GenomeNet

Database: PDB
Entry: 5Z8Y
LinkDB: 5Z8Y
Original site: 5Z8Y 
HEADER    CELL ADHESION                           01-FEB-18   5Z8Y              
TITLE     CRYSTAL STRUCTURE OF HUMAN LRRTM2 IN COMPLEX WITH NEUREXIN 1BETA      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: LEUCINE-RICH REPEAT TRANSMEMBRANE NEURONAL PROTEIN 2;      
COMPND   3 CHAIN: A, C, E, G;                                                   
COMPND   4 SYNONYM: LEUCINE-RICH REPEAT NEURONAL 2 PROTEIN;                     
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MUTATION: YES;                                                       
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: NEUREXIN-1-BETA;                                           
COMPND   9 CHAIN: B, D, F, H;                                                   
COMPND  10 SYNONYM: NEUREXIN I-BETA;                                            
COMPND  11 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: LRRTM2, KIAA0416, LRRN2;                                       
SOURCE   6 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE   7 EXPRESSION_SYSTEM_COMMON: HUMAN;                                     
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE   9 EXPRESSION_SYSTEM_CELL_LINE: EXPI293F;                               
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  12 ORGANISM_COMMON: HUMAN;                                              
SOURCE  13 ORGANISM_TAXID: 9606;                                                
SOURCE  14 GENE: NRXN1;                                                         
SOURCE  15 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE  16 EXPRESSION_SYSTEM_COMMON: HUMAN;                                     
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE  18 EXPRESSION_SYSTEM_CELL_LINE: EXPI293F                                
KEYWDS    SYNAPSE, LEUCINE-RICH REPEAT, SYNAPTIC ORGANIZER, CELL ADHESION       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.YAMAGATA,S.FUKAI                                                    
REVDAT   3   29-JUL-20 5Z8Y    1       COMPND REMARK HETNAM LINK                
REVDAT   3 2                   1       SITE   ATOM                              
REVDAT   2   31-OCT-18 5Z8Y    1       TITLE  COMPND                            
REVDAT   1   10-OCT-18 5Z8Y    0                                                
JRNL        AUTH   A.YAMAGATA,S.GOTO-ITO,Y.SATO,T.SHIROSHIMA,A.MAEDA,           
JRNL        AUTH 2 M.WATANABE,T.SAITOH,K.MAENAKA,T.TERADA,T.YOSHIDA,T.UEMURA,   
JRNL        AUTH 3 S.FUKAI                                                      
JRNL        TITL   STRUCTURAL INSIGHTS INTO MODULATION AND SELECTIVITY OF       
JRNL        TITL 2 TRANSSYNAPTIC NEUREXIN-LRRTM INTERACTION.                    
JRNL        REF    NAT COMMUN                    V.   9  3964 2018              
JRNL        REFN                   ESSN 2041-1723                               
JRNL        PMID   30262834                                                     
JRNL        DOI    10.1038/S41467-018-06333-8                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.40 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) : 3.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 49.82                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.990                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 49545                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.210                           
REMARK   3   R VALUE            (WORKING SET) : 0.209                           
REMARK   3   FREE R VALUE                     : 0.241                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.820                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2387                            
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 49.8205 -  8.7280    0.97     2778   182  0.1714 0.2411        
REMARK   3     2  8.7280 -  6.9336    0.98     2796   199  0.2027 0.2144        
REMARK   3     3  6.9336 -  6.0589    0.98     2822   154  0.2228 0.2633        
REMARK   3     4  6.0589 -  5.5057    0.98     2814   136  0.2144 0.2567        
REMARK   3     5  5.5057 -  5.1115    0.98     2874   140  0.2054 0.2490        
REMARK   3     6  5.1115 -  4.8104    0.98     2807   137  0.1698 0.1671        
REMARK   3     7  4.8104 -  4.5697    0.97     2786   143  0.1717 0.1998        
REMARK   3     8  4.5697 -  4.3709    0.97     2840   123  0.1879 0.1965        
REMARK   3     9  4.3709 -  4.2027    0.96     2788   143  0.2073 0.2506        
REMARK   3    10  4.2027 -  4.0577    0.96     2786   104  0.2114 0.2349        
REMARK   3    11  4.0577 -  3.9309    0.96     2812   109  0.2212 0.2562        
REMARK   3    12  3.9309 -  3.8186    0.96     2819   108  0.2315 0.2778        
REMARK   3    13  3.8186 -  3.7181    0.95     2821   107  0.2392 0.2808        
REMARK   3    14  3.7181 -  3.6274    0.95     2747   110  0.2515 0.2375        
REMARK   3    15  3.6274 -  3.5450    0.95     2732   152  0.2577 0.2864        
REMARK   3    16  3.5450 -  3.4695    0.94     2681   192  0.2868 0.2723        
REMARK   3    17  3.4695 -  3.4002    0.85     2455   148  0.2865 0.3519        
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)     : 0.440            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.640           
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          16824                                  
REMARK   3   ANGLE     :  0.890          22764                                  
REMARK   3   CHIRALITY :  0.038           2624                                  
REMARK   3   PLANARITY :  0.003           2880                                  
REMARK   3   DIHEDRAL  : 13.642           6068                                  
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): -21.4377  23.7672  -3.8036              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5825 T22:   0.6028                                     
REMARK   3      T33:   0.4975 T12:   0.0259                                     
REMARK   3      T13:  -0.0306 T23:   0.0772                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3445 L22:   0.4272                                     
REMARK   3      L33:  -0.1151 L12:   0.0683                                     
REMARK   3      L13:   0.0030 L23:  -0.0166                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0253 S12:  -0.0048 S13:  -0.0049                       
REMARK   3      S21:  -0.0052 S22:   0.0214 S23:  -0.0232                       
REMARK   3      S31:   0.0129 S32:   0.0226 S33:  -0.0043                       
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 5Z8Y COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 06-FEB-18.                  
REMARK 100 THE DEPOSITION ID IS D_1300006679.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 12-MAY-17                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.8                                
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 PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 49781                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.400                              
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     (%) : 96.3                               
REMARK 200  DATA REDUNDANCY                : 3.000                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.10500                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.2000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.40                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.46                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 93.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.50                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.42700                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 5Z8X,3B3Q                                            
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 69.26                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.00                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 15% PEG 3350, 0.1 M SODIUM/POTASSIUM     
REMARK 280  PHOSPHATE, PH 6.8, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE       
REMARK 280  293K                                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4                                              
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, I                               
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, J                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F, K                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H, L                               
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     ASN A   362                                                      
REMARK 465     LEU A   363                                                      
REMARK 465     SER A   364                                                      
REMARK 465     THR A   365                                                      
REMARK 465     THR A   366                                                      
REMARK 465     VAL A   367                                                      
REMARK 465     THR A   368                                                      
REMARK 465     VAL A   369                                                      
REMARK 465     MET A   370                                                      
REMARK 465     ALA A   371                                                      
REMARK 465     GLY A   372                                                      
REMARK 465     SER A   373                                                      
REMARK 465     HIS A   374                                                      
REMARK 465     HIS A   375                                                      
REMARK 465     HIS A   376                                                      
REMARK 465     HIS A   377                                                      
REMARK 465     HIS A   378                                                      
REMARK 465     HIS A   379                                                      
REMARK 465     ASP B    82                                                      
REMARK 465     ALA B    83                                                      
REMARK 465     ALA B    84                                                      
REMARK 465     GLY B   263                                                      
REMARK 465     GLU B   264                                                      
REMARK 465     VAL B   265                                                      
REMARK 465     PRO B   266                                                      
REMARK 465     GLY B   267                                                      
REMARK 465     SER B   268                                                      
REMARK 465     HIS B   269                                                      
REMARK 465     HIS B   270                                                      
REMARK 465     HIS B   271                                                      
REMARK 465     HIS B   272                                                      
REMARK 465     HIS B   273                                                      
REMARK 465     HIS B   274                                                      
REMARK 465     ASN C   362                                                      
REMARK 465     LEU C   363                                                      
REMARK 465     SER C   364                                                      
REMARK 465     THR C   365                                                      
REMARK 465     THR C   366                                                      
REMARK 465     VAL C   367                                                      
REMARK 465     THR C   368                                                      
REMARK 465     VAL C   369                                                      
REMARK 465     MET C   370                                                      
REMARK 465     ALA C   371                                                      
REMARK 465     GLY C   372                                                      
REMARK 465     SER C   373                                                      
REMARK 465     HIS C   374                                                      
REMARK 465     HIS C   375                                                      
REMARK 465     HIS C   376                                                      
REMARK 465     HIS C   377                                                      
REMARK 465     HIS C   378                                                      
REMARK 465     HIS C   379                                                      
REMARK 465     ASP D    82                                                      
REMARK 465     ALA D    83                                                      
REMARK 465     ALA D    84                                                      
REMARK 465     GLY D   263                                                      
REMARK 465     GLU D   264                                                      
REMARK 465     VAL D   265                                                      
REMARK 465     PRO D   266                                                      
REMARK 465     GLY D   267                                                      
REMARK 465     SER D   268                                                      
REMARK 465     HIS D   269                                                      
REMARK 465     HIS D   270                                                      
REMARK 465     HIS D   271                                                      
REMARK 465     HIS D   272                                                      
REMARK 465     HIS D   273                                                      
REMARK 465     HIS D   274                                                      
REMARK 465     ASN E   362                                                      
REMARK 465     LEU E   363                                                      
REMARK 465     SER E   364                                                      
REMARK 465     THR E   365                                                      
REMARK 465     THR E   366                                                      
REMARK 465     VAL E   367                                                      
REMARK 465     THR E   368                                                      
REMARK 465     VAL E   369                                                      
REMARK 465     MET E   370                                                      
REMARK 465     ALA E   371                                                      
REMARK 465     GLY E   372                                                      
REMARK 465     SER E   373                                                      
REMARK 465     HIS E   374                                                      
REMARK 465     HIS E   375                                                      
REMARK 465     HIS E   376                                                      
REMARK 465     HIS E   377                                                      
REMARK 465     HIS E   378                                                      
REMARK 465     HIS E   379                                                      
REMARK 465     ASP F    82                                                      
REMARK 465     ALA F    83                                                      
REMARK 465     ALA F    84                                                      
REMARK 465     GLY F   263                                                      
REMARK 465     GLU F   264                                                      
REMARK 465     VAL F   265                                                      
REMARK 465     PRO F   266                                                      
REMARK 465     GLY F   267                                                      
REMARK 465     SER F   268                                                      
REMARK 465     HIS F   269                                                      
REMARK 465     HIS F   270                                                      
REMARK 465     HIS F   271                                                      
REMARK 465     HIS F   272                                                      
REMARK 465     HIS F   273                                                      
REMARK 465     HIS F   274                                                      
REMARK 465     ASN G   362                                                      
REMARK 465     LEU G   363                                                      
REMARK 465     SER G   364                                                      
REMARK 465     THR G   365                                                      
REMARK 465     THR G   366                                                      
REMARK 465     VAL G   367                                                      
REMARK 465     THR G   368                                                      
REMARK 465     VAL G   369                                                      
REMARK 465     MET G   370                                                      
REMARK 465     ALA G   371                                                      
REMARK 465     GLY G   372                                                      
REMARK 465     SER G   373                                                      
REMARK 465     HIS G   374                                                      
REMARK 465     HIS G   375                                                      
REMARK 465     HIS G   376                                                      
REMARK 465     HIS G   377                                                      
REMARK 465     HIS G   378                                                      
REMARK 465     HIS G   379                                                      
REMARK 465     ASP H    82                                                      
REMARK 465     ALA H    83                                                      
REMARK 465     ALA H    84                                                      
REMARK 465     GLY H   263                                                      
REMARK 465     GLU H   264                                                      
REMARK 465     VAL H   265                                                      
REMARK 465     PRO H   266                                                      
REMARK 465     GLY H   267                                                      
REMARK 465     SER H   268                                                      
REMARK 465     HIS H   269                                                      
REMARK 465     HIS H   270                                                      
REMARK 465     HIS H   271                                                      
REMARK 465     HIS H   272                                                      
REMARK 465     HIS H   273                                                      
REMARK 465     HIS H   274                                                      
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   OD1  ASP B   141     O    VAL B   158              1.99            
REMARK 500   OD1  ASP D   141     O    VAL D   158              2.01            
REMARK 500   OD1  ASP F   141     O    VAL F   158              2.05            
REMARK 500   OD1  ASP H   141     O    VAL H   158              2.05            
REMARK 500   O    ARG C   157     OG   SER C   182              2.10            
REMARK 500   O    ARG A   157     OG   SER A   182              2.11            
REMARK 500   O    ARG G   157     OG   SER G   182              2.12            
REMARK 500   O    ARG E   157     OG   SER E   182              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    LYS A  42     -128.53   -146.71                                   
REMARK 500    ASN A  71     -168.17   -104.54                                   
REMARK 500    ASN A 119     -162.83   -126.25                                   
REMARK 500    GLN A 144       40.38   -105.36                                   
REMARK 500    LEU A 156       53.62   -111.41                                   
REMARK 500    ASN A 191     -159.77   -124.38                                   
REMARK 500    LEU A 204       41.98   -101.85                                   
REMARK 500    ASN A 215     -149.04   -107.40                                   
REMARK 500    ASN A 239     -150.51   -104.50                                   
REMARK 500    ASN A 263     -153.59    -98.89                                   
REMARK 500    MET A 276       74.76   -119.87                                   
REMARK 500    ASN A 287     -162.28   -111.00                                   
REMARK 500    SER A 291     -179.98   -172.47                                   
REMARK 500    LEU A 312       55.24    -91.26                                   
REMARK 500    ASN B 173       35.45    -92.61                                   
REMARK 500    LYS C  42     -128.34   -146.67                                   
REMARK 500    ASN C  71     -168.25   -105.07                                   
REMARK 500    ASN C 119     -162.91   -126.35                                   
REMARK 500    GLN C 144       40.55   -105.62                                   
REMARK 500    LEU C 156       53.62   -111.29                                   
REMARK 500    ASN C 191     -160.06   -124.39                                   
REMARK 500    LEU C 204       42.12   -101.90                                   
REMARK 500    ASN C 215     -149.37   -107.51                                   
REMARK 500    ASN C 239     -150.78   -104.77                                   
REMARK 500    ASN C 263     -153.63    -99.05                                   
REMARK 500    MET C 276       74.31   -119.91                                   
REMARK 500    ASN C 287     -162.53   -111.35                                   
REMARK 500    LEU C 312       55.39    -91.12                                   
REMARK 500    ASN D 173       35.25    -92.62                                   
REMARK 500    LYS E  42     -127.54   -147.23                                   
REMARK 500    ASN E  71     -168.06   -105.20                                   
REMARK 500    ASN E 119     -162.42   -125.98                                   
REMARK 500    GLN E 144       40.58   -105.30                                   
REMARK 500    LEU E 156       53.94   -111.46                                   
REMARK 500    ASN E 191     -159.98   -124.24                                   
REMARK 500    LEU E 204       43.06   -100.98                                   
REMARK 500    ASN E 215     -148.50   -107.60                                   
REMARK 500    ASN E 239     -150.76   -104.28                                   
REMARK 500    ASN E 263     -153.11    -98.44                                   
REMARK 500    MET E 276       74.93   -119.68                                   
REMARK 500    ASN E 287     -162.04   -110.93                                   
REMARK 500    SER E 291     -179.82   -172.28                                   
REMARK 500    LEU E 312       55.98    -90.94                                   
REMARK 500    ASN F 173       35.25    -92.16                                   
REMARK 500    LYS G  42     -127.86   -147.26                                   
REMARK 500    ASN G  71     -168.32   -105.10                                   
REMARK 500    HIS G  72       62.63   -119.04                                   
REMARK 500    ASN G 119     -162.85   -126.03                                   
REMARK 500    GLN G 144       40.73   -105.85                                   
REMARK 500    LEU G 156       53.91   -111.05                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      59 RAMACHANDRAN OUTLIERS.                        
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                              ZN A 404  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  53   NE2                                                    
REMARK 620 2 HIS A  72   ND1 117.2                                              
REMARK 620 3 HIS E  53   NE2  85.1 113.3                                        
REMARK 620 4 HIS E  72   ND1 115.0 111.6 112.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B 301  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 141   OD1                                                    
REMARK 620 2 ASP B 141   OD2  55.1                                              
REMARK 620 3 VAL B 158   O    49.3  61.2                                        
REMARK 620 4 ILE B 210   O    82.1 135.6  82.8                                  
REMARK 620 5 ASN B 212   OD1 158.7 141.1 143.2  83.4                            
REMARK 620 6 HOH B 401   O   109.0  95.1  59.7  87.3  85.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN C 404  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS C  53   NE2                                                    
REMARK 620 2 HIS C  72   ND1 110.5                                              
REMARK 620 3 HIS G  53   NE2  91.7 111.0                                        
REMARK 620 4 HIS G  72   ND1 116.5 118.8 104.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA D 301  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH C 501   O                                                      
REMARK 620 2 ASP D 141   OD1 117.4                                              
REMARK 620 3 ASP D 141   OD2  92.7  55.2                                        
REMARK 620 4 VAL D 158   O    67.8  49.9  61.2                                  
REMARK 620 5 ILE D 210   O    97.7  81.7 135.3  83.0                            
REMARK 620 6 ASN D 212   OD1  80.7 158.7 139.8 144.1  84.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA F 301  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP F 141   OD1                                                    
REMARK 620 2 ASP F 141   OD2  55.3                                              
REMARK 620 3 VAL F 158   O    51.0  61.5                                        
REMARK 620 4 ILE F 210   O    82.1 135.9  84.2                                  
REMARK 620 5 ASN F 212   OD1 159.2 140.2 142.2  83.9                            
REMARK 620 6 HOH F 401   O   110.7  94.6  59.7  90.3  84.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA H 301  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP H 141   OD1                                                    
REMARK 620 2 ASP H 141   OD2  55.3                                              
REMARK 620 3 VAL H 158   O    51.0  61.3                                        
REMARK 620 4 ILE H 210   O    81.8 135.6  84.0                                  
REMARK 620 5 ASN H 212   OD1 159.9 139.1 142.5  85.3                            
REMARK 620 6 HOH H 401   O   114.9  96.9  63.9  90.8  80.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 SEQUENCE OF NEUREXIN-1-BETA WAS BASED ON ISOFORM 3B OF DATABASE      
REMARK 999 P58400 (NRX1B_HUMAN).                                                
DBREF  5Z8Y A   34   371  UNP    O43300   LRRT2_HUMAN     34    371             
DBREF  5Z8Y B   86   266  UNP    P58400   NRX1B_HUMAN     86    266             
DBREF  5Z8Y C   34   371  UNP    O43300   LRRT2_HUMAN     34    371             
DBREF  5Z8Y D   86   266  UNP    P58400   NRX1B_HUMAN     86    266             
DBREF  5Z8Y E   34   371  UNP    O43300   LRRT2_HUMAN     34    371             
DBREF  5Z8Y F   86   266  UNP    P58400   NRX1B_HUMAN     86    266             
DBREF  5Z8Y G   34   371  UNP    O43300   LRRT2_HUMAN     34    371             
DBREF  5Z8Y H   86   266  UNP    P58400   NRX1B_HUMAN     86    266             
SEQADV 5Z8Y ALA A  355  UNP  O43300    HIS   355 ENGINEERED MUTATION            
SEQADV 5Z8Y GLY A  372  UNP  O43300              EXPRESSION TAG                 
SEQADV 5Z8Y SER A  373  UNP  O43300              EXPRESSION TAG                 
SEQADV 5Z8Y HIS A  374  UNP  O43300              EXPRESSION TAG                 
SEQADV 5Z8Y HIS A  375  UNP  O43300              EXPRESSION TAG                 
SEQADV 5Z8Y HIS A  376  UNP  O43300              EXPRESSION TAG                 
SEQADV 5Z8Y HIS A  377  UNP  O43300              EXPRESSION TAG                 
SEQADV 5Z8Y HIS A  378  UNP  O43300              EXPRESSION TAG                 
SEQADV 5Z8Y HIS A  379  UNP  O43300              EXPRESSION TAG                 
SEQADV 5Z8Y ASP B   82  UNP  P58400              EXPRESSION TAG                 
SEQADV 5Z8Y ALA B   83  UNP  P58400              EXPRESSION TAG                 
SEQADV 5Z8Y ALA B   84  UNP  P58400              EXPRESSION TAG                 
SEQADV 5Z8Y SER B   85  UNP  P58400              EXPRESSION TAG                 
SEQADV 5Z8Y GLY B  267  UNP  P58400              EXPRESSION TAG                 
SEQADV 5Z8Y SER B  268  UNP  P58400              EXPRESSION TAG                 
SEQADV 5Z8Y HIS B  269  UNP  P58400              EXPRESSION TAG                 
SEQADV 5Z8Y HIS B  270  UNP  P58400              EXPRESSION TAG                 
SEQADV 5Z8Y HIS B  271  UNP  P58400              EXPRESSION TAG                 
SEQADV 5Z8Y HIS B  272  UNP  P58400              EXPRESSION TAG                 
SEQADV 5Z8Y HIS B  273  UNP  P58400              EXPRESSION TAG                 
SEQADV 5Z8Y HIS B  274  UNP  P58400              EXPRESSION TAG                 
SEQADV 5Z8Y ALA C  355  UNP  O43300    HIS   355 ENGINEERED MUTATION            
SEQADV 5Z8Y GLY C  372  UNP  O43300              EXPRESSION TAG                 
SEQADV 5Z8Y SER C  373  UNP  O43300              EXPRESSION TAG                 
SEQADV 5Z8Y HIS C  374  UNP  O43300              EXPRESSION TAG                 
SEQADV 5Z8Y HIS C  375  UNP  O43300              EXPRESSION TAG                 
SEQADV 5Z8Y HIS C  376  UNP  O43300              EXPRESSION TAG                 
SEQADV 5Z8Y HIS C  377  UNP  O43300              EXPRESSION TAG                 
SEQADV 5Z8Y HIS C  378  UNP  O43300              EXPRESSION TAG                 
SEQADV 5Z8Y HIS C  379  UNP  O43300              EXPRESSION TAG                 
SEQADV 5Z8Y ASP D   82  UNP  P58400              EXPRESSION TAG                 
SEQADV 5Z8Y ALA D   83  UNP  P58400              EXPRESSION TAG                 
SEQADV 5Z8Y ALA D   84  UNP  P58400              EXPRESSION TAG                 
SEQADV 5Z8Y SER D   85  UNP  P58400              EXPRESSION TAG                 
SEQADV 5Z8Y GLY D  267  UNP  P58400              EXPRESSION TAG                 
SEQADV 5Z8Y SER D  268  UNP  P58400              EXPRESSION TAG                 
SEQADV 5Z8Y HIS D  269  UNP  P58400              EXPRESSION TAG                 
SEQADV 5Z8Y HIS D  270  UNP  P58400              EXPRESSION TAG                 
SEQADV 5Z8Y HIS D  271  UNP  P58400              EXPRESSION TAG                 
SEQADV 5Z8Y HIS D  272  UNP  P58400              EXPRESSION TAG                 
SEQADV 5Z8Y HIS D  273  UNP  P58400              EXPRESSION TAG                 
SEQADV 5Z8Y HIS D  274  UNP  P58400              EXPRESSION TAG                 
SEQADV 5Z8Y ALA E  355  UNP  O43300    HIS   355 ENGINEERED MUTATION            
SEQADV 5Z8Y GLY E  372  UNP  O43300              EXPRESSION TAG                 
SEQADV 5Z8Y SER E  373  UNP  O43300              EXPRESSION TAG                 
SEQADV 5Z8Y HIS E  374  UNP  O43300              EXPRESSION TAG                 
SEQADV 5Z8Y HIS E  375  UNP  O43300              EXPRESSION TAG                 
SEQADV 5Z8Y HIS E  376  UNP  O43300              EXPRESSION TAG                 
SEQADV 5Z8Y HIS E  377  UNP  O43300              EXPRESSION TAG                 
SEQADV 5Z8Y HIS E  378  UNP  O43300              EXPRESSION TAG                 
SEQADV 5Z8Y HIS E  379  UNP  O43300              EXPRESSION TAG                 
SEQADV 5Z8Y ASP F   82  UNP  P58400              EXPRESSION TAG                 
SEQADV 5Z8Y ALA F   83  UNP  P58400              EXPRESSION TAG                 
SEQADV 5Z8Y ALA F   84  UNP  P58400              EXPRESSION TAG                 
SEQADV 5Z8Y SER F   85  UNP  P58400              EXPRESSION TAG                 
SEQADV 5Z8Y GLY F  267  UNP  P58400              EXPRESSION TAG                 
SEQADV 5Z8Y SER F  268  UNP  P58400              EXPRESSION TAG                 
SEQADV 5Z8Y HIS F  269  UNP  P58400              EXPRESSION TAG                 
SEQADV 5Z8Y HIS F  270  UNP  P58400              EXPRESSION TAG                 
SEQADV 5Z8Y HIS F  271  UNP  P58400              EXPRESSION TAG                 
SEQADV 5Z8Y HIS F  272  UNP  P58400              EXPRESSION TAG                 
SEQADV 5Z8Y HIS F  273  UNP  P58400              EXPRESSION TAG                 
SEQADV 5Z8Y HIS F  274  UNP  P58400              EXPRESSION TAG                 
SEQADV 5Z8Y ALA G  355  UNP  O43300    HIS   355 ENGINEERED MUTATION            
SEQADV 5Z8Y GLY G  372  UNP  O43300              EXPRESSION TAG                 
SEQADV 5Z8Y SER G  373  UNP  O43300              EXPRESSION TAG                 
SEQADV 5Z8Y HIS G  374  UNP  O43300              EXPRESSION TAG                 
SEQADV 5Z8Y HIS G  375  UNP  O43300              EXPRESSION TAG                 
SEQADV 5Z8Y HIS G  376  UNP  O43300              EXPRESSION TAG                 
SEQADV 5Z8Y HIS G  377  UNP  O43300              EXPRESSION TAG                 
SEQADV 5Z8Y HIS G  378  UNP  O43300              EXPRESSION TAG                 
SEQADV 5Z8Y HIS G  379  UNP  O43300              EXPRESSION TAG                 
SEQADV 5Z8Y ASP H   82  UNP  P58400              EXPRESSION TAG                 
SEQADV 5Z8Y ALA H   83  UNP  P58400              EXPRESSION TAG                 
SEQADV 5Z8Y ALA H   84  UNP  P58400              EXPRESSION TAG                 
SEQADV 5Z8Y SER H   85  UNP  P58400              EXPRESSION TAG                 
SEQADV 5Z8Y GLY H  267  UNP  P58400              EXPRESSION TAG                 
SEQADV 5Z8Y SER H  268  UNP  P58400              EXPRESSION TAG                 
SEQADV 5Z8Y HIS H  269  UNP  P58400              EXPRESSION TAG                 
SEQADV 5Z8Y HIS H  270  UNP  P58400              EXPRESSION TAG                 
SEQADV 5Z8Y HIS H  271  UNP  P58400              EXPRESSION TAG                 
SEQADV 5Z8Y HIS H  272  UNP  P58400              EXPRESSION TAG                 
SEQADV 5Z8Y HIS H  273  UNP  P58400              EXPRESSION TAG                 
SEQADV 5Z8Y HIS H  274  UNP  P58400              EXPRESSION TAG                 
SEQRES   1 A  346  CYS PRO PRO LYS CYS ARG CYS GLU LYS LEU LEU PHE TYR          
SEQRES   2 A  346  CYS ASP SER GLN GLY PHE HIS SER VAL PRO ASN ALA THR          
SEQRES   3 A  346  ASP LYS GLY SER LEU GLY LEU SER LEU ARG HIS ASN HIS          
SEQRES   4 A  346  ILE THR GLU LEU GLU ARG ASP GLN PHE ALA SER PHE SER          
SEQRES   5 A  346  GLN LEU THR TRP LEU HIS LEU ASP HIS ASN GLN ILE SER          
SEQRES   6 A  346  THR VAL LYS GLU ASP ALA PHE GLN GLY LEU TYR LYS LEU          
SEQRES   7 A  346  LYS GLU LEU ILE LEU SER SER ASN LYS ILE PHE TYR LEU          
SEQRES   8 A  346  PRO ASN THR THR PHE THR GLN LEU ILE ASN LEU GLN ASN          
SEQRES   9 A  346  LEU ASP LEU SER PHE ASN GLN LEU SER SER LEU HIS PRO          
SEQRES  10 A  346  GLU LEU PHE TYR GLY LEU ARG LYS LEU GLN THR LEU HIS          
SEQRES  11 A  346  LEU ARG SER ASN SER LEU ARG THR ILE PRO VAL ARG LEU          
SEQRES  12 A  346  PHE TRP ASP CYS ARG SER LEU GLU PHE LEU ASP LEU SER          
SEQRES  13 A  346  THR ASN ARG LEU ARG SER LEU ALA ARG ASN GLY PHE ALA          
SEQRES  14 A  346  GLY LEU ILE LYS LEU ARG GLU LEU HIS LEU GLU HIS ASN          
SEQRES  15 A  346  GLN LEU THR LYS ILE ASN PHE ALA HIS PHE LEU ARG LEU          
SEQRES  16 A  346  SER SER LEU HIS THR LEU PHE LEU GLN TRP ASN LYS ILE          
SEQRES  17 A  346  SER ASN LEU THR CYS GLY MET GLU TRP THR TRP GLY THR          
SEQRES  18 A  346  LEU GLU LYS LEU ASP LEU THR GLY ASN GLU ILE LYS ALA          
SEQRES  19 A  346  ILE ASP LEU THR VAL PHE GLU THR MET PRO ASN LEU LYS          
SEQRES  20 A  346  ILE LEU LEU MET ASP ASN ASN LYS LEU ASN SER LEU ASP          
SEQRES  21 A  346  SER LYS ILE LEU ASN SER LEU ARG SER LEU THR THR VAL          
SEQRES  22 A  346  GLY LEU SER GLY ASN LEU TRP GLU CYS SER ALA ARG ILE          
SEQRES  23 A  346  CYS ALA LEU ALA SER TRP LEU GLY SER PHE GLN GLY ARG          
SEQRES  24 A  346  TRP GLU HIS SER ILE LEU CYS HIS SER PRO ASP HIS THR          
SEQRES  25 A  346  GLN GLY GLU ASP ILE LEU ASP ALA VAL ALA GLY PHE GLN          
SEQRES  26 A  346  LEU CYS TRP ASN LEU SER THR THR VAL THR VAL MET ALA          
SEQRES  27 A  346  GLY SER HIS HIS HIS HIS HIS HIS                              
SEQRES   1 B  193  ASP ALA ALA SER HIS ALA GLY THR THR TYR ILE PHE SER          
SEQRES   2 B  193  LYS GLY GLY GLY GLN ILE THR TYR LYS TRP PRO PRO ASN          
SEQRES   3 B  193  ASP ARG PRO SER THR ARG ALA ASP ARG LEU ALA ILE GLY          
SEQRES   4 B  193  PHE SER THR VAL GLN LYS GLU ALA VAL LEU VAL ARG VAL          
SEQRES   5 B  193  ASP SER SER SER GLY LEU GLY ASP TYR LEU GLU LEU HIS          
SEQRES   6 B  193  ILE HIS GLN GLY LYS ILE GLY VAL LYS PHE ASN VAL GLY          
SEQRES   7 B  193  THR ASP ASP ILE ALA ILE GLU GLU SER ASN ALA ILE ILE          
SEQRES   8 B  193  ASN ASP GLY LYS TYR HIS VAL VAL ARG PHE THR ARG SER          
SEQRES   9 B  193  GLY GLY ASN ALA THR LEU GLN VAL ASP SER TRP PRO VAL          
SEQRES  10 B  193  ILE GLU ARG TYR PRO ALA GLY ARG GLN LEU THR ILE PHE          
SEQRES  11 B  193  ASN SER GLN ALA THR ILE ILE ILE GLY GLY LYS GLU GLN          
SEQRES  12 B  193  GLY GLN PRO PHE GLN GLY GLN LEU SER GLY LEU TYR TYR          
SEQRES  13 B  193  ASN GLY LEU LYS VAL LEU ASN MET ALA ALA GLU ASN ASP          
SEQRES  14 B  193  ALA ASN ILE ALA ILE VAL GLY ASN VAL ARG LEU VAL GLY          
SEQRES  15 B  193  GLU VAL PRO GLY SER HIS HIS HIS HIS HIS HIS                  
SEQRES   1 C  346  CYS PRO PRO LYS CYS ARG CYS GLU LYS LEU LEU PHE TYR          
SEQRES   2 C  346  CYS ASP SER GLN GLY PHE HIS SER VAL PRO ASN ALA THR          
SEQRES   3 C  346  ASP LYS GLY SER LEU GLY LEU SER LEU ARG HIS ASN HIS          
SEQRES   4 C  346  ILE THR GLU LEU GLU ARG ASP GLN PHE ALA SER PHE SER          
SEQRES   5 C  346  GLN LEU THR TRP LEU HIS LEU ASP HIS ASN GLN ILE SER          
SEQRES   6 C  346  THR VAL LYS GLU ASP ALA PHE GLN GLY LEU TYR LYS LEU          
SEQRES   7 C  346  LYS GLU LEU ILE LEU SER SER ASN LYS ILE PHE TYR LEU          
SEQRES   8 C  346  PRO ASN THR THR PHE THR GLN LEU ILE ASN LEU GLN ASN          
SEQRES   9 C  346  LEU ASP LEU SER PHE ASN GLN LEU SER SER LEU HIS PRO          
SEQRES  10 C  346  GLU LEU PHE TYR GLY LEU ARG LYS LEU GLN THR LEU HIS          
SEQRES  11 C  346  LEU ARG SER ASN SER LEU ARG THR ILE PRO VAL ARG LEU          
SEQRES  12 C  346  PHE TRP ASP CYS ARG SER LEU GLU PHE LEU ASP LEU SER          
SEQRES  13 C  346  THR ASN ARG LEU ARG SER LEU ALA ARG ASN GLY PHE ALA          
SEQRES  14 C  346  GLY LEU ILE LYS LEU ARG GLU LEU HIS LEU GLU HIS ASN          
SEQRES  15 C  346  GLN LEU THR LYS ILE ASN PHE ALA HIS PHE LEU ARG LEU          
SEQRES  16 C  346  SER SER LEU HIS THR LEU PHE LEU GLN TRP ASN LYS ILE          
SEQRES  17 C  346  SER ASN LEU THR CYS GLY MET GLU TRP THR TRP GLY THR          
SEQRES  18 C  346  LEU GLU LYS LEU ASP LEU THR GLY ASN GLU ILE LYS ALA          
SEQRES  19 C  346  ILE ASP LEU THR VAL PHE GLU THR MET PRO ASN LEU LYS          
SEQRES  20 C  346  ILE LEU LEU MET ASP ASN ASN LYS LEU ASN SER LEU ASP          
SEQRES  21 C  346  SER LYS ILE LEU ASN SER LEU ARG SER LEU THR THR VAL          
SEQRES  22 C  346  GLY LEU SER GLY ASN LEU TRP GLU CYS SER ALA ARG ILE          
SEQRES  23 C  346  CYS ALA LEU ALA SER TRP LEU GLY SER PHE GLN GLY ARG          
SEQRES  24 C  346  TRP GLU HIS SER ILE LEU CYS HIS SER PRO ASP HIS THR          
SEQRES  25 C  346  GLN GLY GLU ASP ILE LEU ASP ALA VAL ALA GLY PHE GLN          
SEQRES  26 C  346  LEU CYS TRP ASN LEU SER THR THR VAL THR VAL MET ALA          
SEQRES  27 C  346  GLY SER HIS HIS HIS HIS HIS HIS                              
SEQRES   1 D  193  ASP ALA ALA SER HIS ALA GLY THR THR TYR ILE PHE SER          
SEQRES   2 D  193  LYS GLY GLY GLY GLN ILE THR TYR LYS TRP PRO PRO ASN          
SEQRES   3 D  193  ASP ARG PRO SER THR ARG ALA ASP ARG LEU ALA ILE GLY          
SEQRES   4 D  193  PHE SER THR VAL GLN LYS GLU ALA VAL LEU VAL ARG VAL          
SEQRES   5 D  193  ASP SER SER SER GLY LEU GLY ASP TYR LEU GLU LEU HIS          
SEQRES   6 D  193  ILE HIS GLN GLY LYS ILE GLY VAL LYS PHE ASN VAL GLY          
SEQRES   7 D  193  THR ASP ASP ILE ALA ILE GLU GLU SER ASN ALA ILE ILE          
SEQRES   8 D  193  ASN ASP GLY LYS TYR HIS VAL VAL ARG PHE THR ARG SER          
SEQRES   9 D  193  GLY GLY ASN ALA THR LEU GLN VAL ASP SER TRP PRO VAL          
SEQRES  10 D  193  ILE GLU ARG TYR PRO ALA GLY ARG GLN LEU THR ILE PHE          
SEQRES  11 D  193  ASN SER GLN ALA THR ILE ILE ILE GLY GLY LYS GLU GLN          
SEQRES  12 D  193  GLY GLN PRO PHE GLN GLY GLN LEU SER GLY LEU TYR TYR          
SEQRES  13 D  193  ASN GLY LEU LYS VAL LEU ASN MET ALA ALA GLU ASN ASP          
SEQRES  14 D  193  ALA ASN ILE ALA ILE VAL GLY ASN VAL ARG LEU VAL GLY          
SEQRES  15 D  193  GLU VAL PRO GLY SER HIS HIS HIS HIS HIS HIS                  
SEQRES   1 E  346  CYS PRO PRO LYS CYS ARG CYS GLU LYS LEU LEU PHE TYR          
SEQRES   2 E  346  CYS ASP SER GLN GLY PHE HIS SER VAL PRO ASN ALA THR          
SEQRES   3 E  346  ASP LYS GLY SER LEU GLY LEU SER LEU ARG HIS ASN HIS          
SEQRES   4 E  346  ILE THR GLU LEU GLU ARG ASP GLN PHE ALA SER PHE SER          
SEQRES   5 E  346  GLN LEU THR TRP LEU HIS LEU ASP HIS ASN GLN ILE SER          
SEQRES   6 E  346  THR VAL LYS GLU ASP ALA PHE GLN GLY LEU TYR LYS LEU          
SEQRES   7 E  346  LYS GLU LEU ILE LEU SER SER ASN LYS ILE PHE TYR LEU          
SEQRES   8 E  346  PRO ASN THR THR PHE THR GLN LEU ILE ASN LEU GLN ASN          
SEQRES   9 E  346  LEU ASP LEU SER PHE ASN GLN LEU SER SER LEU HIS PRO          
SEQRES  10 E  346  GLU LEU PHE TYR GLY LEU ARG LYS LEU GLN THR LEU HIS          
SEQRES  11 E  346  LEU ARG SER ASN SER LEU ARG THR ILE PRO VAL ARG LEU          
SEQRES  12 E  346  PHE TRP ASP CYS ARG SER LEU GLU PHE LEU ASP LEU SER          
SEQRES  13 E  346  THR ASN ARG LEU ARG SER LEU ALA ARG ASN GLY PHE ALA          
SEQRES  14 E  346  GLY LEU ILE LYS LEU ARG GLU LEU HIS LEU GLU HIS ASN          
SEQRES  15 E  346  GLN LEU THR LYS ILE ASN PHE ALA HIS PHE LEU ARG LEU          
SEQRES  16 E  346  SER SER LEU HIS THR LEU PHE LEU GLN TRP ASN LYS ILE          
SEQRES  17 E  346  SER ASN LEU THR CYS GLY MET GLU TRP THR TRP GLY THR          
SEQRES  18 E  346  LEU GLU LYS LEU ASP LEU THR GLY ASN GLU ILE LYS ALA          
SEQRES  19 E  346  ILE ASP LEU THR VAL PHE GLU THR MET PRO ASN LEU LYS          
SEQRES  20 E  346  ILE LEU LEU MET ASP ASN ASN LYS LEU ASN SER LEU ASP          
SEQRES  21 E  346  SER LYS ILE LEU ASN SER LEU ARG SER LEU THR THR VAL          
SEQRES  22 E  346  GLY LEU SER GLY ASN LEU TRP GLU CYS SER ALA ARG ILE          
SEQRES  23 E  346  CYS ALA LEU ALA SER TRP LEU GLY SER PHE GLN GLY ARG          
SEQRES  24 E  346  TRP GLU HIS SER ILE LEU CYS HIS SER PRO ASP HIS THR          
SEQRES  25 E  346  GLN GLY GLU ASP ILE LEU ASP ALA VAL ALA GLY PHE GLN          
SEQRES  26 E  346  LEU CYS TRP ASN LEU SER THR THR VAL THR VAL MET ALA          
SEQRES  27 E  346  GLY SER HIS HIS HIS HIS HIS HIS                              
SEQRES   1 F  193  ASP ALA ALA SER HIS ALA GLY THR THR TYR ILE PHE SER          
SEQRES   2 F  193  LYS GLY GLY GLY GLN ILE THR TYR LYS TRP PRO PRO ASN          
SEQRES   3 F  193  ASP ARG PRO SER THR ARG ALA ASP ARG LEU ALA ILE GLY          
SEQRES   4 F  193  PHE SER THR VAL GLN LYS GLU ALA VAL LEU VAL ARG VAL          
SEQRES   5 F  193  ASP SER SER SER GLY LEU GLY ASP TYR LEU GLU LEU HIS          
SEQRES   6 F  193  ILE HIS GLN GLY LYS ILE GLY VAL LYS PHE ASN VAL GLY          
SEQRES   7 F  193  THR ASP ASP ILE ALA ILE GLU GLU SER ASN ALA ILE ILE          
SEQRES   8 F  193  ASN ASP GLY LYS TYR HIS VAL VAL ARG PHE THR ARG SER          
SEQRES   9 F  193  GLY GLY ASN ALA THR LEU GLN VAL ASP SER TRP PRO VAL          
SEQRES  10 F  193  ILE GLU ARG TYR PRO ALA GLY ARG GLN LEU THR ILE PHE          
SEQRES  11 F  193  ASN SER GLN ALA THR ILE ILE ILE GLY GLY LYS GLU GLN          
SEQRES  12 F  193  GLY GLN PRO PHE GLN GLY GLN LEU SER GLY LEU TYR TYR          
SEQRES  13 F  193  ASN GLY LEU LYS VAL LEU ASN MET ALA ALA GLU ASN ASP          
SEQRES  14 F  193  ALA ASN ILE ALA ILE VAL GLY ASN VAL ARG LEU VAL GLY          
SEQRES  15 F  193  GLU VAL PRO GLY SER HIS HIS HIS HIS HIS HIS                  
SEQRES   1 G  346  CYS PRO PRO LYS CYS ARG CYS GLU LYS LEU LEU PHE TYR          
SEQRES   2 G  346  CYS ASP SER GLN GLY PHE HIS SER VAL PRO ASN ALA THR          
SEQRES   3 G  346  ASP LYS GLY SER LEU GLY LEU SER LEU ARG HIS ASN HIS          
SEQRES   4 G  346  ILE THR GLU LEU GLU ARG ASP GLN PHE ALA SER PHE SER          
SEQRES   5 G  346  GLN LEU THR TRP LEU HIS LEU ASP HIS ASN GLN ILE SER          
SEQRES   6 G  346  THR VAL LYS GLU ASP ALA PHE GLN GLY LEU TYR LYS LEU          
SEQRES   7 G  346  LYS GLU LEU ILE LEU SER SER ASN LYS ILE PHE TYR LEU          
SEQRES   8 G  346  PRO ASN THR THR PHE THR GLN LEU ILE ASN LEU GLN ASN          
SEQRES   9 G  346  LEU ASP LEU SER PHE ASN GLN LEU SER SER LEU HIS PRO          
SEQRES  10 G  346  GLU LEU PHE TYR GLY LEU ARG LYS LEU GLN THR LEU HIS          
SEQRES  11 G  346  LEU ARG SER ASN SER LEU ARG THR ILE PRO VAL ARG LEU          
SEQRES  12 G  346  PHE TRP ASP CYS ARG SER LEU GLU PHE LEU ASP LEU SER          
SEQRES  13 G  346  THR ASN ARG LEU ARG SER LEU ALA ARG ASN GLY PHE ALA          
SEQRES  14 G  346  GLY LEU ILE LYS LEU ARG GLU LEU HIS LEU GLU HIS ASN          
SEQRES  15 G  346  GLN LEU THR LYS ILE ASN PHE ALA HIS PHE LEU ARG LEU          
SEQRES  16 G  346  SER SER LEU HIS THR LEU PHE LEU GLN TRP ASN LYS ILE          
SEQRES  17 G  346  SER ASN LEU THR CYS GLY MET GLU TRP THR TRP GLY THR          
SEQRES  18 G  346  LEU GLU LYS LEU ASP LEU THR GLY ASN GLU ILE LYS ALA          
SEQRES  19 G  346  ILE ASP LEU THR VAL PHE GLU THR MET PRO ASN LEU LYS          
SEQRES  20 G  346  ILE LEU LEU MET ASP ASN ASN LYS LEU ASN SER LEU ASP          
SEQRES  21 G  346  SER LYS ILE LEU ASN SER LEU ARG SER LEU THR THR VAL          
SEQRES  22 G  346  GLY LEU SER GLY ASN LEU TRP GLU CYS SER ALA ARG ILE          
SEQRES  23 G  346  CYS ALA LEU ALA SER TRP LEU GLY SER PHE GLN GLY ARG          
SEQRES  24 G  346  TRP GLU HIS SER ILE LEU CYS HIS SER PRO ASP HIS THR          
SEQRES  25 G  346  GLN GLY GLU ASP ILE LEU ASP ALA VAL ALA GLY PHE GLN          
SEQRES  26 G  346  LEU CYS TRP ASN LEU SER THR THR VAL THR VAL MET ALA          
SEQRES  27 G  346  GLY SER HIS HIS HIS HIS HIS HIS                              
SEQRES   1 H  193  ASP ALA ALA SER HIS ALA GLY THR THR TYR ILE PHE SER          
SEQRES   2 H  193  LYS GLY GLY GLY GLN ILE THR TYR LYS TRP PRO PRO ASN          
SEQRES   3 H  193  ASP ARG PRO SER THR ARG ALA ASP ARG LEU ALA ILE GLY          
SEQRES   4 H  193  PHE SER THR VAL GLN LYS GLU ALA VAL LEU VAL ARG VAL          
SEQRES   5 H  193  ASP SER SER SER GLY LEU GLY ASP TYR LEU GLU LEU HIS          
SEQRES   6 H  193  ILE HIS GLN GLY LYS ILE GLY VAL LYS PHE ASN VAL GLY          
SEQRES   7 H  193  THR ASP ASP ILE ALA ILE GLU GLU SER ASN ALA ILE ILE          
SEQRES   8 H  193  ASN ASP GLY LYS TYR HIS VAL VAL ARG PHE THR ARG SER          
SEQRES   9 H  193  GLY GLY ASN ALA THR LEU GLN VAL ASP SER TRP PRO VAL          
SEQRES  10 H  193  ILE GLU ARG TYR PRO ALA GLY ARG GLN LEU THR ILE PHE          
SEQRES  11 H  193  ASN SER GLN ALA THR ILE ILE ILE GLY GLY LYS GLU GLN          
SEQRES  12 H  193  GLY GLN PRO PHE GLN GLY GLN LEU SER GLY LEU TYR TYR          
SEQRES  13 H  193  ASN GLY LEU LYS VAL LEU ASN MET ALA ALA GLU ASN ASP          
SEQRES  14 H  193  ALA ASN ILE ALA ILE VAL GLY ASN VAL ARG LEU VAL GLY          
SEQRES  15 H  193  GLU VAL PRO GLY SER HIS HIS HIS HIS HIS HIS                  
HET    NAG  I   1      14                                                       
HET    NAG  I   2      14                                                       
HET    FUC  I   3      10                                                       
HET    NAG  J   1      14                                                       
HET    NAG  J   2      14                                                       
HET    FUC  J   3      10                                                       
HET    NAG  K   1      14                                                       
HET    NAG  K   2      14                                                       
HET    FUC  K   3      10                                                       
HET    NAG  L   1      14                                                       
HET    NAG  L   2      14                                                       
HET    FUC  L   3      10                                                       
HET    NAG  A 401      14                                                       
HET    NAG  A 402      14                                                       
HET    NAG  A 403      14                                                       
HET     ZN  A 404       1                                                       
HET     CA  B 301       1                                                       
HET    NAG  C 401      14                                                       
HET    NAG  C 402      14                                                       
HET    NAG  C 403      14                                                       
HET     ZN  C 404       1                                                       
HET     CA  D 301       1                                                       
HET    NAG  E1000      14                                                       
HET    NAG  E1001      14                                                       
HET    NAG  E1002      14                                                       
HET     CA  F 301       1                                                       
HET    NAG  G1000      14                                                       
HET    NAG  G1001      14                                                       
HET    NAG  G1002      14                                                       
HET     CA  H 301       1                                                       
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
HETNAM     FUC ALPHA-L-FUCOPYRANOSE                                             
HETNAM      ZN ZINC ION                                                         
HETNAM      CA CALCIUM ION                                                      
FORMUL   9  NAG    20(C8 H15 N O6)                                              
FORMUL   9  FUC    4(C6 H12 O5)                                                 
FORMUL  16   ZN    2(ZN 2+)                                                     
FORMUL  17   CA    4(CA 2+)                                                     
FORMUL  31  HOH   *4(H2 O)                                                      
HELIX    1 AA1 ALA A  223  LEU A  226  5                                   4    
HELIX    2 AA2 ASP A  293  ASN A  298  1                                   6    
HELIX    3 AA3 SER A  316  ARG A  318  5                                   3    
HELIX    4 AA4 ILE A  319  PHE A  329  1                                  11    
HELIX    5 AA5 PRO A  342  GLN A  346  5                                   5    
HELIX    6 AA6 ASP A  349  PHE A  357  1                                   9    
HELIX    7 AA7 LYS B  241  ALA B  247  1                                   7    
HELIX    8 AA8 ALA C  223  LEU C  226  5                                   4    
HELIX    9 AA9 ASP C  293  ASN C  298  1                                   6    
HELIX   10 AB1 SER C  316  ARG C  318  5                                   3    
HELIX   11 AB2 ILE C  319  PHE C  329  1                                  11    
HELIX   12 AB3 PRO C  342  GLN C  346  5                                   5    
HELIX   13 AB4 ASP C  349  PHE C  357  1                                   9    
HELIX   14 AB5 LYS D  241  ALA D  247  1                                   7    
HELIX   15 AB6 ALA E  223  LEU E  226  5                                   4    
HELIX   16 AB7 ASP E  293  ASN E  298  1                                   6    
HELIX   17 AB8 SER E  316  ARG E  318  5                                   3    
HELIX   18 AB9 ILE E  319  PHE E  329  1                                  11    
HELIX   19 AC1 PRO E  342  GLN E  346  5                                   5    
HELIX   20 AC2 ASP E  349  PHE E  357  1                                   9    
HELIX   21 AC3 LYS F  241  ALA F  247  1                                   7    
HELIX   22 AC4 ALA G  223  LEU G  226  5                                   4    
HELIX   23 AC5 ASP G  293  ASN G  298  1                                   6    
HELIX   24 AC6 SER G  316  ARG G  318  5                                   3    
HELIX   25 AC7 ILE G  319  PHE G  329  1                                  11    
HELIX   26 AC8 PRO G  342  GLN G  346  5                                   5    
HELIX   27 AC9 ASP G  349  PHE G  357  1                                   9    
HELIX   28 AD1 LYS H  241  ALA H  247  1                                   7    
SHEET    1 AA113 LEU A  44  TYR A  46  0                                        
SHEET    2 AA113 GLY A  65  SER A  67  1  O  GLY A  65   N  PHE A  45           
SHEET    3 AA113 TRP A  89  HIS A  91  1  O  HIS A  91   N  LEU A  66           
SHEET    4 AA113 GLU A 113  ILE A 115  1  O  GLU A 113   N  LEU A  90           
SHEET    5 AA113 ASN A 137  ASP A 139  1  O  ASN A 137   N  LEU A 114           
SHEET    6 AA113 THR A 161  HIS A 163  1  O  HIS A 163   N  LEU A 138           
SHEET    7 AA113 PHE A 185  ASP A 187  1  O  ASP A 187   N  LEU A 162           
SHEET    8 AA113 GLU A 209  HIS A 211  1  O  HIS A 211   N  LEU A 186           
SHEET    9 AA113 THR A 233  PHE A 235  1  O  PHE A 235   N  LEU A 210           
SHEET   10 AA113 LYS A 257  ASP A 259  1  O  ASP A 259   N  LEU A 234           
SHEET   11 AA113 ILE A 281  LEU A 283  1  O  ILE A 281   N  LEU A 258           
SHEET   12 AA113 THR A 305  GLY A 307  1  O  THR A 305   N  LEU A 282           
SHEET   13 AA113 ARG A 332  TRP A 333  1  O  ARG A 332   N  VAL A 306           
SHEET    1 AA2 2 GLU A  75  LEU A  76  0                                        
SHEET    2 AA2 2 THR A  99  VAL A 100  1  O  THR A  99   N  LEU A  76           
SHEET    1 AA3 3 LYS A 219  ASN A 221  0                                        
SHEET    2 AA3 3 ASN A 243  THR A 245  1  O  THR A 245   N  ILE A 220           
SHEET    3 AA3 3 ALA A 267  ILE A 268  1  O  ALA A 267   N  LEU A 244           
SHEET    1 AA411 ASP B 162  GLU B 166  0                                        
SHEET    2 AA411 LYS B 151  ASN B 157 -1  N  VAL B 154   O  ILE B 165           
SHEET    3 AA411 TYR B 142  HIS B 148 -1  N  GLU B 144   O  LYS B 155           
SHEET    4 AA411 GLU B 127  SER B 135 -1  N  VAL B 131   O  LEU B 145           
SHEET    5 AA411 GLN B 214  ILE B 219 -1  O  ILE B 218   N  ARG B 132           
SHEET    6 AA411 THR B  90  LYS B 103 -1  N  ILE B 100   O  ILE B 219           
SHEET    7 AA411 GLY B 230  TYR B 237 -1  O  GLY B 230   N  PHE B  93           
SHEET    8 AA411 ALA B 114  THR B 123 -1  N  GLY B 120   O  SER B 233           
SHEET    9 AA411 HIS B 178  SER B 185 -1  O  PHE B 182   N  LEU B 117           
SHEET   10 AA411 ASN B 188  GLN B 192 -1  O  THR B 190   N  THR B 183           
SHEET   11 AA411 ILE B 199  ARG B 201 -1  O  ILE B 199   N  LEU B 191           
SHEET    1 AA5 7 ASP B 162  GLU B 166  0                                        
SHEET    2 AA5 7 LYS B 151  ASN B 157 -1  N  VAL B 154   O  ILE B 165           
SHEET    3 AA5 7 TYR B 142  HIS B 148 -1  N  GLU B 144   O  LYS B 155           
SHEET    4 AA5 7 GLU B 127  SER B 135 -1  N  VAL B 131   O  LEU B 145           
SHEET    5 AA5 7 GLN B 214  ILE B 219 -1  O  ILE B 218   N  ARG B 132           
SHEET    6 AA5 7 THR B  90  LYS B 103 -1  N  ILE B 100   O  ILE B 219           
SHEET    7 AA5 7 ALA B 254  ARG B 260 -1  O  ARG B 260   N  ILE B  92           
SHEET    1 AA613 LEU C  44  TYR C  46  0                                        
SHEET    2 AA613 GLY C  65  SER C  67  1  O  GLY C  65   N  PHE C  45           
SHEET    3 AA613 TRP C  89  HIS C  91  1  O  HIS C  91   N  LEU C  66           
SHEET    4 AA613 GLU C 113  ILE C 115  1  O  GLU C 113   N  LEU C  90           
SHEET    5 AA613 ASN C 137  ASP C 139  1  O  ASN C 137   N  LEU C 114           
SHEET    6 AA613 THR C 161  HIS C 163  1  O  HIS C 163   N  LEU C 138           
SHEET    7 AA613 PHE C 185  ASP C 187  1  O  ASP C 187   N  LEU C 162           
SHEET    8 AA613 GLU C 209  HIS C 211  1  O  HIS C 211   N  LEU C 186           
SHEET    9 AA613 THR C 233  PHE C 235  1  O  PHE C 235   N  LEU C 210           
SHEET   10 AA613 LYS C 257  ASP C 259  1  O  ASP C 259   N  LEU C 234           
SHEET   11 AA613 ILE C 281  LEU C 283  1  O  ILE C 281   N  LEU C 258           
SHEET   12 AA613 THR C 305  GLY C 307  1  O  THR C 305   N  LEU C 282           
SHEET   13 AA613 ARG C 332  TRP C 333  1  O  ARG C 332   N  VAL C 306           
SHEET    1 AA7 2 GLU C  75  LEU C  76  0                                        
SHEET    2 AA7 2 THR C  99  VAL C 100  1  O  THR C  99   N  LEU C  76           
SHEET    1 AA8 3 LYS C 219  ASN C 221  0                                        
SHEET    2 AA8 3 ASN C 243  THR C 245  1  O  THR C 245   N  ILE C 220           
SHEET    3 AA8 3 ALA C 267  ILE C 268  1  O  ALA C 267   N  LEU C 244           
SHEET    1 AA911 ASP D 162  GLU D 166  0                                        
SHEET    2 AA911 LYS D 151  ASN D 157 -1  N  VAL D 154   O  ILE D 165           
SHEET    3 AA911 TYR D 142  HIS D 148 -1  N  GLU D 144   O  LYS D 155           
SHEET    4 AA911 GLU D 127  SER D 135 -1  N  VAL D 131   O  LEU D 145           
SHEET    5 AA911 GLN D 214  ILE D 219 -1  O  ILE D 218   N  ARG D 132           
SHEET    6 AA911 THR D  90  LYS D 103 -1  N  ILE D 100   O  ILE D 219           
SHEET    7 AA911 GLY D 230  TYR D 237 -1  O  GLY D 230   N  PHE D  93           
SHEET    8 AA911 ALA D 114  THR D 123 -1  N  GLY D 120   O  SER D 233           
SHEET    9 AA911 HIS D 178  SER D 185 -1  O  PHE D 182   N  LEU D 117           
SHEET   10 AA911 ASN D 188  GLN D 192 -1  O  THR D 190   N  THR D 183           
SHEET   11 AA911 ILE D 199  ARG D 201 -1  O  ILE D 199   N  LEU D 191           
SHEET    1 AB1 7 ASP D 162  GLU D 166  0                                        
SHEET    2 AB1 7 LYS D 151  ASN D 157 -1  N  VAL D 154   O  ILE D 165           
SHEET    3 AB1 7 TYR D 142  HIS D 148 -1  N  GLU D 144   O  LYS D 155           
SHEET    4 AB1 7 GLU D 127  SER D 135 -1  N  VAL D 131   O  LEU D 145           
SHEET    5 AB1 7 GLN D 214  ILE D 219 -1  O  ILE D 218   N  ARG D 132           
SHEET    6 AB1 7 THR D  90  LYS D 103 -1  N  ILE D 100   O  ILE D 219           
SHEET    7 AB1 7 ALA D 254  ARG D 260 -1  O  ARG D 260   N  ILE D  92           
SHEET    1 AB213 LEU E  44  TYR E  46  0                                        
SHEET    2 AB213 GLY E  65  SER E  67  1  O  GLY E  65   N  PHE E  45           
SHEET    3 AB213 TRP E  89  HIS E  91  1  O  HIS E  91   N  LEU E  66           
SHEET    4 AB213 GLU E 113  ILE E 115  1  O  GLU E 113   N  LEU E  90           
SHEET    5 AB213 ASN E 137  ASP E 139  1  O  ASN E 137   N  LEU E 114           
SHEET    6 AB213 THR E 161  HIS E 163  1  O  HIS E 163   N  LEU E 138           
SHEET    7 AB213 PHE E 185  ASP E 187  1  O  ASP E 187   N  LEU E 162           
SHEET    8 AB213 GLU E 209  HIS E 211  1  O  HIS E 211   N  LEU E 186           
SHEET    9 AB213 THR E 233  PHE E 235  1  O  PHE E 235   N  LEU E 210           
SHEET   10 AB213 LYS E 257  ASP E 259  1  O  ASP E 259   N  LEU E 234           
SHEET   11 AB213 ILE E 281  LEU E 283  1  O  ILE E 281   N  LEU E 258           
SHEET   12 AB213 THR E 305  GLY E 307  1  O  THR E 305   N  LEU E 282           
SHEET   13 AB213 ARG E 332  TRP E 333  1  O  ARG E 332   N  VAL E 306           
SHEET    1 AB3 2 GLU E  75  LEU E  76  0                                        
SHEET    2 AB3 2 THR E  99  VAL E 100  1  O  THR E  99   N  LEU E  76           
SHEET    1 AB4 3 LYS E 219  ASN E 221  0                                        
SHEET    2 AB4 3 ASN E 243  THR E 245  1  O  THR E 245   N  ILE E 220           
SHEET    3 AB4 3 ALA E 267  ILE E 268  1  O  ALA E 267   N  LEU E 244           
SHEET    1 AB511 ASP F 162  GLU F 166  0                                        
SHEET    2 AB511 LYS F 151  ASN F 157 -1  N  VAL F 154   O  ILE F 165           
SHEET    3 AB511 TYR F 142  HIS F 148 -1  N  GLU F 144   O  LYS F 155           
SHEET    4 AB511 GLU F 127  SER F 135 -1  N  VAL F 133   O  LEU F 143           
SHEET    5 AB511 GLN F 214  ILE F 219 -1  O  ILE F 218   N  ARG F 132           
SHEET    6 AB511 THR F  90  LYS F 103 -1  N  ILE F 100   O  ILE F 219           
SHEET    7 AB511 GLY F 230  TYR F 237 -1  O  GLY F 230   N  PHE F  93           
SHEET    8 AB511 ALA F 114  THR F 123 -1  N  GLY F 120   O  SER F 233           
SHEET    9 AB511 HIS F 178  SER F 185 -1  O  PHE F 182   N  LEU F 117           
SHEET   10 AB511 ASN F 188  GLN F 192 -1  O  THR F 190   N  THR F 183           
SHEET   11 AB511 ILE F 199  ARG F 201 -1  O  ILE F 199   N  LEU F 191           
SHEET    1 AB6 7 ASP F 162  GLU F 166  0                                        
SHEET    2 AB6 7 LYS F 151  ASN F 157 -1  N  VAL F 154   O  ILE F 165           
SHEET    3 AB6 7 TYR F 142  HIS F 148 -1  N  GLU F 144   O  LYS F 155           
SHEET    4 AB6 7 GLU F 127  SER F 135 -1  N  VAL F 133   O  LEU F 143           
SHEET    5 AB6 7 GLN F 214  ILE F 219 -1  O  ILE F 218   N  ARG F 132           
SHEET    6 AB6 7 THR F  90  LYS F 103 -1  N  ILE F 100   O  ILE F 219           
SHEET    7 AB6 7 ALA F 254  ARG F 260 -1  O  ARG F 260   N  ILE F  92           
SHEET    1 AB713 LEU G  44  TYR G  46  0                                        
SHEET    2 AB713 GLY G  65  SER G  67  1  O  GLY G  65   N  PHE G  45           
SHEET    3 AB713 TRP G  89  HIS G  91  1  O  HIS G  91   N  LEU G  66           
SHEET    4 AB713 GLU G 113  ILE G 115  1  O  GLU G 113   N  LEU G  90           
SHEET    5 AB713 ASN G 137  ASP G 139  1  O  ASN G 137   N  LEU G 114           
SHEET    6 AB713 THR G 161  HIS G 163  1  O  HIS G 163   N  LEU G 138           
SHEET    7 AB713 PHE G 185  ASP G 187  1  O  ASP G 187   N  LEU G 162           
SHEET    8 AB713 GLU G 209  HIS G 211  1  O  HIS G 211   N  LEU G 186           
SHEET    9 AB713 THR G 233  PHE G 235  1  O  PHE G 235   N  LEU G 210           
SHEET   10 AB713 LYS G 257  ASP G 259  1  O  ASP G 259   N  LEU G 234           
SHEET   11 AB713 ILE G 281  LEU G 283  1  O  ILE G 281   N  LEU G 258           
SHEET   12 AB713 THR G 305  GLY G 307  1  O  THR G 305   N  LEU G 282           
SHEET   13 AB713 ARG G 332  TRP G 333  1  O  ARG G 332   N  VAL G 306           
SHEET    1 AB8 2 GLU G  75  LEU G  76  0                                        
SHEET    2 AB8 2 THR G  99  VAL G 100  1  O  THR G  99   N  LEU G  76           
SHEET    1 AB9 3 LYS G 219  ASN G 221  0                                        
SHEET    2 AB9 3 ASN G 243  THR G 245  1  O  THR G 245   N  ILE G 220           
SHEET    3 AB9 3 ALA G 267  ILE G 268  1  O  ALA G 267   N  LEU G 244           
SHEET    1 AC111 ASP H 162  GLU H 166  0                                        
SHEET    2 AC111 LYS H 151  ASN H 157 -1  N  VAL H 154   O  ILE H 165           
SHEET    3 AC111 TYR H 142  HIS H 148 -1  N  GLU H 144   O  LYS H 155           
SHEET    4 AC111 GLU H 127  SER H 135 -1  N  VAL H 133   O  LEU H 143           
SHEET    5 AC111 GLN H 214  ILE H 219 -1  O  ILE H 218   N  ARG H 132           
SHEET    6 AC111 THR H  90  LYS H 103 -1  N  ILE H 100   O  ILE H 219           
SHEET    7 AC111 GLY H 230  TYR H 237 -1  O  GLY H 230   N  PHE H  93           
SHEET    8 AC111 ALA H 114  THR H 123 -1  N  GLY H 120   O  SER H 233           
SHEET    9 AC111 HIS H 178  SER H 185 -1  O  PHE H 182   N  LEU H 117           
SHEET   10 AC111 ASN H 188  GLN H 192 -1  O  THR H 190   N  THR H 183           
SHEET   11 AC111 ILE H 199  ARG H 201 -1  O  ILE H 199   N  LEU H 191           
SHEET    1 AC2 7 ASP H 162  GLU H 166  0                                        
SHEET    2 AC2 7 LYS H 151  ASN H 157 -1  N  VAL H 154   O  ILE H 165           
SHEET    3 AC2 7 TYR H 142  HIS H 148 -1  N  GLU H 144   O  LYS H 155           
SHEET    4 AC2 7 GLU H 127  SER H 135 -1  N  VAL H 133   O  LEU H 143           
SHEET    5 AC2 7 GLN H 214  ILE H 219 -1  O  ILE H 218   N  ARG H 132           
SHEET    6 AC2 7 THR H  90  LYS H 103 -1  N  ILE H 100   O  ILE H 219           
SHEET    7 AC2 7 ALA H 254  ARG H 260 -1  O  ARG H 260   N  ILE H  92           
SSBOND   1 CYS A   34    CYS A   40                          1555   1555  2.03  
SSBOND   2 CYS A   38    CYS A   47                          1555   1555  2.03  
SSBOND   3 CYS A  315    CYS A  339                          1555   1555  2.03  
SSBOND   4 CYS A  320    CYS A  360                          1555   1555  2.03  
SSBOND   5 CYS C   34    CYS C   40                          1555   1555  2.03  
SSBOND   6 CYS C   38    CYS C   47                          1555   1555  2.03  
SSBOND   7 CYS C  315    CYS C  339                          1555   1555  2.02  
SSBOND   8 CYS C  320    CYS C  360                          1555   1555  2.03  
SSBOND   9 CYS E   34    CYS E   40                          1555   1555  2.03  
SSBOND  10 CYS E   38    CYS E   47                          1555   1555  2.03  
SSBOND  11 CYS E  315    CYS E  339                          1555   1555  2.03  
SSBOND  12 CYS E  320    CYS E  360                          1555   1555  2.03  
SSBOND  13 CYS G   34    CYS G   40                          1555   1555  2.03  
SSBOND  14 CYS G   38    CYS G   47                          1555   1555  2.03  
SSBOND  15 CYS G  315    CYS G  339                          1555   1555  2.03  
SSBOND  16 CYS G  320    CYS G  360                          1555   1555  2.03  
LINK         ND2 ASN A  57                 C1  NAG A 403     1555   1555  1.45  
LINK         ND2 ASN A 126                 C1  NAG A 402     1555   1555  1.43  
LINK         ND2 ASN A 243                 C1  NAG A 401     1555   1555  1.44  
LINK         ND2 ASN B 188                 C1  NAG I   1     1555   1555  1.42  
LINK         ND2 ASN C  57                 C1  NAG C 403     1555   1555  1.45  
LINK         ND2 ASN C 126                 C1  NAG C 402     1555   1555  1.43  
LINK         ND2 ASN C 243                 C1  NAG C 401     1555   1555  1.44  
LINK         ND2 ASN D 188                 C1  NAG J   1     1555   1555  1.42  
LINK         ND2 ASN E  57                 C1  NAG E1002     1555   1555  1.45  
LINK         ND2 ASN E 126                 C1  NAG E1001     1555   1555  1.43  
LINK         ND2 ASN E 243                 C1  NAG E1000     1555   1555  1.44  
LINK         ND2 ASN F 188                 C1  NAG K   1     1555   1555  1.42  
LINK         ND2 ASN G  57                 C1  NAG G1002     1555   1555  1.45  
LINK         ND2 ASN G 126                 C1  NAG G1001     1555   1555  1.43  
LINK         ND2 ASN G 243                 C1  NAG G1000     1555   1555  1.44  
LINK         ND2 ASN H 188                 C1  NAG L   1     1555   1555  1.42  
LINK         O4  NAG I   1                 C1  NAG I   2     1555   1555  1.43  
LINK         O6  NAG I   1                 C1  FUC I   3     1555   1555  1.45  
LINK         O4  NAG J   1                 C1  NAG J   2     1555   1555  1.44  
LINK         O6  NAG J   1                 C1  FUC J   3     1555   1555  1.45  
LINK         O4  NAG K   1                 C1  NAG K   2     1555   1555  1.44  
LINK         O6  NAG K   1                 C1  FUC K   3     1555   1555  1.45  
LINK         O4  NAG L   1                 C1  NAG L   2     1555   1555  1.44  
LINK         O6  NAG L   1                 C1  FUC L   3     1555   1555  1.45  
LINK         NE2 HIS A  53                ZN    ZN A 404     1555   1555  2.03  
LINK         ND1 HIS A  72                ZN    ZN A 404     1555   1555  2.03  
LINK        ZN    ZN A 404                 NE2 HIS E  53     1555   1555  2.02  
LINK        ZN    ZN A 404                 ND1 HIS E  72     1555   1555  2.02  
LINK         OD1 ASP B 141                CA    CA B 301     1555   1555  2.36  
LINK         OD2 ASP B 141                CA    CA B 301     1555   1555  2.37  
LINK         O   VAL B 158                CA    CA B 301     1555   1555  2.40  
LINK         O   ILE B 210                CA    CA B 301     1555   1555  2.40  
LINK         OD1 ASN B 212                CA    CA B 301     1555   1555  2.38  
LINK        CA    CA B 301                 O   HOH B 401     1555   1555  2.39  
LINK         NE2 HIS C  53                ZN    ZN C 404     1555   1555  2.01  
LINK         ND1 HIS C  72                ZN    ZN C 404     1555   1555  1.99  
LINK        ZN    ZN C 404                 NE2 HIS G  53     1555   1555  2.01  
LINK        ZN    ZN C 404                 ND1 HIS G  72     1555   1555  2.00  
LINK         O   HOH C 501                CA    CA D 301     1555   1555  2.39  
LINK         OD1 ASP D 141                CA    CA D 301     1555   1555  2.35  
LINK         OD2 ASP D 141                CA    CA D 301     1555   1555  2.37  
LINK         O   VAL D 158                CA    CA D 301     1555   1555  2.40  
LINK         O   ILE D 210                CA    CA D 301     1555   1555  2.39  
LINK         OD1 ASN D 212                CA    CA D 301     1555   1555  2.38  
LINK         OD1 ASP F 141                CA    CA F 301     1555   1555  2.36  
LINK         OD2 ASP F 141                CA    CA F 301     1555   1555  2.37  
LINK         O   VAL F 158                CA    CA F 301     1555   1555  2.40  
LINK         O   ILE F 210                CA    CA F 301     1555   1555  2.39  
LINK         OD1 ASN F 212                CA    CA F 301     1555   1555  2.38  
LINK        CA    CA F 301                 O   HOH F 401     1555   1555  2.39  
LINK         OD1 ASP H 141                CA    CA H 301     1555   1555  2.35  
LINK         OD2 ASP H 141                CA    CA H 301     1555   1555  2.37  
LINK         O   VAL H 158                CA    CA H 301     1555   1555  2.40  
LINK         O   ILE H 210                CA    CA H 301     1555   1555  2.39  
LINK         OD1 ASN H 212                CA    CA H 301     1555   1555  2.38  
LINK        CA    CA H 301                 O   HOH H 401     1555   1555  2.39  
CISPEP   1 SER A  341    PRO A  342          0        -0.65                     
CISPEP   2 SER C  341    PRO C  342          0        -0.52                     
CISPEP   3 SER E  341    PRO E  342          0        -0.19                     
CISPEP   4 SER G  341    PRO G  342          0        -0.35                     
CRYST1   99.184   99.858  109.633  91.30  91.20 116.47 P 1           4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.010082  0.005020  0.000390        0.00000                         
SCALE2      0.000000  0.011187  0.000401        0.00000                         
SCALE3      0.000000  0.000000  0.009129        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system