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Database: PDB
Entry: 3ZYG
LinkDB: 3ZYG
Original site: 3ZYG 
HEADER    CELL ADHESION                           22-AUG-11   3ZYG              
TITLE     NETRING2 LAM AND EGF1 DOMAINS                                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: NETRIN-G2;                                                 
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: LAM AND EGF1 DOMAINS, RESIDUES 423-767;                    
COMPND   5 SYNONYM: LAMINET-2, NETRING;                                         
COMPND   6 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_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PHLSEC                                    
KEYWDS    CELL ADHESION, 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   3   16-NOV-11 3ZYG    1       JRNL                                     
REVDAT   2   26-OCT-11 3ZYG    1       JRNL                                     
REVDAT   1   05-OCT-11 3ZYG    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                 
JRNL        TITL 2 THROUGH 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.    2.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.6.0077                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.13                          
REMARK   3   NUMBER OF REFLECTIONS             : 40042                          
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) : 0.25056                         
REMARK   3   R VALUE            (WORKING SET) : 0.24816                         
REMARK   3   FREE R VALUE                     : 0.29684                         
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.0                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 2125                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.202                        
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.259                        
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2801                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 95.78                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.305                        
REMARK   3   BIN FREE R VALUE SET COUNT          : 153                          
REMARK   3   BIN FREE R VALUE                    : 0.370                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5117                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 58                                      
REMARK   3   SOLVENT ATOMS            : 208                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 25.277                         
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.64                                                
REMARK   3    B22 (A**2) : -0.55                                                
REMARK   3    B33 (A**2) : 2.24                                                 
REMARK   3    B12 (A**2) : 0.00                                                 
REMARK   3    B13 (A**2) : 0.10                                                 
REMARK   3    B23 (A**2) : 0.00                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.301         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.245         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.181         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 13.952        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.932                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.893                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  5330 ; 0.014 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  7237 ; 1.862 ; 1.960       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   634 ; 3.581 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   254 ;34.555 ;22.756       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   859 ;15.178 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    48 ;18.274 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   756 ; 0.135 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4122 ; 0.009 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 2                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    19        A   345                          
REMARK   3    ORIGIN FOR THE GROUP (A): -13.7241 -19.1720  10.5690              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0186 T22:   0.0094                                     
REMARK   3      T33:   0.0247 T12:  -0.0017                                     
REMARK   3      T13:  -0.0045 T23:   0.0040                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4976 L22:   0.2593                                     
REMARK   3      L33:   0.2947 L12:   0.2146                                     
REMARK   3      L13:   0.1539 L23:   0.2388                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0094 S12:  -0.0417 S13:  -0.0001                       
REMARK   3      S21:   0.0017 S22:  -0.0118 S23:   0.0291                       
REMARK   3      S31:   0.0067 S32:   0.0026 S33:   0.0024                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B    19        B   345                          
REMARK   3    ORIGIN FOR THE GROUP (A):   0.5251   5.1947  48.1741              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0127 T22:   0.0066                                     
REMARK   3      T33:   0.0281 T12:   0.0035                                     
REMARK   3      T13:  -0.0040 T23:  -0.0077                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4077 L22:   0.3247                                     
REMARK   3      L33:   0.2536 L12:  -0.2443                                     
REMARK   3      L13:   0.1323 L23:  -0.2231                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0175 S12:   0.0399 S13:  -0.0206                       
REMARK   3      S21:  -0.0021 S22:  -0.0257 S23:  -0.0017                       
REMARK   3      S31:  -0.0019 S32:   0.0062 S33:   0.0083                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN USED IF PRESENT       
REMARK   3  PRESENT IN THE INPUT.                                               
REMARK   4                                                                      
REMARK   4 3ZYG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 23-AUG-11.                  
REMARK 100 THE PDBE ID CODE IS EBI-49426.                                       
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                       : I03                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0, 0.979400                      
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   : 42208                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.20                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 29.20                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.0                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.9                               
REMARK 200  DATA REDUNDANCY                : 3.6                                
REMARK 200  R MERGE                    (I) : 0.32                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 6.40                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.40                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.4                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.84                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.35                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: OTHER                        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1TVG                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 52.69                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.60                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% MME550, 0.1M NACL, 0.1M              
REMARK 280  BICINE PH9                                                          
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
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+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       55.75000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       32.44000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       55.75000            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       32.44000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     LEU A     2                                                      
REMARK 465     HIS A     3                                                      
REMARK 465     LEU A     4                                                      
REMARK 465     LEU A     5                                                      
REMARK 465     ALA A     6                                                      
REMARK 465     LEU A     7                                                      
REMARK 465     PHE A     8                                                      
REMARK 465     LEU A     9                                                      
REMARK 465     HIS A    10                                                      
REMARK 465     CYS A    11                                                      
REMARK 465     LEU A    12                                                      
REMARK 465     PRO A    13                                                      
REMARK 465     LEU A    14                                                      
REMARK 465     ALA A    15                                                      
REMARK 465     SER A    16                                                      
REMARK 465     GLY A    17                                                      
REMARK 465     ASP A    18                                                      
REMARK 465     ALA A   203                                                      
REMARK 465     GLY A   204                                                      
REMARK 465     SER A   205                                                      
REMARK 465     LYS A   206                                                      
REMARK 465     LYS A   207                                                      
REMARK 465     GLY A   346                                                      
REMARK 465     THR A   347                                                      
REMARK 465     HIS A   348                                                      
REMARK 465     HIS A   349                                                      
REMARK 465     HIS A   350                                                      
REMARK 465     HIS A   351                                                      
REMARK 465     HIS A   352                                                      
REMARK 465     HIS A   353                                                      
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     ASP B    18                                                      
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     ALA B   203                                                      
REMARK 465     GLY B   204                                                      
REMARK 465     SER B   205                                                      
REMARK 465     LYS B   206                                                      
REMARK 465     LYS B   207                                                      
REMARK 465     GLY B   346                                                      
REMARK 465     THR B   347                                                      
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     ASP A  29    CG   OD1  OD2                                       
REMARK 470     GLU A  30    CG   CD   OE1  OE2                                  
REMARK 470     GLU A  72    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 208    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 228    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 241    CG   CD   CE   NZ                                   
REMARK 470     GLU A 245    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 321    CG   CD   CE   NZ                                   
REMARK 470     GLU B  35    CG   CD   OE1  OE2                                  
REMARK 470     ARG B 192    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B 208    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 241    CG   CD   CE   NZ                                   
REMARK 470     GLU B 245    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 321    CG   CD   CE   NZ                                   
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    THR A  28     -169.43   -104.34                                   
REMARK 500    ASN A  73       75.25   -119.38                                   
REMARK 500    CYS A  77       51.45     39.45                                   
REMARK 500    TRP A 112       40.45    -83.17                                   
REMARK 500    GLU A 214       99.75    -69.19                                   
REMARK 500    ASN A 229       59.24   -100.51                                   
REMARK 500    ASN B  73       74.58   -119.82                                   
REMARK 500    TYR B  75      -54.91   -124.39                                   
REMARK 500    CYS B  77       48.90     37.79                                   
REMARK 500    TRP B 112       43.48    -84.22                                   
REMARK 500    TYR B 143       53.46   -117.95                                   
REMARK 500    GLU B 214       99.68    -67.65                                   
REMARK 500    ASN B 229       61.11   -101.73                                   
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 A1348  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR A 105   OG1                                                    
REMARK 620 2 GLU A  99   OE2  86.6                                              
REMARK 620 3 THR A 105   O    68.2  80.3                                        
REMARK 620 4 SER A 279   O   152.3  91.1  84.3                                  
REMARK 620 5 HOH A2035   O   125.6  85.7 159.8  81.6                            
REMARK 620 6 LEU A  94   O    92.7 165.5  86.0  82.8 106.3                      
REMARK 620 7 ASP A  97   OD1  69.7 117.1 133.0 134.2  66.7  76.0                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B1348  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 LEU B  94   O                                                      
REMARK 620 2 ASP B  97   OD1  78.3                                              
REMARK 620 3 HOH B2030   O   100.6  67.6                                        
REMARK 620 4 THR B 105   OG1  99.4  69.8 127.4                                  
REMARK 620 5 GLU B  99   OE2 167.6 113.4  88.2  81.7                            
REMARK 620 6 THR B 105   O    87.9 133.3 159.0  68.9  81.0                      
REMARK 620 7 SER B 279   O    82.7 138.0  79.8 151.0  90.3  82.4                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA A1348                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA B1348                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN A OF SUGAR BOUND TO ASN A   
REMARK 800   122 RESIDUES 1347 TO 1347                                          
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   128 RESIDUES 1346 TO 1346                                          
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN B OF SUGAR BOUND TO ASN B   
REMARK 800   122 RESIDUES 1347 TO 1347                                          
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN B OF MONO-SACCHARIDE  NAG   
REMARK 800   B1346 BOUND TO ASN B 128                                           
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3ZYJ   RELATED DB: PDB                                   
REMARK 900  NETRING1 IN COMPLEX WITH NGL1                                       
REMARK 900 RELATED ID: 3ZYI   RELATED DB: PDB                                   
REMARK 900  NETRING2 IN COMPLEX WITH NGL2                                       
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 N-TERMINAL SECRETION SIGNAL IS CLEAVED DURING PROTEIN                
REMARK 999 PRODUCTION. C-TERMINUS CONTAINS 6X HISTIDINE TAG.                    
DBREF  3ZYG A    1   345  UNP    Q96CW9   NTNG2_HUMAN    423    767             
DBREF  3ZYG B    1   345  UNP    Q96CW9   NTNG2_HUMAN    423    767             
SEQADV 3ZYG GLY A  346  UNP  Q96CW9              EXPRESSION TAG                 
SEQADV 3ZYG THR A  347  UNP  Q96CW9              EXPRESSION TAG                 
SEQADV 3ZYG HIS A  348  UNP  Q96CW9              EXPRESSION TAG                 
SEQADV 3ZYG HIS A  349  UNP  Q96CW9              EXPRESSION TAG                 
SEQADV 3ZYG HIS A  350  UNP  Q96CW9              EXPRESSION TAG                 
SEQADV 3ZYG HIS A  351  UNP  Q96CW9              EXPRESSION TAG                 
SEQADV 3ZYG HIS A  352  UNP  Q96CW9              EXPRESSION TAG                 
SEQADV 3ZYG HIS A  353  UNP  Q96CW9              EXPRESSION TAG                 
SEQADV 3ZYG GLY B  346  UNP  Q96CW9              EXPRESSION TAG                 
SEQADV 3ZYG THR B  347  UNP  Q96CW9              EXPRESSION TAG                 
SEQADV 3ZYG HIS B  348  UNP  Q96CW9              EXPRESSION TAG                 
SEQADV 3ZYG HIS B  349  UNP  Q96CW9              EXPRESSION TAG                 
SEQADV 3ZYG HIS B  350  UNP  Q96CW9              EXPRESSION TAG                 
SEQADV 3ZYG HIS B  351  UNP  Q96CW9              EXPRESSION TAG                 
SEQADV 3ZYG HIS B  352  UNP  Q96CW9              EXPRESSION TAG                 
SEQADV 3ZYG HIS B  353  UNP  Q96CW9              EXPRESSION TAG                 
SEQRES   1 A  353  MET LEU HIS LEU LEU ALA LEU PHE LEU HIS CYS LEU PRO          
SEQRES   2 A  353  LEU ALA SER GLY ASP TYR ASP ILE CYS LYS SER TRP VAL          
SEQRES   3 A  353  THR THR ASP GLU GLY PRO THR TRP GLU PHE TYR ALA CYS          
SEQRES   4 A  353  GLN PRO LYS VAL MET ARG LEU LYS ASP TYR VAL LYS VAL          
SEQRES   5 A  353  LYS VAL GLU PRO SER GLY ILE THR CYS GLY ASP PRO PRO          
SEQRES   6 A  353  GLU ARG PHE CYS SER HIS GLU ASN PRO TYR LEU CYS SER          
SEQRES   7 A  353  ASN GLU CYS ASP ALA SER ASN PRO ASP LEU ALA HIS PRO          
SEQRES   8 A  353  PRO ARG LEU MET PHE ASP LYS GLU GLU GLU GLY LEU ALA          
SEQRES   9 A  353  THR TYR TRP GLN SER ILE THR TRP SER ARG TYR PRO SER          
SEQRES  10 A  353  PRO LEU GLU ALA ASN ILE THR LEU SER TRP ASN LYS THR          
SEQRES  11 A  353  VAL GLU LEU THR ASP ASP VAL VAL MET THR PHE GLU TYR          
SEQRES  12 A  353  GLY ARG PRO THR VAL MET VAL LEU GLU LYS SER LEU ASP          
SEQRES  13 A  353  ASN GLY ARG THR TRP GLN PRO TYR GLN PHE TYR ALA GLU          
SEQRES  14 A  353  ASP CYS MET GLU ALA PHE GLY MET SER ALA ARG ARG ALA          
SEQRES  15 A  353  ARG ASP MET SER SER SER SER ALA HIS ARG VAL LEU CYS          
SEQRES  16 A  353  THR GLU GLU TYR SER ARG TRP ALA GLY SER LYS LYS GLU          
SEQRES  17 A  353  LYS HIS VAL ARG PHE GLU VAL ARG ASP ARG PHE ALA ILE          
SEQRES  18 A  353  PHE ALA GLY PRO ASP LEU ARG ASN MET ASP ASN LEU TYR          
SEQRES  19 A  353  THR ARG LEU GLU SER ALA LYS GLY LEU LYS GLU PHE PHE          
SEQRES  20 A  353  THR LEU THR ASP LEU ARG MET ARG LEU LEU ARG PRO ALA          
SEQRES  21 A  353  LEU GLY GLY THR TYR VAL GLN ARG GLU ASN LEU TYR LYS          
SEQRES  22 A  353  TYR PHE TYR ALA ILE SER ASN ILE GLU VAL ILE GLY ARG          
SEQRES  23 A  353  CYS LYS CYS ASN LEU HIS ALA ASN LEU CYS SER MET ARG          
SEQRES  24 A  353  GLU GLY SER LEU GLN CYS GLU CYS GLU HIS ASN THR THR          
SEQRES  25 A  353  GLY PRO ASP CYS GLY LYS CYS LYS LYS ASN PHE ARG THR          
SEQRES  26 A  353  ARG SER TRP ARG ALA GLY SER TYR LEU PRO LEU PRO HIS          
SEQRES  27 A  353  GLY SER PRO ASN ALA CYS ALA GLY THR HIS HIS HIS HIS          
SEQRES  28 A  353  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  A1346      14                                                       
HET    NAG  A1347      14                                                       
HET     CA  A1348       1                                                       
HET    NAG  B1346      14                                                       
HET    NAG  B1347      14                                                       
HET     CA  B1348       1                                                       
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM      CA CALCIUM ION                                                      
FORMUL   3  NAG    4(C8 H15 N O6)                                               
FORMUL   4   CA    2(CA 2+)                                                     
FORMUL   5  HOH   *208(H2 O)                                                    
HELIX    1   1 LYS A   47  VAL A   50  5                                   4    
HELIX    2   2 ASN A   85  ALA A   89  5                                   5    
HELIX    3   3 PRO A   91  PHE A   96  5                                   6    
HELIX    4   4 ASP A  170  GLY A  176  1                                   7    
HELIX    5   5 ARG A  181  MET A  185  5                                   5    
HELIX    6   6 VAL A  215  GLY A  224  1                                  10    
HELIX    7   7 ASN A  229  ALA A  240  1                                  12    
HELIX    8   8 GLY A  242  PHE A  247  1                                   6    
HELIX    9   9 ASN A  270  TYR A  274  5                                   5    
HELIX   10  10 LYS B   47  VAL B   50  5                                   4    
HELIX   11  11 PRO B   91  PHE B   96  5                                   6    
HELIX   12  12 ASP B  170  GLY B  176  1                                   7    
HELIX   13  13 ARG B  181  MET B  185  5                                   5    
HELIX   14  14 VAL B  215  GLY B  224  1                                  10    
HELIX   15  15 ASN B  229  ALA B  240  1                                  12    
HELIX   16  16 GLY B  242  PHE B  247  1                                   6    
HELIX   17  17 ASN B  270  TYR B  274  5                                   5    
SHEET    1  AA 2 LYS A  23  THR A  27  0                                        
SHEET    2  AA 2 PRO A  32  PHE A  36 -1  O  THR A  33   N  VAL A  26           
SHEET    1  AB 7 MET A  44  ARG A  45  0                                        
SHEET    2  AB 7 ILE A 284  CYS A 287 -1  O  GLY A 285   N  MET A  44           
SHEET    3  AB 7 ALA A 121  LEU A 133  1  O  GLU A 132   N  ARG A 286           
SHEET    4  AB 7 THR A 248  ARG A 258 -1  O  LEU A 249   N  VAL A 131           
SHEET    5  AB 7 VAL A 148  SER A 154 -1  O  VAL A 148   N  LEU A 257           
SHEET    6  AB 7 GLN A 162  ALA A 168 -1  O  GLN A 162   N  LYS A 153           
SHEET    7  AB 7 CYS A 195  THR A 196  1  O  THR A 196   N  ALA A 168           
SHEET    1  AC 4 MET A  44  ARG A  45  0                                        
SHEET    2  AC 4 ILE A 284  CYS A 287 -1  O  GLY A 285   N  MET A  44           
SHEET    3  AC 4 ALA A 121  LEU A 133  1  O  GLU A 132   N  ARG A 286           
SHEET    4  AC 4 LYS A  51  GLU A  55 -1  O  LYS A  51   N  SER A 126           
SHEET    1  AD 2 GLU A  66  PHE A  68  0                                        
SHEET    2  AD 2 ASN A  79  CYS A  81 -1  O  ASN A  79   N  PHE A  68           
SHEET    1  AE 4 TRP A 107  GLN A 108  0                                        
SHEET    2  AE 4 ALA A 277  GLU A 282 -1  O  ILE A 278   N  TRP A 107           
SHEET    3  AE 4 VAL A 137  PHE A 141 -1  O  VAL A 138   N  GLU A 282           
SHEET    4  AE 4 HIS A 210  PHE A 213 -1  O  VAL A 211   N  MET A 139           
SHEET    1  AF 2 CYS A 296  ARG A 299  0                                        
SHEET    2  AF 2 SER A 302  CYS A 305 -1  O  SER A 302   N  ARG A 299           
SHEET    1  AG 2 THR A 311  THR A 312  0                                        
SHEET    2  AG 2 LYS A 318  CYS A 319 -1  O  LYS A 318   N  THR A 312           
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  LEU B 257           
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   22    CYS A   39                          1555   1555  2.04  
SSBOND   2 CYS A   61    CYS A   81                          1555   1555  2.04  
SSBOND   3 CYS A   69    CYS A   77                          1555   1555  2.04  
SSBOND   4 CYS A  171    CYS A  195                          1555   1555  2.04  
SSBOND   5 CYS A  287    CYS A  296                          1555   1555  2.05  
SSBOND   6 CYS A  289    CYS A  305                          1555   1555  2.01  
SSBOND   7 CYS A  307    CYS A  316                          1555   1555  2.05  
SSBOND   8 CYS A  319    CYS A  344                          1555   1555  2.05  
SSBOND   9 CYS B   22    CYS B   39                          1555   1555  2.05  
SSBOND  10 CYS B   61    CYS B   81                          1555   1555  2.04  
SSBOND  11 CYS B   69    CYS B   77                          1555   1555  2.04  
SSBOND  12 CYS B  171    CYS B  195                          1555   1555  2.05  
SSBOND  13 CYS B  287    CYS B  296                          1555   1555  2.05  
SSBOND  14 CYS B  289    CYS B  305                          1555   1555  2.02  
SSBOND  15 CYS B  307    CYS B  316                          1555   1555  2.06  
SSBOND  16 CYS B  319    CYS B  344                          1555   1555  2.05  
LINK         ND2 ASN A 122                 C1  NAG A1347     1555   1555  1.49  
LINK         ND2 ASN A 128                 C1  NAG A1346     1555   1555  1.44  
LINK        CA    CA A1348                 OG1 THR A 105     1555   1555  2.65  
LINK        CA    CA A1348                 OE2 GLU A  99     1555   1555  2.34  
LINK        CA    CA A1348                 O   THR A 105     1555   1555  2.43  
LINK        CA    CA A1348                 O   SER A 279     1555   1555  2.29  
LINK        CA    CA A1348                 O   HOH A2035     1555   1555  2.54  
LINK        CA    CA A1348                 O   LEU A  94     1555   1555  2.18  
LINK        CA    CA A1348                 OD1 ASP A  97     1555   1555  2.42  
LINK         ND2 ASN B 122                 C1  NAG B1347     1555   1555  1.48  
LINK         ND2 ASN B 128                 C1  NAG B1346     1555   1555  1.45  
LINK        CA    CA B1348                 OD1 ASP B  97     1555   1555  2.38  
LINK        CA    CA B1348                 O   HOH B2030     1555   1555  2.49  
LINK        CA    CA B1348                 OG1 THR B 105     1555   1555  2.87  
LINK        CA    CA B1348                 OE2 GLU B  99     1555   1555  2.34  
LINK        CA    CA B1348                 O   THR B 105     1555   1555  2.37  
LINK        CA    CA B1348                 O   SER B 279     1555   1555  2.29  
LINK        CA    CA B1348                 O   LEU B  94     1555   1555  2.16  
CISPEP   1 GLU A   55    PRO A   56          0        -0.04                     
CISPEP   2 ASP A   63    PRO A   64          0         3.98                     
CISPEP   3 TYR A  115    PRO A  116          0         7.96                     
CISPEP   4 LEU A  334    PRO A  335          0         0.56                     
CISPEP   5 LEU A  336    PRO A  337          0         7.91                     
CISPEP   6 GLU B   55    PRO B   56          0        -1.40                     
CISPEP   7 ASP B   63    PRO B   64          0         5.66                     
CISPEP   8 TYR B  115    PRO B  116          0         3.75                     
CISPEP   9 LEU B  334    PRO B  335          0         2.64                     
CISPEP  10 LEU B  336    PRO B  337          0         5.97                     
SITE     1 AC1  6 LEU A  94  ASP A  97  GLU A  99  THR A 105                    
SITE     2 AC1  6 SER A 279  HOH A2035                                          
SITE     1 AC2  6 LEU B  94  ASP B  97  GLU B  99  THR B 105                    
SITE     2 AC2  6 SER B 279  HOH B2030                                          
SITE     1 AC3  5 PRO A  56  GLU A 120  ASN A 122  ARG A 253                    
SITE     2 AC3  5 HOH A2083                                                     
SITE     1 AC4  7 LYS A  51  ASN A 128  GLU A 300  SER A 302                    
SITE     2 AC4  7 GLN A 304  HOH A2055  HOH A2095                               
SITE     1 AC5  4 PRO B  56  ASN B 122  ARG B 253  ARG B 255                    
SITE     1 AC6  8 LYS B  51  ASN B 128  GLU B 300  SER B 302                    
SITE     2 AC6  8 GLN B 304  HOH B2048  HOH B2092  HOH B2101                    
CRYST1  111.500   64.880  120.080  90.00 103.06  90.00 C 1 2 1       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      0.008969  0.000000  0.002080        0.00000                         
SCALE2      0.000000  0.015413  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008549        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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