   8 A   94  THR LEU GLU                                                  
SEQRES   1 B  238  ILE VAL GLY GLY GLN GLU CYS LYS ASP GLY GLU CYS PRO          
SEQRES   2 B  238  TRP GLN ALA LEU LEU ILE ASN GLU GLU ASN GLU GLY PHE          
SEQRES   3 B  238  CYS GLY GLY THR ILE LEU SER GLU PHE TYR ILE LEU THR          
SEQRES   4 B  238  ALA ALA HIS CYS LEU TYR GLN ALA LYS ARG PHE LYS VAL          
SEQRES   5 B  238  ARG VAL GLY ASP ARG ASN THR GLU GLN GLU GLU GLY GLY          
SEQRES   6 B  238  GLU ALA VAL HIS GLU VAL GLU VAL VAL ILE LYS HIS ASN          
SEQRES   7 B  238  ARG PHE THR LYS GLU THR TYR ASP PHE ASP ILE ALA VAL          
SEQRES   8 B  238  LEU ARG LEU LYS THR PRO ILE THR PHE ARG MET ASN VAL          
SEQRES   9 B  238  ALA PRO ALA CYS LEU PRO GLU ARG ASP TRP ALA GLU SER          
SEQRES  10 B  238  THR LEU MET THR GLN LYS THR GLY ILE VAL SER GLY PHE          
SEQRES  11 B  238  GLY ARG THR HIS GLU LYS GLY ARG GLN SER THR ARG LEU          
SEQRES  12 B  238  LYS MET LEU GLU VAL PRO TYR VAL ASP ARG ASN SER CYS          
SEQRES  13 B  238  LYS LEU SER SER SER PHE ILE ILE THR GLN ASN MET PHE          
SEQRES  14 B  238  CYS ALA GLY TYR ASP THR LYS GLN GLU ASP ALA CYS GLN          
SEQRES  15 B  238  GLY ASP SER GLY GLY PRO HIS VAL THR ARG PHE LYS ASP          
SEQRES  16 B  238  THR TYR PHE VAL THR GLY ILE VAL SER TRP GLY GLU GLY          
SEQRES  17 B  238  CYS ALA ARG LYS GLY LYS TYR GLY ILE TYR THR LYS VAL          
SEQRES  18 B  238  THR ALA PHE LEU LYS TRP ILE ASP ARG SER MET LYS THR          
SEQRES  19 B  238  ARG GLY LEU PRO                                              
SEQRES   1 C   94  LYS ASP GLY ASP GLN CYS GLU THR SER PRO CYS GLN ASN          
SEQRES   2 C   94  GLN GLY LYS CYS LYS ASP GLY LEU GLY GLU TYR THR CYS          
SEQRES   3 C   94  THR CYS LEU GLU GLY PHE GLU GLY LYS ASN CYS GLU LEU          
SEQRES   4 C   94  PHE THR ARG LYS LEU CYS SER LEU ASP ASN GLY ASP CYS          
SEQRES   5 C   94  ASP GLN PHE CYS HIS GLU GLU GLN ASN SER VAL VAL CYS          
SEQRES   6 C   94  SER CYS ALA ARG GLY TYR THR LEU ALA ASP ASN GLY LYS          
SEQRES   7 C   94  ALA CYS ILE PRO THR GLY PRO TYR PRO CYS GLY LYS GLN          
SEQRES   8 C   94  THR LEU GLU                                                  
SEQRES   1 D  238  ILE VAL GLY GLY GLN GLU CYS LYS ASP GLY GLU CYS PRO          
SEQRES   2 D  238  TRP GLN ALA LEU LEU ILE ASN GLU GLU ASN GLU GLY PHE          
SEQRES   3 D  238  CYS GLY GLY THR ILE LEU SER GLU PHE TYR ILE LEU THR          
SEQRES   4 D  238  ALA ALA HIS CYS LEU TYR GLN ALA LYS ARG PHE LYS VAL          
SEQRES   5 D  238  ARG VAL GLY ASP ARG ASN THR GLU GLN GLU GLU GLY GLY          
SEQRES   6 D  238  GLU ALA VAL HIS GLU VAL GLU VAL VAL ILE LYS HIS ASN          
SEQRES   7 D  238  ARG PHE THR LYS GLU THR TYR ASP PHE ASP ILE ALA VAL          
SEQRES   8 D  238  LEU ARG LEU LYS THR PRO ILE THR PHE ARG MET ASN VAL          
SEQRES   9 D  238  ALA PRO ALA CYS LEU PRO GLU ARG ASP TRP ALA GLU SER          
SEQRES  10 D  238  THR LEU MET THR GLN LYS THR GLY ILE VAL SER GLY PHE          
SEQRES  11 D  238  GLY ARG THR HIS GLU LYS GLY ARG GLN SER THR ARG LEU          
SEQRES  12 D  238  LYS MET LEU GLU VAL PRO TYR VAL ASP ARG ASN SER CYS          
SEQRES  13 D  238  LYS LEU SER SER SER PHE ILE ILE THR GLN ASN MET PHE          
SEQRES  14 D  238  CYS ALA GLY TYR ASP THR LYS GLN GLU ASP ALA CYS GLN          
SEQRES  15 D  238  GLY ASP SER GLY GLY PRO HIS VAL THR ARG PHE LYS ASP          
SEQRES  16 D  238  THR TYR PHE VAL THR GLY ILE VAL SER TRP GLY GLU GLY          
SEQRES  17 D  238  CYS ALA ARG LYS GLY LYS TYR GLY ILE TYR THR LYS VAL          
SEQRES  18 D  238  THR ALA PHE LEU LYS TRP ILE ASP ARG SER MET LYS THR          
SEQRES  19 D  238  ARG GLY LEU PRO                                              
HET    GOL  A   7       6                                                       
HET    GOL  A  21       6                                                       
HET    YET  B   1      32                                                       
HET     CA  B 249       1                                                       
HET     NA  B   3       1                                                       
HET    GOL  B   8       6                                                       
HET    MES  B   9      12                                                       
HET    ACT  B  11       4                                                       
HET    ACT  B  14       4                                                       
HET    ACT  B 250       4                                                       
HET    DMS  B 251       4                                                       
HET    ACT  B 252       4                                                       
HET    YET  D   2      32                                                       
HET     CA  D 249       1                                                       
HET     NA  D   4       1                                                       
HET    GOL  D   5       6                                                       
HET    GOL  D   6       6                                                       
HET    MES  D  10      12                                                       
HET    ACT  D  12       4                                                       
HET    ACT  D  13       4                                                       
HET    ACT  D  15       4                                                       
HET    DMS  D 250       4                                                       
HET    ACT  D 251       4                                                       
HETNAM     GOL GLYCEROL                                                         
HETNAM     YET 1-CYANO-2-(2-METHYL-1-BENZOFURAN-5-YL)-3-[(3S)-2-OXO-1-          
HETNAM   2 YET  (2-OXO-2-PYRROLIDIN-1-YLETHYL)AZEPAN-3-YL]GUANIDINE             
HETNAM      CA CALCIUM ION                                                      
HETNAM      NA SODIUM ION                                                       
HETNAM     MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID                             
HETNAM     ACT ACETATE ION                                                      
HETNAM     DMS DIMETHYL SULFOXIDE                                               
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   5  GOL    5(C3 H8 O3)                                                  
FORMUL   7  YET    2(C23 H28 N6 O3)                                             
FORMUL   8   CA    2(CA 2+)                                                     
FORMUL   9   NA    2(NA 1+)                                                     
FORMUL  11  MES    2(C6 H13 N O4 S)                                             
FORMUL  12  ACT    8(C2 H3 O2 1-)                                               
FORMUL  15  DMS    2(C2 H6 O S)                                                 
FORMUL  28  HOH   *554(H2 O)                                                    
HELIX    1   1 LEU A  131  CYS A  136  5                                   6    
HELIX    2   2 ALA B   55  TYR B   60  1                                   6    
HELIX    3   3 GLU B  124A LEU B  131A 1                                   9    
HELIX    4   4 ASP B  164  SER B  172  1                                   9    
HELIX    5   5 PHE B  234  THR B  244  1                                  11    
HELIX    6   6 LEU C  131  CYS C  136  5                                   6    
HELIX    7   7 ALA D   55  ALA D   61A 5                                   8    
HELIX    8   8 GLU D  124A LEU D  131A 1                                   9    
HELIX    9   9 ASP D  164  SER D  172  1                                   9    
HELIX   10  10 PHE D  234  THR D  244  1                                  11    
SHEET    1   A 2 LYS A 100  LYS A 102  0                                        
SHEET    2   A 2 THR A 109  THR A 111 -1  O  THR A 109   N  LYS A 102           
SHEET    1   B 2 PHE A 116  GLU A 117  0                                        
SHEET    2   B 2 LEU A 123  PHE A 124 -1  O  LEU A 123   N  GLU A 117           
SHEET    1   C 2 PHE A 139  GLU A 142  0                                        
SHEET    2   C 2 VAL A 147  SER A 150 -1  O  VAL A 148   N  HIS A 141           
SHEET    1   D 2 TYR A 155  LEU A 157  0                                        
SHEET    2   D 2 CYS A 164  PRO A 166 -1  O  ILE A 165   N  THR A 156           
SHEET    1   E 8 GLN B  20  GLU B  21  0                                        
SHEET    2   E 8 LYS B 156  VAL B 163 -1  O  MET B 157   N  GLN B  20           
SHEET    3   E 8 MET B 180  ALA B 183 -1  O  CYS B 182   N  VAL B 163           
SHEET    4   E 8 GLY B 226  LYS B 230 -1  O  TYR B 228   N  PHE B 181           
SHEET    5   E 8 THR B 206  TRP B 215 -1  N  TRP B 215   O  ILE B 227           
SHEET    6   E 8 PRO B 198  PHE B 203 -1  N  HIS B 199   O  THR B 210           
SHEET    7   E 8 THR B 135  GLY B 140 -1  N  ILE B 137   O  VAL B 200           
SHEET    8   E 8 LYS B 156  VAL B 163 -1  O  VAL B 160   N  GLY B 136           
SHEET    1   F 7 GLN B  30  ILE B  34  0                                        
SHEET    2   F 7 GLY B  40  ILE B  46 -1  O  CYS B  42   N  LEU B  33           
SHEET    3   F 7 TYR B  51  THR B  54 -1  O  LEU B  53   N  THR B  45           
SHEET    4   F 7 ALA B 104  LEU B 108 -1  O  ALA B 104   N  THR B  54           
SHEET    5   F 7 ALA B  81  LYS B  90 -1  N  ILE B  89   O  VAL B 105           
SHEET    6   F 7 LYS B  65  VAL B  68 -1  N  VAL B  66   O  HIS B  83           
SHEET    7   F 7 GLN B  30  ILE B  34 -1  N  LEU B  32   O  ARG B  67           
SHEET    1   G 2 LYS C 100  LYS C 102  0                                        
SHEET    2   G 2 THR C 109  THR C 111 -1  O  THR C 109   N  LYS C 102           
SHEET    1   H 2 PHE C 116  GLU C 117  0                                        
SHEET    2   H 2 LEU C 123  PHE C 124 -1  O  LEU C 123   N  GLU C 117           
SHEET    1   I 2 PHE C 139  GLU C 142  0                                        
SHEET    2   I 2 VAL C 147  SER C 150 -1  O  VAL C 148   N  HIS C 141           
SHEET    1   J 2 TYR C 155  LEU C 157  0                                        
SHEET    2   J 2 CYS C 164  PRO C 166 -1  O  ILE C 165   N  THR C 156           
SHEET    1   K 8 GLN D  20  GLU D  21  0                                        
SHEET    2   K 8 LYS D 156  VAL D 163 -1  O  MET D 157   N  GLN D  20           
SHEET    3   K 8 MET D 180  ALA D 183 -1  O  CYS D 182   N  VAL D 163           
SHEET    4   K 8 GLY D 226  LYS D 230 -1  O  TYR D 228   N  PHE D 181           
SHEET    5   K 8 THR D 206  TRP D 215 -1  N  TRP D 215   O  ILE D 227           
SHEET    6   K 8 PRO D 198  PHE D 203 -1  N  HIS D 199   O  THR D 210           
SHEET    7   K 8 THR D 135  GLY D 140 -1  N  ILE D 137   O  VAL D 200           
SHEET    8   K 8 LYS D 156  VAL D 163 -1  O  VAL D 160   N  GLY D 136           
SHEET    1   L 7 GLN D  30  ASN D  35  0                                        
SHEET    2   L 7 GLY D  40  ILE D  46 -1  O  CYS D  42   N  LEU D  33           
SHEET    3   L 7 TYR D  51  THR D  54 -1  O  LEU D  53   N  THR D  45           
SHEET    4   L 7 ALA D 104  LEU D 108 -1  O  ALA D 104   N  THR D  54           
SHEET    5   L 7 ALA D  81  LYS D  90 -1  N  GLU D  86   O  ARG D 107           
SHEET    6   L 7 PHE D  64  VAL D  68 -1  N  VAL D  66   O  HIS D  83           
SHEET    7   L 7 GLN D  30  ASN D  35 -1  N  LEU D  32   O  ARG D  67           
SSBOND   1 CYS A   90    CYS A  101                          1555   1555  2.05  
SSBOND   2 CYS A   95    CYS A  110                          1555   1555  2.03  
SSBOND   3 CYS A  112    CYS A  121                          1555   1555  2.02  
SSBOND   4 CYS A  129    CYS A  140                          1555   1555  2.06  
SSBOND   5 CYS A  136    CYS A  149                          1555   1555  2.03  
SSBOND   6 CYS A  151    CYS A  164                          1555   1555  2.04  
SSBOND   7 CYS A  172    CYS B  122                          1555   1555  2.05  
SSBOND   8 CYS B   22    CYS B   27                          1555   1555  2.04  
SSBOND   9 CYS B   42    CYS B   58                          1555   1555  2.04  
SSBOND  10 CYS B  168    CYS B  182                          1555   1555  1.99  
SSBOND  11 CYS B  191    CYS B  220                          1555   1555  2.01  
SSBOND  12 CYS C   90    CYS C  101                          1555   1555  2.04  
SSBOND  13 CYS C   95    CYS C  110                          1555   1555  2.04  
SSBOND  14 CYS C  112    CYS C  121                          1555   1555  2.04  
SSBOND  15 CYS C  129    CYS C  140                          1555   1555  2.04  
SSBOND  16 CYS C  136    CYS C  149                          1555   1555  2.04  
SSBOND  17 CYS C  151    CYS C  164                          1555   1555  2.03  
SSBOND  18 CYS C  172    CYS D  122                          1555   1555  2.04  
SSBOND  19 CYS D   22    CYS D   27                          1555   1555  2.03  
SSBOND  20 CYS D   42    CYS D   58                          1555   1555  2.06  
SSBOND  21 CYS D  168    CYS D  182                          1555   1555  2.01  
SSBOND  22 CYS D  191    CYS D  220                          1555   1555  2.02  
LINK         OD1 ASP B  70                CA    CA B 249     1555   1555  2.62  
LINK         O   ASN B  72                CA    CA B 249     1555   1555  2.24  
LINK         O   GLN B  75                CA    CA B 249     1555   1555  2.44  
LINK         OE2 GLU B  80                CA    CA B 249     1555   1555  2.22  
LINK         O   TYR B 185                NA    NA B   3     1555   1555  2.29  
LINK         O   ASP B 185A               NA    NA B   3     1555   1555  2.71  
LINK         O   ARG B 222                NA    NA B   3     1555   1555  2.37  
LINK         O   LYS B 224                NA    NA B   3     1555   1555  2.21  
LINK         OD1 ASP D  70                CA    CA D 249     1555   1555  2.63  
LINK         O   ASN D  72                CA    CA D 249     1555   1555  2.34  
LINK         O   GLN D  75                CA    CA D 249     1555   1555  2.88  
LINK         OE2 GLU D  80                CA    CA D 249     1555   1555  2.40  
LINK         O   TYR D 185                NA    NA D   4     1555   1555  2.35  
LINK         O   ASP D 185A               NA    NA D   4     1555   1555  2.79  
LINK         O   ARG D 222                NA    NA D   4     1555   1555  2.47  
LINK         O   LYS D 224                NA    NA D   4     1555   1555  2.41  
LINK        NA    NA B   3                 O   HOH B 317     1555   1555  2.35  
LINK        NA    NA B   3                 O   HOH B 323     1555   1555  2.83  
LINK        CA    CA D 249                 O   HOH D 491     1555   1555  2.70  
LINK        NA    NA D   4                 O   HOH D 342     1555   1555  2.46  
LINK        NA    NA D   4                 O   HOH D 330     1555   1555  2.66  
SITE     1 AC1  4 GOL A  21  PRO A 166  GLY A 168  HOH A 321                    
SITE     1 AC2  7 GOL A   7  HOH A  28  PRO A 169  PRO A 171                    
SITE     2 AC2  7 LYS A 174  GLN A 175  LEU A 177                               
SITE     1 AC3 18 THR B  98  TYR B  99  GLU B 147  PHE B 174                    
SITE     2 AC3 18 ALA B 190  SER B 195  VAL B 213  TRP B 215                    
SITE     3 AC3 18 GLY B 216  GLY B 218  CYS B 220  GLY B 226                    
SITE     4 AC3 18 ILE B 227  TYR B 228  HOH B 275  HOH B 302                    
SITE     5 AC3 18 HOH B 309  HOH B 469                                          
SITE     1 AC4  4 ASP B  70  ASN B  72  GLN B  75  GLU B  80                    
SITE     1 AC5  6 TYR B 185  ASP B 185A ARG B 222  LYS B 224                    
SITE     2 AC5  6 HOH B 317  HOH B 323                                          
SITE     1 AC6  5 PHE A 139  LEU B 123  PRO B 124  ASP B 239                    
SITE     2 AC6  5 HOH B 356                                                     
SITE     1 AC7  7 PHE B 101  ARG B 125  ASN B 179  ALA B 233                    
SITE     2 AC7  7 LYS B 236  HOH B 283  HOH B 299                               
SITE     1 AC8  5 TYR B 185  ASP B 185A THR B 185B LYS B 186                    
SITE     2 AC8  5 HOH B 442                                                     
SITE     1 AC9  5 GLN B 133  LYS B 204  HOH B 337  HOH B 373                    
SITE     2 AC9  5 HOH B 420                                                     
SITE     1 BC1  4 PHE B  50  ARG B 107  HOH B 395  HOH B 551                    
SITE     1 BC2  6 GLN B  20  MET B 157  LEU B 158  GLU B 159                    
SITE     2 BC2  6 HOH B 326  HOH B 346                                          
SITE     1 BC3  2 PHE B  64  SER C 130                                          
SITE     1 BC4 18 ASN A 120  THR D  98  TYR D  99  GLU D 147                    
SITE     2 BC4 18 ALA D 190  GLN D 192  SER D 195  VAL D 213                    
SITE     3 BC4 18 TRP D 215  GLY D 216  GLY D 218  CYS D 220                    
SITE     4 BC4 18 GLY D 226  ILE D 227  TYR D 228  HOH D 261                    
SITE     5 BC4 18 HOH D 268  HOH D 295                                          
SITE     1 BC5  6 ASP D  70  ASN D  72  GLN D  75  GLU D  80                    
SITE     2 BC5  6 HOH D 360  HOH D 491                                          
SITE     1 BC6  6 TYR D 185  ASP D 185A ARG D 222  LYS D 224                    
SITE     2 BC6  6 HOH D 330  HOH D 342                                          
SITE     1 BC7  7 PHE C 139  LEU D 123  PRO D 124  LEU D 235                    
SITE     2 BC7  7 ASP D 239  HOH D 340  HOH D 386                               
SITE     1 BC8  5 ARG D  93  THR D  95  ASP D 100  HOH D 337                    
SITE     2 BC8  5 HOH D 367                                                     
SITE     1 BC9  7 PHE D 101  ARG D 125  ASN D 179  ALA D 233                    
SITE     2 BC9  7 LYS D 236  HOH D 289  HOH D 413                               
SITE     1 CC1  3 ARG D 202  LYS D 204  HOH D 516                               
SITE     1 CC2  3 ASP D 185A THR D 185B LYS D 186                               
SITE     1 CC3  4 PHE D  50  ARG D 107  HOH D 402  HOH D 544                    
SITE     1 CC4  4 GLN D  20  MET D 157  GLU D 159  HOH D 346                    
SITE     1 CC5  1 PHE D  64                                                     
CRYST1   61.980   78.660   73.670  90.00 102.49  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      0.016134  0.000000  0.003574        0.00000                         
SCALE2      0.000000  0.012713  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013903        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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