GenomeNet

Database: PDB
Entry: 4URT
LinkDB: 4URT
Original site: 4URT 
HEADER    PROTEIN BINDING                         02-JUL-14   4URT              
TITLE     THE CRYSTAL STRUCTURE OF A FRAGMENT OF NETRIN-1 IN COMPLEX WITH FN5-  
TITLE    2 FN6 OF DCC                                                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: NETRIN-1;                                                  
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: VI AND V DOMAINS, RESIDUES 39-453;                         
COMPND   5 SYNONYM: EPIDIDYMIS TISSUE PROTEIN LI 131P;                          
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: NETRIN RECEPTOR DCC;                                       
COMPND   8 CHAIN: B;                                                            
COMPND   9 FRAGMENT: FN5-FN6, RESIDUES 844-1043;                                
COMPND  10 SYNONYM: COLORECTAL CANCER SUPPRESSOR, IMMUNOGLOBULIN SUPERFAMILY DCC
COMPND  11 SUBCLASS MEMBER 1, TUMOR SUPPRESSOR PROTEIN DCC, DELETED IN          
COMPND  12 COLORECTAL CANCER                                                    
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 MOL_ID: 2;                                                           
SOURCE   6 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   7 ORGANISM_COMMON: HUMAN;                                              
SOURCE   8 ORGANISM_TAXID: 9606                                                 
KEYWDS    PROTEIN BINDING, APOPTOSIS, AXON GUIDANCE, DEPENDENCE RECEPTOR        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    L.I.FINCI,N.KRUEGER,X.SUN,J.ZHANG,M.CHEGKAZI,Y.WU,G.SCHENK,           
AUTHOR   2 H.D.T.MERTENS,D.I.SVERGUN,Y.ZHANG,J.-H.WANG,R.MEIJERS                
REVDAT   4   07-MAR-18 4URT    1       REMARK                                   
REVDAT   3   02-DEC-15 4URT    1       CONECT                                   
REVDAT   2   17-DEC-14 4URT    1       REMARK VERSN                             
REVDAT   1   10-SEP-14 4URT    0                                                
JRNL        AUTH   L.I.FINCI,N.KRUEGER,X.SUN,J.ZHANG,M.CHEGKAZI,Y.WU,G.SCHENK,  
JRNL        AUTH 2 H.D.T.MERTENS,D.I.SVERGUN,Y.ZHANG,J.-H.WANG,R.MEIJERS        
JRNL        TITL   THE CRYSTAL STRUCTURE OF NETRIN-1 IN COMPLEX WITH DCC        
JRNL        TITL 2 REVEALS THE BI-FUNCTIONALITY OF NETRIN-1 AS A GUIDANCE CUE   
JRNL        REF    NEURON                        V.  83   839 2014              
JRNL        REFN                   ISSN 0896-6273                               
JRNL        PMID   25123307                                                     
JRNL        DOI    10.1016/J.NEURON.2014.07.010                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE)                               
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 77.66                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 20291                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.231                           
REMARK   3   R VALUE            (WORKING SET) : 0.230                           
REMARK   3   FREE R VALUE                     : 0.265                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1095                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 77.6828 -  6.1991    1.00     2726   124  0.2337 0.2367        
REMARK   3     2  6.1991 -  4.9206    1.00     2582   147  0.2203 0.2779        
REMARK   3     3  4.9206 -  4.2987    1.00     2559   138  0.1990 0.2410        
REMARK   3     4  4.2987 -  3.9057    1.00     2552   128  0.2140 0.2785        
REMARK   3     5  3.9057 -  3.6257    1.00     2506   154  0.2374 0.2517        
REMARK   3     6  3.6257 -  3.4120    1.00     2523   136  0.2523 0.2996        
REMARK   3     7  3.4120 -  3.2411    0.99     2446   141  0.2611 0.3006        
REMARK   3     8  3.2411 -  3.1000    0.95     2397   127  0.2937 0.3364        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.410            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.450           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.021           5267                                  
REMARK   3   ANGLE     :  0.863           7124                                  
REMARK   3   CHIRALITY :  0.121            767                                  
REMARK   3   PLANARITY :  0.003            915                                  
REMARK   3   DIHEDRAL  : 11.026           1918                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4URT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 02-JUL-14.                  
REMARK 100 THE DEPOSITION ID IS D_1290060862.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 14-JUN-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6                                  
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : PETRA III, EMBL C/O DESY           
REMARK 200  BEAMLINE                       : P14 (MX2)                          
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9763                             
REMARK 200  MONOCHROMATOR                  : SI 1 1 1                           
REMARK 200  OPTICS                         : KB MIRRORS                         
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 20291                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.3                               
REMARK 200  DATA REDUNDANCY                : 8.300                              
REMARK 200  R MERGE                    (I) : 0.15000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.8000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.31                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.82000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.800                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ENTRY 4AQT                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 40.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.00                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M MES PH 6.0, 0.15M AMMONIUM          
REMARK 280  SULFATE AND 15% (W/V) PEG 4000                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
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       42.32500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       77.65850            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       43.70500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       77.65850            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       42.32500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       43.70500            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
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: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 5840 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 35660 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -225.0 KCAL/MOL                       
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       43.70500            
REMARK 350   BIOMT3   1  0.000000  0.000000 -1.000000      -77.65850            
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   2  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   ND2  ASN A   116     C1   NAG A  1461              1.86            
REMARK 500   O    PRO A   450     N    ILE A   452              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    PRO A 227   C   -  N   -  CA  ANGL. DEV. =   9.2 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A  43     -159.64    -77.74                                   
REMARK 500    VAL A  66     -169.00   -119.51                                   
REMARK 500    PRO A  74      109.90    -55.26                                   
REMARK 500    GLU A  86     -137.99     60.07                                   
REMARK 500    LYS A 101       41.87    -99.32                                   
REMARK 500    LEU A 111      109.47    -58.18                                   
REMARK 500    ASN A 124      -62.38   -141.88                                   
REMARK 500    TYR A 125       55.78    -99.43                                   
REMARK 500    GLN A 127      -81.29    -91.55                                   
REMARK 500    SER A 178      146.51   -170.37                                   
REMARK 500    THR A 194     -165.90   -114.76                                   
REMARK 500    SER A 252      -98.59    -91.27                                   
REMARK 500    ASP A 264       74.26    -61.22                                   
REMARK 500    ASP A 297     -153.76    -84.50                                   
REMARK 500    ASP A 300       18.62     59.87                                   
REMARK 500    ARG A 307     -168.77   -126.67                                   
REMARK 500    LYS A 363      -53.27   -132.16                                   
REMARK 500    ARG A 372     -168.12    -77.30                                   
REMARK 500    LYS A 384     -179.35    -69.19                                   
REMARK 500    LYS A 399       44.32   -103.83                                   
REMARK 500    CYS A 451      -31.30     47.97                                   
REMARK 500    LEU A 455       97.47    -61.22                                   
REMARK 500    LEU B 855      -60.65   -106.81                                   
REMARK 500    ASP B 858       -7.65   -151.13                                   
REMARK 500    THR B 875      -55.12   -154.20                                   
REMARK 500    PHE B 889       75.01     54.66                                   
REMARK 500    SER B 892      -92.07   -121.33                                   
REMARK 500    ALA B 893       71.35     62.38                                   
REMARK 500    LYS B 894       29.03    -74.92                                   
REMARK 500    TYR B 895      176.07     58.10                                   
REMARK 500    LYS B 896       83.84   -164.43                                   
REMARK 500    ARG B 926       61.97   -105.02                                   
REMARK 500    ARG B 961       -5.73     61.41                                   
REMARK 500    ASP B 994       49.76    -84.52                                   
REMARK 500    TRP B 995     -157.01    -95.07                                   
REMARK 500    ASN B1026     -159.95   -137.73                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     NAG A 1461                                                       
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 A1465  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR A 118   OG1                                                    
REMARK 620 2 THR A 118   O    65.0                                              
REMARK 620 3 ASN A 112   OD1  92.8 101.3                                        
REMARK 620 4 ASP A 110   OD1  74.3 112.2 133.3                                  
REMARK 620 5 PHE A 107   O   106.8  68.8 150.2  74.8                            
REMARK 620 6 SER A 277   O   138.7  76.5  80.2 137.5  70.2                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 1465                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 1466                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1467                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1468                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1469                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1470                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1471                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1472                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1473                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1474                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1475                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1476                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1477                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1478                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1479                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1480                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1481                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1483                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 2051                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 2052                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: Binding site for Poly-Saccharide residues NAG      
REMARK 800  A1459 through NAG A1460 bound to ASN A 95                           
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: Binding site for Poly-Saccharide residues NAG      
REMARK 800  A1463 through NAG A1464 bound to ASN A 131                          
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: Binding site for Poly-Saccharide residues NAG      
REMARK 800  A1461 through NAG A1462                                             
DBREF  4URT A   39   453  UNP    O95631   NET1_HUMAN      39    453             
DBREF  4URT B  844  1043  UNP    P43146   DCC_HUMAN      844   1043             
SEQADV 4URT GLU A  454  UNP  O95631              EXPRESSION TAG                 
SEQADV 4URT LEU A  455  UNP  O95631              EXPRESSION TAG                 
SEQADV 4URT HIS A  456  UNP  O95631              EXPRESSION TAG                 
SEQADV 4URT HIS A  457  UNP  O95631              EXPRESSION TAG                 
SEQADV 4URT HIS A  458  UNP  O95631              EXPRESSION TAG                 
SEQADV 4URT LEU B 1045  UNP  P43146              EXPRESSION TAG                 
SEQADV 4URT GLU B 1046  UNP  P43146              EXPRESSION TAG                 
SEQADV 4URT VAL B 1047  UNP  P43146              EXPRESSION TAG                 
SEQADV 4URT LEU B 1048  UNP  P43146              EXPRESSION TAG                 
SEQADV 4URT PHE B 1049  UNP  P43146              EXPRESSION TAG                 
SEQADV 4URT ALA B 1050  UNP  P43146              EXPRESSION TAG                 
SEQRES   1 A  420  ASP PRO CYS SER ASP GLU ASN GLY HIS PRO ARG ARG CYS          
SEQRES   2 A  420  ILE PRO ASP PHE VAL ASN ALA ALA PHE GLY LYS ASP VAL          
SEQRES   3 A  420  ARG VAL SER SER THR CYS GLY ARG PRO PRO ALA ARG TYR          
SEQRES   4 A  420  CYS VAL VAL SER GLU ARG GLY GLU GLU ARG LEU ARG SER          
SEQRES   5 A  420  CYS HIS LEU CYS ASN ALA SER ASP PRO LYS LYS ALA HIS          
SEQRES   6 A  420  PRO PRO ALA PHE LEU THR ASP LEU ASN ASN PRO HIS ASN          
SEQRES   7 A  420  LEU THR CYS TRP GLN SER GLU ASN TYR LEU GLN PHE PRO          
SEQRES   8 A  420  HIS ASN VAL THR LEU THR LEU SER LEU GLY LYS LYS PHE          
SEQRES   9 A  420  GLU VAL THR TYR VAL SER LEU GLN PHE CYS SER PRO ARG          
SEQRES  10 A  420  PRO GLU SER MET ALA ILE TYR LYS SER MET ASP TYR GLY          
SEQRES  11 A  420  ARG THR TRP VAL PRO PHE GLN PHE TYR SER THR GLN CYS          
SEQRES  12 A  420  ARG LYS MET TYR ASN ARG PRO HIS ARG ALA PRO ILE THR          
SEQRES  13 A  420  LYS GLN ASN GLU GLN GLU ALA VAL CYS THR ASP SER HIS          
SEQRES  14 A  420  THR ASP MET ARG PRO LEU SER GLY GLY LEU ILE ALA PHE          
SEQRES  15 A  420  SER THR LEU ASP GLY ARG PRO SER ALA HIS ASP PHE ASP          
SEQRES  16 A  420  ASN SER PRO VAL LEU GLN ASP TRP VAL THR ALA THR ASP          
SEQRES  17 A  420  ILE ARG VAL ALA PHE SER ARG LEU HIS THR PHE GLY ASP          
SEQRES  18 A  420  GLU ASN GLU ASP ASP SER GLU LEU ALA ARG ASP SER TYR          
SEQRES  19 A  420  PHE TYR ALA VAL SER ASP LEU GLN VAL GLY GLY ARG CYS          
SEQRES  20 A  420  LYS CYS ASN GLY HIS ALA ALA ARG CYS VAL ARG ASP ARG          
SEQRES  21 A  420  ASP ASP SER LEU VAL CYS ASP CYS ARG HIS ASN THR ALA          
SEQRES  22 A  420  GLY PRO GLU CYS ASP ARG CYS LYS PRO PHE HIS TYR ASP          
SEQRES  23 A  420  ARG PRO TRP GLN ARG ALA THR ALA ARG GLU ALA ASN GLU          
SEQRES  24 A  420  CYS VAL ALA CYS ASN CYS ASN LEU HIS ALA ARG ARG CYS          
SEQRES  25 A  420  ARG PHE ASN MET GLU LEU TYR LYS LEU SER GLY ARG LYS          
SEQRES  26 A  420  SER GLY GLY VAL CYS LEU ASN CYS ARG HIS ASN THR ALA          
SEQRES  27 A  420  GLY ARG HIS CYS HIS TYR CYS LYS GLU GLY TYR TYR ARG          
SEQRES  28 A  420  ASP MET GLY LYS PRO ILE THR HIS ARG LYS ALA CYS LYS          
SEQRES  29 A  420  ALA CYS ASP CYS HIS PRO VAL GLY ALA ALA GLY LYS THR          
SEQRES  30 A  420  CYS ASN GLN THR THR GLY GLN CYS PRO CYS LYS ASP GLY          
SEQRES  31 A  420  VAL THR GLY ILE THR CYS ASN ARG CYS ALA LYS GLY TYR          
SEQRES  32 A  420  GLN GLN SER ARG SER PRO ILE ALA PRO CYS ILE LYS GLU          
SEQRES  33 A  420  LEU HIS HIS HIS                                              
SEQRES   1 B  206  MET LEU PRO PRO VAL GLY VAL GLN ALA VAL ALA LEU THR          
SEQRES   2 B  206  HIS ASP ALA VAL ARG VAL SER TRP ALA ASP ASN SER VAL          
SEQRES   3 B  206  PRO LYS ASN GLN LYS THR SER GLU VAL ARG LEU TYR THR          
SEQRES   4 B  206  VAL ARG TRP ARG THR SER PHE SER ALA SER ALA LYS TYR          
SEQRES   5 B  206  LYS SER GLU ASP THR THR SER LEU SER TYR THR ALA THR          
SEQRES   6 B  206  GLY LEU LYS PRO ASN THR MET TYR GLU PHE SER VAL MET          
SEQRES   7 B  206  VAL THR LYS ASN ARG ARG SER SER THR TRP SER MET THR          
SEQRES   8 B  206  ALA HIS ALA THR THR TYR GLU ALA ALA PRO THR SER ALA          
SEQRES   9 B  206  PRO LYS ASP LEU THR VAL ILE THR ARG GLU GLY LYS PRO          
SEQRES  10 B  206  ARG ALA VAL ILE VAL SER TRP GLN PRO PRO LEU GLU ALA          
SEQRES  11 B  206  ASN GLY LYS ILE THR ALA TYR ILE LEU PHE TYR THR LEU          
SEQRES  12 B  206  ASP LYS ASN ILE PRO ILE ASP ASP TRP ILE MET GLU THR          
SEQRES  13 B  206  ILE SER GLY ASP ARG LEU THR HIS GLN ILE MET ASP LEU          
SEQRES  14 B  206  ASN LEU ASP THR MET TYR TYR PHE ARG ILE GLN ALA ARG          
SEQRES  15 B  206  ASN SER LYS GLY VAL GLY PRO LEU SER ASP PRO ILE LEU          
SEQRES  16 B  206  PHE ARG THR LEU LYS LEU GLU VAL LEU PHE ALA                  
MODRES 4URT ASN A   95  ASN  GLYCOSYLATION SITE                                 
MODRES 4URT ASN A  131  ASN  GLYCOSYLATION SITE                                 
HET    NAG  A1459      14                                                       
HET    NAG  A1460      14                                                       
HET    NAG  A1461      14                                                       
HET    NAG  A1462      14                                                       
HET    NAG  A1463      14                                                       
HET    NAG  A1464      14                                                       
HET     CA  A1465       1                                                       
HET     CL  A1466       1                                                       
HET    SO4  A1467       5                                                       
HET    SO4  A1468       5                                                       
HET    SO4  A1469       5                                                       
HET    SO4  A1470       5                                                       
HET    SO4  A1471       5                                                       
HET    SO4  A1472       5                                                       
HET    SO4  A1473       5                                                       
HET    SO4  A1474       5                                                       
HET    SO4  A1475       5                                                       
HET    SO4  A1476       5                                                       
HET    SO4  A1477       5                                                       
HET    SO4  A1478       5                                                       
HET    SO4  A1479       5                                                       
HET    SO4  A1480       5                                                       
HET    SO4  A1481       5                                                       
HET    SO4  A1483       5                                                       
HET    SO4  B2051       5                                                       
HET    GOL  B2052       6                                                       
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM      CA CALCIUM ION                                                      
HETNAM      CL CHLORIDE ION                                                     
HETNAM     SO4 SULFATE ION                                                      
HETNAM     GOL GLYCEROL                                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   3  NAG    6(C8 H15 N O6)                                               
FORMUL   6   CA    CA 2+                                                        
FORMUL   7   CL    CL 1-                                                        
FORMUL   8  SO4    17(O4 S 2-)                                                  
FORMUL  25  GOL    C3 H8 O3                                                     
HELIX    1   1 PRO A  104  LEU A  108  5                                   5    
HELIX    2   2 GLN A  180  TYR A  185  1                                   6    
HELIX    3   3 GLN A  196  GLU A  200  5                                   5    
HELIX    4   4 ARG A  226  ASN A  234  5                                   9    
HELIX    5   5 SER A  235  VAL A  242  1                                   8    
HELIX    6   6 ALA A  268  TYR A  272  5                                   5    
HELIX    7   7 ASN A  353  SER A  360  1                                   8    
HELIX    8   8 LYS B 1043  LEU B 1048  5                                   5    
SHEET    1  AA 2 VAL A  56  ASN A  57  0                                        
SHEET    2  AA 2 ALA A 275  CYS A 285 -1  O  GLY A 283   N  VAL A  56           
SHEET    1  AB 2 TRP A 120  GLN A 121  0                                        
SHEET    2  AB 2 ALA A 275  CYS A 285 -1  O  VAL A 276   N  TRP A 120           
SHEET    1  AC 6 VAL A 202  THR A 204  0                                        
SHEET    2  AC 6 VAL A 172  SER A 178  1  O  PHE A 174   N  VAL A 202           
SHEET    3  AC 6 SER A 158  SER A 164 -1  O  MET A 159   N  TYR A 177           
SHEET    4  AC 6 THR A 243  PHE A 251 -1  N  THR A 245   O  SER A 164           
SHEET    5  AC 6 VAL A 132  PHE A 151 -1  O  VAL A 132   N  PHE A 251           
SHEET    6  AC 6 LEU A 217  SER A 221 -1  O  ILE A 218   N  LEU A 149           
SHEET    1  AD 7 VAL A 202  THR A 204  0                                        
SHEET    2  AD 7 VAL A 172  SER A 178  1  O  PHE A 174   N  VAL A 202           
SHEET    3  AD 7 SER A 158  SER A 164 -1  O  MET A 159   N  TYR A 177           
SHEET    4  AD 7 THR A 243  PHE A 251 -1  N  THR A 245   O  SER A 164           
SHEET    5  AD 7 VAL A 132  PHE A 151 -1  O  VAL A 132   N  PHE A 251           
SHEET    6  AD 7 ALA A 275  CYS A 285 -1  N  SER A 277   O  GLN A 150           
SHEET    7  AD 7 TRP A 120  GLN A 121 -1  O  TRP A 120   N  VAL A 276           
SHEET    1  AE 2 LEU A 217  SER A 221  0                                        
SHEET    2  AE 2 VAL A 132  PHE A 151 -1  O  VAL A 147   N  PHE A 220           
SHEET    1  AF 7 VAL A 202  THR A 204  0                                        
SHEET    2  AF 7 VAL A 172  SER A 178  1  O  PHE A 174   N  VAL A 202           
SHEET    3  AF 7 SER A 158  SER A 164 -1  O  MET A 159   N  TYR A 177           
SHEET    4  AF 7 THR A 243  PHE A 251 -1  N  THR A 245   O  SER A 164           
SHEET    5  AF 7 VAL A 132  PHE A 151 -1  O  VAL A 132   N  PHE A 251           
SHEET    6  AF 7 ALA A 275  CYS A 285 -1  N  SER A 277   O  GLN A 150           
SHEET    7  AF 7 VAL A  56  ASN A  57 -1  O  VAL A  56   N  GLY A 283           
SHEET    1  AG 2 ALA A  75  VAL A  79  0                                        
SHEET    2  AG 2 SER A  90  CYS A  94 -1  O  SER A  90   N  VAL A  79           
SHEET    1  AH 2 CYS A 294  ARG A 296  0                                        
SHEET    2  AH 2 LEU A 302  CYS A 304 -1  O  VAL A 303   N  VAL A 295           
SHEET    1  AI 2 THR A 310  ALA A 311  0                                        
SHEET    2  AI 2 ARG A 317  CYS A 318 -1  O  ARG A 317   N  ALA A 311           
SHEET    1  AJ 2 ARG A 349  PHE A 352  0                                        
SHEET    2  AJ 2 GLY A 366  LEU A 369 -1  O  VAL A 367   N  ARG A 351           
SHEET    1  AK 2 THR A 375  ALA A 376  0                                        
SHEET    2  AK 2 TYR A 382  CYS A 383 -1  O  TYR A 382   N  ALA A 376           
SHEET    1  AL 2 TYR A 387  ARG A 389  0                                        
SHEET    2  AL 2 CYS A 401  ALA A 403 -1  O  LYS A 402   N  TYR A 388           
SHEET    1  AM 2 VAL A 429  THR A 430  0                                        
SHEET    2  AM 2 ARG A 436  CYS A 437 -1  O  ARG A 436   N  THR A 430           
SHEET    1  AN 2 TYR A 441  GLN A 442  0                                        
SHEET    2  AN 2 LYS A 453  GLU A 454 -1  O  LYS A 453   N  GLN A 442           
SHEET    1  BA 3 VAL B 848  ALA B 854  0                                        
SHEET    2  BA 3 VAL B 860  ALA B 865 -1  O  ARG B 861   N  VAL B 853           
SHEET    3  BA 3 SER B 904  ALA B 907 -1  O  TYR B 905   N  VAL B 862           
SHEET    1  BB 4 ASP B 899  THR B 900  0                                        
SHEET    2  BB 4 LEU B 880  THR B 887 -1  O  TYR B 881   N  THR B 900           
SHEET    3  BB 4 MET B 915  LYS B 924 -1  O  GLU B 917   N  ARG B 886           
SHEET    4  BB 4 ARG B 927  SER B 928 -1  O  ARG B 927   N  LYS B 924           
SHEET    1  BC 4 ASP B 899  THR B 900  0                                        
SHEET    2  BC 4 LEU B 880  THR B 887 -1  O  TYR B 881   N  THR B 900           
SHEET    3  BC 4 MET B 915  LYS B 924 -1  O  GLU B 917   N  ARG B 886           
SHEET    4  BC 4 ALA B 935  THR B 938 -1  O  ALA B 935   N  PHE B 918           
SHEET    1  BD 2 ARG B 927  SER B 928  0                                        
SHEET    2  BD 2 MET B 915  LYS B 924 -1  O  LYS B 924   N  ARG B 927           
SHEET    1  BE 3 LYS B 949  THR B 955  0                                        
SHEET    2  BE 3 VAL B 963  GLN B 968 -1  O  ILE B 964   N  ILE B 954           
SHEET    3  BE 3 THR B1006  ILE B1009 -1  O  HIS B1007   N  VAL B 965           
SHEET    1  BF 4 GLU B 998  ILE B1000  0                                        
SHEET    2  BF 4 ALA B 979  THR B 985 -1  O  TYR B 980   N  ILE B1000           
SHEET    3  BF 4 MET B1017  ASN B1026 -1  O  TYR B1019   N  THR B 985           
SHEET    4  BF 4 GLY B1029  VAL B1030 -1  O  GLY B1029   N  ASN B1026           
SHEET    1  BG 4 GLU B 998  ILE B1000  0                                        
SHEET    2  BG 4 ALA B 979  THR B 985 -1  O  TYR B 980   N  ILE B1000           
SHEET    3  BG 4 MET B1017  ASN B1026 -1  O  TYR B1019   N  THR B 985           
SHEET    4  BG 4 PHE B1039  ARG B1040 -1  O  PHE B1039   N  TYR B1018           
SHEET    1  BH 2 GLY B1029  VAL B1030  0                                        
SHEET    2  BH 2 MET B1017  ASN B1026 -1  O  ASN B1026   N  GLY B1029           
SSBOND   1 CYS A   41    CYS A   51                          1555   1555  2.03  
SSBOND   2 CYS A   70    CYS A   94                          1555   1555  2.03  
SSBOND   3 CYS A   78    CYS A   91                          1555   1555  2.03  
SSBOND   4 CYS A  119    CYS A  152                          1555   1555  2.03  
SSBOND   5 CYS A  181    CYS A  203                          1555   1555  2.03  
SSBOND   6 CYS A  285    CYS A  294                          1555   1555  2.04  
SSBOND   7 CYS A  287    CYS A  304                          1555   1555  2.03  
SSBOND   8 CYS A  306    CYS A  315                          1555   1555  2.03  
SSBOND   9 CYS A  318    CYS A  338                          1555   1555  2.03  
SSBOND  10 CYS A  341    CYS A  350                          1555   1555  2.03  
SSBOND  11 CYS A  343    CYS A  368                          1555   1555  2.03  
SSBOND  12 CYS A  371    CYS A  380                          1555   1555  2.03  
SSBOND  13 CYS A  383    CYS A  401                          1555   1555  2.03  
SSBOND  14 CYS A  404    CYS A  416                          1555   1555  2.03  
SSBOND  15 CYS A  406    CYS A  423                          1555   1555  2.03  
SSBOND  16 CYS A  425    CYS A  434                          1555   1555  2.03  
SSBOND  17 CYS A  437    CYS A  451                          1555   1555  2.03  
LINK         ND2 ASN A  95                 C1  NAG A1459     1555   1555  1.50  
LINK         ND2 ASN A 131                 C1  NAG A1463     1555   1555  1.42  
LINK         O4  NAG A1459                 C1  NAG A1460     1555   1555  1.47  
LINK         O4  NAG A1461                 C1  NAG A1462     1555   1555  1.45  
LINK         O4  NAG A1463                 C1  NAG A1464     1555   1555  1.44  
LINK        CA    CA A1465                 OG1 THR A 118     1555   1555  2.35  
LINK        CA    CA A1465                 O   THR A 118     1555   1555  2.49  
LINK        CA    CA A1465                 OD1 ASN A 112     1555   1555  2.43  
LINK        CA    CA A1465                 OD1 ASP A 110     1555   1555  2.42  
LINK        CA    CA A1465                 O   PHE A 107     1555   1555  2.54  
LINK        CA    CA A1465                 O   SER A 277     1555   1555  2.44  
CISPEP   1 ASN A   45    GLY A   46          0         1.89                     
CISPEP   2 ARG A   72    PRO A   73          0        -3.14                     
CISPEP   3 GLU A  123    ASN A  124          0        -5.34                     
CISPEP   4 PHE A  128    PRO A  129          0        -1.44                     
CISPEP   5 ASN B  872    GLN B  873          0         8.08                     
CISPEP   6 LYS B  874    THR B  875          0       -14.07                     
CISPEP   7 ASN B  925    ARG B  926          0         0.24                     
CISPEP   8 GLU B  957    GLY B  958          0        -3.87                     
CISPEP   9 PHE B 1049    ALA B 1050          0        -0.49                     
SITE     1 AC1  5 PHE A 107  ASP A 110  ASN A 112  THR A 118                    
SITE     2 AC1  5 SER A 277                                                     
SITE     1 AC2  7 ARG A 317  CYS A 318  LYS A 319  PRO A 320                    
SITE     2 AC2  7 TYR A 323  THR B 856  ASP B 858                               
SITE     1 AC3  2 TRP A 171  ARG A 248                                          
SITE     1 AC4  4 ASP A 224  GLY A 225  ASP A 427  SO4 A1481                    
SITE     1 AC5  3 ARG A 155  HIS A 207  ASP A 209                               
SITE     1 AC6  3 ARG A 307  HIS A 308  ASN A 309                               
SITE     1 AC7  2 ARG A 349  ASN A 370                                          
SITE     1 AC8  3 GLY A 431  ILE A 432  ARG A 436                               
SITE     1 AC9  5 CYS A 437  TYR A 441  THR B 934  ALA B 935                    
SITE     2 AC9  5 HIS B 936                                                     
SITE     1 BC1  5 ARG A 349  ARG A 351  SO4 A1477  GLY B 909                    
SITE     2 BC1  5 TYR B 916                                                     
SITE     1 BC2  3 TYR A 162  ARG A 248  NAG A1463                               
SITE     1 BC3  3 GLY A 377  ARG A 378  HIS A 381                               
SITE     1 BC4  2 ASN A 370  SO4 A1474                                          
SITE     1 BC5  4 THR A 430  ARG A 436  ALA A 438  LYS A 439                    
SITE     1 BC6  4 ARG A 348  ARG A 372  HIS A 373  ARG A 398                    
SITE     1 BC7  4 ARG A 182  ASN A 186  PRO A 188  SO4 A1483                    
SITE     1 BC8  3 LYS A 426  ASP A 427  SO4 A1468                               
SITE     1 BC9  1 SO4 A1480                                                     
SITE     1 CC1  2 ARG A 317  THR B 906                                          
SITE     1 CC2  2 ALA B 854  THR B 938                                          
SITE     1 CC3  4 PRO A  74  ASN A  95  SER A  97  ASP A  98                    
SITE     1 CC4  3 ASN A 131  TYR A 162  SO4 A1475                               
SITE     1 CC5  2 LYS A 100  ASN A 116                                          
CRYST1   84.650   87.410  155.317  90.00  90.00  90.00 P 21 21 21    4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.011813  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011440  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006438        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system