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Database: PDB
Entry: 4Z6A
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Original site: 4Z6A 
HEADER    HYDROLASE                               04-APR-15   4Z6A              
TITLE     CRYSTAL STRUCTURE OF A FVIIA-TRYPSIN CHIMERA (YT) IN COMPLEX WITH     
TITLE    2 SOLUBLE TISSUE FACTOR                                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: COAGULATION FACTOR VII;                                    
COMPND   3 CHAIN: L;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 108-203;                                      
COMPND   5 SYNONYM: PROCONVERTIN,SERUM PROTHROMBIN CONVERSION ACCELERATOR,SPCA; 
COMPND   6 EC: 3.4.21.21;                                                       
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: COAGULATION FACTOR VII;                                    
COMPND  10 CHAIN: H;                                                            
COMPND  11 FRAGMENT: UNP RESIDUES 213-465;                                      
COMPND  12 SYNONYM: PROCONVERTIN,SERUM PROTHROMBIN CONVERSION ACCELERATOR,SPCA; 
COMPND  13 EC: 3.4.21.21;                                                       
COMPND  14 ENGINEERED: YES;                                                     
COMPND  15 MUTATION: YES;                                                       
COMPND  16 MOL_ID: 3;                                                           
COMPND  17 MOLECULE: TISSUE FACTOR;                                             
COMPND  18 CHAIN: T;                                                            
COMPND  19 FRAGMENT: UNP RESIDUES 36-242;                                       
COMPND  20 SYNONYM: TF,COAGULATION FACTOR III,THROMBOPLASTIN;                   
COMPND  21 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 ORGAN: KIDNEY;                                                       
SOURCE   6 TISSUE: BLOOD;                                                       
SOURCE   7 GENE: F7;                                                            
SOURCE   8 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;                               
SOURCE   9 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;                           
SOURCE  10 EXPRESSION_SYSTEM_TAXID: 10029;                                      
SOURCE  11 EXPRESSION_SYSTEM_CELL_LINE: CHOEBNALT85;                            
SOURCE  12 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  13 EXPRESSION_SYSTEM_PLASMID: PQMCF-5;                                  
SOURCE  14 MOL_ID: 2;                                                           
SOURCE  15 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  16 ORGANISM_COMMON: HUMAN;                                              
SOURCE  17 ORGANISM_TAXID: 9606;                                                
SOURCE  18 ORGAN: KIDNEY;                                                       
SOURCE  19 TISSUE: BLOOD;                                                       
SOURCE  20 GENE: F7;                                                            
SOURCE  21 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;                               
SOURCE  22 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;                           
SOURCE  23 EXPRESSION_SYSTEM_TAXID: 10029;                                      
SOURCE  24 EXPRESSION_SYSTEM_CELL_LINE: CHOEBNALT85;                            
SOURCE  25 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  26 EXPRESSION_SYSTEM_PLASMID: PQMCF-5;                                  
SOURCE  27 MOL_ID: 3;                                                           
SOURCE  28 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  29 ORGANISM_COMMON: HUMAN;                                              
SOURCE  30 ORGANISM_TAXID: 9606;                                                
SOURCE  31 TISSUE: BLOOD;                                                       
SOURCE  32 GENE: F3;                                                            
SOURCE  33 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE  34 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;                           
SOURCE  35 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  36 EXPRESSION_SYSTEM_STRAIN: ORIGAMI 2;                                 
SOURCE  37 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  38 EXPRESSION_SYSTEM_PLASMID: PET3A                                     
KEYWDS    TRYPSIN-FOLD, PROTEIN-PROTEIN COMPLEX, HYDROLASE                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.B.SORENSEN,L.A.SVENSSON,P.S.GANDHI                                  
REVDAT   5   17-JAN-18 4Z6A    1       REMARK                                   
REVDAT   4   21-DEC-16 4Z6A    1       REMARK                                   
REVDAT   3   09-MAR-16 4Z6A    1       JRNL                                     
REVDAT   2   13-JAN-16 4Z6A    1       JRNL                                     
REVDAT   1   30-DEC-15 4Z6A    0                                                
JRNL        AUTH   A.B.SORENSEN,J.J.MADSEN,L.A.SVENSSON,A.A.PEDERSEN,           
JRNL        AUTH 2 H.STERGAARD,M.T.OVERGAARD,O.H.OLSEN,P.S.GANDHI               
JRNL        TITL   MOLECULAR BASIS OF ENHANCED ACTIVITY IN FACTOR VIIA-TRYPSIN  
JRNL        TITL 2 VARIANTS CONVEYS INSIGHTS INTO TISSUE FACTOR-MEDIATED        
JRNL        TITL 3 ALLOSTERIC REGULATION OF FACTOR VIIA ACTIVITY.               
JRNL        REF    J.BIOL.CHEM.                  V. 291  4671 2016              
JRNL        REFN                   ESSN 1083-351X                               
JRNL        PMID   26694616                                                     
JRNL        DOI    10.1074/JBC.M115.698613                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.25 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX                                               
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.25                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.51                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 32041                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.191                           
REMARK   3   R VALUE            (WORKING SET) : 0.188                           
REMARK   3   FREE R VALUE                     : 0.241                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.010                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1605                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 29.5155 -  4.9966    0.99     2997   169  0.1695 0.2083        
REMARK   3     2  4.9966 -  3.9690    0.99     2886   147  0.1319 0.1630        
REMARK   3     3  3.9690 -  3.4682    0.99     2864   138  0.1509 0.2300        
REMARK   3     4  3.4682 -  3.1515    0.99     2835   145  0.1786 0.2419        
REMARK   3     5  3.1515 -  2.9258    0.99     2816   138  0.2103 0.2525        
REMARK   3     6  2.9258 -  2.7534    0.99     2781   171  0.2183 0.2895        
REMARK   3     7  2.7534 -  2.6156    0.98     2806   130  0.2368 0.3269        
REMARK   3     8  2.6156 -  2.5018    0.98     2760   153  0.2566 0.2979        
REMARK   3     9  2.5018 -  2.4056    0.98     2754   150  0.2790 0.3488        
REMARK   3    10  2.4056 -  2.3226    0.95     2679   156  0.2847 0.2996        
REMARK   3    11  2.3226 -  2.2500    0.80     2258   108  0.3111 0.3603        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.320            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.820           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 36.89                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 48.91                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.008           4385                                  
REMARK   3   ANGLE     :  0.900           5976                                  
REMARK   3   CHIRALITY :  0.034            673                                  
REMARK   3   PLANARITY :  0.003            767                                  
REMARK   3   DIHEDRAL  : 12.027           1560                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 18                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'L' AND (RESID 48 THROUGH 86 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  -3.1362 -30.8094   2.8238              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5540 T22:   0.4558                                     
REMARK   3      T33:   0.5229 T12:   0.1526                                     
REMARK   3      T13:  -0.0587 T23:  -0.0915                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.4945 L22:   5.4213                                     
REMARK   3      L33:   3.4654 L12:  -0.2768                                     
REMARK   3      L13:   2.2267 L23:   1.3349                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.5086 S12:   0.6274 S13:  -0.7172                       
REMARK   3      S21:  -0.3789 S22:  -0.1252 S23:  -0.0709                       
REMARK   3      S31:   0.4589 S32:   0.2088 S33:  -0.2414                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'L' AND (RESID 87 THROUGH 143 )                  
REMARK   3    ORIGIN FOR THE GROUP (A): -19.0576 -33.6606  36.0048              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3741 T22:   0.3280                                     
REMARK   3      T33:   0.4900 T12:  -0.0862                                     
REMARK   3      T13:   0.0442 T23:  -0.1009                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1749 L22:   3.2800                                     
REMARK   3      L33:   5.4634 L12:   0.9616                                     
REMARK   3      L13:  -0.6230 L23:   0.7763                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3679 S12:   0.3661 S13:  -0.6800                       
REMARK   3      S21:  -0.1239 S22:  -0.0309 S23:   0.0378                       
REMARK   3      S31:   0.8514 S32:  -0.3607 S33:   0.2387                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'H' AND (RESID 16 THROUGH 50 )                   
REMARK   3    ORIGIN FOR THE GROUP (A): -18.7416 -13.6855  52.2195              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2387 T22:   0.2391                                     
REMARK   3      T33:   0.2824 T12:   0.0321                                     
REMARK   3      T13:   0.0230 T23:  -0.0303                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.5051 L22:   3.4209                                     
REMARK   3      L33:   4.1744 L12:  -0.1922                                     
REMARK   3      L13:   0.0922 L23:  -1.6254                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0620 S12:  -0.2876 S13:  -0.0622                       
REMARK   3      S21:   0.0109 S22:  -0.0340 S23:  -0.0176                       
REMARK   3      S31:  -0.0277 S32:   0.1075 S33:   0.0217                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'H' AND (RESID 51 THROUGH 80 )                   
REMARK   3    ORIGIN FOR THE GROUP (A): -17.2651 -13.8681  59.7693              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2680 T22:   0.2651                                     
REMARK   3      T33:   0.2199 T12:   0.0135                                     
REMARK   3      T13:   0.0524 T23:  -0.0027                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.3934 L22:   3.6344                                     
REMARK   3      L33:   2.9477 L12:  -0.0085                                     
REMARK   3      L13:  -0.0779 L23:   0.2061                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1012 S12:  -0.6136 S13:   0.1034                       
REMARK   3      S21:   0.4457 S22:  -0.0463 S23:   0.2421                       
REMARK   3      S31:  -0.0642 S32:  -0.3352 S33:  -0.0402                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'H' AND (RESID 81 THROUGH 103 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  -5.9343 -20.2578  58.7826              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3216 T22:   0.2714                                     
REMARK   3      T33:   0.3047 T12:   0.0540                                     
REMARK   3      T13:  -0.0305 T23:   0.0084                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.0355 L22:   1.4365                                     
REMARK   3      L33:   1.5004 L12:  -1.5301                                     
REMARK   3      L13:   0.8767 L23:   0.4118                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2396 S12:  -0.2199 S13:  -0.1267                       
REMARK   3      S21:   0.2894 S22:   0.2520 S23:  -0.0223                       
REMARK   3      S31:  -0.0293 S32:   0.2276 S33:   0.0231                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'H' AND (RESID 104 THROUGH 167 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -13.5081 -17.4805  45.4619              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1812 T22:   0.2490                                     
REMARK   3      T33:   0.2920 T12:   0.0184                                     
REMARK   3      T13:  -0.0172 T23:   0.0045                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4218 L22:   1.7726                                     
REMARK   3      L33:   2.8593 L12:  -0.6830                                     
REMARK   3      L13:  -0.7776 L23:   0.5603                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0264 S12:   0.0344 S13:  -0.0666                       
REMARK   3      S21:   0.0125 S22:  -0.0303 S23:   0.0092                       
REMARK   3      S31:   0.0493 S32:   0.0655 S33:   0.0663                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'H' AND (RESID 168 THROUGH 179 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   5.4726 -14.0864  41.7781              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1908 T22:   0.5572                                     
REMARK   3      T33:   0.3972 T12:   0.0236                                     
REMARK   3      T13:   0.0805 T23:   0.0048                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.0976 L22:   6.2269                                     
REMARK   3      L33:   3.6756 L12:   5.4862                                     
REMARK   3      L13:  -2.2848 L23:  -3.3897                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2935 S12:  -0.1124 S13:   0.2401                       
REMARK   3      S21:  -0.0651 S22:  -0.2121 S23:  -0.2272                       
REMARK   3      S31:  -0.0720 S32:   0.8744 S33:  -0.0342                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'H' AND (RESID 180 THROUGH 215 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -10.1409 -14.4526  41.8589              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2344 T22:   0.2316                                     
REMARK   3      T33:   0.3082 T12:   0.0570                                     
REMARK   3      T13:   0.0075 T23:   0.0242                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.9080 L22:   3.7377                                     
REMARK   3      L33:   3.3709 L12:   1.1382                                     
REMARK   3      L13:   0.3907 L23:   1.1884                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0507 S12:   0.0815 S13:   0.0251                       
REMARK   3      S21:  -0.2099 S22:  -0.0152 S23:  -0.1576                       
REMARK   3      S31:  -0.2097 S32:   0.0255 S33:  -0.0247                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN 'H' AND (RESID 216 THROUGH 243 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -4.3633 -19.7376  47.1008              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1585 T22:   0.2685                                     
REMARK   3      T33:   0.3006 T12:   0.0702                                     
REMARK   3      T13:  -0.0328 T23:   0.0198                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2391 L22:   6.5797                                     
REMARK   3      L33:   7.9988 L12:   1.7199                                     
REMARK   3      L13:  -2.1850 L23:  -5.8088                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0591 S12:   0.0711 S13:  -0.1888                       
REMARK   3      S21:  -0.1019 S22:  -0.0694 S23:  -0.5690                       
REMARK   3      S31:   0.3100 S32:   0.2258 S33:   0.0878                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: CHAIN 'H' AND (RESID 244 THROUGH 257 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -4.1785 -28.7656  63.0722              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5412 T22:   0.5128                                     
REMARK   3      T33:   0.4723 T12:  -0.0078                                     
REMARK   3      T13:  -0.0791 T23:   0.1378                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.4400 L22:   8.6493                                     
REMARK   3      L33:   2.2975 L12:   2.9768                                     
REMARK   3      L13:   3.7710 L23:   2.5408                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.7255 S12:  -0.6853 S13:  -0.3465                       
REMARK   3      S21:   1.1267 S22:  -0.1008 S23:  -0.6537                       
REMARK   3      S31:   0.6184 S32:  -1.0422 S33:  -0.4789                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: CHAIN 'T' AND (RESID 4 THROUGH 12 )                    
REMARK   3    ORIGIN FOR THE GROUP (A):  12.5561 -23.4441  24.6854              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5200 T22:   0.7595                                     
REMARK   3      T33:   0.4639 T12:   0.1669                                     
REMARK   3      T13:   0.0269 T23:  -0.0502                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.8936 L22:   8.8895                                     
REMARK   3      L33:   4.1814 L12:  -4.7641                                     
REMARK   3      L13:   4.1728 L23:  -5.6908                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0541 S12:   0.2350 S13:   0.9867                       
REMARK   3      S21:   0.1840 S22:  -0.1934 S23:  -0.9956                       
REMARK   3      S31:   0.3247 S32:   1.0790 S33:   0.1760                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: CHAIN 'T' AND (RESID 13 THROUGH 31 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):   4.3756 -22.6781  13.2547              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4471 T22:   0.5592                                     
REMARK   3      T33:   0.3362 T12:   0.1226                                     
REMARK   3      T13:   0.0952 T23:   0.0473                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.4692 L22:   2.9733                                     
REMARK   3      L33:   6.4241 L12:  -1.3077                                     
REMARK   3      L13:   2.7308 L23:  -1.0692                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1875 S12:  -0.0956 S13:  -0.0057                       
REMARK   3      S21:  -0.2167 S22:  -0.0043 S23:  -0.1384                       
REMARK   3      S31:   0.1067 S32:   0.4713 S33:   0.2086                       
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    SELECTION: CHAIN 'T' AND (RESID 32 THROUGH 70 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  -3.6666 -23.3589  19.4047              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2666 T22:   0.2740                                     
REMARK   3      T33:   0.3066 T12:   0.0604                                     
REMARK   3      T13:   0.0235 T23:  -0.0207                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.6700 L22:   2.3746                                     
REMARK   3      L33:   6.1193 L12:  -0.5409                                     
REMARK   3      L13:   0.9114 L23:  -1.5918                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0536 S12:   0.0522 S13:  -0.0197                       
REMARK   3      S21:  -0.1609 S22:  -0.0085 S23:   0.0300                       
REMARK   3      S31:   0.3015 S32:   0.0409 S33:  -0.0361                       
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    SELECTION: CHAIN 'T' AND (RESID 71 THROUGH 83 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):   2.8747 -25.7528  26.2348              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3296 T22:   0.5003                                     
REMARK   3      T33:   0.5266 T12:   0.1049                                     
REMARK   3      T13:   0.0369 T23:   0.0564                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.3803 L22:   6.9877                                     
REMARK   3      L33:   8.4812 L12:  -4.3683                                     
REMARK   3      L13:   0.9656 L23:   1.7350                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0540 S12:  -0.2792 S13:  -0.6837                       
REMARK   3      S21:   0.1430 S22:   0.4612 S23:   0.1721                       
REMARK   3      S31:   0.0207 S32:   0.1879 S33:  -0.4176                       
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    SELECTION: CHAIN 'T' AND (RESID 90 THROUGH 127 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  -4.5781 -14.1283   0.7085              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3315 T22:   0.2705                                     
REMARK   3      T33:   0.2793 T12:   0.0433                                     
REMARK   3      T13:  -0.0005 T23:   0.0463                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.9686 L22:   1.6763                                     
REMARK   3      L33:   5.4993 L12:  -1.0712                                     
REMARK   3      L13:   3.4208 L23:  -2.2262                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1028 S12:   0.3443 S13:   0.0715                       
REMARK   3      S21:  -0.2368 S22:  -0.0792 S23:   0.0713                       
REMARK   3      S31:   0.0540 S32:   0.6136 S33:  -0.0878                       
REMARK   3   TLS GROUP : 16                                                     
REMARK   3    SELECTION: CHAIN 'T' AND (RESID 128 THROUGH 150 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -13.8921 -17.6557   1.1272              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5923 T22:   0.4979                                     
REMARK   3      T33:   0.4358 T12:   0.1380                                     
REMARK   3      T13:  -0.0958 T23:  -0.0130                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.0337 L22:   6.3357                                     
REMARK   3      L33:   3.4042 L12:  -1.8482                                     
REMARK   3      L13:   1.7680 L23:  -4.3319                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2722 S12:   0.1748 S13:  -0.4359                       
REMARK   3      S21:  -0.4247 S22:  -0.4622 S23:   0.7434                       
REMARK   3      S31:   0.3015 S32:  -0.4237 S33:   0.0501                       
REMARK   3   TLS GROUP : 17                                                     
REMARK   3    SELECTION: CHAIN 'T' AND (RESID 151 THROUGH 178 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -5.0792  -5.2673 -15.8415              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4223 T22:   0.5111                                     
REMARK   3      T33:   0.4585 T12:   0.1174                                     
REMARK   3      T13:  -0.0569 T23:  -0.0191                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.8239 L22:   4.5771                                     
REMARK   3      L33:   2.1921 L12:  -0.0734                                     
REMARK   3      L13:  -1.6011 L23:  -2.1890                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0813 S12:   0.6734 S13:   0.1481                       
REMARK   3      S21:  -0.2528 S22:  -0.1898 S23:  -0.5338                       
REMARK   3      S31:   0.1025 S32:   0.3207 S33:   0.1455                       
REMARK   3   TLS GROUP : 18                                                     
REMARK   3    SELECTION: CHAIN 'T' AND (RESID 179 THROUGH 210 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -2.1697  -8.9778 -12.4035              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5518 T22:   0.4281                                     
REMARK   3      T33:   0.4319 T12:   0.2143                                     
REMARK   3      T13:  -0.0137 T23:   0.0293                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.3909 L22:   3.1473                                     
REMARK   3      L33:   2.4523 L12:  -1.0157                                     
REMARK   3      L13:   0.5251 L23:  -0.4905                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1384 S12:   0.5796 S13:   0.1068                       
REMARK   3      S21:  -0.2963 S22:  -0.1034 S23:  -0.3883                       
REMARK   3      S31:   0.3978 S32:   1.0241 S33:  -0.0258                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4Z6A COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 05-APR-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000208495.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 25-SEP-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.6                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : MAX II                             
REMARK 200  BEAMLINE                       : I911-3                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : SI (111)                           
REMARK 200  OPTICS                         : RH-COATED SI MIRRORS: M1           
REMARK 200                                   COLLIMATING MIRROR, M2 TOROIDAL    
REMARK 200                                   FOCUSING MIRROR                    
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 225 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS MARCH 30, 2013                 
REMARK 200  DATA SCALING SOFTWARE          : XSCALE JULY 4, 2012                
REMARK 200                                   BUILT=20130706                     
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 32041                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.250                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 29.516                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.0                               
REMARK 200  DATA REDUNDANCY                : 4.800                              
REMARK 200  R MERGE                    (I) : 0.14340                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.3300                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.25                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.33                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 81.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 1.43300                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 0.640                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER 2.5.7                                          
REMARK 200 STARTING MODEL: IN-HOUSE FVIIA-WT:STF-FFR SIMILAR TO 1DAN            
REMARK 200                                                                      
REMARK 200 REMARK: ELONGATED HEXGONAL PRISMS                                    
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 55.76                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.78                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M NACITRATE, 16.6% PEG 3350, 12.5%    
REMARK 280  1-PROPANOL, WITH SEEDING, PH 5.6, VAPOR DIFFUSION, HANGING DROP,    
REMARK 280  TEMPERATURE 295K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       33.51500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       62.28000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       40.85000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       62.28000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       33.51500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       40.85000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 5770 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 23770 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: L, H, T                               
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 L   107                                                      
REMARK 465     THR L   108                                                      
REMARK 465     GLU T    84                                                      
REMARK 465     SER T    85                                                      
REMARK 465     THR T    86                                                      
REMARK 465     GLY T    87                                                      
REMARK 465     SER T    88                                                      
REMARK 465     ALA T    89                                                      
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     ASP L  48    CG   OD1  OD2                                       
REMARK 470     GLN L  49    CG   CD   OE1  NE2                                  
REMARK 470     LYS L  62    CG   CD   CE   NZ                                   
REMARK 470     LEU L  65    CG   CD1  CD2                                       
REMARK 470     ASP L  86    CG   OD1  OD2                                       
REMARK 470     ASP L  87    CG   OD1  OD2                                       
REMARK 470     LEU L  89    CG   CD1  CD2                                       
REMARK 470     LYS L 109    CG   CD   CE   NZ                                   
REMARK 470     ARG L 110    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS L 143    CG   CD   CE   NZ                                   
REMARK 470     LYS H  20    CD   CE   NZ                                        
REMARK 470     LYS H  60A   CD   CE   NZ                                        
REMARK 470     LYS H  60C   CG   CD   CE   NZ                                   
REMARK 470     ARG H  62    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS H 175    CG   CD   CE   NZ                                   
REMARK 470     GLU H 245    CG   CD   OE1  OE2                                  
REMARK 470     THR T   4    OG1  CG2                                            
REMARK 470     LYS T  28    CD   CE   NZ                                        
REMARK 470     LYS T  41    CG   CD   CE   NZ                                   
REMARK 470     ASN T  82    CG   OD1  ND2                                       
REMARK 470     LYS T 122    CE   NZ                                             
REMARK 470     ASN T 137    CG   OD1  ND2                                       
REMARK 470     ASN T 138    CG   OD1  ND2                                       
REMARK 470     LYS T 149    CD   CE   NZ                                        
REMARK 470     SER T 160    OG                                                  
REMARK 470     SER T 162    OG                                                  
REMARK 470     LYS T 181    CG   CD   CE   NZ                                   
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   OG   SER H   195     H35  0Z6 H   501              0.44            
REMARK 500   O    GLY H   216     H2   0Z6 H   501              1.15            
REMARK 500   O    GLY H   216     H    0Z6 H   501              1.47            
REMARK 500   O    GLY L    96     N    LYS L   109              2.06            
REMARK 500   OG   SER H   195     O2   0Z6 H   501              2.18            
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    SER L  67     -155.05   -167.57                                   
REMARK 500    GLN L  88       50.37   -151.13                                   
REMARK 500    GLN L 100      -96.69   -121.79                                   
REMARK 500    ASP L 104     -153.08   -105.78                                   
REMARK 500    ARG L 110       35.51     73.63                                   
REMARK 500    SER L 111       88.22     76.80                                   
REMARK 500    VAL L 125      -31.16   -140.52                                   
REMARK 500    LEU H  40      -63.63   -108.23                                   
REMARK 500    HIS H  71      -60.89   -143.83                                   
REMARK 500    THR H 129C     -57.78   -122.38                                   
REMARK 500    SER H 214      -67.08   -122.68                                   
REMARK 500    PHE T  19       -4.00     75.78                                   
REMARK 500    THR T 172     -150.48   -114.15                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH T 463        DISTANCE =  6.58 ANGSTROMS                       
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     BGC L  201                                                       
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 H 502  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU H  70   OE1                                                    
REMARK 620 2 GLU H  70   OE2  51.5                                              
REMARK 620 3 ASP H  72   O    92.3  99.5                                        
REMARK 620 4 GLU H  75   O   163.3 123.9  72.1                                  
REMARK 620 5 GLU H  80   OE1 100.5 107.4 152.7  96.2                            
REMARK 620 6 HOH H 687   O    74.3 125.7  82.9 108.6  77.5                      
REMARK 620 7 HOH H 606   O   106.9  55.6 102.9  72.0  96.4 173.9                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 630                                                                      
REMARK 630 MOLECULE TYPE: PEPTIDE-LIKE INHIBITOR                                
REMARK 630 MOLECULE NAME: D-PHENYLALANYL-N-[(2S,3S)-6-{[AMINO(IMINIO)METHYL]    
REMARK 630 AMINO}-1-CHLORO-2-HYDROXYHEXAN-3-YL]-L-PHENYLALANINAMIDE             
REMARK 630 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 630  SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                           
REMARK 630                                                                      
REMARK 630   M RES C SSSEQI                                                     
REMARK 630     0Z6 H   501                                                      
REMARK 630 SOURCE: NULL                                                         
REMARK 630 TAXONOMY: NULL                                                       
REMARK 630 SUBCOMP:    DPN PHE AR7 0QE                                          
REMARK 630 DETAILS: NULL                                                        
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BGC L 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 0Z6 H 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA H 502                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CIT T 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide FUC L 202 bound   
REMARK 800  to SER L 60                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4YLQ   RELATED DB: PDB                                   
DBREF  4Z6A L   48   143  UNP    P08709   FA7_HUMAN      108    203             
DBREF  4Z6A H   16   257  UNP    P08709   FA7_HUMAN      213    466             
DBREF  4Z6A T    4   210  UNP    P13726   TF_HUMAN        36    242             
SEQADV 4Z6A     H       UNP  P08709    LEU   371 DELETION                       
SEQADV 4Z6A     H       UNP  P08709    GLN   372 DELETION                       
SEQADV 4Z6A     H       UNP  P08709    GLN   373 DELETION                       
SEQADV 4Z6A     H       UNP  P08709    SER   374 DELETION                       
SEQADV 4Z6A     H       UNP  P08709    ARG   375 DELETION                       
SEQADV 4Z6A GLU H  169  UNP  P08709    LYS   376 ENGINEERED MUTATION            
SEQADV 4Z6A ALA H  170  UNP  P08709    VAL   377 ENGINEERED MUTATION            
SEQADV 4Z6A SER H  171  UNP  P08709    GLY   378 ENGINEERED MUTATION            
SEQADV 4Z6A TYR H  172  UNP  P08709    ASP   379 ENGINEERED MUTATION            
SEQADV 4Z6A PRO H  173  UNP  P08709    SER   380 ENGINEERED MUTATION            
SEQADV 4Z6A GLY H  174  UNP  P08709    PRO   381 ENGINEERED MUTATION            
SEQADV 4Z6A LYS H  175  UNP  P08709    ASN   382 ENGINEERED MUTATION            
SEQRES   1 L   96  ASP GLN CYS ALA SER SER PRO CYS GLN ASN GLY GLY SER          
SEQRES   2 L   96  CYS LYS ASP GLN LEU GLN SER TYR ILE CYS PHE CYS LEU          
SEQRES   3 L   96  PRO ALA PHE GLU GLY ARG ASN CYS GLU THR HIS LYS ASP          
SEQRES   4 L   96  ASP GLN LEU ILE CYS VAL ASN GLU ASN GLY GLY CYS GLU          
SEQRES   5 L   96  GLN TYR CYS SER ASP HIS THR GLY THR LYS ARG SER CYS          
SEQRES   6 L   96  ARG CYS HIS GLU GLY TYR SER LEU LEU ALA ASP GLY VAL          
SEQRES   7 L   96  SER CYS THR PRO THR VAL GLU TYR PRO CYS GLY LYS ILE          
SEQRES   8 L   96  PRO ILE LEU GLU LYS                                          
SEQRES   1 H  249  ILE VAL GLY GLY LYS VAL CYS PRO LYS GLY GLU CYS PRO          
SEQRES   2 H  249  TRP GLN VAL LEU LEU LEU VAL ASN GLY ALA GLN LEU CYS          
SEQRES   3 H  249  GLY GLY THR LEU ILE ASN THR ILE TRP VAL VAL SER ALA          
SEQRES   4 H  249  ALA HIS CYS PHE ASP LYS ILE LYS ASN TRP ARG ASN LEU          
SEQRES   5 H  249  ILE ALA VAL LEU GLY GLU HIS ASP LEU SER GLU HIS ASP          
SEQRES   6 H  249  GLY ASP GLU GLN SER ARG ARG VAL ALA GLN VAL ILE ILE          
SEQRES   7 H  249  PRO SER THR TYR VAL PRO GLY THR THR ASN HIS ASP ILE          
SEQRES   8 H  249  ALA LEU LEU ARG LEU HIS GLN PRO VAL VAL LEU THR ASP          
SEQRES   9 H  249  HIS VAL VAL PRO LEU CYS LEU PRO GLU ARG THR PHE SER          
SEQRES  10 H  249  GLU ARG THR LEU ALA PHE VAL ARG PHE SER LEU VAL SER          
SEQRES  11 H  249  GLY TRP GLY GLN LEU LEU ASP ARG GLY ALA THR ALA LEU          
SEQRES  12 H  249  GLU LEU MET VAL LEU ASN VAL PRO ARG LEU MET THR GLN          
SEQRES  13 H  249  ASP CYS GLU ALA SER TYR PRO GLY LYS ILE THR GLU TYR          
SEQRES  14 H  249  MET PHE CYS ALA GLY TYR SER ASP GLY SER LYS ASP SER          
SEQRES  15 H  249  CYS LYS GLY ASP SER GLY GLY PRO HIS ALA THR HIS TYR          
SEQRES  16 H  249  ARG GLY THR TRP TYR LEU THR GLY ILE VAL SER TRP GLY          
SEQRES  17 H  249  GLN GLY CYS ALA THR VAL GLY HIS PHE GLY VAL TYR THR          
SEQRES  18 H  249  ARG VAL SER GLN TYR ILE GLU TRP LEU GLN LYS LEU MET          
SEQRES  19 H  249  ARG SER GLU PRO ARG PRO GLY VAL LEU LEU ARG ALA PRO          
SEQRES  20 H  249  PHE PRO                                                      
SEQRES   1 T  207  THR ASN THR VAL ALA ALA TYR ASN LEU THR TRP LYS SER          
SEQRES   2 T  207  THR ASN PHE LYS THR ILE LEU GLU TRP GLU PRO LYS PRO          
SEQRES   3 T  207  VAL ASN GLN VAL TYR THR VAL GLN ILE SER THR LYS SER          
SEQRES   4 T  207  GLY ASP TRP LYS SER LYS CYS PHE TYR THR THR ASP THR          
SEQRES   5 T  207  GLU CYS ASP LEU THR ASP GLU ILE VAL LYS ASP VAL LYS          
SEQRES   6 T  207  GLN THR TYR LEU ALA ARG VAL PHE SER TYR PRO ALA GLY          
SEQRES   7 T  207  ASN VAL GLU SER THR GLY SER ALA GLY GLU PRO LEU TYR          
SEQRES   8 T  207  GLU ASN SER PRO GLU PHE THR PRO TYR LEU GLU THR ASN          
SEQRES   9 T  207  LEU GLY GLN PRO THR ILE GLN SER PHE GLU GLN VAL GLY          
SEQRES  10 T  207  THR LYS VAL ASN VAL THR VAL GLU ASP GLU ARG THR LEU          
SEQRES  11 T  207  VAL ARG ARG ASN ASN THR PHE LEU SER LEU ARG ASP VAL          
SEQRES  12 T  207  PHE GLY LYS ASP LEU ILE TYR THR LEU TYR TYR TRP LYS          
SEQRES  13 T  207  SER SER SER SER GLY LYS LYS THR ALA LYS THR ASN THR          
SEQRES  14 T  207  ASN GLU PHE LEU ILE ASP VAL ASP LYS GLY GLU ASN TYR          
SEQRES  15 T  207  CYS PHE SER VAL GLN ALA VAL ILE PRO SER ARG THR VAL          
SEQRES  16 T  207  ASN ARG LYS SER THR ASP SER PRO VAL GLU CYS MET              
HET    BGC  L 201      22                                                       
HET    FUC  L 202      20                                                       
HET    0Z6  H 501      70                                                       
HET     CA  H 502       1                                                       
HET    CIT  T 301      18                                                       
HETNAM     BGC BETA-D-GLUCOSE                                                   
HETNAM     FUC ALPHA-L-FUCOSE                                                   
HETNAM     0Z6 D-PHENYLALANYL-N-[(2S,3S)-6-{[AMINO(IMINIO)                      
HETNAM   2 0Z6  METHYL]AMINO}-1-CHLORO-2-HYDROXYHEXAN-3-YL]-L-                  
HETNAM   3 0Z6  PHENYLALANINAMIDE                                               
HETNAM      CA CALCIUM ION                                                      
HETNAM     CIT CITRIC ACID                                                      
HETSYN     0Z6 FFRCK                                                            
FORMUL   4  BGC    C6 H12 O6                                                    
FORMUL   5  FUC    C6 H12 O5                                                    
FORMUL   6  0Z6    C25 H36 CL N6 O3 1+                                          
FORMUL   7   CA    CA 2+                                                        
FORMUL   8  CIT    C6 H8 O7                                                     
FORMUL   9  HOH   *230(H2 O)                                                    
HELIX    1 AA1 ASP L   48  SER L   53  5                                   6    
HELIX    2 AA2 ASN L   93  CYS L   98  5                                   6    
HELIX    3 AA3 ILE L  138  LYS L  143  1                                   6    
HELIX    4 AA4 ALA H   55  ASP H   60  5                                   6    
HELIX    5 AA5 ASN H   60D ARG H   62  5                                   3    
HELIX    6 AA6 GLU H  125  THR H  129C 1                                   8    
HELIX    7 AA7 LEU H  130  VAL H  133  5                                   4    
HELIX    8 AA8 MET H  164  GLU H  169  1                                   6    
HELIX    9 AA9 TYR H  234  MET H  242  1                                   9    
HELIX   10 AB1 LEU T   59  VAL T   64  1                                   6    
HELIX   11 AB2 THR T  101  THR T  106  1                                   6    
HELIX   12 AB3 LEU T  143  GLY T  148  1                                   6    
HELIX   13 AB4 LYS T  149  LEU T  151  5                                   3    
SHEET    1 AA1 2 SER L  60  ASP L  63  0                                        
SHEET    2 AA1 2 TYR L  68  PHE L  71 -1  O  PHE L  71   N  SER L  60           
SHEET    1 AA2 2 PHE L  76  GLU L  77  0                                        
SHEET    2 AA2 2 THR L  83  HIS L  84 -1  O  THR L  83   N  GLU L  77           
SHEET    1 AA3 2 TYR L 101  CYS L 102  0                                        
SHEET    2 AA3 2 CYS L 112  ARG L 113 -1  O  ARG L 113   N  TYR L 101           
SHEET    1 AA4 2 TYR L 118  LEU L 120  0                                        
SHEET    2 AA4 2 CYS L 127  PRO L 129 -1  O  THR L 128   N  SER L 119           
SHEET    1 AA5 8 LYS H  20  VAL H  21  0                                        
SHEET    2 AA5 8 MET H 156  LEU H 163 -1  O  VAL H 157   N  LYS H  20           
SHEET    3 AA5 8 MET H 180  ALA H 183 -1  O  CYS H 182   N  LEU H 163           
SHEET    4 AA5 8 GLY H 226  ARG H 230 -1  O  TYR H 228   N  PHE H 181           
SHEET    5 AA5 8 THR H 206  TRP H 215 -1  N  TRP H 215   O  VAL H 227           
SHEET    6 AA5 8 PRO H 198  TYR H 203 -1  N  TYR H 203   O  THR H 206           
SHEET    7 AA5 8 PHE H 135  GLY H 140 -1  N  LEU H 137   O  ALA H 200           
SHEET    8 AA5 8 MET H 156  LEU H 163 -1  O  VAL H 160   N  SER H 136           
SHEET    1 AA6 8 LEU H 251  ALA H 254  0                                        
SHEET    2 AA6 8 GLN H  81  PRO H  91  1  N  ILE H  90   O  LEU H 252           
SHEET    3 AA6 8 ALA H 104  LEU H 108 -1  O  LEU H 105   N  ILE H  89           
SHEET    4 AA6 8 TRP H  51  SER H  54 -1  N  VAL H  52   O  LEU H 106           
SHEET    5 AA6 8 ALA H  38  LEU H  46 -1  N  THR H  45   O  VAL H  53           
SHEET    6 AA6 8 GLN H  30  VAL H  35 -1  N  VAL H  31   O  GLY H  44           
SHEET    7 AA6 8 LEU H  64  LEU H  68 -1  O  ILE H  65   N  LEU H  34           
SHEET    8 AA6 8 GLN H  81  PRO H  91 -1  O  GLN H  81   N  LEU H  68           
SHEET    1 AA7 3 TYR T  10  THR T  17  0                                        
SHEET    2 AA7 3 LYS T  20  GLU T  26 -1  O  ILE T  22   N  LYS T  15           
SHEET    3 AA7 3 GLU T  56  ASP T  58 -1  O  CYS T  57   N  LEU T  23           
SHEET    1 AA8 4 LYS T  46  THR T  52  0                                        
SHEET    2 AA8 4 GLN T  32  THR T  40 -1  N  TYR T  34   O  THR T  52           
SHEET    3 AA8 4 TYR T  71  PRO T  79 -1  O  PHE T  76   N  THR T  35           
SHEET    4 AA8 4 TYR T  94  ASN T  96 -1  O  GLU T  95   N  VAL T  75           
SHEET    1 AA9 3 ILE T 113  VAL T 119  0                                        
SHEET    2 AA9 3 LYS T 122  VAL T 127 -1  O  ASN T 124   N  GLU T 117           
SHEET    3 AA9 3 GLU T 174  ASP T 178 -1  O  PHE T 175   N  VAL T 125           
SHEET    1 AB1 2 ARG T 131  ARG T 136  0                                        
SHEET    2 AB1 2 THR T 139  SER T 142 -1  O  THR T 139   N  ARG T 136           
SHEET    1 AB2 4 LYS T 166  THR T 170  0                                        
SHEET    2 AB2 4 ILE T 152  LYS T 159 -1  N  TYR T 157   O  LYS T 166           
SHEET    3 AB2 4 TYR T 185  VAL T 192 -1  O  SER T 188   N  TYR T 156           
SHEET    4 AB2 4 GLU T 208  CYS T 209 -1  O  GLU T 208   N  PHE T 187           
SSBOND   1 CYS L   50    CYS L   61                          1555   1555  2.03  
SSBOND   2 CYS L   55    CYS L   70                          1555   1555  2.03  
SSBOND   3 CYS L   72    CYS L   81                          1555   1555  2.04  
SSBOND   4 CYS L   91    CYS L  102                          1555   1555  2.04  
SSBOND   5 CYS L   98    CYS L  112                          1555   1555  2.03  
SSBOND   6 CYS L  114    CYS L  127                          1555   1555  2.03  
SSBOND   7 CYS L  135    CYS H  122                          1555   1555  2.03  
SSBOND   8 CYS H   22    CYS H   27                          1555   1555  2.05  
SSBOND   9 CYS H   41    CYS H   58                          1555   1555  2.04  
SSBOND  10 CYS H  168    CYS H  182                          1555   1555  2.03  
SSBOND  11 CYS H  191    CYS H  219                          1555   1555  2.03  
SSBOND  12 CYS T   49    CYS T   57                          1555   1555  2.05  
SSBOND  13 CYS T  186    CYS T  209                          1555   1555  2.04  
LINK         OG  SER L  60                 C1  FUC L 202     1555   1555  1.37  
LINK         NE2 HIS H  57                 C3  0Z6 H 501     1555   1555  1.43  
LINK         OE1 GLU H  70                CA    CA H 502     1555   1555  2.21  
LINK         OE2 GLU H  70                CA    CA H 502     1555   1555  2.71  
LINK         O   ASP H  72                CA    CA H 502     1555   1555  2.46  
LINK         O   GLU H  75                CA    CA H 502     1555   1555  2.36  
LINK         OE1 GLU H  80                CA    CA H 502     1555   1555  2.50  
LINK         OG  SER H 195                 C2  0Z6 H 501     1555   1555  1.38  
LINK         O   GLY H 216                 N   0Z6 H 501     1555   1555  1.30  
LINK        CA    CA H 502                 O   HOH H 687     1555   1555  2.55  
LINK        CA    CA H 502                 O   HOH H 606     1555   1555  2.49  
CISPEP   1 ASP L  104    HIS L  105          0         6.49                     
CISPEP   2 LYS L  109    ARG L  110          0         6.23                     
CISPEP   3 PHE H  256    PRO H  257          0         3.06                     
CISPEP   4 GLU T   26    PRO T   27          0        -3.28                     
SITE     1 AC1  3 GLN L  49  SER L  52  TYR L  68                               
SITE     1 AC2 17 HIS H  57  GLY H  97  THR H  98  ASP H 189                    
SITE     2 AC2 17 SER H 190  CYS H 191  GLY H 193  SER H 195                    
SITE     3 AC2 17 SER H 214  TRP H 215  GLY H 216  GLN H 217                    
SITE     4 AC2 17 GLY H 218  GLY H 226  HOH H 630  HOH H 644                    
SITE     5 AC2 17 HOH H 681                                                     
SITE     1 AC3  6 GLU H  70  ASP H  72  GLU H  75  GLU H  80                    
SITE     2 AC3  6 HOH H 606  HOH H 687                                          
SITE     1 AC4  4 LYS T 166  ASP T 178  ASP T 180  TYR T 185                    
SITE     1 AC5  5 GLY L  58  SER L  60  PHE L  71  HOH L 319                    
SITE     2 AC5  5 ARG T 131                                                     
CRYST1   67.030   81.700  124.560  90.00  90.00  90.00 P 21 21 21    4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.014919  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.012240  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008028        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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