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Database: PDB
Entry: 3OJY
LinkDB: 3OJY
Original site: 3OJY 
HEADER    IMMUNE SYSTEM                           23-AUG-10   3OJY              
TITLE     CRYSTAL STRUCTURE OF HUMAN COMPLEMENT COMPONENT C8                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: COMPLEMENT COMPONENT C8 ALPHA CHAIN;                       
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 31-584;                                       
COMPND   5 SYNONYM: COMPLEMENT COMPONENT 8 SUBUNIT ALPHA;                       
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: COMPLEMENT COMPONENT C8 BETA CHAIN;                        
COMPND   8 CHAIN: B;                                                            
COMPND   9 FRAGMENT: UNP RESIDUES 55-591;                                       
COMPND  10 SYNONYM: COMPLEMENT COMPONENT 8 SUBUNIT BETA;                        
COMPND  11 MOL_ID: 3;                                                           
COMPND  12 MOLECULE: COMPLEMENT COMPONENT C8 GAMMA CHAIN;                       
COMPND  13 CHAIN: C;                                                            
COMPND  14 FRAGMENT: UNP RESIDUES 21-202                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 TISSUE: BLOOD;                                                       
SOURCE   6 OTHER_DETAILS: PLASMA COHN FRACTION III;                             
SOURCE   7 MOL_ID: 2;                                                           
SOURCE   8 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   9 ORGANISM_COMMON: HUMAN;                                              
SOURCE  10 ORGANISM_TAXID: 9606;                                                
SOURCE  11 TISSUE: BLOOD;                                                       
SOURCE  12 OTHER_DETAILS: PLASMA COHN FRACTION III;                             
SOURCE  13 MOL_ID: 3;                                                           
SOURCE  14 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  15 ORGANISM_COMMON: HUMAN;                                              
SOURCE  16 ORGANISM_TAXID: 9606;                                                
SOURCE  17 TISSUE: BLOOD;                                                       
SOURCE  18 OTHER_DETAILS: PLASMA COHN FRACTION III                              
KEYWDS    MACPF, LIPOCALIN, COMPLEMENT, IMMUNE SYSTEM                           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    L.L.LOVELACE,C.L.COOPER,J.M.SODETZ,L.LEBIODA                          
REVDAT   4   08-NOV-17 3OJY    1       REMARK                                   
REVDAT   3   16-APR-14 3OJY    1       REMARK                                   
REVDAT   2   26-OCT-11 3OJY    1       JRNL   VERSN                             
REVDAT   1   13-APR-11 3OJY    0                                                
JRNL        AUTH   L.L.LOVELACE,C.L.COOPER,J.M.SODETZ,L.LEBIODA                 
JRNL        TITL   STRUCTURE OF HUMAN C8 PROTEIN PROVIDES MECHANISTIC INSIGHT   
JRNL        TITL 2 INTO MEMBRANE PORE FORMATION BY COMPLEMENT.                  
JRNL        REF    J.BIOL.CHEM.                  V. 286 17585 2011              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   21454577                                                     
JRNL        DOI    10.1074/JBC.M111.219766                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.51 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC                                               
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.51                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 45.69                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 93.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 44756                          
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) : 0.253                           
REMARK   3   R VALUE            (WORKING SET) : 0.249                           
REMARK   3   FREE R VALUE                     : 0.337                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2267                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.51                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.58                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2137                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 63.21                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3090                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 103                          
REMARK   3   BIN FREE R VALUE                    : 0.4530                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 9144                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 90                                      
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 52.01                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.69000                                              
REMARK   3    B22 (A**2) : 0.69000                                              
REMARK   3    B33 (A**2) : -1.04000                                             
REMARK   3    B12 (A**2) : 0.35000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.411         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.324         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 14.368        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.916                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.835                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  9461 ; 0.015 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 12799 ; 1.774 ; 1.974       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1134 ; 8.260 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   468 ;38.727 ;23.697       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1583 ;22.690 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    76 ;19.698 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1354 ; 0.132 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  7222 ; 0.008 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  5676 ; 0.820 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  9099 ; 1.565 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3785 ; 2.016 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  3700 ; 3.336 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS U VALUES : REFINED INDIVIDUALLY                           
REMARK   4                                                                      
REMARK   4 3OJY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-AUG-10.                  
REMARK 100 THE DEPOSITION ID IS D_1000061210.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 29-JUL-09                          
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               : APS                                
REMARK 200  BEAMLINE                       : 22-BM                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : NULL                               
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MAR                                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 44803                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 93.3                               
REMARK 200  DATA REDUNDANCY                : 3.200                              
REMARK 200  R MERGE                    (I) : 0.10100                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.54                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 63.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.80                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.41700                            
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: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 2RD7                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 50.67                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.49                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 14-16% PEG 4K, 100MM TAPS PH 9.0,        
REMARK 280  400MM NACL, 10MM SRCL2, VAPOR DIFFUSION, HANGING DROP,              
REMARK 280  TEMPERATURE 281K, PH 7.4                                            
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 63                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z                                                
REMARK 290       3555   -X+Y,-X,Z                                               
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+1/2                                            
REMARK 290       6555   X-Y,X,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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       63.58000            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       63.58000            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       63.58000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 10110 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 56210 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 14.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C                               
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     ALA A     1                                                      
REMARK 465     VAL A    61                                                      
REMARK 465     ARG A    62                                                      
REMARK 465     LYS A   212                                                      
REMARK 465     ASP A   213                                                      
REMARK 465     LYS A   214                                                      
REMARK 465     SER A   215                                                      
REMARK 465     ASP A   216                                                      
REMARK 465     SER A   217                                                      
REMARK 465     PHE A   218                                                      
REMARK 465     GLY A   219                                                      
REMARK 465     VAL A   220                                                      
REMARK 465     THR A   221                                                      
REMARK 465     ILE A   222                                                      
REMARK 465     GLY A   223                                                      
REMARK 465     ILE A   224                                                      
REMARK 465     GLY A   225                                                      
REMARK 465     PRO A   226                                                      
REMARK 465     ALA A   227                                                      
REMARK 465     GLY A   228                                                      
REMARK 465     SER A   229                                                      
REMARK 465     PRO A   230                                                      
REMARK 465     LEU A   231                                                      
REMARK 465     LEU A   232                                                      
REMARK 465     VAL A   233                                                      
REMARK 465     GLY A   234                                                      
REMARK 465     VAL A   235                                                      
REMARK 465     GLY A   236                                                      
REMARK 465     VAL A   237                                                      
REMARK 465     SER A   238                                                      
REMARK 465     HIS A   239                                                      
REMARK 465     SER A   240                                                      
REMARK 465     GLN A   241                                                      
REMARK 465     ASP A   242                                                      
REMARK 465     THR A   243                                                      
REMARK 465     GLU A   355                                                      
REMARK 465     ASP A   356                                                      
REMARK 465     LYS A   357                                                      
REMARK 465     ILE A   358                                                      
REMARK 465     ASN A   359                                                      
REMARK 465     VAL A   360                                                      
REMARK 465     GLY A   361                                                      
REMARK 465     GLY A   362                                                      
REMARK 465     GLY A   363                                                      
REMARK 465     LEU A   364                                                      
REMARK 465     SER A   365                                                      
REMARK 465     GLY A   366                                                      
REMARK 465     ASP A   367                                                      
REMARK 465     SER A   398                                                      
REMARK 465     GLY A   399                                                      
REMARK 465     TRP A   400                                                      
REMARK 465     SER A   401                                                      
REMARK 465     GLY A   402                                                      
REMARK 465     GLY A   403                                                      
REMARK 465     LEU A   404                                                      
REMARK 465     ALA A   405                                                      
REMARK 465     GLN A   406                                                      
REMARK 465     ASN A   407                                                      
REMARK 465     GLN A   500                                                      
REMARK 465     THR A   501                                                      
REMARK 465     GLN A   502                                                      
REMARK 465     THR A   503                                                      
REMARK 465     GLU A   504                                                      
REMARK 465     GLY A   505                                                      
REMARK 465     ASP A   533                                                      
REMARK 465     ASN A   534                                                      
REMARK 465     PRO A   535                                                      
REMARK 465     ALA A   536                                                      
REMARK 465     PRO A   537                                                      
REMARK 465     GLN A   538                                                      
REMARK 465     ASN A   539                                                      
REMARK 465     GLY A   540                                                      
REMARK 465     GLY A   541                                                      
REMARK 465     ALA A   542                                                      
REMARK 465     ALA A   553                                                      
REMARK 465     CYS A   554                                                      
REMARK 465     SER B     1                                                      
REMARK 465     VAL B     2                                                      
REMARK 465     ASP B     3                                                      
REMARK 465     VAL B     4                                                      
REMARK 465     THR B     5                                                      
REMARK 465     LEU B     6                                                      
REMARK 465     LYS B   193                                                      
REMARK 465     MET B   194                                                      
REMARK 465     ALA B   195                                                      
REMARK 465     SER B   196                                                      
REMARK 465     LYS B   197                                                      
REMARK 465     PHE B   329                                                      
REMARK 465     LYS B   330                                                      
REMARK 465     ILE B   331                                                      
REMARK 465     GLY B   332                                                      
REMARK 465     GLY B   333                                                      
REMARK 465     ALA B   334                                                      
REMARK 465     ILE B   335                                                      
REMARK 465     GLU B   336                                                      
REMARK 465     GLU B   337                                                      
REMARK 465     VAL B   338                                                      
REMARK 465     TYR B   339                                                      
REMARK 465     VAL B   340                                                      
REMARK 465     SER B   341                                                      
REMARK 465     LEU B   342                                                      
REMARK 465     GLY B   343                                                      
REMARK 465     VAL B   344                                                      
REMARK 465     GLY B   522                                                      
REMARK 465     GLY B   523                                                      
REMARK 465     SER B   524                                                      
REMARK 465     PRO B   525                                                      
REMARK 465     CYS B   526                                                      
REMARK 465     SER B   537                                                      
REMARK 465     GLN C     1                                                      
REMARK 465     LYS C     2                                                      
REMARK 465     PRO C     3                                                      
REMARK 465     GLN C     4                                                      
REMARK 465     ARG C     5                                                      
REMARK 465     PRO C     6                                                      
REMARK 465     ARG C     7                                                      
REMARK 465     ARG C     8                                                      
REMARK 465     PRO C     9                                                      
REMARK 465     ALA C    10                                                      
REMARK 465     SER C    11                                                      
REMARK 465     PRO C    12                                                      
REMARK 465     ALA C    96                                                      
REMARK 465     ARG C    97                                                      
REMARK 465     ASP C    98                                                      
REMARK 465     ARG C   181                                                      
REMARK 465     ARG C   182                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    GLY B    93     CD2  TYR B   261              2.04            
REMARK 500   NH1  ARG B   266     OD2  ASP B   285              2.09            
REMARK 500   O    ILE B   214     OG   SER B   218              2.13            
REMARK 500   O    CYS B   349     N    GLY B   351              2.13            
REMARK 500   OH   TYR A   321     O    ILE A   411              2.16            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   NE2  GLN A    10     O    GLN B   520     2545     2.07            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    TRP A  14   CG    TRP A  14   CD1     0.127                       
REMARK 500    TRP A 512   CG    TRP A 512   CD1     0.130                       
REMARK 500    TRP A 515   CG    TRP A 515   CD1     0.136                       
REMARK 500    TRP A 518   CG    TRP A 518   CD1     0.134                       
REMARK 500    TRP B  16   CG    TRP B  16   CD1     0.137                       
REMARK 500    TRP B  19   CG    TRP B  19   CD1     0.127                       
REMARK 500    CYS B 467   CB    CYS B 467   SG     -0.129                       
REMARK 500    TRP B 497   CG    TRP B 497   CD1     0.129                       
REMARK 500    TRP B 500   CG    TRP B 500   CD1     0.109                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    CYS B 480   CA  -  CB  -  SG  ANGL. DEV. = -11.7 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    GLN A  24       -2.70   -177.13                                   
REMARK 500    SER A  55       41.42   -153.26                                   
REMARK 500    ALA A  64      105.73    -34.52                                   
REMARK 500    LYS A  73      -82.79    -48.16                                   
REMARK 500    CYS A  85       72.36     55.13                                   
REMARK 500    ASP A  99       -7.99     82.80                                   
REMARK 500    GLU A 101      -85.82    -82.01                                   
REMARK 500    GLU A 108        4.94     57.78                                   
REMARK 500    ASP A 109       72.41     45.23                                   
REMARK 500    CYS A 110      -48.03   -162.17                                   
REMARK 500    ALA A 134     -159.98    -93.60                                   
REMARK 500    TRP A 155       -6.35    -42.96                                   
REMARK 500    GLU A 157      124.60    -21.10                                   
REMARK 500    ASP A 161       81.10   -153.53                                   
REMARK 500    ASP A 171       -8.76    -47.05                                   
REMARK 500    TYR A 180      -37.42    -35.11                                   
REMARK 500    ASP A 192       77.81    -61.36                                   
REMARK 500    VAL A 210      -79.23    -64.15                                   
REMARK 500    GLU A 248       27.71    -68.45                                   
REMARK 500    LEU A 249      -28.35   -145.75                                   
REMARK 500    ASN A 250       26.91    -68.25                                   
REMARK 500    TYR A 252       15.39   -142.17                                   
REMARK 500    GLU A 254      115.15    -36.78                                   
REMARK 500    LYS A 255        8.73    -63.27                                   
REMARK 500    GLU A 290       29.03    -72.46                                   
REMARK 500    SER A 314      170.81    169.29                                   
REMARK 500    CYS A 369       10.99    173.78                                   
REMARK 500    LYS A 371      -19.41   -168.08                                   
REMARK 500    ALA A 383      -57.46    -23.77                                   
REMARK 500    SER A 409     -121.52   -147.62                                   
REMARK 500    LEU A 443       -6.05    -59.05                                   
REMARK 500    LEU A 446       41.18   -167.63                                   
REMARK 500    ARG A 468        1.09    -67.91                                   
REMARK 500    CYS A 469       43.69    -93.26                                   
REMARK 500    ASN A 474       33.65     77.06                                   
REMARK 500    ASN A 475       57.49     36.85                                   
REMARK 500    ARG A 486     -169.42   -123.44                                   
REMARK 500    GLN A 488       46.54   -106.84                                   
REMARK 500    LEU A 491      101.21    -55.12                                   
REMARK 500    CYS A 498      110.80     70.66                                   
REMARK 500    ALA A 508     -170.38    -68.49                                   
REMARK 500    ASP A 509      -89.76   -118.77                                   
REMARK 500    SER A 511      132.53    178.97                                   
REMARK 500    ALA A 523       73.30     61.18                                   
REMARK 500    SER B  14      175.17    -55.03                                   
REMARK 500    CYS B  46       78.87   -109.59                                   
REMARK 500    ASN B  47       58.43    -97.39                                   
REMARK 500    CYS B  56     -166.88   -117.00                                   
REMARK 500    VAL B  57      102.43   -169.95                                   
REMARK 500    ASN B  59      -37.25   -131.54                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     123 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 SER B   96     ASP B   97                  136.90                    
REMARK 500 LYS B  107     CYS B  108                 -148.25                    
REMARK 500 THR C  110     ASP C  111                  147.90                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B 538  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU B  98   OE2                                                    
REMARK 620 2 ASP B  97   OD1 114.1                                              
REMARK 620 3 ASN B  87   OD1  86.3 157.5                                        
REMARK 620 4 LEU B  84   O   101.6  97.6  86.7                                  
REMARK 620 5 ASP B  91   OD2 168.6  72.4  86.0  86.3                            
REMARK 620 6 ASP B  89   O    79.7  81.6  93.6 178.6  92.4                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 555  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN A  86   OD1                                                    
REMARK 620 2 ASP A  96   OD1 166.9                                              
REMARK 620 3 GLU A  97   OE2  84.0  82.9                                        
REMARK 620 4 ASP A  88   O    98.8  79.6  83.3                                  
REMARK 620 5 LEU A  83   O    92.2  87.7  88.6 165.6                            
REMARK 620 6 ASP A  90   OD1  96.4  96.6 171.4  88.1 100.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 555                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 538                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA A 556                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA A 557                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA A 558                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA A 559                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA B 539                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA B 540                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA B 541                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA B 542                 
DBREF  3OJY A    1   554  UNP    P07357   CO8A_HUMAN      31    584             
DBREF  3OJY B    1   537  UNP    P07358   CO8B_HUMAN      55    591             
DBREF  3OJY C    1   182  UNP    P07360   CO8G_HUMAN      21    202             
SEQRES   1 A  554  ALA ALA THR PRO ALA ALA VAL THR CYS GLN LEU SER ASN          
SEQRES   2 A  554  TRP SER GLU TRP THR ASP CYS PHE PRO CYS GLN ASP LYS          
SEQRES   3 A  554  LYS TYR ARG HIS ARG SER LEU LEU GLN PRO ASN LYS PHE          
SEQRES   4 A  554  GLY GLY THR ILE CYS SER GLY ASP ILE TRP ASP GLN ALA          
SEQRES   5 A  554  SER CYS SER SER SER THR THR CYS VAL ARG GLN ALA GLN          
SEQRES   6 A  554  CYS GLY GLN ASP PHE GLN CYS LYS GLU THR GLY ARG CYS          
SEQRES   7 A  554  LEU LYS ARG HIS LEU VAL CYS ASN GLY ASP GLN ASP CYS          
SEQRES   8 A  554  LEU ASP GLY SER ASP GLU ASP ASP CYS GLU ASP VAL ARG          
SEQRES   9 A  554  ALA ILE ASP GLU ASP CYS SER GLN TYR GLU PRO ILE PRO          
SEQRES  10 A  554  GLY SER GLN LYS ALA ALA LEU GLY TYR ASN ILE LEU THR          
SEQRES  11 A  554  GLN GLU ASP ALA GLN SER VAL TYR ASP ALA SER TYR TYR          
SEQRES  12 A  554  GLY GLY GLN CYS GLU THR VAL TYR ASN GLY GLU TRP ARG          
SEQRES  13 A  554  GLU LEU ARG TYR ASP SER THR CYS GLU ARG LEU TYR TYR          
SEQRES  14 A  554  GLY ASP ASP GLU LYS TYR PHE ARG LYS PRO TYR ASN PHE          
SEQRES  15 A  554  LEU LYS TYR HIS PHE GLU ALA LEU ALA ASP THR GLY ILE          
SEQRES  16 A  554  SER SER GLU PHE TYR ASP ASN ALA ASN ASP LEU LEU SER          
SEQRES  17 A  554  LYS VAL LYS LYS ASP LYS SER ASP SER PHE GLY VAL THR          
SEQRES  18 A  554  ILE GLY ILE GLY PRO ALA GLY SER PRO LEU LEU VAL GLY          
SEQRES  19 A  554  VAL GLY VAL SER HIS SER GLN ASP THR SER PHE LEU ASN          
SEQRES  20 A  554  GLU LEU ASN LYS TYR ASN GLU LYS LYS PHE ILE PHE THR          
SEQRES  21 A  554  ARG ILE PHE THR LYS VAL GLN THR ALA HIS PHE LYS MET          
SEQRES  22 A  554  ARG LYS ASP ASP ILE MET LEU ASP GLU GLY MET LEU GLN          
SEQRES  23 A  554  SER LEU MET GLU LEU PRO ASP GLN TYR ASN TYR GLY MET          
SEQRES  24 A  554  TYR ALA LYS PHE ILE ASN ASP TYR GLY THR HIS TYR ILE          
SEQRES  25 A  554  THR SER GLY SER MET GLY GLY ILE TYR GLU TYR ILE LEU          
SEQRES  26 A  554  VAL ILE ASP LYS ALA LYS MET GLU SER LEU GLY ILE THR          
SEQRES  27 A  554  SER ARG ASP ILE THR THR CYS PHE GLY GLY SER LEU GLY          
SEQRES  28 A  554  ILE GLN TYR GLU ASP LYS ILE ASN VAL GLY GLY GLY LEU          
SEQRES  29 A  554  SER GLY ASP HIS CYS LYS LYS PHE GLY GLY GLY LYS THR          
SEQRES  30 A  554  GLU ARG ALA ARG LYS ALA MET ALA VAL GLU ASP ILE ILE          
SEQRES  31 A  554  SER ARG VAL ARG GLY GLY SER SER GLY TRP SER GLY GLY          
SEQRES  32 A  554  LEU ALA GLN ASN ARG SER THR ILE THR TYR ARG SER TRP          
SEQRES  33 A  554  GLY ARG SER LEU LYS TYR ASN PRO VAL VAL ILE ASP PHE          
SEQRES  34 A  554  GLU MET GLN PRO ILE HIS GLU VAL LEU ARG HIS THR SER          
SEQRES  35 A  554  LEU GLY PRO LEU GLU ALA LYS ARG GLN ASN LEU ARG ARG          
SEQRES  36 A  554  ALA LEU ASP GLN TYR LEU MET GLU PHE ASN ALA CYS ARG          
SEQRES  37 A  554  CYS GLY PRO CYS PHE ASN ASN GLY VAL PRO ILE LEU GLU          
SEQRES  38 A  554  GLY THR SER CYS ARG CYS GLN CYS ARG LEU GLY SER LEU          
SEQRES  39 A  554  GLY ALA ALA CYS GLU GLN THR GLN THR GLU GLY ALA LYS          
SEQRES  40 A  554  ALA ASP GLY SER TRP SER CYS TRP SER SER TRP SER VAL          
SEQRES  41 A  554  CYS ARG ALA GLY ILE GLN GLU ARG ARG ARG GLU CYS ASP          
SEQRES  42 A  554  ASN PRO ALA PRO GLN ASN GLY GLY ALA SER CYS PRO GLY          
SEQRES  43 A  554  ARG LYS VAL GLN THR GLN ALA CYS                              
SEQRES   1 B  537  SER VAL ASP VAL THR LEU MET PRO ILE ASP CYS GLU LEU          
SEQRES   2 B  537  SER SER TRP SER SER TRP THR THR CYS ASP PRO CYS GLN          
SEQRES   3 B  537  LYS LYS ARG TYR ARG TYR ALA TYR LEU LEU GLN PRO SER          
SEQRES   4 B  537  GLN PHE HIS GLY GLU PRO CYS ASN PHE SER ASP LYS GLU          
SEQRES   5 B  537  VAL GLU ASP CYS VAL THR ASN ARG PRO CYS ARG SER GLN          
SEQRES   6 B  537  VAL ARG CYS GLU GLY PHE VAL CYS ALA GLN THR GLY ARG          
SEQRES   7 B  537  CYS VAL ASN ARG ARG LEU LEU CYS ASN GLY ASP ASN ASP          
SEQRES   8 B  537  CYS GLY ASP GLN SER ASP GLU ALA ASN CYS ARG ARG ILE          
SEQRES   9 B  537  TYR LYS LYS CYS GLN HIS GLU MET ASP GLN TYR TRP GLY          
SEQRES  10 B  537  ILE GLY SER LEU ALA SER GLY ILE ASN LEU PHE THR ASN          
SEQRES  11 B  537  SER PHE GLU GLY PRO VAL LEU ASP HIS ARG TYR TYR ALA          
SEQRES  12 B  537  GLY GLY CYS SER PRO HIS TYR ILE LEU ASN THR ARG PHE          
SEQRES  13 B  537  ARG LYS PRO TYR ASN VAL GLU SER TYR THR PRO GLN THR          
SEQRES  14 B  537  GLN GLY LYS TYR GLU PHE ILE LEU LYS GLU TYR GLU SER          
SEQRES  15 B  537  TYR SER ASP PHE GLU ARG ASN VAL THR GLU LYS MET ALA          
SEQRES  16 B  537  SER LYS SER GLY PHE SER PHE GLY PHE LYS ILE PRO GLY          
SEQRES  17 B  537  ILE PHE GLU LEU GLY ILE SER SER GLN SER ASP ARG GLY          
SEQRES  18 B  537  LYS HIS TYR ILE ARG ARG THR LYS ARG PHE SER HIS THR          
SEQRES  19 B  537  LYS SER VAL PHE LEU HIS ALA ARG SER ASP LEU GLU VAL          
SEQRES  20 B  537  ALA HIS TYR LYS LEU LYS PRO ARG SER LEU MET LEU HIS          
SEQRES  21 B  537  TYR GLU PHE LEU GLN ARG VAL LYS ARG LEU PRO LEU GLU          
SEQRES  22 B  537  TYR SER TYR GLY GLU TYR ARG ASP LEU PHE ARG ASP PHE          
SEQRES  23 B  537  GLY THR HIS TYR ILE THR GLU ALA VAL LEU GLY GLY ILE          
SEQRES  24 B  537  TYR GLU TYR THR LEU VAL MET ASN LYS GLU ALA MET GLU          
SEQRES  25 B  537  ARG GLY ASP TYR THR LEU ASN ASN VAL HIS ALA CYS ALA          
SEQRES  26 B  537  LYS ASN ASP PHE LYS ILE GLY GLY ALA ILE GLU GLU VAL          
SEQRES  27 B  537  TYR VAL SER LEU GLY VAL SER VAL GLY LYS CYS ARG GLY          
SEQRES  28 B  537  ILE LEU ASN GLU ILE LYS ASP ARG ASN LYS ARG ASP TPO          
SEQRES  29 B  537  MET VAL GLU ASP LEU VAL VAL LEU VAL ARG GLY GLY ALA          
SEQRES  30 B  537  SER GLU HIS ILE THR THR LEU ALA TYR GLN GLU LEU PRO          
SEQRES  31 B  537  THR ALA ASP LEU MET GLN GLU TRP GLY ASP ALA VAL GLN          
SEQRES  32 B  537  TYR ASN PRO ALA ILE ILE LYS VAL LYS VAL GLU PRO LEU          
SEQRES  33 B  537  TYR GLU LEU VAL THR ALA THR ASP PHE ALA TYR SER SER          
SEQRES  34 B  537  THR VAL ARG GLN ASN MET LYS GLN ALA LEU GLU GLU PHE          
SEQRES  35 B  537  GLN LYS GLU VAL SER SER CYS HIS CYS ALA PRO CYS GLN          
SEQRES  36 B  537  GLY ASN GLY VAL PRO VAL LEU LYS GLY SER ARG CYS ASP          
SEQRES  37 B  537  CYS ILE CYS PRO VAL GLY SER GLN GLY LEU ALA CYS GLU          
SEQRES  38 B  537  VAL SER TYR ARG LYS ASN THR PRO ILE ASP GLY LYS TRP          
SEQRES  39 B  537  ASN CYS TRP SER ASN TRP SER SER CYS SER GLY ARG ARG          
SEQRES  40 B  537  LYS THR ARG GLN ARG GLN CYS ASN ASN PRO PRO PRO GLN          
SEQRES  41 B  537  ASN GLY GLY SER PRO CYS SER GLY PRO ALA SER GLU THR          
SEQRES  42 B  537  LEU ASP CYS SER                                              
SEQRES   1 C  182  GLN LYS PRO GLN ARG PRO ARG ARG PRO ALA SER PRO ILE          
SEQRES   2 C  182  SER THR ILE GLN PRO LYS ALA ASN PHE ASP ALA GLN GLN          
SEQRES   3 C  182  PHE ALA GLY THR TRP LEU LEU VAL ALA VAL GLY SER ALA          
SEQRES   4 C  182  CYS ARG PHE LEU GLN GLU GLN GLY HIS ARG ALA GLU ALA          
SEQRES   5 C  182  THR THR LEU HIS VAL ALA PRO GLN GLY THR ALA MET ALA          
SEQRES   6 C  182  VAL SER THR PHE ARG LYS LEU ASP GLY ILE CYS TRP GLN          
SEQRES   7 C  182  VAL ARG GLN LEU TYR GLY ASP THR GLY VAL LEU GLY ARG          
SEQRES   8 C  182  PHE LEU LEU GLN ALA ARG ASP ALA ARG GLY ALA VAL HIS          
SEQRES   9 C  182  VAL VAL VAL ALA GLU THR ASP TYR GLN SER PHE ALA VAL          
SEQRES  10 C  182  LEU TYR LEU GLU ARG ALA GLY GLN LEU SER VAL LYS LEU          
SEQRES  11 C  182  TYR ALA ARG SER LEU PRO VAL SER ASP SER VAL LEU SER          
SEQRES  12 C  182  GLY PHE GLU GLN ARG VAL GLN GLU ALA HIS LEU THR GLU          
SEQRES  13 C  182  ASP GLN ILE PHE TYR PHE PRO LYS TYR GLY PHE CYS GLU          
SEQRES  14 C  182  ALA ALA ASP GLN PHE HIS VAL LEU ASP GLU VAL ARG ARG          
MODRES 3OJY TPO B  364  THR  PHOSPHOTHREONINE                                   
HET    TPO  B 364      11                                                       
HET     CA  A 555       1                                                       
HET    BMA  A 556      11                                                       
HET    BMA  A 557      11                                                       
HET    BMA  A 558      11                                                       
HET    BMA  A 559      11                                                       
HET     CA  B 538       1                                                       
HET    BMA  B 539      11                                                       
HET    BMA  B 540      11                                                       
HET    BMA  B 541      11                                                       
HET    BMA  B 542      11                                                       
HETNAM     TPO PHOSPHOTHREONINE                                                 
HETNAM      CA CALCIUM ION                                                      
HETNAM     BMA BETA-D-MANNOSE                                                   
HETSYN     TPO PHOSPHONOTHREONINE                                               
FORMUL   2  TPO    C4 H10 N O6 P                                                
FORMUL   4   CA    2(CA 2+)                                                     
FORMUL   5  BMA    8(C6 H12 O6)                                                 
HELIX    1   1 LYS A   80  VAL A   84  5                                   5    
HELIX    2   2 GLY A  118  ALA A  123  1                                   6    
HELIX    3   3 SER A  162  GLU A  165  5                                   4    
HELIX    4   4 GLY A  170  GLU A  173  5                                   4    
HELIX    5   5 ASN A  202  LYS A  211  1                                  10    
HELIX    6   6 LEU A  246  ASN A  250  5                                   5    
HELIX    7   7 ASP A  281  GLU A  290  1                                  10    
HELIX    8   8 ASN A  296  GLY A  308  1                                  13    
HELIX    9   9 LYS A  329  LEU A  335  1                                   7    
HELIX   10  10 THR A  338  SER A  349  1                                  12    
HELIX   11  11 THR A  377  MET A  384  1                                   8    
HELIX   12  12 THR A  412  LEU A  420  1                                   9    
HELIX   13  13 LYS A  421  ASN A  423  5                                   3    
HELIX   14  14 HIS A  435  THR A  441  5                                   7    
HELIX   15  15 LEU A  446  PHE A  464  1                                  19    
HELIX   16  16 ASN A  465  CYS A  469  5                                   5    
HELIX   17  17 ASN B   81  LEU B   85  5                                   5    
HELIX   18  18 GLY B  117  LEU B  121  5                                   5    
HELIX   19  19 SER B  182  GLU B  187  1                                   6    
HELIX   20  20 GLY B  221  ARG B  230  1                                  10    
HELIX   21  21 HIS B  260  LYS B  268  1                                   9    
HELIX   22  22 SER B  275  GLY B  287  1                                  13    
HELIX   23  23 LYS B  308  GLU B  312  1                                   5    
HELIX   24  24 THR B  317  ALA B  325  1                                   9    
HELIX   25  25 ASN B  354  ARG B  359  1                                   6    
HELIX   26  26 LEU B  394  TYR B  404  1                                  11    
HELIX   27  27 TYR B  417  VAL B  420  5                                   4    
HELIX   28  28 TYR B  427  VAL B  446  1                                  20    
HELIX   29  29 SER B  447  CYS B  451  5                                   5    
HELIX   30  30 GLY B  477  GLU B  481  5                                   5    
HELIX   31  31 CYS C   40  GLU C   45  1                                   6    
HELIX   32  32 GLN C   46  ALA C   50  5                                   5    
HELIX   33  33 SER C  138  GLN C  150  1                                  13    
HELIX   34  34 THR C  155  ASP C  157  5                                   3    
SHEET    1   A 2 GLN A  10  LEU A  11  0                                        
SHEET    2   A 2 LEU A  33  GLN A  35 -1  O  GLN A  35   N  GLN A  10           
SHEET    1   B 2 LYS A  26  HIS A  30  0                                        
SHEET    2   B 2 TRP A  49  SER A  53 -1  O  ALA A  52   N  LYS A  27           
SHEET    1   C 2 PHE A  70  GLN A  71  0                                        
SHEET    2   C 2 CYS A  78  LEU A  79 -1  O  LEU A  79   N  PHE A  70           
SHEET    1   D 2 LEU A 124  ASN A 127  0                                        
SHEET    2   D 2 GLU A 132  SER A 136 -1  O  ALA A 134   N  GLY A 125           
SHEET    1   E 2 GLU A 148  TYR A 151  0                                        
SHEET    2   E 2 TYR A 175  LYS A 178 -1  O  PHE A 176   N  VAL A 150           
SHEET    1   F 2 ARG A 159  ASP A 161  0                                        
SHEET    2   F 2 ARG A 166  TYR A 168 -1  O  TYR A 168   N  ARG A 159           
SHEET    1   G 4 PHE A 182  PHE A 187  0                                        
SHEET    2   G 4 PHE A 257  MET A 273 -1  O  HIS A 270   N  HIS A 186           
SHEET    3   G 4 HIS A 310  ASP A 328 -1  O  TYR A 323   N  ILE A 262           
SHEET    4   G 4 VAL A 386  SER A 391 -1  O  ASP A 388   N  VAL A 326           
SHEET    1   H 4 SER A 196  TYR A 200  0                                        
SHEET    2   H 4 PHE A 257  MET A 273 -1  O  PHE A 259   N  TYR A 200           
SHEET    3   H 4 HIS A 310  ASP A 328 -1  O  TYR A 323   N  ILE A 262           
SHEET    4   H 4 VAL A 425  PRO A 433 -1  O  VAL A 425   N  GLY A 318           
SHEET    1   I 2 PRO A 478  GLU A 481  0                                        
SHEET    2   I 2 SER A 484  CYS A 487 -1  O  ARG A 486   N  ILE A 479           
SHEET    1   J 2 GLN A 526  ARG A 529  0                                        
SHEET    2   J 2 VAL A 549  GLN A 552 -1  O  GLN A 550   N  ARG A 528           
SHEET    1   K 2 GLU B  12  LEU B  13  0                                        
SHEET    2   K 2 LEU B  35  GLN B  37 -1  O  GLN B  37   N  GLU B  12           
SHEET    1   L 2 LYS B  28  TYR B  32  0                                        
SHEET    2   L 2 LYS B  51  ASP B  55 -1  O  GLU B  54   N  ARG B  29           
SHEET    1   M 3 SER B  39  GLN B  40  0                                        
SHEET    2   M 3 ARG B 466  ILE B 470  1  O  CYS B 467   N  SER B  39           
SHEET    3   M 3 VAL B 459  LYS B 463 -1  N  VAL B 459   O  ILE B 470           
SHEET    1   N 2 PHE B  71  VAL B  72  0                                        
SHEET    2   N 2 CYS B  79  VAL B  80 -1  O  VAL B  80   N  PHE B  71           
SHEET    1   O 2 SER B 123  ILE B 125  0                                        
SHEET    2   O 2 PHE B 132  PRO B 135 -1  O  GLU B 133   N  GLY B 124           
SHEET    1   P 2 SER B 147  ILE B 151  0                                        
SHEET    2   P 2 THR B 154  LYS B 158 -1  O  PHE B 156   N  HIS B 149           
SHEET    1   Q 5 VAL B 162  PRO B 167  0                                        
SHEET    2   Q 5 LEU B 245  LEU B 252 -1  O  LYS B 251   N  GLU B 163           
SHEET    3   Q 5 HIS B 289  GLY B 298 -1  O  THR B 292   N  LEU B 252           
SHEET    4   Q 5 ALA B 407  PRO B 415 -1  O  LYS B 412   N  GLU B 293           
SHEET    5   Q 5 PHE B 210  GLU B 211 -1  N  PHE B 210   O  VAL B 411           
SHEET    1   R 4 PHE B 175  TYR B 180  0                                        
SHEET    2   R 4 SER B 236  SER B 243 -1  O  ARG B 242   N  ILE B 176           
SHEET    3   R 4 GLU B 301  ASN B 307 -1  O  TYR B 302   N  ALA B 241           
SHEET    4   R 4 VAL B 366  LEU B 372 -1  O  LEU B 372   N  GLU B 301           
SHEET    1   S 2 SER B 475  GLN B 476  0                                        
SHEET    2   S 2 VAL B 482  SER B 483 -1  O  VAL B 482   N  GLN B 476           
SHEET    1   T 2 ARG B 506  THR B 509  0                                        
SHEET    2   T 2 SER B 531  LEU B 534 -1  O  GLU B 532   N  LYS B 508           
SHEET    1   U 6 ILE C 159  TYR C 161  0                                        
SHEET    2   U 6 GLY C  29  GLY C  37 -1  N  VAL C  36   O  PHE C 160           
SHEET    3   U 6 THR C  54  GLN C  60 -1  O  LEU C  55   N  TRP C  31           
SHEET    4   U 6 ALA C  63  LEU C  72 -1  O  SER C  67   N  HIS C  56           
SHEET    5   U 6 ILE C  75  ASP C  85 -1  O  VAL C  79   N  THR C  68           
SHEET    6   U 6 VAL C 176  LEU C 177  1  O  LEU C 177   N  ARG C  80           
SHEET    1   V 8 ILE C 159  TYR C 161  0                                        
SHEET    2   V 8 GLY C  29  GLY C  37 -1  N  VAL C  36   O  PHE C 160           
SHEET    3   V 8 GLN C 125  ALA C 132 -1  O  ALA C 132   N  LEU C  32           
SHEET    4   V 8 PHE C 115  ARG C 122 -1  N  ARG C 122   O  GLN C 125           
SHEET    5   V 8 VAL C 103  THR C 110 -1  N  GLU C 109   O  VAL C 117           
SHEET    6   V 8 ARG C  91  LEU C  94 -1  N  LEU C  94   O  VAL C 103           
SHEET    7   V 8 ILE C  75  ASP C  85 -1  N  GLY C  84   O  LEU C  93           
SHEET    8   V 8 VAL C 176  LEU C 177  1  O  LEU C 177   N  ARG C  80           
SSBOND   1 CYS A    9    CYS A   44                          1555   1555  2.07  
SSBOND   2 CYS A   20    CYS A   54                          1555   1555  2.06  
SSBOND   3 CYS A   23    CYS A   60                          1555   1555  2.07  
SSBOND   4 CYS A   66    CYS A   78                          1555   1555  2.03  
SSBOND   5 CYS A   72    CYS A   91                          1555   1555  2.06  
SSBOND   6 CYS A   85    CYS A  100                          1555   1555  2.03  
SSBOND   7 CYS A  110    CYS A  147                          1555   1555  2.03  
SSBOND   8 CYS A  164    CYS C   40                          1555   1555  2.07  
SSBOND   9 CYS A  467    CYS A  514                          1555   1555  2.08  
SSBOND  10 CYS A  469    CYS A  485                          1555   1555  2.02  
SSBOND  11 CYS A  472    CYS A  487                          1555   1555  1.99  
SSBOND  12 CYS A  489    CYS A  498                          1555   1555  2.04  
SSBOND  13 CYS A  532    CYS A  544                          1555   1555  2.07  
SSBOND  14 CYS B   11    CYS B   46                          1555   1555  2.05  
SSBOND  15 CYS B   22    CYS B   56                          1555   1555  2.05  
SSBOND  16 CYS B   25    CYS B   62                          1555   1555  2.07  
SSBOND  17 CYS B   68    CYS B   79                          1555   1555  2.05  
SSBOND  18 CYS B   73    CYS B   92                          1555   1555  2.06  
SSBOND  19 CYS B   86    CYS B  101                          1555   1555  2.05  
SSBOND  20 CYS B  324    CYS B  349                          1555   1555  2.07  
SSBOND  21 CYS B  449    CYS B  496                          1555   1555  2.05  
SSBOND  22 CYS B  451    CYS B  467                          1555   1555  2.05  
SSBOND  23 CYS B  454    CYS B  469                          1555   1555  2.06  
SSBOND  24 CYS B  471    CYS B  480                          1555   1555  1.99  
SSBOND  25 CYS B  503    CYS B  536                          1555   1555  2.05  
SSBOND  26 CYS C   76    CYS C  168                          1555   1555  2.06  
LINK         C   ASP B 363                 N   TPO B 364     1555   1555  1.35  
LINK         C   TPO B 364                 N   MET B 365     1555   1555  1.35  
LINK         OE2 GLU B  98                CA    CA B 538     1555   1555  1.94  
LINK         OD1 ASP B  97                CA    CA B 538     1555   1555  2.07  
LINK         OD1 ASN B  87                CA    CA B 538     1555   1555  2.11  
LINK         OD1 ASN A  86                CA    CA A 555     1555   1555  2.13  
LINK         OD1 ASP A  96                CA    CA A 555     1555   1555  2.20  
LINK         O   LEU B  84                CA    CA B 538     1555   1555  2.32  
LINK         OD2 ASP B  91                CA    CA B 538     1555   1555  2.34  
LINK         OE2 GLU A  97                CA    CA A 555     1555   1555  2.35  
LINK         O   ASP A  88                CA    CA A 555     1555   1555  2.36  
LINK         O   LEU A  83                CA    CA A 555     1555   1555  2.37  
LINK         OD1 ASP A  90                CA    CA A 555     1555   1555  2.39  
LINK         O   ASP B  89                CA    CA B 538     1555   1555  2.60  
LINK         CD1 TRP A  14                 C1  BMA A 556     1555   1555  1.48  
LINK         CD1 TRP A 512                 C1  BMA A 557     1555   1555  1.47  
LINK         CD1 TRP A 515                 C1  BMA A 558     1555   1555  1.49  
LINK         CD1 TRP A 518                 C1  BMA A 559     1555   1555  1.50  
LINK         CD1 TRP B  16                 C1  BMA B 539     1555   1555  1.49  
LINK         CD1 TRP B  19                 C1  BMA B 540     1555   1555  1.47  
LINK         CD1 TRP B 497                 C1  BMA B 541     1555   1555  1.50  
LINK         CD1 TRP B 500                 C1  BMA B 542     1555   1555  1.48  
CISPEP   1 GLY B   93    ASP B   94          0        -3.51                     
CISPEP   2 LEU C  135    PRO C  136          0        -1.88                     
SITE     1 AC1  6 LEU A  83  ASN A  86  ASP A  88  ASP A  90                    
SITE     2 AC1  6 ASP A  96  GLU A  97                                          
SITE     1 AC2  6 LEU B  84  ASN B  87  ASP B  89  ASP B  91                    
SITE     2 AC2  6 ASP B  97  GLU B  98                                          
SITE     1 AC3  4 ASN A  13  TRP A  14  ARG A  29  GLU C 169                    
SITE     1 AC4  3 SER A 511  TRP A 512  ARG A 530                               
SITE     1 AC5  3 LEU A 461  TRP A 515  ARG A 528                               
SITE     1 AC6  2 TRP A 518  GLN B 511                                          
SITE     1 AC7  3 SER B  15  TRP B  16  ARG B  31                               
SITE     1 AC8  2 TRP B  19  ARG B  29                                          
SITE     1 AC9  6 GLN B 443  LYS B 444  SER B 447  CYS B 496                    
SITE     2 AC9  6 TRP B 497  LYS B 508                                          
SITE     1 BC1  3 LYS B 444  TRP B 500  ARG B 506                               
CRYST1  139.575  139.575  127.160  90.00  90.00 120.00 P 63          6          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.007165  0.004136  0.000000        0.00000                         
SCALE2      0.000000  0.008273  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007864        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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