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Database: PDB
Entry: 5H7V
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HEADER    HYDROLASE INHIBITOR                     21-NOV-16   5H7V              
TITLE     STRUCTURE OF FULL-LENGTH EXTRACELLULAR DOMAIN OF HAI-1 AT PH 4.6      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: KUNITZ-TYPE PROTEASE INHIBITOR 1;                          
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: LIGAND BINDING REGION, UNP RESIDUES 36-441;                
COMPND   5 SYNONYM: HEPATOCYTE GROWTH FACTOR ACTIVATOR INHIBITOR TYPE 1,HAI-1;  
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: SPINT1, HAI1, UNQ223/PRO256;                                   
SOURCE   6 EXPRESSION_SYSTEM: DROSOPHILA MELANOGASTER;                          
SOURCE   7 EXPRESSION_SYSTEM_COMMON: FRUIT FLY;                                 
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7227;                                       
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: S2 CELLS;                                  
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: PMT/BIP                                   
KEYWDS    HAI-1, HYDROLASE INHIBITOR                                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.LIU,M.HUANG                                                         
REVDAT   3   31-MAY-17 5H7V    1       JRNL                                     
REVDAT   2   19-APR-17 5H7V    1       JRNL                                     
REVDAT   1   29-MAR-17 5H7V    0                                                
JRNL        AUTH   M.LIU,C.YUAN,J.K.JENSEN,B.ZHAO,Y.JIANG,L.JIANG,M.HUANG       
JRNL        TITL   THE CRYSTAL STRUCTURE OF A MULTIDOMAIN PROTEASE INHIBITOR    
JRNL        TITL 2 (HAI-1) REVEALS THE MECHANISM OF ITS AUTO-INHIBITION         
JRNL        REF    J. BIOL. CHEM.                V. 292  8412 2017              
JRNL        REFN                   ESSN 1083-351X                               
JRNL        PMID   28348076                                                     
JRNL        DOI    10.1074/JBC.M117.779256                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.82 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (1.10.1_2155: ???)                            
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) : 3.82                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 38.09                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.400                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 5986                           
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.256                           
REMARK   3   R VALUE            (WORKING SET) : 0.253                           
REMARK   3   FREE R VALUE                     : 0.328                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.790                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 287                             
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
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)     : 0.400            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.320           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 170.9                          
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      :   NULL           NULL                                  
REMARK   3   ANGLE     :   NULL           NULL                                  
REMARK   3   CHIRALITY :   NULL           NULL                                  
REMARK   3   PLANARITY :   NULL           NULL                                  
REMARK   3   DIHEDRAL  :   NULL           NULL                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 20                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 45:53)                              
REMARK   3    ORIGIN FOR THE GROUP (A): -42.5442  27.7576 -18.8125              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5127 T22:   2.3422                                     
REMARK   3      T33:   1.5995 T12:   0.2357                                     
REMARK   3      T13:   0.8816 T23:   0.9138                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.6467 L22:   9.7358                                     
REMARK   3      L33:   5.4940 L12:   3.6498                                     
REMARK   3      L13:   6.8638 L23:   3.4664                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3151 S12:   0.3043 S13:  -1.9656                       
REMARK   3      S21:  -1.2152 S22:   1.2271 S23:  -1.9637                       
REMARK   3      S31:  -0.6798 S32:  -0.1026 S33:   0.6706                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 54:77)                              
REMARK   3    ORIGIN FOR THE GROUP (A): -23.7775  34.7322 -10.4763              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0666 T22:   1.4767                                     
REMARK   3      T33:   0.9997 T12:   0.0213                                     
REMARK   3      T13:   0.0914 T23:  -0.0097                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.9092 L22:   5.6038                                     
REMARK   3      L33:   1.0118 L12:   3.5390                                     
REMARK   3      L13:  -1.9951 L23:  -0.4431                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   1.1799 S12:  -1.8146 S13:   0.1521                       
REMARK   3      S21:  -1.0431 S22:  -1.5212 S23:   0.2750                       
REMARK   3      S31:  -0.1835 S32:   0.1047 S33:   0.1258                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 78:104)                             
REMARK   3    ORIGIN FOR THE GROUP (A): -33.0695  35.5720 -18.6638              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.2449 T22:   1.6382                                     
REMARK   3      T33:   1.7290 T12:   0.3344                                     
REMARK   3      T13:   0.1950 T23:   0.5702                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.7998 L22:   4.7873                                     
REMARK   3      L33:   6.6024 L12:  -0.7716                                     
REMARK   3      L13:   5.1280 L23:  -3.2280                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   1.9526 S12:   2.0433 S13:   0.6655                       
REMARK   3      S21:   0.1763 S22:  -0.2626 S23:   1.7462                       
REMARK   3      S31:  -0.3154 S32:  -0.7049 S33:  -1.4795                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 105:110)                            
REMARK   3    ORIGIN FOR THE GROUP (A): -38.5124  49.1447  -9.5170              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   3.9001 T22:   1.1086                                     
REMARK   3      T33:   2.8347 T12:   0.7142                                     
REMARK   3      T13:   1.5180 T23:  -0.5206                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.8096 L22:   4.0636                                     
REMARK   3      L33:   0.1094 L12:   1.4862                                     
REMARK   3      L13:  -0.4721 L23:  -0.6166                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0812 S12:  -0.6472 S13:   1.7168                       
REMARK   3      S21:   0.8239 S22:   0.6401 S23:  -0.4553                       
REMARK   3      S31:  -0.6206 S32:   0.4539 S33:  -0.1413                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 111:132)                            
REMARK   3    ORIGIN FOR THE GROUP (A): -24.2647  31.9554 -12.2854              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6606 T22:   1.0949                                     
REMARK   3      T33:   0.8544 T12:   0.0443                                     
REMARK   3      T13:   0.0605 T23:  -0.0386                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.3235 L22:   3.4734                                     
REMARK   3      L33:   7.0757 L12:   4.6984                                     
REMARK   3      L13:  -0.5474 L23:  -0.4067                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.9996 S12:  -0.1370 S13:   0.6170                       
REMARK   3      S21:  -0.3750 S22:  -0.7530 S23:  -0.8037                       
REMARK   3      S31:  -0.6241 S32:  -1.2881 S33:  -0.6512                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 133:147)                            
REMARK   3    ORIGIN FOR THE GROUP (A): -30.6110  32.2270  -7.6466              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0057 T22:   1.4741                                     
REMARK   3      T33:   0.6893 T12:   0.3885                                     
REMARK   3      T13:   0.0407 T23:   0.0194                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.4781 L22:   2.2064                                     
REMARK   3      L33:   2.8991 L12:   0.6879                                     
REMARK   3      L13:   0.9682 L23:  -2.2178                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1016 S12:  -0.4224 S13:   0.6023                       
REMARK   3      S21:   0.9788 S22:   0.5014 S23:   1.0629                       
REMARK   3      S31:  -0.1298 S32:  -1.1088 S33:  -0.4019                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 148:154)                            
REMARK   3    ORIGIN FOR THE GROUP (A): -25.7339  21.1483   0.8285              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0995 T22:   3.0052                                     
REMARK   3      T33:   1.6960 T12:   0.2783                                     
REMARK   3      T13:  -0.2427 T23:   1.2336                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7220 L22:   5.5525                                     
REMARK   3      L33:   1.9906 L12:  -1.6084                                     
REMARK   3      L13:  -2.5040 L23:   3.9075                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3116 S12:  -2.6231 S13:  -3.0321                       
REMARK   3      S21:   0.6441 S22:  -1.0430 S23:  -1.6927                       
REMARK   3      S31:   4.1024 S32:  -0.2399 S33:  -0.1602                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 166:179)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  -7.6502  12.4940 -17.0102              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.2815 T22:   1.5630                                     
REMARK   3      T33:   1.6110 T12:  -0.3173                                     
REMARK   3      T13:  -0.4335 T23:   0.4683                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9835 L22:   3.7526                                     
REMARK   3      L33:   5.1568 L12:  -4.2155                                     
REMARK   3      L13:  -6.7396 L23:   1.2661                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4135 S12:   2.7104 S13:  -1.2967                       
REMARK   3      S21:  -1.1791 S22:  -1.0765 S23:   2.3520                       
REMARK   3      S31:   0.1090 S32:  -1.5183 S33:   0.4916                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 180:191)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  -8.3102   5.8228  -6.0382              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0138 T22:   2.2628                                     
REMARK   3      T33:   1.2660 T12:  -0.8179                                     
REMARK   3      T13:   0.1619 T23:   0.4338                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.1145 L22:   3.1449                                     
REMARK   3      L33:   2.0036 L12:  -3.5276                                     
REMARK   3      L13:   6.9421 L23:   0.4629                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.9887 S12:  -0.0691 S13:  -1.4776                       
REMARK   3      S21:  -1.9246 S22:   1.7523 S23:   0.2313                       
REMARK   3      S31:   3.6051 S32:   0.2915 S33:  -0.3634                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: (CHAIN A AND RESID 192:203)                            
REMARK   3    ORIGIN FOR THE GROUP (A): -10.3402   0.2194 -16.0588              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.6714 T22:   1.4585                                     
REMARK   3      T33:   2.5087 T12:  -0.0321                                     
REMARK   3      T13:  -0.2621 T23:   0.3694                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.2164 L22:   4.5081                                     
REMARK   3      L33:   3.9457 L12:  -2.9334                                     
REMARK   3      L13:   1.1497 L23:   1.4231                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   1.0917 S12:  -1.0724 S13:   1.5220                       
REMARK   3      S21:   0.1860 S22:  -2.4623 S23:   0.3508                       
REMARK   3      S31:   2.9347 S32:  -0.9169 S33:   0.5144                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: (CHAIN A AND RESID 204:220)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  -7.0116   5.2415 -15.3677              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.8131 T22:   1.3367                                     
REMARK   3      T33:   2.0408 T12:  -0.1313                                     
REMARK   3      T13:   0.3358 T23:   0.0974                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.3391 L22:   4.6654                                     
REMARK   3      L33:   2.7282 L12:  -5.2368                                     
REMARK   3      L13:  -0.3149 L23:   0.4511                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3696 S12:  -0.3268 S13:  -1.0188                       
REMARK   3      S21:   0.6509 S22:  -0.0673 S23:   4.4614                       
REMARK   3      S31:   1.4302 S32:  -1.1827 S33:   0.0902                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: (CHAIN A AND RESID 221:233)                            
REMARK   3    ORIGIN FOR THE GROUP (A): -16.3972   5.7425  -3.3017              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   2.7701 T22:   3.6233                                     
REMARK   3      T33:   3.4238 T12:  -1.4689                                     
REMARK   3      T13:   1.2002 T23:  -2.2656                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.1925 L22:   3.5173                                     
REMARK   3      L33:   6.6217 L12:   1.6762                                     
REMARK   3      L13:  -1.1894 L23:  -4.6624                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1408 S12:  -0.6179 S13:   1.0387                       
REMARK   3      S21:  -0.1405 S22:   0.9951 S23:  -1.1835                       
REMARK   3      S31:   2.4022 S32:  -1.6270 S33:   1.3320                       
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    SELECTION: (CHAIN A AND RESID 234:244)                            
REMARK   3    ORIGIN FOR THE GROUP (A): -12.8762  13.3616 -20.6109              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.1804 T22:   2.4153                                     
REMARK   3      T33:   0.5751 T12:  -0.1475                                     
REMARK   3      T13:  -0.0390 T23:  -0.2734                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6960 L22:   7.2207                                     
REMARK   3      L33:   2.2787 L12:  -2.2327                                     
REMARK   3      L13:  -1.2580 L23:   4.0552                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   2.0669 S12:  -1.4823 S13:   1.8799                       
REMARK   3      S21:  -1.3417 S22:   1.3606 S23:  -0.3102                       
REMARK   3      S31:  -0.0299 S32:  -1.1371 S33:  -1.7137                       
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    SELECTION: (CHAIN A AND RESID 245:254)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  -7.0603  24.2458 -27.9241              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.5527 T22:   1.5050                                     
REMARK   3      T33:   1.2231 T12:  -0.5605                                     
REMARK   3      T13:  -0.2928 T23:  -0.3597                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   9.2870 L22:   3.2339                                     
REMARK   3      L33:   7.4725 L12:  -0.7770                                     
REMARK   3      L13:  -7.2848 L23:  -1.7567                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -4.1935 S12:   3.5741 S13:  -1.2982                       
REMARK   3      S21:  -1.7636 S22:   2.5198 S23:  -0.4638                       
REMARK   3      S31:  -1.7343 S32:  -0.1555 S33:   0.4060                       
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    SELECTION: (CHAIN A AND RESID 255:260)                            
REMARK   3    ORIGIN FOR THE GROUP (A): -11.6718  41.4578 -22.9676              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.2894 T22:   1.5900                                     
REMARK   3      T33:   1.9775 T12:  -0.2789                                     
REMARK   3      T13:  -0.7398 T23:   0.8586                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.6021 L22:   8.9268                                     
REMARK   3      L33:   9.0127 L12:   5.5273                                     
REMARK   3      L13:   4.6597 L23:   6.0027                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3915 S12:   1.5083 S13:  -0.4168                       
REMARK   3      S21:   0.1221 S22:   2.6134 S23:   0.8938                       
REMARK   3      S31:  -0.3623 S32:   1.2253 S33:   2.8218                       
REMARK   3   TLS GROUP : 16                                                     
REMARK   3    SELECTION: (CHAIN A AND RESID 261:303)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  -3.6378  27.9318 -19.6960              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0276 T22:   1.2151                                     
REMARK   3      T33:   1.2856 T12:  -0.1379                                     
REMARK   3      T13:  -0.2246 T23:   0.1122                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.6110 L22:   5.1467                                     
REMARK   3      L33:   9.1850 L12:   1.1546                                     
REMARK   3      L13:   3.4640 L23:   0.3213                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3434 S12:   0.5640 S13:   0.1886                       
REMARK   3      S21:  -1.6733 S22:   1.0189 S23:   2.1404                       
REMARK   3      S31:   1.0921 S32:   0.8143 S33:  -1.4148                       
REMARK   3   TLS GROUP : 17                                                     
REMARK   3    SELECTION: (CHAIN A AND RESID 304:358)                            
REMARK   3    ORIGIN FOR THE GROUP (A): -13.9919  28.9203 -32.2175              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   2.8432 T22:   1.3988                                     
REMARK   3      T33:   1.3454 T12:   0.8431                                     
REMARK   3      T13:  -0.0110 T23:   0.1020                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.5774 L22:   2.0207                                     
REMARK   3      L33:   6.2237 L12:  -3.6009                                     
REMARK   3      L13:   2.1127 L23:   5.2894                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -2.6985 S12:  -0.2379 S13:  -0.4800                       
REMARK   3      S21:   2.1610 S22:  -1.1836 S23:   1.7470                       
REMARK   3      S31:   0.5127 S32:   0.3753 S33:   2.7792                       
REMARK   3   TLS GROUP : 18                                                     
REMARK   3    SELECTION: (CHAIN A AND RESID 359:365)                            
REMARK   3    ORIGIN FOR THE GROUP (A): -20.9640  44.0607 -24.6133              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2472 T22:   1.3242                                     
REMARK   3      T33:   2.3315 T12:  -0.1534                                     
REMARK   3      T13:   1.0722 T23:   0.5431                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.4342 L22:   3.0140                                     
REMARK   3      L33:   4.7047 L12:   0.7462                                     
REMARK   3      L13:   4.9919 L23:   1.3063                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1886 S12:  -2.7347 S13:  -1.3710                       
REMARK   3      S21:   0.6136 S22:  -1.1581 S23:  -0.8703                       
REMARK   3      S31:   0.0574 S32:   2.5485 S33:  -1.7562                       
REMARK   3   TLS GROUP : 19                                                     
REMARK   3    SELECTION: (CHAIN A AND RESID 366:380)                            
REMARK   3    ORIGIN FOR THE GROUP (A): -18.2705  37.6637  -0.3290              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.1231 T22:   1.4751                                     
REMARK   3      T33:   1.3665 T12:  -0.1084                                     
REMARK   3      T13:  -0.1425 T23:  -0.2880                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4929 L22:   0.8911                                     
REMARK   3      L33:   9.3941 L12:  -0.8469                                     
REMARK   3      L13:  -0.8258 L23:  -1.6303                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   1.0051 S12:  -1.2685 S13:  -0.3421                       
REMARK   3      S21:  -0.1196 S22:  -0.4855 S23:  -1.0360                       
REMARK   3      S31:  -1.0653 S32:   1.8673 S33:  -0.5069                       
REMARK   3   TLS GROUP : 20                                                     
REMARK   3    SELECTION: (CHAIN A AND RESID 381:425)                            
REMARK   3    ORIGIN FOR THE GROUP (A): -11.4277  27.2723   8.6760              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.3139 T22:   2.8820                                     
REMARK   3      T33:   1.7438 T12:  -0.3185                                     
REMARK   3      T13:  -0.2072 T23:  -0.3928                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.0532 L22:   8.3397                                     
REMARK   3      L33:   8.0113 L12:  -5.0486                                     
REMARK   3      L13:   1.6955 L23:  -1.9700                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2951 S12:  -1.1929 S13:   1.5034                       
REMARK   3      S21:   0.7089 S22:   1.4228 S23:  -1.7905                       
REMARK   3      S31:  -0.2458 S32:  -1.5696 S33:  -1.0322                       
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 5H7V COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 25-NOV-16.                  
REMARK 100 THE DEPOSITION ID IS D_1300002168.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 20-DEC-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 4.6                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRF                               
REMARK 200  BEAMLINE                       : BL18U1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9778                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS3 S 6M              
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XIA2                               
REMARK 200  DATA SCALING SOFTWARE          : XIA2                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 5987                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.820                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 38.090                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 25.20                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 17.4700                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHENIX                                                
REMARK 200 STARTING MODEL: 2MSX                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 59.14                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.01                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.6M AMMONIUM SULFATE, 20% (V/V)         
REMARK 280  GLYCEROL, 0.08M SODIUM ACETATE, PH 4.6, VAPOR DIFFUSION, SITTING    
REMARK 280  DROP, TEMPERATURE 293K                                              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y+1/2,X+1/2,Z+1/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+3/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+1/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+3/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z+1/2                                            
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       62.29000            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       47.81000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       47.81000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       31.14500            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       47.81000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       47.81000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       93.43500            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       47.81000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       47.81000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       31.14500            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       47.81000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       47.81000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       93.43500            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       62.29000            
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: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 0 ANGSTROM**2                             
REMARK 350 SURFACE AREA OF THE COMPLEX: 19100 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 KCAL/MOL                          
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 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     ARG A    31                                                      
REMARK 465     SER A    32                                                      
REMARK 465     PRO A    33                                                      
REMARK 465     TRP A    34                                                      
REMARK 465     PRO A    35                                                      
REMARK 465     GLY A    36                                                      
REMARK 465     PRO A    37                                                      
REMARK 465     PRO A    38                                                      
REMARK 465     PRO A    39                                                      
REMARK 465     ALA A    40                                                      
REMARK 465     PRO A    41                                                      
REMARK 465     PRO A    42                                                      
REMARK 465     GLY A    43                                                      
REMARK 465     LEU A    44                                                      
REMARK 465     GLN A   155                                                      
REMARK 465     GLY A   156                                                      
REMARK 465     PHE A   157                                                      
REMARK 465     GLY A   158                                                      
REMARK 465     GLY A   159                                                      
REMARK 465     SER A   160                                                      
REMARK 465     GLY A   161                                                      
REMARK 465     ILE A   162                                                      
REMARK 465     PRO A   163                                                      
REMARK 465     LYS A   164                                                      
REMARK 465     ALA A   165                                                      
REMARK 465     THR A   225                                                      
REMARK 465     SER A   226                                                      
REMARK 465     SER A   227                                                      
REMARK 465     ASP A   228                                                      
REMARK 465     HIS A   229                                                      
REMARK 465     PRO A   230                                                      
REMARK 465     GLU A   231                                                      
REMARK 465     MET A   308                                                      
REMARK 465     GLU A   309                                                      
REMARK 465     ARG A   310                                                      
REMARK 465     ARG A   311                                                      
REMARK 465     HIS A   312                                                      
REMARK 465     PRO A   313                                                      
REMARK 465     VAL A   314                                                      
REMARK 465     CYS A   315                                                      
REMARK 465     SER A   316                                                      
REMARK 465     GLY A   317                                                      
REMARK 465     THR A   318                                                      
REMARK 465     CYS A   319                                                      
REMARK 465     GLN A   320                                                      
REMARK 465     PRO A   321                                                      
REMARK 465     THR A   322                                                      
REMARK 465     GLN A   323                                                      
REMARK 465     PHE A   324                                                      
REMARK 465     ARG A   325                                                      
REMARK 465     CYS A   326                                                      
REMARK 465     SER A   327                                                      
REMARK 465     ASN A   328                                                      
REMARK 465     GLY A   329                                                      
REMARK 465     CYS A   330                                                      
REMARK 465     CYS A   331                                                      
REMARK 465     ILE A   332                                                      
REMARK 465     ASP A   333                                                      
REMARK 465     SER A   334                                                      
REMARK 465     PHE A   335                                                      
REMARK 465     LEU A   336                                                      
REMARK 465     GLU A   337                                                      
REMARK 465     CYS A   338                                                      
REMARK 465     ASP A   339                                                      
REMARK 465     ASP A   340                                                      
REMARK 465     THR A   341                                                      
REMARK 465     PRO A   342                                                      
REMARK 465     ASN A   343                                                      
REMARK 465     CYS A   344                                                      
REMARK 465     PRO A   345                                                      
REMARK 465     ASP A   346                                                      
REMARK 465     ALA A   347                                                      
REMARK 465     SER A   348                                                      
REMARK 465     ASP A   349                                                      
REMARK 465     GLU A   350                                                      
REMARK 465     ARG A   426                                                      
REMARK 465     GLY A   427                                                      
REMARK 465     ILE A   428                                                      
REMARK 465     SER A   429                                                      
REMARK 465     LYS A   430                                                      
REMARK 465     LYS A   431                                                      
REMARK 465     ASP A   432                                                      
REMARK 465     VAL A   433                                                      
REMARK 465     PHE A   434                                                      
REMARK 465     GLY A   435                                                      
REMARK 465     LEU A   436                                                      
REMARK 465     ARG A   437                                                      
REMARK 465     ARG A   438                                                      
REMARK 465     GLU A   439                                                      
REMARK 465     ILE A   440                                                      
REMARK 465     PRO A   441                                                      
REMARK 465     THR A   442                                                      
REMARK 465     ARG A   443                                                      
REMARK 465     THR A   444                                                      
REMARK 465     GLY A   445                                                      
REMARK 465     HIS A   446                                                      
REMARK 465     HIS A   447                                                      
REMARK 465     HIS A   448                                                      
REMARK 465     HIS A   449                                                      
REMARK 465     HIS A   450                                                      
REMARK 465     HIS A   451                                                      
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     ARG A 108    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ILE A 113    CG1  CG2  CD1                                       
REMARK 470     TRP A 166    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP A 166    CZ3  CH2                                            
REMARK 470     ARG A 190    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN A 304    CG   CD   OE1  NE2                                  
REMARK 470     PHE A 368    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     HIS A 374    CG   ND1  CD2  CE1  NE2                             
REMARK 470     PHE A 415    CD1  CD2  CE1  CE2  CZ                              
REMARK 470     GLU A 416    CD   OE1  OE2                                       
REMARK 470     LEU A 422    CD1  CD2                                            
REMARK 470     GLU A 423    CD   OE1  OE2                                       
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OH   TYR A   123     OE1  GLU A   295              2.12            
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    ASP A  49      -73.13    -57.85                                   
REMARK 500    CYS A  50      -65.78     17.79                                   
REMARK 500    LEU A  51      -36.46    -27.46                                   
REMARK 500    VAL A  62      148.25   -173.76                                   
REMARK 500    THR A  65      -75.24     59.72                                   
REMARK 500    LEU A  76     -133.35   -111.60                                   
REMARK 500    GLN A 105       90.48     50.69                                   
REMARK 500    ASP A 107      -52.76     80.58                                   
REMARK 500    ARG A 108       50.58    -67.25                                   
REMARK 500    GLU A 110      -61.88    -97.02                                   
REMARK 500    ASP A 111       47.81    -91.24                                   
REMARK 500    ALA A 112       60.90   -115.60                                   
REMARK 500    ALA A 115      -54.68   -146.20                                   
REMARK 500    CYS A 116     -148.96     67.28                                   
REMARK 500    PHE A 117      131.60    123.51                                   
REMARK 500    GLU A 124       82.16     58.48                                   
REMARK 500    ARG A 134      -75.13   -150.36                                   
REMARK 500    GLU A 135     -135.07   -150.19                                   
REMARK 500    LEU A 141     -162.32   -100.22                                   
REMARK 500    ARG A 143      -67.29     58.95                                   
REMARK 500    VAL A 145     -130.77     53.61                                   
REMARK 500    TYR A 146       25.16     38.19                                   
REMARK 500    ARG A 147        6.59    -68.14                                   
REMARK 500    GLN A 151        9.19     56.45                                   
REMARK 500    ALA A 167     -150.79    -80.36                                   
REMARK 500    GLU A 177      -47.71   -133.68                                   
REMARK 500    LEU A 181     -163.55   -161.47                                   
REMARK 500    VAL A 184      102.81     57.96                                   
REMARK 500    GLU A 185     -162.87    -67.82                                   
REMARK 500    ASN A 186     -136.48     48.98                                   
REMARK 500    THR A 187     -134.00   -176.23                                   
REMARK 500    ASP A 188       89.02     64.01                                   
REMARK 500    LEU A 192      -10.20   -160.97                                   
REMARK 500    LYS A 203     -132.96   -113.72                                   
REMARK 500    ASN A 206      106.58     52.26                                   
REMARK 500    GLN A 207       88.77   -167.47                                   
REMARK 500    PHE A 220     -169.46   -127.50                                   
REMARK 500    THR A 223       97.04    -66.94                                   
REMARK 500    ALA A 234      113.30   -161.25                                   
REMARK 500    ASN A 254     -176.32    -68.28                                   
REMARK 500    SER A 262       62.38   -158.70                                   
REMARK 500    LEU A 284       12.18     56.33                                   
REMARK 500    ASN A 289      119.59   -173.34                                   
REMARK 500    CYS A 300     -151.99   -126.10                                   
REMARK 500    ARG A 301      138.68     66.06                                   
REMARK 500    CYS A 353     -116.22    -70.82                                   
REMARK 500    GLU A 354      -47.65   -144.82                                   
REMARK 500    TYR A 356      148.66     67.10                                   
REMARK 500    SER A 358      120.88   -177.95                                   
REMARK 500    ASP A 361      -19.03   -150.58                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      61 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 GLU A  144     VAL A  145                 -147.94                    
REMARK 500 TYR A  149     ARG A  150                  149.52                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  5H7V A   36   441  UNP    O43278   SPIT1_HUMAN     36    441             
SEQADV 5H7V ARG A   31  UNP  O43278              EXPRESSION TAG                 
SEQADV 5H7V SER A   32  UNP  O43278              EXPRESSION TAG                 
SEQADV 5H7V PRO A   33  UNP  O43278              EXPRESSION TAG                 
SEQADV 5H7V TRP A   34  UNP  O43278              EXPRESSION TAG                 
SEQADV 5H7V PRO A   35  UNP  O43278              EXPRESSION TAG                 
SEQADV 5H7V THR A  442  UNP  O43278              EXPRESSION TAG                 
SEQADV 5H7V ARG A  443  UNP  O43278              EXPRESSION TAG                 
SEQADV 5H7V THR A  444  UNP  O43278              EXPRESSION TAG                 
SEQADV 5H7V GLY A  445  UNP  O43278              EXPRESSION TAG                 
SEQADV 5H7V HIS A  446  UNP  O43278              EXPRESSION TAG                 
SEQADV 5H7V HIS A  447  UNP  O43278              EXPRESSION TAG                 
SEQADV 5H7V HIS A  448  UNP  O43278              EXPRESSION TAG                 
SEQADV 5H7V HIS A  449  UNP  O43278              EXPRESSION TAG                 
SEQADV 5H7V HIS A  450  UNP  O43278              EXPRESSION TAG                 
SEQADV 5H7V HIS A  451  UNP  O43278              EXPRESSION TAG                 
SEQRES   1 A  421  ARG SER PRO TRP PRO GLY PRO PRO PRO ALA PRO PRO GLY          
SEQRES   2 A  421  LEU PRO ALA GLY ALA ASP CYS LEU ASN SER PHE THR ALA          
SEQRES   3 A  421  GLY VAL PRO GLY PHE VAL LEU ASP THR ASN ALA SER VAL          
SEQRES   4 A  421  SER ASN GLY ALA THR PHE LEU GLU SER PRO THR VAL ARG          
SEQRES   5 A  421  ARG GLY TRP ASP CYS VAL ARG ALA CYS CYS THR THR GLN          
SEQRES   6 A  421  ASN CYS ASN LEU ALA LEU VAL GLU LEU GLN PRO ASP ARG          
SEQRES   7 A  421  GLY GLU ASP ALA ILE ALA ALA CYS PHE LEU ILE ASN CYS          
SEQRES   8 A  421  LEU TYR GLU GLN ASN PHE VAL CYS LYS PHE ALA PRO ARG          
SEQRES   9 A  421  GLU GLY PHE ILE ASN TYR LEU THR ARG GLU VAL TYR ARG          
SEQRES  10 A  421  SER TYR ARG GLN LEU ARG THR GLN GLY PHE GLY GLY SER          
SEQRES  11 A  421  GLY ILE PRO LYS ALA TRP ALA GLY ILE ASP LEU LYS VAL          
SEQRES  12 A  421  GLN PRO GLN GLU PRO LEU VAL LEU LYS ASP VAL GLU ASN          
SEQRES  13 A  421  THR ASP TRP ARG LEU LEU ARG GLY ASP THR ASP VAL ARG          
SEQRES  14 A  421  VAL GLU ARG LYS ASP PRO ASN GLN VAL GLU LEU TRP GLY          
SEQRES  15 A  421  LEU LYS GLU GLY THR TYR LEU PHE GLN LEU THR VAL THR          
SEQRES  16 A  421  SER SER ASP HIS PRO GLU ASP THR ALA ASN VAL THR VAL          
SEQRES  17 A  421  THR VAL LEU SER THR LYS GLN THR GLU ASP TYR CYS LEU          
SEQRES  18 A  421  ALA SER ASN LYS VAL GLY ARG CYS ARG GLY SER PHE PRO          
SEQRES  19 A  421  ARG TRP TYR TYR ASP PRO THR GLU GLN ILE CYS LYS SER          
SEQRES  20 A  421  PHE VAL TYR GLY GLY CYS LEU GLY ASN LYS ASN ASN TYR          
SEQRES  21 A  421  LEU ARG GLU GLU GLU CYS ILE LEU ALA CYS ARG GLY VAL          
SEQRES  22 A  421  GLN GLY PRO SER MET GLU ARG ARG HIS PRO VAL CYS SER          
SEQRES  23 A  421  GLY THR CYS GLN PRO THR GLN PHE ARG CYS SER ASN GLY          
SEQRES  24 A  421  CYS CYS ILE ASP SER PHE LEU GLU CYS ASP ASP THR PRO          
SEQRES  25 A  421  ASN CYS PRO ASP ALA SER ASP GLU ALA ALA CYS GLU LYS          
SEQRES  26 A  421  TYR THR SER GLY PHE ASP GLU LEU GLN ARG ILE HIS PHE          
SEQRES  27 A  421  PRO SER ASP LYS GLY HIS CYS VAL ASP LEU PRO ASP THR          
SEQRES  28 A  421  GLY LEU CYS LYS GLU SER ILE PRO ARG TRP TYR TYR ASN          
SEQRES  29 A  421  PRO PHE SER GLU HIS CYS ALA ARG PHE THR TYR GLY GLY          
SEQRES  30 A  421  CYS TYR GLY ASN LYS ASN ASN PHE GLU GLU GLU GLN GLN          
SEQRES  31 A  421  CYS LEU GLU SER CYS ARG GLY ILE SER LYS LYS ASP VAL          
SEQRES  32 A  421  PHE GLY LEU ARG ARG GLU ILE PRO THR ARG THR GLY HIS          
SEQRES  33 A  421  HIS HIS HIS HIS HIS                                          
HELIX    1 AA1 ASP A   49  PHE A   54  5                                   6    
HELIX    2 AA2 SER A   68  GLY A   72  5                                   5    
HELIX    3 AA3 ARG A   83  THR A   93  1                                  11    
HELIX    4 AA4 SER A  242  CYS A  250  1                                   9    
HELIX    5 AA5 ARG A  292  CYS A  300  1                                   9    
HELIX    6 AA6 GLU A  417  SER A  424  1                                   8    
SHEET    1 AA1 2 GLY A  60  LEU A  63  0                                        
SHEET    2 AA1 2 PHE A 131  GLU A 135 -1  O  ARG A 134   N  GLY A  60           
SHEET    1 AA2 3 LEU A 118  ILE A 119  0                                        
SHEET    2 AA2 3 LEU A  99  GLU A 103 -1  N  LEU A  99   O  ILE A 119           
SHEET    3 AA2 3 PHE A 137  TYR A 140 -1  O  TYR A 140   N  ALA A 100           
SHEET    1 AA3 4 ASP A 170  VAL A 173  0                                        
SHEET    2 AA3 4 THR A 237  VAL A 240  1  O  THR A 239   N  LEU A 171           
SHEET    3 AA3 4 GLY A 216  LEU A 222 -1  N  TYR A 218   O  VAL A 238           
SHEET    4 AA3 4 TRP A 189  LEU A 191 -1  N  ARG A 190   O  GLN A 221           
SHEET    1 AA4 2 VAL A 200  LYS A 203  0                                        
SHEET    2 AA4 2 GLN A 207  LEU A 210 -1  O  GLU A 209   N  GLU A 201           
SHEET    1 AA5 2 PHE A 263  ASP A 269  0                                        
SHEET    2 AA5 2 ILE A 274  TYR A 280 -1  O  ILE A 274   N  ASP A 269           
SHEET    1 AA6 2 ILE A 388  ASN A 394  0                                        
SHEET    2 AA6 2 HIS A 399  TYR A 405 -1  O  TYR A 405   N  ILE A 388           
SSBOND   1 CYS A   50    CYS A   92                          1555   1555  2.03  
SSBOND   2 CYS A   87    CYS A  116                          1555   1555  2.04  
SSBOND   3 CYS A   91    CYS A   97                          1555   1555  2.03  
SSBOND   4 CYS A  121    CYS A  129                          1555   1555  2.02  
SSBOND   5 CYS A  250    CYS A  300                          1555   1555  2.03  
SSBOND   6 CYS A  259    CYS A  283                          1555   1555  2.03  
SSBOND   7 CYS A  275    CYS A  296                          1555   1555  2.04  
SSBOND   8 CYS A  375    CYS A  425                          1555   1555  2.03  
SSBOND   9 CYS A  384    CYS A  408                          1555   1555  2.04  
SSBOND  10 CYS A  400    CYS A  421                          1555   1555  2.04  
CISPEP   1 LEU A  152    ARG A  153          0        -0.26                     
CISPEP   2 ASP A  204    PRO A  205          0        -0.37                     
CISPEP   3 TYR A  356    THR A  357          0         6.57                     
CISPEP   4 PHE A  360    ASP A  361          0         9.39                     
CISPEP   5 HIS A  374    CYS A  375          0       -10.85                     
CRYST1   95.620   95.620  124.580  90.00  90.00  90.00 P 41 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      0.010458  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010458  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008027        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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