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Database: PDB
Entry: 4OVE
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Original site: 4OVE 
HEADER    APOPTOSIS                               21-FEB-14   4OVE              
TITLE     X-RAY CRYSTAL STRUCTURE OF MOUSE NETRIN-1                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: NETRIN-1;                                                  
COMPND   3 CHAIN: A;                                                            
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE   3 ORGANISM_COMMON: MOUSE;                                              
SOURCE   4 ORGANISM_TAXID: 10090;                                               
SOURCE   5 GENE: NTN1;                                                          
SOURCE   6 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE   8 EXPRESSION_SYSTEM_CELL_LINE: HEK293;                                 
SOURCE   9 EXPRESSION_SYSTEM_ORGAN: KIDNEY;                                     
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: PCEP-PU                                   
KEYWDS    SIMILAR TO LAMININ GAMMA-1, DOMAIN VI: BETA-SANDWICH JELLY-ROLL,      
KEYWDS   2 DOMAINS V-1, V-2, V-3: LAMININ-TYPE EPIDERMAL GROWTH FACTOR,         
KEYWDS   3 STRUCTURAL CALCIUM, AXON GUIDANCE CUE, SURVIVAL FACTOR, NEOGENIN,    
KEYWDS   4 DCC, UNC5A, UNC5B, UNC5C, UNC5D, DSCAM, EXTRACELLULAR MATRIX,        
KEYWDS   5 APOPTOSIS                                                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.MEIER,D.NIKODEMUS,R.REUTEN,T.R.PATEL,G.ORRISS,N.OKUN,M.KOCH,        
AUTHOR   2 J.STETEFELD                                                          
REVDAT   4   25-OCT-17 4OVE    1       REMARK                                   
REVDAT   3   17-FEB-16 4OVE    1       JRNL                                     
REVDAT   2   11-MAR-15 4OVE    1       SHEET                                    
REVDAT   1   25-FEB-15 4OVE    0                                                
JRNL        AUTH   M.GRANDIN,M.MEIER,J.G.DELCROS,D.NIKODEMUS,R.REUTEN,          
JRNL        AUTH 2 T.R.PATEL,D.GOLDSCHNEIDER,G.ORRISS,N.KRAHN,A.BOUSSOUAR,      
JRNL        AUTH 3 R.ABES,Y.DEAN,D.NEVES,A.BERNET,S.DEPIL,F.SCHNEIDERS,K.POOLE, 
JRNL        AUTH 4 R.DANTE,M.KOCH,P.MEHLEN,J.STETEFELD                          
JRNL        TITL   STRUCTURAL DECODING OF THE NETRIN-1/UNC5 INTERACTION AND ITS 
JRNL        TITL 2 THERAPEUTICAL IMPLICATIONS IN CANCERS.                       
JRNL        REF    CANCER CELL                   V.  29   173 2016              
JRNL        REFN                   ISSN 1535-6108                               
JRNL        PMID   26859457                                                     
JRNL        DOI    10.1016/J.CCELL.2016.01.001                                  
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.64 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0049                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.64                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 89.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 24458                          
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) : 0.233                           
REMARK   3   R VALUE            (WORKING SET) : 0.230                           
REMARK   3   FREE R VALUE                     : 0.288                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1308                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE SET COUNT          : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3309                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 105                                     
REMARK   3   SOLVENT ATOMS            : 97                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 60.10                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 64.55                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.84000                                             
REMARK   3    B22 (A**2) : -0.84000                                             
REMARK   3    B33 (A**2) : 2.72000                                              
REMARK   3    B12 (A**2) : -0.42000                                             
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): 0.362         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.299         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.267         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 29.397        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.926                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.862                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3662 ; 0.017 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  3265 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4985 ; 1.806 ; 1.988       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  7484 ; 0.857 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   440 ;13.261 ; 5.148       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   176 ;36.259 ;22.443       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   557 ;18.164 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    40 ;15.243 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   537 ; 0.086 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4161 ; 0.008 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   897 ; 0.001 ; 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):  1726 ; 3.621 ; 4.680       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  1724 ; 3.622 ; 4.679       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2163 ; 5.951 ; 7.013       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1936 ; 3.878 ; 5.257       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 7                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    35        A   456                          
REMARK   3    RESIDUE RANGE :   A   509        A   509                          
REMARK   3    RESIDUE RANGE :   A   501        A   505                          
REMARK   3    RESIDUE RANGE :   A   506        A   507                          
REMARK   3    RESIDUE RANGE :   A   508        A   508                          
REMARK   3    RESIDUE RANGE :   A   510        A   510                          
REMARK   3    RESIDUE RANGE :   A   601        A   697                          
REMARK   3    ORIGIN FOR THE GROUP (A):  29.0771  15.8929   3.8209              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0711 T22:   0.0822                                     
REMARK   3      T33:   0.0237 T12:   0.0258                                     
REMARK   3      T13:   0.0085 T23:   0.0231                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5237 L22:   0.3894                                     
REMARK   3      L33:   4.0219 L12:   0.3001                                     
REMARK   3      L13:  -0.9402 L23:  -0.9701                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0510 S12:   0.1256 S13:   0.0392                       
REMARK   3      S21:  -0.0033 S22:   0.0180 S23:  -0.0184                       
REMARK   3      S31:  -0.0270 S32:  -0.2278 S33:   0.0331                       
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:                                           
REMARK   3  HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.                  
REMARK   3                                                                      
REMARK   3  THE DIFFRACTION PATTERN OF NETRIN-1 CRYSTALS SHOWS STRONG           
REMARK   3  ANISOTROPY. THE RESOLUTION LIMITS IN DIRECTION A*/B* ARE 44.85 -    
REMARK   3  2.80 A AND IN DIRECTION C* 44.85 - 2.64 A. COMPLETENESS OF THE      
REMARK   3  DATASET IN THE RESOLUTION RANGE OF INF - 2.80 A IS 0.999, IN THE    
REMARK   3  RANGE OF INF - 2.64 A IT IS 0.896. THE WILSON B-FACTOR CALCULATED   
REMARK   3  FROM THE LINEAR RANGE OF THE DATA IS 68.0 A**2.                     
REMARK   3                                                                      
REMARK   3  THE ELLIPSOIDAL OUTER SHELL IN THE RANGE OF 2.90 - 2.80 A (A*/B*)   
REMARK   3  AND 2.74 - 2.64 A (C*) CONTAINS 2564 REFLECTIONS, HAS A             
REMARK   3  COMPLETENESS OF 1.0, A REDUNDANCY OF 10.8, I/SIGMAI OF 2.0, RMEAS   
REMARK   3  OF 1.344, RMERGE OF 1.280 AND RPIM OF 0.406.                        
REMARK   3                                                                      
REMARK   3  FOR REFINEMENT, AN ELLIPSOIDAL TRUNCTION (LIMIT OF 2.80 A IN A*/B*, 
REMARK   3  LIMIT OF 2.50 A IN C*), ANISOTROPIC SCALING AND A NEGATIVE          
REMARK   3  ISOTROPIC B-FACTOR CORRECTION OF 50% OF THE B-FACTOR IN DIRECTION   
REMARK   3  OF THE LOWEST FALL-OFF (C*) WAS APPLIED ACCORDING TO THE PROCEDURE  
REMARK   3  DESCRIBED BY M. STRONG, M.R. SAWAYA, S. WANG, M. PHILLIPS, D.       
REMARK   3  CASCIO, D. EISENBERG, PROC NATL ACAD SCI USA. 103, 8060-8-65, 2006. 
REMARK   3                                                                      
REMARK   3  AFTER ABOVE ANISOTROPY CORRECTION AND CONVERSION TO AMPLITUDES,     
REMARK   3  THE COMPLETENESS OF THE REFINEMENT DATASET IS AS FOLLOWS: INF -     
REMARK   3  2.80 A: 0.996, INF - 2.50 A: 0.807. THE WILSON B-FACTOR CALCULATED  
REMARK   3  FROM THE LINEAR RANGE OF DATA IS 60.1 A**2.                         
REMARK   4                                                                      
REMARK   4 4OVE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-FEB-14.                  
REMARK 100 THE DEPOSITION ID IS D_1000084996.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 14-OCT-11; 12-OCT-05               
REMARK 200  TEMPERATURE           (KELVIN) : 100; 100                           
REMARK 200  PH                             : 7.7                                
REMARK 200  NUMBER OF CRYSTALS USED        : 2                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y; Y                               
REMARK 200  RADIATION SOURCE               : CLSI; SLS                          
REMARK 200  BEAMLINE                       : 08B1-1; X06SA                      
REMARK 200  X-RAY GENERATOR MODEL          : NULL; NULL                         
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M; M                               
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.25440; 1.25470, 1.25520,         
REMARK 200                                   1.24210                            
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL MONOCHROMATOR       
REMARK 200                                   (DCM) WITH WATER-COOLED FIRST      
REMARK 200                                   CRYSTAL; LIQUID NITROGEN COOLED    
REMARK 200                                   FIXED-EXIT SI(111) MONOCHROMATOR   
REMARK 200  OPTICS                         : VERTICAL COLLIMATING MIRROR,       
REMARK 200                                   TOROIDAL FOCUSING MIRROR;          
REMARK 200                                   DYNAMICALLY BENDABLE MIRROR        
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD; CCD                           
REMARK 200  DETECTOR MANUFACTURER          : RAYONIX MX-300; RAYONIX MX-225     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 27279                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 80.9                               
REMARK 200  DATA REDUNDANCY                : 10.50                              
REMARK 200  R MERGE                    (I) : 0.12900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.8000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; SIRAS                       
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SIRAS                        
REMARK 200 SOFTWARE USED: SHARP                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 74.37                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.80                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M HEPES, 2.7-2.8 M NACL, 0.02-0.2    
REMARK 280  M GLYCINE, PH 7.7, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE       
REMARK 280  293K                                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+1/3                                           
REMARK 290       6555   -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      223.20133            
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      111.60067            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000      111.60067            
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      223.20133            
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 300 REMARK: NETRIN-1 WITHOUT C-TERMINAL DOMAIN FORMS MONOMERS, DIMERS,   
REMARK 300 AND HIGHER ORDER OLIGOMERS IN SOLUTION, AS EVIDENCED BY DYNAMIC      
REMARK 300 LIGHT SCATTERING (DLS), SIZE EXCLUSION CHROMATOGRAPHY (SEC), AND     
REMARK 300 SMALL ANGLE X-RAY SCATTERING (SAXS). IN THE PRESENCE OF GLYCINE AND  
REMARK 300 HIGH CONCENTRATIONS OF SODIUM CHLORIDE, THE DIMERIC FORM CAN BE      
REMARK 300 STABILIZED. THE ASYMMETRIC UNIT CONTAINS ONE MONOMER. A DIMER THAT   
REMARK 300 RESEMBLES THE SHAPE MODEL OBTAINED FROM SAXS CAN BE OBTAINED BY      
REMARK 300 APPLYING THE FOLLOWING CRYSTALLOGRAPHIC SYMMETRY OPERATION: X-Y, -Y, 
REMARK 300 -Z+1/3.                                                              
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: 6770 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 46900 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   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      111.60067            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     ARG A    23                                                      
REMARK 465     GLY A    24                                                      
REMARK 465     GLY A    25                                                      
REMARK 465     PRO A    26                                                      
REMARK 465     GLY A    27                                                      
REMARK 465     LEU A    28                                                      
REMARK 465     SER A    29                                                      
REMARK 465     MET A    30                                                      
REMARK 465     PHE A    31                                                      
REMARK 465     ALA A    32                                                      
REMARK 465     GLY A    33                                                      
REMARK 465     GLN A    34                                                      
REMARK 465     ALA A   457                                                      
REMARK 465     LEU A   458                                                      
REMARK 465     GLU A   459                                                      
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   N    HIS A   373     O    HOH A   691              2.05            
REMARK 500   OD1  ASN A   131     OG   SER A   252              2.06            
REMARK 500   OG1  THR A   375     O    HOH A   691              2.17            
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    PRO A  74      151.32    -47.50                                   
REMARK 500    HIS A 115       -4.47     74.80                                   
REMARK 500    ASN A 116       47.17   -163.39                                   
REMARK 500    SER A 178      155.12    178.98                                   
REMARK 500    ASP A 259      -60.78     77.66                                   
REMARK 500    SER A 265       91.28    -66.09                                   
REMARK 500    ASP A 299        6.51     84.25                                   
REMARK 500    HIS A 373       56.23   -119.90                                   
REMARK 500    CYS A 380       55.20     37.72                                   
REMARK 500    ASP A 390       93.50    -67.16                                   
REMARK 500    LYS A 399       44.29     73.50                                   
REMARK 500    ASP A 405       56.08   -113.69                                   
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 509  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SER A 277   O                                                      
REMARK 620 2 HOH A 604   O    68.9                                              
REMARK 620 3 THR A 118   OG1 147.1 143.3                                        
REMARK 620 4 ASP A 110   OD1 127.8  68.5  77.2                                  
REMARK 620 5 PHE A 107   O    81.2  89.5  90.7  69.6                            
REMARK 620 6 THR A 118   O    76.1 145.0  71.4 139.4  85.4                      
REMARK 620 7 ASN A 112   OD1  78.3  78.9 109.1 120.6 159.0  94.1                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA A 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 505                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 506                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 507                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 508                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 509                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 510                  
DBREF  4OVE A   23   457  UNP    O09118   NET1_MOUSE      23    457             
SEQADV 4OVE LEU A  458  UNP  O09118              EXPRESSION TAG                 
SEQADV 4OVE GLU A  459  UNP  O09118              EXPRESSION TAG                 
SEQRES   1 A  437  ARG GLY GLY PRO GLY LEU SER MET PHE ALA GLY GLN ALA          
SEQRES   2 A  437  ALA GLN PRO ASP PRO CYS SER ASP GLU ASN GLY HIS PRO          
SEQRES   3 A  437  ARG ARG CYS ILE PRO ASP PHE VAL ASN ALA ALA PHE GLY          
SEQRES   4 A  437  LYS ASP VAL ARG VAL SER SER THR CYS GLY ARG PRO PRO          
SEQRES   5 A  437  ALA ARG TYR CYS VAL VAL SER GLU ARG GLY GLU GLU ARG          
SEQRES   6 A  437  LEU ARG SER CYS HIS LEU CYS ASN SER SER ASP PRO LYS          
SEQRES   7 A  437  LYS ALA HIS PRO PRO ALA PHE LEU THR ASP LEU ASN ASN          
SEQRES   8 A  437  PRO HIS ASN LEU THR CYS TRP GLN SER GLU ASN TYR LEU          
SEQRES   9 A  437  GLN PHE PRO HIS ASN VAL THR LEU THR LEU SER LEU GLY          
SEQRES  10 A  437  LYS LYS PHE GLU VAL THR TYR VAL SER LEU GLN PHE CYS          
SEQRES  11 A  437  SER PRO ARG PRO GLU SER MET ALA ILE TYR LYS SER MET          
SEQRES  12 A  437  ASP TYR GLY ARG THR TRP VAL PRO PHE GLN PHE TYR SER          
SEQRES  13 A  437  THR GLN CYS ARG LYS MET TYR ASN ARG PRO HIS ARG ALA          
SEQRES  14 A  437  PRO ILE THR LYS GLN ASN GLU GLN GLU ALA VAL CYS THR          
SEQRES  15 A  437  ASP SER HIS THR ASP MET ARG PRO LEU SER GLY GLY LEU          
SEQRES  16 A  437  ILE ALA PHE SER THR LEU ASP GLY ARG PRO SER ALA HIS          
SEQRES  17 A  437  ASP PHE ASP ASN SER PRO VAL LEU GLN ASP TRP VAL THR          
SEQRES  18 A  437  ALA THR ASP ILE ARG VAL ALA PHE SER ARG LEU HIS THR          
SEQRES  19 A  437  PHE GLY ASP GLU ASN GLU ASP ASP SER GLU LEU ALA ARG          
SEQRES  20 A  437  ASP SER TYR TYR TYR ALA VAL SER ASP LEU GLN VAL GLY          
SEQRES  21 A  437  GLY ARG CYS LYS CYS ASN GLY HIS ALA ALA ARG CYS VAL          
SEQRES  22 A  437  ARG ASP ARG ASP ASP SER LEU VAL CYS ASP CYS ARG HIS          
SEQRES  23 A  437  ASN THR ALA GLY PRO GLU CYS ASP ARG CYS LYS PRO PHE          
SEQRES  24 A  437  HIS TYR ASP ARG PRO TRP GLN ARG ALA THR ALA ARG GLU          
SEQRES  25 A  437  ALA ASN GLU CYS VAL ALA CYS ASN CYS ASN LEU HIS ALA          
SEQRES  26 A  437  ARG ARG CYS ARG PHE ASN MET GLU LEU TYR LYS LEU SER          
SEQRES  27 A  437  GLY ARG LYS SER GLY GLY VAL CYS LEU ASN CYS ARG HIS          
SEQRES  28 A  437  ASN THR ALA GLY ARG HIS CYS HIS TYR CYS LYS GLU GLY          
SEQRES  29 A  437  PHE TYR ARG ASP MET GLY LYS PRO ILE THR HIS ARG LYS          
SEQRES  30 A  437  ALA CYS LYS ALA CYS ASP CYS HIS PRO VAL GLY ALA ALA          
SEQRES  31 A  437  GLY LYS THR CYS ASN GLN THR THR GLY GLN CYS PRO CYS          
SEQRES  32 A  437  LYS ASP GLY VAL THR GLY ILE THR CYS ASN ARG CYS ALA          
SEQRES  33 A  437  LYS GLY TYR GLN GLN SER ARG SER PRO ILE ALA PRO CYS          
SEQRES  34 A  437  ILE LYS ILE PRO VAL ALA LEU GLU                              
MODRES 4OVE ASN A  116  ASN  GLYCOSYLATION SITE                                 
MODRES 4OVE ASN A  131  ASN  GLYCOSYLATION SITE                                 
MODRES 4OVE ASN A   95  ASN  GLYCOSYLATION SITE                                 
HET    NAG  A 501      14                                                       
HET    NAG  A 502      14                                                       
HET    BMA  A 503      11                                                       
HET    MAN  A 504      11                                                       
HET    MAN  A 505      11                                                       
HET    NAG  A 506      42                                                       
HET    NAG  A 507      42                                                       
HET    NAG  A 508      14                                                       
HET     CA  A 509       1                                                       
HET     CL  A 510       1                                                       
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     BMA BETA-D-MANNOSE                                                   
HETNAM     MAN ALPHA-D-MANNOSE                                                  
HETNAM      CA CALCIUM ION                                                      
HETNAM      CL CHLORIDE ION                                                     
FORMUL   2  NAG    5(C8 H15 N O6)                                               
FORMUL   2  BMA    C6 H12 O6                                                    
FORMUL   2  MAN    2(C6 H12 O6)                                                 
FORMUL   5   CA    CA 2+                                                        
FORMUL   6   CL    CL 1-                                                        
FORMUL   7  HOH   *97(H2 O)                                                     
HELIX    1   1 PRO A  104  THR A  109  5                                   6    
HELIX    2   2 GLN A  180  ASN A  186  1                                   7    
HELIX    3   3 THR A  194  GLU A  198  5                                   5    
HELIX    4   4 ASP A  205  ASP A  209  5                                   5    
HELIX    5   5 ARG A  226  ASN A  234  5                                   9    
HELIX    6   6 SER A  235  VAL A  242  1                                   8    
HELIX    7   7 ASN A  353  SER A  360  1                                   8    
SHEET    1   A 2 VAL A  56  ASN A  57  0                                        
SHEET    2   A 2 ALA A 275  CYS A 285 -1  O  GLY A 283   N  VAL A  56           
SHEET    1   B 7 TRP A 120  GLN A 121  0                                        
SHEET    2   B 7 ALA A 275  CYS A 285 -1  O  VAL A 276   N  TRP A 120           
SHEET    3   B 7 VAL A 132  PHE A 151 -1  N  GLU A 143   O  ARG A 284           
SHEET    4   B 7 THR A 243  ARG A 253 -1  O  ILE A 247   N  LEU A 136           
SHEET    5   B 7 SER A 158  SER A 164 -1  N  TYR A 162   O  ARG A 248           
SHEET    6   B 7 VAL A 172  TYR A 177 -1  O  PHE A 174   N  ILE A 161           
SHEET    7   B 7 CYS A 203  THR A 204  1  O  THR A 204   N  PHE A 176           
SHEET    1   C 3 ARG A  65  VAL A  66  0                                        
SHEET    2   C 3 VAL A 132  PHE A 151 -1  O  THR A 135   N  ARG A  65           
SHEET    3   C 3 LEU A 217  SER A 221 -1  O  PHE A 220   N  VAL A 147           
SHEET    1   D 2 ALA A  75  SER A  81  0                                        
SHEET    2   D 2 LEU A  88  CYS A  94 -1  O  HIS A  92   N  TYR A  77           
SHEET    1   E 2 CYS A 294  ARG A 296  0                                        
SHEET    2   E 2 LEU A 302  CYS A 304 -1  O  VAL A 303   N  VAL A 295           
SHEET    1   F 2 THR A 310  ALA A 311  0                                        
SHEET    2   F 2 ARG A 317  CYS A 318 -1  O  ARG A 317   N  ALA A 311           
SHEET    1   G 2 ARG A 349  PHE A 352  0                                        
SHEET    2   G 2 GLY A 366  LEU A 369 -1  O  VAL A 367   N  ARG A 351           
SHEET    1   H 2 THR A 375  ALA A 376  0                                        
SHEET    2   H 2 TYR A 382  CYS A 383 -1  O  TYR A 382   N  ALA A 376           
SHEET    1   I 2 PHE A 387  ARG A 389  0                                        
SHEET    2   I 2 CYS A 401  ALA A 403 -1  O  LYS A 402   N  TYR A 388           
SHEET    1   J 2 VAL A 429  THR A 430  0                                        
SHEET    2   J 2 ARG A 436  CYS A 437 -1  O  ARG A 436   N  THR A 430           
SHEET    1   K 2 TYR A 441  GLN A 443  0                                        
SHEET    2   K 2 CYS A 451  LYS A 453 -1  O  ILE A 452   N  GLN A 442           
SSBOND   1 CYS A   51    CYS A   41                          1555   1555  2.05  
SSBOND   2 CYS A   91    CYS A   78                          1555   1555  2.06  
SSBOND   3 CYS A   94    CYS A   70                          1555   1555  2.07  
SSBOND   4 CYS A  119    CYS A  152                          1555   1555  2.08  
SSBOND   5 CYS A  203    CYS A  181                          1555   1555  2.08  
SSBOND   6 CYS A  294    CYS A  285                          1555   1555  2.09  
SSBOND   7 CYS A  304    CYS A  287                          1555   1555  2.06  
SSBOND   8 CYS A  315    CYS A  306                          1555   1555  2.06  
SSBOND   9 CYS A  338    CYS A  318                          1555   1555  2.08  
SSBOND  10 CYS A  350    CYS A  341                          1555   1555  1.97  
SSBOND  11 CYS A  368    CYS A  343                          1555   1555  2.02  
SSBOND  12 CYS A  380    CYS A  371                          1555   1555  2.05  
SSBOND  13 CYS A  401    CYS A  383                          1555   1555  2.06  
SSBOND  14 CYS A  416    CYS A  404                          1555   1555  2.08  
SSBOND  15 CYS A  423    CYS A  406                          1555   1555  2.07  
SSBOND  16 CYS A  434    CYS A  425                          1555   1555  2.06  
SSBOND  17 CYS A  451    CYS A  437                          1555   1555  2.03  
LINK         O4 CNAG A 506                 C1 CNAG A 507     1555   1555  1.44  
LINK         O4 ANAG A 506                 C1 ANAG A 507     1555   1555  1.44  
LINK         ND2 ASN A 116                 C1  NAG A 508     1555   1555  1.44  
LINK         O4 BNAG A 506                 C1 BNAG A 507     1555   1555  1.44  
LINK         O4  NAG A 501                 C1  NAG A 502     1555   1555  1.45  
LINK         O3  BMA A 503                 C1  MAN A 504     1555   1555  1.45  
LINK         ND2AASN A 131                 C1 ANAG A 506     1555   1555  1.46  
LINK         O4  NAG A 502                 C1  BMA A 503     1555   1555  1.46  
LINK         ND2 ASN A  95                 C1  NAG A 501     1555   1555  1.46  
LINK         ND2CASN A 131                 C1 CNAG A 506     1555   1555  1.46  
LINK         ND2BASN A 131                 C1 BNAG A 506     1555   1555  1.47  
LINK         O6  BMA A 503                 C1  MAN A 505     1555   1555  1.47  
LINK         O   SER A 277                CA    CA A 509     1555   1555  2.19  
LINK        CA    CA A 509                 O   HOH A 604     1555   1555  2.22  
LINK         OG1 THR A 118                CA    CA A 509     1555   1555  2.33  
LINK         OD1 ASP A 110                CA    CA A 509     1555   1555  2.35  
LINK         O   PHE A 107                CA    CA A 509     1555   1555  2.44  
LINK         O   THR A 118                CA    CA A 509     1555   1555  2.54  
LINK         OD1 ASN A 112                CA    CA A 509     1555   1555  2.89  
CISPEP   1 ARG A   72    PRO A   73          0        -0.75                     
CISPEP   2 PHE A  128    PRO A  129          0         6.44                     
SITE     1 AC1  3 ASN A  95  ASP A  98  NAG A 502                               
SITE     1 AC2  3 NAG A 501  BMA A 503  MAN A 504                               
SITE     1 AC3  3 NAG A 502  MAN A 504  MAN A 505                               
SITE     1 AC4  3 NAG A 502  BMA A 503  MAN A 505                               
SITE     1 AC5  2 BMA A 503  MAN A 504                                          
SITE     1 AC6  4 ASN A 131  TYR A 162  ALA A 250  NAG A 507                    
SITE     1 AC7  2 ARG A 248  NAG A 506                                          
SITE     1 AC8  1 ASN A 116                                                     
SITE     1 AC9  6 PHE A 107  ASP A 110  ASN A 112  THR A 118                    
SITE     2 AC9  6 SER A 277  HOH A 604                                          
SITE     1 BC1  4 PHE A 321  TYR A 323  ARG A 349  CYS A 350                    
CRYST1   69.754   69.754  334.802  90.00  90.00 120.00 P 32 2 1      6          
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      0.014336  0.008277  0.000000        0.00000                         
SCALE2      0.000000  0.016554  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.002987        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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