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Database: PDB
Entry: 3HO5
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HEADER    SIGNALING PROTEIN                       01-JUN-09   3HO5              
TITLE     CRYSTAL STRUCTURE OF HEDGEHOG-INTERACTING PROTEIN (HHIP) AND SONIC    
TITLE    2 HEDGEHOG (SHH) COMPLEX                                               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HEDGEHOG-INTERACTING PROTEIN;                              
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: UNP RESIDUES 193-667;                                      
COMPND   5 SYNONYM: HHIP, HIP;                                                  
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: SONIC HEDGEHOG PROTEIN;                                    
COMPND   9 CHAIN: H;                                                            
COMPND  10 FRAGMENT: UNP RESIDUES 29-197;                                       
COMPND  11 SYNONYM: SHH, HHG-1, SONIC HEDGEHOG PROTEIN N-PRODUCT, SONIC HEDGEHOG
COMPND  12 PROTEIN C-PRODUCT;                                                   
COMPND  13 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: HHIP, HIP, UNQ5825/PRO19644;                                   
SOURCE   6 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;                                  
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7111;                                       
SOURCE   8 EXPRESSION_SYSTEM_CELL_LINE: INSECT CELLS;                           
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: GATEWAY VECTOR PENTR/D-TOPO           
SOURCE  10 (INVITROGEN);                                                        
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: PENTR/D-TOPO WITH HONEYBEE MELITTIN       
SOURCE  12 SECRETION SIGNAL;                                                    
SOURCE  13 MOL_ID: 2;                                                           
SOURCE  14 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  15 ORGANISM_COMMON: HUMAN;                                              
SOURCE  16 ORGANISM_TAXID: 9606;                                                
SOURCE  17 GENE: SHH;                                                           
SOURCE  18 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  19 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  20 EXPRESSION_SYSTEM_CELL_LINE: ROSETTA 2 (NOVAGEN);                    
SOURCE  21 EXPRESSION_SYSTEM_VECTOR_TYPE: PET101/D-TOPO (INVITROGEN) WITH T7    
SOURCE  22 PROMOTER;                                                            
SOURCE  23 EXPRESSION_SYSTEM_PLASMID: PET101/D-TOPO (INVITROGEN)                
KEYWDS    RECEPTOR ECTODOMAIN, SIX-BLADED-PROPELLER DOMAIN, EGF DOMAIN,         
KEYWDS   2 DISULFIDE BOND, CALCIUM CATION, ZINC CATION, CELL MEMBRANE, EGF-LIKE 
KEYWDS   3 DOMAIN, GLYCOPROTEIN, MEMBRANE, SECRETED, AUTOCATALYTIC CLEAVAGE,    
KEYWDS   4 DEVELOPMENTAL PROTEIN, DISEASE MUTATION, HOLOPROSENCEPHALY,          
KEYWDS   5 HYDROLASE, LIPOPROTEIN, MICROPHTHALMIA, PALMITATE, PROTEASE,         
KEYWDS   6 SIGNALING PROTEIN                                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.G.HYMOWITZ,I.BOSANAC                                                
REVDAT   3   13-JUL-11 3HO5    1       VERSN                                    
REVDAT   2   28-APR-10 3HO5    1       JRNL                                     
REVDAT   1   23-JUN-09 3HO5    0                                                
JRNL        AUTH   I.BOSANAC,H.R.MAUN,S.J.SCALES,X.WEN,A.LINGEL,J.F.BAZAN,      
JRNL        AUTH 2 F.J.DE SAUVAGE,S.G.HYMOWITZ,R.A.LAZARUS                      
JRNL        TITL   THE STRUCTURE OF SHH IN COMPLEX WITH HHIP REVEALS A          
JRNL        TITL 2 RECOGNITION ROLE FOR THE SHH PSEUDO ACTIVE SITE IN           
JRNL        TITL 3 SIGNALING.                                                   
JRNL        REF    NAT.STRUCT.MOL.BIOL.          V.  16   691 2009              
JRNL        REFN                   ISSN 1545-9993                               
JRNL        PMID   19561609                                                     
JRNL        DOI    10.1038/NSMB.1632                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.01 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.01                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 35147                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.234                           
REMARK   3   R VALUE            (WORKING SET) : 0.231                           
REMARK   3   FREE R VALUE                     : 0.287                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1874                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 25                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 3.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.07                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2039                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.44                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2930                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 103                          
REMARK   3   BIN FREE R VALUE                    : 0.3400                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 8251                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 4                                       
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 96.67                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 4.78000                                              
REMARK   3    B22 (A**2) : 4.78000                                              
REMARK   3    B33 (A**2) : -7.17000                                             
REMARK   3    B12 (A**2) : 2.39000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 1.342         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.425         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.336         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 40.143        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.921                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.885                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  8444 ; 0.008 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 11395 ; 1.186 ; 1.960       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1044 ; 6.529 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   394 ;33.348 ;23.680       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1425 ;19.747 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    58 ;15.728 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1198 ; 0.080 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  6462 ; 0.003 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  3517 ; 0.204 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  5485 ; 0.306 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   242 ; 0.141 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    61 ; 0.200 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     3 ; 0.224 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  5344 ; 2.161 ; 2.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  8350 ; 3.635 ; 5.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3463 ; 1.997 ; 2.500       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  3045 ; 3.223 ; 5.000       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 7                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   214        A   603                          
REMARK   3    ORIGIN FOR THE GROUP (A):  13.5418  28.7701  48.7252              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.5773 T22:   0.0072                                     
REMARK   3      T33:  -0.5072 T12:  -0.2034                                     
REMARK   3      T13:  -0.0647 T23:  -0.1130                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.2304 L22:   2.2035                                     
REMARK   3      L33:   5.6920 L12:  -0.8665                                     
REMARK   3      L13:  -1.0870 L23:   0.0995                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0035 S12:   1.4707 S13:   0.1007                       
REMARK   3      S21:  -0.4375 S22:   0.0482 S23:  -0.0093                       
REMARK   3      S31:  -0.0521 S32:   0.0539 S33:  -0.0516                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   604        A   637                          
REMARK   3    ORIGIN FOR THE GROUP (A):  41.0485  17.6891  39.6322              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0738 T22:   0.9407                                     
REMARK   3      T33:  -0.0092 T12:   0.0831                                     
REMARK   3      T13:   0.0702 T23:  -0.4029                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  19.0273 L22:   0.6190                                     
REMARK   3      L33:  11.6971 L12:   3.4319                                     
REMARK   3      L13: -14.9186 L23:  -2.6908                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.5742 S12:   0.9847 S13:  -0.5733                       
REMARK   3      S21:  -0.5663 S22:  -0.8648 S23:  -0.3755                       
REMARK   3      S31:   0.7574 S32:   0.4312 S33:   1.4389                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   638        A   669                          
REMARK   3    ORIGIN FOR THE GROUP (A):  63.2572  24.0824  30.9176              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.3984 T22:  -0.5158                                     
REMARK   3      T33:  -0.2734 T12:   0.0479                                     
REMARK   3      T13:   0.1202 T23:  -0.0557                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  19.5851 L22:  10.8279                                     
REMARK   3      L33:  25.7191 L12:  -3.5468                                     
REMARK   3      L13:  11.0969 L23:   2.6616                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.5733 S12:  -0.0285 S13:   1.8190                       
REMARK   3      S21:   0.1869 S22:  -0.5694 S23:  -0.1920                       
REMARK   3      S31:  -2.4019 S32:  -0.8979 S33:  -0.0039                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   214        B   603                          
REMARK   3    ORIGIN FOR THE GROUP (A):   7.0523  25.9662  98.6709              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.3603 T22:  -0.4969                                     
REMARK   3      T33:  -0.3930 T12:   0.0667                                     
REMARK   3      T13:   0.0250 T23:   0.1228                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.1991 L22:   1.9124                                     
REMARK   3      L33:   6.3512 L12:  -0.5354                                     
REMARK   3      L13:  -0.4551 L23:   0.8778                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2454 S12:  -0.6976 S13:  -0.3102                       
REMARK   3      S21:   0.5887 S22:   0.1954 S23:   0.0436                       
REMARK   3      S31:   0.7498 S32:   0.2605 S33:   0.0500                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   604        B   637                          
REMARK   3    ORIGIN FOR THE GROUP (A): -15.5961  44.2787 108.6657              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.4438 T22:   0.1957                                     
REMARK   3      T33:  -0.3473 T12:   0.2062                                     
REMARK   3      T13:   0.1719 T23:  -0.1343                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8966 L22:   7.9702                                     
REMARK   3      L33:   8.3801 L12:  -0.2110                                     
REMARK   3      L13:  -0.1629 L23:   6.3729                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3586 S12:  -0.7337 S13:  -0.1109                       
REMARK   3      S21:   0.4230 S22:  -0.1590 S23:   0.4796                       
REMARK   3      S31:  -0.5194 S32:  -0.9657 S33:   0.5176                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   638        B   669                          
REMARK   3    ORIGIN FOR THE GROUP (A): -19.9242  64.3175 122.8157              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.7689 T22:  -0.4586                                     
REMARK   3      T33:  -0.6479 T12:  -0.1707                                     
REMARK   3      T13:   0.0987 T23:  -0.0418                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  24.2735 L22:  31.4133                                     
REMARK   3      L33:  14.1006 L12:  -5.1463                                     
REMARK   3      L13:   1.1620 L23:   0.6334                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.9788 S12:  -0.5984 S13:   1.0498                       
REMARK   3      S21:   1.2449 S22:   1.3659 S23:  -1.0860                       
REMARK   3      S31:  -0.0503 S32:   2.3235 S33:  -0.3871                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   H    38        H   191                          
REMARK   3    ORIGIN FOR THE GROUP (A):  17.4700  34.0870 136.9189              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7295 T22:   1.2638                                     
REMARK   3      T33:  -0.1123 T12:   0.2086                                     
REMARK   3      T13:  -0.2030 T23:   0.0130                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.4315 L22:   6.0294                                     
REMARK   3      L33:   5.6755 L12:   1.3144                                     
REMARK   3      L13:   0.4240 L23:  -0.5407                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0538 S12:  -1.1717 S13:   0.1966                       
REMARK   3      S21:   0.8086 S22:   0.0638 S23:  -0.3688                       
REMARK   3      S31:  -0.1383 S32:   0.3085 S33:  -0.0100                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 3HO5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-JUN-09.                  
REMARK 100 THE RCSB ID CODE IS RCSB053374.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 06-JUN-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRL                               
REMARK 200  BEAMLINE                       : BL11-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97839                            
REMARK 200  MONOCHROMATOR                  : SIDE SCATTERING BENT CUBE-ROOT I   
REMARK 200                                   -BEAM SINGLE CRYSTAL; ASYMMETRIC   
REMARK 200                                   CUT 4.965 DEGS                     
REMARK 200  OPTICS                         : FLAT MIRROR (VERTICAL FOCUSING);   
REMARK 200                                   SINGLE CRYSTAL SI(111) BENT        
REMARK 200                                   MONOCHROMATOR (HO RIZONTAL         
REMARK 200                                   FOCUSING)                          
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 325 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 37106                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 8.700                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.08500                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 24.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.11                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 8.90                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.58900                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.300                              
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, 3HO4                               
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 65.31                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.55                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M BIS-TRIS PROPANE PH 7.0 AND 2.2-   
REMARK 280  2.5 M SODIUM FORMATE, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE    
REMARK 280  292K                                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+2/3                                           
REMARK 290       6555   -X,-X+Y,-Z+1/3                                          
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      100.94333            
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      201.88667            
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      201.88667            
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      100.94333            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2010 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 28520 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -58.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, H                                  
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 400                                                                      
REMARK 400 COMPOUND                                                             
REMARK 400 THE SECOND MOLECULE OF SONIC HEDGEHOG PROTEIN WAS CRYSTALLIZED BUT   
REMARK 400 APPEARED TO BE LARGELY DISORDERED AND WAS NOT INCLUDED IN THE FINAL  
REMARK 400 MODEL. THE SEQUENCE IS:                                              
REMARK 400 GFGKRRHPKKLTPLAYKQFIPNVAEKTLGASGRYEGKISRNSERFKELTPNYNPDIIFKDEENTGADR 
REMARK 400  LMTQRCKDKLNALAISVMNQWPGV                                            
REMARK 400  KLRVTEGWDEDGHHSEESLHYEGRAVDITTSDRDRSKYGMLARLAVEAGFDWVYYESKAHIHCSVKA 
REMARK 400  ENSVAAKSGG                                                          
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     SER A   193                                                      
REMARK 465     ASN A   194                                                      
REMARK 465     TYR A   195                                                      
REMARK 465     LEU A   196                                                      
REMARK 465     ASP A   197                                                      
REMARK 465     GLN A   198                                                      
REMARK 465     MET A   199                                                      
REMARK 465     GLU A   200                                                      
REMARK 465     GLU A   201                                                      
REMARK 465     TYR A   202                                                      
REMARK 465     ASP A   203                                                      
REMARK 465     LYS A   204                                                      
REMARK 465     VAL A   205                                                      
REMARK 465     GLU A   206                                                      
REMARK 465     GLU A   207                                                      
REMARK 465     ILE A   208                                                      
REMARK 465     SER A   209                                                      
REMARK 465     ARG A   210                                                      
REMARK 465     LYS A   211                                                      
REMARK 465     HIS A   212                                                      
REMARK 465     LYS A   213                                                      
REMARK 465     GLN A   307                                                      
REMARK 465     GLU A   308                                                      
REMARK 465     ASN A   419                                                      
REMARK 465     GLN A   420                                                      
REMARK 465     PRO A   421                                                      
REMARK 465     PRO A   441                                                      
REMARK 465     THR A   442                                                      
REMARK 465     ASP A   443                                                      
REMARK 465     ILE A   444                                                      
REMARK 465     ASN A   445                                                      
REMARK 465     ILE A   446                                                      
REMARK 465     HIS A   671                                                      
REMARK 465     HIS A   672                                                      
REMARK 465     HIS A   673                                                      
REMARK 465     SER B   193                                                      
REMARK 465     ASN B   194                                                      
REMARK 465     TYR B   195                                                      
REMARK 465     LEU B   196                                                      
REMARK 465     ASP B   197                                                      
REMARK 465     GLN B   198                                                      
REMARK 465     MET B   199                                                      
REMARK 465     GLU B   200                                                      
REMARK 465     GLU B   201                                                      
REMARK 465     TYR B   202                                                      
REMARK 465     ASP B   203                                                      
REMARK 465     LYS B   204                                                      
REMARK 465     VAL B   205                                                      
REMARK 465     GLU B   206                                                      
REMARK 465     GLU B   207                                                      
REMARK 465     ILE B   208                                                      
REMARK 465     SER B   209                                                      
REMARK 465     ARG B   210                                                      
REMARK 465     LYS B   211                                                      
REMARK 465     HIS B   212                                                      
REMARK 465     LYS B   213                                                      
REMARK 465     PRO B   441                                                      
REMARK 465     THR B   442                                                      
REMARK 465     ASP B   443                                                      
REMARK 465     ILE B   444                                                      
REMARK 465     ASN B   445                                                      
REMARK 465     ILE B   446                                                      
REMARK 465     HIS B   671                                                      
REMARK 465     HIS B   672                                                      
REMARK 465     HIS B   673                                                      
REMARK 465     GLY H    29                                                      
REMARK 465     PHE H    30                                                      
REMARK 465     GLY H    31                                                      
REMARK 465     LYS H    32                                                      
REMARK 465     ARG H    33                                                      
REMARK 465     ARG H    34                                                      
REMARK 465     HIS H    35                                                      
REMARK 465     PRO H    36                                                      
REMARK 465     LYS H    37                                                      
REMARK 465     ALA H   192                                                      
REMARK 465     ALA H   193                                                      
REMARK 465     LYS H   194                                                      
REMARK 465     SER H   195                                                      
REMARK 465     GLY H   196                                                      
REMARK 465     GLY H   197                                                      
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     ARG A  410   CB   CG   CD   NE   CZ   NH1  NH2                   
REMARK 480     LYS A  458   CB   CG   CD   CE   NZ                              
REMARK 480     ARG A  460   CB   CG   CD   NE   CZ   NH1  NH2                   
REMARK 480     ARG B  410   CB   CG   CD   NE   CZ   NH1  NH2                   
REMARK 480     LYS B  458   CB   CG   CD   CE   NZ                              
REMARK 480     ARG B  460   CB   CG   CD   NE   CZ   NH1  NH2                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    THR A   527     N    GLN A   529              2.15            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    ARG A 460   CA    ARG A 460   CB     -0.210                       
REMARK 500    CYS B 218   CB    CYS B 218   SG     -0.102                       
REMARK 500    ARG B 410   CA    ARG B 410   CB     -0.142                       
REMARK 500    LYS B 458   CA    LYS B 458   CB     -0.147                       
REMARK 500    ARG B 460   CA    ARG B 460   CB     -0.231                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    LYS A 458   CB  -  CA  -  C   ANGL. DEV. = -14.4 DEGREES          
REMARK 500    ARG A 460   N   -  CA  -  CB  ANGL. DEV. =  12.2 DEGREES          
REMARK 500    LEU B 299   CA  -  CB  -  CG  ANGL. DEV. =  18.2 DEGREES          
REMARK 500    ARG B 460   N   -  CA  -  CB  ANGL. DEV. = -19.3 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    GLN A 228       82.50     21.52                                   
REMARK 500    GLN A 240       45.01    -82.23                                   
REMARK 500    ILE A 276     -102.20    -11.68                                   
REMARK 500    LYS A 277      -74.13      8.33                                   
REMARK 500    ALA A 311       32.88   -145.07                                   
REMARK 500    ASP A 362       -8.80     70.25                                   
REMARK 500    HIS A 430      -90.73   -107.82                                   
REMARK 500    ASP A 431       77.41   -117.05                                   
REMARK 500    LYS A 458       53.27   -112.43                                   
REMARK 500    ARG A 460     -162.63     56.18                                   
REMARK 500    ILE A 469     -161.12     63.49                                   
REMARK 500    SER A 487      -32.59   -138.94                                   
REMARK 500    ASN A 488       32.99    -85.99                                   
REMARK 500    CYS A 500      -37.22   -131.23                                   
REMARK 500    THR A 527       50.22   -106.63                                   
REMARK 500    LYS A 528       22.76    -12.29                                   
REMARK 500    SER A 542        2.44    -62.94                                   
REMARK 500    CYS A 612      103.95    -58.26                                   
REMARK 500    ARG A 613      -94.85    -43.80                                   
REMARK 500    SER B 224     -156.81   -129.03                                   
REMARK 500    GLN B 228       72.95     38.52                                   
REMARK 500    GLN B 240       49.69    -71.90                                   
REMARK 500    ILE B 276      -55.35   -133.52                                   
REMARK 500    ASN B 292       42.81   -106.72                                   
REMARK 500    LYS B 295      -62.20   -103.62                                   
REMARK 500    GLN B 307      -52.49     63.08                                   
REMARK 500    GLU B 308       51.85     27.33                                   
REMARK 500    ASP B 377      -71.15    -57.87                                   
REMARK 500    HIS B 430      -80.05   -116.46                                   
REMARK 500    LYS B 458       66.41    -69.49                                   
REMARK 500    ARG B 460      -97.86    -61.21                                   
REMARK 500    SER B 461      108.18   -167.07                                   
REMARK 500    ILE B 469     -171.20     59.95                                   
REMARK 500    LEU B 480       65.34   -110.37                                   
REMARK 500    PRO B 485       30.26    -97.53                                   
REMARK 500    ASN B 576       45.39   -142.75                                   
REMARK 500    PRO B 627      115.02    -30.18                                   
REMARK 500    HIS B 669      -71.90   -127.34                                   
REMARK 500    ALA H  58     -103.89   -103.94                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 GLY A  275     ILE A  276                  149.82                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN                            
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE                   
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    ARG A 460        24.1      L          L   OUTSIDE RANGE           
REMARK 500    LYS A 528        24.9      L          L   OUTSIDE RANGE           
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 H 400  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 383   OD2                                                    
REMARK 620 2 HIS H 140   NE2 103.2                                              
REMARK 620 3 ASP H 147   OD1 138.4  99.2                                        
REMARK 620 4 HIS H 182   ND1  98.0 105.5 109.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA H 401  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU H  89   OE1                                                    
REMARK 620 2 GLU H  89   OE2  55.8                                              
REMARK 620 3 GLU H  90   OE1  72.7  83.1                                        
REMARK 620 4 GLU H  90   OE2 119.3  86.4  55.5                                  
REMARK 620 5 ASP H  95   OD1 140.3 159.5  90.7  74.1                            
REMARK 620 6 ASP H  95   OD2  85.1 140.4  79.3 111.2  56.0                      
REMARK 620 7 THR H 125   O    88.4 104.9 150.7 151.1  90.0  76.8                
REMARK 620 8 GLU H 126   OE2 145.0  91.4 119.3  63.8  74.6 128.1  89.1          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA H 402  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU H  90   OE2                                                    
REMARK 620 2 GLU H 126   OE1 120.1                                              
REMARK 620 3 GLU H 126   OE2  64.1  56.4                                        
REMARK 620 4 ASP H 129   OD1 158.5  72.9 123.6                                  
REMARK 620 5 ASP H 131   OD2 104.2 128.1 156.9  74.9                            
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 H 400                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA H 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA H 402                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 902                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3HO3   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3HO4   RELATED DB: PDB                                   
DBREF  3HO5 A  193   667  UNP    Q96QV1   HHIP_HUMAN     193    667             
DBREF  3HO5 B  193   667  UNP    Q96QV1   HHIP_HUMAN     193    667             
DBREF  3HO5 H   29   197  UNP    Q15465   SHH_HUMAN       29    197             
SEQADV 3HO5 HIS A  668  UNP  Q96QV1              EXPRESSION TAG                 
SEQADV 3HO5 HIS A  669  UNP  Q96QV1              EXPRESSION TAG                 
SEQADV 3HO5 HIS A  670  UNP  Q96QV1              EXPRESSION TAG                 
SEQADV 3HO5 HIS A  671  UNP  Q96QV1              EXPRESSION TAG                 
SEQADV 3HO5 HIS A  672  UNP  Q96QV1              EXPRESSION TAG                 
SEQADV 3HO5 HIS A  673  UNP  Q96QV1              EXPRESSION TAG                 
SEQADV 3HO5 HIS B  668  UNP  Q96QV1              EXPRESSION TAG                 
SEQADV 3HO5 HIS B  669  UNP  Q96QV1              EXPRESSION TAG                 
SEQADV 3HO5 HIS B  670  UNP  Q96QV1              EXPRESSION TAG                 
SEQADV 3HO5 HIS B  671  UNP  Q96QV1              EXPRESSION TAG                 
SEQADV 3HO5 HIS B  672  UNP  Q96QV1              EXPRESSION TAG                 
SEQADV 3HO5 HIS B  673  UNP  Q96QV1              EXPRESSION TAG                 
SEQRES   1 A  481  SER ASN TYR LEU ASP GLN MET GLU GLU TYR ASP LYS VAL          
SEQRES   2 A  481  GLU GLU ILE SER ARG LYS HIS LYS HIS ASN CYS PHE CYS          
SEQRES   3 A  481  ILE GLN GLU VAL VAL SER GLY LEU ARG GLN PRO VAL GLY          
SEQRES   4 A  481  ALA LEU HIS SER GLY ASP GLY SER GLN ARG LEU PHE ILE          
SEQRES   5 A  481  LEU GLU LYS GLU GLY TYR VAL LYS ILE LEU THR PRO GLU          
SEQRES   6 A  481  GLY GLU ILE PHE LYS GLU PRO TYR LEU ASP ILE HIS LYS          
SEQRES   7 A  481  LEU VAL GLN SER GLY ILE LYS GLY GLY ASP GLU ARG GLY          
SEQRES   8 A  481  LEU LEU SER LEU ALA PHE HIS PRO ASN TYR LYS LYS ASN          
SEQRES   9 A  481  GLY LYS LEU TYR VAL SER TYR THR THR ASN GLN GLU ARG          
SEQRES  10 A  481  TRP ALA ILE GLY PRO HIS ASP HIS ILE LEU ARG VAL VAL          
SEQRES  11 A  481  GLU TYR THR VAL SER ARG LYS ASN PRO HIS GLN VAL ASP          
SEQRES  12 A  481  LEU ARG THR ALA ARG VAL PHE LEU GLU VAL ALA GLU LEU          
SEQRES  13 A  481  HIS ARG LYS HIS LEU GLY GLY GLN LEU LEU PHE GLY PRO          
SEQRES  14 A  481  ASP GLY PHE LEU TYR ILE ILE LEU GLY ASP GLY MET ILE          
SEQRES  15 A  481  THR LEU ASP ASP MET GLU GLU MET ASP GLY LEU SER ASP          
SEQRES  16 A  481  PHE THR GLY SER VAL LEU ARG LEU ASP VAL ASP THR ASP          
SEQRES  17 A  481  MET CYS ASN VAL PRO TYR SER ILE PRO ARG SER ASN PRO          
SEQRES  18 A  481  HIS PHE ASN SER THR ASN GLN PRO PRO GLU VAL PHE ALA          
SEQRES  19 A  481  HIS GLY LEU HIS ASP PRO GLY ARG CYS ALA VAL ASP ARG          
SEQRES  20 A  481  HIS PRO THR ASP ILE ASN ILE ASN LEU THR ILE LEU CYS          
SEQRES  21 A  481  SER ASP SER ASN GLY LYS ASN ARG SER SER ALA ARG ILE          
SEQRES  22 A  481  LEU GLN ILE ILE LYS GLY LYS ASP TYR GLU SER GLU PRO          
SEQRES  23 A  481  SER LEU LEU GLU PHE LYS PRO PHE SER ASN GLY PRO LEU          
SEQRES  24 A  481  VAL GLY GLY PHE VAL TYR ARG GLY CYS GLN SER GLU ARG          
SEQRES  25 A  481  LEU TYR GLY SER TYR VAL PHE GLY ASP ARG ASN GLY ASN          
SEQRES  26 A  481  PHE LEU THR LEU GLN GLN SER PRO VAL THR LYS GLN TRP          
SEQRES  27 A  481  GLN GLU LYS PRO LEU CYS LEU GLY THR SER GLY SER CYS          
SEQRES  28 A  481  ARG GLY TYR PHE SER GLY HIS ILE LEU GLY PHE GLY GLU          
SEQRES  29 A  481  ASP GLU LEU GLY GLU VAL TYR ILE LEU SER SER SER LYS          
SEQRES  30 A  481  SER MET THR GLN THR HIS ASN GLY LYS LEU TYR LYS ILE          
SEQRES  31 A  481  VAL ASP PRO LYS ARG PRO LEU MET PRO GLU GLU CYS ARG          
SEQRES  32 A  481  ALA THR VAL GLN PRO ALA GLN THR LEU THR SER GLU CYS          
SEQRES  33 A  481  SER ARG LEU CYS ARG ASN GLY TYR CYS THR PRO THR GLY          
SEQRES  34 A  481  LYS CYS CYS CYS SER PRO GLY TRP GLU GLY ASP PHE CYS          
SEQRES  35 A  481  ARG THR ALA LYS CYS GLU PRO ALA CYS ARG HIS GLY GLY          
SEQRES  36 A  481  VAL CYS VAL ARG PRO ASN LYS CYS LEU CYS LYS LYS GLY          
SEQRES  37 A  481  TYR LEU GLY PRO GLN CYS GLU HIS HIS HIS HIS HIS HIS          
SEQRES   1 B  481  SER ASN TYR LEU ASP GLN MET GLU GLU TYR ASP LYS VAL          
SEQRES   2 B  481  GLU GLU ILE SER ARG LYS HIS LYS HIS ASN CYS PHE CYS          
SEQRES   3 B  481  ILE GLN GLU VAL VAL SER GLY LEU ARG GLN PRO VAL GLY          
SEQRES   4 B  481  ALA LEU HIS SER GLY ASP GLY SER GLN ARG LEU PHE ILE          
SEQRES   5 B  481  LEU GLU LYS GLU GLY TYR VAL LYS ILE LEU THR PRO GLU          
SEQRES   6 B  481  GLY GLU ILE PHE LYS GLU PRO TYR LEU ASP ILE HIS LYS          
SEQRES   7 B  481  LEU VAL GLN SER GLY ILE LYS GLY GLY ASP GLU ARG GLY          
SEQRES   8 B  481  LEU LEU SER LEU ALA PHE HIS PRO ASN TYR LYS LYS ASN          
SEQRES   9 B  481  GLY LYS LEU TYR VAL SER TYR THR THR ASN GLN GLU ARG          
SEQRES  10 B  481  TRP ALA ILE GLY PRO HIS ASP HIS ILE LEU ARG VAL VAL          
SEQRES  11 B  481  GLU TYR THR VAL SER ARG LYS ASN PRO HIS GLN VAL ASP          
SEQRES  12 B  481  LEU ARG THR ALA ARG VAL PHE LEU GLU VAL ALA GLU LEU          
SEQRES  13 B  481  HIS ARG LYS HIS LEU GLY GLY GLN LEU LEU PHE GLY PRO          
SEQRES  14 B  481  ASP GLY PHE LEU TYR ILE ILE LEU GLY ASP GLY MET ILE          
SEQRES  15 B  481  THR LEU ASP ASP MET GLU GLU MET ASP GLY LEU SER ASP          
SEQRES  16 B  481  PHE THR GLY SER VAL LEU ARG LEU ASP VAL ASP THR ASP          
SEQRES  17 B  481  MET CYS ASN VAL PRO TYR SER ILE PRO ARG SER ASN PRO          
SEQRES  18 B  481  HIS PHE ASN SER THR ASN GLN PRO PRO GLU VAL PHE ALA          
SEQRES  19 B  481  HIS GLY LEU HIS ASP PRO GLY ARG CYS ALA VAL ASP ARG          
SEQRES  20 B  481  HIS PRO THR ASP ILE ASN ILE ASN LEU THR ILE LEU CYS          
SEQRES  21 B  481  SER ASP SER ASN GLY LYS ASN ARG SER SER ALA ARG ILE          
SEQRES  22 B  481  LEU GLN ILE ILE LYS GLY LYS ASP TYR GLU SER GLU PRO          
SEQRES  23 B  481  SER LEU LEU GLU PHE LYS PRO PHE SER ASN GLY PRO LEU          
SEQRES  24 B  481  VAL GLY GLY PHE VAL TYR ARG GLY CYS GLN SER GLU ARG          
SEQRES  25 B  481  LEU TYR GLY SER TYR VAL PHE GLY ASP ARG ASN GLY ASN          
SEQRES  26 B  481  PHE LEU THR LEU GLN GLN SER PRO VAL THR LYS GLN TRP          
SEQRES  27 B  481  GLN GLU LYS PRO LEU CYS LEU GLY THR SER GLY SER CYS          
SEQRES  28 B  481  ARG GLY TYR PHE SER GLY HIS ILE LEU GLY PHE GLY GLU          
SEQRES  29 B  481  ASP GLU LEU GLY GLU VAL TYR ILE LEU SER SER SER LYS          
SEQRES  30 B  481  SER MET THR GLN THR HIS ASN GLY LYS LEU TYR LYS ILE          
SEQRES  31 B  481  VAL ASP PRO LYS ARG PRO LEU MET PRO GLU GLU CYS ARG          
SEQRES  32 B  481  ALA THR VAL GLN PRO ALA GLN THR LEU THR SER GLU CYS          
SEQRES  33 B  481  SER ARG LEU CYS ARG ASN GLY TYR CYS THR PRO THR GLY          
SEQRES  34 B  481  LYS CYS CYS CYS SER PRO GLY TRP GLU GLY ASP PHE CYS          
SEQRES  35 B  481  ARG THR ALA LYS CYS GLU PRO ALA CYS ARG HIS GLY GLY          
SEQRES  36 B  481  VAL CYS VAL ARG PRO ASN LYS CYS LEU CYS LYS LYS GLY          
SEQRES  37 B  481  TYR LEU GLY PRO GLN CYS GLU HIS HIS HIS HIS HIS HIS          
SEQRES   1 H  169  GLY PHE GLY LYS ARG ARG HIS PRO LYS LYS LEU THR PRO          
SEQRES   2 H  169  LEU ALA TYR LYS GLN PHE ILE PRO ASN VAL ALA GLU LYS          
SEQRES   3 H  169  THR LEU GLY ALA SER GLY ARG TYR GLU GLY LYS ILE SER          
SEQRES   4 H  169  ARG ASN SER GLU ARG PHE LYS GLU LEU THR PRO ASN TYR          
SEQRES   5 H  169  ASN PRO ASP ILE ILE PHE LYS ASP GLU GLU ASN THR GLY          
SEQRES   6 H  169  ALA ASP ARG LEU MET THR GLN ARG CYS LYS ASP LYS LEU          
SEQRES   7 H  169  ASN ALA LEU ALA ILE SER VAL MET ASN GLN TRP PRO GLY          
SEQRES   8 H  169  VAL LYS LEU ARG VAL THR GLU GLY TRP ASP GLU ASP GLY          
SEQRES   9 H  169  HIS HIS SER GLU GLU SER LEU HIS TYR GLU GLY ARG ALA          
SEQRES  10 H  169  VAL ASP ILE THR THR SER ASP ARG ASP ARG SER LYS TYR          
SEQRES  11 H  169  GLY MET LEU ALA ARG LEU ALA VAL GLU ALA GLY PHE ASP          
SEQRES  12 H  169  TRP VAL TYR TYR GLU SER LYS ALA HIS ILE HIS CYS SER          
SEQRES  13 H  169  VAL LYS ALA GLU ASN SER VAL ALA ALA LYS SER GLY GLY          
HET     ZN  H 400       1                                                       
HET     CA  H 401       1                                                       
HET     CA  H 402       1                                                       
HET     ZN  A 902       1                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM      CA CALCIUM ION                                                      
FORMUL   4   ZN    2(ZN 2+)                                                     
FORMUL   5   CA    2(CA 2+)                                                     
HELIX    1   1 ASN A  292  GLY A  297  1                                   6    
HELIX    2   2 PRO A  361  GLY A  363  5                                   3    
HELIX    3   3 THR A  375  MET A  382  1                                   8    
HELIX    4   4 PRO A  591  ARG A  595  5                                   5    
HELIX    5   5 SER A  606  CYS A  612  1                                   7    
HELIX    6   6 ASN B  292  GLY B  297  1                                   6    
HELIX    7   7 THR B  375  GLU B  381  1                                   7    
HELIX    8   8 SER B  568  HIS B  575  1                                   8    
HELIX    9   9 PRO B  591  ARG B  595  5                                   5    
HELIX   10  10 SER B  606  CYS B  612  1                                   7    
HELIX   11  11 GLY H   93  ASP H   95  5                                   3    
HELIX   12  12 THR H   99  TRP H  117  1                                  19    
HELIX   13  13 ASP H  154  SER H  156  5                                   3    
HELIX   14  14 LYS H  157  GLY H  169  1                                  13    
SHEET    1   A 4 CYS A 218  LEU A 226  0                                        
SHEET    2   A 4 GLY A 577  VAL A 583 -1  O  VAL A 583   N  CYS A 218           
SHEET    3   A 4 VAL A 562  SER A 567 -1  N  ILE A 564   O  TYR A 580           
SHEET    4   A 4 HIS A 550  GLU A 556 -1  N  HIS A 550   O  SER A 567           
SHEET    1   B 4 PRO A 229  LEU A 233  0                                        
SHEET    2   B 4 LEU A 242  GLU A 246 -1  O  PHE A 243   N  LEU A 233           
SHEET    3   B 4 TYR A 250  LEU A 254 -1  O  LEU A 254   N  LEU A 242           
SHEET    4   B 4 LEU A 266  ASP A 267 -1  O  LEU A 266   N  VAL A 251           
SHEET    1   C 4 LEU A 284  PHE A 289  0                                        
SHEET    2   C 4 LYS A 298  THR A 305 -1  O  SER A 302   N  SER A 286           
SHEET    3   C 4 HIS A 317  VAL A 326 -1  O  ARG A 320   N  TYR A 303           
SHEET    4   C 4 VAL A 334  GLU A 347 -1  O  PHE A 342   N  VAL A 321           
SHEET    1   D 4 GLY A 354  PHE A 359  0                                        
SHEET    2   D 4 LEU A 365  LEU A 369 -1  O  TYR A 366   N  LEU A 358           
SHEET    3   D 4 SER A 391  LEU A 395 -1  O  LEU A 395   N  LEU A 365           
SHEET    4   D 4 VAL A 424  HIS A 427 -1  O  PHE A 425   N  VAL A 392           
SHEET    1   E 4 ALA A 436  ASP A 438  0                                        
SHEET    2   E 4 THR A 449  ASP A 454 -1  O  THR A 449   N  ASP A 438           
SHEET    3   E 4 SER A 462  GLN A 467 -1  O  ARG A 464   N  CYS A 452           
SHEET    4   E 4 LEU A 481  PHE A 483 -1  O  PHE A 483   N  ALA A 463           
SHEET    1   F 4 GLY A 493  VAL A 496  0                                        
SHEET    2   F 4 TYR A 509  GLY A 512 -1  O  VAL A 510   N  PHE A 495           
SHEET    3   F 4 PHE A 518  GLN A 523 -1  O  LEU A 519   N  PHE A 511           
SHEET    4   F 4 TRP A 530  GLU A 532 -1  O  GLN A 531   N  GLN A 522           
SHEET    1   G 2 TRP A 629  GLU A 630  0                                        
SHEET    2   G 2 THR A 636  ALA A 637 -1  O  THR A 636   N  GLU A 630           
SHEET    1   H 2 VAL A 648  ARG A 651  0                                        
SHEET    2   H 2 LYS A 654  LEU A 656 -1  O  LEU A 656   N  VAL A 648           
SHEET    1   I 4 CYS B 218  LEU B 226  0                                        
SHEET    2   I 4 GLY B 577  VAL B 583 -1  O  GLY B 577   N  LEU B 226           
SHEET    3   I 4 VAL B 562  SER B 567 -1  N  ILE B 564   O  TYR B 580           
SHEET    4   I 4 HIS B 550  GLU B 556 -1  N  LEU B 552   O  LEU B 565           
SHEET    1   J 4 PRO B 229  LEU B 233  0                                        
SHEET    2   J 4 LEU B 242  GLU B 246 -1  O  PHE B 243   N  LEU B 233           
SHEET    3   J 4 TYR B 250  LEU B 254 -1  O  TYR B 250   N  GLU B 246           
SHEET    4   J 4 LEU B 266  ASP B 267 -1  O  LEU B 266   N  VAL B 251           
SHEET    1   K 4 LEU B 284  PHE B 289  0                                        
SHEET    2   K 4 LYS B 298  THR B 305 -1  O  SER B 302   N  LEU B 285           
SHEET    3   K 4 HIS B 317  VAL B 326 -1  O  ARG B 320   N  TYR B 303           
SHEET    4   K 4 VAL B 334  GLU B 347 -1  O  ARG B 340   N  GLU B 323           
SHEET    1   L 4 GLY B 354  PHE B 359  0                                        
SHEET    2   L 4 LEU B 365  LEU B 369 -1  O  TYR B 366   N  LEU B 358           
SHEET    3   L 4 SER B 391  LEU B 395 -1  O  LEU B 395   N  LEU B 365           
SHEET    4   L 4 VAL B 424  HIS B 427 -1  O  PHE B 425   N  VAL B 392           
SHEET    1   M 4 ALA B 436  ASP B 438  0                                        
SHEET    2   M 4 THR B 449  ASP B 454 -1  O  THR B 449   N  ASP B 438           
SHEET    3   M 4 SER B 462  GLN B 467 -1  O  SER B 462   N  ASP B 454           
SHEET    4   M 4 LEU B 481  PHE B 483 -1  O  PHE B 483   N  ALA B 463           
SHEET    1   N 4 GLY B 493  VAL B 496  0                                        
SHEET    2   N 4 TYR B 509  GLY B 512 -1  O  VAL B 510   N  PHE B 495           
SHEET    3   N 4 PHE B 518  GLN B 523 -1  O  LEU B 519   N  PHE B 511           
SHEET    4   N 4 TRP B 530  LEU B 535 -1  O  LYS B 533   N  THR B 520           
SHEET    1   O 2 GLY B 615  CYS B 617  0                                        
SHEET    2   O 2 CYS B 623  CYS B 625 -1  O  CYS B 624   N  TYR B 616           
SHEET    1   P 2 TRP B 629  GLU B 630  0                                        
SHEET    2   P 2 THR B 636  ALA B 637 -1  O  THR B 636   N  GLU B 630           
SHEET    1   Q 2 VAL B 648  ARG B 651  0                                        
SHEET    2   Q 2 LYS B 654  LEU B 656 -1  O  LEU B 656   N  VAL B 648           
SHEET    1   R 6 PHE H  47  ILE H  48  0                                        
SHEET    2   R 6 TRP H 172  TYR H 174 -1  O  VAL H 173   N  ILE H  48           
SHEET    3   R 6 ILE H 181  SER H 184 -1  O  HIS H 182   N  TYR H 174           
SHEET    4   R 6 ALA H 145  THR H 150 -1  N  ILE H 148   O  ILE H 181           
SHEET    5   R 6 LEU H 122  GLU H 126 -1  N  ARG H 123   O  THR H 149           
SHEET    6   R 6 ILE H  84  PHE H  86  1  N  ILE H  85   O  VAL H 124           
SHEET    1   S 2 THR H  77  PRO H  78  0                                        
SHEET    2   S 2 LEU H  97  MET H  98 -1  O  MET H  98   N  THR H  77           
SSBOND   1 CYS A  216    CYS A  536                          1555   1555  2.04  
SSBOND   2 CYS A  218    CYS A  543                          1555   1555  2.04  
SSBOND   3 CYS A  402    CYS A  624                          1555   1555  2.03  
SSBOND   4 CYS A  435    CYS A  452                          1555   1555  2.04  
SSBOND   5 CYS A  500    CYS A  594                          1555   1555  2.03  
SSBOND   6 CYS A  608    CYS A  617                          1555   1555  2.04  
SSBOND   7 CYS A  612    CYS A  623                          1555   1555  2.04  
SSBOND   8 CYS A  625    CYS A  634                          1555   1555  2.03  
SSBOND   9 CYS A  639    CYS A  649                          1555   1555  2.04  
SSBOND  10 CYS A  643    CYS A  655                          1555   1555  2.03  
SSBOND  11 CYS A  657    CYS A  666                          1555   1555  2.04  
SSBOND  12 CYS B  216    CYS B  536                          1555   1555  2.04  
SSBOND  13 CYS B  218    CYS B  543                          1555   1555  2.05  
SSBOND  14 CYS B  402    CYS B  624                          1555   1555  2.03  
SSBOND  15 CYS B  435    CYS B  452                          1555   1555  2.03  
SSBOND  16 CYS B  500    CYS B  594                          1555   1555  2.04  
SSBOND  17 CYS B  608    CYS B  617                          1555   1555  2.03  
SSBOND  18 CYS B  612    CYS B  623                          1555   1555  2.04  
SSBOND  19 CYS B  625    CYS B  634                          1555   1555  2.02  
SSBOND  20 CYS B  639    CYS B  649                          1555   1555  2.04  
SSBOND  21 CYS B  643    CYS B  655                          1555   1555  2.05  
SSBOND  22 CYS B  657    CYS B  666                          1555   1555  2.03  
LINK         OD2 ASP B 383                ZN    ZN H 400     1555   1555  2.17  
LINK         OE1 GLU H  89                CA    CA H 401     1555   1555  2.33  
LINK         OE2 GLU H  89                CA    CA H 401     1555   1555  2.34  
LINK         OE1 GLU H  90                CA    CA H 401     1555   1555  2.34  
LINK         OE2 GLU H  90                CA    CA H 401     1555   1555  2.35  
LINK         OE2 GLU H  90                CA    CA H 402     1555   1555  2.33  
LINK         OD1 ASP H  95                CA    CA H 401     1555   1555  2.33  
LINK         OD2 ASP H  95                CA    CA H 401     1555   1555  2.33  
LINK         O   THR H 125                CA    CA H 401     1555   1555  2.36  
LINK         OE1 GLU H 126                CA    CA H 402     1555   1555  2.33  
LINK         OE2 GLU H 126                CA    CA H 401     1555   1555  2.34  
LINK         OE2 GLU H 126                CA    CA H 402     1555   1555  2.33  
LINK         OD1 ASP H 129                CA    CA H 402     1555   1555  2.32  
LINK         OD2 ASP H 131                CA    CA H 402     1555   1555  2.34  
LINK         NE2 HIS H 140                ZN    ZN H 400     1555   1555  2.07  
LINK         OD1 ASP H 147                ZN    ZN H 400     1555   1555  2.00  
LINK         ND1 HIS H 182                ZN    ZN H 400     1555   1555  2.07  
LINK         OD1 ASP A 383                ZN    ZN A 902     1555   1555  2.56  
CISPEP   1 ILE H   48    PRO H   49          0         3.29                     
SITE     1 AC1  4 ASP B 383  HIS H 140  ASP H 147  HIS H 182                    
SITE     1 AC2  5 GLU H  89  GLU H  90  ASP H  95  THR H 125                    
SITE     2 AC2  5 GLU H 126                                                     
SITE     1 AC3  4 GLU H  90  GLU H 126  ASP H 129  ASP H 131                    
SITE     1 AC4  1 ASP A 383                                                     
CRYST1  101.618  101.618  302.830  90.00  90.00 120.00 P 31 2 1     12          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.009841  0.005682  0.000000        0.00000                         
SCALE2      0.000000  0.011363  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003302        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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