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Database: PDB
Entry: 4V06
LinkDB: 4V06
Original site: 4V06 
HEADER    OXIDOREDUCTASE                          11-SEP-14   4V06              
TITLE     CRYSTAL STRUCTURE OF HUMAN TRYPTOPHAN HYDROXYLASE 2 (TPH2), CATALYTIC 
TITLE    2 DOMAIN                                                               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TRYPTOPHAN 5-HYDROXYLASE 2;                                
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: CATALYTIC DOMAIN, RESIDUES 148-490;                        
COMPND   5 SYNONYM: NEURONAL TRYPTOPHAN HYDROXYLASE, TRYPTOPHAN 5-MONOOXYGENASE 
COMPND   6 2;                                                                   
COMPND   7 EC: 1.14.16.4;                                                       
COMPND   8 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_VARIANT: ROSETTA;                                  
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PNIC28-BSA                                
KEYWDS    OXIDOREDUCTASE                                                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.KOPEC,A.OBERHOLZER,F.FITZPATRICK,J.NEWMAN,C.TALLANT,W.KIYANI,       
AUTHOR   2 L.SHRESTHA,N.BURGESS-BROWN,F.VON DELFT,C.ARROWSMITH,A.EDWARDS,       
AUTHOR   3 C.BOUNTRA,W.W.YUE                                                    
REVDAT   3   24-JAN-18 4V06    1       JRNL                                     
REVDAT   2   13-SEP-17 4V06    1       REMARK                                   
REVDAT   1   15-OCT-14 4V06    0                                                
JRNL        AUTH   J.KOPEC,A.OBERHOLZER,F.FITZPATRICK,J.NEWMAN,C.TALLANT,       
JRNL        AUTH 2 L.SHRESTHA,N.BURGESS-BROWN,F.VON DELFT,C.ARROWSMITH,         
JRNL        AUTH 3 A.EDWARDS,C.BOUNTRA,W.W.YUE                                  
JRNL        TITL   CRYSTAL STRUCTURE OF HUMAN TRYPTOPHANE HYDROXYLASE 2 (TPH2), 
JRNL        TITL 2 CATALYTIC DOMAIN                                             
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.63 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE)                               
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) : 2.63                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 44.50                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 26100                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.200                           
REMARK   3   R VALUE            (WORKING SET) : 0.198                           
REMARK   3   FREE R VALUE                     : 0.242                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1301                            
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 44.5107 -  5.4677    0.99     2853   219  0.1865 0.2188        
REMARK   3     2  5.4677 -  4.3411    1.00     2783   142  0.1722 0.2092        
REMARK   3     3  4.3411 -  3.7927    1.00     2819   116  0.1648 0.2152        
REMARK   3     4  3.7927 -  3.4461    1.00     2723   142  0.1956 0.2283        
REMARK   3     5  3.4461 -  3.1991    1.00     2752   117  0.2263 0.3098        
REMARK   3     6  3.1991 -  3.0106    1.00     2762   113  0.2307 0.2980        
REMARK   3     7  3.0106 -  2.8598    1.00     2712   156  0.2395 0.3002        
REMARK   3     8  2.8598 -  2.7353    1.00     2692   155  0.2649 0.3432        
REMARK   3     9  2.7353 -  2.6301    1.00     2703   141  0.2914 0.3356        
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)     : 0.380            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.340           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 58.83                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
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      :  0.002           5354                                  
REMARK   3   ANGLE     :  0.531           7292                                  
REMARK   3   CHIRALITY :  0.020            810                                  
REMARK   3   PLANARITY :  0.002            953                                  
REMARK   3   DIHEDRAL  : 10.821           1849                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 14                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 142 THROUGH 213 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -19.7290  29.7997 -43.1616              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4104 T22:   0.3080                                     
REMARK   3      T33:   0.4217 T12:   0.0482                                     
REMARK   3      T13:   0.0322 T23:   0.0346                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5038 L22:   0.2580                                     
REMARK   3      L33:   0.2919 L12:  -0.5356                                     
REMARK   3      L13:  -0.1234 L23:   0.4826                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0519 S12:  -0.1100 S13:   0.0549                       
REMARK   3      S21:  -0.0015 S22:  -0.0218 S23:  -0.0842                       
REMARK   3      S31:  -0.0492 S32:  -0.1761 S33:  -0.0001                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 214 THROUGH 270 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   3.0041  33.0733 -40.3152              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3964 T22:   0.7113                                     
REMARK   3      T33:   0.8205 T12:  -0.0328                                     
REMARK   3      T13:  -0.0052 T23:  -0.2552                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2434 L22:   0.1610                                     
REMARK   3      L33:   0.4366 L12:  -0.1240                                     
REMARK   3      L13:  -0.0580 L23:   0.0914                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0594 S12:   0.0598 S13:   0.6278                       
REMARK   3      S21:   0.1018 S22:   0.5547 S23:  -0.7108                       
REMARK   3      S31:  -0.3269 S32:   0.8379 S33:   0.1796                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 271 THROUGH 383 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -7.7899  21.6024 -39.1259              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4144 T22:   0.4590                                     
REMARK   3      T33:   0.3921 T12:   0.1225                                     
REMARK   3      T13:  -0.0071 T23:  -0.0952                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4905 L22:   0.5896                                     
REMARK   3      L33:   0.8254 L12:  -0.0133                                     
REMARK   3      L13:  -0.2096 L23:   0.1689                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0792 S12:  -0.1940 S13:   0.1259                       
REMARK   3      S21:   0.4505 S22:   0.2063 S23:  -0.1019                       
REMARK   3      S31:   0.3867 S32:   0.1683 S33:   0.3242                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 384 THROUGH 437 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -3.1398  11.3503 -32.2382              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7544 T22:   0.6835                                     
REMARK   3      T33:   0.6391 T12:   0.2735                                     
REMARK   3      T13:  -0.3002 T23:  -0.1950                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3032 L22:   0.0685                                     
REMARK   3      L33:   0.0073 L12:   0.1233                                     
REMARK   3      L13:   0.0433 L23:   0.0013                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2915 S12:  -0.3758 S13:  -0.8613                       
REMARK   3      S21:   0.4273 S22:   0.1923 S23:  -0.3242                       
REMARK   3      S31:   0.4784 S32:   0.3688 S33:   0.0282                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 438 THROUGH 490 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -4.2391   6.8907 -62.6839              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2758 T22:   0.2283                                     
REMARK   3      T33:   0.1998 T12:  -0.0361                                     
REMARK   3      T13:   0.0001 T23:   0.0131                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3186 L22:   0.5151                                     
REMARK   3      L33:   0.1593 L12:  -0.0349                                     
REMARK   3      L13:   0.1888 L23:  -0.0854                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1970 S12:   0.3634 S13:   0.0898                       
REMARK   3      S21:  -0.1412 S22:  -0.0198 S23:   0.1596                       
REMARK   3      S31:  -0.0832 S32:  -0.0153 S33:   0.1189                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 150 THROUGH 171 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   5.8547  31.4680 -71.8408              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5450 T22:   0.4955                                     
REMARK   3      T33:   0.8510 T12:  -0.0215                                     
REMARK   3      T13:   0.0467 T23:   0.2546                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0412 L22:   0.0097                                     
REMARK   3      L33:  -0.0070 L12:  -0.0324                                     
REMARK   3      L13:  -0.0208 L23:   0.0057                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2365 S12:   0.3138 S13:   0.5338                       
REMARK   3      S21:   0.4771 S22:  -0.0779 S23:   0.5390                       
REMARK   3      S31:  -0.0043 S32:   0.2194 S33:  -0.0016                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 172 THROUGH 234 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -14.5633  37.5279 -83.6474              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.3455 T22:   0.7978                                     
REMARK   3      T33:   1.0115 T12:   0.0911                                     
REMARK   3      T13:  -0.4142 T23:   0.4475                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2232 L22:   0.0446                                     
REMARK   3      L33:   0.3223 L12:  -0.0386                                     
REMARK   3      L13:  -0.2698 L23:  -0.0337                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2509 S12:   0.6382 S13:   0.8235                       
REMARK   3      S21:  -0.1245 S22:  -0.1517 S23:   0.7473                       
REMARK   3      S31:  -0.8890 S32:  -1.0133 S33:  -0.3324                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 235 THROUGH 329 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -13.1371  27.6625 -78.1602              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5285 T22:   0.7267                                     
REMARK   3      T33:   0.5637 T12:  -0.0292                                     
REMARK   3      T13:  -0.1752 T23:   0.4173                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5543 L22:   0.3960                                     
REMARK   3      L33:   0.2850 L12:  -0.3233                                     
REMARK   3      L13:   0.1642 L23:  -0.2062                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3185 S12:   0.3203 S13:   0.9301                       
REMARK   3      S21:  -0.4709 S22:   0.0922 S23:   0.0538                       
REMARK   3      S31:  -0.2222 S32:  -0.3472 S33:  -0.1813                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 330 THROUGH 359 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   1.5825  18.0367 -79.1124              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6194 T22:   0.8273                                     
REMARK   3      T33:   0.3379 T12:  -0.1005                                     
REMARK   3      T13:   0.0282 T23:   0.1624                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0130 L22:   0.2535                                     
REMARK   3      L33:   0.0447 L12:   0.0997                                     
REMARK   3      L13:   0.0402 L23:  -0.0174                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1862 S12:   0.6634 S13:   0.0858                       
REMARK   3      S21:  -0.4765 S22:  -0.0087 S23:  -0.1194                       
REMARK   3      S31:  -0.1797 S32:   0.0390 S33:  -0.0786                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 360 THROUGH 375 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -11.2801  12.7747 -88.0650              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9941 T22:   1.3205                                     
REMARK   3      T33:   0.6492 T12:  -0.1963                                     
REMARK   3      T13:  -0.1837 T23:   0.0435                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0237 L22:   0.0004                                     
REMARK   3      L33:   0.0024 L12:   0.0023                                     
REMARK   3      L13:  -0.0122 L23:  -0.0121                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3767 S12:   0.2929 S13:  -0.4012                       
REMARK   3      S21:  -0.0922 S22:  -0.3204 S23:   0.2829                       
REMARK   3      S31:  -0.2485 S32:   0.3353 S33:  -0.0001                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 376 THROUGH 396 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -14.0560  18.3000 -94.0834              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8413 T22:   1.4675                                     
REMARK   3      T33:  -0.0627 T12:   0.0017                                     
REMARK   3      T13:  -0.4518 T23:   0.5133                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0095 L22:  -0.0050                                     
REMARK   3      L33:   0.0628 L12:   0.0047                                     
REMARK   3      L13:   0.0447 L23:   0.0044                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0837 S12:   0.1644 S13:  -0.0101                       
REMARK   3      S21:  -0.2679 S22:  -0.1421 S23:   0.0609                       
REMARK   3      S31:   0.0183 S32:  -0.0968 S33:  -0.1793                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 397 THROUGH 436 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -1.7981  11.8097 -87.1788              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8153 T22:   0.9983                                     
REMARK   3      T33:   0.8911 T12:   0.0356                                     
REMARK   3      T13:  -0.0311 T23:   0.0834                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0082 L22:   0.1012                                     
REMARK   3      L33:   0.0197 L12:   0.0091                                     
REMARK   3      L13:  -0.0028 L23:   0.0542                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0322 S12:   0.8004 S13:  -0.5461                       
REMARK   3      S21:  -0.5074 S22:   0.3363 S23:  -0.3371                       
REMARK   3      S31:   0.3268 S32:   0.1749 S33:   0.0000                       
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 437 THROUGH 459 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   6.9460  16.4262 -66.0285              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3804 T22:   0.3970                                     
REMARK   3      T33:   0.5066 T12:  -0.0186                                     
REMARK   3      T13:  -0.0124 T23:   0.0597                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1278 L22:   0.0952                                     
REMARK   3      L33:   0.0580 L12:   0.0437                                     
REMARK   3      L13:   0.1289 L23:   0.0718                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2297 S12:   0.1894 S13:  -0.1251                       
REMARK   3      S21:   0.0772 S22:  -0.0932 S23:  -0.2119                       
REMARK   3      S31:  -0.1864 S32:  -0.1414 S33:   0.0000                       
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 460 THROUGH 490 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -6.0483   1.8534 -55.4260              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3905 T22:   0.2430                                     
REMARK   3      T33:   0.3952 T12:  -0.0143                                     
REMARK   3      T13:   0.0211 T23:   0.0127                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0015 L22:   0.0283                                     
REMARK   3      L33:  -0.0031 L12:   0.0385                                     
REMARK   3      L13:  -0.0272 L23:   0.0914                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3096 S12:  -0.4266 S13:   0.3278                       
REMARK   3      S21:   0.1650 S22:  -0.1559 S23:   0.1033                       
REMARK   3      S31:  -0.0369 S32:   0.0188 S33:   0.0357                       
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 4V06 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 11-SEP-14.                  
REMARK 100 THE DEPOSITION ID IS D_1290061742.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 12-JUL-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I02                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9795                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 26141                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.630                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 44.500                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 5.600                              
REMARK 200  R MERGE                    (I) : 0.12000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.63                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.75                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 1.32000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.500                              
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 2PAH                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 54.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.70                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.20M SODIUM ACETATE; 0.1M BIS-TRIS-     
REMARK 280  PROPANE PH 6.5; 20.0% PEG 3350; 10.0% ETHYLENE GLYCOL               
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X+1/2,Y+1/2,-Z                                         
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        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       47.98000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       50.09950            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       47.98000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       50.09950            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: 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 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     LEU B   142                                                      
REMARK 465     TYR B   143                                                      
REMARK 465     PHE B   144                                                      
REMARK 465     GLN B   145                                                      
REMARK 465     SER B   146                                                      
REMARK 465     MET B   147                                                      
REMARK 465     LEU B   148                                                      
REMARK 465     GLU B   149                                                      
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     GLN A 145    CG   CD   OE1  NE2                                  
REMARK 470     GLU A 149    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 202    CG   CD   CE   NZ                                   
REMARK 470     GLN A 205    CG   CD   OE1  NE2                                  
REMARK 470     GLU A 214    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 218    CG   CD   CE   NZ                                   
REMARK 470     ARG A 237    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 241    CG   CD   CE   NZ                                   
REMARK 470     LYS A 331    CG   CD   CE   NZ                                   
REMARK 470     LYS A 368    CG   CD   CE   NZ                                   
REMARK 470     GLN A 372    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 388    CG   CD   CE   NZ                                   
REMARK 470     LYS A 394    CG   CD   CE   NZ                                   
REMARK 470     CYS A 396    SG                                                  
REMARK 470     LYS A 398    CG   CD   CE   NZ                                   
REMARK 470     LYS A 403    CG   CD   CE   NZ                                   
REMARK 470     LEU A 407    CG   CD1  CD2                                       
REMARK 470     GLU A 409    CG   CD   OE1  OE2                                  
REMARK 470     THR A 413    OG1  CG2                                            
REMARK 470     THR A 414    OG1  CG2                                            
REMARK 470     GLU A 417    CG   CD   OE1  OE2                                  
REMARK 470     SER A 422    OG                                                  
REMARK 470     GLU A 426    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 431    CG   CD   CE   NZ                                   
REMARK 470     ARG B 156    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU B 169    CG   CD1  CD2                                       
REMARK 470     MET B 170    CG   SD   CE                                        
REMARK 470     SER B 173    OG                                                  
REMARK 470     GLU B 174    CG   CD   OE1  OE2                                  
REMARK 470     LEU B 175    CG   CD1  CD2                                       
REMARK 470     ASP B 176    CG   OD1  OD2                                       
REMARK 470     ASP B 178    CG   OD1  OD2                                       
REMARK 470     HIS B 179    CG   ND1  CD2  CE1  NE2                             
REMARK 470     PRO B 180    CG   CD                                             
REMARK 470     PHE B 182    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LYS B 183    CG   CD   CE   NZ                                   
REMARK 470     ASP B 184    CG   OD1  OD2                                       
REMARK 470     ASN B 185    CG   OD1  ND2                                       
REMARK 470     VAL B 186    CG1  CG2                                            
REMARK 470     TYR B 187    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ARG B 188    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN B 189    CG   CD   OE1  NE2                                  
REMARK 470     ARG B 190    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 192    CG   CD   CE   NZ                                   
REMARK 470     ASP B 196    CG   OD1  OD2                                       
REMARK 470     VAL B 197    CG1  CG2                                            
REMARK 470     LYS B 202    CG   CD   CE   NZ                                   
REMARK 470     GLN B 205    CG   CD   OE1  NE2                                  
REMARK 470     ARG B 209    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B 211    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 214    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 215    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 218    CG   CD   CE   NZ                                   
REMARK 470     ARG B 225    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU B 227    CG   CD1  CD2                                       
REMARK 470     LYS B 229    CG   CD   CE   NZ                                   
REMARK 470     ARG B 237    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 241    CG   CD   CE   NZ                                   
REMARK 470     LYS B 248    CG   CD   CE   NZ                                   
REMARK 470     ARG B 253    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B 254    CG   CD   OE1  OE2                                  
REMARK 470     ASP B 255    CG   OD1  OD2                                       
REMARK 470     ASN B 256    CG   OD1  ND2                                       
REMARK 470     GLN B 259    CG   CD   OE1  NE2                                  
REMARK 470     TYR B 281    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     HIS B 304    CG   ND1  CD2  CE1  NE2                             
REMARK 470     ASP B 307    CG   OD1  OD2                                       
REMARK 470     PRO B 308    CG   CD                                             
REMARK 470     LEU B 309    CG   CD1  CD2                                       
REMARK 470     TYR B 310    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     THR B 311    OG1  CG2                                            
REMARK 470     GLN B 352    CG   CD   OE1  NE2                                  
REMARK 470     GLN B 369    CG   CD   OE1  NE2                                  
REMARK 470     GLU B 370    CG   CD   OE1  OE2                                  
REMARK 470     GLN B 372    CG   CD   OE1  NE2                                  
REMARK 470     ARG B 374    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 388    CG   CD   CE   NZ                                   
REMARK 470     LEU B 391    CG   CD1  CD2                                       
REMARK 470     SER B 392    OG                                                  
REMARK 470     ASP B 393    CG   OD1  OD2                                       
REMARK 470     LYS B 394    CG   CD   CE   NZ                                   
REMARK 470     CYS B 396    SG                                                  
REMARK 470     VAL B 397    CG1  CG2                                            
REMARK 470     LYS B 398    CG   CD   CE   NZ                                   
REMARK 470     LEU B 407    CG   CD1  CD2                                       
REMARK 470     GLN B 408    CG   CD   OE1  NE2                                  
REMARK 470     GLU B 409    CG   CD   OE1  OE2                                  
REMARK 470     CYS B 410    SG                                                  
REMARK 470     ILE B 412    CG1  CG2  CD1                                       
REMARK 470     THR B 413    OG1  CG2                                            
REMARK 470     THR B 414    OG1  CG2                                            
REMARK 470     PHE B 415    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     GLU B 417    CG   CD   OE1  OE2                                  
REMARK 470     TYR B 419    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     GLU B 426    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 427    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 430    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 431    CG   CD   CE   NZ                                   
REMARK 470     ASP B 434    CG   OD1  OD2                                       
REMARK 470     LYS B 437    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   O    GLU B   215     OG1  THR B   219              2.19            
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    THR A 361      -75.67   -131.31                                   
REMARK 500    THR A 414      151.81    -43.51                                   
REMARK 500    TYR B 212     -166.07   -119.77                                   
REMARK 500    PRO B 314       87.52    -64.15                                   
REMARK 500    THR B 361      -75.85   -135.38                                   
REMARK 500    LEU B 391       59.59    -92.14                                   
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 A2027        DISTANCE =  5.92 ANGSTROMS                       
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                              FE A1491  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 IMD A 600   N1                                                     
REMARK 620 2 GLU A 363   OE1 106.5                                              
REMARK 620 3 HIS A 323   NE2 113.4  94.8                                        
REMARK 620 4 HIS A 318   NE2 110.6 131.9  97.5                                  
REMARK 620 5 GLU A 363   OE2 123.4  55.6 120.8  78.4                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              FE B1491  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 IMD B 600   N1                                                     
REMARK 620 2 HIS B 323   NE2 107.0                                              
REMARK 620 3 GLU B 363   OE1 115.2 114.3                                        
REMARK 620 4 GLU B 363   OE2 111.0 141.0  55.3                                  
REMARK 620 5 HIS B 318   NE2  96.4  86.6 132.3  81.0                            
REMARK 620 N                    1     2     3     4                             
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IMD A 600                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IMD B 600                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE A 1491                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE B 1491                 
DBREF  4V06 A  148   490  UNP    Q8IWU9   TPH2_HUMAN     148    490             
DBREF  4V06 B  148   490  UNP    Q8IWU9   TPH2_HUMAN     148    490             
SEQADV 4V06 LEU A  142  UNP  Q8IWU9              EXPRESSION TAG                 
SEQADV 4V06 TYR A  143  UNP  Q8IWU9              EXPRESSION TAG                 
SEQADV 4V06 PHE A  144  UNP  Q8IWU9              EXPRESSION TAG                 
SEQADV 4V06 GLN A  145  UNP  Q8IWU9              EXPRESSION TAG                 
SEQADV 4V06 SER A  146  UNP  Q8IWU9              EXPRESSION TAG                 
SEQADV 4V06 MET A  147  UNP  Q8IWU9              EXPRESSION TAG                 
SEQADV 4V06 LEU B  142  UNP  Q8IWU9              EXPRESSION TAG                 
SEQADV 4V06 TYR B  143  UNP  Q8IWU9              EXPRESSION TAG                 
SEQADV 4V06 PHE B  144  UNP  Q8IWU9              EXPRESSION TAG                 
SEQADV 4V06 GLN B  145  UNP  Q8IWU9              EXPRESSION TAG                 
SEQADV 4V06 SER B  146  UNP  Q8IWU9              EXPRESSION TAG                 
SEQADV 4V06 MET B  147  UNP  Q8IWU9              EXPRESSION TAG                 
SEQRES   1 A  349  LEU TYR PHE GLN SER MET LEU GLU ASP VAL PRO TRP PHE          
SEQRES   2 A  349  PRO ARG LYS ILE SER GLU LEU ASP LYS CYS SER HIS ARG          
SEQRES   3 A  349  VAL LEU MET TYR GLY SER GLU LEU ASP ALA ASP HIS PRO          
SEQRES   4 A  349  GLY PHE LYS ASP ASN VAL TYR ARG GLN ARG ARG LYS TYR          
SEQRES   5 A  349  PHE VAL ASP VAL ALA MET GLY TYR LYS TYR GLY GLN PRO          
SEQRES   6 A  349  ILE PRO ARG VAL GLU TYR THR GLU GLU GLU THR LYS THR          
SEQRES   7 A  349  TRP GLY VAL VAL PHE ARG GLU LEU SER LYS LEU TYR PRO          
SEQRES   8 A  349  THR HIS ALA CYS ARG GLU TYR LEU LYS ASN PHE PRO LEU          
SEQRES   9 A  349  LEU THR LYS TYR CYS GLY TYR ARG GLU ASP ASN VAL PRO          
SEQRES  10 A  349  GLN LEU GLU ASP VAL SER MET PHE LEU LYS GLU ARG SER          
SEQRES  11 A  349  GLY PHE THR VAL ARG PRO VAL ALA GLY TYR LEU SER PRO          
SEQRES  12 A  349  ARG ASP PHE LEU ALA GLY LEU ALA TYR ARG VAL PHE HIS          
SEQRES  13 A  349  CYS THR GLN TYR ILE ARG HIS GLY SER ASP PRO LEU TYR          
SEQRES  14 A  349  THR PRO GLU PRO ASP THR CYS HIS GLU LEU LEU GLY HIS          
SEQRES  15 A  349  VAL PRO LEU LEU ALA ASP PRO LYS PHE ALA GLN PHE SER          
SEQRES  16 A  349  GLN GLU ILE GLY LEU ALA SER LEU GLY ALA SER ASP GLU          
SEQRES  17 A  349  ASP VAL GLN LYS LEU ALA THR CYS TYR PHE PHE THR ILE          
SEQRES  18 A  349  GLU PHE GLY LEU CYS LYS GLN GLU GLY GLN LEU ARG ALA          
SEQRES  19 A  349  TYR GLY ALA GLY LEU LEU SER SER ILE GLY GLU LEU LYS          
SEQRES  20 A  349  HIS ALA LEU SER ASP LYS ALA CYS VAL LYS ALA PHE ASP          
SEQRES  21 A  349  PRO LYS THR THR CYS LEU GLN GLU CYS LEU ILE THR THR          
SEQRES  22 A  349  PHE GLN GLU ALA TYR PHE VAL SER GLU SER PHE GLU GLU          
SEQRES  23 A  349  ALA LYS GLU LYS MET ARG ASP PHE ALA LYS SER ILE THR          
SEQRES  24 A  349  ARG PRO PHE SER VAL TYR PHE ASN PRO TYR THR GLN SER          
SEQRES  25 A  349  ILE GLU ILE LEU LYS ASP THR ARG SER ILE GLU ASN VAL          
SEQRES  26 A  349  VAL GLN ASP LEU ARG SER ASP LEU ASN THR VAL CYS ASP          
SEQRES  27 A  349  ALA LEU ASN LYS MET ASN GLN TYR LEU GLY ILE                  
SEQRES   1 B  349  LEU TYR PHE GLN SER MET LEU GLU ASP VAL PRO TRP PHE          
SEQRES   2 B  349  PRO ARG LYS ILE SER GLU LEU ASP LYS CYS SER HIS ARG          
SEQRES   3 B  349  VAL LEU MET TYR GLY SER GLU LEU ASP ALA ASP HIS PRO          
SEQRES   4 B  349  GLY PHE LYS ASP ASN VAL TYR ARG GLN ARG ARG LYS TYR          
SEQRES   5 B  349  PHE VAL ASP VAL ALA MET GLY TYR LYS TYR GLY GLN PRO          
SEQRES   6 B  349  ILE PRO ARG VAL GLU TYR THR GLU GLU GLU THR LYS THR          
SEQRES   7 B  349  TRP GLY VAL VAL PHE ARG GLU LEU SER LYS LEU TYR PRO          
SEQRES   8 B  349  THR HIS ALA CYS ARG GLU TYR LEU LYS ASN PHE PRO LEU          
SEQRES   9 B  349  LEU THR LYS TYR CYS GLY TYR ARG GLU ASP ASN VAL PRO          
SEQRES  10 B  349  GLN LEU GLU ASP VAL SER MET PHE LEU LYS GLU ARG SER          
SEQRES  11 B  349  GLY PHE THR VAL ARG PRO VAL ALA GLY TYR LEU SER PRO          
SEQRES  12 B  349  ARG ASP PHE LEU ALA GLY LEU ALA TYR ARG VAL PHE HIS          
SEQRES  13 B  349  CYS THR GLN TYR ILE ARG HIS GLY SER ASP PRO LEU TYR          
SEQRES  14 B  349  THR PRO GLU PRO ASP THR CYS HIS GLU LEU LEU GLY HIS          
SEQRES  15 B  349  VAL PRO LEU LEU ALA ASP PRO LYS PHE ALA GLN PHE SER          
SEQRES  16 B  349  GLN GLU ILE GLY LEU ALA SER LEU GLY ALA SER ASP GLU          
SEQRES  17 B  349  ASP VAL GLN LYS LEU ALA THR CYS TYR PHE PHE THR ILE          
SEQRES  18 B  349  GLU PHE GLY LEU CYS LYS GLN GLU GLY GLN LEU ARG ALA          
SEQRES  19 B  349  TYR GLY ALA GLY LEU LEU SER SER ILE GLY GLU LEU LYS          
SEQRES  20 B  349  HIS ALA LEU SER ASP LYS ALA CYS VAL LYS ALA PHE ASP          
SEQRES  21 B  349  PRO LYS THR THR CYS LEU GLN GLU CYS LEU ILE THR THR          
SEQRES  22 B  349  PHE GLN GLU ALA TYR PHE VAL SER GLU SER PHE GLU GLU          
SEQRES  23 B  349  ALA LYS GLU LYS MET ARG ASP PHE ALA LYS SER ILE THR          
SEQRES  24 B  349  ARG PRO PHE SER VAL TYR PHE ASN PRO TYR THR GLN SER          
SEQRES  25 B  349  ILE GLU ILE LEU LYS ASP THR ARG SER ILE GLU ASN VAL          
SEQRES  26 B  349  VAL GLN ASP LEU ARG SER ASP LEU ASN THR VAL CYS ASP          
SEQRES  27 B  349  ALA LEU ASN LYS MET ASN GLN TYR LEU GLY ILE                  
HET    IMD  A 600       5                                                       
HET     FE  A1491       1                                                       
HET    IMD  B 600       5                                                       
HET     FE  B1491       1                                                       
HETNAM     IMD IMIDAZOLE                                                        
HETNAM      FE FE (III) ION                                                     
FORMUL   3  IMD    2(C3 H5 N2 1+)                                               
FORMUL   4   FE    2(FE 3+)                                                     
FORMUL   7  HOH   *111(H2 O)                                                    
HELIX    1   1 LEU A  142  ASP A  150  1                                   9    
HELIX    2   2 ILE A  158  GLU A  160  5                                   3    
HELIX    3   3 LEU A  161  HIS A  166  1                                   6    
HELIX    4   4 ASP A  184  GLY A  200  1                                  17    
HELIX    5   5 THR A  213  LYS A  229  1                                  17    
HELIX    6   6 LEU A  230  ALA A  235  1                                   6    
HELIX    7   7 CYS A  236  CYS A  250  1                                  15    
HELIX    8   8 GLN A  259  SER A  271  1                                  13    
HELIX    9   9 SER A  283  ALA A  292  1                                  10    
HELIX   10  10 ASP A  315  HIS A  323  1                                   9    
HELIX   11  11 HIS A  323  ALA A  328  1                                   6    
HELIX   12  12 ASP A  329  LEU A  344  1                                  16    
HELIX   13  13 SER A  347  PHE A  360  1                                  14    
HELIX   14  14 GLY A  377  SER A  383  1                                   7    
HELIX   15  15 SER A  383  LEU A  391  1                                   9    
HELIX   16  16 ASP A  401  CYS A  406  1                                   6    
HELIX   17  17 SER A  424  ALA A  436  1                                  13    
HELIX   18  18 ASP A  459  GLY A  489  1                                  31    
HELIX   19  19 ILE B  158  GLU B  160  5                                   3    
HELIX   20  20 LEU B  161  HIS B  166  1                                   6    
HELIX   21  21 ASP B  184  TYR B  201  1                                  18    
HELIX   22  22 THR B  213  SER B  228  1                                  16    
HELIX   23  23 LEU B  230  ALA B  235  1                                   6    
HELIX   24  24 CYS B  236  TYR B  249  1                                  14    
HELIX   25  25 GLN B  259  GLU B  269  1                                  11    
HELIX   26  26 SER B  283  ALA B  292  1                                  10    
HELIX   27  27 ASP B  315  HIS B  323  1                                   9    
HELIX   28  28 HIS B  323  ALA B  328  1                                   6    
HELIX   29  29 ASP B  329  LEU B  344  1                                  16    
HELIX   30  30 SER B  347  PHE B  360  1                                  14    
HELIX   31  31 SER B  383  LEU B  391  1                                   9    
HELIX   32  32 ASP B  401  CYS B  406  1                                   6    
HELIX   33  33 SER B  424  LYS B  437  1                                  14    
HELIX   34  34 ASP B  459  GLY B  489  1                                  31    
SHEET    1  AA 2 VAL A 168  TYR A 171  0                                        
SHEET    2  AA 2 GLY A 280  LEU A 282 -1  O  TYR A 281   N  LEU A 169           
SHEET    1  AB 2 THR A 274  PRO A 277  0                                        
SHEET    2  AB 2 VAL A 295  CYS A 298  1  O  PHE A 296   N  ARG A 276           
SHEET    1  AC 4 GLN A 372  ALA A 375  0                                        
SHEET    2  AC 4 GLY A 365  GLN A 369 -1  O  CYS A 367   N  ARG A 374           
SHEET    3  AC 4 TYR A 419  SER A 422  1  O  PHE A 420   N  LEU A 366           
SHEET    4  AC 4 VAL A 397  ALA A 399  1  O  LYS A 398   N  VAL A 421           
SHEET    1  AD 2 SER A 444  ASN A 448  0                                        
SHEET    2  AD 2 SER A 453  LEU A 457 -1  O  SER A 453   N  ASN A 448           
SHEET    1  BA 2 VAL B 168  TYR B 171  0                                        
SHEET    2  BA 2 GLY B 280  LEU B 282 -1  O  TYR B 281   N  LEU B 169           
SHEET    1  BB 2 THR B 274  PRO B 277  0                                        
SHEET    2  BB 2 VAL B 295  CYS B 298  1  O  PHE B 296   N  ARG B 276           
SHEET    1  BC 4 LEU B 373  ALA B 375  0                                        
SHEET    2  BC 4 LEU B 366  LYS B 368 -1  O  CYS B 367   N  ARG B 374           
SHEET    3  BC 4 TYR B 419  SER B 422  1  O  PHE B 420   N  LEU B 366           
SHEET    4  BC 4 VAL B 397  ALA B 399  1  O  LYS B 398   N  VAL B 421           
SHEET    1  BD 2 SER B 444  ASN B 448  0                                        
SHEET    2  BD 2 SER B 453  LEU B 457 -1  O  SER B 453   N  ASN B 448           
LINK         N1  IMD A 600                FE    FE A1491     1555   1555  1.90  
LINK        FE    FE A1491                 OE1 GLU A 363     1555   1555  2.57  
LINK        FE    FE A1491                 NE2 HIS A 323     1555   1555  2.07  
LINK        FE    FE A1491                 NE2 HIS A 318     1555   1555  2.28  
LINK        FE    FE A1491                 OE2 GLU A 363     1555   1555  2.01  
LINK         N1  IMD B 600                FE    FE B1491     1555   1555  1.88  
LINK        FE    FE B1491                 NE2 HIS B 323     1555   1555  2.20  
LINK        FE    FE B1491                 OE1 GLU B 363     1555   1555  2.37  
LINK        FE    FE B1491                 OE2 GLU B 363     1555   1555  2.36  
LINK        FE    FE B1491                 NE2 HIS B 318     1555   1555  2.28  
CISPEP   1 THR A  414    PHE A  415          0         3.92                     
CISPEP   2 GLN B  369    GLU B  370          0         1.89                     
CISPEP   3 GLU B  370    GLY B  371          0         1.89                     
SITE     1 AC1  7 PHE A 296  HIS A 318  GLU A 319  HIS A 323                    
SITE     2 AC1  7 GLU A 363   FE A1491  HOH A2054                               
SITE     1 AC2  7 PRO B 314  HIS B 318  GLU B 319  HIS B 323                    
SITE     2 AC2  7 GLU B 363   FE B1491  HOH B2013                               
SITE     1 AC3  4 HIS A 318  HIS A 323  GLU A 363  IMD A 600                    
SITE     1 AC4  4 HIS B 318  HIS B 323  GLU B 363  IMD B 600                    
CRYST1   95.960  100.199   89.009  90.00  90.00  90.00 P 21 21 2     8          
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      0.010421  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009980  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011235        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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