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Database: PDB
Entry: 2WFX
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HEADER    SIGNALING PROTEIN                       15-APR-09   2WFX              
TITLE     CRYSTAL STRUCTURE OF THE COMPLEX BETWEEN HUMAN HEDGEHOG-              
TITLE    2 INTERACTING PROTEIN HIP AND SONIC HEDGEHOG IN THE PRESENCE           
TITLE    3 OF CALCIUM                                                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SONIC HEDGEHOG PROTEIN N-PRODUCT;                          
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: N-TERMINAL SIGNALLING DOMAIN OF SHH, RESIDUES              
COMPND   5  40-191;                                                             
COMPND   6 SYNONYM: SONIC HEDGEHOG SHH, SONIC HEDGEHOG PROTEIN,                 
COMPND   7  HHG-1, SHH;                                                         
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MOL_ID: 2;                                                           
COMPND  10 MOLECULE: HEDGEHOG-INTERACTING PROTEIN;                              
COMPND  11 CHAIN: B;                                                            
COMPND  12 FRAGMENT: C-TERMINAL DOMAIN OF HIP, RESIDUES 214-670;                
COMPND  13 SYNONYM: HHIP, HIP, HEDGEHOG-INTERACTING PROTEIN HIP;                
COMPND  14 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE   3 ORGANISM_COMMON: MOUSE;                                              
SOURCE   4 ORGANISM_TAXID: 10090;                                               
SOURCE   5 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE   6 EXPRESSION_SYSTEM_COMMON: HUMAN;                                     
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE   8 EXPRESSION_SYSTEM_CELL_LINE: HUMAN EMBRYONIC KIDNEY (HEK)            
SOURCE   9  293T CELLS;                                                         
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PHLSEC;                                   
SOURCE  11 OTHER_DETAILS: IMAGE CLONE;                                          
SOURCE  12 MOL_ID: 2;                                                           
SOURCE  13 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  14 ORGANISM_COMMON: HUMAN;                                              
SOURCE  15 ORGANISM_TAXID: 9606;                                                
SOURCE  16 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE  17 EXPRESSION_SYSTEM_COMMON: HUMAN;                                     
SOURCE  18 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE  19 EXPRESSION_SYSTEM_CELL_LINE: HUMAN EMBRYONIC KIDNEY (HEK)            
SOURCE  20  293T CELLS;                                                         
SOURCE  21 EXPRESSION_SYSTEM_PLASMID: PHLSEC;                                   
SOURCE  22 OTHER_DETAILS: IMAGE CLONE                                           
KEYWDS    SIGNALING PROTEIN, AUTOCATALYTIC CLEAVAGE, PROTEASE,                  
KEYWDS   2 MEMBRANE, SECRETED, PALMITATE, HYDROLASE, SIGNAL                     
KEYWDS   3 TRANSDUCTION, DEVELOPMENTAL PROTEIN, LIPOPROTEIN,                    
KEYWDS   4 DEVELOPMENT, GLYCOPROTEIN, CELL MEMBRANE, DISULFIDE BOND,            
KEYWDS   5 EGF-LIKE DOMAIN, HEDGEHOG SIGNALING                                  
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 2WFX    1       JRNL                                     
REVDAT   1   30-JUN-09 2WFX    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.    3.20 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) : 3.200                          
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.774                         
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.33                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.04                          
REMARK   3   NUMBER OF REFLECTIONS             : 13372                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.2448                          
REMARK   3   R VALUE            (WORKING SET) : 0.2400                          
REMARK   3   FREE R VALUE                     : 0.3003                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%) :  7.9                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 1056                            
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 19.7739 -  6.3381    1.00     1634   151  0.2674 0.3053        
REMARK   3     2  6.3381 -  5.0585    1.00     1576   145  0.1969 0.2406        
REMARK   3     3  5.0585 -  4.4272    1.00     1547   128  0.1607 0.2254        
REMARK   3     4  4.4272 -  4.0262    1.00     1575   109  0.1814 0.2167        
REMARK   3     5  4.0262 -  3.7397    0.98     1509   118  0.2418 0.3412        
REMARK   3     6  3.7397 -  3.5205    0.95     1448   135  0.3012 0.3834        
REMARK   3     7  3.5205 -  3.3451    1.00     1508   138  0.2856 0.3727        
REMARK   3     8  3.3451 -  3.2001    1.00     1519   132  0.3272 0.3853        
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              : 0.248                                         
REMARK   3   B_SOL              : 7.909                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.48             
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 32.48            
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 60.28                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 12.8101                                              
REMARK   3    B22 (A**2) : 12.8101                                              
REMARK   3    B33 (A**2) : -25.6202                                             
REMARK   3    B12 (A**2) : 0.0000                                               
REMARK   3    B13 (A**2) : -0.0000                                              
REMARK   3    B23 (A**2) : 0.0000                                               
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      :  0.004           4592                                  
REMARK   3   ANGLE     :  0.524           6166                                  
REMARK   3   CHIRALITY :  0.032            667                                  
REMARK   3   PLANARITY :  0.002            810                                  
REMARK   3   DIHEDRAL  : 13.433           1680                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 9                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 40:50)                              
REMARK   3    ORIGIN FOR THE GROUP (A): -15.5353  22.8480   0.3450              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5297 T22:   1.0370                                     
REMARK   3      T33:   0.6838 T12:  -0.1245                                     
REMARK   3      T13:  -0.1163 T23:  -0.2138                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  -2.4294 L22:   4.9135                                     
REMARK   3      L33:   2.1742 L12:  -3.1334                                     
REMARK   3      L13:   4.7320 L23:   1.6174                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0499 S12:  -0.8210 S13:  -1.2316                       
REMARK   3      S21:   0.4665 S22:   1.4941 S23:  -0.7643                       
REMARK   3      S31:  -0.0026 S32:  -0.2846 S33:  -1.1499                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 51:77)                              
REMARK   3    ORIGIN FOR THE GROUP (A): -11.8330  34.0435 -19.9891              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8607 T22:   1.0365                                     
REMARK   3      T33:   0.4562 T12:   0.0941                                     
REMARK   3      T13:  -0.0032 T23:  -0.0106                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.1371 L22:   7.5743                                     
REMARK   3      L33:  -4.9182 L12:  -1.8838                                     
REMARK   3      L13:  -0.4953 L23:   1.6011                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.5495 S12:   1.0968 S13:   0.1377                       
REMARK   3      S21:  -1.5653 S22:  -0.4481 S23:  -0.2300                       
REMARK   3      S31:   0.0118 S32:  -0.2764 S33:  -0.0682                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 78:129)                             
REMARK   3    ORIGIN FOR THE GROUP (A): -26.3295  36.9906  -9.4577              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5165 T22:   0.9748                                     
REMARK   3      T33:   0.5970 T12:   0.0075                                     
REMARK   3      T13:  -0.0886 T23:   0.0304                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3094 L22:   1.4462                                     
REMARK   3      L33:   2.6502 L12:  -0.4983                                     
REMARK   3      L13:  -0.7001 L23:   0.5389                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2247 S12:   1.1195 S13:  -0.1708                       
REMARK   3      S21:  -0.3408 S22:  -0.1539 S23:   0.4019                       
REMARK   3      S31:  -0.1673 S32:  -1.1965 S33:  -0.1407                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 130:188)                            
REMARK   3    ORIGIN FOR THE GROUP (A): -16.9924  32.7139  -5.8563              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2992 T22:   0.7566                                     
REMARK   3      T33:   0.4464 T12:   0.0356                                     
REMARK   3      T13:  -0.0703 T23:  -0.1785                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1435 L22:   0.0843                                     
REMARK   3      L33:   1.3815 L12:   0.2477                                     
REMARK   3      L13:   1.2833 L23:  -0.5812                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2039 S12:   0.2014 S13:   0.1094                       
REMARK   3      S21:   0.0043 S22:   0.3389 S23:   0.0046                       
REMARK   3      S31:   0.1828 S32:  -0.7050 S33:  -0.1783                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: (CHAIN B AND RESID 215:276)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  20.1565  45.0919  17.4177              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3652 T22:   0.7194                                     
REMARK   3      T33:   0.5277 T12:  -0.0163                                     
REMARK   3      T13:  -0.0330 T23:  -0.0506                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5604 L22:   0.1235                                     
REMARK   3      L33:   0.4431 L12:  -0.7924                                     
REMARK   3      L13:  -0.1874 L23:   0.4841                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0197 S12:   0.4995 S13:   0.3204                       
REMARK   3      S21:  -0.0475 S22:  -0.0054 S23:  -0.1371                       
REMARK   3      S31:  -0.0953 S32:   0.4436 S33:  -0.0138                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: (CHAIN B AND RESID 277:442)                            
REMARK   3    ORIGIN FOR THE GROUP (A):   3.0018  34.6198  12.6870              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2723 T22:   0.7624                                     
REMARK   3      T33:   0.3937 T12:   0.0659                                     
REMARK   3      T13:  -0.0213 T23:  -0.0981                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  -0.0457 L22:   1.3461                                     
REMARK   3      L33:   1.1187 L12:  -0.3737                                     
REMARK   3      L13:   0.4248 L23:  -0.3078                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0491 S12:   0.2367 S13:  -0.1060                       
REMARK   3      S21:   0.0121 S22:  -0.0761 S23:   0.0342                       
REMARK   3      S31:   0.0209 S32:  -0.0927 S33:   0.0906                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: (CHAIN B AND RESID 443:530)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  -2.1887  44.9735  30.0318              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1597 T22:   0.7029                                     
REMARK   3      T33:   0.4017 T12:   0.1170                                     
REMARK   3      T13:   0.0120 T23:  -0.1089                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7905 L22:   1.2980                                     
REMARK   3      L33:   1.0919 L12:   0.7218                                     
REMARK   3      L13:   0.3897 L23:   0.0143                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0249 S12:  -0.5464 S13:   0.2577                       
REMARK   3      S21:   0.1862 S22:  -0.0851 S23:   0.3193                       
REMARK   3      S31:   0.0958 S32:  -0.3845 S33:   0.0153                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: (CHAIN B AND RESID 531:637)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  17.2663  35.2201  22.3916              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2732 T22:   0.7627                                     
REMARK   3      T33:   0.3600 T12:   0.1215                                     
REMARK   3      T13:   0.0217 T23:  -0.0559                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2024 L22:   1.2333                                     
REMARK   3      L33:  -0.0351 L12:  -0.1183                                     
REMARK   3      L13:  -0.1388 L23:  -0.0028                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2409 S12:  -0.2881 S13:   0.1975                       
REMARK   3      S21:  -0.1675 S22:  -0.1381 S23:  -0.5438                       
REMARK   3      S31:   0.0483 S32:   0.0114 S33:  -0.1052                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: (CHAIN B AND RESID 638:666)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  15.4861  -1.5974  -6.2923              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.6644 T22:   1.5525                                     
REMARK   3      T33:   1.2350 T12:   0.5014                                     
REMARK   3      T13:  -0.2514 T23:  -0.1946                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.3785 L22:   3.5831                                     
REMARK   3      L33:   1.8269 L12:  -0.2190                                     
REMARK   3      L13:   2.6373 L23:  -0.9309                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3035 S12:   0.1657 S13:   1.0410                       
REMARK   3      S21:  -1.0186 S22:  -0.9270 S23:  -0.1415                       
REMARK   3      S31:   0.6768 S32:  -0.1210 S33:   0.5289                       
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 2WFX 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-39471.                                       
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   : 13529                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.20                               
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     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 6.5                                
REMARK 200  R MERGE                    (I) : 0.19                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.60                              
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.30                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.7                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.73                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.50                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRIES 1VHH AND 2WFT                            
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 67                                        
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA):3.14                      
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M SODIUM ACETATE, PH 4.6             
REMARK 280  0.5 M POTASSIUM THIOCYANATE 5 MM CACL                               
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 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+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+1/3                                           
REMARK 290       6555   -X,-X+Y,-Z+2/3                                          
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      114.28600            
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       57.14300            
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       57.14300            
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      114.28600            
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 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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2360 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 26460 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -90.88 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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     HIS B   279                                                      
REMARK 465     GLY B   279                                                      
REMARK 465     GLN B   308                                                      
REMARK 465     GLU B   309                                                      
REMARK 465     ARG B   310                                                      
REMARK 465     TRP B   311                                                      
REMARK 465     ALA B   312                                                      
REMARK 465     ILE B   313                                                      
REMARK 465     GLY B   314                                                      
REMARK 465     PRO B   315                                                      
REMARK 465     GLY B   458                                                      
REMARK 465     LYS B   459                                                      
REMARK 465     GLY B   539                                                      
REMARK 465     THR B   540                                                      
REMARK 465     SER B   541                                                      
REMARK 465     GLY B   542                                                      
REMARK 465     SER B   543                                                      
REMARK 465     CYS B   544                                                      
REMARK 465     ARG B   545                                                      
REMARK 465     GLY B   546                                                      
REMARK 465     TYR B   547                                                      
REMARK 465     PHE B   548                                                      
REMARK 465     SER B   549                                                      
REMARK 465     SER B   569                                                      
REMARK 465     LYS B   570                                                      
REMARK 465     SER B   571                                                      
REMARK 465     MET B   572                                                      
REMARK 465     THR B   573                                                      
REMARK 465     LYS B   659                                                      
REMARK 465     LYS B   660                                                      
REMARK 465     GLN B   669                                                      
REMARK 465     VAL B   670                                                      
REMARK 465     ASP B   671                                                      
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     GLU A 189    CG   CD   OE1  OE2                                  
REMARK 470     SER A 191    OG                                                  
REMARK 470     LYS B 277    CG   CD   CE   NZ                                   
REMARK 470     ARG B 460    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B 651    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     TYR B 661    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     GLU B 667    CA   C    O    CB   CG   CD   OE1  OE2              
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    LYS A  55       54.04   -104.95                                   
REMARK 500    ALA A  59     -129.10   -103.31                                   
REMARK 500    ASN A  92       -5.10     69.41                                   
REMARK 500    ASP A 132     -172.96    152.33                                   
REMARK 500    HIS A 134      -13.83    171.90                                   
REMARK 500    GLU A 137      152.21    -41.22                                   
REMARK 500    ARG A 154       -3.72     63.23                                   
REMARK 500    ASP A 155      104.80    -57.88                                   
REMARK 500    TRP A 173      108.18   -169.59                                   
REMARK 500    GLU A 177      -72.29    -45.50                                   
REMARK 500    GLN B 240       27.84     49.95                                   
REMARK 500    ILE B 268       30.52   -141.35                                   
REMARK 500    SER B 274     -114.31    -74.56                                   
REMARK 500    LEU B 285      -64.24    -92.92                                   
REMARK 500    ARG B 350       41.97   -108.44                                   
REMARK 500    ASP B 400       38.05    -94.11                                   
REMARK 500    THR B 418       49.72   -109.06                                   
REMARK 500    ASN B 419      -16.73   -157.46                                   
REMARK 500    HIS B 430      -82.35   -132.63                                   
REMARK 500    ASP B 431       73.95   -117.23                                   
REMARK 500    SER B 462     -140.52   -115.75                                   
REMARK 500    ALA B 463      110.62   -174.03                                   
REMARK 500    SER B 487      -72.66    -46.71                                   
REMARK 500    GLN B 523     -153.22   -103.98                                   
REMARK 500    THR B 527      -26.71     67.05                                   
REMARK 500    ASN B 576        9.64   -159.08                                   
REMARK 500    MET B 590       80.71   -151.94                                   
REMARK 500    ALA B 596      108.56   -166.11                                   
REMARK 500    LEU B 611       48.69   -142.65                                   
REMARK 500    ARG B 644      -97.91    -93.07                                   
REMARK 500    VAL B 650      -89.51   -128.51                                   
REMARK 500    PRO B 652      105.49    -41.82                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620  (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;              
REMARK 620   SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA B1668  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 TYR B 474   O                                                      
REMARK 620 2 GLU B 475   OE1  66.4                                              
REMARK 620 3 ARG B 410   O   126.7 150.3                                        
REMARK 620 4 ASN B 412   O    70.9 124.2  84.8                                  
REMARK 620 5 ASP B 473   OD1  84.7  90.8  66.8 119.3                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA B1669  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ILE B 446   O                                                      
REMARK 620 2 PRO B 441   O   114.7                                              
REMARK 620 3 ASP B 443   O    75.8  83.3                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A1193  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  96   OD1                                                    
REMARK 620 2 ASP A  96   OD2  50.2                                              
REMARK 620 3 THR A 126   O   101.1  74.3                                        
REMARK 620 4 GLU A  90   OE2 150.1 144.6 108.2                                  
REMARK 620 5 GLU A  91   OE1  78.5 118.4 158.7  72.2                            
REMARK 620 6 GLU A  91   OE2  68.2  78.8 151.0  88.0  48.6                      
REMARK 620 7 GLU A  90   OE1 140.8  94.7  81.3  52.4 112.7  90.8                
REMARK 620 8 GLU A 127   OE1  98.6 133.4  81.3  80.6  77.7 125.9 120.2          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A1194  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A  91   OE1                                                    
REMARK 620 2 GLU A 127   OE2  96.5                                              
REMARK 620 3 ASP A 130   OD1 153.3  89.1                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A1192  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 141   NE2                                                    
REMARK 620 2 ASP A 148   OD1  97.5                                              
REMARK 620 3 HIS A 183   ND1  96.0  94.2                                        
REMARK 620 4 ASP B 383   OD1  87.1 128.0 137.1                                  
REMARK 620 5 ASP B 383   OD2 147.5  91.7 114.4  63.2                            
REMARK 620 N                    1     2     3     4                             
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN A1192                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA A1193                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA A1194                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  NA B1667                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  NA B1668                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  NA B1669                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA B1670                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2WFT   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE HUMAN HIP                                  
REMARK 900  ECTODOMAIN                                                          
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: 1VHH   RELATED DB: PDB                                   
REMARK 900  MOL_ID: 1; MOLECULE: SONIC HEDGEHOG; CHAIN:                         
REMARK 900  NULL; DOMAIN: AMINO-TERMINAL DOMAIN (RESIDUES                       
REMARK 900   34 - 195); SYNONYM: HHG-1, VHH-1;                                  
REMARK 900  ENGINEERED: YES                                                     
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: 2WGR   RELATED DB: PDB                                   
REMARK 900  COMBINING CRYSTALLOGRAPHY AND MOLECULAR DYNAMICS                    
REMARK 900  : THE CASE OF SCHISTOSOMA MANSONI                                   
REMARK 900  PHOSPHOLIPID GLUTATHIONE PEROXIDASE                                 
REMARK 900 RELATED ID: 2WGQ   RELATED DB: PDB                                   
REMARK 900  ZINC SUBSTITUTED E COLI COPPER AMINE OXIDASE                        
REMARK 900  , A MODEL FOR THE PRECURSOR FOR 2,4,5-                              
REMARK 900  TRIHYDROXYPHENYLALANINEQUINONE FORMATION                            
DBREF  2WFX A   40   191  UNP    Q62226   SHH_MOUSE       40    191             
DBREF  2WFX B  214   670  UNP    Q96QV1   HHIP_HUMAN     214    670             
SEQRES   1 A  152  LEU THR PRO LEU ALA TYR LYS GLN PHE ILE PRO ASN VAL          
SEQRES   2 A  152  ALA GLU LYS THR LEU GLY ALA SER GLY ARG TYR GLU GLY          
SEQRES   3 A  152  LYS ILE THR ARG ASN SER GLU ARG PHE LYS GLU LEU THR          
SEQRES   4 A  152  PRO ASN TYR ASN PRO ASP ILE ILE PHE LYS ASP GLU GLU          
SEQRES   5 A  152  ASN THR GLY ALA ASP ARG LEU MET THR GLN ARG CYS LYS          
SEQRES   6 A  152  ASP LYS LEU ASN ALA LEU ALA ILE SER VAL MET ASN GLN          
SEQRES   7 A  152  TRP PRO GLY VAL LYS LEU ARG VAL THR GLU GLY TRP ASP          
SEQRES   8 A  152  GLU ASP GLY HIS HIS SER GLU GLU SER LEU HIS TYR GLU          
SEQRES   9 A  152  GLY ARG ALA VAL ASP ILE THR THR SER ASP ARG ASP ARG          
SEQRES  10 A  152  SER LYS TYR GLY MET LEU ALA ARG LEU ALA VAL GLU ALA          
SEQRES  11 A  152  GLY PHE ASP TRP VAL TYR TYR GLU SER LYS ALA HIS ILE          
SEQRES  12 A  152  HIS CYS SER VAL LYS ALA GLU ASN SER                          
SEQRES   1 B  457  HIS ASN CYS PHE CYS ILE GLN GLU VAL VAL SER GLY LEU          
SEQRES   2 B  457  ARG GLN PRO VAL GLY ALA LEU HIS SER GLY ASP GLY SER          
SEQRES   3 B  457  GLN ARG LEU PHE ILE LEU GLU LYS GLU GLY TYR VAL LYS          
SEQRES   4 B  457  ILE LEU THR PRO GLU GLY GLU ILE PHE LYS GLU PRO TYR          
SEQRES   5 B  457  LEU ASP ILE HIS LYS LEU VAL GLN SER GLY ILE LYS GLY          
SEQRES   6 B  457  GLY ASP GLU ARG GLY LEU LEU SER LEU ALA PHE HIS PRO          
SEQRES   7 B  457  ASN TYR LYS LYS ASN GLY LYS LEU TYR VAL SER TYR THR          
SEQRES   8 B  457  THR ASN GLN GLU ARG TRP ALA ILE GLY PRO HIS ASP HIS          
SEQRES   9 B  457  ILE LEU ARG VAL VAL GLU TYR THR VAL SER ARG LYS ASN          
SEQRES  10 B  457  PRO HIS GLN VAL ASP LEU ARG THR ALA ARG VAL PHE LEU          
SEQRES  11 B  457  GLU VAL ALA GLU LEU HIS ARG LYS HIS LEU GLY GLY GLN          
SEQRES  12 B  457  LEU LEU PHE GLY PRO ASP GLY PHE LEU TYR ILE ILE LEU          
SEQRES  13 B  457  GLY ASP GLY MET ILE THR LEU ASP ASP MET GLU GLU MET          
SEQRES  14 B  457  ASP GLY LEU SER ASP PHE THR GLY SER VAL LEU ARG LEU          
SEQRES  15 B  457  ASP VAL ASP THR ASP MET CYS ASN VAL PRO TYR SER ILE          
SEQRES  16 B  457  PRO ARG SER ASN PRO HIS PHE ASN SER THR ASN GLN PRO          
SEQRES  17 B  457  PRO GLU VAL PHE ALA HIS GLY LEU HIS ASP PRO GLY ARG          
SEQRES  18 B  457  CYS ALA VAL ASP ARG HIS PRO THR ASP ILE ASN ILE ASN          
SEQRES  19 B  457  LEU THR ILE LEU CYS SER ASP SER ASN GLY LYS ASN ARG          
SEQRES  20 B  457  SER SER ALA ARG ILE LEU GLN ILE ILE LYS GLY LYS ASP          
SEQRES  21 B  457  TYR GLU SER GLU PRO SER LEU LEU GLU PHE LYS PRO PHE          
SEQRES  22 B  457  SER ASN GLY PRO LEU VAL GLY GLY PHE VAL TYR ARG GLY          
SEQRES  23 B  457  CYS GLN SER GLU ARG LEU TYR GLY SER TYR VAL PHE GLY          
SEQRES  24 B  457  ASP ARG ASN GLY ASN PHE LEU THR LEU GLN GLN SER PRO          
SEQRES  25 B  457  VAL THR LYS GLN TRP GLN GLU LYS PRO LEU CYS LEU GLY          
SEQRES  26 B  457  THR SER GLY SER CYS ARG GLY TYR PHE SER GLY HIS ILE          
SEQRES  27 B  457  LEU GLY PHE GLY GLU ASP GLU LEU GLY GLU VAL TYR ILE          
SEQRES  28 B  457  LEU SER SER SER LYS SER MET THR GLN THR HIS ASN GLY          
SEQRES  29 B  457  LYS LEU TYR LYS ILE VAL ASP PRO LYS ARG PRO LEU MET          
SEQRES  30 B  457  PRO GLU GLU CYS ARG ALA THR VAL GLN PRO ALA GLN THR          
SEQRES  31 B  457  LEU THR SER GLU CYS SER ARG LEU CYS ARG ASN GLY TYR          
SEQRES  32 B  457  CYS THR PRO THR GLY LYS CYS CYS CYS SER PRO GLY TRP          
SEQRES  33 B  457  GLU GLY ASP PHE CYS ARG THR ALA LYS CYS GLU PRO ALA          
SEQRES  34 B  457  CYS ARG HIS GLY GLY VAL CYS VAL ARG PRO ASN LYS CYS          
SEQRES  35 B  457  LEU CYS LYS LYS GLY TYR LEU GLY PRO GLN CYS GLU GLN          
SEQRES  36 B  457  VAL ASP                                                      
HET     ZN  A1192       1                                                       
HET     CA  A1193       1                                                       
HET     CA  A1194       1                                                       
HET     NA  B1667       1                                                       
HET     NA  B1668       1                                                       
HET     NA  B1669       1                                                       
HET     CA  B1670       1                                                       
HETNAM      NA SODIUM ION                                                       
HETNAM      CA CALCIUM ION                                                      
HETNAM      ZN ZINC ION                                                         
FORMUL   3   NA    3(NA 1+)                                                     
FORMUL   4   CA    3(CA 2+)                                                     
FORMUL   5   ZN    ZN 2+                                                        
HELIX    1   1 SER A   71  LEU A   77  5                                   7    
HELIX    2   2 THR A  100  TRP A  118  1                                  19    
HELIX    3   3 ASP A  155  SER A  157  5                                   3    
HELIX    4   4 LYS A  158  GLY A  170  1                                  13    
HELIX    5   5 ASN B  292  GLY B  297  1                                   6    
HELIX    6   6 THR B  375  MET B  382  1                                   8    
HELIX    7   7 PRO B  591  ARG B  595  5                                   5    
HELIX    8   8 SER B  606  CYS B  612  1                                   7    
SHEET    1  AA 6 PHE A  48  ILE A  49  0                                        
SHEET    2  AA 6 TRP A 173  SER A 178 -1  O  VAL A 174   N  ILE A  49           
SHEET    3  AA 6 HIS A 181  SER A 185 -1  O  HIS A 181   N  SER A 178           
SHEET    4  AA 6 ALA A 146  THR A 151 -1  O  VAL A 147   N  CYS A 184           
SHEET    5  AA 6 LEU A 123  GLU A 127 -1  O  ARG A 124   N  THR A 150           
SHEET    6  AA 6 ILE A  85  PHE A  87  1  O  ILE A  86   N  VAL A 125           
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 566 -1  O  VAL B 562   N  ILE B 582           
SHEET    4  BA 4 ILE B 551  GLU B 556 -1  N  LEU B 552   O  LEU B 565           
SHEET    1  BB 4 PRO B 229  LEU B 233  0                                        
SHEET    2  BB 4 PHE B 243  GLU B 246 -1  O  PHE B 243   N  LEU B 233           
SHEET    3  BB 4 TYR B 250  LYS B 252 -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 GLN B 356  PHE B 359  0                                        
SHEET    2  BD 4 LEU B 365  ILE B 368 -1  O  TYR B 366   N  LEU B 358           
SHEET    3  BD 4 SER B 391  LEU B 395 -1  O  LEU B 393   N  ILE B 367           
SHEET    4  BD 4 VAL B 424  HIS B 427 -1  N  PHE B 425   O  VAL B 392           
SHEET    1  BE 4 ALA B 436  ASP B 438  0                                        
SHEET    2  BE 4 ILE B 446  CYS B 452 -1  O  THR B 449   N  ASP B 438           
SHEET    3  BE 4 ARG B 464  ILE B 469 -1  O  ARG B 464   N  CYS B 452           
SHEET    4  BE 4 LEU B 481  GLU B 482 -1  O  LEU B 481   N  ILE B 465           
SHEET    1  BF 4 GLY B 493  VAL B 496  0                                        
SHEET    2  BF 4 TYR B 509  GLY B 512 -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           
SSBOND   1 CYS B  216    CYS B  536                          1555   1555  2.03  
SSBOND   2 CYS B  402    CYS B  624                          1555   1555  2.03  
SSBOND   3 CYS B  435    CYS B  452                          1555   1555  2.03  
SSBOND   4 CYS B  500    CYS B  594                          1555   1555  2.03  
SSBOND   5 CYS B  608    CYS B  617                          1555   1555  2.03  
SSBOND   6 CYS B  612    CYS B  623                          1555   1555  2.03  
SSBOND   7 CYS B  625    CYS B  634                          1555   1555  2.03  
SSBOND   8 CYS B  639    CYS B  649                          1555   1555  2.03  
SSBOND   9 CYS B  643    CYS B  655                          1555   1555  2.03  
SSBOND  10 CYS B  657    CYS B  666                          1555   1555  2.03  
LINK        ZN    ZN A1192                 NE2 HIS A 141     1555   1555  2.01  
LINK        ZN    ZN A1192                 OD2 ASP B 383     1555   1555  2.07  
LINK        ZN    ZN A1192                 OD1 ASP B 383     1555   1555  2.12  
LINK        ZN    ZN A1192                 ND1 HIS A 183     1555   1555  2.00  
LINK        ZN    ZN A1192                 OD1 ASP A 148     1555   1555  2.03  
LINK        CA    CA A1193                 OD1 ASP A  96     1555   1555  2.75  
LINK        CA    CA A1193                 OD2 ASP A  96     1555   1555  2.36  
LINK        CA    CA A1193                 O   THR A 126     1555   1555  2.39  
LINK        CA    CA A1193                 OE2 GLU A  90     1555   1555  2.30  
LINK        CA    CA A1193                 OE1 GLU A  91     1555   1555  2.37  
LINK        CA    CA A1193                 OE1 GLU A 127     1555   1555  2.40  
LINK        CA    CA A1193                 OE1 GLU A  90     1555   1555  2.63  
LINK        CA    CA A1193                 OE2 GLU A  91     1555   1555  2.86  
LINK        CA    CA A1194                 OE1 GLU A  91     1555   1555  2.39  
LINK        CA    CA A1194                 OE2 GLU A 127     1555   1555  2.29  
LINK        CA    CA A1194                 OD1 ASP A 130     1555   1555  2.40  
LINK        NA    NA B1668                 OE1 GLU B 475     1555   1555  2.50  
LINK        NA    NA B1668                 O   TYR B 474     1555   1555  2.57  
LINK        NA    NA B1668                 O   ASN B 412     1555   1555  2.51  
LINK        NA    NA B1668                 O   ARG B 410     1555   1555  2.53  
LINK        NA    NA B1668                 OD1 ASP B 473     1555   1555  2.51  
LINK        NA    NA B1669                 O   ASP B 443     1555   1555  2.49  
LINK        NA    NA B1669                 O   PRO B 441     1555   1555  2.55  
LINK        NA    NA B1669                 O   ILE B 446     1555   1555  2.47  
LINK        CA    CA B1670                 O   GLY B 354     1555   1555  3.09  
CISPEP   1 ILE A   49    PRO A   50          0         0.12                     
CISPEP   2 GLY B  354    GLY B  355          0        -6.68                     
CISPEP   3 GLU B  640    PRO B  641          0         0.49                     
CISPEP   4 GLY B  646    GLY B  647          0        -0.76                     
SITE     1 AC1  4 HIS A 141  ASP A 148  HIS A 183  ASP B 383                    
SITE     1 AC2  5 GLU A  90  GLU A  91  ASP A  96  THR A 126                    
SITE     2 AC2  5 GLU A 127                                                     
SITE     1 AC3  3 GLU A  91  GLU A 127  ASP A 130                               
SITE     1 AC4  2 CYS B 623  GLY B 631                                          
SITE     1 AC5  5 ARG B 410  ASN B 412  ASP B 473  TYR B 474                    
SITE     2 AC5  5 GLU B 475                                                     
SITE     1 AC6  3 PRO B 441  ASP B 443  ILE B 446                               
SITE     1 AC7  1 GLY B 354                                                     
CRYST1   89.150   89.150  171.429  90.00  90.00 120.00 P 32 2 1      6          
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      0.011217  0.006476  0.000000        0.00000                         
SCALE2      0.000000  0.012952  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005833        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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