GenomeNet

Database: PDB
Entry: 4PLO
LinkDB: 4PLO
Original site: 4PLO 
HEADER    PROTEIN BINDING                         18-MAY-14   4PLO              
TITLE     CRYSTAL STRUCTURE OF CHICKEN NETRIN-1 (LN-LE3) IN COMPLEX WITH MOUSE  
TITLE    2 DCC (FN4-5)                                                          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: NETRIN RECEPTOR DCC;                                       
COMPND   3 CHAIN: B;                                                            
COMPND   4 FRAGMENT: FN4-4 (UNP RESIDUES 721-922);                              
COMPND   5 SYNONYM: TUMOR SUPPRESSOR PROTEIN DCC;                               
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: NETRIN-1;                                                  
COMPND   8 CHAIN: A;                                                            
COMPND   9 FRAGMENT: LN-LE3 (UNP RESIDUES 26-457);                              
COMPND  10 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE   3 ORGANISM_COMMON: MOUSE;                                              
SOURCE   4 ORGANISM_TAXID: 10090;                                               
SOURCE   5 MOL_ID: 2;                                                           
SOURCE   6 ORGANISM_SCIENTIFIC: GALLUS GALLUS;                                  
SOURCE   7 ORGANISM_COMMON: CHICKEN;                                            
SOURCE   8 ORGANISM_TAXID: 9031;                                                
SOURCE   9 GENE: NTN1;                                                          
SOURCE  10 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE  11 EXPRESSION_SYSTEM_TAXID: 9606                                        
KEYWDS    ELONGATED, COMPLEX, PROTEIN BINDING                                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.XU,D.B.NIKOLOV                                                      
REVDAT   3   27-SEP-17 4PLO    1       COMPND SOURCE JRNL   REMARK              
REVDAT   2   25-JUN-14 4PLO    1       JRNL                                     
REVDAT   1   18-JUN-14 4PLO    0                                                
JRNL        AUTH   K.XU,Z.WU,N.RENIER,A.ANTIPENKO,D.TZVETKOVA-ROBEV,Y.XU,       
JRNL        AUTH 2 M.MINCHENKO,V.NARDI-DEI,K.R.RAJASHANKAR,J.HIMANEN,           
JRNL        AUTH 3 M.TESSIER-LAVIGNE,D.B.NIKOLOV                                
JRNL        TITL   NEURAL MIGRATION. STRUCTURES OF NETRIN-1 BOUND TO TWO        
JRNL        TITL 2 RECEPTORS PROVIDE INSIGHT INTO ITS AXON GUIDANCE MECHANISM.  
JRNL        REF    SCIENCE                       V. 344  1275 2014              
JRNL        REFN                   ESSN 1095-9203                               
JRNL        PMID   24876346                                                     
JRNL        DOI    10.1126/SCIENCE.1255149                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.8.2_1309)                   
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 48.75                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 22776                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.229                           
REMARK   3   R VALUE            (WORKING SET) : 0.224                           
REMARK   3   FREE R VALUE                     : 0.288                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 8.760                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1995                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 48.7565 -  6.9863    0.97     1651   159  0.2327 0.2770        
REMARK   3     2  6.9863 -  5.5478    0.98     1555   150  0.2327 0.2788        
REMARK   3     3  5.5478 -  4.8472    0.99     1571   151  0.2034 0.2625        
REMARK   3     4  4.8472 -  4.4044    0.98     1532   147  0.1686 0.2182        
REMARK   3     5  4.4044 -  4.0888    0.99     1535   147  0.1866 0.2601        
REMARK   3     6  4.0888 -  3.8479    1.00     1528   147  0.2048 0.2908        
REMARK   3     7  3.8479 -  3.6552    0.99     1549   148  0.2157 0.2953        
REMARK   3     8  3.6552 -  3.4962    0.99     1510   145  0.2125 0.2762        
REMARK   3     9  3.4962 -  3.3616    0.94     1448   139  0.2291 0.3229        
REMARK   3    10  3.3616 -  3.2456    0.95     1447   139  0.2478 0.3606        
REMARK   3    11  3.2456 -  3.1442    0.94     1419   136  0.2864 0.3421        
REMARK   3    12  3.1442 -  3.0543    0.93     1422   138  0.3048 0.3662        
REMARK   3    13  3.0543 -  2.9739    0.90     1387   132  0.3284 0.4677        
REMARK   3    14  2.9739 -  2.9010    0.82     1227   117  0.3727 0.3857        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.460            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 31.410           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 68.74                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.009           4926                                  
REMARK   3   ANGLE     :  1.414           6665                                  
REMARK   3   CHIRALITY :  0.112            722                                  
REMARK   3   PLANARITY :  0.008            862                                  
REMARK   3   DIHEDRAL  : 17.340           1804                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4PLO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-MAY-14.                  
REMARK 100 THE DEPOSITION ID IS D_1000201637.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-APR-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 24-ID-C                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9792                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M-F               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 22875                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.900                              
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     (%) : 96.1                               
REMARK 200  DATA REDUNDANCY                : 4.100                              
REMARK 200  R MERGE                    (I) : 0.11300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 5.8000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.95                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 85.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.10                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.88200                            
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: NULL                         
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 65.91                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.61                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.05 M AMMONIUM SULFATE, 0.05 M BIS      
REMARK 280  -TRIS PH 6.5, 30% V/V PENTAERYTHRITOL ETHOXYLATE, VAPOR             
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 298K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       24.73900            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      142.57950            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       36.46950            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      142.57950            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       24.73900            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       36.46950            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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 APPLY THE FOLLOWING TO CHAINS: B, A                                  
REMARK 350   BIOMT1   2  1.000000  0.000000  0.000000       49.47800            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000      -72.93900            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     PRO B   850                                                      
REMARK 465     LYS B   851                                                      
REMARK 465     ASN B   852                                                      
REMARK 465     GLN B   853                                                      
REMARK 465     LYS B   854                                                      
REMARK 465     THR B   855                                                      
REMARK 465     SER B   856                                                      
REMARK 465     ASP B   857                                                      
REMARK 465     VAL B   858                                                      
REMARK 465     PHE B   869                                                      
REMARK 465     SER B   870                                                      
REMARK 465     ALA B   871                                                      
REMARK 465     SER B   923                                                      
REMARK 465     GLY B   924                                                      
REMARK 465     GLY A    26                                                      
REMARK 465     TYR A    27                                                      
REMARK 465     PRO A    28                                                      
REMARK 465     GLY A    29                                                      
REMARK 465     LEU A    30                                                      
REMARK 465     ASN A    31                                                      
REMARK 465     MET A    32                                                      
REMARK 465     PHE A    33                                                      
REMARK 465     ALA A    34                                                      
REMARK 465     VAL A    35                                                      
REMARK 465     GLN A    36                                                      
REMARK 465     THR A    37                                                      
REMARK 465     ALA A    38                                                      
REMARK 465     GLN A    39                                                      
REMARK 465     GLY A   260                                                      
REMARK 465     ASP A   261                                                      
REMARK 465     GLU A   262                                                      
REMARK 465     ASN A   263                                                      
REMARK 465     GLU A   264                                                      
REMARK 465     PRO A   457                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     SER A 108    OG                                                  
REMARK 470     ASP A 265    CG   OD1  OD2                                       
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   OE1  GLU A   159     OG1  THR A   181              2.06            
REMARK 500   OG   SER A   362     O    SER A   366              2.12            
REMARK 500   O    ASP A   207     OG1  THR A   210              2.15            
REMARK 500   ND2  ASN A   346     O    HOH A   641              2.16            
REMARK 500   O    LEU A   347     O    HOH A   616              2.16            
REMARK 500   CB   CYS A   406     SG   CYS A   418              2.19            
REMARK 500   O    HOH A   606     O    HOH A   628              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
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   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    PHE A 109   C     PHE A 109   O      -0.130                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    PRO A  75   C   -  N   -  CA  ANGL. DEV. = -10.2 DEGREES          
REMARK 500    PRO A 116   C   -  N   -  CD  ANGL. DEV. =  13.4 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    PRO B 767       43.32    -92.58                                   
REMARK 500    LYS A  74      -73.95    -54.65                                   
REMARK 500    ASP A 112     -179.74    -67.06                                   
REMARK 500    PRO A 131       49.32    -87.08                                   
REMARK 500    SER A 254      -60.84   -103.72                                   
REMARK 500    LYS A 309       77.53   -118.74                                   
REMARK 500    LEU A 347       -3.55     67.99                                   
REMARK 500    LYS A 365      -76.19   -108.98                                   
REMARK 500    LEU A 371      -77.67    -91.28                                   
REMARK 500    LEU A 393      -14.46     69.85                                   
REMARK 500    THR A 421      -60.02   -104.27                                   
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   63     LYS A   64                 -147.51                    
REMARK 500 LYS A   74     PRO A   75                  143.74                    
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 PHE A 109   O                                                      
REMARK 620 2 ASP A 112   OD1  94.0                                              
REMARK 620 3 THR A 120   O    81.5 145.4                                        
REMARK 620 4 THR A 120   OG1  95.0  74.3  72.0                                  
REMARK 620 5 SER A 279   O    76.6 138.2  74.3 146.1                            
REMARK 620 6 HOH A 607   O   157.7 108.0  78.2  87.5  89.0                      
REMARK 620 7 HOH A 619   O    96.6  65.3 149.2 138.6  75.3  96.1                
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 SO4 A 504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 505                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 506                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 507                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 508                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 509                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 501 bound   
REMARK 800  to ASN A 97                                                         
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 502 bound   
REMARK 800  to ASN A 118                                                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 503 bound   
REMARK 800  to ASN A 133                                                        
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4PLM   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4PLN   RELATED DB: PDB                                   
DBREF  4PLO B  721   922  UNP    P70211   DCC_MOUSE      721    922             
DBREF  4PLO A   26   457  UNP    Q90922   NET1_CHICK      26    457             
SEQADV 4PLO GLY B  719  UNP  P70211              EXPRESSION TAG                 
SEQADV 4PLO ALA B  720  UNP  P70211              EXPRESSION TAG                 
SEQADV 4PLO SER B  923  UNP  P70211              EXPRESSION TAG                 
SEQADV 4PLO GLY B  924  UNP  P70211              EXPRESSION TAG                 
SEQRES   1 B  206  GLY ALA ASP GLU SER GLN VAL PRO ASP GLN PRO SER SER          
SEQRES   2 B  206  LEU HIS VAL ARG PRO GLN THR ASN CYS ILE ILE MET SER          
SEQRES   3 B  206  TRP THR PRO PRO LEU ASN PRO ASN ILE VAL VAL ARG GLY          
SEQRES   4 B  206  TYR ILE ILE GLY TYR GLY VAL GLY SER PRO TYR ALA GLU          
SEQRES   5 B  206  THR VAL ARG VAL ASP SER LYS GLN ARG TYR TYR SER ILE          
SEQRES   6 B  206  GLU ARG LEU GLU SER SER SER HIS TYR VAL ILE SER LEU          
SEQRES   7 B  206  LYS ALA PHE ASN ASN ALA GLY GLU GLY VAL PRO LEU TYR          
SEQRES   8 B  206  GLU SER ALA THR THR ARG SER ILE THR ASP VAL SER THR          
SEQRES   9 B  206  PRO MET LEU PRO PRO VAL GLY VAL GLN ALA VAL ALA LEU          
SEQRES  10 B  206  THR HIS GLU ALA VAL ARG VAL SER TRP ALA ASP ASN SER          
SEQRES  11 B  206  VAL PRO LYS ASN GLN LYS THR SER ASP VAL ARG LEU TYR          
SEQRES  12 B  206  THR VAL ARG TRP ARG THR SER PHE SER ALA SER ALA LYS          
SEQRES  13 B  206  TYR LYS SER GLU ASP THR THR SER LEU SER TYR THR ALA          
SEQRES  14 B  206  THR GLY LEU LYS PRO ASN THR MET TYR GLU PHE SER VAL          
SEQRES  15 B  206  MET VAL THR LYS ASN ARG ARG SER SER THR TRP SER MET          
SEQRES  16 B  206  THR ALA HIS ALA THR THR TYR GLU ALA SER GLY                  
SEQRES   1 A  432  GLY TYR PRO GLY LEU ASN MET PHE ALA VAL GLN THR ALA          
SEQRES   2 A  432  GLN PRO ASP PRO CYS TYR ASP GLU HIS GLY LEU PRO ARG          
SEQRES   3 A  432  ARG CYS ILE PRO ASP PHE VAL ASN SER ALA PHE GLY LYS          
SEQRES   4 A  432  GLU VAL LYS VAL SER SER THR CYS GLY LYS PRO PRO SER          
SEQRES   5 A  432  ARG TYR CYS VAL VAL THR GLU LYS GLY GLU GLU GLN VAL          
SEQRES   6 A  432  ARG SER CYS HIS LEU CYS ASN ALA SER ASP PRO LYS ARG          
SEQRES   7 A  432  ALA HIS PRO PRO SER PHE LEU THR ASP LEU ASN ASN PRO          
SEQRES   8 A  432  HIS ASN LEU THR CYS TRP GLN SER ASP SER TYR VAL GLN          
SEQRES   9 A  432  TYR PRO HIS ASN VAL THR LEU THR LEU SER LEU GLY LYS          
SEQRES  10 A  432  LYS PHE GLU VAL THR TYR VAL SER LEU GLN PHE CYS SER          
SEQRES  11 A  432  PRO ARG PRO GLU SER MET ALA ILE TYR LYS SER MET ASP          
SEQRES  12 A  432  TYR GLY LYS THR TRP VAL PRO PHE GLN PHE TYR SER THR          
SEQRES  13 A  432  GLN CYS ARG LYS MET TYR ASN LYS PRO SER ARG ALA ALA          
SEQRES  14 A  432  ILE THR LYS GLN ASN GLU GLN GLU ALA ILE CYS THR ASP          
SEQRES  15 A  432  SER HIS THR ASP VAL ARG PRO LEU SER GLY GLY LEU ILE          
SEQRES  16 A  432  ALA PHE SER THR LEU ASP GLY ARG PRO THR ALA HIS ASP          
SEQRES  17 A  432  PHE ASP ASN SER PRO VAL LEU GLN ASP TRP VAL THR ALA          
SEQRES  18 A  432  THR ASP ILE LYS VAL THR PHE SER ARG LEU HIS THR PHE          
SEQRES  19 A  432  GLY ASP GLU ASN GLU ASP ASP SER GLU LEU ALA ARG ASP          
SEQRES  20 A  432  SER TYR PHE TYR ALA VAL SER ASP LEU GLN VAL GLY GLY          
SEQRES  21 A  432  ARG CYS LYS CYS ASN GLY HIS ALA SER ARG CYS VAL ARG          
SEQRES  22 A  432  ASP ARG ASP ASP ASN LEU VAL CYS ASP CYS LYS HIS ASN          
SEQRES  23 A  432  THR ALA GLY PRO GLU CYS ASP ARG CYS LYS PRO PHE HIS          
SEQRES  24 A  432  TYR ASP ARG PRO TRP GLN ARG ALA THR ALA ARG GLU ALA          
SEQRES  25 A  432  ASN GLU CYS VAL ALA CYS ASN CYS ASN LEU HIS ALA ARG          
SEQRES  26 A  432  ARG CYS ARG PHE ASN MET GLU LEU TYR LYS LEU SER GLY          
SEQRES  27 A  432  ARG LYS SER GLY GLY VAL CYS LEU ASN CYS ARG HIS ASN          
SEQRES  28 A  432  THR ALA GLY ARG HIS CYS HIS TYR CYS LYS GLU GLY PHE          
SEQRES  29 A  432  TYR ARG ASP LEU SER LYS PRO ILE SER HIS ARG LYS ALA          
SEQRES  30 A  432  CYS LYS GLU CYS ASP CYS HIS PRO VAL GLY ALA ALA GLY          
SEQRES  31 A  432  GLN THR CYS ASN GLN THR THR GLY GLN CYS PRO CYS LYS          
SEQRES  32 A  432  ASP GLY VAL THR GLY ILE THR CYS ASN ARG CYS ALA LYS          
SEQRES  33 A  432  GLY TYR GLN GLN SER ARG SER PRO ILE ALA PRO CYS ILE          
SEQRES  34 A  432  LYS ILE PRO                                                  
HET    NAG  A 501      14                                                       
HET    NAG  A 502      14                                                       
HET    NAG  A 503      14                                                       
HET    SO4  A 504       5                                                       
HET    SO4  A 505       5                                                       
HET    SO4  A 506       5                                                       
HET    SO4  A 507       5                                                       
HET    SO4  A 508       5                                                       
HET     CA  A 509       1                                                       
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     SO4 SULFATE ION                                                      
HETNAM      CA CALCIUM ION                                                      
FORMUL   3  NAG    3(C8 H15 N O6)                                               
FORMUL   6  SO4    5(O4 S 2-)                                                   
FORMUL  11   CA    CA 2+                                                        
FORMUL  12  HOH   *72(H2 O)                                                     
HELIX    1 AA1 ILE B  817  THR B  822  1                                   6    
HELIX    2 AA2 PRO A  107  ASP A  112  1                                   6    
HELIX    3 AA3 GLN A  182  TYR A  187  1                                   6    
HELIX    4 AA4 ASP A  233  ASN A  236  5                                   4    
HELIX    5 AA5 SER A  237  VAL A  244  1                                   8    
HELIX    6 AA6 SER A  267  SER A  273  1                                   7    
HELIX    7 AA7 ASN A  355  SER A  362  1                                   8    
SHEET    1 AA1 3 LEU B 732  PRO B 736  0                                        
SHEET    2 AA1 3 ILE B 741  TRP B 745 -1  O  ILE B 742   N  ARG B 735           
SHEET    3 AA1 3 TYR B 780  ILE B 783 -1  O  TYR B 781   N  MET B 743           
SHEET    1 AA2 4 GLU B 770  ARG B 773  0                                        
SHEET    2 AA2 4 GLY B 757  VAL B 764 -1  N  TYR B 762   O  GLU B 770           
SHEET    3 AA2 4 HIS B 791  ASN B 800 -1  O  VAL B 793   N  GLY B 763           
SHEET    4 AA2 4 GLY B 803  GLU B 804 -1  O  GLY B 803   N  ASN B 800           
SHEET    1 AA3 4 GLU B 770  ARG B 773  0                                        
SHEET    2 AA3 4 GLY B 757  VAL B 764 -1  N  TYR B 762   O  GLU B 770           
SHEET    3 AA3 4 HIS B 791  ASN B 800 -1  O  VAL B 793   N  GLY B 763           
SHEET    4 AA3 4 LEU B 808  THR B 813 -1  O  GLU B 810   N  ILE B 794           
SHEET    1 AA4 3 VAL B 828  ALA B 834  0                                        
SHEET    2 AA4 3 ALA B 839  ALA B 845 -1  O  ARG B 841   N  VAL B 833           
SHEET    3 AA4 3 SER B 884  THR B 888 -1  O  ALA B 887   N  VAL B 840           
SHEET    1 AA5 4 LYS B 876  THR B 880  0                                        
SHEET    2 AA5 4 LEU B 860  THR B 867 -1  N  TYR B 861   O  THR B 880           
SHEET    3 AA5 4 MET B 895  LYS B 904 -1  O  SER B 899   N  ARG B 864           
SHEET    4 AA5 4 ARG B 907  SER B 908 -1  O  ARG B 907   N  LYS B 904           
SHEET    1 AA6 4 LYS B 876  THR B 880  0                                        
SHEET    2 AA6 4 LEU B 860  THR B 867 -1  N  TYR B 861   O  THR B 880           
SHEET    3 AA6 4 MET B 895  LYS B 904 -1  O  SER B 899   N  ARG B 864           
SHEET    4 AA6 4 ALA B 915  THR B 918 -1  O  ALA B 917   N  TYR B 896           
SHEET    1 AA7 3 VAL A  58  ASN A  59  0                                        
SHEET    2 AA7 3 ALA A 277  CYS A 287 -1  O  GLY A 285   N  VAL A  58           
SHEET    3 AA7 3 TRP A 122  GLN A 123 -1  N  TRP A 122   O  VAL A 278           
SHEET    1 AA8 3 ALA A 277  CYS A 287  0                                        
SHEET    2 AA8 3 VAL A 134  PHE A 153 -1  N  GLN A 152   O  SER A 279           
SHEET    3 AA8 3 LYS A  67  VAL A  68 -1  N  LYS A  67   O  THR A 137           
SHEET    1 AA9 6 GLY A 218  SER A 223  0                                        
SHEET    2 AA9 6 VAL A 134  PHE A 153 -1  N  PHE A 153   O  GLY A 218           
SHEET    3 AA9 6 THR A 245  ARG A 255 -1  O  VAL A 251   N  LEU A 136           
SHEET    4 AA9 6 SER A 160  SER A 166 -1  N  SER A 160   O  SER A 254           
SHEET    5 AA9 6 TRP A 173  TYR A 179 -1  O  PHE A 176   N  ILE A 163           
SHEET    6 AA9 6 ILE A 204  THR A 206  1  O  ILE A 204   N  PHE A 178           
SHEET    1 AB1 2 SER A  77  LYS A  85  0                                        
SHEET    2 AB1 2 GLU A  88  CYS A  96 -1  O  VAL A  90   N  THR A  83           
SHEET    1 AB2 2 CYS A 296  ARG A 298  0                                        
SHEET    2 AB2 2 LEU A 304  CYS A 306 -1  O  VAL A 305   N  VAL A 297           
SHEET    1 AB3 2 THR A 312  ALA A 313  0                                        
SHEET    2 AB3 2 ARG A 319  CYS A 320 -1  O  ARG A 319   N  ALA A 313           
SHEET    1 AB4 2 CYS A 352  PHE A 354  0                                        
SHEET    2 AB4 2 GLY A 368  CYS A 370 -1  O  VAL A 369   N  ARG A 353           
SHEET    1 AB5 2 THR A 377  ALA A 378  0                                        
SHEET    2 AB5 2 TYR A 384  CYS A 385 -1  O  TYR A 384   N  ALA A 378           
SHEET    1 AB6 2 PHE A 389  ARG A 391  0                                        
SHEET    2 AB6 2 CYS A 403  GLU A 405 -1  O  LYS A 404   N  TYR A 390           
SHEET    1 AB7 2 VAL A 431  THR A 432  0                                        
SHEET    2 AB7 2 ARG A 438  CYS A 439 -1  O  ARG A 438   N  THR A 432           
SHEET    1 AB8 2 TYR A 443  GLN A 445  0                                        
SHEET    2 AB8 2 CYS A 453  LYS A 455 -1  O  ILE A 454   N  GLN A 444           
SSBOND   1 CYS A   43    CYS A   53                          1555   1555  1.98  
SSBOND   2 CYS A   72    CYS A   96                          1555   1555  2.04  
SSBOND   3 CYS A   80    CYS A   93                          1555   1555  2.06  
SSBOND   4 CYS A  121    CYS A  154                          1555   1555  2.05  
SSBOND   5 CYS A  183    CYS A  205                          1555   1555  2.05  
SSBOND   6 CYS A  287    CYS A  296                          1555   1555  2.07  
SSBOND   7 CYS A  289    CYS A  306                          1555   1555  2.03  
SSBOND   8 CYS A  308    CYS A  317                          1555   1555  2.06  
SSBOND   9 CYS A  320    CYS A  340                          1555   1555  2.05  
SSBOND  10 CYS A  343    CYS A  352                          1555   1555  2.04  
SSBOND  11 CYS A  345    CYS A  370                          1555   1555  2.03  
SSBOND  12 CYS A  373    CYS A  382                          1555   1555  2.04  
SSBOND  13 CYS A  385    CYS A  403                          1555   1555  2.05  
SSBOND  14 CYS A  406    CYS A  418                          1555   1555  2.03  
SSBOND  15 CYS A  408    CYS A  425                          1555   1555  2.03  
SSBOND  16 CYS A  427    CYS A  436                          1555   1555  2.04  
SSBOND  17 CYS A  439    CYS A  453                          1555   1555  2.04  
LINK         ND2 ASN A  97                 C1  NAG A 501     1555   1555  1.45  
LINK         O   PHE A 109                CA    CA A 509     1555   1555  2.81  
LINK         OD1 ASP A 112                CA    CA A 509     1555   1555  2.44  
LINK         ND2 ASN A 118                 C1  NAG A 502     1555   1555  1.48  
LINK         O   THR A 120                CA    CA A 509     1555   1555  2.83  
LINK         OG1 THR A 120                CA    CA A 509     1555   1555  2.86  
LINK         ND2 ASN A 133                 C1  NAG A 503     1555   1555  1.45  
LINK         O   SER A 279                CA    CA A 509     1555   1555  2.39  
LINK        CA    CA A 509                 O   HOH A 607     1555   1555  2.50  
LINK        CA    CA A 509                 O   HOH A 619     1555   1555  2.38  
CISPEP   1 TYR A  130    PRO A  131          0        -2.18                     
CISPEP   2 ARG A  213    PRO A  214          0         7.44                     
CISPEP   3 SER A  366    GLY A  367          0        -0.05                     
CISPEP   4 GLY A  379    ARG A  380          0        15.50                     
SITE     1 AC1  3 HIS A  94  LEU A  95  ARG A 103                               
SITE     1 AC2  4 ARG A 157  HIS A 209  HOH A 620  HOH A 631                    
SITE     1 AC3  8 THR A 181  GLN A 182  CYS A 183  ARG A 184                    
SITE     2 AC3  8 SER A 191  ARG A 295  VAL A 297  HOH A 602                    
SITE     1 AC4  3 ARG A 350  ARG A 351  ASN A 372                               
SITE     1 AC5  4 GLY A 379  ARG A 380  HIS A 383  TYR A 384                    
SITE     1 AC6  6 PHE A 109  ASP A 112  THR A 120  SER A 279                    
SITE     2 AC6  6 HOH A 607  HOH A 619                                          
SITE     1 AC7  3 PRO A  76  ASN A  97  ASP A 100                               
SITE     1 AC8  4 PRO A 101  ASN A 118  LEU A 119  THR A 120                    
SITE     1 AC9  4 ASN A 133  TYR A 164  HOH A 611  HOH A 614                    
CRYST1   49.478   72.939  285.159  90.00  90.00  90.00 P 21 21 21    4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.020211  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.013710  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003507        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system