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Database: PDB
Entry: 3D68
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Original site: 3D68 
HEADER    HYDROLASE                               19-MAY-08   3D68              
TITLE     CRYSTAL STRUCTURE OF A T325I/T329I/H333Y/H335Q MUTANT OF THROMBIN-    
TITLE    2 ACTIVATABLE FIBRINOLYSIS INHIBITOR (TAFI-IIYQ)                       
CAVEAT     3D68    NAG A 603 HAS WRONG CHIRALITY AT ATOM C1 NAG B 602 HAS WRONG 
CAVEAT   2 3D68    CHIRALITY AT ATOM C1                                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CARBOXYPEPTIDASE B2;                                       
COMPND   3 CHAIN: A, B, C;                                                      
COMPND   4 FRAGMENT: TAFI-IIYQ, UNP RESIDUES 24-423;                            
COMPND   5 SYNONYM: CARBOXYPEPTIDASE U, CPU, THROMBIN-ACTIVABLE FIBRINOLYSIS    
COMPND   6 INHIBITOR, TAFI, PLASMA CARBOXYPEPTIDASE B, PCPB;                    
COMPND   7 EC: 3.4.17.20;                                                       
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: CPB2;                                                          
SOURCE   6 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE   7 EXPRESSION_SYSTEM_COMMON: HUMAN;                                     
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE   9 EXPRESSION_SYSTEM_CELL_LINE: HEK293ES;                               
SOURCE  10 EXPRESSION_SYSTEM_CELL: EMBRYONIC KIDNEY CELL;                       
SOURCE  11 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  12 EXPRESSION_SYSTEM_PLASMID: PABC345                                   
KEYWDS    ALPHA/BETA HYDROLASE FOLD, CARBOXYPEPTIDASE, GLYCOPROTEIN, METAL-     
KEYWDS   2 BINDING, METALLOPROTEASE, PROTEASE, SECRETED, ZYMOGEN, HYDROLASE     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    T.H.C.BRONDIJK,E.G.HUIZINGA                                           
REVDAT   6   29-JUL-20 3D68    1       CAVEAT COMPND REMARK SEQADV              
REVDAT   6 2                   1       HETNAM LINK   SITE                       
REVDAT   5   20-JUN-18 3D68    1       SOURCE                                   
REVDAT   4   13-JUL-11 3D68    1       VERSN                                    
REVDAT   3   24-FEB-09 3D68    1       VERSN                                    
REVDAT   2   14-OCT-08 3D68    1       JRNL                                     
REVDAT   1   01-JUL-08 3D68    0                                                
JRNL        AUTH   P.F.MARX,T.H.BRONDIJK,T.PLUG,R.A.ROMIJN,W.HEMRIKA,           
JRNL        AUTH 2 J.C.M.MEIJERS,E.G.HUIZINGA                                   
JRNL        TITL   CRYSTAL STRUCTURES OF TAFI ELUCIDATE THE INACTIVATION        
JRNL        TITL 2 MECHANISM OF ACTIVATED TAFI: A NOVEL MECHANISM FOR ENZYME    
JRNL        TITL 3 AUTOREGULATION                                               
JRNL        REF    BLOOD                         V. 112  2803 2008              
JRNL        REFN                   ISSN 0006-4971                               
JRNL        PMID   18559974                                                     
JRNL        DOI    10.1182/BLOOD-2008-03-146001                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.3.0008                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 49.03                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 48058                          
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) : 0.190                           
REMARK   3   R VALUE            (WORKING SET) : 0.188                           
REMARK   3   FREE R VALUE                     : 0.232                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2582                            
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) : 2.80                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.87                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3489                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.97                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3470                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 193                          
REMARK   3   BIN FREE R VALUE                    : 0.3910                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 9747                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 193                                     
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 57.60                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 2.53000                                              
REMARK   3    B22 (A**2) : 2.53000                                              
REMARK   3    B33 (A**2) : -3.80000                                             
REMARK   3    B12 (A**2) : 1.27000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.585         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.300         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.248         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 29.163        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.951                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.929                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 10215 ; 0.018 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  6865 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 13890 ; 1.871 ; 1.949       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 16574 ; 1.027 ; 3.002       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1200 ; 8.307 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   480 ;34.557 ;23.500       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1668 ;19.436 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    60 ;16.974 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1520 ; 0.108 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 11195 ; 0.006 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  2163 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  2414 ; 0.246 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  7107 ; 0.206 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  4982 ; 0.209 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  5458 ; 0.103 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   204 ; 0.160 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):     1 ; 0.066 ; 0.200       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):     4 ; 0.103 ; 0.200       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    12 ; 0.253 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    37 ; 0.275 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     3 ; 0.160 ; 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):  7631 ; 0.924 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  2426 ; 0.128 ; 1.500       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  9750 ; 1.119 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  5042 ; 1.539 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  4140 ; 2.265 ; 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 : 1                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : A B C                           
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A      1       A     650      4                      
REMARK   3           1     B      1       B     650      4                      
REMARK   3           1     C      1       C     650      4                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  1    A    (A):   5585 ;  0.46 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  1    B    (A):   5585 ;  0.49 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  1    C    (A):   5585 ;  0.41 ;  0.50           
REMARK   3   MEDIUM THERMAL     1    A (A**2):   5585 ;  2.98 ;  NULL           
REMARK   3   MEDIUM THERMAL     1    B (A**2):   5585 ;  4.01 ;  NULL           
REMARK   3   MEDIUM THERMAL     1    C (A**2):   5585 ;  2.76 ;  NULL           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 6                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     1        A    92                          
REMARK   3    RESIDUE RANGE :   A   601        A   604                          
REMARK   3    ORIGIN FOR THE GROUP (A):  44.7643  55.3095  50.5661              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1123 T22:  -0.2091                                     
REMARK   3      T33:  -0.1693 T12:  -0.0431                                     
REMARK   3      T13:  -0.1735 T23:   0.1060                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.0614 L22:   3.7636                                     
REMARK   3      L33:   6.4372 L12:   0.3066                                     
REMARK   3      L13:   2.5110 L23:   1.3983                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0541 S12:  -0.3535 S13:   0.6387                       
REMARK   3      S21:   0.0557 S22:  -0.2094 S23:  -0.4513                       
REMARK   3      S31:  -0.4855 S32:   0.1252 S33:   0.1553                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    93        A   401                          
REMARK   3    RESIDUE RANGE :   A   501        A   501                          
REMARK   3    ORIGIN FOR THE GROUP (A):  33.4433  36.3912  37.6867              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1823 T22:  -0.2959                                     
REMARK   3      T33:  -0.3080 T12:   0.0170                                     
REMARK   3      T13:  -0.0918 T23:   0.0930                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2361 L22:   2.5960                                     
REMARK   3      L33:   5.9694 L12:  -0.3185                                     
REMARK   3      L13:   1.5874 L23:   1.1139                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1702 S12:  -0.1445 S13:   0.0166                       
REMARK   3      S21:   0.0540 S22:  -0.2830 S23:  -0.1740                       
REMARK   3      S31:   0.4786 S32:  -0.4164 S33:   0.1127                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B     1        B    92                          
REMARK   3    RESIDUE RANGE :   B   601        B   604                          
REMARK   3    ORIGIN FOR THE GROUP (A):  66.9100 -15.7114  11.8044              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1151 T22:  -0.1278                                     
REMARK   3      T33:  -0.0037 T12:   0.2910                                     
REMARK   3      T13:   0.0399 T23:   0.0735                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.1381 L22:   4.1479                                     
REMARK   3      L33:   5.1373 L12:   1.1337                                     
REMARK   3      L13:  -2.1901 L23:  -0.8472                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0616 S12:   0.3061 S13:  -0.1150                       
REMARK   3      S21:  -0.0053 S22:   0.1398 S23:  -0.6889                       
REMARK   3      S31:   0.5108 S32:   0.3943 S33:  -0.0782                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B    93        B   401                          
REMARK   3    RESIDUE RANGE :   B   501        B   501                          
REMARK   3    ORIGIN FOR THE GROUP (A):  47.5176  -5.0783  24.4376              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1490 T22:  -0.3385                                     
REMARK   3      T33:  -0.3672 T12:   0.0733                                     
REMARK   3      T13:   0.0369 T23:   0.1323                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.8572 L22:   3.5308                                     
REMARK   3      L33:   4.7415 L12:  -0.4731                                     
REMARK   3      L13:  -0.9699 L23:  -0.6566                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0162 S12:  -0.1246 S13:   0.0378                       
REMARK   3      S21:   0.1345 S22:  -0.0193 S23:  -0.2137                       
REMARK   3      S31:   0.3075 S32:  -0.3059 S33:   0.0031                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C     1        C    92                          
REMARK   3    RESIDUE RANGE :   C   601        C   604                          
REMARK   3    ORIGIN FOR THE GROUP (A):  63.6979  36.6268 -16.1290              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1742 T22:   0.3918                                     
REMARK   3      T33:   0.2385 T12:   0.1076                                     
REMARK   3      T13:   0.0404 T23:   0.3447                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.9689 L22:   4.9760                                     
REMARK   3      L33:   4.6747 L12:   1.2470                                     
REMARK   3      L13:  -1.1168 L23:  -1.9813                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0674 S12:   0.3464 S13:   0.3452                       
REMARK   3      S21:  -0.1421 S22:  -0.1166 S23:  -0.8155                       
REMARK   3      S31:  -0.1751 S32:   0.6903 S33:   0.1840                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C    93        C   401                          
REMARK   3    RESIDUE RANGE :   C   501        C   501                          
REMARK   3    ORIGIN FOR THE GROUP (A):  42.0760  29.4954  -5.1667              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.3723 T22:  -0.2424                                     
REMARK   3      T33:  -0.2344 T12:   0.1743                                     
REMARK   3      T13:   0.0185 T23:   0.1475                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4072 L22:   2.6039                                     
REMARK   3      L33:   4.1198 L12:  -0.7692                                     
REMARK   3      L13:  -0.2617 L23:  -1.0086                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1272 S12:  -0.0206 S13:   0.2213                       
REMARK   3      S21:  -0.0123 S22:  -0.1830 S23:  -0.3211                       
REMARK   3      S31:   0.0563 S32:   0.1516 S33:   0.3102                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
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 3D68 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 22-MAY-08.                  
REMARK 100 THE DEPOSITION ID IS D_1000047643.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 06-OCT-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID23-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97295                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XDS, SCALA                         
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 50644                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 49.030                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.700                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 4.300                              
REMARK 200  R MERGE                    (I) : 0.06700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 13.8000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.95                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.60000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.100                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 3D66                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 64.81                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.50                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 16-18% PEG 3000, 0.18-0.22MM NA/K        
REMARK 280  -TARTRATE, 50MM L-GLUTAMATE, 50MM L-ARGININE, PH 6.0, VAPOR         
REMARK 280  DIFFUSION, TEMPERATURE 277K                                         
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+2/3                                           
REMARK 290       6555   -X,-X+Y,-Z+1/3                                          
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       46.39333            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       92.78667            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       92.78667            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       46.39333            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3                                                 
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     GLY A   -22                                                      
REMARK 465     SER A   -21                                                      
REMARK 465     HIS A   -20                                                      
REMARK 465     HIS A   -19                                                      
REMARK 465     HIS A   -18                                                      
REMARK 465     HIS A   -17                                                      
REMARK 465     HIS A   -16                                                      
REMARK 465     HIS A   -15                                                      
REMARK 465     ASP A   -14                                                      
REMARK 465     TYR A   -13                                                      
REMARK 465     ASP A   -12                                                      
REMARK 465     ILE A   -11                                                      
REMARK 465     PRO A   -10                                                      
REMARK 465     SER A    -9                                                      
REMARK 465     SER A    -8                                                      
REMARK 465     GLU A    -7                                                      
REMARK 465     ASN A    -6                                                      
REMARK 465     LEU A    -5                                                      
REMARK 465     TYR A    -4                                                      
REMARK 465     PHE A    -3                                                      
REMARK 465     GLN A    -2                                                      
REMARK 465     GLY A    -1                                                      
REMARK 465     SER A     0                                                      
REMARK 465     GLY B   -22                                                      
REMARK 465     SER B   -21                                                      
REMARK 465     HIS B   -20                                                      
REMARK 465     HIS B   -19                                                      
REMARK 465     HIS B   -18                                                      
REMARK 465     HIS B   -17                                                      
REMARK 465     HIS B   -16                                                      
REMARK 465     HIS B   -15                                                      
REMARK 465     ASP B   -14                                                      
REMARK 465     TYR B   -13                                                      
REMARK 465     ASP B   -12                                                      
REMARK 465     ILE B   -11                                                      
REMARK 465     PRO B   -10                                                      
REMARK 465     SER B    -9                                                      
REMARK 465     SER B    -8                                                      
REMARK 465     GLU B    -7                                                      
REMARK 465     ASN B    -6                                                      
REMARK 465     LEU B    -5                                                      
REMARK 465     TYR B    -4                                                      
REMARK 465     PHE B    -3                                                      
REMARK 465     GLN B    -2                                                      
REMARK 465     GLY B    -1                                                      
REMARK 465     SER B     0                                                      
REMARK 465     GLY C   -22                                                      
REMARK 465     SER C   -21                                                      
REMARK 465     HIS C   -20                                                      
REMARK 465     HIS C   -19                                                      
REMARK 465     HIS C   -18                                                      
REMARK 465     HIS C   -17                                                      
REMARK 465     HIS C   -16                                                      
REMARK 465     HIS C   -15                                                      
REMARK 465     ASP C   -14                                                      
REMARK 465     TYR C   -13                                                      
REMARK 465     ASP C   -12                                                      
REMARK 465     ILE C   -11                                                      
REMARK 465     PRO C   -10                                                      
REMARK 465     SER C    -9                                                      
REMARK 465     SER C    -8                                                      
REMARK 465     GLU C    -7                                                      
REMARK 465     ASN C    -6                                                      
REMARK 465     LEU C    -5                                                      
REMARK 465     TYR C    -4                                                      
REMARK 465     PHE C    -3                                                      
REMARK 465     GLN C    -2                                                      
REMARK 465     GLY C    -1                                                      
REMARK 465     SER C     0                                                      
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   OH   TYR B   108     O    PRO B   135              2.17            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
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   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    GLU B 338   CB    GLU B 338   CG      0.132                       
REMARK 500    GLU B 338   CG    GLU B 338   CD      0.121                       
REMARK 500    GLU C 116   CG    GLU C 116   CD      0.097                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ASP A 366   N   -  CA  -  C   ANGL. DEV. = -21.6 DEGREES          
REMARK 500    PRO B 297   CA  -  C   -  N   ANGL. DEV. = -16.2 DEGREES          
REMARK 500    ASP C 120   CB  -  CG  -  OD1 ANGL. DEV. =   5.9 DEGREES          
REMARK 500    ILE C 125   CG1 -  CB  -  CG2 ANGL. DEV. = -15.9 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    GLN A   2      -58.48   -120.34                                   
REMARK 500    ASP A  38      -50.45     -5.59                                   
REMARK 500    LYS A  42      -95.38    -66.96                                   
REMARK 500    LYS A  43       40.47    -71.71                                   
REMARK 500    SER A  53      -34.21    -36.91                                   
REMARK 500    VAL A  89      -97.32    -37.11                                   
REMARK 500    ALA A  93        9.10     58.58                                   
REMARK 500    HIS A 118       56.11   -142.62                                   
REMARK 500    MET A 121      -47.78   -137.96                                   
REMARK 500    SER A 130     -176.98    -67.49                                   
REMARK 500    SER A 142     -152.97   -160.66                                   
REMARK 500    GLN A 146       80.53     39.30                                   
REMARK 500    THR A 147       81.95   -158.30                                   
REMARK 500    ASN A 202       59.87    -98.00                                   
REMARK 500    LYS A 212      -64.97    -99.06                                   
REMARK 500    ASN A 219     -176.54    -38.68                                   
REMARK 500    ALA A 224      -79.06    -18.31                                   
REMARK 500    HIS A 241       48.08   -104.20                                   
REMARK 500    GLU A 244     -148.71   -100.58                                   
REMARK 500    SER A 291      -14.43    128.39                                   
REMARK 500    GLN A 292       68.76     62.86                                   
REMARK 500    PRO A 297      161.47    -48.46                                   
REMARK 500    TYR A 298       86.70     54.43                                   
REMARK 500    LYS A 327     -136.20     72.31                                   
REMARK 500    LEU A 340      -90.71    -86.47                                   
REMARK 500    TYR A 341      171.06    176.28                                   
REMARK 500    LEU A 364     -155.39    -82.58                                   
REMARK 500    ASP A 366      162.31    168.29                                   
REMARK 500    LEU A 373       46.87    -95.58                                   
REMARK 500    GLN B   2      -50.84   -121.65                                   
REMARK 500    LEU B  10       89.43   -158.64                                   
REMARK 500    LYS B  42      -81.08    -32.33                                   
REMARK 500    LYS B  43       43.42   -100.11                                   
REMARK 500    THR B  88      -30.59     82.52                                   
REMARK 500    VAL B  89      -83.56    -36.76                                   
REMARK 500    LYS B 133       31.82     77.14                                   
REMARK 500    SER B 142      -95.14   -154.26                                   
REMARK 500    GLN B 146       66.51     12.38                                   
REMARK 500    ASN B 202       58.96    -92.73                                   
REMARK 500    ASN B 219     -178.99    -41.47                                   
REMARK 500    ALA B 224     -119.90     18.04                                   
REMARK 500    LYS B 240        4.85    -67.96                                   
REMARK 500    HIS B 241       44.27   -152.68                                   
REMARK 500    GLU B 244     -159.18    -95.40                                   
REMARK 500    TYR B 290     -167.64   -117.44                                   
REMARK 500    SER B 291      -11.98    120.01                                   
REMARK 500    PRO B 297      158.58    -42.54                                   
REMARK 500    TYR B 298       89.73     56.59                                   
REMARK 500    LYS B 327     -109.65     28.71                                   
REMARK 500    ASN B 328       61.65   -109.69                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      78 RAMACHANDRAN OUTLIERS.                        
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 ALA A   37     ASP A   38                  145.37                    
REMARK 500 PRO A  297     TYR A  298                 -143.26                    
REMARK 500 SER A  326     LYS A  327                  138.08                    
REMARK 500 ARG A  365     ASP A  366                  113.15                    
REMARK 500 PRO B  297     TYR B  298                 -143.25                    
REMARK 500 SER B  326     LYS B  327                  147.69                    
REMARK 500 LYS C  218     ASN C  219                  147.09                    
REMARK 500 PRO C  297     TYR C  298                  -96.99                    
REMARK 500 SER C  326     LYS C  327                  145.63                    
REMARK 500 LEU C  364     ARG C  365                 -144.41                    
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    PRO C 297        -11.94                                           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 501  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 159   ND1                                                    
REMARK 620 2 GLU A 162   OE1 113.4                                              
REMARK 620 3 HIS A 288   ND1  99.1  80.2                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 501  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B 159   ND1                                                    
REMARK 620 2 GLU B 162   OE1 112.6                                              
REMARK 620 3 HIS B 288   ND1 108.7  85.1                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN C 501  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS C 159   ND1                                                    
REMARK 620 2 GLU C 162   OE1 101.1                                              
REMARK 620 3 HIS C 288   ND1 106.1  88.3                                        
REMARK 620 N                    1     2                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3D66   RELATED DB: PDB                                   
REMARK 900 THROMBIN ACTIVATABLE FIBRINOLYSIS INHIBITOR                          
REMARK 900 RELATED ID: 3D67   RELATED DB: PDB                                   
REMARK 900 THROMBIN ACTIVATABLE FIBRINOLYSIS INHIBITOR IN COMPLEX WITH GEMSA    
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 THE SEQUENCE IS A NATURALLY OCCURING VARIANT BASED ON DBSNP:         
REMARK 999 RS3742264 (NCBI).                                                    
DBREF  3D68 A    2   401  UNP    Q96IY4   CBPB2_HUMAN     24    423             
DBREF  3D68 B    2   401  UNP    Q96IY4   CBPB2_HUMAN     24    423             
DBREF  3D68 C    2   401  UNP    Q96IY4   CBPB2_HUMAN     24    423             
SEQADV 3D68 GLY A  -22  UNP  Q96IY4              EXPRESSION TAG                 
SEQADV 3D68 SER A  -21  UNP  Q96IY4              EXPRESSION TAG                 
SEQADV 3D68 HIS A  -20  UNP  Q96IY4              EXPRESSION TAG                 
SEQADV 3D68 HIS A  -19  UNP  Q96IY4              EXPRESSION TAG                 
SEQADV 3D68 HIS A  -18  UNP  Q96IY4              EXPRESSION TAG                 
SEQADV 3D68 HIS A  -17  UNP  Q96IY4              EXPRESSION TAG                 
SEQADV 3D68 HIS A  -16  UNP  Q96IY4              EXPRESSION TAG                 
SEQADV 3D68 HIS A  -15  UNP  Q96IY4              EXPRESSION TAG                 
SEQADV 3D68 ASP A  -14  UNP  Q96IY4              EXPRESSION TAG                 
SEQADV 3D68 TYR A  -13  UNP  Q96IY4              EXPRESSION TAG                 
SEQADV 3D68 ASP A  -12  UNP  Q96IY4              EXPRESSION TAG                 
SEQADV 3D68 ILE A  -11  UNP  Q96IY4              EXPRESSION TAG                 
SEQADV 3D68 PRO A  -10  UNP  Q96IY4              EXPRESSION TAG                 
SEQADV 3D68 SER A   -9  UNP  Q96IY4              EXPRESSION TAG                 
SEQADV 3D68 SER A   -8  UNP  Q96IY4              EXPRESSION TAG                 
SEQADV 3D68 GLU A   -7  UNP  Q96IY4              EXPRESSION TAG                 
SEQADV 3D68 ASN A   -6  UNP  Q96IY4              EXPRESSION TAG                 
SEQADV 3D68 LEU A   -5  UNP  Q96IY4              EXPRESSION TAG                 
SEQADV 3D68 TYR A   -4  UNP  Q96IY4              EXPRESSION TAG                 
SEQADV 3D68 PHE A   -3  UNP  Q96IY4              EXPRESSION TAG                 
SEQADV 3D68 GLN A   -2  UNP  Q96IY4              EXPRESSION TAG                 
SEQADV 3D68 GLY A   -1  UNP  Q96IY4              EXPRESSION TAG                 
SEQADV 3D68 SER A    0  UNP  Q96IY4              EXPRESSION TAG                 
SEQADV 3D68 ALA A    1  UNP  Q96IY4              EXPRESSION TAG                 
SEQADV 3D68 THR A  147  UNP  Q96IY4    ALA   169 SEE REMARK 999                 
SEQADV 3D68 ILE A  325  UNP  Q96IY4    THR   347 ENGINEERED                     
SEQADV 3D68 ILE A  329  UNP  Q96IY4    THR   351 ENGINEERED                     
SEQADV 3D68 TYR A  333  UNP  Q96IY4    HIS   355 ENGINEERED                     
SEQADV 3D68 GLN A  335  UNP  Q96IY4    HIS   357 ENGINEERED                     
SEQADV 3D68 GLY B  -22  UNP  Q96IY4              EXPRESSION TAG                 
SEQADV 3D68 SER B  -21  UNP  Q96IY4              EXPRESSION TAG                 
SEQADV 3D68 HIS B  -20  UNP  Q96IY4              EXPRESSION TAG                 
SEQADV 3D68 HIS B  -19  UNP  Q96IY4              EXPRESSION TAG                 
SEQADV 3D68 HIS B  -18  UNP  Q96IY4              EXPRESSION TAG                 
SEQADV 3D68 HIS B  -17  UNP  Q96IY4              EXPRESSION TAG                 
SEQADV 3D68 HIS B  -16  UNP  Q96IY4              EXPRESSION TAG                 
SEQADV 3D68 HIS B  -15  UNP  Q96IY4              EXPRESSION TAG                 
SEQADV 3D68 ASP B  -14  UNP  Q96IY4              EXPRESSION TAG                 
SEQADV 3D68 TYR B  -13  UNP  Q96IY4              EXPRESSION TAG                 
SEQADV 3D68 ASP B  -12  UNP  Q96IY4              EXPRESSION TAG                 
SEQADV 3D68 ILE B  -11  UNP  Q96IY4              EXPRESSION TAG                 
SEQADV 3D68 PRO B  -10  UNP  Q96IY4              EXPRESSION TAG                 
SEQADV 3D68 SER B   -9  UNP  Q96IY4              EXPRESSION TAG                 
SEQADV 3D68 SER B   -8  UNP  Q96IY4              EXPRESSION TAG                 
SEQADV 3D68 GLU B   -7  UNP  Q96IY4              EXPRESSION TAG                 
SEQADV 3D68 ASN B   -6  UNP  Q96IY4              EXPRESSION TAG                 
SEQADV 3D68 LEU B   -5  UNP  Q96IY4              EXPRESSION TAG                 
SEQADV 3D68 TYR B   -4  UNP  Q96IY4              EXPRESSION TAG                 
SEQADV 3D68 PHE B   -3  UNP  Q96IY4              EXPRESSION TAG                 
SEQADV 3D68 GLN B   -2  UNP  Q96IY4              EXPRESSION TAG                 
SEQADV 3D68 GLY B   -1  UNP  Q96IY4              EXPRESSION TAG                 
SEQADV 3D68 SER B    0  UNP  Q96IY4              EXPRESSION TAG                 
SEQADV 3D68 ALA B    1  UNP  Q96IY4              EXPRESSION TAG                 
SEQADV 3D68 THR B  147  UNP  Q96IY4    ALA   169 SEE REMARK 999                 
SEQADV 3D68 ILE B  325  UNP  Q96IY4    THR   347 ENGINEERED                     
SEQADV 3D68 ILE B  329  UNP  Q96IY4    THR   351 ENGINEERED                     
SEQADV 3D68 TYR B  333  UNP  Q96IY4    HIS   355 ENGINEERED                     
SEQADV 3D68 GLN B  335  UNP  Q96IY4    HIS   357 ENGINEERED                     
SEQADV 3D68 GLY C  -22  UNP  Q96IY4              EXPRESSION TAG                 
SEQADV 3D68 SER C  -21  UNP  Q96IY4              EXPRESSION TAG                 
SEQADV 3D68 HIS C  -20  UNP  Q96IY4              EXPRESSION TAG                 
SEQADV 3D68 HIS C  -19  UNP  Q96IY4              EXPRESSION TAG                 
SEQADV 3D68 HIS C  -18  UNP  Q96IY4              EXPRESSION TAG                 
SEQADV 3D68 HIS C  -17  UNP  Q96IY4              EXPRESSION TAG                 
SEQADV 3D68 HIS C  -16  UNP  Q96IY4              EXPRESSION TAG                 
SEQADV 3D68 HIS C  -15  UNP  Q96IY4              EXPRESSION TAG                 
SEQADV 3D68 ASP C  -14  UNP  Q96IY4              EXPRESSION TAG                 
SEQADV 3D68 TYR C  -13  UNP  Q96IY4              EXPRESSION TAG                 
SEQADV 3D68 ASP C  -12  UNP  Q96IY4              EXPRESSION TAG                 
SEQADV 3D68 ILE C  -11  UNP  Q96IY4              EXPRESSION TAG                 
SEQADV 3D68 PRO C  -10  UNP  Q96IY4              EXPRESSION TAG                 
SEQADV 3D68 SER C   -9  UNP  Q96IY4              EXPRESSION TAG                 
SEQADV 3D68 SER C   -8  UNP  Q96IY4              EXPRESSION TAG                 
SEQADV 3D68 GLU C   -7  UNP  Q96IY4              EXPRESSION TAG                 
SEQADV 3D68 ASN C   -6  UNP  Q96IY4              EXPRESSION TAG                 
SEQADV 3D68 LEU C   -5  UNP  Q96IY4              EXPRESSION TAG                 
SEQADV 3D68 TYR C   -4  UNP  Q96IY4              EXPRESSION TAG                 
SEQADV 3D68 PHE C   -3  UNP  Q96IY4              EXPRESSION TAG                 
SEQADV 3D68 GLN C   -2  UNP  Q96IY4              EXPRESSION TAG                 
SEQADV 3D68 GLY C   -1  UNP  Q96IY4              EXPRESSION TAG                 
SEQADV 3D68 SER C    0  UNP  Q96IY4              EXPRESSION TAG                 
SEQADV 3D68 ALA C    1  UNP  Q96IY4              EXPRESSION TAG                 
SEQADV 3D68 THR C  147  UNP  Q96IY4    ALA   169 SEE REMARK 999                 
SEQADV 3D68 ILE C  325  UNP  Q96IY4    THR   347 ENGINEERED                     
SEQADV 3D68 ILE C  329  UNP  Q96IY4    THR   351 ENGINEERED                     
SEQADV 3D68 TYR C  333  UNP  Q96IY4    HIS   355 ENGINEERED                     
SEQADV 3D68 GLN C  335  UNP  Q96IY4    HIS   357 ENGINEERED                     
SEQRES   1 A  424  GLY SER HIS HIS HIS HIS HIS HIS ASP TYR ASP ILE PRO          
SEQRES   2 A  424  SER SER GLU ASN LEU TYR PHE GLN GLY SER ALA GLN SER          
SEQRES   3 A  424  GLY GLN VAL LEU ALA ALA LEU PRO ARG THR SER ARG GLN          
SEQRES   4 A  424  VAL GLN VAL LEU GLN ASN LEU THR THR THR TYR GLU ILE          
SEQRES   5 A  424  VAL LEU TRP GLN PRO VAL THR ALA ASP LEU ILE VAL LYS          
SEQRES   6 A  424  LYS LYS GLN VAL HIS PHE PHE VAL ASN ALA SER ASP VAL          
SEQRES   7 A  424  ASP ASN VAL LYS ALA HIS LEU ASN VAL SER GLY ILE PRO          
SEQRES   8 A  424  CYS SER VAL LEU LEU ALA ASP VAL GLU ASP LEU ILE GLN          
SEQRES   9 A  424  GLN GLN ILE SER ASN ASP THR VAL SER PRO ARG ALA SER          
SEQRES  10 A  424  ALA SER TYR TYR GLU GLN TYR HIS SER LEU ASN GLU ILE          
SEQRES  11 A  424  TYR SER TRP ILE GLU PHE ILE THR GLU ARG HIS PRO ASP          
SEQRES  12 A  424  MET LEU THR LYS ILE HIS ILE GLY SER SER PHE GLU LYS          
SEQRES  13 A  424  TYR PRO LEU TYR VAL LEU LYS VAL SER GLY LYS GLU GLN          
SEQRES  14 A  424  THR ALA LYS ASN ALA ILE TRP ILE ASP CYS GLY ILE HIS          
SEQRES  15 A  424  ALA ARG GLU TRP ILE SER PRO ALA PHE CYS LEU TRP PHE          
SEQRES  16 A  424  ILE GLY HIS ILE THR GLN PHE TYR GLY ILE ILE GLY GLN          
SEQRES  17 A  424  TYR THR ASN LEU LEU ARG LEU VAL ASP PHE TYR VAL MET          
SEQRES  18 A  424  PRO VAL VAL ASN VAL ASP GLY TYR ASP TYR SER TRP LYS          
SEQRES  19 A  424  LYS ASN ARG MET TRP ARG LYS ASN ARG SER PHE TYR ALA          
SEQRES  20 A  424  ASN ASN HIS CYS ILE GLY THR ASP LEU ASN ARG ASN PHE          
SEQRES  21 A  424  ALA SER LYS HIS TRP CYS GLU GLU GLY ALA SER SER SER          
SEQRES  22 A  424  SER CYS SER GLU THR TYR CYS GLY LEU TYR PRO GLU SER          
SEQRES  23 A  424  GLU PRO GLU VAL LYS ALA VAL ALA SER PHE LEU ARG ARG          
SEQRES  24 A  424  ASN ILE ASN GLN ILE LYS ALA TYR ILE SER MET HIS SER          
SEQRES  25 A  424  TYR SER GLN HIS ILE VAL PHE PRO TYR SER TYR THR ARG          
SEQRES  26 A  424  SER LYS SER LYS ASP HIS GLU GLU LEU SER LEU VAL ALA          
SEQRES  27 A  424  SER GLU ALA VAL ARG ALA ILE GLU LYS ILE SER LYS ASN          
SEQRES  28 A  424  ILE ARG TYR THR TYR GLY GLN GLY SER GLU THR LEU TYR          
SEQRES  29 A  424  LEU ALA PRO GLY GLY GLY ASP ASP TRP ILE TYR ASP LEU          
SEQRES  30 A  424  GLY ILE LYS TYR SER PHE THR ILE GLU LEU ARG ASP THR          
SEQRES  31 A  424  GLY THR TYR GLY PHE LEU LEU PRO GLU ARG TYR ILE LYS          
SEQRES  32 A  424  PRO THR CYS ARG GLU ALA PHE ALA ALA VAL SER LYS ILE          
SEQRES  33 A  424  ALA TRP HIS VAL ILE ARG ASN VAL                              
SEQRES   1 B  424  GLY SER HIS HIS HIS HIS HIS HIS ASP TYR ASP ILE PRO          
SEQRES   2 B  424  SER SER GLU ASN LEU TYR PHE GLN GLY SER ALA GLN SER          
SEQRES   3 B  424  GLY GLN VAL LEU ALA ALA LEU PRO ARG THR SER ARG GLN          
SEQRES   4 B  424  VAL GLN VAL LEU GLN ASN LEU THR THR THR TYR GLU ILE          
SEQRES   5 B  424  VAL LEU TRP GLN PRO VAL THR ALA ASP LEU ILE VAL LYS          
SEQRES   6 B  424  LYS LYS GLN VAL HIS PHE PHE VAL ASN ALA SER ASP VAL          
SEQRES   7 B  424  ASP ASN VAL LYS ALA HIS LEU ASN VAL SER GLY ILE PRO          
SEQRES   8 B  424  CYS SER VAL LEU LEU ALA ASP VAL GLU ASP LEU ILE GLN          
SEQRES   9 B  424  GLN GLN ILE SER ASN ASP THR VAL SER PRO ARG ALA SER          
SEQRES  10 B  424  ALA SER TYR TYR GLU GLN TYR HIS SER LEU ASN GLU ILE          
SEQRES  11 B  424  TYR SER TRP ILE GLU PHE ILE THR GLU ARG HIS PRO ASP          
SEQRES  12 B  424  MET LEU THR LYS ILE HIS ILE GLY SER SER PHE GLU LYS          
SEQRES  13 B  424  TYR PRO LEU TYR VAL LEU LYS VAL SER GLY LYS GLU GLN          
SEQRES  14 B  424  THR ALA LYS ASN ALA ILE TRP ILE ASP CYS GLY ILE HIS          
SEQRES  15 B  424  ALA ARG GLU TRP ILE SER PRO ALA PHE CYS LEU TRP PHE          
SEQRES  16 B  424  ILE GLY HIS ILE THR GLN PHE TYR GLY ILE ILE GLY GLN          
SEQRES  17 B  424  TYR THR ASN LEU LEU ARG LEU VAL ASP PHE TYR VAL MET          
SEQRES  18 B  424  PRO VAL VAL ASN VAL ASP GLY TYR ASP TYR SER TRP LYS          
SEQRES  19 B  424  LYS ASN ARG MET TRP ARG LYS ASN ARG SER PHE TYR ALA          
SEQRES  20 B  424  ASN ASN HIS CYS ILE GLY THR ASP LEU ASN ARG ASN PHE          
SEQRES  21 B  424  ALA SER LYS HIS TRP CYS GLU GLU GLY ALA SER SER SER          
SEQRES  22 B  424  SER CYS SER GLU THR TYR CYS GLY LEU TYR PRO GLU SER          
SEQRES  23 B  424  GLU PRO GLU VAL LYS ALA VAL ALA SER PHE LEU ARG ARG          
SEQRES  24 B  424  ASN ILE ASN GLN ILE LYS ALA TYR ILE SER MET HIS SER          
SEQRES  25 B  424  TYR SER GLN HIS ILE VAL PHE PRO TYR SER TYR THR ARG          
SEQRES  26 B  424  SER LYS SER LYS ASP HIS GLU GLU LEU SER LEU VAL ALA          
SEQRES  27 B  424  SER GLU ALA VAL ARG ALA ILE GLU LYS ILE SER LYS ASN          
SEQRES  28 B  424  ILE ARG TYR THR TYR GLY GLN GLY SER GLU THR LEU TYR          
SEQRES  29 B  424  LEU ALA PRO GLY GLY GLY ASP ASP TRP ILE TYR ASP LEU          
SEQRES  30 B  424  GLY ILE LYS TYR SER PHE THR ILE GLU LEU ARG ASP THR          
SEQRES  31 B  424  GLY THR TYR GLY PHE LEU LEU PRO GLU ARG TYR ILE LYS          
SEQRES  32 B  424  PRO THR CYS ARG GLU ALA PHE ALA ALA VAL SER LYS ILE          
SEQRES  33 B  424  ALA TRP HIS VAL ILE ARG ASN VAL                              
SEQRES   1 C  424  GLY SER HIS HIS HIS HIS HIS HIS ASP TYR ASP ILE PRO          
SEQRES   2 C  424  SER SER GLU ASN LEU TYR PHE GLN GLY SER ALA GLN SER          
SEQRES   3 C  424  GLY GLN VAL LEU ALA ALA LEU PRO ARG THR SER ARG GLN          
SEQRES   4 C  424  VAL GLN VAL LEU GLN ASN LEU THR THR THR TYR GLU ILE          
SEQRES   5 C  424  VAL LEU TRP GLN PRO VAL THR ALA ASP LEU ILE VAL LYS          
SEQRES   6 C  424  LYS LYS GLN VAL HIS PHE PHE VAL ASN ALA SER ASP VAL          
SEQRES   7 C  424  ASP ASN VAL LYS ALA HIS LEU ASN VAL SER GLY ILE PRO          
SEQRES   8 C  424  CYS SER VAL LEU LEU ALA ASP VAL GLU ASP LEU ILE GLN          
SEQRES   9 C  424  GLN GLN ILE SER ASN ASP THR VAL SER PRO ARG ALA SER          
SEQRES  10 C  424  ALA SER TYR TYR GLU GLN TYR HIS SER LEU ASN GLU ILE          
SEQRES  11 C  424  TYR SER TRP ILE GLU PHE ILE THR GLU ARG HIS PRO ASP          
SEQRES  12 C  424  MET LEU THR LYS ILE HIS ILE GLY SER SER PHE GLU LYS          
SEQRES  13 C  424  TYR PRO LEU TYR VAL LEU LYS VAL SER GLY LYS GLU GLN          
SEQRES  14 C  424  THR ALA LYS ASN ALA ILE TRP ILE ASP CYS GLY ILE HIS          
SEQRES  15 C  424  ALA ARG GLU TRP ILE SER PRO ALA PHE CYS LEU TRP PHE          
SEQRES  16 C  424  ILE GLY HIS ILE THR GLN PHE TYR GLY ILE ILE GLY GLN          
SEQRES  17 C  424  TYR THR ASN LEU LEU ARG LEU VAL ASP PHE TYR VAL MET          
SEQRES  18 C  424  PRO VAL VAL ASN VAL ASP GLY TYR ASP TYR SER TRP LYS          
SEQRES  19 C  424  LYS ASN ARG MET TRP ARG LYS ASN ARG SER PHE TYR ALA          
SEQRES  20 C  424  ASN ASN HIS CYS ILE GLY THR ASP LEU ASN ARG ASN PHE          
SEQRES  21 C  424  ALA SER LYS HIS TRP CYS GLU GLU GLY ALA SER SER SER          
SEQRES  22 C  424  SER CYS SER GLU THR TYR CYS GLY LEU TYR PRO GLU SER          
SEQRES  23 C  424  GLU PRO GLU VAL LYS ALA VAL ALA SER PHE LEU ARG ARG          
SEQRES  24 C  424  ASN ILE ASN GLN ILE LYS ALA TYR ILE SER MET HIS SER          
SEQRES  25 C  424  TYR SER GLN HIS ILE VAL PHE PRO TYR SER TYR THR ARG          
SEQRES  26 C  424  SER LYS SER LYS ASP HIS GLU GLU LEU SER LEU VAL ALA          
SEQRES  27 C  424  SER GLU ALA VAL ARG ALA ILE GLU LYS ILE SER LYS ASN          
SEQRES  28 C  424  ILE ARG TYR THR TYR GLY GLN GLY SER GLU THR LEU TYR          
SEQRES  29 C  424  LEU ALA PRO GLY GLY GLY ASP ASP TRP ILE TYR ASP LEU          
SEQRES  30 C  424  GLY ILE LYS TYR SER PHE THR ILE GLU LEU ARG ASP THR          
SEQRES  31 C  424  GLY THR TYR GLY PHE LEU LEU PRO GLU ARG TYR ILE LYS          
SEQRES  32 C  424  PRO THR CYS ARG GLU ALA PHE ALA ALA VAL SER LYS ILE          
SEQRES  33 C  424  ALA TRP HIS VAL ILE ARG ASN VAL                              
MODRES 3D68 ASN A   22  ASN  GLYCOSYLATION SITE                                 
MODRES 3D68 ASN A   51  ASN  GLYCOSYLATION SITE                                 
MODRES 3D68 ASN A   63  ASN  GLYCOSYLATION SITE                                 
MODRES 3D68 ASN A   86  ASN  GLYCOSYLATION SITE                                 
MODRES 3D68 ASN B   22  ASN  GLYCOSYLATION SITE                                 
MODRES 3D68 ASN B   51  ASN  GLYCOSYLATION SITE                                 
MODRES 3D68 ASN B   63  ASN  GLYCOSYLATION SITE                                 
MODRES 3D68 ASN B   86  ASN  GLYCOSYLATION SITE                                 
MODRES 3D68 ASN C   22  ASN  GLYCOSYLATION SITE                                 
MODRES 3D68 ASN C   51  ASN  GLYCOSYLATION SITE                                 
MODRES 3D68 ASN C   86  ASN  GLYCOSYLATION SITE                                 
HET    NAG  A 601      14                                                       
HET    NAG  A 602      14                                                       
HET    NAG  A 603      14                                                       
HET    NAG  A 604      14                                                       
HET     ZN  A 501       1                                                       
HET    ARG  A 650      12                                                       
HET    NAG  B 601      14                                                       
HET    NAG  B 602      14                                                       
HET    NAG  B 603      14                                                       
HET    NAG  B 604      14                                                       
HET     ZN  B 501       1                                                       
HET    ARG  B 650      12                                                       
HET    NAG  C 601      14                                                       
HET    NAG  C 602      14                                                       
HET    NAG  C 604      14                                                       
HET     ZN  C 501       1                                                       
HET    ARG  C 650      12                                                       
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
HETNAM      ZN ZINC ION                                                         
HETNAM     ARG ARGININE                                                         
FORMUL   4  NAG    11(C8 H15 N O6)                                              
FORMUL   8   ZN    3(ZN 2+)                                                     
FORMUL   9  ARG    3(C6 H15 N4 O2 1+)                                           
HELIX    1   1 THR A   13  TYR A   27  1                                  15    
HELIX    2   2 THR A   36  ILE A   40  5                                   5    
HELIX    3   3 ALA A   52  SER A   65  1                                  14    
HELIX    4   4 ASP A   75  ASN A   86  1                                  12    
HELIX    5   5 ASP A   87  VAL A   89  5                                   3    
HELIX    6   6 ALA A   95  GLN A  100  5                                   6    
HELIX    7   7 SER A  103  HIS A  118  1                                  16    
HELIX    8   8 TRP A  163  TYR A  180  1                                  18    
HELIX    9   9 ILE A  183  VAL A  193  1                                  11    
HELIX   10  10 ASN A  202  LYS A  212  1                                  11    
HELIX   11  11 ASP A  232  ASN A  236  5                                   5    
HELIX   12  12 GLU A  264  ILE A  278  1                                  15    
HELIX   13  13 ASP A  307  SER A  326  1                                  20    
HELIX   14  14 GLY A  336  LEU A  340  1                                   5    
HELIX   15  15 GLY A  346  LEU A  354  1                                   9    
HELIX   16  16 TYR A  370  LEU A  374  5                                   5    
HELIX   17  17 PRO A  375  ARG A  377  5                                   3    
HELIX   18  18 TYR A  378  VAL A  401  1                                  24    
HELIX   19  19 THR B   13  TYR B   27  1                                  15    
HELIX   20  20 THR B   36  ILE B   40  5                                   5    
HELIX   21  21 ALA B   52  SER B   65  1                                  14    
HELIX   22  22 ASP B   75  ASN B   86  1                                  12    
HELIX   23  23 SER B   96  GLN B  100  5                                   5    
HELIX   24  24 SER B  103  HIS B  118  1                                  16    
HELIX   25  25 TRP B  163  TYR B  180  1                                  18    
HELIX   26  26 ILE B  183  LEU B  192  1                                  10    
HELIX   27  27 ASN B  202  LYS B  212  1                                  11    
HELIX   28  28 ASP B  232  ASN B  236  5                                   5    
HELIX   29  29 GLU B  264  ARG B  276  1                                  13    
HELIX   30  30 ASP B  307  SER B  326  1                                  20    
HELIX   31  31 GLY B  336  LEU B  340  1                                   5    
HELIX   32  32 GLY B  346  LEU B  354  1                                   9    
HELIX   33  33 PRO B  375  ARG B  377  5                                   3    
HELIX   34  34 TYR B  378  ASN B  400  1                                  23    
HELIX   35  35 THR C   13  TYR C   27  1                                  15    
HELIX   36  36 THR C   36  ILE C   40  5                                   5    
HELIX   37  37 ASP C   54  SER C   65  1                                  12    
HELIX   38  38 ASP C   75  ASN C   86  1                                  12    
HELIX   39  39 SER C   94  GLN C  100  5                                   7    
HELIX   40  40 SER C  103  HIS C  118  1                                  16    
HELIX   41  41 TRP C  163  TYR C  180  1                                  18    
HELIX   42  42 ILE C  183  VAL C  193  1                                  11    
HELIX   43  43 ASN C  202  LYS C  212  1                                  11    
HELIX   44  44 ASP C  232  ASN C  236  5                                   5    
HELIX   45  45 GLU C  264  ASN C  277  1                                  14    
HELIX   46  46 ASP C  307  SER C  326  1                                  20    
HELIX   47  47 GLY C  336  LEU C  340  1                                   5    
HELIX   48  48 GLY C  346  LEU C  354  1                                   9    
HELIX   49  49 TYR C  370  LEU C  374  5                                   5    
HELIX   50  50 PRO C  375  VAL C  401  1                                  27    
SHEET    1   A 4 ILE A  29  GLN A  33  0                                        
SHEET    2   A 4 VAL A  46  ASN A  51 -1  O  HIS A  47   N  GLN A  33           
SHEET    3   A 4 GLY A   4  ALA A   9 -1  N  GLN A   5   O  VAL A  50           
SHEET    4   A 4 CYS A  69  LEU A  73 -1  O  SER A  70   N  ALA A   8           
SHEET    1   B 8 LEU A 122  SER A 129  0                                        
SHEET    2   B 8 PRO A 135  VAL A 141 -1  O  LEU A 136   N  GLY A 128           
SHEET    3   B 8 ASP A 194  MET A 198 -1  O  PHE A 195   N  VAL A 141           
SHEET    4   B 8 ALA A 151  ASP A 155  1  N  ILE A 154   O  TYR A 196           
SHEET    5   B 8 ILE A 281  HIS A 288  1  O  MET A 287   N  ASP A 155           
SHEET    6   B 8 TYR A 358  GLU A 363  1  O  PHE A 360   N  TYR A 284           
SHEET    7   B 8 HIS A 293  PHE A 296 -1  N  HIS A 293   O  GLU A 363           
SHEET    8   B 8 THR A 332  GLN A 335  1  O  THR A 332   N  ILE A 294           
SHEET    1   C 4 ILE B  29  GLN B  33  0                                        
SHEET    2   C 4 VAL B  46  ASN B  51 -1  O  HIS B  47   N  GLN B  33           
SHEET    3   C 4 GLY B   4  ALA B   9 -1  N  GLN B   5   O  VAL B  50           
SHEET    4   C 4 CYS B  69  LEU B  73 -1  O  SER B  70   N  ALA B   8           
SHEET    1   D 8 LEU B 122  SER B 129  0                                        
SHEET    2   D 8 PRO B 135  VAL B 141 -1  O  VAL B 138   N  ILE B 125           
SHEET    3   D 8 VAL B 193  MET B 198 -1  O  PHE B 195   N  VAL B 141           
SHEET    4   D 8 ASN B 150  ASP B 155  1  N  ILE B 154   O  TYR B 196           
SHEET    5   D 8 ILE B 281  SER B 289  1  O  ILE B 285   N  TRP B 153           
SHEET    6   D 8 TYR B 358  LEU B 364  1  O  LEU B 364   N  HIS B 288           
SHEET    7   D 8 HIS B 293  PHE B 296 -1  N  HIS B 293   O  GLU B 363           
SHEET    8   D 8 THR B 332  GLN B 335  1  O  THR B 332   N  ILE B 294           
SHEET    1   E 4 ILE C  29  GLN C  33  0                                        
SHEET    2   E 4 VAL C  46  ASN C  51 -1  O  HIS C  47   N  GLN C  33           
SHEET    3   E 4 GLY C   4  ALA C   9 -1  N  LEU C   7   O  PHE C  48           
SHEET    4   E 4 CYS C  69  LEU C  73 -1  O  SER C  70   N  ALA C   8           
SHEET    1   F 8 LEU C 122  SER C 129  0                                        
SHEET    2   F 8 PRO C 135  VAL C 141 -1  O  VAL C 138   N  ILE C 125           
SHEET    3   F 8 ASP C 194  MET C 198 -1  O  VAL C 197   N  LEU C 139           
SHEET    4   F 8 ALA C 151  ASP C 155  1  N  ILE C 154   O  TYR C 196           
SHEET    5   F 8 ILE C 281  HIS C 288  1  O  LYS C 282   N  ALA C 151           
SHEET    6   F 8 TYR C 358  GLU C 363  1  O  PHE C 360   N  SER C 286           
SHEET    7   F 8 HIS C 293  PHE C 296 -1  N  VAL C 295   O  THR C 361           
SHEET    8   F 8 THR C 332  GLN C 335  1  O  THR C 332   N  ILE C 294           
SSBOND   1 CYS A  156    CYS A  169                          1555   1555  2.04  
SSBOND   2 CYS A  228    CYS A  252                          1555   1555  2.07  
SSBOND   3 CYS A  243    CYS A  257                          1555   1555  2.09  
SSBOND   4 CYS B  156    CYS B  169                          1555   1555  2.01  
SSBOND   5 CYS B  228    CYS B  252                          1555   1555  2.08  
SSBOND   6 CYS B  243    CYS B  257                          1555   1555  2.13  
SSBOND   7 CYS C  156    CYS C  169                          1555   1555  2.02  
SSBOND   8 CYS C  228    CYS C  252                          1555   1555  2.09  
SSBOND   9 CYS C  243    CYS C  257                          1555   1555  2.08  
LINK         ND2 ASN A  22                 C1  NAG A 601     1555   1555  1.47  
LINK         ND2 ASN A  51                 C1  NAG A 602     1555   1555  1.45  
LINK         ND2 ASN A  63                 C1  NAG A 603     1555   1555  1.51  
LINK         ND2 ASN A  86                 C1  NAG A 604     1555   1555  1.47  
LINK         ND2 ASN B  22                 C1  NAG B 601     1555   1555  1.46  
LINK         ND2 ASN B  51                 C1  NAG B 602     1555   1555  1.44  
LINK         ND2 ASN B  63                 C1  NAG B 603     1555   1555  1.48  
LINK         ND2 ASN B  86                 C1  NAG B 604     1555   1555  1.47  
LINK         ND2 ASN C  22                 C1  NAG C 601     1555   1555  1.47  
LINK         ND2 ASN C  51                 C1  NAG C 602     1555   1555  1.46  
LINK         ND2 ASN C  86                 C1  NAG C 604     1555   1555  1.44  
LINK         ND1 HIS A 159                ZN    ZN A 501     1555   1555  2.17  
LINK         OE1 GLU A 162                ZN    ZN A 501     1555   1555  2.03  
LINK         ND1 HIS A 288                ZN    ZN A 501     1555   1555  2.11  
LINK         ND1 HIS B 159                ZN    ZN B 501     1555   1555  2.01  
LINK         OE1 GLU B 162                ZN    ZN B 501     1555   1555  2.01  
LINK         ND1 HIS B 288                ZN    ZN B 501     1555   1555  1.98  
LINK         ND1 HIS C 159                ZN    ZN C 501     1555   1555  1.88  
LINK         OE1 GLU C 162                ZN    ZN C 501     1555   1555  2.17  
LINK         ND1 HIS C 288                ZN    ZN C 501     1555   1555  2.10  
CISPEP   1 GLN A   33    PRO A   34          0        -0.34                     
CISPEP   2 GLY A  143    LYS A  144          0        -1.01                     
CISPEP   3 SER A  289    TYR A  290          0        -2.12                     
CISPEP   4 GLN B   33    PRO B   34          0        -6.19                     
CISPEP   5 GLY B  143    LYS B  144          0       -12.92                     
CISPEP   6 SER B  289    TYR B  290          0        -3.52                     
CISPEP   7 GLN C   33    PRO C   34          0       -10.72                     
CISPEP   8 GLY C  143    LYS C  144          0        -0.42                     
CISPEP   9 SER C  289    TYR C  290          0        -4.43                     
CRYST1  159.460  159.460  139.180  90.00  90.00 120.00 P 31 2 1     18          
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      0.006271  0.003621  0.000000        0.00000                         
SCALE2      0.000000  0.007241  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007185        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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