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Database: PDB
Entry: 6FKQ
LinkDB: 6FKQ
Original site: 6FKQ 
HEADER    SIGNALING PROTEIN                       24-JAN-18   6FKQ              
TITLE     THE CRYSTAL STRUCTURE OF A FRAGMENT OF NETRIN-1 IN COMPLEX WITH A     
TITLE    2 FRAGMENT OF DRAXIN                                                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: NETRIN-1;                                                  
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: EPIDIDYMIS TISSUE PROTEIN LI 131P;                          
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 OTHER_DETAILS: NETRIN-1 IS A PROTOTYPICAL AXON GUIDANCE CUE THAT     
COMPND   7 BINDS TO THE RECEPTOR DELETED IN COLORECTAL CANCER (DCC).;           
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: DRAXIN;                                                    
COMPND  10 CHAIN: B;                                                            
COMPND  11 FRAGMENT: UNP RESIDUES 225-243;                                      
COMPND  12 SYNONYM: DORSAL INHIBITORY AXON GUIDANCE PROTEIN,DORSAL REPULSIVE    
COMPND  13 AXON GUIDANCE PROTEIN,NEUCRIN;                                       
COMPND  14 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: NTN1, NTN1L;                                                   
SOURCE   6 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE   7 EXPRESSION_SYSTEM_COMMON: HUMAN;                                     
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE   9 EXPRESSION_SYSTEM_CELL_LINE: HEK293T;                                
SOURCE  10 EXPRESSION_SYSTEM_ATCC_NUMBER: 293T/17 [HEK 293T/17] ATCC CRL-11268; 
SOURCE  11 EXPRESSION_SYSTEM_TISSUE: KIDNEY;                                    
SOURCE  12 EXPRESSION_SYSTEM_PLASMID: PXLG;                                     
SOURCE  13 MOL_ID: 2;                                                           
SOURCE  14 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  15 ORGANISM_COMMON: HUMAN;                                              
SOURCE  16 ORGANISM_TAXID: 9606;                                                
SOURCE  17 GENE: DRAXIN, C1ORF187, PSEC0258, UNQ3119/PRO10268;                  
SOURCE  18 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE  19 EXPRESSION_SYSTEM_COMMON: HUMAN;                                     
SOURCE  20 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE  21 EXPRESSION_SYSTEM_CELL_LINE: HEK293T;                                
SOURCE  22 EXPRESSION_SYSTEM_ATCC_NUMBER: (HEK 293T/17] ATCC CRL-11268;         
SOURCE  23 EXPRESSION_SYSTEM_TISSUE: KIDNEY;                                    
SOURCE  24 EXPRESSION_SYSTEM_PLASMID: PXLG                                      
KEYWDS    AXON GUIDANCE CUE, NETRIN-1, DRAXIN, COMMISSURAL NEURON, SIGNALING    
KEYWDS   2 PROTEIN                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    T.BHOWMICK,R.MEIJERS                                                  
REVDAT   2   04-APR-18 6FKQ    1       JRNL                                     
REVDAT   1   21-MAR-18 6FKQ    0                                                
JRNL        AUTH   Y.LIU,T.BHOWMICK,Y.LIU,X.GAO,H.D.T.MERTENS,D.I.SVERGUN,      
JRNL        AUTH 2 J.XIAO,Y.ZHANG,J.H.WANG,R.MEIJERS                            
JRNL        TITL   STRUCTURAL BASIS FOR DRAXIN-MODULATED AXON GUIDANCE AND      
JRNL        TITL 2 FASCICULATION BY NETRIN-1 THROUGH DCC.                       
JRNL        REF    NEURON                        V.  97  1261 2018              
JRNL        REFN                   ISSN 1097-4199                               
JRNL        PMID   29503192                                                     
JRNL        DOI    10.1016/J.NEURON.2018.02.010                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.07 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0155                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.07                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 54.01                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 17128                          
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) : 0.237                           
REMARK   3   R VALUE            (WORKING SET) : 0.235                           
REMARK   3   FREE R VALUE                     : 0.271                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 874                             
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) : 3.07                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.15                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1222                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.30                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3950                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 63                           
REMARK   3   BIN FREE R VALUE                    : 0.3380                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3420                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 155                                     
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 76.42                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 2.42000                                              
REMARK   3    B22 (A**2) : 2.42000                                              
REMARK   3    B33 (A**2) : -7.84000                                             
REMARK   3    B12 (A**2) : 1.21000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.826         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.387         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.375         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 23.425        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.908                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.866                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3684 ; 0.012 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  3250 ; 0.010 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4993 ; 1.881 ; 1.982       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  7507 ; 1.744 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   432 ; 8.003 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   178 ;35.405 ;22.753       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   568 ;18.113 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    37 ;17.203 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   532 ; 0.094 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4087 ; 0.006 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   874 ; 0.023 ; 0.020       
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):  1736 ; 4.394 ; 7.334       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  1735 ; 4.381 ; 7.331       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2164 ; 7.186 ;10.994       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  2165 ; 7.185 ;10.998       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1948 ; 4.887 ; 7.987       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  1948 ; 4.886 ; 7.987       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  2830 ; 7.436 ;11.789       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  3929 ;11.160 ;87.838       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  3929 ;11.160 ;87.834       
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  : NULL                                       
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 ADDED IN THE RIDING   
REMARK   3   POSITIONS                                                          
REMARK   4                                                                      
REMARK   4 6FKQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 24-JAN-18.                  
REMARK 100 THE DEPOSITION ID IS D_1200008351.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 10-SEP-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 4-5                                
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) : 0.987                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS3 6M                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS 3.3.22                     
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 18063                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.070                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 54.130                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 32.90                              
REMARK 200  R MERGE                    (I) : 0.58700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.7000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.07                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.23                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 18.60                              
REMARK 200  R MERGE FOR SHELL          (I) : 2.89700                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 4URT                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 73.38                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.62                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.6 M AMMONIUM SULPHATE AND 0.1 M        
REMARK 280  SODIUM CITRATE, AT PH 4 TO PH 5, VAPOR DIFFUSION, TEMPERATURE       
REMARK 280  298K, VAPOR DIFFUSION, SITTING DROP                                 
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 64 2 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   -X,-Y,Z                                                 
REMARK 290       5555   Y,-X+Y,Z+1/3                                            
REMARK 290       6555   X-Y,X,Z+2/3                                             
REMARK 290       7555   Y,X,-Z+1/3                                              
REMARK 290       8555   X-Y,-Y,-Z                                               
REMARK 290       9555   -X,-X+Y,-Z+2/3                                          
REMARK 290      10555   -Y,-X,-Z+1/3                                            
REMARK 290      11555   -X+Y,Y,-Z                                               
REMARK 290      12555   X,X-Y,-Z+2/3                                            
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       61.29000            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      122.58000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       61.29000            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000      122.58000            
REMARK 290   SMTRY1   7 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       61.29000            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   9 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   9  0.000000  0.000000 -1.000000      122.58000            
REMARK 290   SMTRY1  10  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  10 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000       61.29000            
REMARK 290   SMTRY1  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  11  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1  12  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  12  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000      122.58000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4220 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 25880 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -98.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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   O7   NAG A   505     O2   SO4 A   516              1.11            
REMARK 500   ND2  ASN A   131     O5   NAG A   506              1.93            
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    ARG A  65   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES          
REMARK 500    ARG A  65   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.1 DEGREES          
REMARK 500    PRO A 129   C   -  N   -  CD  ANGL. DEV. =  16.7 DEGREES          
REMARK 500    ARG A 182   NE  -  CZ  -  NH1 ANGL. DEV. =   3.5 DEGREES          
REMARK 500    PRO A 212   C   -  N   -  CA  ANGL. DEV. = -10.2 DEGREES          
REMARK 500    CYS A 338   CA  -  CB  -  SG  ANGL. DEV. =   7.3 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    HIS A 103       59.10   -144.55                                   
REMARK 500    ASN A 116       64.71   -150.47                                   
REMARK 500    HIS A 130      124.67    -30.58                                   
REMARK 500    TYR A 167     -128.94     60.64                                   
REMARK 500    ARG A 190       49.52     31.46                                   
REMARK 500    ASP A 259      -73.30    -91.25                                   
REMARK 500    GLU A 260       77.65     54.92                                   
REMARK 500    ASP A 264        0.39    -65.40                                   
REMARK 500    ASP A 270        4.75    -69.35                                   
REMARK 500    CYS A 287      137.46    -31.99                                   
REMARK 500    ASP A 297     -165.23   -121.71                                   
REMARK 500    PRO A 320      136.61    -37.83                                   
REMARK 500    HIS A 373       37.70     73.97                                   
REMARK 500    ASP A 390       99.25    -68.96                                   
REMARK 500    MET A 391     -177.41    -63.01                                   
REMARK 500    LYS A 399       58.61   -118.18                                   
REMARK 500    ASP A 405       77.49     52.91                                   
REMARK 500    THR A 420      -12.38     78.95                                   
REMARK 500    ARG A 436      142.09   -173.83                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 GLY A  168     ARG A  169                 -143.66                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 508  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 PHE A 107   O                                                      
REMARK 620 2 ASP A 110   OD1  72.7                                              
REMARK 620 3 ASN A 112   OD1 148.9 106.5                                        
REMARK 620 4 THR A 118   O    78.7 128.1 119.7                                  
REMARK 620 5 THR A 118   OG1  87.6  76.5 122.9  59.6                            
REMARK 620 6 SER A 277   O    79.8 132.4  78.8  81.5 140.8                      
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 508                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 509                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 510                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 511                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 512                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 513                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 514                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 515                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 516                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 517                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 518                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 519                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues ASP A    
REMARK 800  98 through NAG A 502 bound to ASN A 95                              
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A    
REMARK 800  503 through NAG A 505 bound to ASN A 116                            
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A    
REMARK 800  506 through NAG A 507 bound to ASN A 131                            
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4URT   RELATED DB: PDB                                   
REMARK 900 NETRIN/DCC COMPLEX                                                   
DBREF  6FKQ A   39   453  UNP    O95631   NET1_HUMAN      39    453             
DBREF  6FKQ B  225   243  UNP    Q8NBI3   DRAXI_HUMAN    225    243             
SEQRES   1 A  415  ASP PRO CYS SER ASP GLU ASN GLY HIS PRO ARG ARG CYS          
SEQRES   2 A  415  ILE PRO ASP PHE VAL ASN ALA ALA PHE GLY LYS ASP VAL          
SEQRES   3 A  415  ARG VAL SER SER THR CYS GLY ARG PRO PRO ALA ARG TYR          
SEQRES   4 A  415  CYS VAL VAL SER GLU ARG GLY GLU GLU ARG LEU ARG SER          
SEQRES   5 A  415  CYS HIS LEU CYS ASN ALA SER ASP PRO LYS LYS ALA HIS          
SEQRES   6 A  415  PRO PRO ALA PHE LEU THR ASP LEU ASN ASN PRO HIS ASN          
SEQRES   7 A  415  LEU THR CYS TRP GLN SER GLU ASN TYR LEU GLN PHE PRO          
SEQRES   8 A  415  HIS ASN VAL THR LEU THR LEU SER LEU GLY LYS LYS PHE          
SEQRES   9 A  415  GLU VAL THR TYR VAL SER LEU GLN PHE CYS SER PRO ARG          
SEQRES  10 A  415  PRO GLU SER MET ALA ILE TYR LYS SER MET ASP TYR GLY          
SEQRES  11 A  415  ARG THR TRP VAL PRO PHE GLN PHE TYR SER THR GLN CYS          
SEQRES  12 A  415  ARG LYS MET TYR ASN ARG PRO HIS ARG ALA PRO ILE THR          
SEQRES  13 A  415  LYS GLN ASN GLU GLN GLU ALA VAL CYS THR ASP SER HIS          
SEQRES  14 A  415  THR ASP MET ARG PRO LEU SER GLY GLY LEU ILE ALA PHE          
SEQRES  15 A  415  SER THR LEU ASP GLY ARG PRO SER ALA HIS ASP PHE ASP          
SEQRES  16 A  415  ASN SER PRO VAL LEU GLN ASP TRP VAL THR ALA THR ASP          
SEQRES  17 A  415  ILE ARG VAL ALA PHE SER ARG LEU HIS THR PHE GLY ASP          
SEQRES  18 A  415  GLU ASN GLU ASP ASP SER GLU LEU ALA ARG ASP SER TYR          
SEQRES  19 A  415  PHE TYR ALA VAL SER ASP LEU GLN VAL GLY GLY ARG CYS          
SEQRES  20 A  415  LYS CYS ASN GLY HIS ALA ALA ARG CYS VAL ARG ASP ARG          
SEQRES  21 A  415  ASP ASP SER LEU VAL CYS ASP CYS ARG HIS ASN THR ALA          
SEQRES  22 A  415  GLY PRO GLU CYS ASP ARG CYS LYS PRO PHE HIS TYR ASP          
SEQRES  23 A  415  ARG PRO TRP GLN ARG ALA THR ALA ARG GLU ALA ASN GLU          
SEQRES  24 A  415  CYS VAL ALA CYS ASN CYS ASN LEU HIS ALA ARG ARG CYS          
SEQRES  25 A  415  ARG PHE ASN MET GLU LEU TYR LYS LEU SER GLY ARG LYS          
SEQRES  26 A  415  SER GLY GLY VAL CYS LEU ASN CYS ARG HIS ASN THR ALA          
SEQRES  27 A  415  GLY ARG HIS CYS HIS TYR CYS LYS GLU GLY TYR TYR ARG          
SEQRES  28 A  415  ASP MET GLY LYS PRO ILE THR HIS ARG LYS ALA CYS LYS          
SEQRES  29 A  415  ALA CYS ASP CYS HIS PRO VAL GLY ALA ALA GLY LYS THR          
SEQRES  30 A  415  CYS ASN GLN THR THR GLY GLN CYS PRO CYS LYS ASP GLY          
SEQRES  31 A  415  VAL THR GLY ILE THR CYS ASN ARG CYS ALA LYS GLY TYR          
SEQRES  32 A  415  GLN GLN SER ARG SER PRO ILE ALA PRO CYS ILE LYS              
SEQRES   1 B   19  MET PRO THR LEU ASP MET ALA LEU PHE ASP TRP THR ASP          
SEQRES   2 B   19  TYR GLU ASP LEU LYS PRO                                      
HET    NAG  A 501      14                                                       
HET    NAG  A 502      14                                                       
HET    NAG  A 503      14                                                       
HET    NAG  A 504      14                                                       
HET    NAG  A 505      14                                                       
HET    NAG  A 506      14                                                       
HET    NAG  A 507      14                                                       
HET     CA  A 508       1                                                       
HET    SO4  A 509       5                                                       
HET    SO4  A 510       5                                                       
HET    SO4  A 511       5                                                       
HET    SO4  A 512       5                                                       
HET    SO4  A 513       5                                                       
HET    SO4  A 514       5                                                       
HET    SO4  A 515       5                                                       
HET    SO4  A 516       5                                                       
HET    SO4  A 517       5                                                       
HET    SO4  A 518       5                                                       
HET    GOL  A 519       6                                                       
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM      CA CALCIUM ION                                                      
HETNAM     SO4 SULFATE ION                                                      
HETNAM     GOL GLYCEROL                                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   3  NAG    7(C8 H15 N O6)                                               
FORMUL   6   CA    CA 2+                                                        
FORMUL   7  SO4    10(O4 S 2-)                                                  
FORMUL  17  GOL    C3 H8 O3                                                     
HELIX    1 AA1 ASP A   98  ALA A  102  5                                   5    
HELIX    2 AA2 PRO A  105  ASP A  110  1                                   6    
HELIX    3 AA3 GLN A  180  ASN A  186  1                                   7    
HELIX    4 AA4 THR A  194  GLU A  198  5                                   5    
HELIX    5 AA5 ASP A  231  ASN A  234  5                                   4    
HELIX    6 AA6 SER A  235  VAL A  242  1                                   8    
HELIX    7 AA7 ASP A  264  ASP A  270  1                                   7    
HELIX    8 AA8 ASN A  353  SER A  360  1                                   8    
HELIX    9 AA9 TYR B  238  LYS B  242  5                                   5    
SHEET    1   A 2 ALA A  75  ARG A  83  0                                        
SHEET    2   A 2 GLU A  86  CYS A  94 -1                                        
SHEET    1   B 4 VAL A 132  SER A 137  0                                        
SHEET    2   B 4 ASP A 246  PHE A 251 -1                                        
SHEET    3   B 4 SER A 158  SER A 164 -1                                        
SHEET    4   B 4 VAL A 172  SER A 178 -1                                        
SHEET    1   C 3 LEU A 217  SER A 221  0                                        
SHEET    2   C 3 PHE A 142  GLN A 150 -1                                        
SHEET    3   C 3 ASP A 278  CYS A 285 -1                                        
SHEET    1   D 2 ARG A 349  PHE A 352  0                                        
SHEET    2   D 2 GLY A 366  LEU A 369 -1                                        
SHEET    1   E 2 TYR A 387  ARG A 389  0                                        
SHEET    2   E 2 CYS A 401  ALA A 403 -1                                        
SHEET    1   F 2 ALA A 291  ARG A 296  0                                        
SHEET    2   F 2 LEU A 302  CYS A 306 -1                                        
SSBOND   1 CYS A   41    CYS A   51                          1555   1555  2.06  
SSBOND   2 CYS A   70    CYS A   94                          1555   1555  2.05  
SSBOND   3 CYS A   78    CYS A   91                          1555   1555  2.07  
SSBOND   4 CYS A  119    CYS A  152                          1555   1555  2.05  
SSBOND   5 CYS A  181    CYS A  203                          1555   1555  2.04  
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  2.04  
SSBOND   9 CYS A  318    CYS A  338                          1555   1555  2.05  
SSBOND  10 CYS A  341    CYS A  350                          1555   1555  2.04  
SSBOND  11 CYS A  343    CYS A  368                          1555   1555  2.01  
SSBOND  12 CYS A  371    CYS A  380                          1555   1555  2.00  
SSBOND  13 CYS A  383    CYS A  401                          1555   1555  2.04  
SSBOND  14 CYS A  404    CYS A  416                          1555   1555  2.03  
SSBOND  15 CYS A  406    CYS A  423                          1555   1555  2.05  
SSBOND  16 CYS A  425    CYS A  434                          1555   1555  2.03  
SSBOND  17 CYS A  437    CYS A  451                          1555   1555  2.06  
LINK         NH2 ARG A  65                 O3  SO4 A 511     1555   1555  1.43  
LINK         ND2 ASN A  95                 C1  NAG A 501     1555   1555  1.46  
LINK         CB  ASP A  98                 O6  NAG A 501     1555   1555  1.37  
LINK         O   PHE A 107                CA    CA A 508     1555   1555  2.35  
LINK         OD1 ASP A 110                CA    CA A 508     1555   1555  2.35  
LINK         OD1 ASN A 112                CA    CA A 508     1555   1555  2.39  
LINK         ND2 ASN A 116                 C1  NAG A 503     1555   1555  1.46  
LINK         O   THR A 118                CA    CA A 508     1555   1555  2.37  
LINK         OG1 THR A 118                CA    CA A 508     1555   1555  2.33  
LINK         ND2 ASN A 131                 C1  NAG A 506     1555   1555  1.31  
LINK         NH2 ARG A 155                 O4  SO4 A 509     1555   1555  1.43  
LINK         NH2 ARG A 248                 O1  SO4 A 511     1555   1555  1.43  
LINK         O   SER A 277                CA    CA A 508     1555   1555  2.27  
LINK         NH2 ARG A 436                 O1  SO4 A 514     1555   1555  1.42  
LINK         O4  NAG A 501                 C1  NAG A 502     1555   1555  1.45  
LINK         O4  NAG A 503                 C1  NAG A 504     1555   1555  1.48  
LINK         O4  NAG A 504                 C1  NAG A 505     1555   1555  1.48  
LINK         O4  NAG A 506                 C1  NAG A 507     1555   1555  1.42  
CISPEP   1 ARG A   72    PRO A   73          0       -10.37                     
CISPEP   2 PHE A  128    PRO A  129          0        -9.50                     
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  3 ARG A 155  HIS A 207  ASP A 209                               
SITE     1 AC3  4 ARG A 190  ARG A 211  PHE A 257  GLY A 258                    
SITE     1 AC4  5 ARG A  65  ARG A 248  GLY A 413  LYS A 414                    
SITE     2 AC4  5 THR A 415                                                     
SITE     1 AC5  2 ASN A 309  HIS A 322                                          
SITE     1 AC6  3 GLY A 431  ILE A 432  ARG A 436                               
SITE     1 AC7  4 THR A 430  ARG A 436  ALA A 438  LYS A 439                    
SITE     1 AC8  3 ASN A 116  HIS A 230  NAG A 503                               
SITE     1 AC9  2 ARG A  50  NAG A 505                                          
SITE     1 AD1  2 LYS A  62  ASP A  63                                          
SITE     1 AD2  4 CYS A  91  HIS A  92  LEU A  93  LYS A 101                    
SITE     1 AD3  2 ARG A 307  HIS A 308                                          
SITE     1 AD4  7 ASN A  95  ALA A  96  SER A  97  PRO A  99                    
SITE     2 AD4  7 LYS A 100  LYS A 101  ALA A 102                               
SITE     1 AD5  5 ARG A  50  ASN A 116  ASP A 233  SO4 A 515                    
SITE     2 AD5  5 SO4 A 516                                                     
SITE     1 AD6  3 PRO A 129  ASN A 131  GLU A 385                               
CRYST1  130.794  130.794  183.870  90.00  90.00 120.00 P 64 2 2     12          
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      0.007646  0.004414  0.000000        0.00000                         
SCALE2      0.000000  0.008828  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005439        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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