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Database: PDB
Entry: 2XRC
LinkDB: 2XRC
Original site: 2XRC 
HEADER    IMMUNE SYSTEM                           13-SEP-10   2XRC              
TITLE     HUMAN COMPLEMENT FACTOR I                                             
CAVEAT     2XRC    NAG A 646 HAS WRONG CHIRALITY AT ATOM C1 NAG A 659 HAS WRONG 
CAVEAT   2 2XRC    CHIRALITY AT ATOM C1 NAG A 676 HAS WRONG CHIRALITY AT ATOM   
CAVEAT   3 2XRC    C1 NAG B 646 HAS WRONG CHIRALITY AT ATOM C1 NAG D 646 HAS    
CAVEAT   4 2XRC    WRONG CHIRALITY AT ATOM C1                                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HUMAN COMPLEMENT FACTOR I;                                 
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 SYNONYM: C3B/C4B INACTIVATOR, COMPLEMENT FACTOR I HEAVY CHAIN,       
COMPND   5 COMPLEMENT FACTOR I LIGHT CHAIN, KAF;                                
COMPND   6 EC: 3.4.21.45                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 TISSUE: SERUM                                                        
KEYWDS    IMMUNE SYSTEM, HYDROLASE, CONGLUTINOGEN ACTIVATING FACTOR, SERINE     
KEYWDS   2 PROTEASE, COMPLEMENT SYSTEM                                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    P.ROVERSI,S.JOHNSON,S.M.LEA                                           
REVDAT   3   29-JUL-20 2XRC    1       CAVEAT COMPND REMARK HETNAM              
REVDAT   3 2                   1       LINK   SITE                              
REVDAT   2   17-AUG-11 2XRC    1       JRNL                                     
REVDAT   1   13-JUL-11 2XRC    0                                                
JRNL        AUTH   P.ROVERSI,S.JOHNSON,J.J.CAESAR,F.MCLEAN,K.J.LEATH,           
JRNL        AUTH 2 S.A.TSIFTSOGLOU,B.P.MORGAN,C.L.HARRIS,R.B.SIM,S.M.LEA        
JRNL        TITL   STRUCTURAL BASIS FOR COMPLEMENT FACTOR I CONTROL AND ITS     
JRNL        TITL 2 DISEASE-ASSOCIATED SEQUENCE POLYMORPHISMS.                   
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 108 12839 2011              
JRNL        REFN                   ISSN 0027-8424                               
JRNL        PMID   21768352                                                     
JRNL        DOI    10.1073/PNAS.1102167108                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.69 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.6.0079                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.69                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 79.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 90.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 61930                          
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) : 0.202                           
REMARK   3   R VALUE            (WORKING SET) : 0.200                           
REMARK   3   FREE R VALUE                     : 0.238                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3252                            
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) : 2.69                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.76                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3877                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 78.18                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2320                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 236                          
REMARK   3   BIN FREE R VALUE                    : 0.3010                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 14581                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 316                                     
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 53.40                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 43.17                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 40.54000                                             
REMARK   3    B22 (A**2) : -24.97000                                            
REMARK   3    B33 (A**2) : -15.57000                                            
REMARK   3    B12 (A**2) : -11.14000                                            
REMARK   3    B13 (A**2) : 5.73000                                              
REMARK   3    B23 (A**2) : -8.07000                                             
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.302         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.070         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.318         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 16.144        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.911                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.876                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 15290 ; 0.006 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A): 10328 ; 0.006 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 20687 ; 0.900 ; 1.961       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 25170 ; 0.765 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1827 ; 5.518 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   675 ;33.756 ;24.474       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  2552 ;14.637 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    70 ; 9.848 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  2248 ; 0.054 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 16707 ; 0.003 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  3039 ; 0.001 ; 0.020       
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):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
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  TWIN DETAILS                                                        
REMARK   3   NUMBER OF TWIN DOMAINS  : 4                                        
REMARK   3      TWIN DOMAIN   : 1                                               
REMARK   3      TWIN OPERATOR : H, K, L                                         
REMARK   3      TWIN FRACTION : 0.334                                           
REMARK   3      TWIN DOMAIN   : 2                                               
REMARK   3      TWIN OPERATOR : -H, K, -L                                       
REMARK   3      TWIN FRACTION : 0.359                                           
REMARK   3      TWIN DOMAIN   : 3                                               
REMARK   3      TWIN OPERATOR : -H,-K,L                                         
REMARK   3      TWIN FRACTION : 0.187                                           
REMARK   3      TWIN DOMAIN   : 4                                               
REMARK   3      TWIN OPERATOR : H,-K,-L                                         
REMARK   3      TWIN FRACTION : 0.119                                           
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. HYDROGENS HAVE BEEN USED BUT NOT DEPOSITED.              
REMARK   3  TETARTOHEDRAL TWINNING                                              
REMARK   4                                                                      
REMARK   4 2XRC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 13-SEP-10.                  
REMARK 100 THE DEPOSITION ID IS D_1290045377.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 30-NOV-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 120                                
REMARK 200  PH                             : 4.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I02                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97950                            
REMARK 200  MONOCHROMATOR                  : CRYSTAL                            
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC CCD                           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 68978                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.650                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 79.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 90.8                               
REMARK 200  DATA REDUNDANCY                : 2.900                              
REMARK 200  R MERGE                    (I) : 0.11000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.65                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.79                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 90.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.41000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRIES 1EKB, 1BY2, 1J8E AND 3B4V                
REMARK 200                                                                      
REMARK 200 REMARK: THE CRYSTAL AND DATA WERE TETARTOHEDRALLY TWINNED.           
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 54.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.65                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20.0-23.5% PEG 1500, 0.1M SODIUM         
REMARK 280  SUCCINATE PH 4.0, 1MM CACL2                                         
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4                                              
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
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 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     LYS A     1                                                      
REMARK 465     VAL A     2                                                      
REMARK 465     THR A     3                                                      
REMARK 465     TYR A     4                                                      
REMARK 465     THR A     5                                                      
REMARK 465     SER A     6                                                      
REMARK 465     GLN A     7                                                      
REMARK 465     LYS A   200                                                      
REMARK 465     ALA A   201                                                      
REMARK 465     ASP A   202                                                      
REMARK 465     SER A   203                                                      
REMARK 465     PRO A   204                                                      
REMARK 465     MET A   205                                                      
REMARK 465     ASP A   206                                                      
REMARK 465     ASP A   207                                                      
REMARK 465     PHE A   208                                                      
REMARK 465     GLY A   277                                                      
REMARK 465     PHE A   278                                                      
REMARK 465     ALA A   279                                                      
REMARK 465     SER A   280                                                      
REMARK 465     VAL A   281                                                      
REMARK 465     ALA A   282                                                      
REMARK 465     GLN A   283                                                      
REMARK 465     GLU A   284                                                      
REMARK 465     GLU A   285                                                      
REMARK 465     THR A   286                                                      
REMARK 465     GLU A   287                                                      
REMARK 465     ILE A   288                                                      
REMARK 465     LEU A   289                                                      
REMARK 465     THR A   290                                                      
REMARK 465     ALA A   291                                                      
REMARK 465     ASP A   292                                                      
REMARK 465     LYS A   312                                                      
REMARK 465     ASN A   313                                                      
REMARK 465     ARG A   314                                                      
REMARK 465     MET A   315                                                      
REMARK 465     HIS A   316                                                      
REMARK 465     ILE A   317                                                      
REMARK 465     ARG A   318                                                      
REMARK 465     ARG A   319                                                      
REMARK 465     LYS A   320                                                      
REMARK 465     ARG A   321                                                      
REMARK 465     ILE A   322                                                      
REMARK 465     VAL A   323                                                      
REMARK 465     GLY A   324                                                      
REMARK 465     GLY A   325                                                      
REMARK 465     LYS A   326                                                      
REMARK 465     ARG A   327                                                      
REMARK 465     ALA A   328                                                      
REMARK 465     GLN A   329                                                      
REMARK 465     LEU A   330                                                      
REMARK 465     GLY A   331                                                      
REMARK 465     THR A   377                                                      
REMARK 465     VAL A   378                                                      
REMARK 465     VAL A   379                                                      
REMARK 465     ASP A   380                                                      
REMARK 465     TRP A   381                                                      
REMARK 465     ILE A   382                                                      
REMARK 465     HIS A   383                                                      
REMARK 465     PRO A   384                                                      
REMARK 465     ASP A   385                                                      
REMARK 465     LEU A   386                                                      
REMARK 465     LYS A   387                                                      
REMARK 465     ARG A   388                                                      
REMARK 465     ILE A   389                                                      
REMARK 465     TRP A   454                                                      
REMARK 465     GLY A   455                                                      
REMARK 465     ARG A   456                                                      
REMARK 465     GLU A   457                                                      
REMARK 465     LYS A   458                                                      
REMARK 465     ASP A   459                                                      
REMARK 465     ASN A   460                                                      
REMARK 465     GLU A   461                                                      
REMARK 465     ARG A   462                                                      
REMARK 465     VAL A   463                                                      
REMARK 465     PHE A   464                                                      
REMARK 465     SER A   465                                                      
REMARK 465     LEU A   466                                                      
REMARK 465     ASP A   497                                                      
REMARK 465     GLY A   498                                                      
REMARK 465     SER A   499                                                      
REMARK 465     ILE A   500                                                      
REMARK 465     ASP A   501                                                      
REMARK 465     ALA A   502                                                      
REMARK 465     CYS A   503                                                      
REMARK 465     LYS A   504                                                      
REMARK 465     GLY A   505                                                      
REMARK 465     ASP A   506                                                      
REMARK 465     GLY A   529                                                      
REMARK 465     GLU A   530                                                      
REMARK 465     ASN A   531                                                      
REMARK 465     CYS A   532                                                      
REMARK 465     GLY A   533                                                      
REMARK 465     LYS A   534                                                      
REMARK 465     GLY A   556                                                      
REMARK 465     ARG A   557                                                      
REMARK 465     PRO A   558                                                      
REMARK 465     PHE A   559                                                      
REMARK 465     ILE A   560                                                      
REMARK 465     SER A   561                                                      
REMARK 465     GLN A   562                                                      
REMARK 465     TYR A   563                                                      
REMARK 465     ASN A   564                                                      
REMARK 465     VAL A   565                                                      
REMARK 465     LYS B     1                                                      
REMARK 465     VAL B     2                                                      
REMARK 465     THR B     3                                                      
REMARK 465     TYR B     4                                                      
REMARK 465     THR B     5                                                      
REMARK 465     SER B     6                                                      
REMARK 465     GLN B     7                                                      
REMARK 465     GLU B     8                                                      
REMARK 465     GLN B   199                                                      
REMARK 465     LYS B   200                                                      
REMARK 465     ALA B   201                                                      
REMARK 465     ASP B   202                                                      
REMARK 465     SER B   203                                                      
REMARK 465     PRO B   204                                                      
REMARK 465     MET B   205                                                      
REMARK 465     ASP B   206                                                      
REMARK 465     ASP B   207                                                      
REMARK 465     ALA B   276                                                      
REMARK 465     GLY B   277                                                      
REMARK 465     PHE B   278                                                      
REMARK 465     ALA B   279                                                      
REMARK 465     SER B   280                                                      
REMARK 465     VAL B   281                                                      
REMARK 465     ALA B   282                                                      
REMARK 465     GLN B   283                                                      
REMARK 465     GLU B   284                                                      
REMARK 465     GLU B   285                                                      
REMARK 465     THR B   286                                                      
REMARK 465     GLU B   287                                                      
REMARK 465     ILE B   288                                                      
REMARK 465     GLY B   310                                                      
REMARK 465     VAL B   311                                                      
REMARK 465     LYS B   312                                                      
REMARK 465     ASN B   313                                                      
REMARK 465     ARG B   314                                                      
REMARK 465     MET B   315                                                      
REMARK 465     HIS B   316                                                      
REMARK 465     ILE B   317                                                      
REMARK 465     ARG B   318                                                      
REMARK 465     ARG B   319                                                      
REMARK 465     LYS B   320                                                      
REMARK 465     ARG B   321                                                      
REMARK 465     THR B   377                                                      
REMARK 465     VAL B   378                                                      
REMARK 465     VAL B   379                                                      
REMARK 465     ASP B   380                                                      
REMARK 465     TRP B   381                                                      
REMARK 465     ILE B   382                                                      
REMARK 465     HIS B   383                                                      
REMARK 465     PRO B   384                                                      
REMARK 465     ASP B   385                                                      
REMARK 465     LEU B   386                                                      
REMARK 465     LYS B   387                                                      
REMARK 465     LYS B   419                                                      
REMARK 465     ASP B   420                                                      
REMARK 465     GLY B   421                                                      
REMARK 465     ASN B   422                                                      
REMARK 465     LYS B   423                                                      
REMARK 465     LYS B   424                                                      
REMARK 465     ASP B   425                                                      
REMARK 465     GLY B   455                                                      
REMARK 465     ARG B   456                                                      
REMARK 465     GLU B   457                                                      
REMARK 465     LYS B   458                                                      
REMARK 465     ASP B   459                                                      
REMARK 465     ASN B   460                                                      
REMARK 465     GLU B   461                                                      
REMARK 465     ARG B   462                                                      
REMARK 465     VAL B   463                                                      
REMARK 465     PHE B   464                                                      
REMARK 465     SER B   465                                                      
REMARK 465     ASP B   497                                                      
REMARK 465     GLY B   498                                                      
REMARK 465     SER B   499                                                      
REMARK 465     ILE B   500                                                      
REMARK 465     ASP B   501                                                      
REMARK 465     ALA B   502                                                      
REMARK 465     CYS B   503                                                      
REMARK 465     LYS B   504                                                      
REMARK 465     GLY B   505                                                      
REMARK 465     LYS C     1                                                      
REMARK 465     VAL C     2                                                      
REMARK 465     THR C     3                                                      
REMARK 465     TYR C     4                                                      
REMARK 465     THR C     5                                                      
REMARK 465     SER C     6                                                      
REMARK 465     GLN C     7                                                      
REMARK 465     ILE C   158                                                      
REMARK 465     ASN C   159                                                      
REMARK 465     SER C   160                                                      
REMARK 465     THR C   161                                                      
REMARK 465     GLU C   162                                                      
REMARK 465     GLN C   199                                                      
REMARK 465     LYS C   200                                                      
REMARK 465     ALA C   201                                                      
REMARK 465     ASP C   202                                                      
REMARK 465     SER C   203                                                      
REMARK 465     PRO C   204                                                      
REMARK 465     MET C   205                                                      
REMARK 465     ASP C   206                                                      
REMARK 465     PHE C   278                                                      
REMARK 465     ALA C   279                                                      
REMARK 465     SER C   280                                                      
REMARK 465     VAL C   281                                                      
REMARK 465     ALA C   282                                                      
REMARK 465     GLN C   283                                                      
REMARK 465     GLU C   284                                                      
REMARK 465     GLU C   285                                                      
REMARK 465     THR C   286                                                      
REMARK 465     GLU C   287                                                      
REMARK 465     ILE C   288                                                      
REMARK 465     LEU C   289                                                      
REMARK 465     THR C   290                                                      
REMARK 465     ALA C   291                                                      
REMARK 465     ASP C   292                                                      
REMARK 465     LYS C   312                                                      
REMARK 465     ASN C   313                                                      
REMARK 465     ARG C   314                                                      
REMARK 465     MET C   315                                                      
REMARK 465     HIS C   316                                                      
REMARK 465     ILE C   317                                                      
REMARK 465     ARG C   318                                                      
REMARK 465     ARG C   319                                                      
REMARK 465     LYS C   320                                                      
REMARK 465     ARG C   321                                                      
REMARK 465     ILE C   322                                                      
REMARK 465     VAL C   323                                                      
REMARK 465     GLY C   324                                                      
REMARK 465     GLY C   325                                                      
REMARK 465     LYS C   326                                                      
REMARK 465     ARG C   327                                                      
REMARK 465     ALA C   328                                                      
REMARK 465     GLN C   329                                                      
REMARK 465     LEU C   330                                                      
REMARK 465     GLY C   331                                                      
REMARK 465     ASP C   332                                                      
REMARK 465     LEU C   333                                                      
REMARK 465     SER C   343                                                      
REMARK 465     GLY C   344                                                      
REMARK 465     ARG C   365                                                      
REMARK 465     ALA C   366                                                      
REMARK 465     SER C   367                                                      
REMARK 465     LYS C   368                                                      
REMARK 465     VAL C   379                                                      
REMARK 465     ASP C   380                                                      
REMARK 465     TRP C   381                                                      
REMARK 465     ILE C   382                                                      
REMARK 465     HIS C   383                                                      
REMARK 465     PRO C   384                                                      
REMARK 465     ASP C   385                                                      
REMARK 465     LEU C   386                                                      
REMARK 465     LYS C   387                                                      
REMARK 465     GLY C   455                                                      
REMARK 465     ARG C   456                                                      
REMARK 465     GLU C   457                                                      
REMARK 465     LYS C   458                                                      
REMARK 465     ASP C   459                                                      
REMARK 465     ASN C   460                                                      
REMARK 465     GLU C   461                                                      
REMARK 465     ARG C   462                                                      
REMARK 465     VAL C   463                                                      
REMARK 465     PHE C   464                                                      
REMARK 465     SER C   465                                                      
REMARK 465     TYR C   496                                                      
REMARK 465     ASP C   497                                                      
REMARK 465     GLY C   498                                                      
REMARK 465     SER C   499                                                      
REMARK 465     ILE C   500                                                      
REMARK 465     ASP C   501                                                      
REMARK 465     ALA C   502                                                      
REMARK 465     CYS C   503                                                      
REMARK 465     LYS C   504                                                      
REMARK 465     GLY C   505                                                      
REMARK 465     ASP C   506                                                      
REMARK 465     SER C   507                                                      
REMARK 465     GLY C   508                                                      
REMARK 465     GLY C   509                                                      
REMARK 465     CYS C   532                                                      
REMARK 465     GLY C   533                                                      
REMARK 465     LYS C   534                                                      
REMARK 465     PRO C   535                                                      
REMARK 465     GLY C   556                                                      
REMARK 465     ARG C   557                                                      
REMARK 465     PRO C   558                                                      
REMARK 465     PHE C   559                                                      
REMARK 465     ILE C   560                                                      
REMARK 465     SER C   561                                                      
REMARK 465     GLN C   562                                                      
REMARK 465     TYR C   563                                                      
REMARK 465     ASN C   564                                                      
REMARK 465     VAL C   565                                                      
REMARK 465     LYS D     1                                                      
REMARK 465     VAL D     2                                                      
REMARK 465     THR D     3                                                      
REMARK 465     TYR D     4                                                      
REMARK 465     THR D     5                                                      
REMARK 465     SER D     6                                                      
REMARK 465     GLN D     7                                                      
REMARK 465     GLU D     8                                                      
REMARK 465     ASP D     9                                                      
REMARK 465     ASP D   155                                                      
REMARK 465     LEU D   156                                                      
REMARK 465     SER D   157                                                      
REMARK 465     ILE D   158                                                      
REMARK 465     ASN D   159                                                      
REMARK 465     SER D   160                                                      
REMARK 465     THR D   161                                                      
REMARK 465     THR D   185                                                      
REMARK 465     MET D   186                                                      
REMARK 465     GLY D   187                                                      
REMARK 465     TYR D   188                                                      
REMARK 465     GLN D   189                                                      
REMARK 465     ALA D   201                                                      
REMARK 465     ASP D   202                                                      
REMARK 465     SER D   203                                                      
REMARK 465     PRO D   204                                                      
REMARK 465     MET D   205                                                      
REMARK 465     ASP D   206                                                      
REMARK 465     ASP D   207                                                      
REMARK 465     PHE D   278                                                      
REMARK 465     ALA D   279                                                      
REMARK 465     SER D   280                                                      
REMARK 465     VAL D   281                                                      
REMARK 465     ALA D   282                                                      
REMARK 465     GLN D   283                                                      
REMARK 465     GLU D   284                                                      
REMARK 465     GLU D   285                                                      
REMARK 465     THR D   286                                                      
REMARK 465     GLU D   287                                                      
REMARK 465     ILE D   288                                                      
REMARK 465     LEU D   289                                                      
REMARK 465     THR D   290                                                      
REMARK 465     ALA D   291                                                      
REMARK 465     ASP D   292                                                      
REMARK 465     ARG D   314                                                      
REMARK 465     MET D   315                                                      
REMARK 465     HIS D   316                                                      
REMARK 465     ILE D   317                                                      
REMARK 465     ARG D   318                                                      
REMARK 465     ARG D   319                                                      
REMARK 465     LYS D   320                                                      
REMARK 465     ARG D   321                                                      
REMARK 465     ILE D   322                                                      
REMARK 465     VAL D   323                                                      
REMARK 465     GLY D   324                                                      
REMARK 465     GLY D   325                                                      
REMARK 465     LYS D   326                                                      
REMARK 465     ARG D   327                                                      
REMARK 465     ALA D   328                                                      
REMARK 465     GLN D   329                                                      
REMARK 465     LEU D   330                                                      
REMARK 465     VAL D   378                                                      
REMARK 465     VAL D   379                                                      
REMARK 465     ASP D   380                                                      
REMARK 465     TRP D   381                                                      
REMARK 465     ILE D   382                                                      
REMARK 465     HIS D   383                                                      
REMARK 465     PRO D   384                                                      
REMARK 465     ASP D   385                                                      
REMARK 465     LEU D   386                                                      
REMARK 465     LYS D   387                                                      
REMARK 465     ARG D   388                                                      
REMARK 465     ARG D   430                                                      
REMARK 465     SER D   431                                                      
REMARK 465     ILE D   432                                                      
REMARK 465     GLY D   455                                                      
REMARK 465     ARG D   456                                                      
REMARK 465     GLU D   457                                                      
REMARK 465     LYS D   458                                                      
REMARK 465     ASP D   459                                                      
REMARK 465     ASN D   460                                                      
REMARK 465     GLU D   461                                                      
REMARK 465     ARG D   462                                                      
REMARK 465     VAL D   463                                                      
REMARK 465     PHE D   464                                                      
REMARK 465     SER D   465                                                      
REMARK 465     LEU D   466                                                      
REMARK 465     GLN D   467                                                      
REMARK 465     TRP D   468                                                      
REMARK 465     LYS D   504                                                      
REMARK 465     GLY D   505                                                      
REMARK 465     ASP D   506                                                      
REMARK 465     GLY D   556                                                      
REMARK 465     ARG D   557                                                      
REMARK 465     PRO D   558                                                      
REMARK 465     PHE D   559                                                      
REMARK 465     ILE D   560                                                      
REMARK 465     SER D   561                                                      
REMARK 465     GLN D   562                                                      
REMARK 465     TYR D   563                                                      
REMARK 465     ASN D   564                                                      
REMARK 465     VAL D   565                                                      
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    ARG B 184   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    LYS A  19       76.65     45.64                                   
REMARK 500    TRP A  33       34.68    -93.81                                   
REMARK 500    PRO A  78      151.07    -49.71                                   
REMARK 500    THR A  80       89.46    -64.49                                   
REMARK 500    LEU A  83      -51.00   -130.55                                   
REMARK 500    HIS A 100       71.97     53.94                                   
REMARK 500    VAL A 114      -50.64    -23.78                                   
REMARK 500    ASP A 155     -158.66     67.28                                   
REMARK 500    LEU A 156      125.85     72.54                                   
REMARK 500    ILE A 158       45.64   -108.23                                   
REMARK 500    SER A 174      144.41   -173.05                                   
REMARK 500    THR A 198       76.92   -117.96                                   
REMARK 500    GLN A 232       74.50     53.79                                   
REMARK 500    CYS A 237       69.60   -119.51                                   
REMARK 500    GLN A 242      -77.85    -83.06                                   
REMARK 500    ASN A 402       41.44    -95.75                                   
REMARK 500    LYS A 419      -60.17     76.22                                   
REMARK 500    ASP A 420      176.10     61.08                                   
REMARK 500    LYS A 423      -22.57   -160.18                                   
REMARK 500    LYS A 424     -110.20   -138.77                                   
REMARK 500    TRP B  33       30.75    -87.36                                   
REMARK 500    ASN B  60        0.70    -68.30                                   
REMARK 500    GLN B 116      -45.14   -139.29                                   
REMARK 500    TRP B 127       89.32   -158.41                                   
REMARK 500    LYS B 152      117.39   -170.15                                   
REMARK 500    SER B 154      -81.17     51.83                                   
REMARK 500    LEU B 156      170.97     69.08                                   
REMARK 500    ILE B 158     -153.96     68.42                                   
REMARK 500    ASN B 159      163.58     68.41                                   
REMARK 500    SER B 160       78.22     55.83                                   
REMARK 500    GLU B 162      110.44    -14.93                                   
REMARK 500    THR B 185     -124.28    103.72                                   
REMARK 500    MET B 186     -172.05    147.60                                   
REMARK 500    TYR B 188      -11.29     70.62                                   
REMARK 500    GLN B 189      -87.03   -155.41                                   
REMARK 500    CYS B 237       75.18   -161.17                                   
REMARK 500    GLN B 242      -75.63    -93.83                                   
REMARK 500    LYS B 244       51.44   -102.93                                   
REMARK 500    ASP B 292       88.22     61.50                                   
REMARK 500    SER B 308       58.21    -96.25                                   
REMARK 500    VAL B 323     -171.03     62.08                                   
REMARK 500    LYS B 326     -105.99   -101.83                                   
REMARK 500    ARG B 327      -57.93   -146.06                                   
REMARK 500    ALA B 328      155.95     98.78                                   
REMARK 500    GLN B 329      -76.62     62.52                                   
REMARK 500    TYR B 408       15.05     56.20                                   
REMARK 500    ARG B 430       79.16     55.06                                   
REMARK 500    ASN B 446      -18.15     74.41                                   
REMARK 500    ASN B 476       75.08     58.03                                   
REMARK 500    TYR B 481      -47.34   -140.90                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      91 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 ARG B  184     THR B  185                  143.41                    
REMARK 500 THR B  185     MET B  186                 -137.02                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 600                                                                      
REMARK 600 HETEROGEN                                                            
REMARK 600                                                                      
REMARK 600 N-ACETYLGLUCOSAMINE (NAG): N-LINKED GLYCOSYLATION                    
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 601  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 LYS A 221   O                                                      
REMARK 620 2 ASP A 224   OD1  80.7                                              
REMARK 620 3 ILE A 226   O   167.1  88.5                                        
REMARK 620 4 ASP A 228   OD2 100.2 101.6  75.1                                  
REMARK 620 5 ASP A 234   OD1 109.5 168.4  82.0  82.3                            
REMARK 620 6 GLU A 235   OE2 110.7  92.5  76.6 147.8  79.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 600  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 TYR A 258   O                                                      
REMARK 620 2 ASN A 261   OD1  91.0                                              
REMARK 620 3 GLU A 263   O   162.0  92.1                                        
REMARK 620 4 ASP A 265   OD2 102.2 114.4  92.6                                  
REMARK 620 5 ASP A 271   OD2  80.1 161.2  91.6  83.9                            
REMARK 620 6 GLU A 272   OE1  86.0  72.8  78.0 168.7  90.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B 601  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 LYS B 221   O                                                      
REMARK 620 2 ASP B 224   OD1  69.2                                              
REMARK 620 3 ILE B 226   O   162.5  93.5                                        
REMARK 620 4 ASP B 228   OD2  96.7 100.4  83.7                                  
REMARK 620 5 ASP B 234   OD1 113.1 168.9  84.4  90.2                            
REMARK 620 6 GLU B 235   OE2  98.1  84.5  82.0 165.2  84.4                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B 600  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 TYR B 258   O                                                      
REMARK 620 2 ASN B 261   OD1  75.6                                              
REMARK 620 3 GLU B 263   O   145.6  70.1                                        
REMARK 620 4 ASP B 271   OD2  97.4 171.7 117.0                                  
REMARK 620 5 GLU B 272   OE1  90.6  83.7  84.1 100.9                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA C 601  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 LYS C 221   O                                                      
REMARK 620 2 ASP C 224   OD1  75.8                                              
REMARK 620 3 ILE C 226   O   164.1  88.7                                        
REMARK 620 4 ASP C 228   OD2  97.1  88.6  78.4                                  
REMARK 620 5 ASP C 234   OD1  80.7 156.1 115.0  98.6                            
REMARK 620 6 GLU C 235   OE2  81.6  97.2 104.5 173.5  74.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA C 600  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 TYR C 258   O                                                      
REMARK 620 2 ASN C 261   OD1  85.5                                              
REMARK 620 3 GLU C 263   O   166.0 104.0                                        
REMARK 620 4 ASP C 265   OD2  65.5 106.9 101.5                                  
REMARK 620 5 ASP C 271   OD2  89.5 172.2  81.9  76.4                            
REMARK 620 6 GLU C 272   OE1 117.1  79.1  75.2 173.8  97.8                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA D 601  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 LYS D 221   O                                                      
REMARK 620 2 ASP D 224   OD1  67.6                                              
REMARK 620 3 ILE D 226   O   142.3  74.9                                        
REMARK 620 4 ASP D 228   OD2  78.2  93.8 100.4                                  
REMARK 620 5 ASP D 234   OD1 106.9 164.5 110.5  99.3                            
REMARK 620 6 GLU D 235   OE2  82.4  69.4  88.8 158.2  95.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA D 600  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 TYR D 258   O                                                      
REMARK 620 2 ASN D 261   OD1  71.0                                              
REMARK 620 3 GLU D 263   O   152.7  84.6                                        
REMARK 620 4 ASP D 265   OD2  82.9 110.6  94.9                                  
REMARK 620 5 ASP D 271   OD2 112.5 162.1  94.5  87.3                            
REMARK 620 6 GLU D 272   OE1 100.8  78.8  85.9 170.6  83.3                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 700                                                                      
REMARK 700 SHEET                                                                
REMARK 700 DETERMINATION METHOD: DSSP                                           
REMARK 700 THE SHEETS PRESENTED AS "AI" IN EACH CHAIN ON SHEET RECORDS          
REMARK 700 BELOW IS ACTUALLY AN  6-STRANDED BARREL THIS IS REPRESENTED BY       
REMARK 700 A  7-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS              
REMARK 700 ARE IDENTICAL.                                                       
REMARK 700 THE SHEETS PRESENTED AS "BG" IN EACH CHAIN ON SHEET RECORDS          
REMARK 700 BELOW IS ACTUALLY AN  6-STRANDED BARREL THIS IS REPRESENTED BY       
REMARK 700 A  7-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS              
REMARK 700 ARE IDENTICAL.                                                       
REMARK 700 THE SHEETS PRESENTED AS "BH" IN EACH CHAIN ON SHEET RECORDS          
REMARK 700 BELOW IS ACTUALLY AN  6-STRANDED BARREL THIS IS REPRESENTED BY       
REMARK 700 A  7-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS              
REMARK 700 ARE IDENTICAL.                                                       
REMARK 700 THE SHEETS PRESENTED AS "CI" IN EACH CHAIN ON SHEET RECORDS          
REMARK 700 BELOW IS ACTUALLY AN  6-STRANDED BARREL THIS IS REPRESENTED BY       
REMARK 700 A  7-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS              
REMARK 700 ARE IDENTICAL.                                                       
REMARK 700 THE SHEETS PRESENTED AS "DI" IN EACH CHAIN ON SHEET RECORDS          
REMARK 700 BELOW IS ACTUALLY AN  6-STRANDED BARREL THIS IS REPRESENTED BY       
REMARK 700 A  7-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS              
REMARK 700 ARE IDENTICAL.                                                       
REMARK 700 THE SHEETS PRESENTED AS "DJ" IN EACH CHAIN ON SHEET RECORDS          
REMARK 700 BELOW IS ACTUALLY AN -2-STRANDED BARREL THIS IS REPRESENTED BY       
REMARK 700 A -1-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS              
REMARK 700 ARE IDENTICAL.                                                       
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 THE PROTEIN IN THIS ENTRY IS THE MATURE FORM OF FACTOR I.            
REMARK 999 THEREFORE THE SIGNAL PEPTIDE (FIRST 18 RESIDUES) OF THE              
REMARK 999 UNIPROT ENTRY IS MISSING FROM THE SAMPLE, AND SO IS THE              
REMARK 999 SEQUENCE RRKR AT RESIDUE NUMBERS 336-339.                            
DBREF  2XRC A    1   565  UNP    P05156   CFAI_HUMAN      19    583             
DBREF  2XRC B    1   565  UNP    P05156   CFAI_HUMAN      19    583             
DBREF  2XRC C    1   565  UNP    P05156   CFAI_HUMAN      19    583             
DBREF  2XRC D    1   565  UNP    P05156   CFAI_HUMAN      19    583             
SEQRES   1 A  565  LYS VAL THR TYR THR SER GLN GLU ASP LEU VAL GLU LYS          
SEQRES   2 A  565  LYS CYS LEU ALA LYS LYS TYR THR HIS LEU SER CYS ASP          
SEQRES   3 A  565  LYS VAL PHE CYS GLN PRO TRP GLN ARG CYS ILE GLU GLY          
SEQRES   4 A  565  THR CYS VAL CYS LYS LEU PRO TYR GLN CYS PRO LYS ASN          
SEQRES   5 A  565  GLY THR ALA VAL CYS ALA THR ASN ARG ARG SER PHE PRO          
SEQRES   6 A  565  THR TYR CYS GLN GLN LYS SER LEU GLU CYS LEU HIS PRO          
SEQRES   7 A  565  GLY THR LYS PHE LEU ASN ASN GLY THR CYS THR ALA GLU          
SEQRES   8 A  565  GLY LYS PHE SER VAL SER LEU LYS HIS GLY ASN THR ASP          
SEQRES   9 A  565  SER GLU GLY ILE VAL GLU VAL LYS LEU VAL ASP GLN ASP          
SEQRES  10 A  565  LYS THR MET PHE ILE CYS LYS SER SER TRP SER MET ARG          
SEQRES  11 A  565  GLU ALA ASN VAL ALA CYS LEU ASP LEU GLY PHE GLN GLN          
SEQRES  12 A  565  GLY ALA ASP THR GLN ARG ARG PHE LYS LEU SER ASP LEU          
SEQRES  13 A  565  SER ILE ASN SER THR GLU CYS LEU HIS VAL HIS CYS ARG          
SEQRES  14 A  565  GLY LEU GLU THR SER LEU ALA GLU CYS THR PHE THR LYS          
SEQRES  15 A  565  ARG ARG THR MET GLY TYR GLN ASP PHE ALA ASP VAL VAL          
SEQRES  16 A  565  CYS TYR THR GLN LYS ALA ASP SER PRO MET ASP ASP PHE          
SEQRES  17 A  565  PHE GLN CYS VAL ASN GLY LYS TYR ILE SER GLN MET LYS          
SEQRES  18 A  565  ALA CYS ASP GLY ILE ASN ASP CYS GLY ASP GLN SER ASP          
SEQRES  19 A  565  GLU LEU CYS CYS LYS ALA CYS GLN GLY LYS GLY PHE HIS          
SEQRES  20 A  565  CYS LYS SER GLY VAL CYS ILE PRO SER GLN TYR GLN CYS          
SEQRES  21 A  565  ASN GLY GLU VAL ASP CYS ILE THR GLY GLU ASP GLU VAL          
SEQRES  22 A  565  GLY CYS ALA GLY PHE ALA SER VAL ALA GLN GLU GLU THR          
SEQRES  23 A  565  GLU ILE LEU THR ALA ASP MET ASP ALA GLU ARG ARG ARG          
SEQRES  24 A  565  ILE LYS SER LEU LEU PRO LYS LEU SER CYS GLY VAL LYS          
SEQRES  25 A  565  ASN ARG MET HIS ILE ARG ARG LYS ARG ILE VAL GLY GLY          
SEQRES  26 A  565  LYS ARG ALA GLN LEU GLY ASP LEU PRO TRP GLN VAL ALA          
SEQRES  27 A  565  ILE LYS ASP ALA SER GLY ILE THR CYS GLY GLY ILE TYR          
SEQRES  28 A  565  ILE GLY GLY CYS TRP ILE LEU THR ALA ALA HIS CYS LEU          
SEQRES  29 A  565  ARG ALA SER LYS THR HIS ARG TYR GLN ILE TRP THR THR          
SEQRES  30 A  565  VAL VAL ASP TRP ILE HIS PRO ASP LEU LYS ARG ILE VAL          
SEQRES  31 A  565  ILE GLU TYR VAL ASP ARG ILE ILE PHE HIS GLU ASN TYR          
SEQRES  32 A  565  ASN ALA GLY THR TYR GLN ASN ASP ILE ALA LEU ILE GLU          
SEQRES  33 A  565  MET LYS LYS ASP GLY ASN LYS LYS ASP CYS GLU LEU PRO          
SEQRES  34 A  565  ARG SER ILE PRO ALA CYS VAL PRO TRP SER PRO TYR LEU          
SEQRES  35 A  565  PHE GLN PRO ASN ASP THR CYS ILE VAL SER GLY TRP GLY          
SEQRES  36 A  565  ARG GLU LYS ASP ASN GLU ARG VAL PHE SER LEU GLN TRP          
SEQRES  37 A  565  GLY GLU VAL LYS LEU ILE SER ASN CYS SER LYS PHE TYR          
SEQRES  38 A  565  GLY ASN ARG PHE TYR GLU LYS GLU MET GLU CYS ALA GLY          
SEQRES  39 A  565  THR TYR ASP GLY SER ILE ASP ALA CYS LYS GLY ASP SER          
SEQRES  40 A  565  GLY GLY PRO LEU VAL CYS MET ASP ALA ASN ASN VAL THR          
SEQRES  41 A  565  TYR VAL TRP GLY VAL VAL SER TRP GLY GLU ASN CYS GLY          
SEQRES  42 A  565  LYS PRO GLU PHE PRO GLY VAL TYR THR LYS VAL ALA ASN          
SEQRES  43 A  565  TYR PHE ASP TRP ILE SER TYR HIS VAL GLY ARG PRO PHE          
SEQRES  44 A  565  ILE SER GLN TYR ASN VAL                                      
SEQRES   1 B  565  LYS VAL THR TYR THR SER GLN GLU ASP LEU VAL GLU LYS          
SEQRES   2 B  565  LYS CYS LEU ALA LYS LYS TYR THR HIS LEU SER CYS ASP          
SEQRES   3 B  565  LYS VAL PHE CYS GLN PRO TRP GLN ARG CYS ILE GLU GLY          
SEQRES   4 B  565  THR CYS VAL CYS LYS LEU PRO TYR GLN CYS PRO LYS ASN          
SEQRES   5 B  565  GLY THR ALA VAL CYS ALA THR ASN ARG ARG SER PHE PRO          
SEQRES   6 B  565  THR TYR CYS GLN GLN LYS SER LEU GLU CYS LEU HIS PRO          
SEQRES   7 B  565  GLY THR LYS PHE LEU ASN ASN GLY THR CYS THR ALA GLU          
SEQRES   8 B  565  GLY LYS PHE SER VAL SER LEU LYS HIS GLY ASN THR ASP          
SEQRES   9 B  565  SER GLU GLY ILE VAL GLU VAL LYS LEU VAL ASP GLN ASP          
SEQRES  10 B  565  LYS THR MET PHE ILE CYS LYS SER SER TRP SER MET ARG          
SEQRES  11 B  565  GLU ALA ASN VAL ALA CYS LEU ASP LEU GLY PHE GLN GLN          
SEQRES  12 B  565  GLY ALA ASP THR GLN ARG ARG PHE LYS LEU SER ASP LEU          
SEQRES  13 B  565  SER ILE ASN SER THR GLU CYS LEU HIS VAL HIS CYS ARG          
SEQRES  14 B  565  GLY LEU GLU THR SER LEU ALA GLU CYS THR PHE THR LYS          
SEQRES  15 B  565  ARG ARG THR MET GLY TYR GLN ASP PHE ALA ASP VAL VAL          
SEQRES  16 B  565  CYS TYR THR GLN LYS ALA ASP SER PRO MET ASP ASP PHE          
SEQRES  17 B  565  PHE GLN CYS VAL ASN GLY LYS TYR ILE SER GLN MET LYS          
SEQRES  18 B  565  ALA CYS ASP GLY ILE ASN ASP CYS GLY ASP GLN SER ASP          
SEQRES  19 B  565  GLU LEU CYS CYS LYS ALA CYS GLN GLY LYS GLY PHE HIS          
SEQRES  20 B  565  CYS LYS SER GLY VAL CYS ILE PRO SER GLN TYR GLN CYS          
SEQRES  21 B  565  ASN GLY GLU VAL ASP CYS ILE THR GLY GLU ASP GLU VAL          
SEQRES  22 B  565  GLY CYS ALA GLY PHE ALA SER VAL ALA GLN GLU GLU THR          
SEQRES  23 B  565  GLU ILE LEU THR ALA ASP MET ASP ALA GLU ARG ARG ARG          
SEQRES  24 B  565  ILE LYS SER LEU LEU PRO LYS LEU SER CYS GLY VAL LYS          
SEQRES  25 B  565  ASN ARG MET HIS ILE ARG ARG LYS ARG ILE VAL GLY GLY          
SEQRES  26 B  565  LYS ARG ALA GLN LEU GLY ASP LEU PRO TRP GLN VAL ALA          
SEQRES  27 B  565  ILE LYS ASP ALA SER GLY ILE THR CYS GLY GLY ILE TYR          
SEQRES  28 B  565  ILE GLY GLY CYS TRP ILE LEU THR ALA ALA HIS CYS LEU          
SEQRES  29 B  565  ARG ALA SER LYS THR HIS ARG TYR GLN ILE TRP THR THR          
SEQRES  30 B  565  VAL VAL ASP TRP ILE HIS PRO ASP LEU LYS ARG ILE VAL          
SEQRES  31 B  565  ILE GLU TYR VAL ASP ARG ILE ILE PHE HIS GLU ASN TYR          
SEQRES  32 B  565  ASN ALA GLY THR TYR GLN ASN ASP ILE ALA LEU ILE GLU          
SEQRES  33 B  565  MET LYS LYS ASP GLY ASN LYS LYS ASP CYS GLU LEU PRO          
SEQRES  34 B  565  ARG SER ILE PRO ALA CYS VAL PRO TRP SER PRO TYR LEU          
SEQRES  35 B  565  PHE GLN PRO ASN ASP THR CYS ILE VAL SER GLY TRP GLY          
SEQRES  36 B  565  ARG GLU LYS ASP ASN GLU ARG VAL PHE SER LEU GLN TRP          
SEQRES  37 B  565  GLY GLU VAL LYS LEU ILE SER ASN CYS SER LYS PHE TYR          
SEQRES  38 B  565  GLY ASN ARG PHE TYR GLU LYS GLU MET GLU CYS ALA GLY          
SEQRES  39 B  565  THR TYR ASP GLY SER ILE ASP ALA CYS LYS GLY ASP SER          
SEQRES  40 B  565  GLY GLY PRO LEU VAL CYS MET ASP ALA ASN ASN VAL THR          
SEQRES  41 B  565  TYR VAL TRP GLY VAL VAL SER TRP GLY GLU ASN CYS GLY          
SEQRES  42 B  565  LYS PRO GLU PHE PRO GLY VAL TYR THR LYS VAL ALA ASN          
SEQRES  43 B  565  TYR PHE ASP TRP ILE SER TYR HIS VAL GLY ARG PRO PHE          
SEQRES  44 B  565  ILE SER GLN TYR ASN VAL                                      
SEQRES   1 C  565  LYS VAL THR TYR THR SER GLN GLU ASP LEU VAL GLU LYS          
SEQRES   2 C  565  LYS CYS LEU ALA LYS LYS TYR THR HIS LEU SER CYS ASP          
SEQRES   3 C  565  LYS VAL PHE CYS GLN PRO TRP GLN ARG CYS ILE GLU GLY          
SEQRES   4 C  565  THR CYS VAL CYS LYS LEU PRO TYR GLN CYS PRO LYS ASN          
SEQRES   5 C  565  GLY THR ALA VAL CYS ALA THR ASN ARG ARG SER PHE PRO          
SEQRES   6 C  565  THR TYR CYS GLN GLN LYS SER LEU GLU CYS LEU HIS PRO          
SEQRES   7 C  565  GLY THR LYS PHE LEU ASN ASN GLY THR CYS THR ALA GLU          
SEQRES   8 C  565  GLY LYS PHE SER VAL SER LEU LYS HIS GLY ASN THR ASP          
SEQRES   9 C  565  SER GLU GLY ILE VAL GLU VAL LYS LEU VAL ASP GLN ASP          
SEQRES  10 C  565  LYS THR MET PHE ILE CYS LYS SER SER TRP SER MET ARG          
SEQRES  11 C  565  GLU ALA ASN VAL ALA CYS LEU ASP LEU GLY PHE GLN GLN          
SEQRES  12 C  565  GLY ALA ASP THR GLN ARG ARG PHE LYS LEU SER ASP LEU          
SEQRES  13 C  565  SER ILE ASN SER THR GLU CYS LEU HIS VAL HIS CYS ARG          
SEQRES  14 C  565  GLY LEU GLU THR SER LEU ALA GLU CYS THR PHE THR LYS          
SEQRES  15 C  565  ARG ARG THR MET GLY TYR GLN ASP PHE ALA ASP VAL VAL          
SEQRES  16 C  565  CYS TYR THR GLN LYS ALA ASP SER PRO MET ASP ASP PHE          
SEQRES  17 C  565  PHE GLN CYS VAL ASN GLY LYS TYR ILE SER GLN MET LYS          
SEQRES  18 C  565  ALA CYS ASP GLY ILE ASN ASP CYS GLY ASP GLN SER ASP          
SEQRES  19 C  565  GLU LEU CYS CYS LYS ALA CYS GLN GLY LYS GLY PHE HIS          
SEQRES  20 C  565  CYS LYS SER GLY VAL CYS ILE PRO SER GLN TYR GLN CYS          
SEQRES  21 C  565  ASN GLY GLU VAL ASP CYS ILE THR GLY GLU ASP GLU VAL          
SEQRES  22 C  565  GLY CYS ALA GLY PHE ALA SER VAL ALA GLN GLU GLU THR          
SEQRES  23 C  565  GLU ILE LEU THR ALA ASP MET ASP ALA GLU ARG ARG ARG          
SEQRES  24 C  565  ILE LYS SER LEU LEU PRO LYS LEU SER CYS GLY VAL LYS          
SEQRES  25 C  565  ASN ARG MET HIS ILE ARG ARG LYS ARG ILE VAL GLY GLY          
SEQRES  26 C  565  LYS ARG ALA GLN LEU GLY ASP LEU PRO TRP GLN VAL ALA          
SEQRES  27 C  565  ILE LYS ASP ALA SER GLY ILE THR CYS GLY GLY ILE TYR          
SEQRES  28 C  565  ILE GLY GLY CYS TRP ILE LEU THR ALA ALA HIS CYS LEU          
SEQRES  29 C  565  ARG ALA SER LYS THR HIS ARG TYR GLN ILE TRP THR THR          
SEQRES  30 C  565  VAL VAL ASP TRP ILE HIS PRO ASP LEU LYS ARG ILE VAL          
SEQRES  31 C  565  ILE GLU TYR VAL ASP ARG ILE ILE PHE HIS GLU ASN TYR          
SEQRES  32 C  565  ASN ALA GLY THR TYR GLN ASN ASP ILE ALA LEU ILE GLU          
SEQRES  33 C  565  MET LYS LYS ASP GLY ASN LYS LYS ASP CYS GLU LEU PRO          
SEQRES  34 C  565  ARG SER ILE PRO ALA CYS VAL PRO TRP SER PRO TYR LEU          
SEQRES  35 C  565  PHE GLN PRO ASN ASP THR CYS ILE VAL SER GLY TRP GLY          
SEQRES  36 C  565  ARG GLU LYS ASP ASN GLU ARG VAL PHE SER LEU GLN TRP          
SEQRES  37 C  565  GLY GLU VAL LYS LEU ILE SER ASN CYS SER LYS PHE TYR          
SEQRES  38 C  565  GLY ASN ARG PHE TYR GLU LYS GLU MET GLU CYS ALA GLY          
SEQRES  39 C  565  THR TYR ASP GLY SER ILE ASP ALA CYS LYS GLY ASP SER          
SEQRES  40 C  565  GLY GLY PRO LEU VAL CYS MET ASP ALA ASN ASN VAL THR          
SEQRES  41 C  565  TYR VAL TRP GLY VAL VAL SER TRP GLY GLU ASN CYS GLY          
SEQRES  42 C  565  LYS PRO GLU PHE PRO GLY VAL TYR THR LYS VAL ALA ASN          
SEQRES  43 C  565  TYR PHE ASP TRP ILE SER TYR HIS VAL GLY ARG PRO PHE          
SEQRES  44 C  565  ILE SER GLN TYR ASN VAL                                      
SEQRES   1 D  565  LYS VAL THR TYR THR SER GLN GLU ASP LEU VAL GLU LYS          
SEQRES   2 D  565  LYS CYS LEU ALA LYS LYS TYR THR HIS LEU SER CYS ASP          
SEQRES   3 D  565  LYS VAL PHE CYS GLN PRO TRP GLN ARG CYS ILE GLU GLY          
SEQRES   4 D  565  THR CYS VAL CYS LYS LEU PRO TYR GLN CYS PRO LYS ASN          
SEQRES   5 D  565  GLY THR ALA VAL CYS ALA THR ASN ARG ARG SER PHE PRO          
SEQRES   6 D  565  THR TYR CYS GLN GLN LYS SER LEU GLU CYS LEU HIS PRO          
SEQRES   7 D  565  GLY THR LYS PHE LEU ASN ASN GLY THR CYS THR ALA GLU          
SEQRES   8 D  565  GLY LYS PHE SER VAL SER LEU LYS HIS GLY ASN THR ASP          
SEQRES   9 D  565  SER GLU GLY ILE VAL GLU VAL LYS LEU VAL ASP GLN ASP          
SEQRES  10 D  565  LYS THR MET PHE ILE CYS LYS SER SER TRP SER MET ARG          
SEQRES  11 D  565  GLU ALA ASN VAL ALA CYS LEU ASP LEU GLY PHE GLN GLN          
SEQRES  12 D  565  GLY ALA ASP THR GLN ARG ARG PHE LYS LEU SER ASP LEU          
SEQRES  13 D  565  SER ILE ASN SER THR GLU CYS LEU HIS VAL HIS CYS ARG          
SEQRES  14 D  565  GLY LEU GLU THR SER LEU ALA GLU CYS THR PHE THR LYS          
SEQRES  15 D  565  ARG ARG THR MET GLY TYR GLN ASP PHE ALA ASP VAL VAL          
SEQRES  16 D  565  CYS TYR THR GLN LYS ALA ASP SER PRO MET ASP ASP PHE          
SEQRES  17 D  565  PHE GLN CYS VAL ASN GLY LYS TYR ILE SER GLN MET LYS          
SEQRES  18 D  565  ALA CYS ASP GLY ILE ASN ASP CYS GLY ASP GLN SER ASP          
SEQRES  19 D  565  GLU LEU CYS CYS LYS ALA CYS GLN GLY LYS GLY PHE HIS          
SEQRES  20 D  565  CYS LYS SER GLY VAL CYS ILE PRO SER GLN TYR GLN CYS          
SEQRES  21 D  565  ASN GLY GLU VAL ASP CYS ILE THR GLY GLU ASP GLU VAL          
SEQRES  22 D  565  GLY CYS ALA GLY PHE ALA SER VAL ALA GLN GLU GLU THR          
SEQRES  23 D  565  GLU ILE LEU THR ALA ASP MET ASP ALA GLU ARG ARG ARG          
SEQRES  24 D  565  ILE LYS SER LEU LEU PRO LYS LEU SER CYS GLY VAL LYS          
SEQRES  25 D  565  ASN ARG MET HIS ILE ARG ARG LYS ARG ILE VAL GLY GLY          
SEQRES  26 D  565  LYS ARG ALA GLN LEU GLY ASP LEU PRO TRP GLN VAL ALA          
SEQRES  27 D  565  ILE LYS ASP ALA SER GLY ILE THR CYS GLY GLY ILE TYR          
SEQRES  28 D  565  ILE GLY GLY CYS TRP ILE LEU THR ALA ALA HIS CYS LEU          
SEQRES  29 D  565  ARG ALA SER LYS THR HIS ARG TYR GLN ILE TRP THR THR          
SEQRES  30 D  565  VAL VAL ASP TRP ILE HIS PRO ASP LEU LYS ARG ILE VAL          
SEQRES  31 D  565  ILE GLU TYR VAL ASP ARG ILE ILE PHE HIS GLU ASN TYR          
SEQRES  32 D  565  ASN ALA GLY THR TYR GLN ASN ASP ILE ALA LEU ILE GLU          
SEQRES  33 D  565  MET LYS LYS ASP GLY ASN LYS LYS ASP CYS GLU LEU PRO          
SEQRES  34 D  565  ARG SER ILE PRO ALA CYS VAL PRO TRP SER PRO TYR LEU          
SEQRES  35 D  565  PHE GLN PRO ASN ASP THR CYS ILE VAL SER GLY TRP GLY          
SEQRES  36 D  565  ARG GLU LYS ASP ASN GLU ARG VAL PHE SER LEU GLN TRP          
SEQRES  37 D  565  GLY GLU VAL LYS LEU ILE SER ASN CYS SER LYS PHE TYR          
SEQRES  38 D  565  GLY ASN ARG PHE TYR GLU LYS GLU MET GLU CYS ALA GLY          
SEQRES  39 D  565  THR TYR ASP GLY SER ILE ASP ALA CYS LYS GLY ASP SER          
SEQRES  40 D  565  GLY GLY PRO LEU VAL CYS MET ASP ALA ASN ASN VAL THR          
SEQRES  41 D  565  TYR VAL TRP GLY VAL VAL SER TRP GLY GLU ASN CYS GLY          
SEQRES  42 D  565  LYS PRO GLU PHE PRO GLY VAL TYR THR LYS VAL ALA ASN          
SEQRES  43 D  565  TYR PHE ASP TRP ILE SER TYR HIS VAL GLY ARG PRO PHE          
SEQRES  44 D  565  ILE SER GLN TYR ASN VAL                                      
MODRES 2XRC ASN A   52  ASN  GLYCOSYLATION SITE                                 
MODRES 2XRC ASN A   85  ASN  GLYCOSYLATION SITE                                 
MODRES 2XRC ASN A  159  ASN  GLYCOSYLATION SITE                                 
MODRES 2XRC ASN A  446  ASN  GLYCOSYLATION SITE                                 
MODRES 2XRC ASN A  476  ASN  GLYCOSYLATION SITE                                 
MODRES 2XRC ASN A  518  ASN  GLYCOSYLATION SITE                                 
MODRES 2XRC ASN B   52  ASN  GLYCOSYLATION SITE                                 
MODRES 2XRC ASN B   85  ASN  GLYCOSYLATION SITE                                 
MODRES 2XRC ASN B  159  ASN  GLYCOSYLATION SITE                                 
MODRES 2XRC ASN B  446  ASN  GLYCOSYLATION SITE                                 
MODRES 2XRC ASN B  476  ASN  GLYCOSYLATION SITE                                 
MODRES 2XRC ASN B  518  ASN  GLYCOSYLATION SITE                                 
MODRES 2XRC ASN C   52  ASN  GLYCOSYLATION SITE                                 
MODRES 2XRC ASN C   85  ASN  GLYCOSYLATION SITE                                 
MODRES 2XRC ASN C  446  ASN  GLYCOSYLATION SITE                                 
MODRES 2XRC ASN C  476  ASN  GLYCOSYLATION SITE                                 
MODRES 2XRC ASN C  518  ASN  GLYCOSYLATION SITE                                 
MODRES 2XRC ASN D   52  ASN  GLYCOSYLATION SITE                                 
MODRES 2XRC ASN D   85  ASN  GLYCOSYLATION SITE                                 
MODRES 2XRC ASN D  446  ASN  GLYCOSYLATION SITE                                 
MODRES 2XRC ASN D  476  ASN  GLYCOSYLATION SITE                                 
MODRES 2XRC ASN D  518  ASN  GLYCOSYLATION SITE                                 
HET     CA  A 600       1                                                       
HET     CA  A 601       1                                                       
HET    NAG  A 618      14                                                       
HET    NAG  A 646      14                                                       
HET    NAG  A 652      14                                                       
HET    NAG  A 659      14                                                       
HET    NAG  A 676      14                                                       
HET    NAG  A 685      14                                                       
HET     CA  B 600       1                                                       
HET     CA  B 601       1                                                       
HET    NAG  B 618      14                                                       
HET    NAG  B 646      14                                                       
HET    NAG  B 652      14                                                       
HET    NAG  B 659      14                                                       
HET    NAG  B 676      14                                                       
HET    NAG  B 685      14                                                       
HET     CA  C 600       1                                                       
HET     CA  C 601       1                                                       
HET    NAG  C 618      14                                                       
HET    NAG  C 646      14                                                       
HET    NAG  C 652      14                                                       
HET    NAG  C 676      14                                                       
HET    NAG  C 685      14                                                       
HET     CA  D 600       1                                                       
HET     CA  D 601       1                                                       
HET    NAG  D 618      14                                                       
HET    NAG  D 646      14                                                       
HET    NAG  D 652      14                                                       
HET    NAG  D 676      14                                                       
HET    NAG  D 685      14                                                       
HETNAM      CA CALCIUM ION                                                      
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
FORMUL   5   CA    8(CA 2+)                                                     
FORMUL   7  NAG    22(C8 H15 N O6)                                              
HELIX    1   1 CYS A   25  VAL A   28  5                                   4    
HELIX    2   2 LEU A   45  CYS A   49  5                                   5    
HELIX    3   3 THR A   66  HIS A   77  1                                  12    
HELIX    4   4 SER A  128  LEU A  139  1                                  12    
HELIX    5   5 SER A  174  CYS A  178  5                                   5    
HELIX    6   6 PRO A  255  GLN A  259  5                                   5    
HELIX    7   7 MET A  293  SER A  302  1                                  10    
HELIX    8   8 ALA A  360  ARG A  365  1                                   6    
HELIX    9   9 CYS A  477  GLY A  482  1                                   6    
HELIX   10  10 TYR A  547  VAL A  555  1                                   9    
HELIX   11  11 GLU B   12  LEU B   16  5                                   5    
HELIX   12  12 LEU B   45  CYS B   49  5                                   5    
HELIX   13  13 THR B   66  HIS B   77  1                                  12    
HELIX   14  14 SER B  128  GLY B  140  1                                  13    
HELIX   15  15 SER B  174  CYS B  178  5                                   5    
HELIX   16  16 SER B  218  ALA B  222  5                                   5    
HELIX   17  17 GLN B  232  LEU B  236  5                                   5    
HELIX   18  18 GLN B  257  GLN B  259  5                                   3    
HELIX   19  19 GLY B  269  VAL B  273  5                                   5    
HELIX   20  20 ASP B  292  LEU B  304  1                                  13    
HELIX   21  21 ALA B  361  ALA B  366  1                                   6    
HELIX   22  22 ASN B  476  PHE B  480  5                                   5    
HELIX   23  23 TYR B  547  VAL B  555  1                                   9    
HELIX   24  24 GLU C   12  ALA C   17  1                                   6    
HELIX   25  25 LEU C   45  CYS C   49  5                                   5    
HELIX   26  26 THR C   66  HIS C   77  1                                  12    
HELIX   27  27 SER C  128  LEU C  139  1                                  12    
HELIX   28  28 MET C  220  ALA C  222  5                                   3    
HELIX   29  29 GLN C  232  LEU C  236  5                                   5    
HELIX   30  30 GLN C  257  GLN C  259  5                                   3    
HELIX   31  31 GLY C  269  VAL C  273  5                                   5    
HELIX   32  32 MET C  293  SER C  302  1                                  10    
HELIX   33  33 CYS C  477  GLY C  482  1                                   6    
HELIX   34  34 ASN C  483  PHE C  485  5                                   3    
HELIX   35  35 TYR C  547  VAL C  555  1                                   9    
HELIX   36  36 LEU D   45  CYS D   49  5                                   5    
HELIX   37  37 THR D   66  HIS D   77  1                                  12    
HELIX   38  38 SER D  128  ASP D  138  1                                  11    
HELIX   39  39 SER D  174  CYS D  178  5                                   5    
HELIX   40  40 SER D  218  ALA D  222  5                                   5    
HELIX   41  41 GLN D  232  LEU D  236  5                                   5    
HELIX   42  42 GLY D  269  VAL D  273  5                                   5    
HELIX   43  43 MET D  293  SER D  302  1                                  10    
HELIX   44  44 CYS D  363  SER D  367  5                                   5    
HELIX   45  45 TYR D  547  VAL D  555  1                                   9    
SHEET    1  AA-5 GLN A  34  ILE A  37  0                                        
SHEET    2  AA-5 THR A  40  CYS A  43 -1  O  THR A  40   N  ILE A  37           
SHEET    1  AB-4 ARG A  62  PHE A  64  0                                        
SHEET    2  AB-4 VAL A  56  ALA A  58 -1  O  VAL A  56   N  PHE A  64           
SHEET    3  AB-4 PHE A  82  ASN A  85 -1  N  LEU A  83   O  CYS A  57           
SHEET    1  AC-5 SER A  95  LYS A  99  0                                        
SHEET    2  AC-5 GLU A 106  LYS A 112 -1  O  ILE A 108   N  LYS A  99           
SHEET    1  AD-5 MET A 120  PHE A 121  0                                        
SHEET    2  AD-5 GLU A 106  LYS A 112  1  O  VAL A 111   N  MET A 120           
SHEET    1  AE-5 ASP A 193  VAL A 195  0                                        
SHEET    2  AE-5 GLU A 106  LYS A 112 -1  O  GLY A 107   N  VAL A 194           
SHEET    1  AF-5 HIS A 165  HIS A 167  0                                        
SHEET    2  AF-5 THR A 179  THR A 181 -1  O  THR A 179   N  HIS A 167           
SHEET    1  AG-5 PHE A 246  CYS A 248  0                                        
SHEET    2  AG-5 VAL A 252  ILE A 254 -1  O  VAL A 252   N  CYS A 248           
SHEET    1  AH-1 ALA A 338  ASP A 341  0                                        
SHEET    2  AH-1 TYR A 372  TRP A 375 -1  O  GLN A 373   N  LYS A 340           
SHEET    3  AH-1 ILE A 391  PHE A 399 -1  O  GLU A 392   N  ILE A 374           
SHEET    4  AH-1 ALA A 413  MET A 417 -1  O  LEU A 414   N  ILE A 398           
SHEET    5  AH-1 TRP A 356  THR A 359 -1  O  ILE A 357   N  ILE A 415           
SHEET    6  AH-1 ILE A 350  GLY A 353 -1  O  ILE A 350   N  LEU A 358           
SHEET    1  AI 0 THR A 448  SER A 452  0                                        
SHEET    2  AI 0 TRP A 468  LEU A 473 -1  O  GLY A 469   N  VAL A 451           
SHEET    3  AI 0 MET A 490  THR A 495 -1  O  GLY A 494   N  LYS A 472           
SHEET    4  AI 0 GLY A 539  LYS A 543 -1  O  GLY A 539   N  ALA A 493           
SHEET    5  AI 0 THR A 520  TRP A 528 -1  O  VAL A 525   N  THR A 542           
SHEET    6  AI 0 PRO A 510  MET A 514 -1  O  LEU A 511   N  TRP A 523           
SHEET    7  AI 0 THR A 448  SER A 452 -1  O  ILE A 450   N  VAL A 512           
SHEET    1  BA-5 GLN B  34  ILE B  37  0                                        
SHEET    2  BA-5 THR B  40  CYS B  43 -1  O  THR B  40   N  ILE B  37           
SHEET    1  BB-4 ARG B  62  PHE B  64  0                                        
SHEET    2  BB-4 VAL B  56  ALA B  58 -1  O  VAL B  56   N  PHE B  64           
SHEET    3  BB-4 PHE B  82  ASN B  84 -1  N  LEU B  83   O  CYS B  57           
SHEET    1  BC-4 SER B  95  LYS B  99  0                                        
SHEET    2  BC-4 GLU B 106  LYS B 112 -1  O  ILE B 108   N  LYS B  99           
SHEET    3  BC-4 ASP B 193  VAL B 195 -1  O  VAL B 194   N  GLY B 107           
SHEET    1  BD-5 PHE B 121  ILE B 122  0                                        
SHEET    2  BD-5 CYS B 163  LEU B 164  1  N  LEU B 164   O  PHE B 121           
SHEET    1  BE-5 PHE B 209  GLN B 210  0                                        
SHEET    2  BE-5 TYR B 216  ILE B 217 -1  O  ILE B 217   N  PHE B 209           
SHEET    1  BF-5 GLY B 245  CYS B 248  0                                        
SHEET    2  BF-5 VAL B 252  PRO B 255 -1  O  VAL B 252   N  CYS B 248           
SHEET    1  BG 0 GLN B 336  LYS B 340  0                                        
SHEET    2  BG 0 THR B 346  GLY B 353 -1  O  CYS B 347   N  ILE B 339           
SHEET    3  BG 0 TRP B 356  THR B 359 -1  O  TRP B 356   N  ILE B 352           
SHEET    4  BG 0 ALA B 413  MET B 417 -1  O  ALA B 413   N  THR B 359           
SHEET    5  BG 0 ILE B 391  PHE B 399 -1  N  ASP B 395   O  GLU B 416           
SHEET    6  BG 0 GLN B 373  TRP B 375 -1  O  ILE B 374   N  GLU B 392           
SHEET    7  BG 0 GLN B 336  LYS B 340 -1  O  ALA B 338   N  TRP B 375           
SHEET    1  BH 0 THR B 448  SER B 452  0                                        
SHEET    2  BH 0 TRP B 468  LEU B 473 -1  O  GLY B 469   N  VAL B 451           
SHEET    3  BH 0 MET B 490  THR B 495 -1  O  GLY B 494   N  LYS B 472           
SHEET    4  BH 0 GLY B 539  LYS B 543 -1  O  GLY B 539   N  ALA B 493           
SHEET    5  BH 0 THR B 520  TRP B 528 -1  O  VAL B 525   N  THR B 542           
SHEET    6  BH 0 PRO B 510  MET B 514 -1  O  LEU B 511   N  TRP B 523           
SHEET    7  BH 0 THR B 448  SER B 452 -1  O  ILE B 450   N  VAL B 512           
SHEET    1  CA-5 GLN C  34  ILE C  37  0                                        
SHEET    2  CA-5 THR C  40  CYS C  43 -1  O  THR C  40   N  ILE C  37           
SHEET    1  CB-4 SER C  63  PHE C  64  0                                        
SHEET    2  CB-4 VAL C  56  ALA C  58 -1  O  VAL C  56   N  PHE C  64           
SHEET    3  CB-4 PHE C  82  ASN C  85 -1  N  LEU C  83   O  CYS C  57           
SHEET    1  CC-5 SER C  95  THR C 103  0                                        
SHEET    2  CC-5 GLU C 106  LYS C 112 -1  O  GLU C 106   N  THR C 103           
SHEET    1  CD-5 THR C 119  PHE C 121  0                                        
SHEET    2  CD-5 GLU C 106  LYS C 112  1  O  VAL C 111   N  MET C 120           
SHEET    1  CE-5 ASP C 193  VAL C 195  0                                        
SHEET    2  CE-5 GLU C 106  LYS C 112 -1  O  GLY C 107   N  VAL C 194           
SHEET    1  CF-5 LEU C 164  HIS C 167  0                                        
SHEET    2  CF-5 THR C 179  LYS C 182 -1  O  THR C 179   N  HIS C 167           
SHEET    1  CG-5 PHE C 208  GLN C 210  0                                        
SHEET    2  CG-5 TYR C 216  SER C 218 -1  O  ILE C 217   N  PHE C 209           
SHEET    1  CH-5 GLY C 245  CYS C 248  0                                        
SHEET    2  CH-5 VAL C 252  PRO C 255 -1  O  VAL C 252   N  CYS C 248           
SHEET    1  CI 0 GLN C 336  LYS C 340  0                                        
SHEET    2  CI 0 THR C 346  TYR C 351 -1  O  CYS C 347   N  ILE C 339           
SHEET    3  CI 0 TRP C 356  THR C 359 -1  O  LEU C 358   N  ILE C 350           
SHEET    4  CI 0 ALA C 413  MET C 417 -1  O  ALA C 413   N  THR C 359           
SHEET    5  CI 0 ILE C 391  PHE C 399 -1  N  ASP C 395   O  GLU C 416           
SHEET    6  CI 0 GLN C 373  THR C 376 -1  O  ILE C 374   N  GLU C 392           
SHEET    7  CI 0 GLN C 336  LYS C 340 -1  O  ALA C 338   N  TRP C 375           
SHEET    1  CJ 0 THR C 520  TYR C 521  0                                        
SHEET    2  CJ 0 LEU C 511  MET C 514 -1  O  CYS C 513   N  TYR C 521           
SHEET    3  CJ 0 THR C 448  GLY C 453 -1  O  THR C 448   N  MET C 514           
SHEET    4  CJ 0 GLN C 467  LEU C 473 -1  O  GLN C 467   N  GLY C 453           
SHEET    5  CJ 0 MET C 490  GLY C 494 -1  O  GLY C 494   N  LYS C 472           
SHEET    6  CJ 0 GLY C 539  LYS C 543 -1  O  GLY C 539   N  ALA C 493           
SHEET    7  CJ 0 GLY C 524  TRP C 528 -1  O  VAL C 525   N  THR C 542           
SHEET    1  DA-5 GLN D  34  ILE D  37  0                                        
SHEET    2  DA-5 THR D  40  CYS D  43 -1  O  THR D  40   N  ILE D  37           
SHEET    1  DB-4 SER D  63  PHE D  64  0                                        
SHEET    2  DB-4 VAL D  56  ALA D  58 -1  O  VAL D  56   N  PHE D  64           
SHEET    3  DB-4 PHE D  82  ASN D  85 -1  N  LEU D  83   O  CYS D  57           
SHEET    1  DC-5 SER D  95  LYS D  99  0                                        
SHEET    2  DC-5 GLU D 106  LYS D 112 -1  O  ILE D 108   N  LYS D  99           
SHEET    1  DD-2 THR D 179  LYS D 182  0                                        
SHEET    2  DD-2 CYS D 163  HIS D 167 -1  O  HIS D 165   N  THR D 181           
SHEET    3  DD-2 MET D 120  ILE D 122  1  O  PHE D 121   N  LEU D 164           
SHEET    4  DD-2 GLU D 106  LYS D 112 -1  O  VAL D 109   N  ILE D 122           
SHEET    5  DD-2 ASP D 193  VAL D 195  1  O  VAL D 194   N  GLY D 107           
SHEET    1  DE-2 THR D 179  LYS D 182  0                                        
SHEET    2  DE-2 CYS D 163  HIS D 167 -1  O  HIS D 165   N  THR D 181           
SHEET    3  DE-2 MET D 120  ILE D 122  1  O  PHE D 121   N  LEU D 164           
SHEET    4  DE-2 GLU D 106  LYS D 112 -1  O  VAL D 109   N  ILE D 122           
SHEET    5  DE-2 SER D  95  LYS D  99 -1  O  SER D  95   N  LYS D 112           
SHEET    1  DF-5 ASP D 193  VAL D 195  0                                        
SHEET    2  DF-5 GLU D 106  LYS D 112  1  O  GLY D 107   N  VAL D 194           
SHEET    1  DG-5 PHE D 209  GLN D 210  0                                        
SHEET    2  DG-5 TYR D 216  ILE D 217 -1  O  ILE D 217   N  PHE D 209           
SHEET    1  DH-5 GLY D 245  HIS D 247  0                                        
SHEET    2  DH-5 CYS D 253  PRO D 255 -1  O  ILE D 254   N  PHE D 246           
SHEET    1  DI 0 GLN D 336  ASP D 341  0                                        
SHEET    2  DI 0 THR D 346  TYR D 351 -1  O  CYS D 347   N  ILE D 339           
SHEET    3  DI 0 TRP D 356  THR D 359 -1  O  LEU D 358   N  ILE D 350           
SHEET    4  DI 0 ALA D 413  MET D 417 -1  O  ALA D 413   N  THR D 359           
SHEET    5  DI 0 ILE D 391  PHE D 399 -1  N  ASP D 395   O  GLU D 416           
SHEET    6  DI 0 TYR D 372  TRP D 375 -1  O  TYR D 372   N  VAL D 394           
SHEET    7  DI 0 GLN D 336  ASP D 341 -1  O  ALA D 338   N  TRP D 375           
SHEET    1  DJ 5 THR D 448  VAL D 451  0                                        
SHEET    2  DJ 5 GLU D 470  LEU D 473 -1  O  VAL D 471   N  CYS D 449           
SHEET    3  DJ 5 MET D 490  THR D 495  0                                        
SHEET    4  DJ 5 PRO D 510  MET D 514  0                                        
SHEET    5  DJ 5 THR D 520  TRP D 528  0                                        
SHEET    6  DJ 5 GLY D 539  LYS D 543  0                                        
SHEET    7  DJ 5 MET D 490  THR D 495 -1  O  GLU D 491   N  TYR D 541           
SSBOND   1 CYS A   15    CYS A  237                          1555   1555  2.03  
SSBOND   2 CYS A   25    CYS A   36                          1555   1555  2.03  
SSBOND   3 CYS A   30    CYS A   41                          1555   1555  2.04  
SSBOND   4 CYS A   43    CYS A   75                          1555   1555  2.03  
SSBOND   5 CYS A   49    CYS A   68                          1555   1555  2.04  
SSBOND   6 CYS A   57    CYS A   88                          1555   1555  2.03  
SSBOND   7 CYS A  123    CYS A  163                          1555   1555  2.03  
SSBOND   8 CYS A  136    CYS A  196                          1555   1555  2.04  
SSBOND   9 CYS A  168    CYS A  178                          1555   1555  2.03  
SSBOND  10 CYS A  211    CYS A  229                          1555   1555  2.03  
SSBOND  11 CYS A  223    CYS A  238                          1555   1555  2.03  
SSBOND  12 CYS A  241    CYS A  253                          1555   1555  2.04  
SSBOND  13 CYS A  248    CYS A  266                          1555   1555  2.04  
SSBOND  14 CYS A  260    CYS A  275                          1555   1555  2.03  
SSBOND  15 CYS A  309    CYS A  435                          1555   1555  2.03  
SSBOND  16 CYS A  347    CYS A  363                          1555   1555  2.04  
SSBOND  17 CYS A  355    CYS A  426                          1555   1555  2.03  
SSBOND  18 CYS A  449    CYS A  513                          1555   1555  2.03  
SSBOND  19 CYS A  477    CYS A  492                          1555   1555  2.03  
SSBOND  20 CYS B   15    CYS B  237                          1555   1555  2.04  
SSBOND  21 CYS B   25    CYS B   36                          1555   1555  2.03  
SSBOND  22 CYS B   30    CYS B   41                          1555   1555  2.04  
SSBOND  23 CYS B   43    CYS B   75                          1555   1555  2.03  
SSBOND  24 CYS B   49    CYS B   68                          1555   1555  2.04  
SSBOND  25 CYS B   57    CYS B   88                          1555   1555  2.04  
SSBOND  26 CYS B  123    CYS B  163                          1555   1555  2.04  
SSBOND  27 CYS B  136    CYS B  196                          1555   1555  2.03  
SSBOND  28 CYS B  168    CYS B  178                          1555   1555  2.03  
SSBOND  29 CYS B  211    CYS B  229                          1555   1555  2.03  
SSBOND  30 CYS B  223    CYS B  238                          1555   1555  2.03  
SSBOND  31 CYS B  241    CYS B  253                          1555   1555  2.03  
SSBOND  32 CYS B  248    CYS B  266                          1555   1555  2.04  
SSBOND  33 CYS B  260    CYS B  275                          1555   1555  2.03  
SSBOND  34 CYS B  309    CYS B  435                          1555   1555  2.04  
SSBOND  35 CYS B  347    CYS B  363                          1555   1555  2.03  
SSBOND  36 CYS B  355    CYS B  426                          1555   1555  2.03  
SSBOND  37 CYS B  449    CYS B  513                          1555   1555  2.03  
SSBOND  38 CYS B  477    CYS B  492                          1555   1555  2.03  
SSBOND  39 CYS C   15    CYS C  237                          1555   1555  2.04  
SSBOND  40 CYS C   25    CYS C   36                          1555   1555  2.03  
SSBOND  41 CYS C   30    CYS C   41                          1555   1555  2.04  
SSBOND  42 CYS C   43    CYS C   75                          1555   1555  2.03  
SSBOND  43 CYS C   49    CYS C   68                          1555   1555  2.05  
SSBOND  44 CYS C   57    CYS C   88                          1555   1555  2.04  
SSBOND  45 CYS C  123    CYS C  163                          1555   1555  2.04  
SSBOND  46 CYS C  136    CYS C  196                          1555   1555  2.04  
SSBOND  47 CYS C  168    CYS C  178                          1555   1555  2.04  
SSBOND  48 CYS C  211    CYS C  229                          1555   1555  2.03  
SSBOND  49 CYS C  223    CYS C  238                          1555   1555  2.03  
SSBOND  50 CYS C  241    CYS C  253                          1555   1555  2.04  
SSBOND  51 CYS C  248    CYS C  266                          1555   1555  2.04  
SSBOND  52 CYS C  260    CYS C  275                          1555   1555  2.04  
SSBOND  53 CYS C  309    CYS C  435                          1555   1555  2.03  
SSBOND  54 CYS C  347    CYS C  363                          1555   1555  2.04  
SSBOND  55 CYS C  355    CYS C  426                          1555   1555  2.02  
SSBOND  56 CYS C  449    CYS C  513                          1555   1555  2.03  
SSBOND  57 CYS C  477    CYS C  492                          1555   1555  2.03  
SSBOND  58 CYS D   15    CYS D  237                          1555   1555  2.03  
SSBOND  59 CYS D   25    CYS D   36                          1555   1555  2.03  
SSBOND  60 CYS D   30    CYS D   41                          1555   1555  2.04  
SSBOND  61 CYS D   43    CYS D   75                          1555   1555  2.04  
SSBOND  62 CYS D   49    CYS D   68                          1555   1555  2.04  
SSBOND  63 CYS D   57    CYS D   88                          1555   1555  2.03  
SSBOND  64 CYS D  123    CYS D  163                          1555   1555  2.03  
SSBOND  65 CYS D  136    CYS D  196                          1555   1555  2.04  
SSBOND  66 CYS D  168    CYS D  178                          1555   1555  2.03  
SSBOND  67 CYS D  211    CYS D  229                          1555   1555  2.03  
SSBOND  68 CYS D  223    CYS D  238                          1555   1555  2.03  
SSBOND  69 CYS D  241    CYS D  253                          1555   1555  2.04  
SSBOND  70 CYS D  248    CYS D  266                          1555   1555  2.04  
SSBOND  71 CYS D  260    CYS D  275                          1555   1555  2.04  
SSBOND  72 CYS D  309    CYS D  435                          1555   1555  2.03  
SSBOND  73 CYS D  347    CYS D  363                          1555   1555  2.03  
SSBOND  74 CYS D  355    CYS D  426                          1555   1555  2.03  
SSBOND  75 CYS D  449    CYS D  513                          1555   1555  2.04  
SSBOND  76 CYS D  477    CYS D  492                          1555   1555  2.03  
SSBOND  77 CYS D  503    CYS D  532                          1555   1555  2.03  
LINK         ND2 ASN A  52                 C1  NAG A 652     1555   1555  1.44  
LINK         ND2 ASN A  85                 C1  NAG A 685     1555   1555  1.45  
LINK         ND2 ASN A 159                 C1  NAG A 659     1555   1555  1.44  
LINK         ND2 ASN A 446                 C1  NAG A 646     1555   1555  1.45  
LINK         ND2 ASN A 476                 C1  NAG A 676     1555   1555  1.45  
LINK         ND2 ASN A 518                 C1  NAG A 618     1555   1555  1.44  
LINK         ND2 ASN B  52                 C1  NAG B 652     1555   1555  1.44  
LINK         ND2 ASN B  85                 C1  NAG B 685     1555   1555  1.45  
LINK         ND2 ASN B 159                 C1  NAG B 659     1555   1555  1.45  
LINK         ND2 ASN B 446                 C1  NAG B 646     1555   1555  1.45  
LINK         ND2 ASN B 476                 C1  NAG B 676     1555   1555  1.44  
LINK         ND2 ASN B 518                 C1  NAG B 618     1555   1555  1.44  
LINK         ND2 ASN C  52                 C1  NAG C 652     1555   1555  1.45  
LINK         ND2 ASN C  85                 C1  NAG C 685     1555   1555  1.45  
LINK         ND2 ASN C 446                 C1  NAG C 646     1555   1555  1.45  
LINK         ND2 ASN C 476                 C1  NAG C 676     1555   1555  1.44  
LINK         ND2 ASN C 518                 C1  NAG C 618     1555   1555  1.45  
LINK         ND2 ASN D  52                 C1  NAG D 652     1555   1555  1.44  
LINK         ND2 ASN D  85                 C1  NAG D 685     1555   1555  1.45  
LINK         ND2 ASN D 446                 C1  NAG D 646     1555   1555  1.45  
LINK         ND2 ASN D 476                 C1  NAG D 676     1555   1555  1.45  
LINK         ND2 ASN D 518                 C1  NAG D 618     1555   1555  1.45  
LINK         O   LYS A 221                CA    CA A 601     1555   1555  2.31  
LINK         OD1 ASP A 224                CA    CA A 601     1555   1555  2.45  
LINK         O   ILE A 226                CA    CA A 601     1555   1555  2.45  
LINK         OD2 ASP A 228                CA    CA A 601     1555   1555  2.56  
LINK         OD1 ASP A 234                CA    CA A 601     1555   1555  2.43  
LINK         OE2 GLU A 235                CA    CA A 601     1555   1555  2.34  
LINK         O   TYR A 258                CA    CA A 600     1555   1555  2.14  
LINK         OD1 ASN A 261                CA    CA A 600     1555   1555  2.30  
LINK         O   GLU A 263                CA    CA A 600     1555   1555  2.35  
LINK         OD2 ASP A 265                CA    CA A 600     1555   1555  2.12  
LINK         OD2 ASP A 271                CA    CA A 600     1555   1555  2.48  
LINK         OE1 GLU A 272                CA    CA A 600     1555   1555  2.65  
LINK         O   LYS B 221                CA    CA B 601     1555   1555  2.83  
LINK         OD1 ASP B 224                CA    CA B 601     1555   1555  2.36  
LINK         O   ILE B 226                CA    CA B 601     1555   1555  2.31  
LINK         OD2 ASP B 228                CA    CA B 601     1555   1555  2.18  
LINK         OD1 ASP B 234                CA    CA B 601     1555   1555  2.39  
LINK         OE2 GLU B 235                CA    CA B 601     1555   1555  2.14  
LINK         O   TYR B 258                CA    CA B 600     1555   1555  2.23  
LINK         OD1 ASN B 261                CA    CA B 600     1555   1555  2.60  
LINK         O   GLU B 263                CA    CA B 600     1555   1555  2.46  
LINK         OD2 ASP B 271                CA    CA B 600     1555   1555  2.38  
LINK         OE1 GLU B 272                CA    CA B 600     1555   1555  2.50  
LINK         O   LYS C 221                CA    CA C 601     1555   1555  2.33  
LINK         OD1 ASP C 224                CA    CA C 601     1555   1555  2.31  
LINK         O   ILE C 226                CA    CA C 601     1555   1555  2.34  
LINK         OD2 ASP C 228                CA    CA C 601     1555   1555  2.34  
LINK         OD1 ASP C 234                CA    CA C 601     1555   1555  2.32  
LINK         OE2 GLU C 235                CA    CA C 601     1555   1555  2.60  
LINK         O   TYR C 258                CA    CA C 600     1555   1555  2.36  
LINK         OD1 ASN C 261                CA    CA C 600     1555   1555  2.36  
LINK         O   GLU C 263                CA    CA C 600     1555   1555  2.13  
LINK         OD2 ASP C 265                CA    CA C 600     1555   1555  2.57  
LINK         OD2 ASP C 271                CA    CA C 600     1555   1555  2.52  
LINK         OE1 GLU C 272                CA    CA C 600     1555   1555  2.80  
LINK         O   LYS D 221                CA    CA D 601     1555   1555  2.56  
LINK         OD1 ASP D 224                CA    CA D 601     1555   1555  2.58  
LINK         O   ILE D 226                CA    CA D 601     1555   1555  2.44  
LINK         OD2 ASP D 228                CA    CA D 601     1555   1555  2.36  
LINK         OD1 ASP D 234                CA    CA D 601     1555   1555  2.34  
LINK         OE2 GLU D 235                CA    CA D 601     1555   1555  2.53  
LINK         O   TYR D 258                CA    CA D 600     1555   1555  2.33  
LINK         OD1 ASN D 261                CA    CA D 600     1555   1555  2.43  
LINK         O   GLU D 263                CA    CA D 600     1555   1555  2.28  
LINK         OD2 ASP D 265                CA    CA D 600     1555   1555  2.84  
LINK         OD2 ASP D 271                CA    CA D 600     1555   1555  2.40  
LINK         OE1 GLU D 272                CA    CA D 600     1555   1555  2.55  
CISPEP   1 GLY A  187    TYR A  188          0         2.35                     
CISPEP   2 TYR A  188    GLN A  189          0        -1.72                     
CISPEP   3 MET B  186    GLY B  187          0         4.55                     
CISPEP   4 GLY B  325    LYS B  326          0        -0.83                     
CISPEP   5 GLY B  331    ASP B  332          0        -3.40                     
CISPEP   6 CYS B  532    GLY B  533          0        -1.06                     
CISPEP   7 PRO B  535    GLU B  536          0         2.84                     
CISPEP   8 VAL B  555    GLY B  556          0        -4.32                     
CISPEP   9 SER B  561    GLN B  562          0        27.86                     
CISPEP  10 ASN B  564    VAL B  565          0         6.40                     
CISPEP  11 PRO C  429    ARG C  430          0        -1.96                     
CISPEP  12 ARG C  430    SER C  431          0        22.12                     
CISPEP  13 ASP D  497    GLY D  498          0        -4.14                     
CRYST1   71.317  234.721   40.300  89.98  90.18  90.03 P 1           4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.014022  0.000007  0.000044        0.00000                         
SCALE2      0.000000  0.004260  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.024814        0.00000                         
MTRIX1   1 -0.999323  0.011615 -0.034902      104.70230    1                    
MTRIX2   1 -0.011806 -0.999916  0.005260      211.24460    1                    
MTRIX3   1 -0.034838  0.005669  0.999377        6.73820    1                    
MTRIX1   2  0.999688 -0.009196  0.023227      -34.10960    1                    
MTRIX2   2 -0.009214 -0.999957  0.000657       93.71870    1                    
MTRIX3   2  0.023220 -0.000871 -0.999730       -6.74570    1                    
MTRIX1   3 -0.999998  0.000797  0.002081       70.56010    1                    
MTRIX2   3  0.000797  1.000000 -0.000346     -117.31520    1                    
MTRIX3   3 -0.002081 -0.000344 -0.999998        0.11910    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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