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Database: PDB
Entry: 3ZYI
LinkDB: 3ZYI
Original site: 3ZYI 
HEADER    CELL ADHESION                           23-AUG-11   3ZYI              
TITLE     NETRING2 IN COMPLEX WITH NGL2                                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: LEUCINE-RICH REPEAT-CONTAINING PROTEIN 4;                  
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: LRR AND IG DOMAINS, RESIDUES 1-444;                        
COMPND   5 SYNONYM: BRAIN TUMOR-ASSOCIATED PROTEIN BAG, NASOPHARYNGEAL          
COMPND   6  CARCINOMA-ASSOCIATED GENE 14 PROTEIN, NETRIN-G2 LIGAND, NGL-2;      
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: NETRIN-G2;                                                 
COMPND  10 CHAIN: B;                                                            
COMPND  11 FRAGMENT: LAM AND EGF1 DOMAINS, RESIDUES 423-767;                    
COMPND  12 SYNONYM: LAMINET-2, NETRING2;                                        
COMPND  13 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE   6 EXPRESSION_SYSTEM_COMMON: HUMAN;                                     
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE   8 EXPRESSION_SYSTEM_CELL_LINE: HEK 293 GNTI(-);                        
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PHLSEC;                                   
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  12 ORGANISM_COMMON: HUMAN;                                              
SOURCE  13 ORGANISM_TAXID: 9606;                                                
SOURCE  14 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE  15 EXPRESSION_SYSTEM_COMMON: HUMAN;                                     
SOURCE  16 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE  17 EXPRESSION_SYSTEM_CELL_LINE: 293 HEK GNTI (-);                       
SOURCE  18 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  19 EXPRESSION_SYSTEM_PLASMID: PHLSEC                                    
KEYWDS    CELL ADHESION, LRRC4 COMPLEX, SYNAPSE                                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    E.SEIRADAKE,C.H.COLES,P.V.PERESTENKO,K.HARLOS,R.A.J.MCILHINNEY,       
AUTHOR   2 A.R.ARICESCU,E.Y.JONES                                               
REVDAT   2   16-NOV-11 3ZYI    1       JRNL                                     
REVDAT   1   05-OCT-11 3ZYI    0                                                
JRNL        AUTH   E.SEIRADAKE,C.H.COLES,P.V.PERESTENKO,K.HARLOS,               
JRNL        AUTH 2 R.A.J.MCILHINNEY,A.R.ARICESCU,E.Y.JONES                      
JRNL        TITL   STRUCTURAL BASIS FOR CELL SURFACE PATTERNING THROUGH         
JRNL        TITL 2 NETRING-NGL INTERACTIONS                                     
JRNL        REF    EMBO J.                       V.  30  4479 2011              
JRNL        REFN                   ISSN 0261-4189                               
JRNL        PMID   21946559                                                     
JRNL        DOI    10.1038/EMBOJ.2011.346                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER 2.9.2                                         
REMARK   3   AUTHORS     : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,              
REMARK   3               : PACIOREK,ROVERSI,SMART,VONRHEIN,WOMACK,              
REMARK   3               : MATTHEWS,TEN EYCK,TRONRUD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 28.95                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.0                            
REMARK   3   COMPLETENESS FOR RANGE        (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 28340                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD           : THROUGHOUT                     
REMARK   3   FREE R VALUE TEST SET SELECTION   : RANDOM                         
REMARK   3   R VALUE     (WORKING + TEST SET)  : 0.2456                         
REMARK   3   R VALUE            (WORKING SET)  : 0.2434                         
REMARK   3   FREE R VALUE                      : 0.2868                         
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 5.08                           
REMARK   3   FREE R VALUE TEST SET COUNT       : 1439                           
REMARK   3   ESTIMATED ERROR OF FREE R VALUE   : NULL                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED               : 14                       
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 2.60                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 2.70                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : NULL                     
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 2924                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2846                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 2771                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2816                   
REMARK   3   BIN FREE R VALUE                        : 0.3433                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 5.23                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 153                      
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE     : NULL                     
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5411                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 39                                      
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 67.21                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 58.89                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -25.3293                                             
REMARK   3    B22 (A**2) : 26.7385                                              
REMARK   3    B33 (A**2) : -1.4092                                              
REMARK   3    B12 (A**2) : 0.0000                                               
REMARK   3    B13 (A**2) : 0.0000                                               
REMARK   3    B23 (A**2) : 0.0000                                               
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : 0.460               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : NULL                
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : NULL                
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : NULL                
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : NULL                
REMARK   3                                                                      
REMARK   3   REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797                
REMARK   3               CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601     
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.8699                        
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.8368                        
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 5596   ; 2.00   ; HARMONIC            
REMARK   3    BOND ANGLES               : 7625   ; 2.00   ; HARMONIC            
REMARK   3    TORSION ANGLES            : 1845   ; 2.00   ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 131    ; 2.00   ; HARMONIC            
REMARK   3    GENERAL PLANES            : 840    ; 5.00   ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 5596   ; 20.00  ; HARMONIC            
REMARK   3    BAD NON-BONDED CONTACTS   : 0      ; 5.00   ; SEMIHARMONIC        
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL                
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : 724    ; 5.00   ; SEMIHARMONIC        
REMARK   3    SUM OF OCCUPANCIES        : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY DISTANCES         : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY ANGLES            : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY TORSION           : NULL   ; NULL   ; NULL                
REMARK   3    IDEAL-DIST CONTACT TERM   : 5745   ; 4.00   ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.008                    
REMARK   3    BOND ANGLES                  (DEGREES) : 1.00                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.14                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 18.28                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3ZYI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 22-AUG-11.                  
REMARK 100 THE PDBE ID CODE IS EBI-49432.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.976300                           
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 28390                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.60                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 29.00                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.0                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.7                               
REMARK 200  DATA REDUNDANCY                : 9.2                                
REMARK 200  R MERGE                    (I) : 0.16                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 16.60                              
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.70                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.3                                
REMARK 200  R MERGE FOR SHELL          (I) : 1.18                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.10                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 3ZYG                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 50.89                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.50                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 50% V/V 2-METHYL-2,                      
REMARK 280  4-PENTANEDIOL, 0.2 M AMMONIUM DI-HYDROGEN PHOSPHATE, 0.1 M          
REMARK 280  TRIS PH 8.5.                                                        
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X,Y,-Z                                                 
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z+1/2                                     
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       37.71000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       76.69500            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       79.36500            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       37.71000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       76.69500            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       79.36500            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       37.71000            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       76.69500            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       79.36500            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       37.71000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       76.69500            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       79.36500            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3040 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 31920 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.9 KCAL/MOL                         
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 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     MET A     1                                                      
REMARK 465     LYS A     2                                                      
REMARK 465     LEU A     3                                                      
REMARK 465     LEU A     4                                                      
REMARK 465     TRP A     5                                                      
REMARK 465     GLN A     6                                                      
REMARK 465     VAL A     7                                                      
REMARK 465     THR A     8                                                      
REMARK 465     VAL A     9                                                      
REMARK 465     HIS A    10                                                      
REMARK 465     HIS A    11                                                      
REMARK 465     HIS A    12                                                      
REMARK 465     THR A    13                                                      
REMARK 465     TRP A    14                                                      
REMARK 465     ASN A    15                                                      
REMARK 465     ALA A    16                                                      
REMARK 465     ILE A    17                                                      
REMARK 465     LEU A    18                                                      
REMARK 465     LEU A    19                                                      
REMARK 465     PRO A    20                                                      
REMARK 465     PHE A    21                                                      
REMARK 465     VAL A    22                                                      
REMARK 465     TYR A    23                                                      
REMARK 465     LEU A    24                                                      
REMARK 465     THR A    25                                                      
REMARK 465     ALA A    26                                                      
REMARK 465     GLN A    27                                                      
REMARK 465     VAL A    28                                                      
REMARK 465     TRP A    29                                                      
REMARK 465     ILE A    30                                                      
REMARK 465     LEU A    31                                                      
REMARK 465     CYS A    32                                                      
REMARK 465     ALA A    33                                                      
REMARK 465     ALA A    34                                                      
REMARK 465     ILE A    35                                                      
REMARK 465     ALA A    36                                                      
REMARK 465     ALA A    37                                                      
REMARK 465     ALA A    38                                                      
REMARK 465     ALA A    39                                                      
REMARK 465     SER A    40                                                      
REMARK 465     ALA A    41                                                      
REMARK 465     GLY A    42                                                      
REMARK 465     PRO A    43                                                      
REMARK 465     PRO A   320                                                      
REMARK 465     THR A   321                                                      
REMARK 465     ASN A   322                                                      
REMARK 465     SER A   442                                                      
REMARK 465     THR A   443                                                      
REMARK 465     ALA A   444                                                      
REMARK 465     GLY A   445                                                      
REMARK 465     THR A   446                                                      
REMARK 465     HIS A   447                                                      
REMARK 465     HIS A   448                                                      
REMARK 465     HIS A   449                                                      
REMARK 465     HIS A   450                                                      
REMARK 465     HIS A   451                                                      
REMARK 465     HIS A   452                                                      
REMARK 465     MET B     1                                                      
REMARK 465     LEU B     2                                                      
REMARK 465     HIS B     3                                                      
REMARK 465     LEU B     4                                                      
REMARK 465     LEU B     5                                                      
REMARK 465     ALA B     6                                                      
REMARK 465     LEU B     7                                                      
REMARK 465     PHE B     8                                                      
REMARK 465     LEU B     9                                                      
REMARK 465     HIS B    10                                                      
REMARK 465     CYS B    11                                                      
REMARK 465     LEU B    12                                                      
REMARK 465     PRO B    13                                                      
REMARK 465     LEU B    14                                                      
REMARK 465     ALA B    15                                                      
REMARK 465     SER B    16                                                      
REMARK 465     GLY B    17                                                      
REMARK 465     VAL B    26                                                      
REMARK 465     THR B    27                                                      
REMARK 465     THR B    28                                                      
REMARK 465     ASP B    29                                                      
REMARK 465     GLU B    30                                                      
REMARK 465     GLY B    31                                                      
REMARK 465     PRO B    32                                                      
REMARK 465     THR B    33                                                      
REMARK 465     SER B   188                                                      
REMARK 465     SER B   189                                                      
REMARK 465     ALA B   190                                                      
REMARK 465     HIS B   191                                                      
REMARK 465     PHE B   222                                                      
REMARK 465     ALA B   223                                                      
REMARK 465     GLY B   224                                                      
REMARK 465     PRO B   225                                                      
REMARK 465     ASP B   226                                                      
REMARK 465     LEU B   227                                                      
REMARK 465     ARG B   228                                                      
REMARK 465     ASN B   229                                                      
REMARK 465     MET B   230                                                      
REMARK 465     ASP B   231                                                      
REMARK 465     ASN B   232                                                      
REMARK 465     LEU B   233                                                      
REMARK 465     TYR B   234                                                      
REMARK 465     THR B   235                                                      
REMARK 465     ARG B   236                                                      
REMARK 465     HIS B   348                                                      
REMARK 465     HIS B   349                                                      
REMARK 465     HIS B   350                                                      
REMARK 465     HIS B   351                                                      
REMARK 465     HIS B   352                                                      
REMARK 465     HIS B   353                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLN A  44    CG   CD   OE1  NE2                                  
REMARK 470     LYS A  58    CG   CD   CE   NZ                                   
REMARK 470     ARG A  63    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A  64    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A  78    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A  84    CG   CD   OE1  OE2                                  
REMARK 470     ARG A  96    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 108    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 148    CG   CD   CE   NZ                                   
REMARK 470     LYS A 182    CG   CD   CE   NZ                                   
REMARK 470     ARG A 290    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 317    CG   CD   OE1  OE2                                  
REMARK 470     ILE A 319    CG1  CG2  CD1                                       
REMARK 470     VAL A 441    CG1  CG2                                            
REMARK 470     ASP B  18    CG   OD1  OD2                                       
REMARK 470     LYS B  23    CG   CD   CE   NZ                                   
REMARK 470     SER B  24    OG                                                  
REMARK 470     TRP B  25    CG   CD1  CD2  NE1  CE2  CE3  CZ2  CZ3              
REMARK 470     TRP B  25    CH2                                                 
REMARK 470     LYS B  42    CG   CD   CE   NZ                                   
REMARK 470     GLU B  80    CG   CD   OE1  OE2                                  
REMARK 470     LYS B  98    CG   CD   CE   NZ                                   
REMARK 470     GLU B 101    CG   CD   OE1  OE2                                  
REMARK 470     ARG B 159    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     SER B 187    OG                                                  
REMARK 470     ARG B 192    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B 201    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 206    CG   CD   CE   NZ                                   
REMARK 470     LYS B 207    CG   CD   CE   NZ                                   
REMARK 470     LEU B 237    CG   CD1  CD2                                       
REMARK 470     GLU B 238    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 241    CG   CD   CE   NZ                                   
REMARK 470     LEU B 243    CG   CD1  CD2                                       
REMARK 470     LYS B 244    CG   CD   CE   NZ                                   
REMARK 470     GLU B 245    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 300    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 320    CG   CD   CE   NZ                                   
REMARK 470     ARG B 326    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU B 334    CG   CD1  CD2                                       
REMARK 470     LEU B 336    CG   CD1  CD2                                       
REMARK 470     HIS B 338    CG   ND1  CD2  CE1  NE2                             
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   O    LYS B   321     O2   PO4 A  1444     8555     1.72            
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    PHE A  56       -2.36     86.99                                   
REMARK 500    ASN A 133     -168.69   -116.64                                   
REMARK 500    GLU A 144      -78.24    -89.06                                   
REMARK 500    TYR A 145       69.69   -109.88                                   
REMARK 500    LEU A 146       54.45   -118.69                                   
REMARK 500    PRO A 158       34.36    -75.34                                   
REMARK 500    PHE A 167       -0.33     71.95                                   
REMARK 500    ASN A 228     -158.86   -110.25                                   
REMARK 500    LEU A 241       56.43   -104.61                                   
REMARK 500    ASN A 251       47.52     32.21                                   
REMARK 500    ASP A 305     -161.38   -107.98                                   
REMARK 500    CYS A 374       70.33   -151.50                                   
REMARK 500    ARG A 400      -50.58   -122.79                                   
REMARK 500    SER A 412      -55.61     69.94                                   
REMARK 500    CYS B  77       66.45   -119.87                                   
REMARK 500    TRP B 112       45.41    -76.63                                   
REMARK 500    ASN B 157       14.16     51.82                                   
REMARK 500    ASP B 184       75.27   -100.65                                   
REMARK 500    GLU B 214       84.90    -68.63                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN                            
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE                   
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    CYS A 326        24.8      L          L   OUTSIDE RANGE           
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 B1349  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B  97   OD1                                                    
REMARK 620 2 THR B 105   OG1  60.9                                              
REMARK 620 3 GLU B  99   OE2 112.9  71.8                                        
REMARK 620 4 LEU B  94   O    78.4  94.3 152.1                                  
REMARK 620 5 THR B 105   O   120.0  67.8  76.0  76.3                            
REMARK 620 6 SER B 279   O   151.4 143.2  93.4  83.4  76.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A1443                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A1444                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA B1349                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN A OF SUGAR BOUND TO ASN A   
REMARK 800   363 RESIDUES 1442 TO 1442                                          
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN B OF MONO-SACCHARIDE  NAG   
REMARK 800   B1348 BOUND TO ASN B 122                                           
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3ZYG   RELATED DB: PDB                                   
REMARK 900  NETRING2 LAM AND EGF1 DOMAINS                                       
REMARK 900 RELATED ID: 2DL9   RELATED DB: PDB                                   
REMARK 900  SOLUTION STRUCTURE OF THE IG-LIKE DOMAIN OF HUMAN                   
REMARK 900  LEUCINE-RICH REPEAT-CONTAINING PROTEIN 4                            
REMARK 900 RELATED ID: 3ZYJ   RELATED DB: PDB                                   
REMARK 900  NETRING1 IN COMPLEX WITH NGL1                                       
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 N-TERMINUS IS CLEAVED DURING PROTEIN PRODUCTION. C-                  
REMARK 999 TERMINUS CONTAINS A 6 X HISTIDINE TAG.                               
DBREF  3ZYI A    1   444  UNP    Q9HBW1   LRRC4_HUMAN      1    444             
DBREF  3ZYI B    1   345  UNP    Q96CW9   NTNG2_HUMAN    423    767             
SEQADV 3ZYI GLY A  445  UNP  Q9HBW1              EXPRESSION TAG                 
SEQADV 3ZYI THR A  446  UNP  Q9HBW1              EXPRESSION TAG                 
SEQADV 3ZYI HIS A  447  UNP  Q9HBW1              EXPRESSION TAG                 
SEQADV 3ZYI HIS A  448  UNP  Q9HBW1              EXPRESSION TAG                 
SEQADV 3ZYI HIS A  449  UNP  Q9HBW1              EXPRESSION TAG                 
SEQADV 3ZYI HIS A  450  UNP  Q9HBW1              EXPRESSION TAG                 
SEQADV 3ZYI HIS A  451  UNP  Q9HBW1              EXPRESSION TAG                 
SEQADV 3ZYI HIS A  452  UNP  Q9HBW1              EXPRESSION TAG                 
SEQADV 3ZYI GLY B  346  UNP  Q96CW9              EXPRESSION TAG                 
SEQADV 3ZYI THR B  347  UNP  Q96CW9              EXPRESSION TAG                 
SEQADV 3ZYI HIS B  348  UNP  Q96CW9              EXPRESSION TAG                 
SEQADV 3ZYI HIS B  349  UNP  Q96CW9              EXPRESSION TAG                 
SEQADV 3ZYI HIS B  350  UNP  Q96CW9              EXPRESSION TAG                 
SEQADV 3ZYI HIS B  351  UNP  Q96CW9              EXPRESSION TAG                 
SEQADV 3ZYI HIS B  352  UNP  Q96CW9              EXPRESSION TAG                 
SEQADV 3ZYI HIS B  353  UNP  Q96CW9              EXPRESSION TAG                 
SEQRES   1 A  452  MET LYS LEU LEU TRP GLN VAL THR VAL HIS HIS HIS THR          
SEQRES   2 A  452  TRP ASN ALA ILE LEU LEU PRO PHE VAL TYR LEU THR ALA          
SEQRES   3 A  452  GLN VAL TRP ILE LEU CYS ALA ALA ILE ALA ALA ALA ALA          
SEQRES   4 A  452  SER ALA GLY PRO GLN ASN CYS PRO SER VAL CYS SER CYS          
SEQRES   5 A  452  SER ASN GLN PHE SER LYS VAL VAL CYS THR ARG ARG GLY          
SEQRES   6 A  452  LEU SER GLU VAL PRO GLN GLY ILE PRO SER ASN THR ARG          
SEQRES   7 A  452  TYR LEU ASN LEU MET GLU ASN ASN ILE GLN MET ILE GLN          
SEQRES   8 A  452  ALA ASP THR PHE ARG HIS LEU HIS HIS LEU GLU VAL LEU          
SEQRES   9 A  452  GLN LEU GLY ARG ASN SER ILE ARG GLN ILE GLU VAL GLY          
SEQRES  10 A  452  ALA PHE ASN GLY LEU ALA SER LEU ASN THR LEU GLU LEU          
SEQRES  11 A  452  PHE ASP ASN TRP LEU THR VAL ILE PRO SER GLY ALA PHE          
SEQRES  12 A  452  GLU TYR LEU SER LYS LEU ARG GLU LEU TRP LEU ARG ASN          
SEQRES  13 A  452  ASN PRO ILE GLU SER ILE PRO SER TYR ALA PHE ASN ARG          
SEQRES  14 A  452  VAL PRO SER LEU MET ARG LEU ASP LEU GLY GLU LEU LYS          
SEQRES  15 A  452  LYS LEU GLU TYR ILE SER GLU GLY ALA PHE GLU GLY LEU          
SEQRES  16 A  452  PHE ASN LEU LYS TYR LEU ASN LEU GLY MET CYS ASN ILE          
SEQRES  17 A  452  LYS ASP MET PRO ASN LEU THR PRO LEU VAL GLY LEU GLU          
SEQRES  18 A  452  GLU LEU GLU MET SER GLY ASN HIS PHE PRO GLU ILE ARG          
SEQRES  19 A  452  PRO GLY SER PHE HIS GLY LEU SER SER LEU LYS LYS LEU          
SEQRES  20 A  452  TRP VAL MET ASN SER GLN VAL SER LEU ILE GLU ARG ASN          
SEQRES  21 A  452  ALA PHE ASP GLY LEU ALA SER LEU VAL GLU LEU ASN LEU          
SEQRES  22 A  452  ALA HIS ASN ASN LEU SER SER LEU PRO HIS ASP LEU PHE          
SEQRES  23 A  452  THR PRO LEU ARG TYR LEU VAL GLU LEU HIS LEU HIS HIS          
SEQRES  24 A  452  ASN PRO TRP ASN CYS ASP CYS ASP ILE LEU TRP LEU ALA          
SEQRES  25 A  452  TRP TRP LEU ARG GLU TYR ILE PRO THR ASN SER THR CYS          
SEQRES  26 A  452  CYS GLY ARG CYS HIS ALA PRO MET HIS MET ARG GLY ARG          
SEQRES  27 A  452  TYR LEU VAL GLU VAL ASP GLN ALA SER PHE GLN CYS SER          
SEQRES  28 A  452  ALA PRO PHE ILE MET ASP ALA PRO ARG ASP LEU ASN ILE          
SEQRES  29 A  452  SER GLU GLY ARG MET ALA GLU LEU LYS CYS ARG THR PRO          
SEQRES  30 A  452  PRO MET SER SER VAL LYS TRP LEU LEU PRO ASN GLY THR          
SEQRES  31 A  452  VAL LEU SER HIS ALA SER ARG HIS PRO ARG ILE SER VAL          
SEQRES  32 A  452  LEU ASN ASP GLY THR LEU ASN PHE SER HIS VAL LEU LEU          
SEQRES  33 A  452  SER ASP THR GLY VAL TYR THR CYS MET VAL THR ASN VAL          
SEQRES  34 A  452  ALA GLY ASN SER ASN ALA SER ALA TYR LEU ASN VAL SER          
SEQRES  35 A  452  THR ALA GLY THR HIS HIS HIS HIS HIS HIS                      
SEQRES   1 B  353  MET LEU HIS LEU LEU ALA LEU PHE LEU HIS CYS LEU PRO          
SEQRES   2 B  353  LEU ALA SER GLY ASP TYR ASP ILE CYS LYS SER TRP VAL          
SEQRES   3 B  353  THR THR ASP GLU GLY PRO THR TRP GLU PHE TYR ALA CYS          
SEQRES   4 B  353  GLN PRO LYS VAL MET ARG LEU LYS ASP TYR VAL LYS VAL          
SEQRES   5 B  353  LYS VAL GLU PRO SER GLY ILE THR CYS GLY ASP PRO PRO          
SEQRES   6 B  353  GLU ARG PHE CYS SER HIS GLU ASN PRO TYR LEU CYS SER          
SEQRES   7 B  353  ASN GLU CYS ASP ALA SER ASN PRO ASP LEU ALA HIS PRO          
SEQRES   8 B  353  PRO ARG LEU MET PHE ASP LYS GLU GLU GLU GLY LEU ALA          
SEQRES   9 B  353  THR TYR TRP GLN SER ILE THR TRP SER ARG TYR PRO SER          
SEQRES  10 B  353  PRO LEU GLU ALA ASN ILE THR LEU SER TRP ASN LYS THR          
SEQRES  11 B  353  VAL GLU LEU THR ASP ASP VAL VAL MET THR PHE GLU TYR          
SEQRES  12 B  353  GLY ARG PRO THR VAL MET VAL LEU GLU LYS SER LEU ASP          
SEQRES  13 B  353  ASN GLY ARG THR TRP GLN PRO TYR GLN PHE TYR ALA GLU          
SEQRES  14 B  353  ASP CYS MET GLU ALA PHE GLY MET SER ALA ARG ARG ALA          
SEQRES  15 B  353  ARG ASP MET SER SER SER SER ALA HIS ARG VAL LEU CYS          
SEQRES  16 B  353  THR GLU GLU TYR SER ARG TRP ALA GLY SER LYS LYS GLU          
SEQRES  17 B  353  LYS HIS VAL ARG PHE GLU VAL ARG ASP ARG PHE ALA ILE          
SEQRES  18 B  353  PHE ALA GLY PRO ASP LEU ARG ASN MET ASP ASN LEU TYR          
SEQRES  19 B  353  THR ARG LEU GLU SER ALA LYS GLY LEU LYS GLU PHE PHE          
SEQRES  20 B  353  THR LEU THR ASP LEU ARG MET ARG LEU LEU ARG PRO ALA          
SEQRES  21 B  353  LEU GLY GLY THR TYR VAL GLN ARG GLU ASN LEU TYR LYS          
SEQRES  22 B  353  TYR PHE TYR ALA ILE SER ASN ILE GLU VAL ILE GLY ARG          
SEQRES  23 B  353  CYS LYS CYS ASN LEU HIS ALA ASN LEU CYS SER MET ARG          
SEQRES  24 B  353  GLU GLY SER LEU GLN CYS GLU CYS GLU HIS ASN THR THR          
SEQRES  25 B  353  GLY PRO ASP CYS GLY LYS CYS LYS LYS ASN PHE ARG THR          
SEQRES  26 B  353  ARG SER TRP ARG ALA GLY SER TYR LEU PRO LEU PRO HIS          
SEQRES  27 B  353  GLY SER PRO ASN ALA CYS ALA GLY THR HIS HIS HIS HIS          
SEQRES  28 B  353  HIS HIS                                                      
HET    NAG  A1442      14                                                       
HET    PO4  A1443       5                                                       
HET    PO4  A1444       5                                                       
HET    NAG  B1348      14                                                       
HET     CA  B1349       1                                                       
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     PO4 PHOSPHATE ION                                                    
HETNAM      CA CALCIUM ION                                                      
FORMUL   3  NAG    2(C8 H15 N O6)                                               
FORMUL   4  PO4    2(O4 P 3-)                                                   
FORMUL   5   CA    CA 2+                                                        
HELIX    1   1 ARG A  234  HIS A  239  5                                   6    
HELIX    2   2 ILE A  308  ILE A  319  1                                  12    
HELIX    3   3 ASP A  344  PHE A  348  5                                   5    
HELIX    4   4 LYS B   47  VAL B   50  5                                   4    
HELIX    5   5 PRO B   91  PHE B   96  5                                   6    
HELIX    6   6 ASP B  170  PHE B  175  1                                   6    
HELIX    7   7 GLU B  214  ALA B  220  1                                   7    
HELIX    8   8 ALA B  240  PHE B  247  1                                   8    
HELIX    9   9 ASN B  270  TYR B  274  5                                   5    
SHEET    1  AA12 SER A  51  CYS A  52  0                                        
SHEET    2  AA12 LYS A  58  VAL A  60 -1  O  VAL A  60   N  SER A  51           
SHEET    3  AA12 TYR A  79  ASN A  81  1  O  TYR A  79   N  VAL A  59           
SHEET    4  AA12 VAL A 103  GLN A 105  1  O  VAL A 103   N  LEU A  80           
SHEET    5  AA12 THR A 127  GLU A 129  1  O  THR A 127   N  LEU A 104           
SHEET    6  AA12 GLU A 151  TRP A 153  1  O  GLU A 151   N  LEU A 128           
SHEET    7  AA12 ARG A 175  ASP A 177  1  O  ARG A 175   N  LEU A 152           
SHEET    8  AA12 TYR A 200  ASN A 202  1  O  TYR A 200   N  LEU A 176           
SHEET    9  AA12 GLU A 222  GLU A 224  1  O  GLU A 222   N  LEU A 201           
SHEET   10  AA12 LYS A 246  TRP A 248  1  O  LYS A 246   N  LEU A 223           
SHEET   11  AA12 GLU A 270  ASN A 272  1  O  GLU A 270   N  LEU A 247           
SHEET   12  AA12 GLU A 294  HIS A 296  1  O  GLU A 294   N  LEU A 271           
SHEET    1  AB 2 MET A  89  ILE A  90  0                                        
SHEET    2  AB 2 GLN A 113  ILE A 114  1  O  GLN A 113   N  ILE A  90           
SHEET    1  AC 2 SER A 161  ILE A 162  0                                        
SHEET    2  AC 2 TYR A 186  ILE A 187  1  O  TYR A 186   N  ILE A 162           
SHEET    1  AD 2 GLU A 232  ILE A 233  0                                        
SHEET    2  AD 2 LEU A 256  ILE A 257  1  O  LEU A 256   N  ILE A 233           
SHEET    1  AE 2 TRP A 302  ASN A 303  0                                        
SHEET    2  AE 2 CYS A 329  ALA A 331  1  N  HIS A 330   O  TRP A 302           
SHEET    1  AF 5 LEU A 362  ASN A 363  0                                        
SHEET    2  AF 5 ASN A 432  ASN A 440  1  O  TYR A 438   N  LEU A 362           
SHEET    3  AF 5 GLY A 420  THR A 427 -1  O  GLY A 420   N  LEU A 439           
SHEET    4  AF 5 SER A 381  LEU A 385 -1  O  SER A 381   N  THR A 427           
SHEET    5  AF 5 VAL A 391  LEU A 392 -1  O  LEU A 392   N  TRP A 384           
SHEET    1  AG 3 GLU A 371  LEU A 372  0                                        
SHEET    2  AG 3 LEU A 409  ASN A 410 -1  O  LEU A 409   N  LEU A 372           
SHEET    3  AG 3 SER A 402  VAL A 403 -1  O  SER A 402   N  ASN A 410           
SHEET    1  BA 2 LYS B  23  SER B  24  0                                        
SHEET    2  BA 2 GLU B  35  PHE B  36 -1  O  GLU B  35   N  SER B  24           
SHEET    1  BB 7 MET B  44  ARG B  45  0                                        
SHEET    2  BB 7 ILE B 284  CYS B 287 -1  O  GLY B 285   N  MET B  44           
SHEET    3  BB 7 ALA B 121  LEU B 133  1  O  GLU B 132   N  ARG B 286           
SHEET    4  BB 7 THR B 248  ARG B 258 -1  O  LEU B 249   N  VAL B 131           
SHEET    5  BB 7 VAL B 148  SER B 154 -1  O  VAL B 148   N  ARG B 258           
SHEET    6  BB 7 GLN B 162  ALA B 168 -1  O  GLN B 162   N  LYS B 153           
SHEET    7  BB 7 CYS B 195  THR B 196  1  O  THR B 196   N  ALA B 168           
SHEET    1  BC 4 MET B  44  ARG B  45  0                                        
SHEET    2  BC 4 ILE B 284  CYS B 287 -1  O  GLY B 285   N  MET B  44           
SHEET    3  BC 4 ALA B 121  LEU B 133  1  O  GLU B 132   N  ARG B 286           
SHEET    4  BC 4 LYS B  51  GLU B  55 -1  O  LYS B  51   N  SER B 126           
SHEET    1  BD 2 GLU B  66  PHE B  68  0                                        
SHEET    2  BD 2 ASN B  79  CYS B  81 -1  O  ASN B  79   N  PHE B  68           
SHEET    1  BE 4 TRP B 107  GLN B 108  0                                        
SHEET    2  BE 4 ALA B 277  GLU B 282 -1  O  ILE B 278   N  TRP B 107           
SHEET    3  BE 4 VAL B 137  PHE B 141 -1  O  VAL B 138   N  GLU B 282           
SHEET    4  BE 4 HIS B 210  PHE B 213 -1  O  VAL B 211   N  MET B 139           
SHEET    1  BF 2 CYS B 296  ARG B 299  0                                        
SHEET    2  BF 2 SER B 302  CYS B 305 -1  O  SER B 302   N  ARG B 299           
SHEET    1  BG 2 THR B 311  THR B 312  0                                        
SHEET    2  BG 2 LYS B 318  CYS B 319 -1  O  LYS B 318   N  THR B 312           
SSBOND   1 CYS A   46    CYS A   52                          1555   1555  2.15  
SSBOND   2 CYS A   50    CYS A   61                          1555   1555  2.04  
SSBOND   3 CYS A  304    CYS A  329                          1555   1555  2.03  
SSBOND   4 CYS A  306    CYS A  350                          1555   1555  2.03  
SSBOND   5 CYS A  374    CYS A  424                          1555   1555  2.03  
SSBOND   6 CYS B   22    CYS B   39                          1555   1555  2.03  
SSBOND   7 CYS B   61    CYS B   81                          1555   1555  2.03  
SSBOND   8 CYS B   69    CYS B   77                          1555   1555  2.03  
SSBOND   9 CYS B  171    CYS B  195                          1555   1555  2.04  
SSBOND  10 CYS B  287    CYS B  296                          1555   1555  2.04  
SSBOND  11 CYS B  289    CYS B  305                          1555   1555  2.03  
SSBOND  12 CYS B  307    CYS B  316                          1555   1555  2.03  
SSBOND  13 CYS B  319    CYS B  344                          1555   1555  2.04  
LINK         ND2 ASN A 363                 C1  NAG A1442     1555   1555  1.44  
LINK         ND2 ASN B 122                 C1  NAG B1348     1555   1555  1.48  
LINK        CA    CA B1349                 O   THR B 105     1555   1555  2.54  
LINK        CA    CA B1349                 OG1 THR B 105     1555   1555  2.78  
LINK        CA    CA B1349                 OE2 GLU B  99     1555   1555  2.20  
LINK        CA    CA B1349                 O   LEU B  94     1555   1555  2.20  
LINK        CA    CA B1349                 O   SER B 279     1555   1555  2.29  
LINK        CA    CA B1349                 OD1 ASP B  97     1555   1555  2.61  
CISPEP   1 ALA A  331    PRO A  332          0        -3.80                     
CISPEP   2 GLU B   55    PRO B   56          0        -0.21                     
CISPEP   3 ASP B   63    PRO B   64          0         0.08                     
CISPEP   4 TYR B  115    PRO B  116          0         5.34                     
CISPEP   5 LEU B  334    PRO B  335          0         0.41                     
CISPEP   6 LEU B  336    PRO B  337          0         4.12                     
SITE     1 AC1  5 HIS A 298  HIS A 299  GLY A 327  ARG A 328                    
SITE     2 AC1  5 HIS A 330                                                     
SITE     1 AC2  5 MET A 335  ARG A 338  SER A 347  LYS B 321                    
SITE     2 AC2  5 ARG B 324                                                     
SITE     1 AC3  5 LEU B  94  ASP B  97  GLU B  99  THR B 105                    
SITE     2 AC3  5 SER B 279                                                     
SITE     1 AC4  3 ALA A 346  ASN A 363  LYS B 321                               
SITE     1 AC5  5 GLU B  55  PRO B  56  ASN B 122  ARG B 253                    
SITE     2 AC5  5 ARG B 255                                                     
CRYST1   75.420  153.390  158.730  90.00  90.00  90.00 I 2 2 2       8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.013259  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006519  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006300        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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