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Database: PDB
Entry: 3LTF
LinkDB: 3LTF
Original site: 3LTF 
HEADER    TRANSFERASE/TRANSFERASE REGULATOR       15-FEB-10   3LTF              
TITLE     CRYSTAL STRUCTURE OF THE DROSOPHILA EPIDERMAL GROWTH FACTOR RECEPTOR  
TITLE    2 ECTODOMAIN IN COMPLEX WITH SPITZ                                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: EPIDERMAL GROWTH FACTOR RECEPTOR;                          
COMPND   3 CHAIN: A, C;                                                         
COMPND   4 FRAGMENT: ECTODOMAIN, RESIDUES 100-688;                              
COMPND   5 SYNONYM: GURKEN RECEPTOR, PROTEIN TORPEDO, DROSOPHILA RELATIVE OF    
COMPND   6 ERBB;                                                                
COMPND   7 EC: 2.7.10.-;                                                        
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MOL_ID: 2;                                                           
COMPND  10 MOLECULE: PROTEIN SPITZ;                                             
COMPND  11 CHAIN: D, B;                                                         
COMPND  12 FRAGMENT: EGF DOMAIN, RESIDUES 76-133;                               
COMPND  13 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: DROSOPHILA MELANOGASTER;                        
SOURCE   3 ORGANISM_COMMON: FRUIT FLY;                                          
SOURCE   4 ORGANISM_TAXID: 7227;                                                
SOURCE   5 GENE: EGFR, DMEL_CG10079, TORPEDO, DEGFR, C-ERBB, DER, TOP;          
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PFASTBAC;                                 
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 ORGANISM_SCIENTIFIC: DROSOPHILA MELANOGASTER;                        
SOURCE  12 ORGANISM_COMMON: FRUIT FLY;                                          
SOURCE  13 ORGANISM_TAXID: 7227;                                                
SOURCE  14 GENE: CG10334, SPI, SPITZ;                                           
SOURCE  15 EXPRESSION_SYSTEM: DROSOPHILA MELANOGASTER;                          
SOURCE  16 EXPRESSION_SYSTEM_COMMON: FRUIT FLY;                                 
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 7227;                                       
SOURCE  18 EXPRESSION_SYSTEM_CELL_LINE: SCHNEIDER 2(S2) CELLS;                  
SOURCE  19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  20 EXPRESSION_SYSTEM_PLASMID: PMT                                       
KEYWDS    RECEPTOR-LIGAND COMPLEX ECTODOMAIN CYSTEINE RICH DOMAIN EGF DOMAIN,   
KEYWDS   2 ATP-BINDING, KINASE, NUCLEOTIDE-BINDING, RECEPTOR, TRANSFERASE,      
KEYWDS   3 TYROSINE-PROTEIN KINASE, CELL MEMBRANE, DEVELOPMENTAL PROTEIN,       
KEYWDS   4 DIFFERENTIATION, DISULFIDE BOND, EGF-LIKE DOMAIN, ENDOPLASMIC        
KEYWDS   5 RETICULUM, GLYCOPROTEIN, GOLGI APPARATUS, MEMBRANE, NEUROGENESIS,    
KEYWDS   6 TRANSMEMBRANE, TRANSFERASE-TRANSFERASE REGULATOR COMPLEX             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.ALVARADO,D.E.KLEIN,M.A.LEMMON                                       
REVDAT   2   08-SEP-10 3LTF    1       JRNL                                     
REVDAT   1   25-AUG-10 3LTF    0                                                
JRNL        AUTH   D.ALVARADO,D.E.KLEIN,M.A.LEMMON                              
JRNL        TITL   STRUCTURAL BASIS FOR NEGATIVE COOPERATIVITY IN GROWTH FACTOR 
JRNL        TITL 2 BINDING TO AN EGF RECEPTOR.                                  
JRNL        REF    CELL(CAMBRIDGE,MASS.)         V. 142   568 2010              
JRNL        REFN                   ISSN 0092-8674                               
JRNL        PMID   20723758                                                     
JRNL        DOI    10.1016/J.CELL.2010.07.015                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0102                                      
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) : 3.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 40.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 41290                          
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) : 0.240                           
REMARK   3   R VALUE            (WORKING SET) : 0.237                           
REMARK   3   FREE R VALUE                     : 0.275                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.000                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 4589                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 3.20                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.28                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2983                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.00                       
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3210                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 343                          
REMARK   3   BIN FREE R VALUE                    : 0.3640                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 9014                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 199                                     
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 68.60                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 80.20                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.30000                                             
REMARK   3    B22 (A**2) : 0.38000                                              
REMARK   3    B33 (A**2) : -0.08000                                             
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  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 1.135         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.432         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.322         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 41.265        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.905                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.868                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  9495 ; 0.007 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 12928 ; 1.126 ; 1.972       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1161 ; 5.464 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   426 ;30.155 ;24.155       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1481 ;17.073 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    53 ;15.641 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1418 ; 0.079 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  7224 ; 0.004 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
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):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
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):  5809 ; 0.314 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  9340 ; 0.608 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3686 ; 0.740 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  3587 ; 1.374 ; 4.500       
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  : 4                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 4                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    -2        A   181                          
REMARK   3    RESIDUE RANGE :   A   182        A   302                          
REMARK   3    RESIDUE RANGE :   A   303        A   493                          
REMARK   3    RESIDUE RANGE :   A   494        A   526                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -8.3440  13.4434  27.4917              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0778 T22:   0.0147                                     
REMARK   3      T33:   0.0652 T12:   0.0046                                     
REMARK   3      T13:   0.0162 T23:  -0.0123                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1859 L22:   1.5396                                     
REMARK   3      L33:   2.0015 L12:  -0.7824                                     
REMARK   3      L13:  -0.3053 L23:   0.7950                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0632 S12:  -0.0513 S13:  -0.0609                       
REMARK   3      S21:  -0.0603 S22:   0.0350 S23:  -0.1212                       
REMARK   3      S31:  -0.2274 S32:  -0.0795 S33:  -0.0982                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 4                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C     0        C   181                          
REMARK   3    RESIDUE RANGE :   C   182        C   302                          
REMARK   3    RESIDUE RANGE :   C   303        C   493                          
REMARK   3    RESIDUE RANGE :   C   494        C   538                          
REMARK   3    ORIGIN FOR THE GROUP (A): -23.2535 -18.9564 -11.6831              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0948 T22:   0.0405                                     
REMARK   3      T33:   0.0412 T12:   0.0119                                     
REMARK   3      T13:  -0.0010 T23:  -0.0327                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4008 L22:   0.4369                                     
REMARK   3      L33:   1.0234 L12:   0.3935                                     
REMARK   3      L13:   0.4437 L23:   0.0231                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0249 S12:  -0.0413 S13:   0.1976                       
REMARK   3      S21:  -0.0801 S22:   0.0411 S23:  -0.0289                       
REMARK   3      S31:  -0.1312 S32:   0.0374 S33:  -0.0162                       
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 :   D     2        D    58                          
REMARK   3    ORIGIN FOR THE GROUP (A): -26.2170 -39.6269 -10.7283              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1027 T22:   0.2044                                     
REMARK   3      T33:   0.3144 T12:   0.0415                                     
REMARK   3      T13:  -0.0091 T23:  -0.0015                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0504 L22:   3.4325                                     
REMARK   3      L33:   3.7555 L12:   0.5462                                     
REMARK   3      L13:   0.5996 L23:  -2.8262                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2219 S12:   0.4109 S13:  -0.5334                       
REMARK   3      S21:  -0.0512 S22:  -0.3907 S23:  -0.4292                       
REMARK   3      S31:   0.4158 S32:   0.4650 S33:   0.1688                       
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     2        B    58                          
REMARK   3    ORIGIN FOR THE GROUP (A):   0.5167  33.5868  31.6403              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6025 T22:   0.2542                                     
REMARK   3      T33:   0.5241 T12:  -0.1182                                     
REMARK   3      T13:   0.0998 T23:  -0.1330                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.5176 L22:   3.5559                                     
REMARK   3      L33:   3.1332 L12:   0.8152                                     
REMARK   3      L13:   0.2316 L23:  -1.8436                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1780 S12:   0.2682 S13:   0.4099                       
REMARK   3      S21:  -0.1688 S22:   0.2007 S23:  -0.6121                       
REMARK   3      S31:  -0.6807 S32:   0.5318 S33:  -0.0227                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
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 3LTF COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-FEB-10.                  
REMARK 100 THE RCSB ID CODE IS RCSB057707.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 03-DEC-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.9                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : CHESS                              
REMARK 200  BEAMLINE                       : F1                                 
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.91790                            
REMARK 200  MONOCHROMATOR                  : HORIZONTAL BENT SI(111),           
REMARK 200                                   ASYMMETRICALLY CUT WITH WATER      
REMARK 200                                   COOLED CU BLOCK                    
REMARK 200  OPTICS                         : RH COATED SI MONOCHROMATIC         
REMARK 200                                   MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 270                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 45880                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.140                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.500                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 6.100                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.14700                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.8000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.34                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.20                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.56700                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.000                              
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: DEGFR DOMAINS I-IV (PDB ENTRY 3I2T)                  
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 73.16                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.58                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.5 M SODIUM POTASSIUM PHOSPHATE, PH     
REMARK 280  6.9 4% TERT-BUTANOL , VAPOR DIFFUSION, HANGING DROP, TEMPERATURE    
REMARK 280  294K                                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       59.10400            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       93.25400            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       62.11950            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       93.25400            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       59.10400            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       62.11950            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
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: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 15160 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 54680 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 3.0 KCAL/MOL                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     HIS A    -5                                                      
REMARK 465     HIS A    -4                                                      
REMARK 465     HIS A    -3                                                      
REMARK 465     VAL A    90                                                      
REMARK 465     GLU A    91                                                      
REMARK 465     TYR A   148                                                      
REMARK 465     ASN A   149                                                      
REMARK 465     TYR A   150                                                      
REMARK 465     ASP A   151                                                      
REMARK 465     PHE A   152                                                      
REMARK 465     THR A   153                                                      
REMARK 465     PRO A   526                                                      
REMARK 465     GLU A   527                                                      
REMARK 465     CYS A   528                                                      
REMARK 465     ARG A   529                                                      
REMARK 465     THR A   530                                                      
REMARK 465     GLY A   533                                                      
REMARK 465     ALA A   534                                                      
REMARK 465     GLY A   535                                                      
REMARK 465     ALA A   536                                                      
REMARK 465     ASP A   537                                                      
REMARK 465     HIS A   538                                                      
REMARK 465     CYS A   539                                                      
REMARK 465     GLN A   540                                                      
REMARK 465     GLU A   541                                                      
REMARK 465     CYS A   542                                                      
REMARK 465     VAL A   543                                                      
REMARK 465     HIS A   544                                                      
REMARK 465     VAL A   545                                                      
REMARK 465     ARG A   546                                                      
REMARK 465     ASP A   547                                                      
REMARK 465     GLY A   548                                                      
REMARK 465     GLN A   549                                                      
REMARK 465     HIS A   550                                                      
REMARK 465     CYS A   551                                                      
REMARK 465     VAL A   552                                                      
REMARK 465     SER A   553                                                      
REMARK 465     GLU A   554                                                      
REMARK 465     CYS A   555                                                      
REMARK 465     PRO A   556                                                      
REMARK 465     LYS A   557                                                      
REMARK 465     ASN A   558                                                      
REMARK 465     LYS A   559                                                      
REMARK 465     TYR A   560                                                      
REMARK 465     ASN A   561                                                      
REMARK 465     ASP A   562                                                      
REMARK 465     ARG A   563                                                      
REMARK 465     GLY A   564                                                      
REMARK 465     VAL A   565                                                      
REMARK 465     CYS A   566                                                      
REMARK 465     ARG A   567                                                      
REMARK 465     GLU A   568                                                      
REMARK 465     CYS A   569                                                      
REMARK 465     HIS A   570                                                      
REMARK 465     ALA A   571                                                      
REMARK 465     THR A   572                                                      
REMARK 465     CYS A   573                                                      
REMARK 465     ASP A   574                                                      
REMARK 465     GLY A   575                                                      
REMARK 465     CYS A   576                                                      
REMARK 465     THR A   577                                                      
REMARK 465     GLY A   578                                                      
REMARK 465     PRO A   579                                                      
REMARK 465     LYS A   580                                                      
REMARK 465     ASP A   581                                                      
REMARK 465     THR A   582                                                      
REMARK 465     ILE A   583                                                      
REMARK 465     GLY A   584                                                      
REMARK 465     ILE A   585                                                      
REMARK 465     GLY A   586                                                      
REMARK 465     ALA A   587                                                      
REMARK 465     CYS A   588                                                      
REMARK 465     THR A   589                                                      
REMARK 465     HIS A   590                                                      
REMARK 465     HIS A   591                                                      
REMARK 465     HIS A   592                                                      
REMARK 465     HIS A   593                                                      
REMARK 465     HIS A   594                                                      
REMARK 465     HIS A   595                                                      
REMARK 465     HIS C    -5                                                      
REMARK 465     HIS C    -4                                                      
REMARK 465     HIS C    -3                                                      
REMARK 465     HIS C    -2                                                      
REMARK 465     HIS C    -1                                                      
REMARK 465     THR C   144                                                      
REMARK 465     ASP C   145                                                      
REMARK 465     ALA C   146                                                      
REMARK 465     TYR C   147                                                      
REMARK 465     TYR C   148                                                      
REMARK 465     ASN C   149                                                      
REMARK 465     TYR C   150                                                      
REMARK 465     ASP C   151                                                      
REMARK 465     PHE C   152                                                      
REMARK 465     GLN C   540                                                      
REMARK 465     GLU C   541                                                      
REMARK 465     CYS C   542                                                      
REMARK 465     VAL C   543                                                      
REMARK 465     HIS C   544                                                      
REMARK 465     VAL C   545                                                      
REMARK 465     ARG C   546                                                      
REMARK 465     ASP C   547                                                      
REMARK 465     GLY C   548                                                      
REMARK 465     GLN C   549                                                      
REMARK 465     HIS C   550                                                      
REMARK 465     CYS C   551                                                      
REMARK 465     VAL C   552                                                      
REMARK 465     SER C   553                                                      
REMARK 465     GLU C   554                                                      
REMARK 465     CYS C   555                                                      
REMARK 465     PRO C   556                                                      
REMARK 465     LYS C   557                                                      
REMARK 465     ASN C   558                                                      
REMARK 465     LYS C   559                                                      
REMARK 465     TYR C   560                                                      
REMARK 465     ASN C   561                                                      
REMARK 465     ASP C   562                                                      
REMARK 465     ARG C   563                                                      
REMARK 465     GLY C   564                                                      
REMARK 465     VAL C   565                                                      
REMARK 465     CYS C   566                                                      
REMARK 465     ARG C   567                                                      
REMARK 465     GLU C   568                                                      
REMARK 465     CYS C   569                                                      
REMARK 465     HIS C   570                                                      
REMARK 465     ALA C   571                                                      
REMARK 465     THR C   572                                                      
REMARK 465     CYS C   573                                                      
REMARK 465     ASP C   574                                                      
REMARK 465     GLY C   575                                                      
REMARK 465     CYS C   576                                                      
REMARK 465     THR C   577                                                      
REMARK 465     GLY C   578                                                      
REMARK 465     PRO C   579                                                      
REMARK 465     LYS C   580                                                      
REMARK 465     ASP C   581                                                      
REMARK 465     THR C   582                                                      
REMARK 465     ILE C   583                                                      
REMARK 465     GLY C   584                                                      
REMARK 465     ILE C   585                                                      
REMARK 465     GLY C   586                                                      
REMARK 465     ALA C   587                                                      
REMARK 465     CYS C   588                                                      
REMARK 465     THR C   589                                                      
REMARK 465     HIS C   590                                                      
REMARK 465     HIS C   591                                                      
REMARK 465     HIS C   592                                                      
REMARK 465     HIS C   593                                                      
REMARK 465     HIS C   594                                                      
REMARK 465     HIS C   595                                                      
REMARK 465     THR D     1                                                      
REMARK 465     THR B     1                                                      
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     HIS A  -1    CG   ND1  CD2  CE1  NE2                             
REMARK 470     GLU A  17    CG   CD   OE1  OE2                                  
REMARK 470     LYS A  70    CG   CD   CE   NZ                                   
REMARK 470     GLU A  92    CG   CD   OE1  OE2                                  
REMARK 470     GLU A  93    CG   CD   OE1  OE2                                  
REMARK 470     ASN A 142    CG   OD1  ND2                                       
REMARK 470     TYR A 147    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     GLU A 156    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 157    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 161    CG   CD   CE   NZ                                   
REMARK 470     LYS A 286    CG   CD   CE   NZ                                   
REMARK 470     LYS A 289    CG   CD   CE   NZ                                   
REMARK 470     ARG A 319    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 350    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 480    CG   CD   OE1  OE2                                  
REMARK 470     PHE A 497    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ILE A 504    CG1  CG2  CD1                                       
REMARK 470     ASP A 506    CG   OD1  OD2                                       
REMARK 470     TYR A 509    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ILE A 510    CG1  CG2  CD1                                       
REMARK 470     ASN A 512    CG   OD1  ND2                                       
REMARK 470     LYS A 515    CG   CD   CE   NZ                                   
REMARK 470     ARG A 519    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 522    CG   CD   CE   NZ                                   
REMARK 470     ILE A 523    CG1  CG2  CD1                                       
REMARK 470     ASN A 532    CG   OD1  ND2                                       
REMARK 470     HIS C   0    CG   ND1  CD2  CE1  NE2                             
REMARK 470     GLU C  91    CG   CD   OE1  OE2                                  
REMARK 470     THR C 153    OG1  CG2                                            
REMARK 470     GLU C 158    CG   CD   OE1  OE2                                  
REMARK 470     GLU C 173    CG   CD   OE1  OE2                                  
REMARK 470     LYS C 176    CG   CD   CE   NZ                                   
REMARK 470     GLU C 266    CG   CD   OE1  OE2                                  
REMARK 470     LYS C 289    CG   CD   CE   NZ                                   
REMARK 470     ASN C 297    CG   OD1  ND2                                       
REMARK 470     LYS C 302    CG   CD   CE   NZ                                   
REMARK 470     GLU C 357    CG   CD   OE1  OE2                                  
REMARK 470     GLU C 453    CG   CD   OE1  OE2                                  
REMARK 470     GLU C 480    CG   CD   OE1  OE2                                  
REMARK 470     ILE C 510    CG1  CG2  CD1                                       
REMARK 470     ILE C 523    CG1  CG2  CD1                                       
REMARK 470     GLU C 527    CG   CD   OE1  OE2                                  
REMARK 470     ARG C 529    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     THR C 530    OG1  CG2                                            
REMARK 470     HIS C 538    CG   ND1  CD2  CE1  NE2                             
REMARK 470     PHE D   2    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ASP D  29    CG   OD1  OD2                                       
REMARK 470     ILE D  39    CG1  CG2  CD1                                       
REMARK 470     ASP B  29    CG   OD1  OD2                                       
REMARK 470     LEU B  30    CG   CD1  CD2                                       
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    HIS A   0      -90.13     64.48                                   
REMARK 500    SER A   8       93.92    -66.45                                   
REMARK 500    LEU A  10       19.94     55.67                                   
REMARK 500    ASN A  29       -4.44     63.42                                   
REMARK 500    TRP A  41       64.76     38.83                                   
REMARK 500    LEU A  49       35.86    -99.36                                   
REMARK 500    ILE A 109       72.17   -119.78                                   
REMARK 500    HIS A 130      -13.78     71.98                                   
REMARK 500    GLN A 135       80.28     68.07                                   
REMARK 500    HIS A 168      -51.55   -133.51                                   
REMARK 500    THR A 185       37.45    -91.32                                   
REMARK 500    GLN A 189       -1.85    -58.93                                   
REMARK 500    CYS A 212      149.31    166.47                                   
REMARK 500    ASN A 225     -121.29   -113.09                                   
REMARK 500    LYS A 302      105.86    -55.41                                   
REMARK 500    TYR A 345       -0.74     81.80                                   
REMARK 500    GLU A 360        0.30    -67.96                                   
REMARK 500    SER A 412       49.70    -98.41                                   
REMARK 500    ARG A 419     -175.96    -66.01                                   
REMARK 500    ASN A 420      -22.08     66.24                                   
REMARK 500    LEU A 421       90.42    -66.45                                   
REMARK 500    CYS A 438      -70.76   -111.48                                   
REMARK 500    ASN A 461     -156.13    -78.99                                   
REMARK 500    THR A 472       72.64    -68.58                                   
REMARK 500    ASP A 476       12.56    -63.63                                   
REMARK 500    ASN A 496     -131.59   -113.17                                   
REMARK 500    ASN A 500     -120.00     66.07                                   
REMARK 500    SER A 511     -131.40     42.92                                   
REMARK 500    LYS C   7       44.37   -156.70                                   
REMARK 500    ARG C   9     -132.00     61.08                                   
REMARK 500    ASN C  29       14.27     59.34                                   
REMARK 500    ILE C 109       61.81   -118.50                                   
REMARK 500    ASP C 111      -12.00     73.87                                   
REMARK 500    HIS C 130       -4.66     80.45                                   
REMARK 500    ALA C 154       71.53     32.63                                   
REMARK 500    HIS C 168     -123.93   -108.27                                   
REMARK 500    ARG C 201       -0.38     93.23                                   
REMARK 500    GLU C 202       41.02   -108.54                                   
REMARK 500    CYS C 212      149.31    169.66                                   
REMARK 500    ASP C 219       40.55    -85.75                                   
REMARK 500    ASN C 225      -81.79   -112.38                                   
REMARK 500    TYR C 247       85.32    -66.44                                   
REMARK 500    ASN C 275      -54.52    -24.02                                   
REMARK 500    LYS C 302      117.17    -36.52                                   
REMARK 500    GLU C 400      179.20     64.00                                   
REMARK 500    LEU C 421      101.42    -57.80                                   
REMARK 500    TYR C 439      -36.20     73.52                                   
REMARK 500    ASN C 496      -88.26   -130.33                                   
REMARK 500    SER C 511      -62.77     56.39                                   
REMARK 500    PRO C 526      -25.25    -37.96                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      52 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 4700                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 4701                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 4702                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 4703                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 4704                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 4705                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 596                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 3830                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 3440                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 3830                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 3831                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 4700                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 4701                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN C 4702                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN C 4703                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MLI A 596                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3I2T   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE INACTIVE DROSOPHILA EPIDERMAL               
REMARK 900 GROWTH FACTOR RECEPTOR ECTODOMAIN.                                   
REMARK 900 RELATED ID: 3LTG   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE DROSOPHILA EPIDERMAL GROWTH FACTOR          
REMARK 900 RECEPTOR ECTODOMAIN COMPLEXED WITH A LOW AFFINITY SPITZ              
REMARK 900 MUTANT.                                                              
DBREF  3LTF A    1   589  UNP    P04412   P04412_DROME   100    688             
DBREF  3LTF C    1   589  UNP    P04412   P04412_DROME   100    688             
DBREF  3LTF D    1    58  UNP    Q01083   SPITZ_DROME     76    133             
DBREF  3LTF B    1    58  UNP    Q01083   SPITZ_DROME     76    133             
SEQADV 3LTF HIS A   -5  UNP  P04412              EXPRESSION TAG                 
SEQADV 3LTF HIS A   -4  UNP  P04412              EXPRESSION TAG                 
SEQADV 3LTF HIS A   -3  UNP  P04412              EXPRESSION TAG                 
SEQADV 3LTF HIS A   -2  UNP  P04412              EXPRESSION TAG                 
SEQADV 3LTF HIS A   -1  UNP  P04412              EXPRESSION TAG                 
SEQADV 3LTF HIS A    0  UNP  P04412              EXPRESSION TAG                 
SEQADV 3LTF GLU A   38  UNP  P04412    LYS   137 CONFLICT                       
SEQADV 3LTF GLY A  230  UNP  P04412    ALA   329 CONFLICT                       
SEQADV 3LTF CYS A  232  UNP  P04412    SER   331 CONFLICT                       
SEQADV 3LTF LEU A  359  UNP  P04412    ARG   458 CONFLICT                       
SEQADV 3LTF ASN A  493  UNP  P04412    THR   592 CONFLICT                       
SEQADV 3LTF HIS A  590  UNP  P04412              EXPRESSION TAG                 
SEQADV 3LTF HIS A  591  UNP  P04412              EXPRESSION TAG                 
SEQADV 3LTF HIS A  592  UNP  P04412              EXPRESSION TAG                 
SEQADV 3LTF HIS A  593  UNP  P04412              EXPRESSION TAG                 
SEQADV 3LTF HIS A  594  UNP  P04412              EXPRESSION TAG                 
SEQADV 3LTF HIS A  595  UNP  P04412              EXPRESSION TAG                 
SEQADV 3LTF HIS C   -5  UNP  P04412              EXPRESSION TAG                 
SEQADV 3LTF HIS C   -4  UNP  P04412              EXPRESSION TAG                 
SEQADV 3LTF HIS C   -3  UNP  P04412              EXPRESSION TAG                 
SEQADV 3LTF HIS C   -2  UNP  P04412              EXPRESSION TAG                 
SEQADV 3LTF HIS C   -1  UNP  P04412              EXPRESSION TAG                 
SEQADV 3LTF HIS C    0  UNP  P04412              EXPRESSION TAG                 
SEQADV 3LTF GLU C   38  UNP  P04412    LYS   137 CONFLICT                       
SEQADV 3LTF GLY C  230  UNP  P04412    ALA   329 CONFLICT                       
SEQADV 3LTF CYS C  232  UNP  P04412    SER   331 CONFLICT                       
SEQADV 3LTF LEU C  359  UNP  P04412    ARG   458 CONFLICT                       
SEQADV 3LTF ASN C  493  UNP  P04412    THR   592 CONFLICT                       
SEQADV 3LTF HIS C  590  UNP  P04412              EXPRESSION TAG                 
SEQADV 3LTF HIS C  591  UNP  P04412              EXPRESSION TAG                 
SEQADV 3LTF HIS C  592  UNP  P04412              EXPRESSION TAG                 
SEQADV 3LTF HIS C  593  UNP  P04412              EXPRESSION TAG                 
SEQADV 3LTF HIS C  594  UNP  P04412              EXPRESSION TAG                 
SEQADV 3LTF HIS C  595  UNP  P04412              EXPRESSION TAG                 
SEQRES   1 A  601  HIS HIS HIS HIS HIS HIS LYS ILE CYS ILE GLY THR LYS          
SEQRES   2 A  601  SER ARG LEU SER VAL PRO SER ASN LYS GLU HIS HIS TYR          
SEQRES   3 A  601  ARG ASN LEU ARG ASP ARG TYR THR ASN CYS THR TYR VAL          
SEQRES   4 A  601  ASP GLY ASN LEU GLU LEU THR TRP LEU PRO ASN GLU ASN          
SEQRES   5 A  601  LEU ASP LEU SER PHE LEU ASP ASN ILE ARG GLU VAL THR          
SEQRES   6 A  601  GLY TYR ILE LEU ILE SER HIS VAL ASP VAL LYS LYS VAL          
SEQRES   7 A  601  VAL PHE PRO LYS LEU GLN ILE ILE ARG GLY ARG THR LEU          
SEQRES   8 A  601  PHE SER LEU SER VAL GLU GLU GLU LYS TYR ALA LEU PHE          
SEQRES   9 A  601  VAL THR TYR SER LYS MET TYR THR LEU GLU ILE PRO ASP          
SEQRES  10 A  601  LEU ARG ASP VAL LEU ASN GLY GLN VAL GLY PHE HIS ASN          
SEQRES  11 A  601  ASN TYR ASN LEU CYS HIS MET ARG THR ILE GLN TRP SER          
SEQRES  12 A  601  GLU ILE VAL SER ASN GLY THR ASP ALA TYR TYR ASN TYR          
SEQRES  13 A  601  ASP PHE THR ALA PRO GLU ARG GLU CYS PRO LYS CYS HIS          
SEQRES  14 A  601  GLU SER CYS THR HIS GLY CYS TRP GLY GLU GLY PRO LYS          
SEQRES  15 A  601  ASN CYS GLN LYS PHE SER LYS LEU THR CYS SER PRO GLN          
SEQRES  16 A  601  CYS ALA GLY GLY ARG CYS TYR GLY PRO LYS PRO ARG GLU          
SEQRES  17 A  601  CYS CYS HIS LEU PHE CYS ALA GLY GLY CYS THR GLY PRO          
SEQRES  18 A  601  THR GLN LYS ASP CYS ILE ALA CYS LYS ASN PHE PHE ASP          
SEQRES  19 A  601  GLU GLY VAL CYS LYS GLU GLU CYS PRO PRO MET ARG LYS          
SEQRES  20 A  601  TYR ASN PRO THR THR TYR VAL LEU GLU THR ASN PRO GLU          
SEQRES  21 A  601  GLY LYS TYR ALA TYR GLY ALA THR CYS VAL LYS GLU CYS          
SEQRES  22 A  601  PRO GLY HIS LEU LEU ARG ASP ASN GLY ALA CYS VAL ARG          
SEQRES  23 A  601  SER CYS PRO GLN ASP LYS MET ASP LYS GLY GLY GLU CYS          
SEQRES  24 A  601  VAL PRO CYS ASN GLY PRO CYS PRO LYS THR CYS PRO GLY          
SEQRES  25 A  601  VAL THR VAL LEU HIS ALA GLY ASN ILE ASP SER PHE ARG          
SEQRES  26 A  601  ASN CYS THR VAL ILE ASP GLY ASN ILE ARG ILE LEU ASP          
SEQRES  27 A  601  GLN THR PHE SER GLY PHE GLN ASP VAL TYR ALA ASN TYR          
SEQRES  28 A  601  THR MET GLY PRO ARG TYR ILE PRO LEU ASP PRO GLU ARG          
SEQRES  29 A  601  LEU GLU VAL PHE SER THR VAL LYS GLU ILE THR GLY TYR          
SEQRES  30 A  601  LEU ASN ILE GLU GLY THR HIS PRO GLN PHE ARG ASN LEU          
SEQRES  31 A  601  SER TYR PHE ARG ASN LEU GLU THR ILE HIS GLY ARG GLN          
SEQRES  32 A  601  LEU MET GLU SER MET PHE ALA ALA LEU ALA ILE VAL LYS          
SEQRES  33 A  601  SER SER LEU TYR SER LEU GLU MET ARG ASN LEU LYS GLN          
SEQRES  34 A  601  ILE SER SER GLY SER VAL VAL ILE GLN HIS ASN ARG ASP          
SEQRES  35 A  601  LEU CYS TYR VAL SER ASN ILE ARG TRP PRO ALA ILE GLN          
SEQRES  36 A  601  LYS GLU PRO GLU GLN LYS VAL TRP VAL ASN GLU ASN LEU          
SEQRES  37 A  601  ARG ALA ASP LEU CYS GLU LYS ASN GLY THR ILE CYS SER          
SEQRES  38 A  601  ASP GLN CYS ASN GLU ASP GLY CYS TRP GLY ALA GLY THR          
SEQRES  39 A  601  ASP GLN CYS LEU ASN CYS LYS ASN PHE ASN PHE ASN GLY          
SEQRES  40 A  601  THR CYS ILE ALA ASP CYS GLY TYR ILE SER ASN ALA TYR          
SEQRES  41 A  601  LYS PHE ASP ASN ARG THR CYS LYS ILE CYS HIS PRO GLU          
SEQRES  42 A  601  CYS ARG THR CYS ASN GLY ALA GLY ALA ASP HIS CYS GLN          
SEQRES  43 A  601  GLU CYS VAL HIS VAL ARG ASP GLY GLN HIS CYS VAL SER          
SEQRES  44 A  601  GLU CYS PRO LYS ASN LYS TYR ASN ASP ARG GLY VAL CYS          
SEQRES  45 A  601  ARG GLU CYS HIS ALA THR CYS ASP GLY CYS THR GLY PRO          
SEQRES  46 A  601  LYS ASP THR ILE GLY ILE GLY ALA CYS THR HIS HIS HIS          
SEQRES  47 A  601  HIS HIS HIS                                                  
SEQRES   1 C  601  HIS HIS HIS HIS HIS HIS LYS ILE CYS ILE GLY THR LYS          
SEQRES   2 C  601  SER ARG LEU SER VAL PRO SER ASN LYS GLU HIS HIS TYR          
SEQRES   3 C  601  ARG ASN LEU ARG ASP ARG TYR THR ASN CYS THR TYR VAL          
SEQRES   4 C  601  ASP GLY ASN LEU GLU LEU THR TRP LEU PRO ASN GLU ASN          
SEQRES   5 C  601  LEU ASP LEU SER PHE LEU ASP ASN ILE ARG GLU VAL THR          
SEQRES   6 C  601  GLY TYR ILE LEU ILE SER HIS VAL ASP VAL LYS LYS VAL          
SEQRES   7 C  601  VAL PHE PRO LYS LEU GLN ILE ILE ARG GLY ARG THR LEU          
SEQRES   8 C  601  PHE SER LEU SER VAL GLU GLU GLU LYS TYR ALA LEU PHE          
SEQRES   9 C  601  VAL THR TYR SER LYS MET TYR THR LEU GLU ILE PRO ASP          
SEQRES  10 C  601  LEU ARG ASP VAL LEU ASN GLY GLN VAL GLY PHE HIS ASN          
SEQRES  11 C  601  ASN TYR ASN LEU CYS HIS MET ARG THR ILE GLN TRP SER          
SEQRES  12 C  601  GLU ILE VAL SER ASN GLY THR ASP ALA TYR TYR ASN TYR          
SEQRES  13 C  601  ASP PHE THR ALA PRO GLU ARG GLU CYS PRO LYS CYS HIS          
SEQRES  14 C  601  GLU SER CYS THR HIS GLY CYS TRP GLY GLU GLY PRO LYS          
SEQRES  15 C  601  ASN CYS GLN LYS PHE SER LYS LEU THR CYS SER PRO GLN          
SEQRES  16 C  601  CYS ALA GLY GLY ARG CYS TYR GLY PRO LYS PRO ARG GLU          
SEQRES  17 C  601  CYS CYS HIS LEU PHE CYS ALA GLY GLY CYS THR GLY PRO          
SEQRES  18 C  601  THR GLN LYS ASP CYS ILE ALA CYS LYS ASN PHE PHE ASP          
SEQRES  19 C  601  GLU GLY VAL CYS LYS GLU GLU CYS PRO PRO MET ARG LYS          
SEQRES  20 C  601  TYR ASN PRO THR THR TYR VAL LEU GLU THR ASN PRO GLU          
SEQRES  21 C  601  GLY LYS TYR ALA TYR GLY ALA THR CYS VAL LYS GLU CYS          
SEQRES  22 C  601  PRO GLY HIS LEU LEU ARG ASP ASN GLY ALA CYS VAL ARG          
SEQRES  23 C  601  SER CYS PRO GLN ASP LYS MET ASP LYS GLY GLY GLU CYS          
SEQRES  24 C  601  VAL PRO CYS ASN GLY PRO CYS PRO LYS THR CYS PRO GLY          
SEQRES  25 C  601  VAL THR VAL LEU HIS ALA GLY ASN ILE ASP SER PHE ARG          
SEQRES  26 C  601  ASN CYS THR VAL ILE ASP GLY ASN ILE ARG ILE LEU ASP          
SEQRES  27 C  601  GLN THR PHE SER GLY PHE GLN ASP VAL TYR ALA ASN TYR          
SEQRES  28 C  601  THR MET GLY PRO ARG TYR ILE PRO LEU ASP PRO GLU ARG          
SEQRES  29 C  601  LEU GLU VAL PHE SER THR VAL LYS GLU ILE THR GLY TYR          
SEQRES  30 C  601  LEU ASN ILE GLU GLY THR HIS PRO GLN PHE ARG ASN LEU          
SEQRES  31 C  601  SER TYR PHE ARG ASN LEU GLU THR ILE HIS GLY ARG GLN          
SEQRES  32 C  601  LEU MET GLU SER MET PHE ALA ALA LEU ALA ILE VAL LYS          
SEQRES  33 C  601  SER SER LEU TYR SER LEU GLU MET ARG ASN LEU LYS GLN          
SEQRES  34 C  601  ILE SER SER GLY SER VAL VAL ILE GLN HIS ASN ARG ASP          
SEQRES  35 C  601  LEU CYS TYR VAL SER ASN ILE ARG TRP PRO ALA ILE GLN          
SEQRES  36 C  601  LYS GLU PRO GLU GLN LYS VAL TRP VAL ASN GLU ASN LEU          
SEQRES  37 C  601  ARG ALA ASP LEU CYS GLU LYS ASN GLY THR ILE CYS SER          
SEQRES  38 C  601  ASP GLN CYS ASN GLU ASP GLY CYS TRP GLY ALA GLY THR          
SEQRES  39 C  601  ASP GLN CYS LEU ASN CYS LYS ASN PHE ASN PHE ASN GLY          
SEQRES  40 C  601  THR CYS ILE ALA ASP CYS GLY TYR ILE SER ASN ALA TYR          
SEQRES  41 C  601  LYS PHE ASP ASN ARG THR CYS LYS ILE CYS HIS PRO GLU          
SEQRES  42 C  601  CYS ARG THR CYS ASN GLY ALA GLY ALA ASP HIS CYS GLN          
SEQRES  43 C  601  GLU CYS VAL HIS VAL ARG ASP GLY GLN HIS CYS VAL SER          
SEQRES  44 C  601  GLU CYS PRO LYS ASN LYS TYR ASN ASP ARG GLY VAL CYS          
SEQRES  45 C  601  ARG GLU CYS HIS ALA THR CYS ASP GLY CYS THR GLY PRO          
SEQRES  46 C  601  LYS ASP THR ILE GLY ILE GLY ALA CYS THR HIS HIS HIS          
SEQRES  47 C  601  HIS HIS HIS                                                  
SEQRES   1 D   58  THR PHE PRO THR TYR LYS CYS PRO GLU THR PHE ASP ALA          
SEQRES   2 D   58  TRP TYR CYS LEU ASN ASP ALA HIS CYS PHE ALA VAL LYS          
SEQRES   3 D   58  ILE ALA ASP LEU PRO VAL TYR SER CYS GLU CYS ALA ILE          
SEQRES   4 D   58  GLY PHE MET GLY GLN ARG CYS GLU TYR LYS GLU ILE ASP          
SEQRES   5 D   58  ASN THR TYR LEU PRO LYS                                      
SEQRES   1 B   58  THR PHE PRO THR TYR LYS CYS PRO GLU THR PHE ASP ALA          
SEQRES   2 B   58  TRP TYR CYS LEU ASN ASP ALA HIS CYS PHE ALA VAL LYS          
SEQRES   3 B   58  ILE ALA ASP LEU PRO VAL TYR SER CYS GLU CYS ALA ILE          
SEQRES   4 B   58  GLY PHE MET GLY GLN ARG CYS GLU TYR LYS GLU ILE ASP          
SEQRES   5 B   58  ASN THR TYR LEU PRO LYS                                      
MODRES 3LTF ASN A  470  ASN  GLYCOSYLATION SITE                                 
MODRES 3LTF ASN C  383  ASN  GLYCOSYLATION SITE                                 
MODRES 3LTF ASN C  470  ASN  GLYCOSYLATION SITE                                 
MODRES 3LTF ASN C   29  ASN  GLYCOSYLATION SITE                                 
MODRES 3LTF ASN C  344  ASN  GLYCOSYLATION SITE                                 
MODRES 3LTF ASN A  383  ASN  GLYCOSYLATION SITE                                 
HET    NAG  A4700      14                                                       
HET    NAG  A4701      14                                                       
HET    MAN  A4702      11                                                       
HET    MAN  A4703      11                                                       
HET    MAN  A4704      11                                                       
HET    MAN  A4705      11                                                       
HET    NAG  C 596      14                                                       
HET    NAG  A3830      14                                                       
HET    NAG  C3440      14                                                       
HET    NAG  C3830      14                                                       
HET    NAG  C3831      14                                                       
HET    NAG  C4700      14                                                       
HET    NAG  C4701      14                                                       
HET    MAN  C4702      11                                                       
HET    MAN  C4703      11                                                       
HET    MLI  A 596       7                                                       
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     MAN ALPHA-D-MANNOSE                                                  
HETNAM     MLI MALONATE ION                                                     
FORMUL   5  NAG    9(C8 H15 N O6)                                               
FORMUL   5  MAN    6(C6 H12 O6)                                                 
FORMUL  11  MLI    C3 H2 O4 2-                                                  
HELIX    1   1 ASN A   15  THR A   28  1                                  14    
HELIX    2   2 LEU A   49  ASN A   54  5                                   6    
HELIX    3   3 HIS A  130  ILE A  134  5                                   5    
HELIX    4   4 GLY A  174  CYS A  178  5                                   5    
HELIX    5   5 SER A  187  ALA A  191  5                                   5    
HELIX    6   6 HIS A  311  ASP A  316  1                                   6    
HELIX    7   7 SER A  317  ARG A  319  5                                   3    
HELIX    8   8 LEU A  331  GLY A  337  1                                   7    
HELIX    9   9 ASP A  355  VAL A  365  5                                  11    
HELIX   10  10 LEU A  384  ARG A  388  5                                   5    
HELIX   11  11 CYS A  438  ASN A  442  5                                   5    
HELIX   12  12 ARG A  444  ILE A  448  5                                   5    
HELIX   13  13 ARG A  463  GLY A  471  1                                   9    
HELIX   14  14 ASN C   15  THR C   28  1                                  14    
HELIX   15  15 LEU C   49  ASP C   53  5                                   5    
HELIX   16  16 SER C  187  ALA C  191  5                                   5    
HELIX   17  17 ASN C  314  ARG C  319  5                                   6    
HELIX   18  18 LEU C  331  GLY C  337  1                                   7    
HELIX   19  19 ASP C  355  VAL C  365  5                                  11    
HELIX   20  20 LEU C  384  ARG C  388  5                                   5    
HELIX   21  21 ARG C  444  ILE C  448  5                                   5    
HELIX   22  22 ARG C  463  GLY C  471  1                                   9    
HELIX   23  23 PRO D    8  TYR D   15  1                                   8    
HELIX   24  24 PRO B    8  TYR B   15  1                                   8    
SHEET    1   A 5 ILE A   2  ILE A   4  0                                        
SHEET    2   A 5 TYR A  32  ASP A  34  1  O  ASP A  34   N  CYS A   3           
SHEET    3   A 5 GLU A  57  VAL A  58  1  O  GLU A  57   N  VAL A  33           
SHEET    4   A 5 ILE A  79  ILE A  80  1  O  ILE A  79   N  VAL A  58           
SHEET    5   A 5 ASP A 114  VAL A 115  1  O  ASP A 114   N  ILE A  80           
SHEET    1   B 4 LEU A  37  LEU A  42  0                                        
SHEET    2   B 4 ILE A  62  VAL A  67  1  O  LEU A  63   N  LEU A  39           
SHEET    3   B 4 TYR A  95  THR A 100  1  O  ALA A  96   N  ILE A  62           
SHEET    4   B 4 GLN A 119  HIS A 123  1  O  GLN A 119   N  ALA A  96           
SHEET    1   C 2 LYS A  71  VAL A  73  0                                        
SHEET    2   C 2 THR A 106  GLU A 108  1  O  GLU A 108   N  VAL A  72           
SHEET    1   D 2 CYS A 208  CYS A 212  0                                        
SHEET    2   D 2 CYS A 220  CYS A 223 -1  O  ALA A 222   N  ALA A 209           
SHEET    1   E 2 PHE A 226  ASP A 228  0                                        
SHEET    2   E 2 VAL A 231  LYS A 233 -1  O  VAL A 231   N  ASP A 228           
SHEET    1   F 2 ARG A 240  ASN A 243  0                                        
SHEET    2   F 2 VAL A 248  THR A 251 -1  O  VAL A 248   N  ASN A 243           
SHEET    1   G 2 TYR A 257  TYR A 259  0                                        
SHEET    2   G 2 THR A 262  VAL A 264 -1  O  THR A 262   N  TYR A 259           
SHEET    1   H 2 LEU A 272  ASP A 274  0                                        
SHEET    2   H 2 ALA A 277  VAL A 279 -1  O  VAL A 279   N  LEU A 272           
SHEET    1   I 2 LYS A 286  LYS A 289  0                                        
SHEET    2   I 2 GLU A 292  PRO A 295 -1  O  VAL A 294   N  MET A 287           
SHEET    1   J 5 THR A 303  PRO A 305  0                                        
SHEET    2   J 5 VAL A 323  ASP A 325  1  O  ASP A 325   N  CYS A 304           
SHEET    3   J 5 GLU A 367  ILE A 368  1  O  GLU A 367   N  ILE A 324           
SHEET    4   J 5 THR A 392  HIS A 394  1  O  HIS A 394   N  ILE A 368           
SHEET    5   J 5 GLN A 423  SER A 425  1  O  GLN A 423   N  ILE A 393           
SHEET    1   K 5 ILE A 328  ILE A 330  0                                        
SHEET    2   K 5 LEU A 372  ILE A 374  1  O  ASN A 373   N  ILE A 328           
SHEET    3   K 5 ALA A 404  VAL A 409  1  O  ALA A 405   N  LEU A 372           
SHEET    4   K 5 SER A 428  GLN A 432  1  O  SER A 428   N  ALA A 405           
SHEET    5   K 5 VAL A 456  ASN A 459  1  O  TRP A 457   N  ILE A 431           
SHEET    1   L 2 GLN A 339  VAL A 341  0                                        
SHEET    2   L 2 MET A 347  ARG A 350 -1  O  GLY A 348   N  ASP A 340           
SHEET    1   M 4 THR A 502  ILE A 504  0                                        
SHEET    2   M 4 PHE A 497  PHE A 499 -1  N  PHE A 499   O  THR A 502           
SHEET    3   M 4 THR A 520  ILE A 523  1  O  CYS A 521   N  ASN A 498           
SHEET    4   M 4 ALA A 513  TYR A 514 -1  N  TYR A 514   O  LYS A 522           
SHEET    1   N 5 ILE C   2  ILE C   4  0                                        
SHEET    2   N 5 TYR C  32  ASP C  34  1  O  ASP C  34   N  CYS C   3           
SHEET    3   N 5 GLU C  57  VAL C  58  1  O  GLU C  57   N  VAL C  33           
SHEET    4   N 5 ILE C  79  ILE C  80  1  O  ILE C  79   N  VAL C  58           
SHEET    5   N 5 ASP C 114  VAL C 115  1  O  ASP C 114   N  ILE C  80           
SHEET    1   O 3 VAL C  12  PRO C  13  0                                        
SHEET    2   O 3 LEU D  30  CYS D  37  1  O  CYS D  37   N  VAL C  12           
SHEET    3   O 3 HIS D  21  ILE D  27 -1  N  VAL D  25   O  VAL D  32           
SHEET    1   P 4 LEU C  37  LEU C  42  0                                        
SHEET    2   P 4 ILE C  62  VAL C  67  1  O  LEU C  63   N  LEU C  39           
SHEET    3   P 4 TYR C  95  THR C 100  1  O  ALA C  96   N  ILE C  62           
SHEET    4   P 4 GLN C 119  HIS C 123  1  O  GLN C 119   N  ALA C  96           
SHEET    1   Q 2 LYS C  71  VAL C  73  0                                        
SHEET    2   Q 2 THR C 106  GLU C 108  1  O  GLU C 108   N  VAL C  72           
SHEET    1   R 2 CYS C 208  CYS C 212  0                                        
SHEET    2   R 2 CYS C 220  CYS C 223 -1  O  ALA C 222   N  ALA C 209           
SHEET    1   S 2 PHE C 226  ASP C 228  0                                        
SHEET    2   S 2 VAL C 231  LYS C 233 -1  O  LYS C 233   N  PHE C 226           
SHEET    1   T 2 ARG C 240  ASN C 243  0                                        
SHEET    2   T 2 VAL C 248  THR C 251 -1  O  GLU C 250   N  LYS C 241           
SHEET    1   U 2 TYR C 257  TYR C 259  0                                        
SHEET    2   U 2 THR C 262  VAL C 264 -1  O  THR C 262   N  TYR C 259           
SHEET    1   V 2 LEU C 272  ASP C 274  0                                        
SHEET    2   V 2 ALA C 277  VAL C 279 -1  O  VAL C 279   N  LEU C 272           
SHEET    1   W 2 LYS C 286  LYS C 289  0                                        
SHEET    2   W 2 GLU C 292  PRO C 295 -1  O  VAL C 294   N  MET C 287           
SHEET    1   X 4 VAL C 323  ILE C 324  0                                        
SHEET    2   X 4 GLU C 367  ILE C 368  1  O  GLU C 367   N  ILE C 324           
SHEET    3   X 4 THR C 392  ILE C 393  1  O  THR C 392   N  ILE C 368           
SHEET    4   X 4 GLN C 423  ILE C 424  1  O  GLN C 423   N  ILE C 393           
SHEET    1   Y 5 ILE C 328  ILE C 330  0                                        
SHEET    2   Y 5 LEU C 372  ILE C 374  1  O  ASN C 373   N  ILE C 328           
SHEET    3   Y 5 ALA C 404  VAL C 409  1  O  ALA C 407   N  ILE C 374           
SHEET    4   Y 5 SER C 428  GLN C 432  1  O  SER C 428   N  ALA C 405           
SHEET    5   Y 5 VAL C 456  ASN C 459  1  O  TRP C 457   N  ILE C 431           
SHEET    1   Z 2 PHE C 338  VAL C 341  0                                        
SHEET    2   Z 2 MET C 347  TYR C 351 -1  O  GLY C 348   N  ASP C 340           
SHEET    1  AA 2 PHE C 497  PHE C 499  0                                        
SHEET    2  AA 2 THR C 502  ILE C 504 -1  O  THR C 502   N  PHE C 499           
SHEET    1  AB 2 ALA C 513  ASP C 517  0                                        
SHEET    2  AB 2 THR C 520  ILE C 523 -1  O  LYS C 522   N  TYR C 514           
SHEET    1  AC 2 PHE D  41  MET D  42  0                                        
SHEET    2  AC 2 TYR D  48  LYS D  49 -1  O  TYR D  48   N  MET D  42           
SHEET    1  AD 2 HIS B  21  LYS B  26  0                                        
SHEET    2  AD 2 PRO B  31  GLU B  36 -1  O  VAL B  32   N  VAL B  25           
SHEET    1  AE 2 PHE B  41  MET B  42  0                                        
SHEET    2  AE 2 TYR B  48  LYS B  49 -1  O  TYR B  48   N  MET B  42           
SSBOND   1 CYS A    3    CYS A   30                          1555   1555  2.03  
SSBOND   2 CYS A  129    CYS A  159                          1555   1555  2.02  
SSBOND   3 CYS A  162    CYS A  170                          1555   1555  2.03  
SSBOND   4 CYS A  166    CYS A  178                          1555   1555  2.04  
SSBOND   5 CYS A  186    CYS A  195                          1555   1555  2.04  
SSBOND   6 CYS A  190    CYS A  203                          1555   1555  2.03  
SSBOND   7 CYS A  204    CYS A  212                          1555   1555  1.99  
SSBOND   8 CYS A  208    CYS A  220                          1555   1555  2.02  
SSBOND   9 CYS A  223    CYS A  232                          1555   1555  2.03  
SSBOND  10 CYS A  236    CYS A  263                          1555   1555  2.04  
SSBOND  11 CYS A  267    CYS A  278                          1555   1555  2.00  
SSBOND  12 CYS A  282    CYS A  293                          1555   1555  2.04  
SSBOND  13 CYS A  296    CYS A  300                          1555   1555  2.04  
SSBOND  14 CYS A  304    CYS A  321                          1555   1555  2.03  
SSBOND  15 CYS A  438    CYS A  467                          1555   1555  2.05  
SSBOND  16 CYS A  474    CYS A  483                          1555   1555  2.03  
SSBOND  17 CYS A  478    CYS A  491                          1555   1555  2.04  
SSBOND  18 CYS A  494    CYS A  503                          1555   1555  2.02  
SSBOND  19 CYS A  507    CYS A  521                          1555   1555  2.04  
SSBOND  20 CYS A  524    CYS A  531                          1555   1555  2.03  
SSBOND  21 CYS C    3    CYS C   30                          1555   1555  2.04  
SSBOND  22 CYS C  129    CYS C  159                          1555   1555  2.01  
SSBOND  23 CYS C  162    CYS C  170                          1555   1555  2.04  
SSBOND  24 CYS C  166    CYS C  178                          1555   1555  2.04  
SSBOND  25 CYS C  186    CYS C  195                          1555   1555  2.04  
SSBOND  26 CYS C  190    CYS C  203                          1555   1555  2.01  
SSBOND  27 CYS C  204    CYS C  212                          1555   1555  2.00  
SSBOND  28 CYS C  208    CYS C  220                          1555   1555  2.03  
SSBOND  29 CYS C  223    CYS C  232                          1555   1555  2.04  
SSBOND  30 CYS C  236    CYS C  263                          1555   1555  2.03  
SSBOND  31 CYS C  267    CYS C  278                          1555   1555  2.04  
SSBOND  32 CYS C  282    CYS C  293                          1555   1555  2.03  
SSBOND  33 CYS C  296    CYS C  300                          1555   1555  2.04  
SSBOND  34 CYS C  304    CYS C  321                          1555   1555  2.03  
SSBOND  35 CYS C  438    CYS C  467                          1555   1555  2.05  
SSBOND  36 CYS C  474    CYS C  483                          1555   1555  2.04  
SSBOND  37 CYS C  478    CYS C  491                          1555   1555  2.03  
SSBOND  38 CYS C  494    CYS C  503                          1555   1555  2.03  
SSBOND  39 CYS C  507    CYS C  521                          1555   1555  2.04  
SSBOND  40 CYS C  524    CYS C  531                          1555   1555  2.03  
SSBOND  41 CYS C  528    CYS C  539                          1555   1555  2.04  
SSBOND  42 CYS D    7    CYS D   22                          1555   1555  2.04  
SSBOND  43 CYS D   16    CYS D   35                          1555   1555  1.98  
SSBOND  44 CYS D   37    CYS D   46                          1555   1555  2.04  
SSBOND  45 CYS B    7    CYS B   22                          1555   1555  2.04  
SSBOND  46 CYS B   16    CYS B   35                          1555   1555  2.03  
SSBOND  47 CYS B   37    CYS B   46                          1555   1555  2.03  
LINK         O4  MAN A4703                 C1  MAN A4704     1555   1555  1.43  
LINK         O4  NAG A4701                 C1  MAN A4702     1555   1555  1.43  
LINK         ND2 ASN A 470                 C1  NAG A4700     1555   1555  1.43  
LINK         ND2 ASN C 383                 C1  NAG C3830     1555   1555  1.44  
LINK         O4  NAG A4700                 C1  NAG A4701     1555   1555  1.44  
LINK         ND2 ASN C 470                 C1  NAG C4700     1555   1555  1.44  
LINK         O4  NAG C4700                 C1  NAG C4701     1555   1555  1.44  
LINK         ND2 ASN C  29                 C1  NAG C 596     1555   1555  1.44  
LINK         ND2 ASN C 344                 C1  NAG C3440     1555   1555  1.44  
LINK         ND2 ASN A 383                 C1  NAG A3830     1555   1555  1.44  
LINK         O4  NAG C4701                 C1  MAN C4702     1555   1555  1.45  
LINK         O6  MAN A4702                 C1  MAN A4705     1555   1555  1.45  
LINK         O3  MAN A4702                 C1  MAN A4703     1555   1555  1.45  
LINK         O4  NAG C3830                 C1  NAG C3831     1555   1555  1.45  
LINK         O3  MAN C4702                 C1  MAN C4703     1555   1555  1.45  
SITE     1 AC1  6 TYR A 414  ASP A 436  LEU A 466  LYS A 469                    
SITE     2 AC1  6 ASN A 470  NAG A4701                                          
SITE     1 AC2  6 TYR A 414  ARG A 435  ASP A 436  LEU A 462                    
SITE     2 AC2  6 NAG A4700  MAN A4702                                          
SITE     1 AC3  4 ARG A 435  NAG A4701  MAN A4703  MAN A4705                    
SITE     1 AC4  5 HIS A 433  GLU A 460  MAN A4702  MAN A4704                    
SITE     2 AC4  5 LEU C 466                                                     
SITE     1 AC5  4 MAN A4703  LEU C 466  NAG C4700  NAG C4701                    
SITE     1 AC6  2 ARG A 435  MAN A4702                                          
SITE     1 AC7  1 ASN C  29                                                     
SITE     1 AC8  2 GLN A 380  ASN A 383                                          
SITE     1 AC9  2 ASN C 344  THR C 346                                          
SITE     1 BC1  5 GLN C 380  ASN C 383  TYR C 386  GLU C 417                    
SITE     2 BC1  5 NAG C3831                                                     
SITE     1 BC2  1 NAG C3830                                                     
SITE     1 BC3  7 MAN A4704  TYR C 414  ASP C 436  LEU C 462                    
SITE     2 BC3  7 LEU C 466  ASN C 470  NAG C4701                               
SITE     1 BC4  6 MAN A4704  TYR C 414  ARG C 435  ASP C 436                    
SITE     2 BC4  6 NAG C4700  MAN C4702                                          
SITE     1 BC5  3 ARG C 435  NAG C4701  MAN C4703                               
SITE     1 BC6  3 ARG A 463  GLU C 460  MAN C4702                               
SITE     1 BC7  3 SER A 441  ARG C 463  ALA C 464                               
CRYST1  118.208  124.239  186.508  90.00  90.00  90.00 P 21 21 21    8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.008460  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008049  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005362        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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