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Database: PDB
Entry: 6CXO
LinkDB: 6CXO
Original site: 6CXO 
HEADER    IMMUNE SYSTEM                           03-APR-18   6CXO              
TITLE     COMPLEMENT COMPONENT-9                                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: COMPLEMENT COMPONENT C9;                                   
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE   3 ORGANISM_COMMON: MOUSE;                                              
SOURCE   4 ORGANISM_TAXID: 10090;                                               
SOURCE   5 GENE: C9;                                                            
SOURCE   6 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE   7 EXPRESSION_SYSTEM_COMMON: HUMAN;                                     
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 9606                                        
KEYWDS    IMMUNITY, COMPLEX, COMPLEMENT, MACPF, IMMUNE SYSTEM                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    R.H.P.LAW,B.A.SPICER,T.T.CARADOC-DAVIES                               
REVDAT   1   05-SEP-18 6CXO    0                                                
JRNL        AUTH   B.A.SPICER,R.H.P.LAW,T.T.CARADOC-DAVIES,S.M.EKKEL,           
JRNL        AUTH 2 C.BAYLY-JONES,S.S.PANG,P.J.CONROY,G.RAMM,M.RADJAINIA,        
JRNL        AUTH 3 H.VENUGOPAL,J.C.WHISSTOCK,M.A.DUNSTONE                       
JRNL        TITL   THE FIRST TRANSMEMBRANE REGION OF COMPLEMENT COMPONENT-9     
JRNL        TITL 2 ACTS AS A BRAKE ON ITS SELF-ASSEMBLY.                        
JRNL        REF    NAT COMMUN                    V.   9  3266 2018              
JRNL        REFN                   ESSN 2041-1723                               
JRNL        PMID   30111885                                                     
JRNL        DOI    10.1038/S41467-018-05717-0                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER 2.10.3                                        
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) : 2.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 49.74                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 66058                          
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)  : 0.211                          
REMARK   3   R VALUE            (WORKING SET)  : 0.209                          
REMARK   3   FREE R VALUE                      : 0.251                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 5.100                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 3369                           
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) : 2.20                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 2.26                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 92.74                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 4520                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2266                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 4314                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2260                   
REMARK   3   BIN FREE R VALUE                        : 0.2390                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 4.56                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 206                      
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            : 7160                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 59                                      
REMARK   3   SOLVENT ATOMS            : 335                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 59.38                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 67.54                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -8.84090                                             
REMARK   3    B22 (A**2) : -3.27760                                             
REMARK   3    B33 (A**2) : 12.11850                                             
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 COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : 0.320               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : 0.216               
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : 0.188               
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : 0.212               
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : 0.187               
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      : 0.942                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.925                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 7390   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 9999   ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 2599   ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 198    ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 1064   ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 7390   ; 20.000 ; HARMONIC            
REMARK   3    BAD NON-BONDED CONTACTS   : 2      ; 5.000  ; SEMIHARMONIC        
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL                
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : 965    ; 5.000  ; SEMIHARMONIC        
REMARK   3    SUM OF OCCUPANCIES        : NULL   ; NULL   ; NULL                
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   : 8213   ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.010                    
REMARK   3    BOND ANGLES                  (DEGREES) : 0.75                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.05                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 6.68                     
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 2                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: { A|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):   23.8414   96.0288   28.0236           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0217 T22:   -0.0297                                    
REMARK   3     T33:   -0.1240 T12:    0.0712                                    
REMARK   3     T13:    0.0305 T23:    0.0071                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.5075 L22:    0.4471                                    
REMARK   3     L33:    1.6284 L12:   -0.0391                                    
REMARK   3     L13:   -0.0345 L23:   -0.2235                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0093 S12:   -0.0926 S13:   -0.0038                     
REMARK   3     S21:    0.1514 S22:    0.0398 S23:    0.0032                     
REMARK   3     S31:    0.1411 S32:    0.3917 S33:   -0.0491                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: { B|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):   47.2713  133.4770   55.8762           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0645 T22:   -0.0495                                    
REMARK   3     T33:   -0.0933 T12:    0.0024                                    
REMARK   3     T13:    0.0255 T23:   -0.0117                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.4577 L22:    0.8116                                    
REMARK   3     L33:    1.3183 L12:   -0.1538                                    
REMARK   3     L13:    0.2160 L23:    0.4638                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0831 S12:   -0.0002 S13:   -0.0030                     
REMARK   3     S21:    0.0545 S22:   -0.0704 S23:    0.1037                     
REMARK   3     S31:    0.0281 S32:   -0.1844 S33:    0.1535                     
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 6CXO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-APR-18.                  
REMARK 100 THE DEPOSITION ID IS D_1000233269.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 29-MAR-17                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.4                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : AUSTRALIAN SYNCHROTRON             
REMARK 200  BEAMLINE                       : MX2                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.20365                            
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL                     
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS EIGER X 16M                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 66078                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 49.740                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.7                               
REMARK 200  DATA REDUNDANCY                : 12.10                              
REMARK 200  R MERGE                    (I) : 0.07500                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 16.8000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.32                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 8.60                               
REMARK 200  R MERGE FOR SHELL          (I) : 1.35900                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.400                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MIRAS                        
REMARK 200 SOFTWARE USED: CRANK2                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: PLATE                                                        
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 49.70                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.44                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 3350, SODIUM MALONATE, ZINC          
REMARK 280  CHLORIDE, PH 7.4, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 2 21                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,-Y,-Z+1/2                                         
REMARK 290       4555   -X+1/2,-Y,Z+1/2                                         
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        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       26.29400            
REMARK 290   SMTRY2   3  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       82.91350            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       26.29400            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       82.91350            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3                                                 
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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: 3                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 7470 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 85600 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -335.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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   BIOMT1   2 -1.000000  0.000000  0.000000      105.17600            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      165.82700            
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   3  1.000000  0.000000  0.000000       26.29400            
REMARK 350   BIOMT2   3  0.000000 -1.000000  0.000000      298.42600            
REMARK 350   BIOMT3   3  0.000000  0.000000 -1.000000       82.91350            
REMARK 350   BIOMT1   4 -1.000000  0.000000  0.000000       78.88200            
REMARK 350   BIOMT2   4  0.000000 -1.000000  0.000000      298.42600            
REMARK 350   BIOMT3   4  0.000000  0.000000  1.000000       82.91350            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A 725  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 818  LIES ON A SPECIAL POSITION.                          
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     ASP A     0                                                      
REMARK 465     GLN A     1                                                      
REMARK 465     MET A     2                                                      
REMARK 465     PRO A     3                                                      
REMARK 465     ILE A     4                                                      
REMARK 465     PRO A     5                                                      
REMARK 465     VAL A     6                                                      
REMARK 465     SER A     7                                                      
REMARK 465     ARG A     8                                                      
REMARK 465     GLU A     9                                                      
REMARK 465     GLU A    10                                                      
REMARK 465     GLN A    11                                                      
REMARK 465     GLU A    12                                                      
REMARK 465     GLN A    13                                                      
REMARK 465     HIS A    14                                                      
REMARK 465     TYR A    15                                                      
REMARK 465     LYS A   227                                                      
REMARK 465     GLY A   228                                                      
REMARK 465     ALA A   229                                                      
REMARK 465     GLY A   230                                                      
REMARK 465     GLU A   231                                                      
REMARK 465     VAL A   232                                                      
REMARK 465     SER A   233                                                      
REMARK 465     PRO A   234                                                      
REMARK 465     ALA A   235                                                      
REMARK 465     GLU A   236                                                      
REMARK 465     HIS A   237                                                      
REMARK 465     SER A   238                                                      
REMARK 465     SER A   239                                                      
REMARK 465     LYS A   240                                                      
REMARK 465     PRO A   241                                                      
REMARK 465     THR A   242                                                      
REMARK 465     ASP A   243                                                      
REMARK 465     ILE A   244                                                      
REMARK 465     SER A   245                                                      
REMARK 465     ALA A   246                                                      
REMARK 465     LYS A   247                                                      
REMARK 465     ARG A   366                                                      
REMARK 465     ILE A   367                                                      
REMARK 465     PRO A   368                                                      
REMARK 465     LEU A   369                                                      
REMARK 465     GLN A   370                                                      
REMARK 465     ASP A   371                                                      
REMARK 465     ASP A   372                                                      
REMARK 465     LEU A   373                                                      
REMARK 465     LYS A   374                                                      
REMARK 465     ASP A   375                                                      
REMARK 465     ALA A   376                                                      
REMARK 465     SER A   377                                                      
REMARK 465     VAL A   378                                                      
REMARK 465     THR A   379                                                      
REMARK 465     ALA A   380                                                      
REMARK 465     SER A   381                                                      
REMARK 465     VAL A   382                                                      
REMARK 465     ASN A   383                                                      
REMARK 465     ALA A   384                                                      
REMARK 465     ASP A   385                                                      
REMARK 465     THR A   390                                                      
REMARK 465     ASP A   391                                                      
REMARK 465     ASN A   392                                                      
REMARK 465     GLY A   393                                                      
REMARK 465     LYS A   394                                                      
REMARK 465     LYS A   527                                                      
REMARK 465     ILE A   528                                                      
REMARK 465     ASP B     0                                                      
REMARK 465     GLN B     1                                                      
REMARK 465     MET B     2                                                      
REMARK 465     PRO B     3                                                      
REMARK 465     ILE B     4                                                      
REMARK 465     PRO B     5                                                      
REMARK 465     VAL B     6                                                      
REMARK 465     SER B     7                                                      
REMARK 465     ARG B     8                                                      
REMARK 465     GLU B     9                                                      
REMARK 465     GLU B    10                                                      
REMARK 465     GLN B    11                                                      
REMARK 465     GLU B    12                                                      
REMARK 465     GLN B    13                                                      
REMARK 465     HIS B    14                                                      
REMARK 465     TYR B    15                                                      
REMARK 465     GLU B    73                                                      
REMARK 465     GLU B    74                                                      
REMARK 465     ILE B    75                                                      
REMARK 465     GLN B    76                                                      
REMARK 465     ASP B   114                                                      
REMARK 465     ASP B   115                                                      
REMARK 465     GLU B   206                                                      
REMARK 465     LYS B   207                                                      
REMARK 465     THR B   208                                                      
REMARK 465     SER B   209                                                      
REMARK 465     ASN B   210                                                      
REMARK 465     PHE B   211                                                      
REMARK 465     ASN B   212                                                      
REMARK 465     ALA B   213                                                      
REMARK 465     GLU B   226                                                      
REMARK 465     LYS B   227                                                      
REMARK 465     GLY B   228                                                      
REMARK 465     ALA B   229                                                      
REMARK 465     GLY B   230                                                      
REMARK 465     GLU B   231                                                      
REMARK 465     VAL B   232                                                      
REMARK 465     SER B   233                                                      
REMARK 465     PRO B   234                                                      
REMARK 465     ALA B   235                                                      
REMARK 465     GLU B   236                                                      
REMARK 465     HIS B   237                                                      
REMARK 465     SER B   238                                                      
REMARK 465     SER B   239                                                      
REMARK 465     LYS B   240                                                      
REMARK 465     PRO B   241                                                      
REMARK 465     THR B   242                                                      
REMARK 465     ASP B   243                                                      
REMARK 465     ILE B   244                                                      
REMARK 465     SER B   245                                                      
REMARK 465     ALA B   246                                                      
REMARK 465     LYS B   247                                                      
REMARK 465     PHE B   248                                                      
REMARK 465     LEU B   365                                                      
REMARK 465     ARG B   366                                                      
REMARK 465     ILE B   367                                                      
REMARK 465     PRO B   368                                                      
REMARK 465     LEU B   369                                                      
REMARK 465     GLN B   370                                                      
REMARK 465     ASP B   371                                                      
REMARK 465     ASP B   372                                                      
REMARK 465     LEU B   373                                                      
REMARK 465     LYS B   374                                                      
REMARK 465     ASP B   375                                                      
REMARK 465     ALA B   376                                                      
REMARK 465     SER B   377                                                      
REMARK 465     VAL B   378                                                      
REMARK 465     THR B   379                                                      
REMARK 465     ALA B   380                                                      
REMARK 465     SER B   381                                                      
REMARK 465     VAL B   382                                                      
REMARK 465     ASN B   383                                                      
REMARK 465     ALA B   384                                                      
REMARK 465     ASP B   385                                                      
REMARK 465     THR B   390                                                      
REMARK 465     ASP B   391                                                      
REMARK 465     ASN B   392                                                      
REMARK 465     GLY B   393                                                      
REMARK 465     LYS B   527                                                      
REMARK 465     ILE B   528                                                      
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  37    CG   CD   CE   NZ                                   
REMARK 470     LYS A  54    CG   CD   CE   NZ                                   
REMARK 470     GLU A  73    CG   CD   OE1  OE2                                  
REMARK 470     GLU A  74    CG   CD   OE1  OE2                                  
REMARK 470     ILE A  75    CG1  CG2  CD1                                       
REMARK 470     ARG A 121    NE   CZ   NH1  NH2                                  
REMARK 470     ARG A 163    NE   CZ   NH1  NH2                                  
REMARK 470     GLU A 165    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 166    CG   CD   CE   NZ                                   
REMARK 470     ARG A 205    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 226    CG   CD   OE1  OE2                                  
REMARK 470     PHE A 248    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LYS A 270    CD   CE   NZ                                        
REMARK 470     MET A 363    CG   SD   CE                                        
REMARK 470     ASP A 364    CG   OD1  OD2                                       
REMARK 470     LEU A 365    CG   CD1  CD2                                       
REMARK 470     LYS A 389    CG   CD   CE   NZ                                   
REMARK 470     ARG A 400    NE   CZ   NH1  NH2                                  
REMARK 470     ASP A 401    CG   OD1  OD2                                       
REMARK 470     PHE A 433    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LYS A 435    CG   CD   CE   NZ                                   
REMARK 470     MET A 515    CG   SD   CE                                        
REMARK 470     MET A 516    CG   SD   CE                                        
REMARK 470     ARG A 518    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN A 526    CG   CD   OE1  NE2                                  
REMARK 470     GLU B  71    CG   CD   OE1  OE2                                  
REMARK 470     GLU B  77    CG   CD   OE1  OE2                                  
REMARK 470     ARG B 117    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B 121    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 166    CG   CD   CE   NZ                                   
REMARK 470     ARG B 205    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP B 214    CG   OD1  OD2                                       
REMARK 470     LYS B 389    CG   CD   CE   NZ                                   
REMARK 470     LYS B 394    CG   CD   CE   NZ                                   
REMARK 470     ARG B 400    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 466    CG   CD   CE   NZ                                   
REMARK 470     TYR B 494    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     MET B 515    CG   SD   CE                                        
REMARK 470     ARG B 518    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN B 526    CG   CD   OE1  NE2                                  
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 121     -129.05     61.57                                   
REMARK 500    ALA A 125       85.31   -150.95                                   
REMARK 500    CYS A 159       71.51   -113.59                                   
REMARK 500    GLU A 165      -96.05     64.16                                   
REMARK 500    SER A 268      -22.25   -146.64                                   
REMARK 500    ASP A 401       31.19    -74.50                                   
REMARK 500    ARG A 518       -8.93   -142.53                                   
REMARK 500    ARG B 121     -104.19     48.01                                   
REMARK 500    ALA B 125       83.80   -150.36                                   
REMARK 500    LYS B 186       10.76     50.85                                   
REMARK 500    ASP B 401       48.47    -81.70                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 830        DISTANCE =  6.01 ANGSTROMS                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 602  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 LEU A  95   O                                                      
REMARK 620 2 ASN A  98   OD1  73.9                                              
REMARK 620 3 ASP A 100   O   175.8 103.3                                        
REMARK 620 4 ASP A 102   OD2  78.7  74.4  97.7                                  
REMARK 620 5 ASP A 108   OD2 100.9 174.8  82.0 105.1                            
REMARK 620 6 GLU A 109   OE2  97.9  93.6  85.2 168.0  86.8                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 604  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SER A 209   O                                                      
REMARK 620 2 ASN A 212   O    88.6                                              
REMARK 620 3 ASP A 214   O   166.8  91.2                                        
REMARK 620 4 HOH A 743   O    79.2 101.2  87.9                                  
REMARK 620 5 HOH A 770   O    99.6  84.4  93.5 174.2                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B 602  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 LEU B  95   O                                                      
REMARK 620 2 ASN B  98   OD1  82.1                                              
REMARK 620 3 ASP B 100   O   171.2  91.6                                        
REMARK 620 4 ASP B 102   OD2  86.5  79.3  86.3                                  
REMARK 620 5 ASP B 108   OD2  96.5 172.7  89.0  93.5                            
REMARK 620 6 GLU B 109   OE2  98.0  83.2  87.2 161.1 104.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 607  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 525   NE2                                                    
REMARK 620 2 HOH A 821   O    74.8                                              
REMARK 620 N                    1                                               
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 601                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 602                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 604                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 606                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 601                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA B 602                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG B 604                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 606                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 607                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 603 bound   
REMARK 800  to THR A 501                                                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 603 bound   
REMARK 800  to THR B 501                                                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues TRP A    
REMARK 800  26 through BMA A 605                                                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues TRP B    
REMARK 800  26 through BMA B 605                                                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: EMD-7773   RELATED DB: EMDB                              
REMARK 900 POLYC9                                                               
DBREF  6CXO A    1   528  UNP    P06683   CO9_MOUSE       21    548             
DBREF  6CXO B    1   528  UNP    P06683   CO9_MOUSE       21    548             
SEQADV 6CXO ASP A    0  UNP  P06683              EXPRESSION TAG                 
SEQADV 6CXO GLU A   28  UNP  P06683    ASN    48 ENGINEERED MUTATION            
SEQADV 6CXO ASP A  243  UNP  P06683    ASN   263 ENGINEERED MUTATION            
SEQADV 6CXO ASP A  397  UNP  P06683    ASN   417 ENGINEERED MUTATION            
SEQADV 6CXO ASP B    0  UNP  P06683              EXPRESSION TAG                 
SEQADV 6CXO GLU B   28  UNP  P06683    ASN    48 ENGINEERED MUTATION            
SEQADV 6CXO ASP B  243  UNP  P06683    ASN   263 ENGINEERED MUTATION            
SEQADV 6CXO ASP B  397  UNP  P06683    ASN   417 ENGINEERED MUTATION            
SEQRES   1 A  529  ASP GLN MET PRO ILE PRO VAL SER ARG GLU GLU GLN GLU          
SEQRES   2 A  529  GLN HIS TYR PRO ILE PRO ILE ASP CYS ARG MET SER PRO          
SEQRES   3 A  529  TRP SER GLU TRP SER GLU CYS ASP PRO CYS LEU LYS GLN          
SEQRES   4 A  529  ARG PHE ARG SER ARG SER ILE LEU ALA PHE GLY GLN PHE          
SEQRES   5 A  529  ASN GLY LYS SER CYS VAL ASP VAL LEU GLY ASP ARG GLN          
SEQRES   6 A  529  GLY CYS GLU PRO THR GLN GLU CYS GLU GLU ILE GLN GLU          
SEQRES   7 A  529  ASN CYS GLY ASN ASP PHE GLN CYS GLU THR GLY ARG CYS          
SEQRES   8 A  529  ILE LYS ARG ARG LEU LEU CYS ASN GLY ASP ASN ASP CYS          
SEQRES   9 A  529  GLY ASP TYR SER ASP GLU ASN ASP CYS ASP ASP ASP PRO          
SEQRES  10 A  529  ARG THR PRO CYS ARG ASP ARG VAL ALA GLU GLU SER GLU          
SEQRES  11 A  529  LEU GLY LEU THR ALA GLY TYR GLY ILE ASN ILE LEU GLY          
SEQRES  12 A  529  MET GLU PRO LEU ARG THR PRO PHE ASP ASN GLU PHE TYR          
SEQRES  13 A  529  ASN GLY LEU CYS ASP ARG VAL ARG ASP GLU LYS THR TYR          
SEQRES  14 A  529  TYR ARG LYS PRO TRP ASN VAL VAL SER LEU ILE TYR GLU          
SEQRES  15 A  529  THR LYS ALA ASP LYS SER PHE ARG THR GLU ASN TYR ASP          
SEQRES  16 A  529  GLU HIS LEU GLU VAL PHE LYS ALA ILE ASN ARG GLU LYS          
SEQRES  17 A  529  THR SER ASN PHE ASN ALA ASP PHE ALA LEU LYS PHE SER          
SEQRES  18 A  529  ALA THR GLU VAL PRO GLU LYS GLY ALA GLY GLU VAL SER          
SEQRES  19 A  529  PRO ALA GLU HIS SER SER LYS PRO THR ASP ILE SER ALA          
SEQRES  20 A  529  LYS PHE LYS PHE SER TYR PHE MET GLY LYS ASN PHE ARG          
SEQRES  21 A  529  ARG LEU SER SER TYR PHE SER GLN SER LYS LYS MET PHE          
SEQRES  22 A  529  VAL HIS LEU ARG GLY VAL VAL GLN LEU GLY ARG PHE VAL          
SEQRES  23 A  529  MET ARG ASN ARG ASP VAL VAL LEU ARG SER THR PHE LEU          
SEQRES  24 A  529  ASP ASP VAL LYS ALA LEU PRO THR SER TYR GLU LYS GLY          
SEQRES  25 A  529  GLU TYR PHE GLY PHE LEU GLU THR TYR GLY THR HIS TYR          
SEQRES  26 A  529  SER THR SER GLY SER LEU GLY GLY GLN TYR GLU ILE VAL          
SEQRES  27 A  529  TYR VAL LEU ASP LYS ALA SER MET LYS GLU LYS GLY VAL          
SEQRES  28 A  529  ASP LEU ASN ASP VAL LYS HIS CYS LEU GLY PHE ASN MET          
SEQRES  29 A  529  ASP LEU ARG ILE PRO LEU GLN ASP ASP LEU LYS ASP ALA          
SEQRES  30 A  529  SER VAL THR ALA SER VAL ASN ALA ASP GLY CYS ILE LYS          
SEQRES  31 A  529  THR ASP ASN GLY LYS THR VAL ASP ILE THR ARG ASP ASN          
SEQRES  32 A  529  ILE ILE ASP ASP VAL ILE SER PHE ILE ARG GLY GLY THR          
SEQRES  33 A  529  ARG GLU GLN ALA ILE LEU LEU LYS GLU LYS ILE LEU ARG          
SEQRES  34 A  529  GLY ASP LYS THR PHE ASP LYS THR ASP PHE ALA ASN TRP          
SEQRES  35 A  529  ALA SER SER LEU ALA ASN ALA PRO ALA LEU ILE SER GLN          
SEQRES  36 A  529  ARG MET SER PRO ILE TYR ASN LEU ILE PRO LEU LYS ILE          
SEQRES  37 A  529  LYS ASP ALA TYR ILE LYS LYS GLN ASN LEU GLU LYS ALA          
SEQRES  38 A  529  VAL GLU ASP TYR ILE ASP GLU PHE SER THR LYS ARG CYS          
SEQRES  39 A  529  TYR PRO CYS LEU ASN GLY GLY THR ILE ILE LEU LEU ASP          
SEQRES  40 A  529  GLY GLN CYS LEU CYS SER CYS PRO MET MET PHE ARG GLY          
SEQRES  41 A  529  MET ALA CYS GLU ILE HIS GLN LYS ILE                          
SEQRES   1 B  529  ASP GLN MET PRO ILE PRO VAL SER ARG GLU GLU GLN GLU          
SEQRES   2 B  529  GLN HIS TYR PRO ILE PRO ILE ASP CYS ARG MET SER PRO          
SEQRES   3 B  529  TRP SER GLU TRP SER GLU CYS ASP PRO CYS LEU LYS GLN          
SEQRES   4 B  529  ARG PHE ARG SER ARG SER ILE LEU ALA PHE GLY GLN PHE          
SEQRES   5 B  529  ASN GLY LYS SER CYS VAL ASP VAL LEU GLY ASP ARG GLN          
SEQRES   6 B  529  GLY CYS GLU PRO THR GLN GLU CYS GLU GLU ILE GLN GLU          
SEQRES   7 B  529  ASN CYS GLY ASN ASP PHE GLN CYS GLU THR GLY ARG CYS          
SEQRES   8 B  529  ILE LYS ARG ARG LEU LEU CYS ASN GLY ASP ASN ASP CYS          
SEQRES   9 B  529  GLY ASP TYR SER ASP GLU ASN ASP CYS ASP ASP ASP PRO          
SEQRES  10 B  529  ARG THR PRO CYS ARG ASP ARG VAL ALA GLU GLU SER GLU          
SEQRES  11 B  529  LEU GLY LEU THR ALA GLY TYR GLY ILE ASN ILE LEU GLY          
SEQRES  12 B  529  MET GLU PRO LEU ARG THR PRO PHE ASP ASN GLU PHE TYR          
SEQRES  13 B  529  ASN GLY LEU CYS ASP ARG VAL ARG ASP GLU LYS THR TYR          
SEQRES  14 B  529  TYR ARG LYS PRO TRP ASN VAL VAL SER LEU ILE TYR GLU          
SEQRES  15 B  529  THR LYS ALA ASP LYS SER PHE ARG THR GLU ASN TYR ASP          
SEQRES  16 B  529  GLU HIS LEU GLU VAL PHE LYS ALA ILE ASN ARG GLU LYS          
SEQRES  17 B  529  THR SER ASN PHE ASN ALA ASP PHE ALA LEU LYS PHE SER          
SEQRES  18 B  529  ALA THR GLU VAL PRO GLU LYS GLY ALA GLY GLU VAL SER          
SEQRES  19 B  529  PRO ALA GLU HIS SER SER LYS PRO THR ASP ILE SER ALA          
SEQRES  20 B  529  LYS PHE LYS PHE SER TYR PHE MET GLY LYS ASN PHE ARG          
SEQRES  21 B  529  ARG LEU SER SER TYR PHE SER GLN SER LYS LYS MET PHE          
SEQRES  22 B  529  VAL HIS LEU ARG GLY VAL VAL GLN LEU GLY ARG PHE VAL          
SEQRES  23 B  529  MET ARG ASN ARG ASP VAL VAL LEU ARG SER THR PHE LEU          
SEQRES  24 B  529  ASP ASP VAL LYS ALA LEU PRO THR SER TYR GLU LYS GLY          
SEQRES  25 B  529  GLU TYR PHE GLY PHE LEU GLU THR TYR GLY THR HIS TYR          
SEQRES  26 B  529  SER THR SER GLY SER LEU GLY GLY GLN TYR GLU ILE VAL          
SEQRES  27 B  529  TYR VAL LEU ASP LYS ALA SER MET LYS GLU LYS GLY VAL          
SEQRES  28 B  529  ASP LEU ASN ASP VAL LYS HIS CYS LEU GLY PHE ASN MET          
SEQRES  29 B  529  ASP LEU ARG ILE PRO LEU GLN ASP ASP LEU LYS ASP ALA          
SEQRES  30 B  529  SER VAL THR ALA SER VAL ASN ALA ASP GLY CYS ILE LYS          
SEQRES  31 B  529  THR ASP ASN GLY LYS THR VAL ASP ILE THR ARG ASP ASN          
SEQRES  32 B  529  ILE ILE ASP ASP VAL ILE SER PHE ILE ARG GLY GLY THR          
SEQRES  33 B  529  ARG GLU GLN ALA ILE LEU LEU LYS GLU LYS ILE LEU ARG          
SEQRES  34 B  529  GLY ASP LYS THR PHE ASP LYS THR ASP PHE ALA ASN TRP          
SEQRES  35 B  529  ALA SER SER LEU ALA ASN ALA PRO ALA LEU ILE SER GLN          
SEQRES  36 B  529  ARG MET SER PRO ILE TYR ASN LEU ILE PRO LEU LYS ILE          
SEQRES  37 B  529  LYS ASP ALA TYR ILE LYS LYS GLN ASN LEU GLU LYS ALA          
SEQRES  38 B  529  VAL GLU ASP TYR ILE ASP GLU PHE SER THR LYS ARG CYS          
SEQRES  39 B  529  TYR PRO CYS LEU ASN GLY GLY THR ILE ILE LEU LEU ASP          
SEQRES  40 B  529  GLY GLN CYS LEU CYS SER CYS PRO MET MET PHE ARG GLY          
SEQRES  41 B  529  MET ALA CYS GLU ILE HIS GLN LYS ILE                          
HET     ZN  A 601       1                                                       
HET     CA  A 602       1                                                       
HET    NAG  A 603      14                                                       
HET     MG  A 604       1                                                       
HET    BMA  A 605      11                                                       
HET     ZN  A 606       1                                                       
HET     ZN  B 601       1                                                       
HET     CA  B 602       1                                                       
HET    NAG  B 603      14                                                       
HET     MG  B 604       1                                                       
HET    BMA  B 605      11                                                       
HET     ZN  B 606       1                                                       
HET     ZN  B 607       1                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM      CA CALCIUM ION                                                      
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     BMA BETA-D-MANNOSE                                                   
FORMUL   3   ZN    5(ZN 2+)                                                     
FORMUL   4   CA    2(CA 2+)                                                     
FORMUL   5  NAG    2(C8 H15 N O6)                                               
FORMUL   6   MG    2(MG 2+)                                                     
FORMUL   7  BMA    2(C6 H12 O6)                                                 
FORMUL  16  HOH   *335(H2 O)                                                    
HELIX    1 AA1 LYS A   92  LEU A   96  5                                   5    
HELIX    2 AA2 SER A  128  ALA A  134  1                                   7    
HELIX    3 AA3 GLU A  195  LYS A  207  1                                  13    
HELIX    4 AA4 THR A  208  ASN A  212  5                                   5    
HELIX    5 AA5 PHE A  253  SER A  263  1                                  11    
HELIX    6 AA6 ARG A  294  ALA A  303  1                                  10    
HELIX    7 AA7 GLU A  309  GLY A  321  1                                  13    
HELIX    8 AA8 LYS A  342  LYS A  348  1                                   7    
HELIX    9 AA9 ASP A  351  GLY A  360  1                                  10    
HELIX   10 AB1 THR A  415  GLY A  429  1                                  15    
HELIX   11 AB2 ASP A  434  SER A  444  1                                  11    
HELIX   12 AB3 TYR A  460  ILE A  463  5                                   4    
HELIX   13 AB4 ASP A  469  PHE A  488  1                                  20    
HELIX   14 AB5 SER A  489  CYS A  493  5                                   5    
HELIX   15 AB6 LYS B   92  LEU B   96  5                                   5    
HELIX   16 AB7 SER B  128  ALA B  134  1                                   7    
HELIX   17 AB8 GLU B  195  ARG B  205  1                                  11    
HELIX   18 AB9 PHE B  253  SER B  263  1                                  11    
HELIX   19 AC1 ARG B  294  ALA B  303  1                                  10    
HELIX   20 AC2 GLU B  309  GLY B  321  1                                  13    
HELIX   21 AC3 LYS B  342  GLY B  349  1                                   8    
HELIX   22 AC4 ASP B  351  GLY B  360  1                                  10    
HELIX   23 AC5 THR B  415  ARG B  428  1                                  14    
HELIX   24 AC6 ASP B  434  LEU B  445  1                                  12    
HELIX   25 AC7 TYR B  460  ILE B  463  5                                   4    
HELIX   26 AC8 ASP B  469  PHE B  488  1                                  20    
HELIX   27 AC9 SER B  489  CYS B  493  5                                   5    
SHEET    1 AA1 2 ARG A  22  MET A  23  0                                        
SHEET    2 AA1 2 ILE A  45  ALA A  47 -1  O  LEU A  46   N  ARG A  22           
SHEET    1 AA2 2 GLN A  38  SER A  42  0                                        
SHEET    2 AA2 2 GLY A  61  GLY A  65 -1  O  ASP A  62   N  ARG A  41           
SHEET    1 AA3 4 GLY A  49  GLN A  50  0                                        
SHEET    2 AA3 4 GLN A 508  SER A 512  1  O  CYS A 509   N  GLY A  49           
SHEET    3 AA3 4 THR A 501  LEU A 505 -1  N  ILE A 503   O  LEU A 510           
SHEET    4 AA3 4 ALA A 216  LEU A 217  1  N  LEU A 217   O  LEU A 504           
SHEET    1 AA4 2 PHE A  83  GLN A  84  0                                        
SHEET    2 AA4 2 CYS A  90  ILE A  91 -1  O  ILE A  91   N  PHE A  83           
SHEET    1 AA5 3 GLU A 126  GLU A 127  0                                        
SHEET    2 AA5 3 THR A 167  ARG A 170  1  O  ARG A 170   N  GLU A 126           
SHEET    3 AA5 3 ARG A 161  ASP A 164 -1  N  VAL A 162   O  TYR A 169           
SHEET    1 AA6 4 ARG A 189  TYR A 193  0                                        
SHEET    2 AA6 4 LYS A 270  MET A 286 -1  O  HIS A 274   N  GLU A 191           
SHEET    3 AA6 4 HIS A 323  ASP A 341 -1  O  TYR A 334   N  GLY A 277           
SHEET    4 AA6 4 ILE A 404  SER A 409 -1  O  ILE A 408   N  VAL A 337           
SHEET    1 AA7 3 GLY A 137  ILE A 138  0                                        
SHEET    2 AA7 3 HIS A 323  ASP A 341 -1  O  HIS A 323   N  ILE A 138           
SHEET    3 AA7 3 ILE A 404  SER A 409 -1  O  ILE A 408   N  VAL A 337           
SHEET    1 AA8 3 ALA A 450  PRO A 458  0                                        
SHEET    2 AA8 3 HIS A 323  ASP A 341 -1  N  SER A 329   O  ILE A 452           
SHEET    3 AA8 3 GLY A 137  ILE A 138 -1  N  ILE A 138   O  HIS A 323           
SHEET    1 AA9 4 VAL A 175  ALA A 184  0                                        
SHEET    2 AA9 4 LYS A 270  MET A 286 -1  O  ARG A 283   N  ILE A 179           
SHEET    3 AA9 4 HIS A 323  ASP A 341 -1  O  TYR A 334   N  GLY A 277           
SHEET    4 AA9 4 ALA A 450  PRO A 458 -1  O  ILE A 452   N  SER A 329           
SHEET    1 AB1 3 ARG A 189  TYR A 193  0                                        
SHEET    2 AB1 3 LYS A 270  MET A 286 -1  O  HIS A 274   N  GLU A 191           
SHEET    3 AB1 3 VAL A 175  ALA A 184 -1  N  ILE A 179   O  ARG A 283           
SHEET    1 AB2 2 ARG B  22  MET B  23  0                                        
SHEET    2 AB2 2 ILE B  45  ALA B  47 -1  O  ALA B  47   N  ARG B  22           
SHEET    1 AB3 2 GLN B  38  SER B  42  0                                        
SHEET    2 AB3 2 GLY B  61  GLY B  65 -1  O  ASP B  62   N  ARG B  41           
SHEET    1 AB4 4 GLY B  49  GLN B  50  0                                        
SHEET    2 AB4 4 GLN B 508  SER B 512  1  O  CYS B 509   N  GLY B  49           
SHEET    3 AB4 4 THR B 501  LEU B 505 -1  N  ILE B 503   O  LEU B 510           
SHEET    4 AB4 4 ALA B 216  LEU B 217  1  N  LEU B 217   O  LEU B 504           
SHEET    1 AB5 2 PHE B  83  GLN B  84  0                                        
SHEET    2 AB5 2 CYS B  90  ILE B  91 -1  O  ILE B  91   N  PHE B  83           
SHEET    1 AB6 2 ARG B 161  ARG B 163  0                                        
SHEET    2 AB6 2 TYR B 168  ARG B 170 -1  O  TYR B 169   N  VAL B 162           
SHEET    1 AB7 4 VAL B 175  ALA B 184  0                                        
SHEET    2 AB7 4 LYS B 270  MET B 286 -1  O  GLN B 280   N  LYS B 183           
SHEET    3 AB7 4 HIS B 323  ASP B 341 -1  O  LEU B 340   N  MET B 271           
SHEET    4 AB7 4 ILE B 404  SER B 409 -1  O  ILE B 408   N  VAL B 337           
SHEET    1 AB8 4 ARG B 189  TYR B 193  0                                        
SHEET    2 AB8 4 LYS B 270  MET B 286 -1  O  ARG B 276   N  ARG B 189           
SHEET    3 AB8 4 HIS B 323  ASP B 341 -1  O  LEU B 340   N  MET B 271           
SHEET    4 AB8 4 ALA B 450  PRO B 458 -1  O  ALA B 450   N  GLY B 331           
SHEET    1 AB9 2 PHE B 517  ARG B 518  0                                        
SHEET    2 AB9 2 ILE B 524  HIS B 525 -1  O  ILE B 524   N  ARG B 518           
SSBOND   1 CYS A   21    CYS A   56                          1555   1555  2.04  
SSBOND   2 CYS A   32    CYS A   66                          1555   1555  2.03  
SSBOND   3 CYS A   79    CYS A   90                          1555   1555  2.04  
SSBOND   4 CYS A   85    CYS A  103                          1555   1555  2.03  
SSBOND   5 CYS A   97    CYS A  112                          1555   1555  2.04  
SSBOND   6 CYS A  120    CYS A  159                          1555   1555  2.05  
SSBOND   7 CYS A  358    CYS A  387                          1555   1555  2.05  
SSBOND   8 CYS A  493    CYS A  509                          1555   1555  2.02  
SSBOND   9 CYS A  496    CYS A  511                          1555   1555  2.04  
SSBOND  10 CYS A  513    CYS A  522                          1555   1555  2.04  
SSBOND  11 CYS B   21    CYS B   56                          1555   1555  2.04  
SSBOND  12 CYS B   32    CYS B   66                          1555   1555  2.04  
SSBOND  13 CYS B   79    CYS B   90                          1555   1555  2.04  
SSBOND  14 CYS B   85    CYS B  103                          1555   1555  2.03  
SSBOND  15 CYS B   97    CYS B  112                          1555   1555  2.04  
SSBOND  16 CYS B  120    CYS B  159                          1555   1555  2.05  
SSBOND  17 CYS B  358    CYS B  387                          1555   1555  2.04  
SSBOND  18 CYS B  493    CYS B  509                          1555   1555  2.02  
SSBOND  19 CYS B  496    CYS B  511                          1555   1555  2.04  
SSBOND  20 CYS B  513    CYS B  522                          1555   1555  2.03  
LINK         CD1 TRP A  26                 C1  BMA A 605     1555   1555  1.50  
LINK         O   LEU A  95                CA    CA A 602     1555   1555  2.48  
LINK         OD1 ASN A  98                CA    CA A 602     1555   1555  2.18  
LINK         O   ASP A 100                CA    CA A 602     1555   1555  2.31  
LINK         OD2 ASP A 102                CA    CA A 602     1555   1555  2.56  
LINK         OD2 ASP A 108                CA    CA A 602     1555   1555  2.12  
LINK         OE2 GLU A 109                CA    CA A 602     1555   1555  2.42  
LINK         O   SER A 209                MG    MG A 604     1555   1555  2.26  
LINK         O   ASN A 212                MG    MG A 604     1555   1555  1.95  
LINK         O   ASP A 214                MG    MG A 604     1555   1555  2.61  
LINK         OG1 THR A 501                 C1  NAG A 603     1555   1555  1.41  
LINK         CD1 TRP B  26                 C1  BMA B 605     1555   1555  1.50  
LINK         O   LEU B  95                CA    CA B 602     1555   1555  2.29  
LINK         OD1 ASN B  98                CA    CA B 602     1555   1555  2.31  
LINK         O   ASP B 100                CA    CA B 602     1555   1555  2.29  
LINK         OD2 ASP B 102                CA    CA B 602     1555   1555  2.50  
LINK         OD2 ASP B 108                CA    CA B 602     1555   1555  2.29  
LINK         OE2 GLU B 109                CA    CA B 602     1555   1555  2.45  
LINK         OG1 THR B 501                 C1  NAG B 603     1555   1555  1.43  
LINK        MG    MG A 604                 O   HOH A 743     1555   1555  2.55  
LINK        MG    MG A 604                 O   HOH A 770     1555   1555  2.27  
LINK        ZN    ZN B 601                 O   HOH B 733     1555   1555  2.51  
LINK         NE2 HIS A 525                ZN    ZN B 607     1555   3475  2.28  
LINK        ZN    ZN B 607                 O   HOH A 821     1555   3575  2.70  
SITE     1 AC1  2 ASP A 194  HIS A 196                                          
SITE     1 AC2  6 LEU A  95  ASN A  98  ASP A 100  ASP A 102                    
SITE     2 AC2  6 ASP A 108  GLU A 109                                          
SITE     1 AC3  5 SER A 209  ASN A 212  ASP A 214  HOH A 743                    
SITE     2 AC3  5 HOH A 770                                                     
SITE     1 AC4  2 HIS A 357  ASN A 362                                          
SITE     1 AC5  3 ASP B 194  HIS B 196  HOH B 733                               
SITE     1 AC6  6 LEU B  95  ASN B  98  ASP B 100  ASP B 102                    
SITE     2 AC6  6 ASP B 108  GLU B 109                                          
SITE     1 AC7  2 ASN B 204  ASP B 214                                          
SITE     1 AC8  2 HIS B 357  ASN B 362                                          
SITE     1 AC9  3 HIS A 525  HOH A 821  HIS B 525                               
SITE     1 AD1  6 LYS A 346  THR A 501  SER A 512  CYS A 513                    
SITE     2 AD1  6 PRO A 514  HOH A 801                                          
SITE     1 AD2  8 HIS B 196  LEU B 197  LYS B 346  GLY B 499                    
SITE     2 AD2  8 THR B 501  SER B 512  CYS B 513  HOH B 771                    
SITE     1 AD3  9 SER A  24  PRO A  25  SER A  27  ARG A  41                    
SITE     2 AD3  9 SER A  42  ARG A  43  LEU A  60  GLY A  61                    
SITE     3 AD3  9 ASP A  62                                                     
SITE     1 AD4 14 SER B  24  PRO B  25  SER B  27  ARG B  41                    
SITE     2 AD4 14 SER B  42  ARG B  43  LEU B  60  GLY B  61                    
SITE     3 AD4 14 ASP B  62  GLU B 478  HOH B 709  HOH B 763                    
SITE     4 AD4 14 HOH B 806  HOH B 822                                          
CRYST1   52.588  149.213  165.827  90.00  90.00  90.00 P 21 2 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      0.019016  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006702  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006030        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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