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Database: PDB
Entry: 5Y31
LinkDB: 5Y31
Original site: 5Y31 
HEADER    CELL ADHESION                           27-JUL-17   5Y31              
TITLE     CRYSTAL STRUCTURE OF HUMAN LGI1-ADAM22 COMPLEX                        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: DISINTEGRIN AND METALLOPROTEINASE DOMAIN-CONTAINING PROTEIN
COMPND   3 22;                                                                  
COMPND   4 CHAIN: A, C;                                                         
COMPND   5 FRAGMENT: UNP RESIDUES 233-729;                                      
COMPND   6 SYNONYM: ADAM 22,METALLOPROTEINASE-DISINTEGRIN ADAM22-3,             
COMPND   7 METALLOPROTEINASE-LIKE,DISINTEGRIN-LIKE,AND CYSTEINE-RICH PROTEIN 2; 
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MOL_ID: 2;                                                           
COMPND  10 MOLECULE: LEUCINE-RICH GLIOMA-INACTIVATED PROTEIN 1;                 
COMPND  11 CHAIN: B, D;                                                         
COMPND  12 FRAGMENT: UNP RESIDUES 37-557;                                       
COMPND  13 SYNONYM: EPITEMPIN-1;                                                
COMPND  14 ENGINEERED: YES;                                                     
COMPND  15 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: ADAM22, MDC2;                                                  
SOURCE   6 EXPRESSION_SYSTEM: MAMMALIA;                                         
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 40674;                                      
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  10 ORGANISM_COMMON: HUMAN;                                              
SOURCE  11 ORGANISM_TAXID: 9606;                                                
SOURCE  12 GENE: LGI1, EPT, UNQ775/PRO1569;                                     
SOURCE  13 EXPRESSION_SYSTEM: MAMMALIA;                                         
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 40674                                       
KEYWDS    EPILEPSY, SYNAPSE, ADAM, EPTP, WD40, CELL ADHESION                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.YAMAGATA,S.FUKAI                                                    
REVDAT   2   07-NOV-18 5Y31    1       TITLE                                    
REVDAT   1   02-MAY-18 5Y31    0                                                
JRNL        AUTH   A.YAMAGATA,Y.MIYAZAKI,N.YOKOI,H.SHIGEMATSU,Y.SATO,           
JRNL        AUTH 2 S.GOTO-ITO,A.MAEDA,T.GOTO,M.SANBO,M.HIRABAYASHI,M.SHIROUZU,  
JRNL        AUTH 3 Y.FUKATA,M.FUKATA,S.FUKAI                                    
JRNL        TITL   STRUCTURAL BASIS OF EPILEPSY-RELATED LIGAND-RECEPTOR COMPLEX 
JRNL        TITL 2 LGI1-ADAM22.                                                 
JRNL        REF    NAT COMMUN                    V.   9  1546 2018              
JRNL        REFN                   ESSN 2041-1723                               
JRNL        PMID   29670100                                                     
JRNL        DOI    10.1038/S41467-018-03947-W                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    7.13 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.9_1692                                      
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 7.13                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 48.99                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.450                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 6086                           
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.268                           
REMARK   3   R VALUE            (WORKING SET) : 0.265                           
REMARK   3   FREE R VALUE                     : 0.316                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.880                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 297                             
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 48.9938 -  8.9684    0.99     2960   155  0.2469 0.2878        
REMARK   3     2  8.9684 -  7.1255    0.96     2829   142  0.3160 0.4046        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 1.370            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 37.830           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.004          16279                                  
REMARK   3   ANGLE     :  0.819          21878                                  
REMARK   3   CHIRALITY :  0.037           2424                                  
REMARK   3   PLANARITY :  0.003           2810                                  
REMARK   3   DIHEDRAL  : 12.531           5914                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: ALL                                                    
REMARK   3    ORIGIN FOR THE GROUP (A):   2.1416  -1.1870  51.1431              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   4.4121 T22:   3.7659                                     
REMARK   3      T33:   4.3694 T12:   0.0583                                     
REMARK   3      T13:  -0.0416 T23:  -0.1017                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7573 L22:   0.3956                                     
REMARK   3      L33:  -0.0244 L12:   0.0663                                     
REMARK   3      L13:  -0.4651 L23:  -0.0649                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0920 S12:   0.4117 S13:   0.1372                       
REMARK   3      S21:   0.0921 S22:  -0.2018 S23:  -0.0261                       
REMARK   3      S31:   0.4914 S32:   0.1550 S33:   0.0103                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5Y31 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 02-AUG-17.                  
REMARK 100 THE DEPOSITION ID IS D_1300004589.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-APR-16                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SPRING-8                           
REMARK 200  BEAMLINE                       : BL41XU                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0000                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS3 6M                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 6092                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : 7.120                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.9                               
REMARK 200  DATA REDUNDANCY                : 7.100                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 13.3000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 7.12                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 7.24                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.60                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.46100                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.600                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 71.99                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.39                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 10 % PEG 8000, 0.1 M ZINC ACETATE, 0.1   
REMARK 280  M MES-NA (PH 6.0), VAPOR DIFFUSION, SITTING DROP, TEMPERATURE       
REMARK 280  293K                                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       62.16200            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     VAL A   626                                                      
REMARK 465     VAL A   627                                                      
REMARK 465     GLN A   628                                                      
REMARK 465     GLN A   629                                                      
REMARK 465     ASP A   719                                                      
REMARK 465     ASP A   720                                                      
REMARK 465     ALA A   721                                                      
REMARK 465     LYS A   722                                                      
REMARK 465     THR A   723                                                      
REMARK 465     GLY A   724                                                      
REMARK 465     ILE A   725                                                      
REMARK 465     THR A   726                                                      
REMARK 465     LEU A   727                                                      
REMARK 465     SER A   728                                                      
REMARK 465     GLY A   729                                                      
REMARK 465     ASP B    21                                                      
REMARK 465     ALA B    22                                                      
REMARK 465     ALA B    23                                                      
REMARK 465     GLN B    24                                                      
REMARK 465     PRO B    25                                                      
REMARK 465     ALA B    26                                                      
REMARK 465     ARG B    27                                                      
REMARK 465     ARG B    28                                                      
REMARK 465     ALA B    29                                                      
REMARK 465     ARG B    30                                                      
REMARK 465     ARG B    31                                                      
REMARK 465     THR B    32                                                      
REMARK 465     TYR B    33                                                      
REMARK 465     GLU B    34                                                      
REMARK 465     ALA B    35                                                      
REMARK 465     TYR B    36                                                      
REMARK 465     PRO B    37                                                      
REMARK 465     ALA B    38                                                      
REMARK 465     LYS B    39                                                      
REMARK 465     PRO B    40                                                      
REMARK 465     ILE B   552                                                      
REMARK 465     VAL B   553                                                      
REMARK 465     ASP B   554                                                      
REMARK 465     LEU B   555                                                      
REMARK 465     SER B   556                                                      
REMARK 465     ALA B   557                                                      
REMARK 465     LYS B   558                                                      
REMARK 465     HIS B   559                                                      
REMARK 465     HIS B   560                                                      
REMARK 465     HIS B   561                                                      
REMARK 465     HIS B   562                                                      
REMARK 465     HIS B   563                                                      
REMARK 465     HIS B   564                                                      
REMARK 465     VAL C   626                                                      
REMARK 465     VAL C   627                                                      
REMARK 465     GLN C   628                                                      
REMARK 465     GLN C   629                                                      
REMARK 465     ASP C   719                                                      
REMARK 465     ASP C   720                                                      
REMARK 465     ALA C   721                                                      
REMARK 465     LYS C   722                                                      
REMARK 465     THR C   723                                                      
REMARK 465     GLY C   724                                                      
REMARK 465     ILE C   725                                                      
REMARK 465     THR C   726                                                      
REMARK 465     LEU C   727                                                      
REMARK 465     SER C   728                                                      
REMARK 465     GLY C   729                                                      
REMARK 465     ASP D    21                                                      
REMARK 465     ALA D    22                                                      
REMARK 465     ALA D    23                                                      
REMARK 465     GLN D    24                                                      
REMARK 465     PRO D    25                                                      
REMARK 465     ALA D    26                                                      
REMARK 465     ARG D    27                                                      
REMARK 465     ARG D    28                                                      
REMARK 465     ALA D    29                                                      
REMARK 465     ARG D    30                                                      
REMARK 465     ARG D    31                                                      
REMARK 465     THR D    32                                                      
REMARK 465     TYR D    33                                                      
REMARK 465     GLU D    34                                                      
REMARK 465     ALA D    35                                                      
REMARK 465     TYR D    36                                                      
REMARK 465     PRO D    37                                                      
REMARK 465     ALA D    38                                                      
REMARK 465     LYS D    39                                                      
REMARK 465     PRO D    40                                                      
REMARK 465     ILE D   552                                                      
REMARK 465     VAL D   553                                                      
REMARK 465     ASP D   554                                                      
REMARK 465     LEU D   555                                                      
REMARK 465     SER D   556                                                      
REMARK 465     ALA D   557                                                      
REMARK 465     LYS D   558                                                      
REMARK 465     HIS D   559                                                      
REMARK 465     HIS D   560                                                      
REMARK 465     HIS D   561                                                      
REMARK 465     HIS D   562                                                      
REMARK 465     HIS D   563                                                      
REMARK 465     HIS D   564                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OH   TYR B   206     O    ASP B   218              1.86            
REMARK 500   ND2  ASN C   675     O5   NAG C   805              1.99            
REMARK 500   OE2  GLU A   359     NH1  ARG B   378              2.07            
REMARK 500   ND2  ASN C   519     O5   NAG C   804              2.13            
REMARK 500   ND2  ASN A   449     OE1  GLU A   453              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   OD1  ASP B   266     NH1  ARG D   273     1655     2.04            
REMARK 500   NH1  ARG A   704     OD2  ASP C   588     1656     2.14            
REMARK 500   NE   ARG B   209     OE1  GLU C   684     2555     2.14            
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    GLU A 336       37.53    -98.20                                   
REMARK 500    SER A 382       99.48    -68.88                                   
REMARK 500    ASP A 383      104.06    -59.01                                   
REMARK 500    TRP A 398      -62.57    -97.03                                   
REMARK 500    SER A 439      -76.07   -110.80                                   
REMARK 500    ASP A 459       99.78   -163.58                                   
REMARK 500    ASP A 482       66.62   -111.81                                   
REMARK 500    LYS A 587       71.48     52.33                                   
REMARK 500    ASP A 597       33.69    -86.93                                   
REMARK 500    LEU B 114       69.33   -119.89                                   
REMARK 500    LEU B 138       58.65    -94.56                                   
REMARK 500    ASP B 178     -165.32   -127.41                                   
REMARK 500    ILE B 223      155.75    170.24                                   
REMARK 500    PRO B 233       49.27    -69.12                                   
REMARK 500    LEU B 237      -65.50   -108.00                                   
REMARK 500    ASN B 333      -17.40   -140.04                                   
REMARK 500    ASN B 342       15.83     58.11                                   
REMARK 500    ASN B 428       -5.91     79.54                                   
REMARK 500    SER B 497     -166.25   -128.99                                   
REMARK 500    PHE B 514      -75.91   -125.77                                   
REMARK 500    GLU C 336       37.79    -96.07                                   
REMARK 500    CYS C 349       -0.32     71.87                                   
REMARK 500    SER C 382       99.98    -69.45                                   
REMARK 500    ASP C 383      104.42    -59.20                                   
REMARK 500    TRP C 398      -61.72    -96.06                                   
REMARK 500    SER C 439      -76.23   -110.71                                   
REMARK 500    ASP C 459      100.07   -163.27                                   
REMARK 500    ASP C 482       66.49   -112.04                                   
REMARK 500    LYS C 587       71.81     51.35                                   
REMARK 500    ASP C 597       33.77    -86.65                                   
REMARK 500    LEU D 138       59.25    -94.41                                   
REMARK 500    ASP D 178     -165.08   -127.12                                   
REMARK 500    ASP D 220      -70.88    -55.23                                   
REMARK 500    ILE D 223      -95.56    -95.23                                   
REMARK 500    PRO D 233       49.43    -69.03                                   
REMARK 500    LEU D 237      -65.65   -108.97                                   
REMARK 500    ASN D 333      -17.16   -140.00                                   
REMARK 500    ASN D 342       15.98     58.29                                   
REMARK 500    ASN D 428       -5.67     79.86                                   
REMARK 500    SER D 497     -165.78   -128.81                                   
REMARK 500    PHE D 514      -75.49   -125.95                                   
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 ILE B  222     ILE B  223                 -143.90                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 801  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 242   OE2                                                    
REMARK 620 2 ASP A 325   OD1  88.1                                              
REMARK 620 3 ASP A 325   OD2 106.2  55.3                                        
REMARK 620 4 CYS A 433   O   147.0  71.7  83.9                                  
REMARK 620 5 ASN A 436   OD1 112.3 119.9 141.2  61.0                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 802  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 446   O                                                      
REMARK 620 2 ASN A 449   OD1  71.3                                              
REMARK 620 3 PHE A 451   O   146.0  74.8                                        
REMARK 620 4 GLU A 453   OE1  88.8 111.8 101.8                                  
REMARK 620 5 GLU A 456   OE1 144.3 117.2  57.5 115.8                            
REMARK 620 6 GLU A 456   OE2  97.1 143.1 111.5 102.6  54.2                      
REMARK 620 7 ASP A 459   OD2  82.7  55.4  80.0 166.4  76.8  89.0                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 803  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 511   OD1                                                    
REMARK 620 2 ASP A 511   OD2  55.1                                              
REMARK 620 3 ILE A 512   O   104.5  96.9                                        
REMARK 620 4 GLU A 514   OE2 144.0 160.1  74.5                                  
REMARK 620 5 ASN A 526   OD1  97.7 105.5 154.9  80.6                            
REMARK 620 6 ILE A 527   O    73.0 127.5  88.2  71.0  87.0                      
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 ASP B 334   OD1                                                    
REMARK 620 2 ASP B 334   OD2  55.2                                              
REMARK 620 3 GLU B 336   OE1  87.0  80.3                                        
REMARK 620 4 ASP B 381   OD1  82.4  93.1 169.3                                  
REMARK 620 5 ASP B 381   OD2 131.6 100.8 134.0  55.2                            
REMARK 620 6 VAL B 382   O   132.0  79.1  70.5 116.6  64.8                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA C 801  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU C 242   OE2                                                    
REMARK 620 2 ASP C 325   OD1  89.1                                              
REMARK 620 3 ASP C 325   OD2 106.9  54.9                                        
REMARK 620 4 CYS C 433   O   148.3  72.3  83.4                                  
REMARK 620 5 ASN C 436   OD1 111.8 119.5 140.9  60.6                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA C 802  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU C 446   O                                                      
REMARK 620 2 ASN C 449   OD1  71.3                                              
REMARK 620 3 PHE C 451   O   147.1  76.0                                        
REMARK 620 4 GLU C 453   OE1  89.3 112.4 100.2                                  
REMARK 620 5 GLU C 456   OE1 144.7 119.3  58.3 113.2                            
REMARK 620 6 GLU C 456   OE2  96.7 144.2 112.0 100.7  54.0                      
REMARK 620 7 ASP C 459   OD2  84.4  55.1  79.7 167.2  77.8  91.0                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA C 803  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP C 511   OD1                                                    
REMARK 620 2 ASP C 511   OD2  55.1                                              
REMARK 620 3 ILE C 512   O   103.7  96.1                                        
REMARK 620 4 GLU C 514   OE2 143.9 159.8  74.4                                  
REMARK 620 5 ASN C 526   OD1  99.3 106.5 154.3  80.3                            
REMARK 620 6 ILE C 527   O    74.3 128.7  87.0  69.6  88.3                      
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 ASP D 334   OD1                                                    
REMARK 620 2 ASP D 334   OD2  55.4                                              
REMARK 620 3 GLU D 336   OE1  88.2  79.7                                        
REMARK 620 4 ASP D 381   OD1  81.5  92.3 169.4                                  
REMARK 620 5 ASP D 381   OD2 130.4  99.1 132.4  55.5                            
REMARK 620 6 VAL D 382   O   131.1  78.0  68.2 117.2  65.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 801                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 802                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 803                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA B 601                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA C 801                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA C 802                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA C 803                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA D 601                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 804 bound   
REMARK 800  to ASN A 519                                                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 805 bound   
REMARK 800  to ASN A 675                                                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 602 bound   
REMARK 800  to ASN B 192                                                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 603 bound   
REMARK 800  to ASN B 277                                                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 604 bound   
REMARK 800  to ASN B 422                                                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG C 804 bound   
REMARK 800  to ASN C 519                                                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG C 805 bound   
REMARK 800  to ASN C 675                                                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG D 602 bound   
REMARK 800  to ASN D 192                                                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues LYS D    
REMARK 800  259 through NAG D 603 bound to ASN D 277                            
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG D 604 bound   
REMARK 800  to ASN D 422                                                        
DBREF  5Y31 A  233   729  UNP    Q9P0K1   ADA22_HUMAN    233    729             
DBREF  5Y31 B   37   557  UNP    O95970   LGI1_HUMAN      37    557             
DBREF  5Y31 C  233   729  UNP    Q9P0K1   ADA22_HUMAN    233    729             
DBREF  5Y31 D   37   557  UNP    O95970   LGI1_HUMAN      37    557             
SEQADV 5Y31 ASP B   21  UNP  O95970              EXPRESSION TAG                 
SEQADV 5Y31 ALA B   22  UNP  O95970              EXPRESSION TAG                 
SEQADV 5Y31 ALA B   23  UNP  O95970              EXPRESSION TAG                 
SEQADV 5Y31 GLN B   24  UNP  O95970              EXPRESSION TAG                 
SEQADV 5Y31 PRO B   25  UNP  O95970              EXPRESSION TAG                 
SEQADV 5Y31 ALA B   26  UNP  O95970              EXPRESSION TAG                 
SEQADV 5Y31 ARG B   27  UNP  O95970              EXPRESSION TAG                 
SEQADV 5Y31 ARG B   28  UNP  O95970              EXPRESSION TAG                 
SEQADV 5Y31 ALA B   29  UNP  O95970              EXPRESSION TAG                 
SEQADV 5Y31 ARG B   30  UNP  O95970              EXPRESSION TAG                 
SEQADV 5Y31 ARG B   31  UNP  O95970              EXPRESSION TAG                 
SEQADV 5Y31 THR B   32  UNP  O95970              EXPRESSION TAG                 
SEQADV 5Y31 TYR B   33  UNP  O95970              EXPRESSION TAG                 
SEQADV 5Y31 GLU B   34  UNP  O95970              EXPRESSION TAG                 
SEQADV 5Y31 ALA B   35  UNP  O95970              EXPRESSION TAG                 
SEQADV 5Y31 TYR B   36  UNP  O95970              EXPRESSION TAG                 
SEQADV 5Y31 ALA B  470  UNP  O95970    ARG   470 ENGINEERED MUTATION            
SEQADV 5Y31 LYS B  558  UNP  O95970              EXPRESSION TAG                 
SEQADV 5Y31 HIS B  559  UNP  O95970              EXPRESSION TAG                 
SEQADV 5Y31 HIS B  560  UNP  O95970              EXPRESSION TAG                 
SEQADV 5Y31 HIS B  561  UNP  O95970              EXPRESSION TAG                 
SEQADV 5Y31 HIS B  562  UNP  O95970              EXPRESSION TAG                 
SEQADV 5Y31 HIS B  563  UNP  O95970              EXPRESSION TAG                 
SEQADV 5Y31 HIS B  564  UNP  O95970              EXPRESSION TAG                 
SEQADV 5Y31 ASP D   21  UNP  O95970              EXPRESSION TAG                 
SEQADV 5Y31 ALA D   22  UNP  O95970              EXPRESSION TAG                 
SEQADV 5Y31 ALA D   23  UNP  O95970              EXPRESSION TAG                 
SEQADV 5Y31 GLN D   24  UNP  O95970              EXPRESSION TAG                 
SEQADV 5Y31 PRO D   25  UNP  O95970              EXPRESSION TAG                 
SEQADV 5Y31 ALA D   26  UNP  O95970              EXPRESSION TAG                 
SEQADV 5Y31 ARG D   27  UNP  O95970              EXPRESSION TAG                 
SEQADV 5Y31 ARG D   28  UNP  O95970              EXPRESSION TAG                 
SEQADV 5Y31 ALA D   29  UNP  O95970              EXPRESSION TAG                 
SEQADV 5Y31 ARG D   30  UNP  O95970              EXPRESSION TAG                 
SEQADV 5Y31 ARG D   31  UNP  O95970              EXPRESSION TAG                 
SEQADV 5Y31 THR D   32  UNP  O95970              EXPRESSION TAG                 
SEQADV 5Y31 TYR D   33  UNP  O95970              EXPRESSION TAG                 
SEQADV 5Y31 GLU D   34  UNP  O95970              EXPRESSION TAG                 
SEQADV 5Y31 ALA D   35  UNP  O95970              EXPRESSION TAG                 
SEQADV 5Y31 TYR D   36  UNP  O95970              EXPRESSION TAG                 
SEQADV 5Y31 ALA D  470  UNP  O95970    ARG   470 ENGINEERED MUTATION            
SEQADV 5Y31 LYS D  558  UNP  O95970              EXPRESSION TAG                 
SEQADV 5Y31 HIS D  559  UNP  O95970              EXPRESSION TAG                 
SEQADV 5Y31 HIS D  560  UNP  O95970              EXPRESSION TAG                 
SEQADV 5Y31 HIS D  561  UNP  O95970              EXPRESSION TAG                 
SEQADV 5Y31 HIS D  562  UNP  O95970              EXPRESSION TAG                 
SEQADV 5Y31 HIS D  563  UNP  O95970              EXPRESSION TAG                 
SEQADV 5Y31 HIS D  564  UNP  O95970              EXPRESSION TAG                 
SEQRES   1 A  497  ASN VAL GLU GLU GLU THR LYS TYR ILE GLU LEU MET ILE          
SEQRES   2 A  497  VAL ASN ASP HIS LEU MET PHE LYS LYS HIS ARG LEU SER          
SEQRES   3 A  497  VAL VAL HIS THR ASN THR TYR ALA LYS SER VAL VAL ASN          
SEQRES   4 A  497  MET ALA ASP LEU ILE TYR LYS ASP GLN LEU LYS THR ARG          
SEQRES   5 A  497  ILE VAL LEU VAL ALA MET GLU THR TRP ALA THR ASP ASN          
SEQRES   6 A  497  LYS PHE ALA ILE SER GLU ASN PRO LEU ILE THR LEU ARG          
SEQRES   7 A  497  GLU PHE MET LYS TYR ARG ARG ASP PHE ILE LYS GLU LYS          
SEQRES   8 A  497  SER ASP ALA VAL HIS LEU PHE SER GLY SER GLN PHE GLU          
SEQRES   9 A  497  SER SER ARG SER GLY ALA ALA TYR ILE GLY GLY ILE CYS          
SEQRES  10 A  497  SER LEU LEU LYS GLY GLY GLY VAL ASN GLU PHE GLY LYS          
SEQRES  11 A  497  THR ASP LEU MET ALA VAL THR LEU ALA GLN SER LEU ALA          
SEQRES  12 A  497  HIS ASN ILE GLY ILE ILE SER ASP LYS ARG LYS LEU ALA          
SEQRES  13 A  497  SER GLY GLU CYS LYS CYS GLU ASP THR TRP SER GLY CYS          
SEQRES  14 A  497  ILE MET GLY ASP THR GLY TYR TYR LEU PRO LYS LYS PHE          
SEQRES  15 A  497  THR GLN CYS ASN ILE GLU GLU TYR HIS ASP PHE LEU ASN          
SEQRES  16 A  497  SER GLY GLY GLY ALA CYS LEU PHE ASN LYS PRO SER LYS          
SEQRES  17 A  497  LEU LEU ASP PRO PRO GLU CYS GLY ASN GLY PHE ILE GLU          
SEQRES  18 A  497  THR GLY GLU GLU CYS ASP CYS GLY THR PRO ALA GLU CYS          
SEQRES  19 A  497  VAL LEU GLU GLY ALA GLU CYS CYS LYS LYS CYS THR LEU          
SEQRES  20 A  497  THR GLN ASP SER GLN CYS SER ASP GLY LEU CYS CYS LYS          
SEQRES  21 A  497  LYS CYS LYS PHE GLN PRO MET GLY THR VAL CYS ARG GLU          
SEQRES  22 A  497  ALA VAL ASN ASP CYS ASP ILE ARG GLU THR CYS SER GLY          
SEQRES  23 A  497  ASN SER SER GLN CYS ALA PRO ASN ILE HIS LYS MET ASP          
SEQRES  24 A  497  GLY TYR SER CYS ASP GLY VAL GLN GLY ILE CYS PHE GLY          
SEQRES  25 A  497  GLY ARG CYS LYS THR ARG ASP ARG GLN CYS LYS TYR ILE          
SEQRES  26 A  497  TRP GLY GLN LYS VAL THR ALA SER ASP LYS TYR CYS TYR          
SEQRES  27 A  497  GLU LYS LEU ASN ILE GLU GLY THR GLU LYS GLY ASN CYS          
SEQRES  28 A  497  GLY LYS ASP LYS ASP THR TRP ILE GLN CYS ASN LYS ARG          
SEQRES  29 A  497  ASP VAL LEU CYS GLY TYR LEU LEU CYS THR ASN ILE GLY          
SEQRES  30 A  497  ASN ILE PRO ARG LEU GLY GLU LEU ASP GLY GLU ILE THR          
SEQRES  31 A  497  SER THR LEU VAL VAL GLN GLN GLY ARG THR LEU ASN CYS          
SEQRES  32 A  497  SER GLY GLY HIS VAL LYS LEU GLU GLU ASP VAL ASP LEU          
SEQRES  33 A  497  GLY TYR VAL GLU ASP GLY THR PRO CYS GLY PRO GLN MET          
SEQRES  34 A  497  MET CYS LEU GLU HIS ARG CYS LEU PRO VAL ALA SER PHE          
SEQRES  35 A  497  ASN PHE SER THR CYS LEU SER SER LYS GLU GLY THR ILE          
SEQRES  36 A  497  CYS SER GLY ASN GLY VAL CYS SER ASN GLU LEU LYS CYS          
SEQRES  37 A  497  VAL CYS ASN ARG HIS TRP ILE GLY SER ASP CYS ASN THR          
SEQRES  38 A  497  TYR PHE PRO HIS ASN ASP ASP ALA LYS THR GLY ILE THR          
SEQRES  39 A  497  LEU SER GLY                                                  
SEQRES   1 B  544  ASP ALA ALA GLN PRO ALA ARG ARG ALA ARG ARG THR TYR          
SEQRES   2 B  544  GLU ALA TYR PRO ALA LYS PRO LYS CYS PRO ALA VAL CYS          
SEQRES   3 B  544  THR CYS THR LYS ASP ASN ALA LEU CYS GLU ASN ALA ARG          
SEQRES   4 B  544  SER ILE PRO ARG THR VAL PRO PRO ASP VAL ILE SER LEU          
SEQRES   5 B  544  SER PHE VAL ARG SER GLY PHE THR GLU ILE SER GLU GLY          
SEQRES   6 B  544  SER PHE LEU PHE THR PRO SER LEU GLN LEU LEU LEU PHE          
SEQRES   7 B  544  THR SER ASN SER PHE ASP VAL ILE SER ASP ASP ALA PHE          
SEQRES   8 B  544  ILE GLY LEU PRO HIS LEU GLU TYR LEU PHE ILE GLU ASN          
SEQRES   9 B  544  ASN ASN ILE LYS SER ILE SER ARG HIS THR PHE ARG GLY          
SEQRES  10 B  544  LEU LYS SER LEU ILE HIS LEU SER LEU ALA ASN ASN ASN          
SEQRES  11 B  544  LEU GLN THR LEU PRO LYS ASP ILE PHE LYS GLY LEU ASP          
SEQRES  12 B  544  SER LEU THR ASN VAL ASP LEU ARG GLY ASN SER PHE ASN          
SEQRES  13 B  544  CYS ASP CYS LYS LEU LYS TRP LEU VAL GLU TRP LEU GLY          
SEQRES  14 B  544  HIS THR ASN ALA THR VAL GLU ASP ILE TYR CYS GLU GLY          
SEQRES  15 B  544  PRO PRO GLU TYR LYS LYS ARG LYS ILE ASN SER LEU SER          
SEQRES  16 B  544  SER LYS ASP PHE ASP CYS ILE ILE THR GLU PHE ALA LYS          
SEQRES  17 B  544  SER GLN ASP LEU PRO TYR GLN SER LEU SER ILE ASP THR          
SEQRES  18 B  544  PHE SER TYR LEU ASN ASP GLU TYR VAL VAL ILE ALA GLN          
SEQRES  19 B  544  PRO PHE THR GLY LYS CYS ILE PHE LEU GLU TRP ASP HIS          
SEQRES  20 B  544  VAL GLU LYS THR PHE ARG ASN TYR ASP ASN ILE THR GLY          
SEQRES  21 B  544  THR SER THR VAL VAL CYS LYS PRO ILE VAL ILE GLU THR          
SEQRES  22 B  544  GLN LEU TYR VAL ILE VAL ALA GLN LEU PHE GLY GLY SER          
SEQRES  23 B  544  HIS ILE TYR LYS ARG ASP SER PHE ALA ASN LYS PHE ILE          
SEQRES  24 B  544  LYS ILE GLN ASP ILE GLU ILE LEU LYS ILE ARG LYS PRO          
SEQRES  25 B  544  ASN ASP ILE GLU THR PHE LYS ILE GLU ASN ASN TRP TYR          
SEQRES  26 B  544  PHE VAL VAL ALA ASP SER SER LYS ALA GLY PHE THR THR          
SEQRES  27 B  544  ILE TYR LYS TRP ASN GLY ASN GLY PHE TYR SER HIS GLN          
SEQRES  28 B  544  SER LEU HIS ALA TRP TYR ARG ASP THR ASP VAL GLU TYR          
SEQRES  29 B  544  LEU GLU ILE VAL ARG THR PRO GLN THR LEU ARG THR PRO          
SEQRES  30 B  544  HIS LEU ILE LEU SER SER SER SER GLN ARG PRO VAL ILE          
SEQRES  31 B  544  TYR GLN TRP ASN LYS ALA THR GLN LEU PHE THR ASN GLN          
SEQRES  32 B  544  THR ASP ILE PRO ASN MET GLU ASP VAL TYR ALA VAL LYS          
SEQRES  33 B  544  HIS PHE SER VAL LYS GLY ASP VAL TYR ILE CYS LEU THR          
SEQRES  34 B  544  ARG PHE ILE GLY ASP SER LYS VAL MET LYS TRP GLY GLY          
SEQRES  35 B  544  SER SER PHE GLN ASP ILE GLN ALA MET PRO SER ARG GLY          
SEQRES  36 B  544  SER MET VAL PHE GLN PRO LEU GLN ILE ASN ASN TYR GLN          
SEQRES  37 B  544  TYR ALA ILE LEU GLY SER ASP TYR SER PHE THR GLN VAL          
SEQRES  38 B  544  TYR ASN TRP ASP ALA GLU LYS ALA LYS PHE VAL LYS PHE          
SEQRES  39 B  544  GLN GLU LEU ASN VAL GLN ALA PRO ARG SER PHE THR HIS          
SEQRES  40 B  544  VAL SER ILE ASN LYS ARG ASN PHE LEU PHE ALA SER SER          
SEQRES  41 B  544  PHE LYS GLY ASN THR GLN ILE TYR LYS HIS VAL ILE VAL          
SEQRES  42 B  544  ASP LEU SER ALA LYS HIS HIS HIS HIS HIS HIS                  
SEQRES   1 C  497  ASN VAL GLU GLU GLU THR LYS TYR ILE GLU LEU MET ILE          
SEQRES   2 C  497  VAL ASN ASP HIS LEU MET PHE LYS LYS HIS ARG LEU SER          
SEQRES   3 C  497  VAL VAL HIS THR ASN THR TYR ALA LYS SER VAL VAL ASN          
SEQRES   4 C  497  MET ALA ASP LEU ILE TYR LYS ASP GLN LEU LYS THR ARG          
SEQRES   5 C  497  ILE VAL LEU VAL ALA MET GLU THR TRP ALA THR ASP ASN          
SEQRES   6 C  497  LYS PHE ALA ILE SER GLU ASN PRO LEU ILE THR LEU ARG          
SEQRES   7 C  497  GLU PHE MET LYS TYR ARG ARG ASP PHE ILE LYS GLU LYS          
SEQRES   8 C  497  SER ASP ALA VAL HIS LEU PHE SER GLY SER GLN PHE GLU          
SEQRES   9 C  497  SER SER ARG SER GLY ALA ALA TYR ILE GLY GLY ILE CYS          
SEQRES  10 C  497  SER LEU LEU LYS GLY GLY GLY VAL ASN GLU PHE GLY LYS          
SEQRES  11 C  497  THR ASP LEU MET ALA VAL THR LEU ALA GLN SER LEU ALA          
SEQRES  12 C  497  HIS ASN ILE GLY ILE ILE SER ASP LYS ARG LYS LEU ALA          
SEQRES  13 C  497  SER GLY GLU CYS LYS CYS GLU ASP THR TRP SER GLY CYS          
SEQRES  14 C  497  ILE MET GLY ASP THR GLY TYR TYR LEU PRO LYS LYS PHE          
SEQRES  15 C  497  THR GLN CYS ASN ILE GLU GLU TYR HIS ASP PHE LEU ASN          
SEQRES  16 C  497  SER GLY GLY GLY ALA CYS LEU PHE ASN LYS PRO SER LYS          
SEQRES  17 C  497  LEU LEU ASP PRO PRO GLU CYS GLY ASN GLY PHE ILE GLU          
SEQRES  18 C  497  THR GLY GLU GLU CYS ASP CYS GLY THR PRO ALA GLU CYS          
SEQRES  19 C  497  VAL LEU GLU GLY ALA GLU CYS CYS LYS LYS CYS THR LEU          
SEQRES  20 C  497  THR GLN ASP SER GLN CYS SER ASP GLY LEU CYS CYS LYS          
SEQRES  21 C  497  LYS CYS LYS PHE GLN PRO MET GLY THR VAL CYS ARG GLU          
SEQRES  22 C  497  ALA VAL ASN ASP CYS ASP ILE ARG GLU THR CYS SER GLY          
SEQRES  23 C  497  ASN SER SER GLN CYS ALA PRO ASN ILE HIS LYS MET ASP          
SEQRES  24 C  497  GLY TYR SER CYS ASP GLY VAL GLN GLY ILE CYS PHE GLY          
SEQRES  25 C  497  GLY ARG CYS LYS THR ARG ASP ARG GLN CYS LYS TYR ILE          
SEQRES  26 C  497  TRP GLY GLN LYS VAL THR ALA SER ASP LYS TYR CYS TYR          
SEQRES  27 C  497  GLU LYS LEU ASN ILE GLU GLY THR GLU LYS GLY ASN CYS          
SEQRES  28 C  497  GLY LYS ASP LYS ASP THR TRP ILE GLN CYS ASN LYS ARG          
SEQRES  29 C  497  ASP VAL LEU CYS GLY TYR LEU LEU CYS THR ASN ILE GLY          
SEQRES  30 C  497  ASN ILE PRO ARG LEU GLY GLU LEU ASP GLY GLU ILE THR          
SEQRES  31 C  497  SER THR LEU VAL VAL GLN GLN GLY ARG THR LEU ASN CYS          
SEQRES  32 C  497  SER GLY GLY HIS VAL LYS LEU GLU GLU ASP VAL ASP LEU          
SEQRES  33 C  497  GLY TYR VAL GLU ASP GLY THR PRO CYS GLY PRO GLN MET          
SEQRES  34 C  497  MET CYS LEU GLU HIS ARG CYS LEU PRO VAL ALA SER PHE          
SEQRES  35 C  497  ASN PHE SER THR CYS LEU SER SER LYS GLU GLY THR ILE          
SEQRES  36 C  497  CYS SER GLY ASN GLY VAL CYS SER ASN GLU LEU LYS CYS          
SEQRES  37 C  497  VAL CYS ASN ARG HIS TRP ILE GLY SER ASP CYS ASN THR          
SEQRES  38 C  497  TYR PHE PRO HIS ASN ASP ASP ALA LYS THR GLY ILE THR          
SEQRES  39 C  497  LEU SER GLY                                                  
SEQRES   1 D  544  ASP ALA ALA GLN PRO ALA ARG ARG ALA ARG ARG THR TYR          
SEQRES   2 D  544  GLU ALA TYR PRO ALA LYS PRO LYS CYS PRO ALA VAL CYS          
SEQRES   3 D  544  THR CYS THR LYS ASP ASN ALA LEU CYS GLU ASN ALA ARG          
SEQRES   4 D  544  SER ILE PRO ARG THR VAL PRO PRO ASP VAL ILE SER LEU          
SEQRES   5 D  544  SER PHE VAL ARG SER GLY PHE THR GLU ILE SER GLU GLY          
SEQRES   6 D  544  SER PHE LEU PHE THR PRO SER LEU GLN LEU LEU LEU PHE          
SEQRES   7 D  544  THR SER ASN SER PHE ASP VAL ILE SER ASP ASP ALA PHE          
SEQRES   8 D  544  ILE GLY LEU PRO HIS LEU GLU TYR LEU PHE ILE GLU ASN          
SEQRES   9 D  544  ASN ASN ILE LYS SER ILE SER ARG HIS THR PHE ARG GLY          
SEQRES  10 D  544  LEU LYS SER LEU ILE HIS LEU SER LEU ALA ASN ASN ASN          
SEQRES  11 D  544  LEU GLN THR LEU PRO LYS ASP ILE PHE LYS GLY LEU ASP          
SEQRES  12 D  544  SER LEU THR ASN VAL ASP LEU ARG GLY ASN SER PHE ASN          
SEQRES  13 D  544  CYS ASP CYS LYS LEU LYS TRP LEU VAL GLU TRP LEU GLY          
SEQRES  14 D  544  HIS THR ASN ALA THR VAL GLU ASP ILE TYR CYS GLU GLY          
SEQRES  15 D  544  PRO PRO GLU TYR LYS LYS ARG LYS ILE ASN SER LEU SER          
SEQRES  16 D  544  SER LYS ASP PHE ASP CYS ILE ILE THR GLU PHE ALA LYS          
SEQRES  17 D  544  SER GLN ASP LEU PRO TYR GLN SER LEU SER ILE ASP THR          
SEQRES  18 D  544  PHE SER TYR LEU ASN ASP GLU TYR VAL VAL ILE ALA GLN          
SEQRES  19 D  544  PRO PHE THR GLY LYS CYS ILE PHE LEU GLU TRP ASP HIS          
SEQRES  20 D  544  VAL GLU LYS THR PHE ARG ASN TYR ASP ASN ILE THR GLY          
SEQRES  21 D  544  THR SER THR VAL VAL CYS LYS PRO ILE VAL ILE GLU THR          
SEQRES  22 D  544  GLN LEU TYR VAL ILE VAL ALA GLN LEU PHE GLY GLY SER          
SEQRES  23 D  544  HIS ILE TYR LYS ARG ASP SER PHE ALA ASN LYS PHE ILE          
SEQRES  24 D  544  LYS ILE GLN ASP ILE GLU ILE LEU LYS ILE ARG LYS PRO          
SEQRES  25 D  544  ASN ASP ILE GLU THR PHE LYS ILE GLU ASN ASN TRP TYR          
SEQRES  26 D  544  PHE VAL VAL ALA ASP SER SER LYS ALA GLY PHE THR THR          
SEQRES  27 D  544  ILE TYR LYS TRP ASN GLY ASN GLY PHE TYR SER HIS GLN          
SEQRES  28 D  544  SER LEU HIS ALA TRP TYR ARG ASP THR ASP VAL GLU TYR          
SEQRES  29 D  544  LEU GLU ILE VAL ARG THR PRO GLN THR LEU ARG THR PRO          
SEQRES  30 D  544  HIS LEU ILE LEU SER SER SER SER GLN ARG PRO VAL ILE          
SEQRES  31 D  544  TYR GLN TRP ASN LYS ALA THR GLN LEU PHE THR ASN GLN          
SEQRES  32 D  544  THR ASP ILE PRO ASN MET GLU ASP VAL TYR ALA VAL LYS          
SEQRES  33 D  544  HIS PHE SER VAL LYS GLY ASP VAL TYR ILE CYS LEU THR          
SEQRES  34 D  544  ARG PHE ILE GLY ASP SER LYS VAL MET LYS TRP GLY GLY          
SEQRES  35 D  544  SER SER PHE GLN ASP ILE GLN ALA MET PRO SER ARG GLY          
SEQRES  36 D  544  SER MET VAL PHE GLN PRO LEU GLN ILE ASN ASN TYR GLN          
SEQRES  37 D  544  TYR ALA ILE LEU GLY SER ASP TYR SER PHE THR GLN VAL          
SEQRES  38 D  544  TYR ASN TRP ASP ALA GLU LYS ALA LYS PHE VAL LYS PHE          
SEQRES  39 D  544  GLN GLU LEU ASN VAL GLN ALA PRO ARG SER PHE THR HIS          
SEQRES  40 D  544  VAL SER ILE ASN LYS ARG ASN PHE LEU PHE ALA SER SER          
SEQRES  41 D  544  PHE LYS GLY ASN THR GLN ILE TYR LYS HIS VAL ILE VAL          
SEQRES  42 D  544  ASP LEU SER ALA LYS HIS HIS HIS HIS HIS HIS                  
HET     CA  A 801       1                                                       
HET     CA  A 802       1                                                       
HET     CA  A 803       1                                                       
HET    NAG  A 804      14                                                       
HET    NAG  A 805      14                                                       
HET     CA  B 601       1                                                       
HET    NAG  B 602      14                                                       
HET    NAG  B 603      14                                                       
HET    NAG  B 604      14                                                       
HET     CA  C 801       1                                                       
HET     CA  C 802       1                                                       
HET     CA  C 803       1                                                       
HET    NAG  C 804      14                                                       
HET    NAG  C 805      14                                                       
HET     CA  D 601       1                                                       
HET    NAG  D 602      14                                                       
HET    NAG  D 603      14                                                       
HET    NAG  D 604      14                                                       
HETNAM      CA CALCIUM ION                                                      
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
FORMUL   5   CA    8(CA 2+)                                                     
FORMUL   8  NAG    10(C8 H15 N O6)                                              
HELIX    1 AA1 ASP A  248  HIS A  255  1                                   8    
HELIX    2 AA2 SER A  258  LEU A  281  1                                  24    
HELIX    3 AA3 ASN A  304  PHE A  319  1                                  16    
HELIX    4 AA4 LYS A  362  GLY A  379  1                                  18    
HELIX    5 AA5 ASP A  383  SER A  389  1                                   7    
HELIX    6 AA6 THR A  415  SER A  428  1                                  14    
HELIX    7 AA7 GLY A  431  PHE A  435  5                                   5    
HELIX    8 AA8 THR A  462  VAL A  467  1                                   6    
HELIX    9 AA9 THR A  549  GLY A  559  1                                  11    
HELIX   10 AB1 ASP A  566  GLY A  577  1                                  12    
HELIX   11 AB2 ALA A  672  ASN A  675  5                                   4    
HELIX   12 AB3 THR A  686  GLY A  690  5                                   5    
HELIX   13 AB4 ASP B  178  LYS B  180  5                                   3    
HELIX   14 AB5 LEU B  181  THR B  191  1                                  11    
HELIX   15 AB6 PRO B  203  LYS B  207  5                                   5    
HELIX   16 AB7 LYS B  210  LEU B  214  5                                   5    
HELIX   17 AB8 SER B  215  PHE B  219  5                                   5    
HELIX   18 AB9 ASP C  248  HIS C  255  1                                   8    
HELIX   19 AC1 SER C  258  LEU C  281  1                                  24    
HELIX   20 AC2 ASN C  304  PHE C  319  1                                  16    
HELIX   21 AC3 LYS C  362  GLY C  379  1                                  18    
HELIX   22 AC4 ASP C  383  SER C  389  1                                   7    
HELIX   23 AC5 THR C  415  SER C  428  1                                  14    
HELIX   24 AC6 GLY C  431  PHE C  435  5                                   5    
HELIX   25 AC7 THR C  462  VAL C  467  1                                   6    
HELIX   26 AC8 THR C  549  GLY C  559  1                                  11    
HELIX   27 AC9 ASP C  566  GLY C  577  1                                  12    
HELIX   28 AD1 ALA C  672  ASN C  675  5                                   4    
HELIX   29 AD2 ILE C  687  GLY C  690  5                                   4    
HELIX   30 AD3 ASP D  178  LYS D  180  5                                   3    
HELIX   31 AD4 LEU D  181  THR D  191  1                                  11    
HELIX   32 AD5 PRO D  203  LYS D  207  5                                   5    
HELIX   33 AD6 LYS D  210  LEU D  214  5                                   5    
HELIX   34 AD7 SER D  215  PHE D  219  5                                   5    
SHEET    1 AA1 5 THR A 283  THR A 292  0                                        
SHEET    2 AA1 5 LYS A 239  ASN A 247  1  N  ILE A 241   O  ARG A 284           
SHEET    3 AA1 5 ALA A 326  SER A 331  1  O  PHE A 330   N  VAL A 246           
SHEET    4 AA1 5 GLY A 355  GLU A 359  1  O  ASN A 358   N  SER A 331           
SHEET    5 AA1 5 GLY A 341  ALA A 343 -1  N  ALA A 342   O  VAL A 357           
SHEET    1 AA2 2 CYS A 491  LYS A 492  0                                        
SHEET    2 AA2 2 LYS A 495  PHE A 496 -1  O  LYS A 495   N  LYS A 492           
SHEET    1 AA3 2 VAL A 502  ARG A 504  0                                        
SHEET    2 AA3 2 GLU A 514  THR A 515 -1  O  GLU A 514   N  ARG A 504           
SHEET    1 AA4 3 SER A 534  CYS A 535  0                                        
SHEET    2 AA4 3 GLY A 540  PHE A 543 -1  O  GLY A 540   N  CYS A 535           
SHEET    3 AA4 3 ARG A 546  LYS A 548 -1  O  ARG A 546   N  PHE A 543           
SHEET    1 AA5 2 THR A 563  ALA A 564  0                                        
SHEET    2 AA5 2 CYS A 605  THR A 606 -1  O  THR A 606   N  THR A 563           
SHEET    1 AA6 3 GLU A 616  LEU A 617  0                                        
SHEET    2 AA6 3 VAL A 640  LYS A 641 -1  O  LYS A 641   N  GLU A 616           
SHEET    3 AA6 3 ASP A 647  LEU A 648 -1  O  LEU A 648   N  VAL A 640           
SHEET    1 AA7 2 THR A 622  THR A 624  0                                        
SHEET    2 AA7 2 CYS A 635  GLY A 637 -1  O  CYS A 635   N  THR A 624           
SHEET    1 AA8 3 PRO A 656  GLY A 658  0                                        
SHEET    2 AA8 3 MET A 661  CYS A 663 -1  O  MET A 661   N  GLY A 658           
SHEET    3 AA8 3 CYS A 668  PRO A 670 -1  O  LEU A 669   N  MET A 662           
SHEET    1 AA9 2 GLY A 692  CYS A 694  0                                        
SHEET    2 AA9 2 CYS A 700  CYS A 702 -1  O  VAL A 701   N  VAL A 693           
SHEET    1 AB1 2 TRP A 706  ILE A 707  0                                        
SHEET    2 AB1 2 THR A 713  TYR A 714 -1  O  THR A 713   N  ILE A 707           
SHEET    1 AB2 8 CYS B  46  CYS B  48  0                                        
SHEET    2 AB2 8 ASN B  52  GLU B  56 -1  O  LEU B  54   N  THR B  47           
SHEET    3 AB2 8 SER B  71  VAL B  75  1  O  SER B  73   N  CYS B  55           
SHEET    4 AB2 8 LEU B  95  THR B  99  1  O  LEU B  97   N  PHE B  74           
SHEET    5 AB2 8 TYR B 119  GLU B 123  1  O  PHE B 121   N  PHE B  98           
SHEET    6 AB2 8 HIS B 143  SER B 145  1  O  SER B 145   N  LEU B 120           
SHEET    7 AB2 8 ASN B 167  ASP B 169  1  O  ASN B 167   N  LEU B 144           
SHEET    8 AB2 8 THR B 194  VAL B 195  1  O  THR B 194   N  VAL B 168           
SHEET    1 AB3 2 GLU B  81  ILE B  82  0                                        
SHEET    2 AB3 2 VAL B 105  ILE B 106  1  O  VAL B 105   N  ILE B  82           
SHEET    1 AB4 2 SER B 102  PHE B 103  0                                        
SHEET    2 AB4 2 ASN B 126  ILE B 127  1  O  ASN B 126   N  PHE B 103           
SHEET    1 AB5 4 PHE B 226  LEU B 232  0                                        
SHEET    2 AB5 4 THR B 545  HIS B 550 -1  O  LYS B 549   N  ALA B 227           
SHEET    3 AB5 4 ARG B 533  SER B 540 -1  N  ALA B 538   O  GLN B 546           
SHEET    4 AB5 4 PRO B 522  ILE B 530 -1  N  VAL B 528   O  PHE B 535           
SHEET    1 AB6 4 ILE B 239  TYR B 244  0                                        
SHEET    2 AB6 4 ASP B 247  ALA B 253 -1  O  VAL B 251   N  ASP B 240           
SHEET    3 AB6 4 LYS B 259  TRP B 265 -1  O  LEU B 263   N  VAL B 250           
SHEET    4 AB6 4 PHE B 272  THR B 279 -1  O  ASP B 276   N  PHE B 262           
SHEET    1 AB7 4 THR B 283  ILE B 291  0                                        
SHEET    2 AB7 4 GLN B 294  GLN B 301 -1  O  TYR B 296   N  ILE B 289           
SHEET    3 AB7 4 HIS B 307  ASP B 312 -1  O  TYR B 309   N  VAL B 297           
SHEET    4 AB7 4 LYS B 317  ASP B 323 -1  O  LYS B 317   N  ASP B 312           
SHEET    1 AB8 4 PRO B 332  ILE B 340  0                                        
SHEET    2 AB8 4 ASN B 343  ASP B 350 -1  O  ALA B 349   N  ASP B 334           
SHEET    3 AB8 4 THR B 357  TRP B 362 -1  O  TYR B 360   N  PHE B 346           
SHEET    4 AB8 4 PHE B 367  LEU B 373 -1  O  GLN B 371   N  ILE B 359           
SHEET    1 AB9 4 ASP B 379  ILE B 387  0                                        
SHEET    2 AB9 4 THR B 396  SER B 403 -1  O  SER B 402   N  THR B 380           
SHEET    3 AB9 4 VAL B 409  ASN B 414 -1  O  TYR B 411   N  LEU B 399           
SHEET    4 AB9 4 LEU B 419  ASP B 425 -1  O  THR B 424   N  ILE B 410           
SHEET    1 AC1 4 ALA B 434  VAL B 440  0                                        
SHEET    2 AC1 4 ASP B 443  THR B 449 -1  O  CYS B 447   N  LYS B 436           
SHEET    3 AC1 4 ILE B 452  GLY B 461 -1  O  TRP B 460   N  VAL B 444           
SHEET    4 AC1 4 SER B 464  ARG B 474 -1  O  SER B 473   N  GLY B 453           
SHEET    1 AC2 4 PHE B 479  ILE B 484  0                                        
SHEET    2 AC2 4 TYR B 487  LEU B 492 -1  O  TYR B 489   N  LEU B 482           
SHEET    3 AC2 4 THR B 499  ASP B 505 -1  O  TYR B 502   N  ALA B 490           
SHEET    4 AC2 4 LYS B 510  LEU B 517 -1  O  VAL B 512   N  ASN B 503           
SHEET    1 AC3 5 THR C 283  THR C 292  0                                        
SHEET    2 AC3 5 LYS C 239  ASN C 247  1  N  ILE C 241   O  ARG C 284           
SHEET    3 AC3 5 ALA C 326  SER C 331  1  O  PHE C 330   N  VAL C 246           
SHEET    4 AC3 5 GLY C 355  GLU C 359  1  O  ASN C 358   N  SER C 331           
SHEET    5 AC3 5 GLY C 341  ALA C 343 -1  N  ALA C 342   O  VAL C 357           
SHEET    1 AC4 2 CYS C 491  LYS C 492  0                                        
SHEET    2 AC4 2 LYS C 495  PHE C 496 -1  O  LYS C 495   N  LYS C 492           
SHEET    1 AC5 2 VAL C 502  ARG C 504  0                                        
SHEET    2 AC5 2 GLU C 514  THR C 515 -1  O  GLU C 514   N  ARG C 504           
SHEET    1 AC6 3 SER C 534  CYS C 535  0                                        
SHEET    2 AC6 3 GLY C 540  PHE C 543 -1  O  GLY C 540   N  CYS C 535           
SHEET    3 AC6 3 ARG C 546  LYS C 548 -1  O  ARG C 546   N  PHE C 543           
SHEET    1 AC7 2 THR C 563  ALA C 564  0                                        
SHEET    2 AC7 2 CYS C 605  THR C 606 -1  O  THR C 606   N  THR C 563           
SHEET    1 AC8 2 LYS C 585  ASP C 586  0                                        
SHEET    2 AC8 2 THR C 589  TRP C 590 -1  O  THR C 589   N  ASP C 586           
SHEET    1 AC9 3 GLU C 616  LEU C 617  0                                        
SHEET    2 AC9 3 VAL C 640  LYS C 641 -1  O  LYS C 641   N  GLU C 616           
SHEET    3 AC9 3 ASP C 647  LEU C 648 -1  O  LEU C 648   N  VAL C 640           
SHEET    1 AD1 2 THR C 622  THR C 624  0                                        
SHEET    2 AD1 2 CYS C 635  GLY C 637 -1  O  CYS C 635   N  THR C 624           
SHEET    1 AD2 3 PRO C 656  GLY C 658  0                                        
SHEET    2 AD2 3 MET C 661  CYS C 663 -1  O  MET C 661   N  GLY C 658           
SHEET    3 AD2 3 CYS C 668  PRO C 670 -1  O  LEU C 669   N  MET C 662           
SHEET    1 AD3 2 GLY C 692  CYS C 694  0                                        
SHEET    2 AD3 2 CYS C 700  CYS C 702 -1  O  VAL C 701   N  VAL C 693           
SHEET    1 AD4 2 TRP C 706  ILE C 707  0                                        
SHEET    2 AD4 2 THR C 713  TYR C 714 -1  O  THR C 713   N  ILE C 707           
SHEET    1 AD5 8 CYS D  46  CYS D  48  0                                        
SHEET    2 AD5 8 ASN D  52  GLU D  56 -1  O  LEU D  54   N  THR D  47           
SHEET    3 AD5 8 SER D  71  VAL D  75  1  O  SER D  73   N  CYS D  55           
SHEET    4 AD5 8 LEU D  95  THR D  99  1  O  LEU D  97   N  PHE D  74           
SHEET    5 AD5 8 TYR D 119  GLU D 123  1  O  PHE D 121   N  LEU D  96           
SHEET    6 AD5 8 HIS D 143  SER D 145  1  O  SER D 145   N  ILE D 122           
SHEET    7 AD5 8 ASN D 167  ASP D 169  1  O  ASN D 167   N  LEU D 144           
SHEET    8 AD5 8 THR D 194  VAL D 195  1  O  THR D 194   N  VAL D 168           
SHEET    1 AD6 2 GLU D  81  ILE D  82  0                                        
SHEET    2 AD6 2 VAL D 105  ILE D 106  1  O  VAL D 105   N  ILE D  82           
SHEET    1 AD7 2 SER D 102  PHE D 103  0                                        
SHEET    2 AD7 2 ASN D 126  ILE D 127  1  O  ASN D 126   N  PHE D 103           
SHEET    1 AD8 4 GLU D 225  LEU D 232  0                                        
SHEET    2 AD8 4 THR D 545  VAL D 551 -1  O  LYS D 549   N  ALA D 227           
SHEET    3 AD8 4 ARG D 533  SER D 540 -1  N  ALA D 538   O  GLN D 546           
SHEET    4 AD8 4 PRO D 522  ILE D 530 -1  N  VAL D 528   O  PHE D 535           
SHEET    1 AD9 4 ILE D 239  TYR D 244  0                                        
SHEET    2 AD9 4 ASP D 247  ALA D 253 -1  O  VAL D 251   N  ASP D 240           
SHEET    3 AD9 4 LYS D 259  TRP D 265 -1  O  LEU D 263   N  VAL D 250           
SHEET    4 AD9 4 PHE D 272  THR D 279 -1  O  ASP D 276   N  PHE D 262           
SHEET    1 AE1 4 THR D 283  ILE D 291  0                                        
SHEET    2 AE1 4 GLN D 294  GLN D 301 -1  O  TYR D 296   N  ILE D 289           
SHEET    3 AE1 4 HIS D 307  ASP D 312 -1  O  TYR D 309   N  VAL D 297           
SHEET    4 AE1 4 LYS D 317  ASP D 323 -1  O  LYS D 317   N  ASP D 312           
SHEET    1 AE2 4 PRO D 332  ILE D 340  0                                        
SHEET    2 AE2 4 ASN D 343  ASP D 350 -1  O  VAL D 347   N  GLU D 336           
SHEET    3 AE2 4 THR D 357  TRP D 362 -1  O  TYR D 360   N  PHE D 346           
SHEET    4 AE2 4 PHE D 367  LEU D 373 -1  O  GLN D 371   N  ILE D 359           
SHEET    1 AE3 4 ASP D 379  ILE D 387  0                                        
SHEET    2 AE3 4 THR D 396  SER D 403 -1  O  SER D 402   N  THR D 380           
SHEET    3 AE3 4 VAL D 409  ASN D 414 -1  O  TYR D 411   N  LEU D 399           
SHEET    4 AE3 4 LEU D 419  ASP D 425 -1  O  THR D 424   N  ILE D 410           
SHEET    1 AE4 4 ALA D 434  VAL D 440  0                                        
SHEET    2 AE4 4 ASP D 443  THR D 449 -1  O  TYR D 445   N  PHE D 438           
SHEET    3 AE4 4 ASP D 454  GLY D 461 -1  O  TRP D 460   N  VAL D 444           
SHEET    4 AE4 4 SER D 464  PRO D 472 -1  O  GLN D 466   N  LYS D 459           
SHEET    1 AE5 4 PHE D 479  ILE D 484  0                                        
SHEET    2 AE5 4 TYR D 487  LEU D 492 -1  O  TYR D 489   N  LEU D 482           
SHEET    3 AE5 4 THR D 499  ASP D 505 -1  O  TYR D 502   N  ALA D 490           
SHEET    4 AE5 4 LYS D 510  LEU D 517 -1  O  VAL D 512   N  ASN D 503           
SSBOND   1 CYS A  349    CYS A  433                          1555   1555  2.03  
SSBOND   2 CYS A  392    CYS A  417                          1555   1555  2.03  
SSBOND   3 CYS A  394    CYS A  401                          1555   1555  2.03  
SSBOND   4 CYS A  447    CYS A  477                          1555   1555  2.03  
SSBOND   5 CYS A  458    CYS A  474                          1555   1555  2.03  
SSBOND   6 CYS A  460    CYS A  466                          1555   1555  2.03  
SSBOND   7 CYS A  473    CYS A  494                          1555   1555  2.03  
SSBOND   8 CYS A  485    CYS A  491                          1555   1555  2.03  
SSBOND   9 CYS A  490    CYS A  516                          1555   1555  2.03  
SSBOND  10 CYS A  503    CYS A  523                          1555   1555  2.03  
SSBOND  11 CYS A  510    CYS A  542                          1555   1555  2.03  
SSBOND  12 CYS A  535    CYS A  547                          1555   1555  2.03  
SSBOND  13 CYS A  554    CYS A  605                          1555   1555  2.03  
SSBOND  14 CYS A  569    CYS A  635                          1555   1555  2.03  
SSBOND  15 CYS A  583    CYS A  593                          1555   1555  2.03  
SSBOND  16 CYS A  600    CYS A  663                          1555   1555  2.03  
SSBOND  17 CYS A  657    CYS A  668                          1555   1555  2.03  
SSBOND  18 CYS A  679    CYS A  694                          1555   1555  2.03  
SSBOND  19 CYS A  688    CYS A  700                          1555   1555  2.03  
SSBOND  20 CYS A  702    CYS A  711                          1555   1555  2.03  
SSBOND  21 CYS B   42    CYS B   48                          1555   1555  2.03  
SSBOND  22 CYS B   46    CYS B   55                          1555   1555  2.03  
SSBOND  23 CYS B  177    CYS B  200                          1555   1555  2.03  
SSBOND  24 CYS B  179    CYS B  221                          1555   1555  2.03  
SSBOND  25 CYS B  260    CYS B  286                          1555   1555  2.03  
SSBOND  26 CYS C  349    CYS C  433                          1555   1555  2.03  
SSBOND  27 CYS C  392    CYS C  417                          1555   1555  2.03  
SSBOND  28 CYS C  394    CYS C  401                          1555   1555  2.03  
SSBOND  29 CYS C  447    CYS C  477                          1555   1555  2.03  
SSBOND  30 CYS C  458    CYS C  474                          1555   1555  2.03  
SSBOND  31 CYS C  460    CYS C  466                          1555   1555  2.03  
SSBOND  32 CYS C  473    CYS C  494                          1555   1555  2.03  
SSBOND  33 CYS C  485    CYS C  491                          1555   1555  2.03  
SSBOND  34 CYS C  490    CYS C  516                          1555   1555  2.03  
SSBOND  35 CYS C  503    CYS C  523                          1555   1555  2.03  
SSBOND  36 CYS C  510    CYS C  542                          1555   1555  2.03  
SSBOND  37 CYS C  535    CYS C  547                          1555   1555  2.03  
SSBOND  38 CYS C  554    CYS C  605                          1555   1555  2.03  
SSBOND  39 CYS C  569    CYS C  635                          1555   1555  2.03  
SSBOND  40 CYS C  583    CYS C  593                          1555   1555  2.03  
SSBOND  41 CYS C  600    CYS C  663                          1555   1555  2.03  
SSBOND  42 CYS C  657    CYS C  668                          1555   1555  2.03  
SSBOND  43 CYS C  679    CYS C  694                          1555   1555  2.03  
SSBOND  44 CYS C  688    CYS C  700                          1555   1555  2.03  
SSBOND  45 CYS C  702    CYS C  711                          1555   1555  2.03  
SSBOND  46 CYS D   42    CYS D   48                          1555   1555  2.03  
SSBOND  47 CYS D   46    CYS D   55                          1555   1555  2.03  
SSBOND  48 CYS D  177    CYS D  200                          1555   1555  2.03  
SSBOND  49 CYS D  179    CYS D  221                          1555   1555  2.04  
SSBOND  50 CYS D  260    CYS D  286                          1555   1555  2.03  
LINK         OE2 GLU A 242                CA    CA A 801     1555   1555  2.36  
LINK         OD1 ASP A 325                CA    CA A 801     1555   1555  2.37  
LINK         OD2 ASP A 325                CA    CA A 801     1555   1555  2.35  
LINK         O   CYS A 433                CA    CA A 801     1555   1555  2.40  
LINK         OD1 ASN A 436                CA    CA A 801     1555   1555  2.39  
LINK         O   GLU A 446                CA    CA A 802     1555   1555  2.36  
LINK         OD1 ASN A 449                CA    CA A 802     1555   1555  2.39  
LINK         O   PHE A 451                CA    CA A 802     1555   1555  2.40  
LINK         OE1 GLU A 453                CA    CA A 802     1555   1555  2.36  
LINK         OE1 GLU A 456                CA    CA A 802     1555   1555  2.35  
LINK         OE2 GLU A 456                CA    CA A 802     1555   1555  2.40  
LINK         OD2 ASP A 459                CA    CA A 802     1555   1555  2.36  
LINK         OD1 ASP A 511                CA    CA A 803     1555   1555  2.36  
LINK         OD2 ASP A 511                CA    CA A 803     1555   1555  2.37  
LINK         O   ILE A 512                CA    CA A 803     1555   1555  2.38  
LINK         OE2 GLU A 514                CA    CA A 803     1555   1555  2.36  
LINK         ND2 ASN A 519                 C1  NAG A 804     1555   1555  1.43  
LINK         OD1 ASN A 526                CA    CA A 803     1555   1555  2.38  
LINK         O   ILE A 527                CA    CA A 803     1555   1555  2.39  
LINK         ND2 ASN A 675                 C1  NAG A 805     1555   1555  1.42  
LINK         ND2 ASN B 192                 C1  NAG B 602     1555   1555  1.46  
LINK         ND2 ASN B 277                 C1  NAG B 603     1555   1555  1.45  
LINK         OD1 ASP B 334                CA    CA B 601     1555   1555  2.37  
LINK         OD2 ASP B 334                CA    CA B 601     1555   1555  2.36  
LINK         OE1 GLU B 336                CA    CA B 601     1555   1555  2.36  
LINK         OD1 ASP B 381                CA    CA B 601     1555   1555  2.36  
LINK         OD2 ASP B 381                CA    CA B 601     1555   1555  2.37  
LINK         O   VAL B 382                CA    CA B 601     1555   1555  2.39  
LINK         ND2 ASN B 422                 C1  NAG B 604     1555   1555  1.44  
LINK         OE2 GLU C 242                CA    CA C 801     1555   1555  2.36  
LINK         OD1 ASP C 325                CA    CA C 801     1555   1555  2.38  
LINK         OD2 ASP C 325                CA    CA C 801     1555   1555  2.35  
LINK         O   CYS C 433                CA    CA C 801     1555   1555  2.40  
LINK         OD1 ASN C 436                CA    CA C 801     1555   1555  2.39  
LINK         O   GLU C 446                CA    CA C 802     1555   1555  2.36  
LINK         OD1 ASN C 449                CA    CA C 802     1555   1555  2.39  
LINK         O   PHE C 451                CA    CA C 802     1555   1555  2.40  
LINK         OE1 GLU C 453                CA    CA C 802     1555   1555  2.37  
LINK         OE1 GLU C 456                CA    CA C 802     1555   1555  2.35  
LINK         OE2 GLU C 456                CA    CA C 802     1555   1555  2.40  
LINK         OD2 ASP C 459                CA    CA C 802     1555   1555  2.37  
LINK         OD1 ASP C 511                CA    CA C 803     1555   1555  2.36  
LINK         OD2 ASP C 511                CA    CA C 803     1555   1555  2.37  
LINK         O   ILE C 512                CA    CA C 803     1555   1555  2.38  
LINK         OE2 GLU C 514                CA    CA C 803     1555   1555  2.36  
LINK         ND2 ASN C 519                 C1  NAG C 804     1555   1555  1.44  
LINK         OD1 ASN C 526                CA    CA C 803     1555   1555  2.38  
LINK         O   ILE C 527                CA    CA C 803     1555   1555  2.39  
LINK         ND2 ASN C 675                 C1  NAG C 805     1555   1555  1.44  
LINK         ND2 ASN D 192                 C1  NAG D 602     1555   1555  1.45  
LINK         NZ  LYS D 259                 O6  NAG D 603     1555   1555  1.30  
LINK         ND2 ASN D 277                 C1  NAG D 603     1555   1555  1.44  
LINK         OD1 ASP D 334                CA    CA D 601     1555   1555  2.37  
LINK         OD2 ASP D 334                CA    CA D 601     1555   1555  2.36  
LINK         OE1 GLU D 336                CA    CA D 601     1555   1555  2.36  
LINK         OD1 ASP D 381                CA    CA D 601     1555   1555  2.36  
LINK         OD2 ASP D 381                CA    CA D 601     1555   1555  2.36  
LINK         O   VAL D 382                CA    CA D 601     1555   1555  2.39  
LINK         ND2 ASN D 422                 C1  NAG D 604     1555   1555  1.44  
CISPEP   1 GLY B  202    PRO B  203          0        -5.02                     
CISPEP   2 THR B  390    PRO B  391          0         2.18                     
CISPEP   3 GLY D  202    PRO D  203          0        -5.38                     
CISPEP   4 ILE D  222    ILE D  223          0         3.23                     
CISPEP   5 THR D  390    PRO D  391          0         2.17                     
SITE     1 AC1  4 GLU A 242  ASP A 325  CYS A 433  ASN A 436                    
SITE     1 AC2  6 GLU A 446  ASN A 449  PHE A 451  GLU A 453                    
SITE     2 AC2  6 GLU A 456  ASP A 459                                          
SITE     1 AC3  5 ASP A 511  ILE A 512  GLU A 514  ASN A 526                    
SITE     2 AC3  5 ILE A 527                                                     
SITE     1 AC4  4 ASP B 334  GLU B 336  ASP B 381  VAL B 382                    
SITE     1 AC5  4 GLU C 242  ASP C 325  CYS C 433  ASN C 436                    
SITE     1 AC6  6 GLU C 446  ASN C 449  PHE C 451  GLU C 453                    
SITE     2 AC6  6 GLU C 456  ASP C 459                                          
SITE     1 AC7  5 ASP C 511  ILE C 512  GLU C 514  ASN C 526                    
SITE     2 AC7  5 ILE C 527                                                     
SITE     1 AC8  4 ASP D 334  GLU D 336  ASP D 381  VAL D 382                    
SITE     1 AC9  1 ASN A 519                                                     
SITE     1 AD1  1 ASN A 675                                                     
SITE     1 AD2  3 ASP B 163  ASN B 192  VAL C 260                               
SITE     1 AD3  3 LYS B 259  ASN B 277  THR B 279                               
SITE     1 AD4  1 ASN B 422                                                     
SITE     1 AD5  1 ASN C 519                                                     
SITE     1 AD6  1 ASN C 675                                                     
SITE     1 AD7  3 VAL A 260  ASP D 163  ASN D 192                               
SITE     1 AD8  8 GLN D 254  THR D 257  GLY D 258  CYS D 260                    
SITE     2 AD8  8 ASN D 274  ASP D 276  ASN D 277  ILE D 278                    
SITE     1 AD9  2 GLN D 412  ASN D 422                                          
CRYST1  105.143  124.324  164.663  90.00 104.80  90.00 P 1 21 1      4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.009511  0.000000  0.002513        0.00000                         
SCALE2      0.000000  0.008043  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006281        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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