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Database: PDB
Entry: 2WFT
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HEADER    SIGNALING PROTEIN                       15-APR-09   2WFT              
TITLE     CRYSTAL STRUCTURE OF THE HUMAN HIP ECTODOMAIN                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HEDGEHOG-INTERACTING PROTEIN;                              
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: C-TERMINAL DOMAIN, RESIDUES 214-671;                       
COMPND   5 SYNONYM: HEDGEHOG-INTERACTING PROTEIN HIP, HIP, HHIP;                
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 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE   7 EXPRESSION_SYSTEM_CELL_LINE: HUMAN EMBRYONIC KIDNEY (HEK)            
SOURCE   8  293T CELLS;                                                         
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PHLSEC                                    
KEYWDS    MEMBRANE, SECRETED, CYTOPLASM, DEVELOPMENT, DISULFIDE BOND,           
KEYWDS   2 EGF-LIKE DOMAIN, HEDGEHOG SIGNALLING, SIGNAL TRANSDUCTION,           
KEYWDS   3 ALTERNATIVE SPLICING, POLYMORPHISM, GLYCOPROTEIN, CELL               
KEYWDS   4 MEMBRANE, SIGNALING PROTEIN                                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    B.BISHOP,A.R.ARICESCU,K.HARLOS,C.A.O'CALLAGHAN,E.Y.JONES,             
AUTHOR   2 C.SIEBOLD                                                            
REVDAT   2   21-JUL-09 2WFT    1       JRNL                                     
REVDAT   1   30-JUN-09 2WFT    0                                                
JRNL        AUTH   B.BISHOP,A.R.ARICESCU,K.HARLOS,C.A.O'CALLAGHAN,              
JRNL        AUTH 2 E.Y.JONES,C.SIEBOLD                                          
JRNL        TITL   STRUCTURAL INSIGHTS INTO HEDGEHOG LIGAND                     
JRNL        TITL 2 SEQUESTRATION BY THE HUMAN HEDGEHOG-INTERACTING              
JRNL        TITL 3 PROTEIN HIP                                                  
JRNL        REF    NAT.STRUCT.MOL.BIOL.          V.  16   698 2009              
JRNL        REFN                   ISSN 1545-9993                               
JRNL        PMID   19561611                                                     
JRNL        DOI    10.1038/NSMB.1607                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE)                               
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.89                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 45390                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.201                           
REMARK   3   R VALUE            (WORKING SET) : 0.199                           
REMARK   3   FREE R VALUE                     : 0.238                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2294                            
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 19.8920 -  6.9601    1.00     2912   142  0.2357 0.2684        
REMARK   3     2  6.9601 -  5.5642    1.00     2754   140  0.1825 0.2203        
REMARK   3     3  5.5642 -  4.8727    1.00     2740   149  0.1442 0.1723        
REMARK   3     4  4.8727 -  4.4326    1.00     2733   138  0.1329 0.1573        
REMARK   3     5  4.4326 -  4.1179    1.00     2723   133  0.1409 0.1952        
REMARK   3     6  4.1179 -  3.8770    1.00     2656   142  0.1588 0.1911        
REMARK   3     7  3.8770 -  3.6841    1.00     2728   141  0.1780 0.2009        
REMARK   3     8  3.6841 -  3.5246    1.00     2669   133  0.1811 0.2319        
REMARK   3     9  3.5246 -  3.3896    1.00     2656   150  0.1928 0.2677        
REMARK   3    10  3.3896 -  3.2732    1.00     2681   134  0.2106 0.2585        
REMARK   3    11  3.2732 -  3.1713    1.00     2631   150  0.2280 0.2382        
REMARK   3    12  3.1713 -  3.0810    1.00     2685   146  0.2353 0.2929        
REMARK   3    13  3.0810 -  3.0001    1.00     2661   145  0.2455 0.3001        
REMARK   3    14  3.0001 -  2.9272    1.00     2623   160  0.2804 0.3456        
REMARK   3    15  2.9272 -  2.8608    1.00     2626   142  0.2810 0.3404        
REMARK   3    16  2.8608 -  2.8001    1.00     2618   149  0.2974 0.3520        
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              : 0.32                                          
REMARK   3   B_SOL              : 50.64                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.320            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.550           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 67.23                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 6.24020                                              
REMARK   3    B22 (A**2) : 6.24020                                              
REMARK   3    B33 (A**2) : -12.48050                                            
REMARK   3    B12 (A**2) : -0.00000                                             
REMARK   3    B13 (A**2) : -0.00000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
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      :  0.014           6746                                  
REMARK   3   ANGLE     :  1.724           9078                                  
REMARK   3   CHIRALITY :  0.117            976                                  
REMARK   3   PLANARITY :  0.006           1194                                  
REMARK   3   DIHEDRAL  : 19.827           2484                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 8                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 214:484)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  82.3912  29.9222  96.0316              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6723 T22:   0.0680                                     
REMARK   3      T33:   0.2259 T12:  -0.1250                                     
REMARK   3      T13:   0.0619 T23:   0.0143                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1278 L22:   1.6209                                     
REMARK   3      L33:   2.7965 L12:   1.1752                                     
REMARK   3      L13:   0.1898 L23:   0.1572                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2906 S12:   0.2096 S13:   0.0733                       
REMARK   3      S21:  -0.7820 S22:   0.3814 S23:  -0.0016                       
REMARK   3      S31:  -0.4111 S32:   0.1504 S33:   0.1943                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 485:532)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  76.9529  10.5907 103.7939              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5873 T22:   0.1217                                     
REMARK   3      T33:   0.4391 T12:  -0.0033                                     
REMARK   3      T13:  -0.0561 T23:  -0.0425                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  -0.0069 L22:   0.0254                                     
REMARK   3      L33:   0.8996 L12:  -0.3526                                     
REMARK   3      L13:  -0.0597 L23:   0.2747                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0597 S12:  -0.2379 S13:  -0.3370                       
REMARK   3      S21:  -0.4551 S22:   0.0246 S23:   0.1584                       
REMARK   3      S31:   0.2390 S32:   0.0784 S33:   0.0000                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 533:624)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  86.9553  25.5032 110.4514              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4904 T22:   0.1964                                     
REMARK   3      T33:   0.4245 T12:  -0.0732                                     
REMARK   3      T13:   0.1199 T23:  -0.0456                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  -0.2841 L22:   0.5208                                     
REMARK   3      L33:   2.6735 L12:   0.4087                                     
REMARK   3      L13:   0.6123 L23:  -0.4777                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0412 S12:  -0.2057 S13:  -0.0875                       
REMARK   3      S21:  -0.4646 S22:   0.0775 S23:  -0.0429                       
REMARK   3      S31:  -0.3067 S32:   0.5959 S33:  -0.0000                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 625:671)                            
REMARK   3    ORIGIN FOR THE GROUP (A): 109.4824  61.8628  82.6065              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6334 T22:   0.4590                                     
REMARK   3      T33:   0.3051 T12:  -0.3533                                     
REMARK   3      T13:   0.1155 T23:   0.0650                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0297 L22:   0.2094                                     
REMARK   3      L33:   0.0342 L12:   0.2795                                     
REMARK   3      L13:  -0.4811 L23:  -0.1192                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3390 S12:  -0.5771 S13:   0.3296                       
REMARK   3      S21:   0.0517 S22:   0.0238 S23:   0.2345                       
REMARK   3      S31:   0.9486 S32:  -1.4085 S33:  -0.0188                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: (CHAIN B AND RESID 214:337)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  72.6542  22.9081 146.7886              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1748 T22:   0.2475                                     
REMARK   3      T33:   0.2134 T12:  -0.0652                                     
REMARK   3      T13:   0.0626 T23:   0.0023                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9603 L22:   0.4277                                     
REMARK   3      L33:   2.3285 L12:   0.1190                                     
REMARK   3      L13:   0.1936 L23:   0.0734                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1680 S12:  -0.3335 S13:  -0.0054                       
REMARK   3      S21:  -0.0028 S22:  -0.0525 S23:   0.0267                       
REMARK   3      S31:  -0.1321 S32:   0.0291 S33:  -0.0001                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: (CHAIN B AND RESID 338:490)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  83.7168  19.6109 162.6518              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5456 T22:   0.9943                                     
REMARK   3      T33:   0.3762 T12:  -0.1283                                     
REMARK   3      T13:  -0.0162 T23:  -0.0023                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9160 L22:   0.2704                                     
REMARK   3      L33:   0.7114 L12:   0.2378                                     
REMARK   3      L13:   0.8034 L23:   0.5003                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0685 S12:  -0.9809 S13:  -0.2238                       
REMARK   3      S21:   0.4476 S22:   0.1524 S23:  -0.0271                       
REMARK   3      S31:   0.0453 S32:   0.3987 S33:  -0.0001                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: (CHAIN B AND RESID 491:627)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  83.2037  15.9889 140.8860              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2718 T22:   0.3491                                     
REMARK   3      T33:   0.3981 T12:  -0.0484                                     
REMARK   3      T13:  -0.0222 T23:   0.0570                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6756 L22:   0.4946                                     
REMARK   3      L33:   2.9525 L12:   0.1837                                     
REMARK   3      L13:  -0.7293 L23:  -0.3988                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0909 S12:  -0.4008 S13:  -0.1465                       
REMARK   3      S21:   0.1169 S22:  -0.1113 S23:  -0.0759                       
REMARK   3      S31:   0.2010 S32:   0.3860 S33:   0.0000                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: (CHAIN B AND RESID 628:670)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  39.4074  13.2750 173.5493              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7676 T22:   0.5557                                     
REMARK   3      T33:   0.5160 T12:  -0.2163                                     
REMARK   3      T13:   0.2729 T23:  -0.0381                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3447 L22:   0.1392                                     
REMARK   3      L33:   0.0842 L12:   0.2180                                     
REMARK   3      L13:  -0.1111 L23:  -0.0600                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2768 S12:   0.5533 S13:   0.1699                       
REMARK   3      S21:  -0.3356 S22:   0.0622 S23:   0.1111                       
REMARK   3      S31:  -1.1761 S32:   0.5627 S33:  -0.0075                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : 1                                           
REMARK   3   NCS GROUP : 1                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN A AND (RESSEQ 215:274 OR RESSEQ       
REMARK   3                          276:306 OR RESSEQ 316:415 OR RESSEQ         
REMARK   3                          421:439 OR RESSEQ 489:521 OR RESSEQ         
REMARK   3                          533:640 OR RESSEQ 648:657 OR RESSEQ         
REMARK   3                          661:668 )                                   
REMARK   3     SELECTION          : CHAIN B AND (RESSEQ 215:274 OR RESSEQ       
REMARK   3                          276:306 OR RESSEQ 316:415 OR RESSEQ         
REMARK   3                          421:439 OR RESSEQ 489:521 OR RESSEQ         
REMARK   3                          533:640 OR RESSEQ 648:657 OR RESSEQ         
REMARK   3                          661:668 )                                   
REMARK   3     ATOM PAIRS NUMBER  : 2875                                        
REMARK   3     RMSD               : 0.131                                       
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2WFT COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 15-APR-09.                  
REMARK 100 THE PDBE ID CODE IS EBI-39464.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
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               : ESRF                               
REMARK 200  BEAMLINE                       : ID29                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9792                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL2000                            
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 45408                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.80                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.00                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.0                                
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.5                               
REMARK 200  DATA REDUNDANCY                : 9.1                                
REMARK 200  R MERGE                    (I) : 0.11                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 14.70                              
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.90                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 8.9                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.73                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.40                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: AUTOSHARP                                             
REMARK 200 STARTING MODEL: NONE                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS  (%): 74.60                                      
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.88                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M TRIS-HCL, PH 8.5 3.5 M             
REMARK 280  POTASSIUM FORMATE                                                   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+2/3                                           
REMARK 290       6555   -X,-X+Y,-Z+1/3                                          
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      101.97200            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      203.94400            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000      203.94400            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000      101.97200            
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 GENERATING THE BIOMOLECULE                                           
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: PQS                                                   
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: PQS                                                   
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     GLN A   307                                                      
REMARK 465     GLU A   308                                                      
REMARK 465     ARG A   309                                                      
REMARK 465     TRP A   310                                                      
REMARK 465     ALA A   311                                                      
REMARK 465     ILE A   312                                                      
REMARK 465     GLY A   313                                                      
REMARK 465     PRO A   314                                                      
REMARK 465     GLY A   457                                                      
REMARK 465     LYS A   458                                                      
REMARK 465     ASN A   459                                                      
REMARK 465     LYS A   470                                                      
REMARK 465     GLY A   471                                                      
REMARK 465     LYS A   472                                                      
REMARK 465     ASP A   473                                                      
REMARK 465     TYR A   474                                                      
REMARK 465     GLU A   475                                                      
REMARK 465     SER A   476                                                      
REMARK 465     GLU A   477                                                      
REMARK 465     PRO A   478                                                      
REMARK 465     GLN B   307                                                      
REMARK 465     GLU B   308                                                      
REMARK 465     ARG B   309                                                      
REMARK 465     TRP B   310                                                      
REMARK 465     ALA B   311                                                      
REMARK 465     ILE B   312                                                      
REMARK 465     GLY B   313                                                      
REMARK 465     ASN B   416                                                      
REMARK 465     SER B   417                                                      
REMARK 465     THR B   418                                                      
REMARK 465     ASN B   419                                                      
REMARK 465     GLN B   420                                                      
REMARK 465     HIS B   440                                                      
REMARK 465     PRO B   441                                                      
REMARK 465     THR B   442                                                      
REMARK 465     ASP B   443                                                      
REMARK 465     ILE B   444                                                      
REMARK 465     ASN B   445                                                      
REMARK 465     ILE B   446                                                      
REMARK 465     ASN B   447                                                      
REMARK 465     GLY B   457                                                      
REMARK 465     LYS B   458                                                      
REMARK 465     ASN B   459                                                      
REMARK 465     ARG B   460                                                      
REMARK 465     LEU B   466                                                      
REMARK 465     GLN B   467                                                      
REMARK 465     ILE B   468                                                      
REMARK 465     ILE B   469                                                      
REMARK 465     LYS B   470                                                      
REMARK 465     GLY B   471                                                      
REMARK 465     LYS B   472                                                      
REMARK 465     ASP B   473                                                      
REMARK 465     TYR B   474                                                      
REMARK 465     GLU B   475                                                      
REMARK 465     SER B   476                                                      
REMARK 465     GLU B   477                                                      
REMARK 465     PRO B   478                                                      
REMARK 465     SER B   479                                                      
REMARK 465     LEU B   480                                                      
REMARK 465     LEU B   481                                                      
REMARK 465     GLU B   482                                                      
REMARK 465     PHE B   483                                                      
REMARK 465     LYS B   484                                                      
REMARK 465     PRO B   485                                                      
REMARK 465     PHE B   486                                                      
REMARK 465     SER B   487                                                      
REMARK 465     ASN B   488                                                      
REMARK 465     THR B   527                                                      
REMARK 465     LYS B   528                                                      
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 671    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     HIS B 214    CG   ND1  CD2  CE1  NE2                             
REMARK 470     ARG B 671    CA   C    O    CB   CG   CD   NE   CZ   NH1  NH2    
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500                                                                      
REMARK 500   OH   TYR A   661     OE1  GLU B   257     5665      2.03           
REMARK 500   OE1  GLU B   257     OH   TYR A   661     5565      2.03           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG A 227   NE  -  CZ  -  NH1 ANGL. DEV. =  -5.4 DEGREES          
REMARK 500    ARG A 227   NE  -  CZ  -  NH2 ANGL. DEV. =   5.8 DEGREES          
REMARK 500    LEU A 287   CA  -  CB  -  CG  ANGL. DEV. =  14.1 DEGREES          
REMARK 500    ARG A 328   CD  -  NE  -  CZ  ANGL. DEV. =   9.1 DEGREES          
REMARK 500    ARG A 328   NE  -  CZ  -  NH1 ANGL. DEV. =   6.1 DEGREES          
REMARK 500    ARG A 328   NE  -  CZ  -  NH2 ANGL. DEV. =  -6.2 DEGREES          
REMARK 500    ARG A 394   CD  -  NE  -  CZ  ANGL. DEV. =   8.7 DEGREES          
REMARK 500    ARG A 394   NE  -  CZ  -  NH1 ANGL. DEV. =  -6.3 DEGREES          
REMARK 500    ARG A 394   NE  -  CZ  -  NH2 ANGL. DEV. =   5.9 DEGREES          
REMARK 500    ARG A 498   CD  -  NE  -  CZ  ANGL. DEV. =   9.2 DEGREES          
REMARK 500    ARG A 498   NE  -  CZ  -  NH1 ANGL. DEV. =   6.2 DEGREES          
REMARK 500    ARG A 498   NE  -  CZ  -  NH2 ANGL. DEV. =  -6.6 DEGREES          
REMARK 500    ARG A 595   CD  -  NE  -  CZ  ANGL. DEV. =   8.6 DEGREES          
REMARK 500    ARG A 595   NE  -  CZ  -  NH1 ANGL. DEV. =   5.7 DEGREES          
REMARK 500    ARG A 595   NE  -  CZ  -  NH2 ANGL. DEV. =  -6.5 DEGREES          
REMARK 500    ARG A 613   CD  -  NE  -  CZ  ANGL. DEV. =   9.3 DEGREES          
REMARK 500    ARG A 613   NE  -  CZ  -  NH1 ANGL. DEV. =   6.3 DEGREES          
REMARK 500    ARG A 613   NE  -  CZ  -  NH2 ANGL. DEV. =  -7.1 DEGREES          
REMARK 500    ARG A 635   CD  -  NE  -  CZ  ANGL. DEV. =   9.6 DEGREES          
REMARK 500    ARG A 635   NE  -  CZ  -  NH1 ANGL. DEV. =   7.0 DEGREES          
REMARK 500    ARG A 635   NE  -  CZ  -  NH2 ANGL. DEV. =  -6.7 DEGREES          
REMARK 500    ARG B 227   NE  -  CZ  -  NH1 ANGL. DEV. =   5.0 DEGREES          
REMARK 500    ARG B 227   NE  -  CZ  -  NH2 ANGL. DEV. =  -6.1 DEGREES          
REMARK 500    ARG B 328   CD  -  NE  -  CZ  ANGL. DEV. =   9.3 DEGREES          
REMARK 500    ARG B 328   NE  -  CZ  -  NH1 ANGL. DEV. =  -5.5 DEGREES          
REMARK 500    ARG B 328   NE  -  CZ  -  NH2 ANGL. DEV. =   6.0 DEGREES          
REMARK 500    ARG B 394   NE  -  CZ  -  NH1 ANGL. DEV. =   5.9 DEGREES          
REMARK 500    ARG B 394   NE  -  CZ  -  NH2 ANGL. DEV. =  -6.5 DEGREES          
REMARK 500    ARG B 498   NE  -  CZ  -  NH1 ANGL. DEV. =  -5.8 DEGREES          
REMARK 500    ARG B 498   NE  -  CZ  -  NH2 ANGL. DEV. =   4.7 DEGREES          
REMARK 500    ARG B 595   CD  -  NE  -  CZ  ANGL. DEV. =   8.8 DEGREES          
REMARK 500    ARG B 595   NE  -  CZ  -  NH1 ANGL. DEV. =  -6.7 DEGREES          
REMARK 500    ARG B 595   NE  -  CZ  -  NH2 ANGL. DEV. =   6.1 DEGREES          
REMARK 500    ARG B 613   CD  -  NE  -  CZ  ANGL. DEV. =   8.7 DEGREES          
REMARK 500    ARG B 613   NE  -  CZ  -  NH1 ANGL. DEV. =  -6.3 DEGREES          
REMARK 500    ARG B 613   NE  -  CZ  -  NH2 ANGL. DEV. =   5.6 DEGREES          
REMARK 500    ARG B 635   CD  -  NE  -  CZ  ANGL. DEV. =  10.2 DEGREES          
REMARK 500    ARG B 635   NE  -  CZ  -  NH1 ANGL. DEV. =  -6.6 DEGREES          
REMARK 500    ARG B 635   NE  -  CZ  -  NH2 ANGL. DEV. =   6.2 DEGREES          
REMARK 500    PRO B 664   C   -  N   -  CA  ANGL. DEV. =   9.0 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    GLN A 228       74.63     36.34                                   
REMARK 500    SER A 274     -136.30    -74.15                                   
REMARK 500    ALA A 339      151.68    -45.67                                   
REMARK 500    ARG A 340       86.53   -164.58                                   
REMARK 500    MET A 373       53.50     33.42                                   
REMARK 500    LEU A 385     -158.36    -89.09                                   
REMARK 500    ASP A 387       -9.85     80.45                                   
REMARK 500    HIS A 414       34.37   -164.87                                   
REMARK 500    ASN A 416      -22.45     77.21                                   
REMARK 500    ALA A 426      155.84    175.02                                   
REMARK 500    HIS A 440       65.60     36.96                                   
REMARK 500    ASP A 443      102.18    -45.74                                   
REMARK 500    SER A 455     -120.83   -106.74                                   
REMARK 500    GLU A 482       77.83   -111.71                                   
REMARK 500    ASN A 488     -145.77   -120.54                                   
REMARK 500    SER A 606      153.37    -48.29                                   
REMARK 500    ASN A 614       67.91   -103.31                                   
REMARK 500    SER A 626     -177.03    -55.84                                   
REMARK 500    ASN B 215       12.30   -166.04                                   
REMARK 500    GLN B 228       73.19     37.97                                   
REMARK 500    SER B 274     -141.57    -75.70                                   
REMARK 500    HIS B 315     -132.18   -120.27                                   
REMARK 500    ASP B 316      -62.56    -96.65                                   
REMARK 500    ARG B 340       85.52   -161.05                                   
REMARK 500    MET B 373       53.51     35.19                                   
REMARK 500    LEU B 385     -156.33    -90.27                                   
REMARK 500    ASP B 387      -10.96     80.25                                   
REMARK 500    HIS B 414       35.39   -161.96                                   
REMARK 500    ALA B 426      154.46    172.66                                   
REMARK 500    ARG B 464      173.77    -37.83                                   
REMARK 500    PRO B 525       29.22    -69.78                                   
REMARK 500    TRP B 530       87.22   -169.00                                   
REMARK 500    LYS B 533      143.02   -170.97                                   
REMARK 500    SER B 606      151.97    -48.02                                   
REMARK 500    PRO B 619      -17.99    -49.79                                   
REMARK 500    SER B 626     -177.12    -58.04                                   
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 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  NA B1671                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  NA A1672                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  NA A1673                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL A1674                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL B1672                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL B1673                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2WFX   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE COMPLEX BETWEEN                            
REMARK 900  HUMAN HEDGEHOG-INTERACTING PROTEIN HIP AND                          
REMARK 900  SONIC HEDGEHOG IN THE PRESENCE OF CALCIUM                           
REMARK 900 RELATED ID: 2WG4   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE COMPLEX BETWEEN                            
REMARK 900  HUMAN HEDGEHOG-INTERACTING PROTEIN HIP AND                          
REMARK 900  SONIC HEDGEHOG WITHOUT CALCIUM                                      
REMARK 900 RELATED ID: 2WG3   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE COMPLEX BETWEEN                            
REMARK 900  HUMAN HEDGEHOG-INTERACTING PROTEIN HIP AND                          
REMARK 900  DESERT HEDGEHOG WITHOUT CALCIUM                                     
REMARK 900 RELATED ID: 2WFQ   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE N-TERMINAL                                 
REMARK 900  SIGNALLING DOMAIN OF HUMAN DHH WITHOUT                              
REMARK 900  CALCIUM                                                             
REMARK 900 RELATED ID: 2WFR   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE N-TERMINAL                                 
REMARK 900  SIGNALLING DOMAIN OF HUMAN DHH WITH CALCIUM                         
DBREF  2WFT A  214   671  UNP    Q96QV1   HHIP_HUMAN     214    671             
DBREF  2WFT B  214   671  UNP    Q96QV1   HHIP_HUMAN     214    671             
SEQRES   1 A  458  HIS ASN CYS PHE CYS ILE GLN GLU VAL VAL SER GLY LEU          
SEQRES   2 A  458  ARG GLN PRO VAL GLY ALA LEU HIS SER GLY ASP GLY SER          
SEQRES   3 A  458  GLN ARG LEU PHE ILE LEU GLU LYS GLU GLY TYR VAL LYS          
SEQRES   4 A  458  ILE LEU THR PRO GLU GLY GLU ILE PHE LYS GLU PRO TYR          
SEQRES   5 A  458  LEU ASP ILE HIS LYS LEU VAL GLN SER GLY ILE LYS GLY          
SEQRES   6 A  458  GLY ASP GLU ARG GLY LEU LEU SER LEU ALA PHE HIS PRO          
SEQRES   7 A  458  ASN TYR LYS LYS ASN GLY LYS LEU TYR VAL SER TYR THR          
SEQRES   8 A  458  THR ASN GLN GLU ARG TRP ALA ILE GLY PRO HIS ASP HIS          
SEQRES   9 A  458  ILE LEU ARG VAL VAL GLU TYR THR VAL SER ARG LYS ASN          
SEQRES  10 A  458  PRO HIS GLN VAL ASP LEU ARG THR ALA ARG VAL PHE LEU          
SEQRES  11 A  458  GLU VAL ALA GLU LEU HIS ARG LYS HIS LEU GLY GLY GLN          
SEQRES  12 A  458  LEU LEU PHE GLY PRO ASP GLY PHE LEU TYR ILE ILE LEU          
SEQRES  13 A  458  GLY ASP GLY MET ILE THR LEU ASP ASP MET GLU GLU MET          
SEQRES  14 A  458  ASP GLY LEU SER ASP PHE THR GLY SER VAL LEU ARG LEU          
SEQRES  15 A  458  ASP VAL ASP THR ASP MET CYS ASN VAL PRO TYR SER ILE          
SEQRES  16 A  458  PRO ARG SER ASN PRO HIS PHE ASN SER THR ASN GLN PRO          
SEQRES  17 A  458  PRO GLU VAL PHE ALA HIS GLY LEU HIS ASP PRO GLY ARG          
SEQRES  18 A  458  CYS ALA VAL ASP ARG HIS PRO THR ASP ILE ASN ILE ASN          
SEQRES  19 A  458  LEU THR ILE LEU CYS SER ASP SER ASN GLY LYS ASN ARG          
SEQRES  20 A  458  SER SER ALA ARG ILE LEU GLN ILE ILE LYS GLY LYS ASP          
SEQRES  21 A  458  TYR GLU SER GLU PRO SER LEU LEU GLU PHE LYS PRO PHE          
SEQRES  22 A  458  SER ASN GLY PRO LEU VAL GLY GLY PHE VAL TYR ARG GLY          
SEQRES  23 A  458  CYS GLN SER GLU ARG LEU TYR GLY SER TYR VAL PHE GLY          
SEQRES  24 A  458  ASP ARG ASN GLY ASN PHE LEU THR LEU GLN GLN SER PRO          
SEQRES  25 A  458  VAL THR LYS GLN TRP GLN GLU LYS PRO LEU CYS LEU GLY          
SEQRES  26 A  458  THR SER GLY SER CYS ARG GLY TYR PHE SER GLY HIS ILE          
SEQRES  27 A  458  LEU GLY PHE GLY GLU ASP GLU LEU GLY GLU VAL TYR ILE          
SEQRES  28 A  458  LEU SER SER SER LYS SER MET THR GLN THR HIS ASN GLY          
SEQRES  29 A  458  LYS LEU TYR LYS ILE VAL ASP PRO LYS ARG PRO LEU MET          
SEQRES  30 A  458  PRO GLU GLU CYS ARG ALA THR VAL GLN PRO ALA GLN THR          
SEQRES  31 A  458  LEU THR SER GLU CYS SER ARG LEU CYS ARG ASN GLY TYR          
SEQRES  32 A  458  CYS THR PRO THR GLY LYS CYS CYS CYS SER PRO GLY TRP          
SEQRES  33 A  458  GLU GLY ASP PHE CYS ARG THR ALA LYS CYS GLU PRO ALA          
SEQRES  34 A  458  CYS ARG HIS GLY GLY VAL CYS VAL ARG PRO ASN LYS CYS          
SEQRES  35 A  458  LEU CYS LYS LYS GLY TYR LEU GLY PRO GLN CYS GLU GLN          
SEQRES  36 A  458  VAL ASP ARG                                                  
SEQRES   1 B  458  HIS ASN CYS PHE CYS ILE GLN GLU VAL VAL SER GLY LEU          
SEQRES   2 B  458  ARG GLN PRO VAL GLY ALA LEU HIS SER GLY ASP GLY SER          
SEQRES   3 B  458  GLN ARG LEU PHE ILE LEU GLU LYS GLU GLY TYR VAL LYS          
SEQRES   4 B  458  ILE LEU THR PRO GLU GLY GLU ILE PHE LYS GLU PRO TYR          
SEQRES   5 B  458  LEU ASP ILE HIS LYS LEU VAL GLN SER GLY ILE LYS GLY          
SEQRES   6 B  458  GLY ASP GLU ARG GLY LEU LEU SER LEU ALA PHE HIS PRO          
SEQRES   7 B  458  ASN TYR LYS LYS ASN GLY LYS LEU TYR VAL SER TYR THR          
SEQRES   8 B  458  THR ASN GLN GLU ARG TRP ALA ILE GLY PRO HIS ASP HIS          
SEQRES   9 B  458  ILE LEU ARG VAL VAL GLU TYR THR VAL SER ARG LYS ASN          
SEQRES  10 B  458  PRO HIS GLN VAL ASP LEU ARG THR ALA ARG VAL PHE LEU          
SEQRES  11 B  458  GLU VAL ALA GLU LEU HIS ARG LYS HIS LEU GLY GLY GLN          
SEQRES  12 B  458  LEU LEU PHE GLY PRO ASP GLY PHE LEU TYR ILE ILE LEU          
SEQRES  13 B  458  GLY ASP GLY MET ILE THR LEU ASP ASP MET GLU GLU MET          
SEQRES  14 B  458  ASP GLY LEU SER ASP PHE THR GLY SER VAL LEU ARG LEU          
SEQRES  15 B  458  ASP VAL ASP THR ASP MET CYS ASN VAL PRO TYR SER ILE          
SEQRES  16 B  458  PRO ARG SER ASN PRO HIS PHE ASN SER THR ASN GLN PRO          
SEQRES  17 B  458  PRO GLU VAL PHE ALA HIS GLY LEU HIS ASP PRO GLY ARG          
SEQRES  18 B  458  CYS ALA VAL ASP ARG HIS PRO THR ASP ILE ASN ILE ASN          
SEQRES  19 B  458  LEU THR ILE LEU CYS SER ASP SER ASN GLY LYS ASN ARG          
SEQRES  20 B  458  SER SER ALA ARG ILE LEU GLN ILE ILE LYS GLY LYS ASP          
SEQRES  21 B  458  TYR GLU SER GLU PRO SER LEU LEU GLU PHE LYS PRO PHE          
SEQRES  22 B  458  SER ASN GLY PRO LEU VAL GLY GLY PHE VAL TYR ARG GLY          
SEQRES  23 B  458  CYS GLN SER GLU ARG LEU TYR GLY SER TYR VAL PHE GLY          
SEQRES  24 B  458  ASP ARG ASN GLY ASN PHE LEU THR LEU GLN GLN SER PRO          
SEQRES  25 B  458  VAL THR LYS GLN TRP GLN GLU LYS PRO LEU CYS LEU GLY          
SEQRES  26 B  458  THR SER GLY SER CYS ARG GLY TYR PHE SER GLY HIS ILE          
SEQRES  27 B  458  LEU GLY PHE GLY GLU ASP GLU LEU GLY GLU VAL TYR ILE          
SEQRES  28 B  458  LEU SER SER SER LYS SER MET THR GLN THR HIS ASN GLY          
SEQRES  29 B  458  LYS LEU TYR LYS ILE VAL ASP PRO LYS ARG PRO LEU MET          
SEQRES  30 B  458  PRO GLU GLU CYS ARG ALA THR VAL GLN PRO ALA GLN THR          
SEQRES  31 B  458  LEU THR SER GLU CYS SER ARG LEU CYS ARG ASN GLY TYR          
SEQRES  32 B  458  CYS THR PRO THR GLY LYS CYS CYS CYS SER PRO GLY TRP          
SEQRES  33 B  458  GLU GLY ASP PHE CYS ARG THR ALA LYS CYS GLU PRO ALA          
SEQRES  34 B  458  CYS ARG HIS GLY GLY VAL CYS VAL ARG PRO ASN LYS CYS          
SEQRES  35 B  458  LEU CYS LYS LYS GLY TYR LEU GLY PRO GLN CYS GLU GLN          
SEQRES  36 B  458  VAL ASP ARG                                                  
HET     NA  B1671       1                                                       
HET     NA  A1672       1                                                       
HET     NA  A1673       1                                                       
HET     CL  A1674       1                                                       
HET     CL  B1672       1                                                       
HET     CL  B1673       1                                                       
HETNAM      NA SODIUM ION                                                       
HETNAM      CL CHLORIDE ION                                                     
FORMUL   3   CL    3(CL 1-)                                                     
FORMUL   4   NA    3(NA 1+)                                                     
FORMUL   5  HOH   *38(H2 O1)                                                    
HELIX    1   1 ASN A  292  GLY A  297  1                                   6    
HELIX    2   2 THR A  375  GLU A  381  1                                   7    
HELIX    3   3 SER A  568  THR A  574  1                                   7    
HELIX    4   4 PRO A  591  ARG A  595  5                                   5    
HELIX    5   5 SER A  606  CYS A  612  1                                   7    
HELIX    6   6 ASN B  292  GLY B  297  1                                   6    
HELIX    7   7 THR B  375  GLU B  381  1                                   7    
HELIX    8   8 SER B  568  THR B  574  1                                   7    
HELIX    9   9 PRO B  591  ARG B  595  5                                   5    
HELIX   10  10 SER B  606  CYS B  612  1                                   7    
SHEET    1  AA 4 CYS A 218  LEU A 226  0                                        
SHEET    2  AA 4 GLY A 577  VAL A 583 -1  O  GLY A 577   N  LEU A 226           
SHEET    3  AA 4 VAL A 562  SER A 567 -1  O  VAL A 562   N  ILE A 582           
SHEET    4  AA 4 HIS A 550  GLU A 556 -1  O  HIS A 550   N  SER A 567           
SHEET    1  AB 4 PRO A 229  LEU A 233  0                                        
SHEET    2  AB 4 LEU A 242  GLU A 246 -1  O  PHE A 243   N  LEU A 233           
SHEET    3  AB 4 TYR A 250  LEU A 254 -1  O  TYR A 250   N  GLU A 246           
SHEET    4  AB 4 LEU A 266  ASP A 267 -1  O  LEU A 266   N  VAL A 251           
SHEET    1  AC 4 LEU A 284  PHE A 289  0                                        
SHEET    2  AC 4 LYS A 298  THR A 305 -1  O  TYR A 300   N  ALA A 288           
SHEET    3  AC 4 HIS A 317  VAL A 326 -1  O  ILE A 318   N  THR A 305           
SHEET    4  AC 4 VAL A 334  GLU A 347 -1  N  ASP A 335   O  THR A 325           
SHEET    1  AD 4 GLY A 354  PHE A 359  0                                        
SHEET    2  AD 4 LEU A 365  LEU A 369 -1  O  TYR A 366   N  LEU A 358           
SHEET    3  AD 4 SER A 391  LEU A 395 -1  O  SER A 391   N  LEU A 369           
SHEET    4  AD 4 VAL A 424  HIS A 427 -1  N  PHE A 425   O  VAL A 392           
SHEET    1  AE 3 ALA A 436  ASP A 438  0                                        
SHEET    2  AE 3 LEU A 448  ASP A 454 -1  O  THR A 449   N  ASP A 438           
SHEET    3  AE 3 SER A 462  ILE A 468 -1  O  SER A 462   N  ASP A 454           
SHEET    1  AF 4 LEU A 491  VAL A 496  0                                        
SHEET    2  AF 4 TYR A 509  ASP A 513 -1  O  VAL A 510   N  PHE A 495           
SHEET    3  AF 4 PHE A 518  GLN A 523 -1  O  LEU A 519   N  PHE A 511           
SHEET    4  AF 4 TRP A 530  LEU A 535 -1  O  GLN A 531   N  GLN A 522           
SHEET    1  AG 2 GLY A 615  CYS A 617  0                                        
SHEET    2  AG 2 CYS A 623  CYS A 625 -1  O  CYS A 624   N  TYR A 616           
SHEET    1  AH 2 TRP A 629  GLU A 630  0                                        
SHEET    2  AH 2 THR A 636  ALA A 637 -1  O  THR A 636   N  GLU A 630           
SHEET    1  AI 2 VAL A 648  ARG A 651  0                                        
SHEET    2  AI 2 LYS A 654  LEU A 656 -1  O  LYS A 654   N  VAL A 650           
SHEET    1  AJ 2 TYR A 661  LEU A 662  0                                        
SHEET    2  AJ 2 GLN A 668  VAL A 669 -1  O  GLN A 668   N  LEU A 662           
SHEET    1  BA 4 CYS B 218  LEU B 226  0                                        
SHEET    2  BA 4 GLY B 577  VAL B 583 -1  O  GLY B 577   N  LEU B 226           
SHEET    3  BA 4 VAL B 562  SER B 567 -1  O  VAL B 562   N  ILE B 582           
SHEET    4  BA 4 HIS B 550  GLU B 556 -1  O  HIS B 550   N  SER B 567           
SHEET    1  BB 4 PRO B 229  LEU B 233  0                                        
SHEET    2  BB 4 LEU B 242  GLU B 246 -1  O  PHE B 243   N  LEU B 233           
SHEET    3  BB 4 TYR B 250  LEU B 254 -1  O  TYR B 250   N  GLU B 246           
SHEET    4  BB 4 LEU B 266  ASP B 267 -1  O  LEU B 266   N  VAL B 251           
SHEET    1  BC 4 LEU B 284  PHE B 289  0                                        
SHEET    2  BC 4 LYS B 298  THR B 305 -1  O  TYR B 300   N  ALA B 288           
SHEET    3  BC 4 HIS B 317  VAL B 326 -1  O  ILE B 318   N  THR B 305           
SHEET    4  BC 4 VAL B 334  GLU B 347 -1  N  ASP B 335   O  THR B 325           
SHEET    1  BD 4 GLY B 354  PHE B 359  0                                        
SHEET    2  BD 4 LEU B 365  LEU B 369 -1  O  TYR B 366   N  LEU B 358           
SHEET    3  BD 4 SER B 391  LEU B 395 -1  O  SER B 391   N  LEU B 369           
SHEET    4  BD 4 VAL B 424  HIS B 427 -1  N  PHE B 425   O  VAL B 392           
SHEET    1  BE 3 ALA B 436  ASP B 438  0                                        
SHEET    2  BE 3 THR B 449  ASP B 454 -1  O  THR B 449   N  ASP B 438           
SHEET    3  BE 3 SER B 462  ARG B 464 -1  O  SER B 462   N  ASP B 454           
SHEET    1  BF 4 LEU B 491  VAL B 496  0                                        
SHEET    2  BF 4 TYR B 509  ASP B 513 -1  O  VAL B 510   N  PHE B 495           
SHEET    3  BF 4 PHE B 518  GLN B 522 -1  O  LEU B 519   N  PHE B 511           
SHEET    4  BF 4 GLN B 531  LEU B 535 -1  O  GLN B 531   N  GLN B 522           
SHEET    1  BG 2 GLY B 615  CYS B 617  0                                        
SHEET    2  BG 2 CYS B 623  CYS B 625 -1  O  CYS B 624   N  TYR B 616           
SHEET    1  BH 2 TRP B 629  GLU B 630  0                                        
SHEET    2  BH 2 THR B 636  ALA B 637 -1  O  THR B 636   N  GLU B 630           
SHEET    1  BI 2 CYS B 649  ARG B 651  0                                        
SHEET    2  BI 2 LYS B 654  CYS B 655 -1  O  LYS B 654   N  VAL B 650           
SHEET    1  BJ 2 TYR B 661  LEU B 662  0                                        
SHEET    2  BJ 2 GLN B 668  VAL B 669 -1  O  GLN B 668   N  LEU B 662           
SSBOND   1 CYS A  216    CYS A  536                          1555   1555  2.05  
SSBOND   2 CYS A  218    CYS A  543                          1555   1555  2.06  
SSBOND   3 CYS A  402    CYS A  624                          1555   1555  2.05  
SSBOND   4 CYS A  435    CYS A  452                          1555   1555  2.03  
SSBOND   5 CYS A  500    CYS A  594                          1555   1555  2.03  
SSBOND   6 CYS A  608    CYS A  617                          1555   1555  2.05  
SSBOND   7 CYS A  612    CYS A  623                          1555   1555  2.03  
SSBOND   8 CYS A  625    CYS A  634                          1555   1555  2.05  
SSBOND   9 CYS A  639    CYS A  649                          1555   1555  2.04  
SSBOND  10 CYS A  643    CYS A  655                          1555   1555  2.05  
SSBOND  11 CYS A  657    CYS A  666                          1555   1555  2.04  
SSBOND  12 CYS B  216    CYS B  536                          1555   1555  2.06  
SSBOND  13 CYS B  218    CYS B  543                          1555   1555  2.08  
SSBOND  14 CYS B  402    CYS B  624                          1555   1555  2.04  
SSBOND  15 CYS B  435    CYS B  452                          1555   1555  2.03  
SSBOND  16 CYS B  500    CYS B  594                          1555   1555  2.03  
SSBOND  17 CYS B  608    CYS B  617                          1555   1555  2.04  
SSBOND  18 CYS B  612    CYS B  623                          1555   1555  2.04  
SSBOND  19 CYS B  625    CYS B  634                          1555   1555  2.03  
SSBOND  20 CYS B  639    CYS B  649                          1555   1555  2.05  
SSBOND  21 CYS B  643    CYS B  655                          1555   1555  2.06  
SSBOND  22 CYS B  657    CYS B  666                          1555   1555  2.05  
CISPEP   1 GLU A  640    PRO A  641          0         1.69                     
CISPEP   2 GLU B  640    PRO B  641          0         1.98                     
CISPEP   3 GLY B  647    VAL B  648          0        -8.85                     
SITE     1 AC1  7 HIS B 234  SER B 235  ASP B 237  SER B 239                    
SITE     2 AC1  7 GLN B 240  ARG B 241  GLU B 558                               
SITE     1 AC2  6 SER A 235  ASP A 237  SER A 239  GLN A 240                    
SITE     2 AC2  6 ARG A 241  GLU A 558                                          
SITE     1 AC3  2 HIS A 440  ASP A 443                                          
SITE     1 AC4  4 HIS A 440  PRO A 441  THR A 442  ASP A 443                    
SITE     1 AC5  3 ARG B 434  VAL B 437  VAL B 496                               
SITE     1 AC6  4 GLY B 631  ASP B 632  PHE B 633  ARG B 635                    
CRYST1  100.976  100.976  305.916  90.00  90.00 120.00 P 31 2 1     12          
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      0.009903  0.005718  0.000000        0.00000                         
SCALE2      0.000000  0.011435  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003269        0.00000                         
MTRIX1   1 -0.601700 -0.793100 -0.094950      160.80000    1                    
MTRIX2   1 -0.787500  0.569200  0.236300       44.49000    1                    
MTRIX3   1 -0.133400  0.217000 -0.967000      252.10000    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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