GenomeNet

Database: PDB
Entry: 3UVJ
LinkDB: 3UVJ
Original site: 3UVJ 
HEADER    LYASE                                   30-NOV-11   3UVJ              
TITLE     CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF THE HETERODIMERIC HUMAN  
TITLE    2 SOLUBLE GUANYLATE CYCLASE 1.                                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GUANYLATE CYCLASE SOLUBLE SUBUNIT ALPHA-3;                 
COMPND   3 CHAIN: A, C;                                                         
COMPND   4 FRAGMENT: SOLUBLE GUANYLATE CYCLASE ALPHA-1 CATALYTIC DOMAIN, UNP    
COMPND   5 RESIDUES 468-690;                                                    
COMPND   6 SYNONYM: GCS-ALPHA-3, GCS-ALPHA-1, SOLUBLE GUANYLATE CYCLASE LARGE   
COMPND   7 SUBUNIT;                                                             
COMPND   8 EC: 4.6.1.2;                                                         
COMPND   9 ENGINEERED: YES;                                                     
COMPND  10 MOL_ID: 2;                                                           
COMPND  11 MOLECULE: GUANYLATE CYCLASE SOLUBLE SUBUNIT BETA-1;                  
COMPND  12 CHAIN: B, D;                                                         
COMPND  13 FRAGMENT: SOLUBLE GUANYLATE CYCLASE BETA-1 CATALYTIC DOMAIN, UNP     
COMPND  14 RESIDUES 408-619;                                                    
COMPND  15 SYNONYM: GCS-BETA-1, GUANYLATE CYCLASE SOLUBLE SUBUNIT BETA-3, GCS-  
COMPND  16 BETA-3, SOLUBLE GUANYLATE CYCLASE SMALL SUBUNIT;                     
COMPND  17 EC: 4.6.1.2;                                                         
COMPND  18 ENGINEERED: YES;                                                     
COMPND  19 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: GUC1A3, GUCSA3, GUCY1A1, GUCY1A3;                              
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)-R3-CHAPERONES;                   
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PNH-TRXT;                                 
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  13 ORGANISM_COMMON: HUMAN;                                              
SOURCE  14 ORGANISM_TAXID: 9606;                                                
SOURCE  15 GENE: GUCY1B3, GUC1B3, GUCSB3, GUCY1B1;                              
SOURCE  16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  18 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)-R3-CHAPERONES;                   
SOURCE  19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  20 EXPRESSION_SYSTEM_PLASMID: PNIC-CTHF                                 
KEYWDS    NITRIC OXIDE, STRUCTURAL GENOMICS, STRUCTURAL GENOMICS CONSORTIUM,    
KEYWDS   2 SGC, CGMP BIOSYNTHESIS, GTP BINDING METAL-BINDING, NUCLEOTIDE-       
KEYWDS   3 BINDING, CYSTOL, LYASE                                               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.K.ALLERSTON,G.BERRIDGE,R.CHALK,C.D.O.COOPER,P.SAVITSKY,M.VOLLMAR,   
AUTHOR   2 C.H.ARROWSMITH,J.WEIGELT,A.EDWARDS,C.BOUNTRA,F.VON DELFT,O.GILEADI,  
AUTHOR   3 STRUCTURAL GENOMICS CONSORTIUM (SGC)                                 
REVDAT   3   31-JAN-18 3UVJ    1       AUTHOR                                   
REVDAT   2   10-APR-13 3UVJ    1       JRNL                                     
REVDAT   1   28-DEC-11 3UVJ    0                                                
JRNL        AUTH   C.K.ALLERSTON,F.VON DELFT,O.GILEADI                          
JRNL        TITL   CRYSTAL STRUCTURES OF THE CATALYTIC DOMAIN OF HUMAN SOLUBLE  
JRNL        TITL 2 GUANYLATE CYCLASE.                                           
JRNL        REF    PLOS ONE                      V.   8 57644 2013              
JRNL        REFN                   ESSN 1932-6203                               
JRNL        PMID   23505436                                                     
JRNL        DOI    10.1371/JOURNAL.PONE.0057644                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.08 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER 2.10.0                                        
REMARK   3   AUTHORS     : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,              
REMARK   3               : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,              
REMARK   3               : WOMACK,MATTHEWS,TEN EYCK,TRONRUD                     
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.08                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 51.50                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 45859                          
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)  : 0.169                          
REMARK   3   R VALUE            (WORKING SET)  : 0.167                          
REMARK   3   FREE R VALUE                      : 0.209                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 5.060                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 2319                           
REMARK   3   ESTIMATED ERROR OF FREE R VALUE   : NULL                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED               : 20                       
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 2.08                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 2.13                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 99.50                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 3408                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2056                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 3229                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2045                   
REMARK   3   BIN FREE R VALUE                        : 0.2243                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 5.25                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 179                      
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE     : NULL                     
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5804                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 32                                      
REMARK   3   SOLVENT ATOMS            : 431                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 36.79                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 39.92                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.92880                                              
REMARK   3    B22 (A**2) : 1.57880                                              
REMARK   3    B33 (A**2) : -3.50750                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.24280                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : 0.230               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : NULL                
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : NULL                
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : 0.192               
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : NULL                
REMARK   3                                                                      
REMARK   3   REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797                
REMARK   3               CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601     
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.957                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.939                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 6041   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 8222   ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 2762   ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 123    ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 915    ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 6041   ; 20.000 ; HARMONIC            
REMARK   3    BAD NON-BONDED CONTACTS   : NULL   ; NULL   ; NULL                
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL                
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : 823    ; 5.000  ; SEMIHARMONIC        
REMARK   3    SUM OF OCCUPANCIES        : 17     ; 1.000  ; HARMONIC            
REMARK   3    UTILITY DISTANCES         : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY ANGLES            : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY TORSION           : NULL   ; NULL   ; NULL                
REMARK   3    IDEAL-DIST CONTACT TERM   : 7225   ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.010                    
REMARK   3    BOND ANGLES                  (DEGREES) : 1.02                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.41                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 2.56                     
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 4                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: { A|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):   24.5106  -34.1361  -29.7870           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0738 T22:   -0.0732                                    
REMARK   3     T33:   -0.0938 T12:    0.0273                                    
REMARK   3     T13:   -0.0011 T23:    0.0095                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    3.2281 L22:    2.0501                                    
REMARK   3     L33:    1.1452 L12:    0.6339                                    
REMARK   3     L13:   -0.1882 L23:   -0.0908                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.1410 S12:    0.1333 S13:   -0.1617                     
REMARK   3     S21:   -0.2022 S22:    0.0573 S23:   -0.1431                     
REMARK   3     S31:    0.1117 S32:    0.0918 S33:    0.0837                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: { B|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):    7.7879  -28.0666  -10.7044           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0670 T22:   -0.0908                                    
REMARK   3     T33:   -0.0705 T12:    0.0063                                    
REMARK   3     T13:    0.0113 T23:    0.0346                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.7616 L22:    1.9175                                    
REMARK   3     L33:    1.6601 L12:    0.4298                                    
REMARK   3     L13:    0.2050 L23:    0.4335                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0780 S12:   -0.2505 S13:   -0.1339                     
REMARK   3     S21:    0.2437 S22:   -0.0684 S23:    0.0297                     
REMARK   3     S31:    0.0519 S32:   -0.0319 S33:   -0.0096                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: { C|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):    4.6863    7.2213  -58.2945           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.0048 T22:   -0.1197                                    
REMARK   3     T33:   -0.0800 T12:    0.0487                                    
REMARK   3     T13:    0.0461 T23:    0.0075                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    2.6020 L22:    1.5740                                    
REMARK   3     L33:    0.9436 L12:    0.2847                                    
REMARK   3     L13:    0.1351 L23:    0.2885                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0730 S12:    0.1315 S13:    0.1859                     
REMARK   3     S21:   -0.1440 S22:    0.0097 S23:    0.0910                     
REMARK   3     S31:   -0.1425 S32:   -0.0568 S33:    0.0633                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: { D|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):   20.4052    1.3418  -38.6840           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0601 T22:   -0.0866                                    
REMARK   3     T33:   -0.1136 T12:    0.0175                                    
REMARK   3     T13:   -0.0162 T23:   -0.0384                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    2.1407 L22:    2.5425                                    
REMARK   3     L33:    1.5228 L12:   -0.3685                                    
REMARK   3     L13:    0.1256 L23:   -0.6843                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0879 S12:   -0.3672 S13:    0.1103                     
REMARK   3     S21:    0.2086 S22:    0.0845 S23:   -0.1871                     
REMARK   3     S31:   -0.1662 S32:   -0.0685 S33:    0.0034                     
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3UVJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-DEC-11.                  
REMARK 100 THE DEPOSITION ID IS D_1000069261.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-OCT-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7                                  
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I04                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.968627                           
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL                     
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 45874                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.080                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 51.500                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY                : 3.300                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.2000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.08                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.16                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 94.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.30                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: BALBES                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 37.77                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.98                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.05M KH2PO4 20% PEG 8000, PH 7, VAPOR   
REMARK 280  DIFFUSION, SITTING DROP, TEMPERATURE 298K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,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        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       69.55000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3320 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 16800 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -19.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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: 3290 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 16990 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -23.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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     SER A   466                                                      
REMARK 465     MET A   467                                                      
REMARK 465     GLN A   468                                                      
REMARK 465     GLY A   469                                                      
REMARK 465     LYS A   590                                                      
REMARK 465     GLN A   662                                                      
REMARK 465     GLY A   663                                                      
REMARK 465     THR A   664                                                      
REMARK 465     ASN A   665                                                      
REMARK 465     SER A   666                                                      
REMARK 465     LYS A   667                                                      
REMARK 465     PRO A   668                                                      
REMARK 465     CYS A   669                                                      
REMARK 465     PHE A   670                                                      
REMARK 465     GLN A   671                                                      
REMARK 465     LYS A   672                                                      
REMARK 465     LYS A   673                                                      
REMARK 465     ASP A   674                                                      
REMARK 465     VAL A   675                                                      
REMARK 465     GLU A   676                                                      
REMARK 465     ASP A   677                                                      
REMARK 465     GLY A   678                                                      
REMARK 465     ASN A   679                                                      
REMARK 465     ALA A   680                                                      
REMARK 465     ASN A   681                                                      
REMARK 465     PHE A   682                                                      
REMARK 465     LEU A   683                                                      
REMARK 465     GLY A   684                                                      
REMARK 465     LYS A   685                                                      
REMARK 465     ALA A   686                                                      
REMARK 465     SER A   687                                                      
REMARK 465     GLY A   688                                                      
REMARK 465     ILE A   689                                                      
REMARK 465     ASP A   690                                                      
REMARK 465     MET B   407                                                      
REMARK 465     HIS B   408                                                      
REMARK 465     LYS B   409                                                      
REMARK 465     ARG B   410                                                      
REMARK 465     PRO B   411                                                      
REMARK 465     VAL B   412                                                      
REMARK 465     THR B   609                                                      
REMARK 465     GLY B   610                                                      
REMARK 465     THR B   611                                                      
REMARK 465     GLU B   612                                                      
REMARK 465     GLU B   613                                                      
REMARK 465     THR B   614                                                      
REMARK 465     LYS B   615                                                      
REMARK 465     GLN B   616                                                      
REMARK 465     ASP B   617                                                      
REMARK 465     ASP B   618                                                      
REMARK 465     ASP B   619                                                      
REMARK 465     ALA B   620                                                      
REMARK 465     GLU B   621                                                      
REMARK 465     ASN B   622                                                      
REMARK 465     LEU B   623                                                      
REMARK 465     TYR B   624                                                      
REMARK 465     PHE B   625                                                      
REMARK 465     GLN B   626                                                      
REMARK 465     SER C   466                                                      
REMARK 465     MET C   467                                                      
REMARK 465     GLN C   468                                                      
REMARK 465     GLY C   469                                                      
REMARK 465     HIS C   539                                                      
REMARK 465     GLN C   662                                                      
REMARK 465     GLY C   663                                                      
REMARK 465     THR C   664                                                      
REMARK 465     ASN C   665                                                      
REMARK 465     SER C   666                                                      
REMARK 465     LYS C   667                                                      
REMARK 465     PRO C   668                                                      
REMARK 465     CYS C   669                                                      
REMARK 465     PHE C   670                                                      
REMARK 465     GLN C   671                                                      
REMARK 465     LYS C   672                                                      
REMARK 465     LYS C   673                                                      
REMARK 465     ASP C   674                                                      
REMARK 465     VAL C   675                                                      
REMARK 465     GLU C   676                                                      
REMARK 465     ASP C   677                                                      
REMARK 465     GLY C   678                                                      
REMARK 465     ASN C   679                                                      
REMARK 465     ALA C   680                                                      
REMARK 465     ASN C   681                                                      
REMARK 465     PHE C   682                                                      
REMARK 465     LEU C   683                                                      
REMARK 465     GLY C   684                                                      
REMARK 465     LYS C   685                                                      
REMARK 465     ALA C   686                                                      
REMARK 465     SER C   687                                                      
REMARK 465     GLY C   688                                                      
REMARK 465     ILE C   689                                                      
REMARK 465     ASP C   690                                                      
REMARK 465     MET D   407                                                      
REMARK 465     HIS D   408                                                      
REMARK 465     LYS D   409                                                      
REMARK 465     ARG D   410                                                      
REMARK 465     PRO D   411                                                      
REMARK 465     ASN D   608                                                      
REMARK 465     THR D   609                                                      
REMARK 465     GLY D   610                                                      
REMARK 465     THR D   611                                                      
REMARK 465     GLU D   612                                                      
REMARK 465     GLU D   613                                                      
REMARK 465     THR D   614                                                      
REMARK 465     LYS D   615                                                      
REMARK 465     GLN D   616                                                      
REMARK 465     ASP D   617                                                      
REMARK 465     ASP D   618                                                      
REMARK 465     ASP D   619                                                      
REMARK 465     ALA D   620                                                      
REMARK 465     GLU D   621                                                      
REMARK 465     ASN D   622                                                      
REMARK 465     LEU D   623                                                      
REMARK 465     TYR D   624                                                      
REMARK 465     PHE D   625                                                      
REMARK 465     GLN D   626                                                      
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     LYS A 475    CE   NZ                                             
REMARK 470     LYS A 476    CE   NZ                                             
REMARK 470     GLN A 515    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 524    NZ                                                  
REMARK 470     LYS A 540    CG   CD   CE   NZ                                   
REMARK 470     GLU A 541    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 555    CE   NZ                                             
REMARK 470     LYS A 572    NZ                                                  
REMARK 470     MET A 591    CG   SD   CE                                        
REMARK 470     ARG A 593    NE   CZ   NH1  NH2                                  
REMARK 470     LYS A 606    CE   NZ                                             
REMARK 470     LYS A 627    CE   NZ                                             
REMARK 470     PRO A 630    CG   CD                                             
REMARK 470     LYS B 436    CG   CD   CE   NZ                                   
REMARK 470     LYS B 445    CE   NZ                                             
REMARK 470     LYS B 465    CG   CD   CE   NZ                                   
REMARK 470     GLU B 473    CG   CD   OE1  OE2                                  
REMARK 470     ILE B 490    CD1                                                 
REMARK 470     GLU B 515    CG   CD   OE1  OE2                                  
REMARK 470     GLN B 535    CG   CD   OE1  NE2                                  
REMARK 470     ARG B 536    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     MET B 537    CG   SD   CE                                        
REMARK 470     ARG B 539    CD   NE   CZ   NH1  NH2                             
REMARK 470     LYS B 559    NZ                                                  
REMARK 470     GLU B 576    OE1  OE2                                            
REMARK 470     LYS B 593    NZ                                                  
REMARK 470     LYS B 596    CG   CD   CE   NZ                                   
REMARK 470     LYS B 607    NZ                                                  
REMARK 470     ASN B 608    CG   OD1  ND2                                       
REMARK 470     LYS C 475    CE   NZ                                             
REMARK 470     LYS C 476    CE   NZ                                             
REMARK 470     GLU C 519    CG   CD   OE1  OE2                                  
REMARK 470     LYS C 524    CE   NZ                                             
REMARK 470     LYS C 540    CG   CD   CE   NZ                                   
REMARK 470     GLU C 541    CG   CD   OE1  OE2                                  
REMARK 470     ASP C 543    CG   OD1  OD2                                       
REMARK 470     LYS C 555    CD   CE   NZ                                        
REMARK 470     ASP C 561    CG   OD1  OD2                                       
REMARK 470     GLU C 569    CG   CD   OE1  OE2                                  
REMARK 470     LYS C 572    NZ                                                  
REMARK 470     LYS C 590    CG   CD   CE   NZ                                   
REMARK 470     ARG C 593    NE   CZ   NH1  NH2                                  
REMARK 470     TYR C 594    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LYS C 606    CD   CE   NZ                                        
REMARK 470     LYS C 627    NZ                                                  
REMARK 470     PRO C 630    CG   CD                                             
REMARK 470     VAL D 412    CG1  CG2                                            
REMARK 470     LYS D 415    CD   CE   NZ                                        
REMARK 470     LYS D 436    CG   CD   CE   NZ                                   
REMARK 470     GLU D 441    CG   CD   OE1  OE2                                  
REMARK 470     LYS D 445    CG   CD   CE   NZ                                   
REMARK 470     LYS D 465    CG   CD   CE   NZ                                   
REMARK 470     GLU D 473    CG   CD   OE1  OE2                                  
REMARK 470     GLU D 487    CG   CD   OE1  OE2                                  
REMARK 470     ILE D 490    CD1                                                 
REMARK 470     GLU D 505    CG   CD   OE1  OE2                                  
REMARK 470     VAL D 512    CG1  CG2                                            
REMARK 470     ASP D 513    CG   OD1  OD2                                       
REMARK 470     GLU D 515    CG   CD   OE1  OE2                                  
REMARK 470     GLN D 535    CG   CD   OE1  NE2                                  
REMARK 470     ARG D 536    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     MET D 537    CG   SD   CE                                        
REMARK 470     ARG D 539    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS D 559    CE   NZ                                             
REMARK 470     LYS D 561    NZ                                                  
REMARK 470     GLN D 581    CG   CD   OE1  NE2                                  
REMARK 470     LYS D 593    CD   CE   NZ                                        
REMARK 470     LYS D 596    CG   CD   CE   NZ                                   
REMARK 470     LYS D 607    CD   CE   NZ                                        
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    ARG A 637     -109.90   -107.38                                   
REMARK 500    ARG C 637     -110.47   -108.13                                   
REMARK 500    HIS D 491       42.03   -106.54                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY                                       
REMARK 500                                                                      
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY                       
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER                 
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;                     
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;                            
REMARK 500 I=INSERTION CODE).                                                   
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        ANGLE                                           
REMARK 500    CYS A 629         11.55                                           
REMARK 500    CYS A 629         11.42                                           
REMARK 500    CYS C 629         11.77                                           
REMARK 500    CYS C 629         11.58                                           
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 EDO A 3                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 5                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 7                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 1                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C 2                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 4                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C 6                   
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2WZ1   RELATED DB: PDB                                   
DBREF  3UVJ A  468   690  UNP    Q02108   GCYA3_HUMAN    468    690             
DBREF  3UVJ B  408   619  UNP    Q02153   GCYB1_HUMAN    408    619             
DBREF  3UVJ C  468   690  UNP    Q02108   GCYA3_HUMAN    468    690             
DBREF  3UVJ D  408   619  UNP    Q02153   GCYB1_HUMAN    408    619             
SEQADV 3UVJ SER A  466  UNP  Q02108              EXPRESSION TAG                 
SEQADV 3UVJ MET A  467  UNP  Q02108              EXPRESSION TAG                 
SEQADV 3UVJ MET B  407  UNP  Q02153              EXPRESSION TAG                 
SEQADV 3UVJ CYS B  476  UNP  Q02153    GLY   476 ENGINEERED MUTATION            
SEQADV 3UVJ SER B  541  UNP  Q02153    CYS   541 ENGINEERED MUTATION            
SEQADV 3UVJ ALA B  620  UNP  Q02153              EXPRESSION TAG                 
SEQADV 3UVJ GLU B  621  UNP  Q02153              EXPRESSION TAG                 
SEQADV 3UVJ ASN B  622  UNP  Q02153              EXPRESSION TAG                 
SEQADV 3UVJ LEU B  623  UNP  Q02153              EXPRESSION TAG                 
SEQADV 3UVJ TYR B  624  UNP  Q02153              EXPRESSION TAG                 
SEQADV 3UVJ PHE B  625  UNP  Q02153              EXPRESSION TAG                 
SEQADV 3UVJ GLN B  626  UNP  Q02153              EXPRESSION TAG                 
SEQADV 3UVJ SER C  466  UNP  Q02108              EXPRESSION TAG                 
SEQADV 3UVJ MET C  467  UNP  Q02108              EXPRESSION TAG                 
SEQADV 3UVJ MET D  407  UNP  Q02153              EXPRESSION TAG                 
SEQADV 3UVJ CYS D  476  UNP  Q02153    GLY   476 ENGINEERED MUTATION            
SEQADV 3UVJ SER D  541  UNP  Q02153    CYS   541 ENGINEERED MUTATION            
SEQADV 3UVJ ALA D  620  UNP  Q02153              EXPRESSION TAG                 
SEQADV 3UVJ GLU D  621  UNP  Q02153              EXPRESSION TAG                 
SEQADV 3UVJ ASN D  622  UNP  Q02153              EXPRESSION TAG                 
SEQADV 3UVJ LEU D  623  UNP  Q02153              EXPRESSION TAG                 
SEQADV 3UVJ TYR D  624  UNP  Q02153              EXPRESSION TAG                 
SEQADV 3UVJ PHE D  625  UNP  Q02153              EXPRESSION TAG                 
SEQADV 3UVJ GLN D  626  UNP  Q02153              EXPRESSION TAG                 
SEQRES   1 A  225  SER MET GLN GLY GLN VAL VAL GLN ALA LYS LYS PHE SER          
SEQRES   2 A  225  ASN VAL THR MET LEU PHE SER ASP ILE VAL GLY PHE THR          
SEQRES   3 A  225  ALA ILE CYS SER GLN CYS SER PRO LEU GLN VAL ILE THR          
SEQRES   4 A  225  MET LEU ASN ALA LEU TYR THR ARG PHE ASP GLN GLN CYS          
SEQRES   5 A  225  GLY GLU LEU ASP VAL TYR LYS VAL GLU THR ILE GLY ASP          
SEQRES   6 A  225  ALA TYR CYS VAL ALA GLY GLY LEU HIS LYS GLU SER ASP          
SEQRES   7 A  225  THR HIS ALA VAL GLN ILE ALA LEU MET ALA LEU LYS MET          
SEQRES   8 A  225  MET GLU LEU SER ASP GLU VAL MET SER PRO HIS GLY GLU          
SEQRES   9 A  225  PRO ILE LYS MET ARG ILE GLY LEU HIS SER GLY SER VAL          
SEQRES  10 A  225  PHE ALA GLY VAL VAL GLY VAL LYS MET PRO ARG TYR CYS          
SEQRES  11 A  225  LEU PHE GLY ASN ASN VAL THR LEU ALA ASN LYS PHE GLU          
SEQRES  12 A  225  SER CYS SER VAL PRO ARG LYS ILE ASN VAL SER PRO THR          
SEQRES  13 A  225  THR TYR ARG LEU LEU LYS ASP CYS PRO GLY PHE VAL PHE          
SEQRES  14 A  225  THR PRO ARG SER ARG GLU GLU LEU PRO PRO ASN PHE PRO          
SEQRES  15 A  225  SER GLU ILE PRO GLY ILE CYS HIS PHE LEU ASP ALA TYR          
SEQRES  16 A  225  GLN GLN GLY THR ASN SER LYS PRO CYS PHE GLN LYS LYS          
SEQRES  17 A  225  ASP VAL GLU ASP GLY ASN ALA ASN PHE LEU GLY LYS ALA          
SEQRES  18 A  225  SER GLY ILE ASP                                              
SEQRES   1 B  220  MET HIS LYS ARG PRO VAL PRO ALA LYS ARG TYR ASP ASN          
SEQRES   2 B  220  VAL THR ILE LEU PHE SER GLY ILE VAL GLY PHE ASN ALA          
SEQRES   3 B  220  PHE CYS SER LYS HIS ALA SER GLY GLU GLY ALA MET LYS          
SEQRES   4 B  220  ILE VAL ASN LEU LEU ASN ASP LEU TYR THR ARG PHE ASP          
SEQRES   5 B  220  THR LEU THR ASP SER ARG LYS ASN PRO PHE VAL TYR LYS          
SEQRES   6 B  220  VAL GLU THR VAL CYS ASP LYS TYR MET THR VAL SER GLY          
SEQRES   7 B  220  LEU PRO GLU PRO CYS ILE HIS HIS ALA ARG SER ILE CYS          
SEQRES   8 B  220  HIS LEU ALA LEU ASP MET MET GLU ILE ALA GLY GLN VAL          
SEQRES   9 B  220  GLN VAL ASP GLY GLU SER VAL GLN ILE THR ILE GLY ILE          
SEQRES  10 B  220  HIS THR GLY GLU VAL VAL THR GLY VAL ILE GLY GLN ARG          
SEQRES  11 B  220  MET PRO ARG TYR SER LEU PHE GLY ASN THR VAL ASN LEU          
SEQRES  12 B  220  THR SER ARG THR GLU THR THR GLY GLU LYS GLY LYS ILE          
SEQRES  13 B  220  ASN VAL SER GLU TYR THR TYR ARG CYS LEU MET SER PRO          
SEQRES  14 B  220  GLU ASN SER ASP PRO GLN PHE HIS LEU GLU HIS ARG GLY          
SEQRES  15 B  220  PRO VAL SER MET LYS GLY LYS LYS GLU PRO MET GLN VAL          
SEQRES  16 B  220  TRP PHE LEU SER ARG LYS ASN THR GLY THR GLU GLU THR          
SEQRES  17 B  220  LYS GLN ASP ASP ASP ALA GLU ASN LEU TYR PHE GLN              
SEQRES   1 C  225  SER MET GLN GLY GLN VAL VAL GLN ALA LYS LYS PHE SER          
SEQRES   2 C  225  ASN VAL THR MET LEU PHE SER ASP ILE VAL GLY PHE THR          
SEQRES   3 C  225  ALA ILE CYS SER GLN CYS SER PRO LEU GLN VAL ILE THR          
SEQRES   4 C  225  MET LEU ASN ALA LEU TYR THR ARG PHE ASP GLN GLN CYS          
SEQRES   5 C  225  GLY GLU LEU ASP VAL TYR LYS VAL GLU THR ILE GLY ASP          
SEQRES   6 C  225  ALA TYR CYS VAL ALA GLY GLY LEU HIS LYS GLU SER ASP          
SEQRES   7 C  225  THR HIS ALA VAL GLN ILE ALA LEU MET ALA LEU LYS MET          
SEQRES   8 C  225  MET GLU LEU SER ASP GLU VAL MET SER PRO HIS GLY GLU          
SEQRES   9 C  225  PRO ILE LYS MET ARG ILE GLY LEU HIS SER GLY SER VAL          
SEQRES  10 C  225  PHE ALA GLY VAL VAL GLY VAL LYS MET PRO ARG TYR CYS          
SEQRES  11 C  225  LEU PHE GLY ASN ASN VAL THR LEU ALA ASN LYS PHE GLU          
SEQRES  12 C  225  SER CYS SER VAL PRO ARG LYS ILE ASN VAL SER PRO THR          
SEQRES  13 C  225  THR TYR ARG LEU LEU LYS ASP CYS PRO GLY PHE VAL PHE          
SEQRES  14 C  225  THR PRO ARG SER ARG GLU GLU LEU PRO PRO ASN PHE PRO          
SEQRES  15 C  225  SER GLU ILE PRO GLY ILE CYS HIS PHE LEU ASP ALA TYR          
SEQRES  16 C  225  GLN GLN GLY THR ASN SER LYS PRO CYS PHE GLN LYS LYS          
SEQRES  17 C  225  ASP VAL GLU ASP GLY ASN ALA ASN PHE LEU GLY LYS ALA          
SEQRES  18 C  225  SER GLY ILE ASP                                              
SEQRES   1 D  220  MET HIS LYS ARG PRO VAL PRO ALA LYS ARG TYR ASP ASN          
SEQRES   2 D  220  VAL THR ILE LEU PHE SER GLY ILE VAL GLY PHE ASN ALA          
SEQRES   3 D  220  PHE CYS SER LYS HIS ALA SER GLY GLU GLY ALA MET LYS          
SEQRES   4 D  220  ILE VAL ASN LEU LEU ASN ASP LEU TYR THR ARG PHE ASP          
SEQRES   5 D  220  THR LEU THR ASP SER ARG LYS ASN PRO PHE VAL TYR LYS          
SEQRES   6 D  220  VAL GLU THR VAL CYS ASP LYS TYR MET THR VAL SER GLY          
SEQRES   7 D  220  LEU PRO GLU PRO CYS ILE HIS HIS ALA ARG SER ILE CYS          
SEQRES   8 D  220  HIS LEU ALA LEU ASP MET MET GLU ILE ALA GLY GLN VAL          
SEQRES   9 D  220  GLN VAL ASP GLY GLU SER VAL GLN ILE THR ILE GLY ILE          
SEQRES  10 D  220  HIS THR GLY GLU VAL VAL THR GLY VAL ILE GLY GLN ARG          
SEQRES  11 D  220  MET PRO ARG TYR SER LEU PHE GLY ASN THR VAL ASN LEU          
SEQRES  12 D  220  THR SER ARG THR GLU THR THR GLY GLU LYS GLY LYS ILE          
SEQRES  13 D  220  ASN VAL SER GLU TYR THR TYR ARG CYS LEU MET SER PRO          
SEQRES  14 D  220  GLU ASN SER ASP PRO GLN PHE HIS LEU GLU HIS ARG GLY          
SEQRES  15 D  220  PRO VAL SER MET LYS GLY LYS LYS GLU PRO MET GLN VAL          
SEQRES  16 D  220  TRP PHE LEU SER ARG LYS ASN THR GLY THR GLU GLU THR          
SEQRES  17 D  220  LYS GLN ASP ASP ASP ALA GLU ASN LEU TYR PHE GLN              
HET    EDO  A   3       4                                                       
HET    EDO  A   5       4                                                       
HET    GOL  A   7       6                                                       
HET    EDO  B   1       4                                                       
HET    EDO  C   2       4                                                       
HET    GOL  C   4       6                                                       
HET    EDO  C   6       4                                                       
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETNAM     GOL GLYCEROL                                                         
HETSYN     EDO ETHYLENE GLYCOL                                                  
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   5  EDO    5(C2 H6 O2)                                                  
FORMUL   7  GOL    2(C3 H8 O3)                                                  
FORMUL  12  HOH   *431(H2 O)                                                    
HELIX    1   1 GLY A  489  CYS A  497  1                                   9    
HELIX    2   2 SER A  498  ASP A  521  1                                  24    
HELIX    3   3 THR A  544  ASP A  561  1                                  18    
HELIX    4   4 GLY A  598  CYS A  610  1                                  13    
HELIX    5   5 SER A  619  LYS A  627  1                                   9    
HELIX    6   6 GLY B  429  LYS B  436  1                                   8    
HELIX    7   7 SER B  439  ASP B  462  1                                  24    
HELIX    8   8 HIS B  491  GLY B  508  1                                  18    
HELIX    9   9 GLY B  544  THR B  556  1                                  13    
HELIX   10  10 GLU B  566  MET B  573  1                                   8    
HELIX   11  11 GLY C  489  CYS C  497  1                                   9    
HELIX   12  12 SER C  498  ASP C  521  1                                  24    
HELIX   13  13 THR C  544  ASP C  561  1                                  18    
HELIX   14  14 GLY C  598  CYS C  610  1                                  13    
HELIX   15  15 SER C  619  LYS C  627  1                                   9    
HELIX   16  16 GLY D  429  HIS D  437  1                                   9    
HELIX   17  17 SER D  439  ASP D  462  1                                  24    
HELIX   18  18 HIS D  491  GLY D  508  1                                  18    
HELIX   19  19 GLY D  544  THR D  556  1                                  13    
HELIX   20  20 GLU D  566  MET D  573  1                                   8    
SHEET    1   A 5 TYR A 523  VAL A 525  0                                        
SHEET    2   A 5 TYR A 532  GLY A 536 -1  O  CYS A 533   N  VAL A 525           
SHEET    3   A 5 VAL A 471  ILE A 487 -1  N  LEU A 483   O  VAL A 534           
SHEET    4   A 5 MET A 573  VAL A 587 -1  O  VAL A 586   N  GLN A 473           
SHEET    5   A 5 ARG A 593  PHE A 597 -1  O  CYS A 595   N  GLY A 585           
SHEET    1   B 7 TYR A 523  VAL A 525  0                                        
SHEET    2   B 7 TYR A 532  GLY A 536 -1  O  CYS A 533   N  VAL A 525           
SHEET    3   B 7 VAL A 471  ILE A 487 -1  N  LEU A 483   O  VAL A 534           
SHEET    4   B 7 MET A 573  VAL A 587 -1  O  VAL A 586   N  GLN A 473           
SHEET    5   B 7 ILE A 616  VAL A 618  1  O  ASN A 617   N  ILE A 575           
SHEET    6   B 7 HIS A 655  TYR A 660 -1  O  HIS A 655   N  VAL A 618           
SHEET    7   B 7 PHE A 632  PRO A 636 -1  N  VAL A 633   O  ASP A 658           
SHEET    1   C 5 TYR B 470  VAL B 472  0                                        
SHEET    2   C 5 TYR B 479  SER B 483 -1  O  VAL B 482   N  TYR B 470           
SHEET    3   C 5 LYS B 415  ILE B 427 -1  N  SER B 425   O  TYR B 479           
SHEET    4   C 5 ILE B 519  ILE B 533 -1  O  VAL B 528   N  TYR B 417           
SHEET    5   C 5 ARG B 539  PHE B 543 -1  O  SER B 541   N  GLY B 531           
SHEET    1   D 7 TYR B 470  VAL B 472  0                                        
SHEET    2   D 7 TYR B 479  SER B 483 -1  O  VAL B 482   N  TYR B 470           
SHEET    3   D 7 LYS B 415  ILE B 427 -1  N  SER B 425   O  TYR B 479           
SHEET    4   D 7 ILE B 519  ILE B 533 -1  O  VAL B 528   N  TYR B 417           
SHEET    5   D 7 ILE B 562  SER B 565  1  O  ASN B 563   N  ILE B 521           
SHEET    6   D 7 MET B 599  ARG B 606 -1  O  TRP B 602   N  VAL B 564           
SHEET    7   D 7 PHE B 582  VAL B 590 -1  N  GLU B 585   O  PHE B 603           
SHEET    1   E 2 GLN B 511  VAL B 512  0                                        
SHEET    2   E 2 GLU B 515  SER B 516 -1  O  GLU B 515   N  VAL B 512           
SHEET    1   F 9 PHE C 632  PRO C 636  0                                        
SHEET    2   F 9 HIS C 655  TYR C 660 -1  O  PHE C 656   N  THR C 635           
SHEET    3   F 9 ILE C 616  VAL C 618 -1  N  VAL C 618   O  HIS C 655           
SHEET    4   F 9 MET C 573  VAL C 587  1  N  ILE C 575   O  ASN C 617           
SHEET    5   F 9 ARG C 593  PHE C 597 -1  O  CYS C 595   N  GLY C 585           
SHEET    6   F 9 TYR C 523  VAL C 525  1  N  LYS C 524   O  TYR C 594           
SHEET    7   F 9 TYR C 532  GLY C 536 -1  O  ALA C 535   N  TYR C 523           
SHEET    8   F 9 VAL C 471  ILE C 487 -1  N  THR C 481   O  GLY C 536           
SHEET    9   F 9 MET C 573  VAL C 587 -1  O  VAL C 582   N  PHE C 477           
SHEET    1   G 5 TYR D 470  VAL D 472  0                                        
SHEET    2   G 5 TYR D 479  SER D 483 -1  O  VAL D 482   N  TYR D 470           
SHEET    3   G 5 LYS D 415  ILE D 427 -1  N  SER D 425   O  TYR D 479           
SHEET    4   G 5 ILE D 519  ILE D 533 -1  O  VAL D 528   N  TYR D 417           
SHEET    5   G 5 ARG D 539  PHE D 543 -1  O  SER D 541   N  GLY D 531           
SHEET    1   H 7 TYR D 470  VAL D 472  0                                        
SHEET    2   H 7 TYR D 479  SER D 483 -1  O  VAL D 482   N  TYR D 470           
SHEET    3   H 7 LYS D 415  ILE D 427 -1  N  SER D 425   O  TYR D 479           
SHEET    4   H 7 ILE D 519  ILE D 533 -1  O  VAL D 528   N  TYR D 417           
SHEET    5   H 7 ILE D 562  SER D 565  1  O  ASN D 563   N  ILE D 521           
SHEET    6   H 7 MET D 599  ARG D 606 -1  O  TRP D 602   N  VAL D 564           
SHEET    7   H 7 PHE D 582  VAL D 590 -1  N  GLU D 585   O  PHE D 603           
SHEET    1   I 2 GLN D 511  VAL D 512  0                                        
SHEET    2   I 2 GLU D 515  SER D 516 -1  O  GLU D 515   N  VAL D 512           
CISPEP   1 LEU B  485    PRO B  486          0         0.02                     
CISPEP   2 LEU D  485    PRO D  486          0         0.75                     
SITE     1 AC1  6 TYR A 510  THR A 527  GLY A 529  ASP A 530                    
SITE     2 AC1  6 ALA A 531  HOH B 346                                          
SITE     1 AC2  4 HOH A 225  LYS A 615  HIS D 586  TRP D 602                    
SITE     1 AC3  7 HOH A 248  VAL A 525  GLU A 526  CYS A 595                    
SITE     2 AC3  7 LEU A 596  VAL B 475  ASP B 477                               
SITE     1 AC4  5 PHE B 468  GLY B 484  LEU B 485  PRO B 486                    
SITE     2 AC4  5 GLU B 487                                                     
SITE     1 AC5  4 HIS B 586  ARG B 587  GLY B 588  PRO C 613                    
SITE     1 AC6 10 HOH C 103  HOH C 151  THR C 527  ILE C 528                    
SITE     2 AC6 10 GLY C 529  VAL D 472  GLU D 473  THR D 474                    
SITE     3 AC6 10 MET D 480  LEU D 542                                          
SITE     1 AC7  4 TRP B 602  HOH C 264  VAL C 612  LYS C 615                    
CRYST1   50.780  139.100   55.460  90.00  91.47  90.00 P 1 21 1      4          
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      0.019693  0.000000  0.000505        0.00000                         
SCALE2      0.000000  0.007189  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.018037        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system