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Database: PDB
Entry: 2WG4
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Original site: 2WG4 
HEADER    SIGNALING PROTEIN                       15-APR-09   2WG4              
TITLE     CRYSTAL STRUCTURE OF THE COMPLEX BETWEEN HUMAN HEDGEHOG-INTERACTING   
TITLE    2 PROTEIN HIP AND SONIC HEDGEHOG WITHOUT 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 40-191;      
COMPND   5 SYNONYM: SONIC HEDGEHOG SHH, SONIC HEDGEHOG PROTEIN, HHG-1, SHH;     
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: HEDGEHOG-INTERACTING PROTEIN;                              
COMPND   9 CHAIN: B;                                                            
COMPND  10 FRAGMENT: C-TERMINAL DOMAIN OF HIP, RESIDUES 214-670;                
COMPND  11 SYNONYM: HHIP, HIP, HEDGEHOG-INTERACTING PROTEIN HIP;                
COMPND  12 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) 293T       
SOURCE   9 CELLS;                                                               
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PHLSEC;                                   
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  13 ORGANISM_COMMON: HUMAN;                                              
SOURCE  14 ORGANISM_TAXID: 9606;                                                
SOURCE  15 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE  16 EXPRESSION_SYSTEM_COMMON: HUMAN;                                     
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE  18 EXPRESSION_SYSTEM_CELL_LINE: HUMAN EMBRYONIC KIDNEY (HEK) 293T       
SOURCE  19 CELLS;                                                               
SOURCE  20 EXPRESSION_SYSTEM_PLASMID: PHLSEC                                    
KEYWDS    AUTOCATALYTIC CLEAVAGE, PROTEASE, MEMBRANE, SECRETED, PALMITATE,      
KEYWDS   2 HYDROLASE, SIGNAL TRANSDUCTION, DEVELOPMENTAL PROTEIN, SIGNALING     
KEYWDS   3 PROTEIN, LIPOPROTEIN, DEVELOPMENT, GLYCOPROTEIN, CELL MEMBRANE,      
KEYWDS   4 DISULFIDE BOND, EGF-LIKE DOMAIN, HEDGEHOG SIGNALING                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    B.BISHOP,A.R.ARICESCU,K.HARLOS,C.A.O'CALLAGHAN,E.Y.JONES,C.SIEBOLD    
REVDAT   3   08-NOV-17 2WG4    1       SOURCE                                   
REVDAT   2   21-JUL-09 2WG4    1       JRNL                                     
REVDAT   1   30-JUN-09 2WG4    0                                                
JRNL        AUTH   B.BISHOP,A.R.ARICESCU,K.HARLOS,C.A.O'CALLAGHAN,E.Y.JONES,    
JRNL        AUTH 2 C.SIEBOLD                                                    
JRNL        TITL   STRUCTURAL INSIGHTS INTO HEDGEHOG LIGAND SEQUESTRATION BY    
JRNL        TITL 2 THE HUMAN HEDGEHOG-INTERACTING 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.    3.15 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE)                               
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.15                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.84                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.900                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 53.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 13824                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.236                           
REMARK   3   R VALUE            (WORKING SET) : 0.234                           
REMARK   3   FREE R VALUE                     : 0.292                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 678                             
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 19.8426 -  5.3582    0.56     2767   124  0.2592 0.2962        
REMARK   3     2  5.3582 -  4.2669    0.54     2638   137  0.1867 0.2556        
REMARK   3     3  4.2669 -  3.7316    0.53     2623   124  0.2118 0.2621        
REMARK   3     4  3.7316 -  3.3922    0.53     2559   149  0.2469 0.3255        
REMARK   3     5  3.3922 -  3.1501    0.53     2559   144  0.2885 0.3413        
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              : 25.94                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.500            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.610           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 58.58                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 3.12370                                              
REMARK   3    B22 (A**2) : 3.12370                                              
REMARK   3    B33 (A**2) : -6.24750                                             
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      :  0.002           4571                                  
REMARK   3   ANGLE     :  0.497           6151                                  
REMARK   3   CHIRALITY :  0.035            662                                  
REMARK   3   PLANARITY :  0.002            805                                  
REMARK   3   DIHEDRAL  : 13.825           1679                                  
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):  16.1113 -21.4745   0.3391              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5249 T22:   0.6279                                     
REMARK   3      T33:   0.6035 T12:  -0.0604                                     
REMARK   3      T13:   0.0149 T23:   0.1655                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.7570 L22:   4.9871                                     
REMARK   3      L33:   6.7105 L12:   1.6584                                     
REMARK   3      L13:   3.0121 L23:  -1.8752                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4391 S12:  -0.7427 S13:   0.6681                       
REMARK   3      S21:   0.3481 S22:  -0.7234 S23:  -0.9425                       
REMARK   3      S31:  -0.2900 S32:   0.3868 S33:   0.1759                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 51:77)                              
REMARK   3    ORIGIN FOR THE GROUP (A):  11.3948 -32.5908 -19.9011              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8003 T22:   0.8644                                     
REMARK   3      T33:   0.4892 T12:  -0.0192                                     
REMARK   3      T13:   0.0328 T23:   0.1778                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1092 L22:   4.5907                                     
REMARK   3      L33:  -0.1245 L12:  -0.7545                                     
REMARK   3      L13:   0.1406 L23:   0.9588                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1527 S12:   0.3709 S13:  -0.0955                       
REMARK   3      S21:  -1.2523 S22:  -0.1130 S23:  -0.2085                       
REMARK   3      S31:  -0.3475 S32:  -0.1446 S33:  -0.0434                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 78:129)                             
REMARK   3    ORIGIN FOR THE GROUP (A):  27.2349 -34.5573  -9.9634              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4072 T22:   1.0787                                     
REMARK   3      T33:   1.0620 T12:  -0.0037                                     
REMARK   3      T13:   0.0970 T23:   0.1186                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  -2.6950 L22:   2.5246                                     
REMARK   3      L33:   2.1096 L12:  -1.2965                                     
REMARK   3      L13:  -0.5643 L23:   0.8372                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1532 S12:   0.7545 S13:  -0.0703                       
REMARK   3      S21:  -0.0577 S22:  -0.0232 S23:  -1.1118                       
REMARK   3      S31:   0.4045 S32:   0.8629 S33:  -0.0679                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 130:188)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  17.3017 -31.4994  -6.0051              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4786 T22:   0.7240                                     
REMARK   3      T33:   0.5801 T12:  -0.0417                                     
REMARK   3      T13:   0.0448 T23:   0.1745                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.5788 L22:   3.8240                                     
REMARK   3      L33:   2.3506 L12:  -1.2856                                     
REMARK   3      L13:  -0.7180 L23:   1.2506                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3452 S12:  -0.1642 S13:  -0.4456                       
REMARK   3      S21:  -0.1898 S22:   0.0536 S23:  -0.6632                       
REMARK   3      S31:   0.1468 S32:   0.5107 S33:   0.3602                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: (CHAIN B AND RESID 215:276)                            
REMARK   3    ORIGIN FOR THE GROUP (A): -19.8267 -44.3701  17.0235              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4562 T22:   0.7003                                     
REMARK   3      T33:   0.5949 T12:  -0.0448                                     
REMARK   3      T13:  -0.0060 T23:   0.1023                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7346 L22:   2.3923                                     
REMARK   3      L33:   0.7836 L12:  -0.6479                                     
REMARK   3      L13:  -0.2224 L23:  -1.6822                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1381 S12:   0.0380 S13:  -0.5800                       
REMARK   3      S21:  -0.1059 S22:  -0.0030 S23:   0.4404                       
REMARK   3      S31:   0.2460 S32:  -0.4005 S33:  -0.1529                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: (CHAIN B AND RESID 277:442)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  -2.5251 -33.7637  12.5131              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4034 T22:   0.5947                                     
REMARK   3      T33:   0.4227 T12:  -0.0047                                     
REMARK   3      T13:  -0.0376 T23:   0.0983                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.1406 L22:   1.9325                                     
REMARK   3      L33:   2.2350 L12:   0.2272                                     
REMARK   3      L13:  -0.2133 L23:  -0.6904                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1428 S12:  -0.0612 S13:   0.0771                       
REMARK   3      S21:   0.0818 S22:   0.0125 S23:  -0.0818                       
REMARK   3      S31:  -0.0662 S32:   0.2437 S33:   0.1025                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: (CHAIN B AND RESID 443:530)                            
REMARK   3    ORIGIN FOR THE GROUP (A):   2.0938 -44.6176  29.9903              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4465 T22:   0.8468                                     
REMARK   3      T33:   0.5577 T12:   0.0337                                     
REMARK   3      T13:  -0.0596 T23:   0.1365                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0658 L22:  -0.2398                                     
REMARK   3      L33:   1.2913 L12:   0.0839                                     
REMARK   3      L13:  -0.5072 L23:  -0.7907                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1104 S12:  -0.6509 S13:  -0.0015                       
REMARK   3      S21:   0.0621 S22:   0.0046 S23:   0.2030                       
REMARK   3      S31:   0.0910 S32:   0.2721 S33:  -0.1013                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: (CHAIN B AND RESID 531:637)                            
REMARK   3    ORIGIN FOR THE GROUP (A): -16.8388 -34.3769  22.3161              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5698 T22:   0.7207                                     
REMARK   3      T33:   0.5062 T12:  -0.0311                                     
REMARK   3      T13:   0.0185 T23:   0.0597                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9330 L22:   2.1701                                     
REMARK   3      L33:   0.6281 L12:  -0.0856                                     
REMARK   3      L13:   0.6306 L23:  -1.5368                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1042 S12:  -0.4678 S13:  -0.2025                       
REMARK   3      S21:  -0.1417 S22:   0.1662 S23:   0.5404                       
REMARK   3      S31:  -0.0684 S32:  -0.3142 S33:  -0.2097                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: (CHAIN B AND RESID 638:666)                            
REMARK   3    ORIGIN FOR THE GROUP (A): -13.9440   4.1008  -6.2016              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0457 T22:   0.5114                                     
REMARK   3      T33:   0.9893 T12:   0.1409                                     
REMARK   3      T13:  -0.0352 T23:  -0.0523                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.2019 L22:   3.1623                                     
REMARK   3      L33:   3.0328 L12:  -6.9671                                     
REMARK   3      L13:  -1.4008 L23:  -1.6476                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   1.1144 S12:  -1.4527 S13:  -0.6254                       
REMARK   3      S21:  -3.0351 S22:  -0.4690 S23:   1.7427                       
REMARK   3      S31:   0.0642 S32:   0.7669 S33:  -0.5332                       
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 2WG4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 15-APR-09.                  
REMARK 100 THE DEPOSITION ID IS D_1290039480.                                   
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               : DIAMOND                            
REMARK 200  BEAMLINE                       : I03                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.89                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC CCD                           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 13878                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.150                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.2                               
REMARK 200  DATA REDUNDANCY                : 7.500                              
REMARK 200  R MERGE                    (I) : 0.21000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.9000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.15                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.25                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.80                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.88000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.800                              
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   (%): 67.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.08                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M SODIUM ACETATE, PH 4.6 0.5 M       
REMARK 280  POTASSIUM THIOCYANATE                                               
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      114.63067            
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       57.31533            
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       57.31533            
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      114.63067            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2180 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 26650 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -75.7 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     GLU A    90                                                      
REMARK 465     GLU A    91                                                      
REMARK 465     ASN A    92                                                      
REMARK 465     THR A    93                                                      
REMARK 465     GLY A    94                                                      
REMARK 465     ASN A   190                                                      
REMARK 465     SER A   191                                                      
REMARK 465     VAL A   192                                                      
REMARK 465     ALA A   193                                                      
REMARK 465     ALA A   194                                                      
REMARK 465     HIS B   214                                                      
REMARK 465     GLY B   278                                                      
REMARK 465     GLY B   279                                                      
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     PRO B   314                                                      
REMARK 465     GLY B   457                                                      
REMARK 465     LYS B   458                                                      
REMARK 465     ASN B   459                                                      
REMARK 465     GLY B   538                                                      
REMARK 465     THR B   539                                                      
REMARK 465     SER B   540                                                      
REMARK 465     GLY B   541                                                      
REMARK 465     SER B   542                                                      
REMARK 465     CYS B   543                                                      
REMARK 465     ARG B   544                                                      
REMARK 465     GLY B   545                                                      
REMARK 465     TYR B   546                                                      
REMARK 465     PHE B   547                                                      
REMARK 465     SER B   548                                                      
REMARK 465     GLY B   549                                                      
REMARK 465     SER B   568                                                      
REMARK 465     LYS B   569                                                      
REMARK 465     SER B   570                                                      
REMARK 465     MET B   571                                                      
REMARK 465     THR B   572                                                      
REMARK 465     GLN B   573                                                      
REMARK 465     THR B   574                                                      
REMARK 465     GLU B   667                                                      
REMARK 465     GLN B   668                                                      
REMARK 465     VAL B   669                                                      
REMARK 465     ASP B   670                                                      
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     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 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASN A  51       46.05    -77.94                                   
REMARK 500    LYS A  55       31.83    -92.00                                   
REMARK 500    ALA A  59     -111.40   -103.34                                   
REMARK 500    THR A  68     -163.89   -106.32                                   
REMARK 500    TYR A  81       42.03    -96.44                                   
REMARK 500    ASP A 132      129.23   -179.27                                   
REMARK 500    HIS A 134       -2.41     63.17                                   
REMARK 500    TRP A 173      116.04   -165.04                                   
REMARK 500    TYR A 176       74.19    -68.93                                   
REMARK 500    ALA A 188     -159.30   -111.94                                   
REMARK 500    ASN B 306     -165.93   -163.64                                   
REMARK 500    HIS B 317     -168.78   -170.81                                   
REMARK 500    HIS B 430      -74.75   -147.28                                   
REMARK 500    SER B 461      129.21    177.95                                   
REMARK 500    PHE B 486     -179.85    -61.85                                   
REMARK 500    SER B 487      -79.60   -107.09                                   
REMARK 500    ASN B 488      -67.80   -129.64                                   
REMARK 500    PRO B 490     -142.64    -64.47                                   
REMARK 500    LEU B 491      121.90    164.17                                   
REMARK 500    GLN B 523     -156.37    -91.09                                   
REMARK 500    THR B 527      -40.66     68.57                                   
REMARK 500    PRO B 591      155.37    -49.81                                   
REMARK 500    ARG B 610      -79.05    -65.50                                   
REMARK 500    LEU B 611       60.57   -109.12                                   
REMARK 500    PRO B 619       -5.23    -56.73                                   
REMARK 500    VAL B 650      -72.23   -132.17                                   
REMARK 500    PRO B 652       94.19    -51.85                                   
REMARK 500    LYS B 658     -175.11    -66.21                                   
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                              ZN A1190  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 141   NE2                                                    
REMARK 620 2 ASP B 383   OD2  90.2                                              
REMARK 620 3 HIS A 183   ND1 106.9 110.1                                        
REMARK 620 4 ASP A 148   OD1 115.4 125.4 107.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA B1667  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 TYR B 474   O                                                      
REMARK 620 2 ASP B 473   OD1  83.3                                              
REMARK 620 3 ASN B 412   O    79.9 126.7                                        
REMARK 620 4 ARG B 410   O   131.2  70.9  83.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 1190                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 1667                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 1668                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 1669                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 1670                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2WFX   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE COMPLEX BETWEEN HUMAN HEDGEHOG-INTERACTING  
REMARK 900 PROTEIN HIP AND SONIC HEDGEHOG IN THE PRESENCE OF CALCIUM            
REMARK 900 RELATED ID: 2WFT   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE HUMAN HIP ECTODOMAIN                        
REMARK 900 RELATED ID: 1VHH   RELATED DB: PDB                                   
REMARK 900 MOL_ID: 1; MOLECULE: SONIC HEDGEHOG; CHAIN: NULL; DOMAIN: AMINO-     
REMARK 900 TERMINAL DOMAIN (RESIDUES 34 - 195); SYNONYM: HHG-1, VHH-1;          
REMARK 900 ENGINEERED: YES                                                      
REMARK 900 RELATED ID: 2WFQ   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE N-TERMINAL SIGNALLING DOMAIN OF HUMAN DHH   
REMARK 900 WITHOUT CALCIUM                                                      
REMARK 900 RELATED ID: 2WFR   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE N-TERMINAL SIGNALLING DOMAIN OF HUMAN DHH   
REMARK 900 WITH CALCIUM                                                         
REMARK 900 RELATED ID: 2WG3   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE COMPLEX BETWEEN HUMAN HEDGEHOG-INTERACTING  
REMARK 900 PROTEIN HIP AND DESERT HEDGEHOG WITHOUT CALCIUM                      
DBREF  2WG4 A   40   191  UNP    Q62226   SHH_MOUSE       40    191             
DBREF  2WG4 B  214   670  UNP    Q96QV1   HHIP_HUMAN     214    670             
SEQRES   1 A  155  LEU THR PRO LEU ALA TYR LYS GLN PHE ILE PRO ASN VAL          
SEQRES   2 A  155  ALA GLU LYS THR LEU GLY ALA SER GLY ARG TYR GLU GLY          
SEQRES   3 A  155  LYS ILE THR ARG ASN SER GLU ARG PHE LYS GLU LEU THR          
SEQRES   4 A  155  PRO ASN TYR ASN PRO ASP ILE ILE PHE LYS ASP GLU GLU          
SEQRES   5 A  155  ASN THR GLY ALA ASP ARG LEU MET THR GLN ARG CYS LYS          
SEQRES   6 A  155  ASP LYS LEU ASN ALA LEU ALA ILE SER VAL MET ASN GLN          
SEQRES   7 A  155  TRP PRO GLY VAL LYS LEU ARG VAL THR GLU GLY TRP ASP          
SEQRES   8 A  155  GLU ASP GLY HIS HIS SER GLU GLU SER LEU HIS TYR GLU          
SEQRES   9 A  155  GLY ARG ALA VAL ASP ILE THR THR SER ASP ARG ASP ARG          
SEQRES  10 A  155  SER LYS TYR GLY MET LEU ALA ARG LEU ALA VAL GLU ALA          
SEQRES  11 A  155  GLY PHE ASP TRP VAL TYR TYR GLU SER LYS ALA HIS ILE          
SEQRES  12 A  155  HIS CYS SER VAL LYS ALA GLU ASN SER VAL ALA ALA              
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  A1190       1                                                       
HET     NA  B1667       1                                                       
HET     NA  B1668       1                                                       
HET     NA  B1669       1                                                       
HET     NA  B1670       1                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM      NA SODIUM ION                                                       
FORMUL   3   ZN    ZN 2+                                                        
FORMUL   4   NA    4(NA 1+)                                                     
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 SER A  139  GLY A  144  5                                   6    
HELIX    4   4 LYS A  158  ALA A  169  1                                  12    
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 SER B  606  LEU B  611  1                                   6    
SHEET    1  AA 6 PHE A  48  ILE A  49  0                                        
SHEET    2  AA 6 TRP A 173  TYR A 175 -1  O  VAL A 174   N  ILE A  49           
SHEET    3  AA 6 ILE A 182  SER A 185 -1  O  HIS A 183   N  TYR A 175           
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  AB 2 THR A  78  PRO A  79  0                                        
SHEET    2  AB 2 LEU A  98  MET A  99 -1  O  MET A  99   N  THR A  78           
SHEET    1  BA 4 CYS B 218  VAL B 223  0                                        
SHEET    2  BA 4 LYS B 578  VAL B 583 -1  O  LEU B 579   N  VAL B 222           
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 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 4 ALA B 436  ASP B 438  0                                        
SHEET    2  BE 4 LEU B 448  ASP B 454 -1  O  THR B 449   N  ASP B 438           
SHEET    3  BE 4 SER B 462  ILE B 468 -1  O  SER B 462   N  ASP B 454           
SHEET    4  BE 4 LEU B 481  PHE B 483 -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 A1190                 NE2 HIS A 141     1555   1555  2.01  
LINK        ZN    ZN A1190                 OD2 ASP B 383     1555   1555  2.06  
LINK        ZN    ZN A1190                 ND1 HIS A 183     1555   1555  2.01  
LINK        ZN    ZN A1190                 OD1 ASP A 148     1555   1555  2.05  
LINK        NA    NA B1667                 O   TYR B 474     1555   1555  2.53  
LINK        NA    NA B1667                 OD1 ASP B 473     1555   1555  2.44  
LINK        NA    NA B1667                 O   ASN B 412     1555   1555  2.47  
LINK        NA    NA B1667                 O   ARG B 410     1555   1555  2.51  
CISPEP   1 ILE A   49    PRO A   50          0         2.32                     
CISPEP   2 GLU B  640    PRO B  641          0        -0.91                     
SITE     1 AC1  4 HIS A 141  ASP A 148  HIS A 183  ASP B 383                    
SITE     1 AC2  5 ARG B 410  SER B 411  ASN B 412  ASP B 473                    
SITE     2 AC2  5 TYR B 474                                                     
SITE     1 AC3  3 PRO B 441  ASP B 443  ILE B 446                               
SITE     1 AC4  3 SER B 286  LEU B 287  LEU B 357                               
SITE     1 AC5  3 HIS B 269  VAL B 272  GLN B 273                               
CRYST1   88.055   88.055  171.946  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      0.011357  0.006557  0.000000        0.00000                         
SCALE2      0.000000  0.013113  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005816        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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