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Database: PDB
Entry: 4PLM
LinkDB: 4PLM
Original site: 4PLM 
HEADER    PROTEIN BINDING                         18-MAY-14   4PLM              
TITLE     CRYSTAL STRUCTURE OF CHICKEN NETRIN-1 (LN-LE3)                        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: NETRIN-1;                                                  
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: LN-LE3 (UNP RESIDUES 26-457);                              
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: GALLUS GALLUS;                                  
SOURCE   3 ORGANISM_COMMON: CHICKEN;                                            
SOURCE   4 ORGANISM_TAXID: 9031;                                                
SOURCE   5 GENE: NTN1;                                                          
SOURCE   6 EXPRESSION_SYSTEM: BACULOVIRIDAE;                                    
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 10442                                       
KEYWDS    ELONGATED, CYSTEINE RICH, GLYCOPROTEIN, PROTEIN BINDING               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.XU,D.B.NIKOLOV                                                      
REVDAT   4   27-SEP-17 4PLM    1       COMPND SOURCE JRNL   REMARK              
REVDAT   3   25-FEB-15 4PLM    1       REMARK                                   
REVDAT   2   25-JUN-14 4PLM    1       JRNL                                     
REVDAT   1   18-JUN-14 4PLM    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.    2.80 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) : 2.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 28.64                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 28902                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.199                           
REMARK   3   R VALUE            (WORKING SET) : 0.192                           
REMARK   3   FREE R VALUE                     : 0.257                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.080                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 2913                            
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 28.6403 -  7.6790    0.94     1176   126  0.2071 0.2507        
REMARK   3     2  7.6790 -  6.1146    0.99     1234   140  0.1965 0.2650        
REMARK   3     3  6.1146 -  5.3474    0.99     1248   138  0.1696 0.2501        
REMARK   3     4  5.3474 -  4.8610    1.00     1226   132  0.1452 0.2065        
REMARK   3     5  4.8610 -  4.5141    1.00     1231   151  0.1328 0.1493        
REMARK   3     6  4.5141 -  4.2488    1.00     1271   136  0.1437 0.2074        
REMARK   3     7  4.2488 -  4.0366    0.99     1245   139  0.1622 0.2649        
REMARK   3     8  4.0366 -  3.8614    0.99     1215   140  0.1708 0.2283        
REMARK   3     9  3.8614 -  3.7130    1.00     1244   144  0.1757 0.2743        
REMARK   3    10  3.7130 -  3.5851    0.99     1262   137  0.1744 0.2303        
REMARK   3    11  3.5851 -  3.4732    0.99     1205   130  0.1832 0.2544        
REMARK   3    12  3.4732 -  3.3741    1.00     1265   146  0.1939 0.2440        
REMARK   3    13  3.3741 -  3.2854    1.00     1238   134  0.2115 0.3429        
REMARK   3    14  3.2854 -  3.2054    0.99     1270   150  0.2457 0.3061        
REMARK   3    15  3.2054 -  3.1326    1.00     1170   135  0.2666 0.3622        
REMARK   3    16  3.1326 -  3.0660    0.99     1285   153  0.2613 0.3331        
REMARK   3    17  3.0660 -  3.0047    0.99     1186   133  0.2793 0.3324        
REMARK   3    18  3.0047 -  2.9481    0.99     1283   139  0.2909 0.3788        
REMARK   3    19  2.9481 -  2.8955    0.99     1242   138  0.3215 0.3735        
REMARK   3    20  2.8955 -  2.8465    0.99     1185   130  0.3110 0.4035        
REMARK   3    21  2.8465 -  2.8010    0.99     1308   142  0.3357 0.4315        
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)     : 0.390            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 30.430           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 63.72                          
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           3398                                  
REMARK   3   ANGLE     :  1.401           4578                                  
REMARK   3   CHIRALITY :  0.116            485                                  
REMARK   3   PLANARITY :  0.008            604                                  
REMARK   3   DIHEDRAL  : 17.143           1259                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 3                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 40 THROUGH 265 )                  
REMARK   3    ORIGIN FOR THE GROUP (A): -33.0828   3.7588  22.7374              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5369 T22:   0.4073                                     
REMARK   3      T33:   0.3736 T12:   0.0318                                     
REMARK   3      T13:  -0.0353 T23:  -0.0279                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.5748 L22:   4.5461                                     
REMARK   3      L33:   4.9281 L12:  -0.2343                                     
REMARK   3      L13:   0.2120 L23:   1.6445                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0294 S12:   0.0018 S13:  -0.5363                       
REMARK   3      S21:  -0.0400 S22:   0.0537 S23:  -0.1214                       
REMARK   3      S31:   0.4674 S32:  -0.0698 S33:  -0.0390                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 266 THROUGH 456 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -19.7163  26.7398  62.9174              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5405 T22:   0.7020                                     
REMARK   3      T33:   0.3855 T12:  -0.0283                                     
REMARK   3      T13:  -0.0550 T23:  -0.1372                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0397 L22:   0.7145                                     
REMARK   3      L33:   3.1371 L12:   0.0751                                     
REMARK   3      L13:   0.5975 L23:   0.8520                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0457 S12:   0.1072 S13:  -0.0858                       
REMARK   3      S21:  -0.3432 S22:  -0.0308 S23:  -0.0765                       
REMARK   3      S31:  -0.4906 S32:  -0.0487 S33:   0.0457                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 457 THROUGH 457 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -13.2825  52.9017 113.5523              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.7799 T22:   1.2725                                     
REMARK   3      T33:   0.7277 T12:  -0.3573                                     
REMARK   3      T13:  -0.1843 T23:  -0.0715                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0000 L22:   2.0000                                     
REMARK   3      L33:   2.0000 L12:   2.0000                                     
REMARK   3      L13:  -5.7603 L23:   4.3710                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -2.5986 S12:  -1.8799 S13:   0.5639                       
REMARK   3      S21:  -1.2777 S22:   2.2659 S23:  -0.4032                       
REMARK   3      S31:   2.7211 S32:   1.2861 S33:   0.3613                       
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 4PLM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-JUN-14.                  
REMARK 100 THE DEPOSITION ID IS D_1000201633.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-JAN-00                          
REMARK 200  TEMPERATURE           (KELVIN) : 298                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X9A                                
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                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MAR CCD 165 MM                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL                                
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 17693                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.700                              
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     (%) : 98.8                               
REMARK 200  DATA REDUNDANCY                : 5.200                              
REMARK 200  R MERGE                    (I) : 0.08500                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.3000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.80                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.10                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.73400                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 62.39                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.27                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NAOAC, NACACODYLATE, PH 6.5, VAPOR       
REMARK 280  DIFFUSION, TEMPERATURE 298K                                         
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      179.85867            
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       89.92933            
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       89.92933            
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      179.85867            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4290 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 45430 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -72.0 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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 350   BIOMT2   2 -0.866025  0.500000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      179.85867            
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     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     GLU A   262                                                      
REMARK 465     ASN A   263                                                      
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     GLU A 264    CG   CD   OE1  OE2                                  
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   O    HOH A   601     O    HOH A   603              2.06            
REMARK 500   O    HOH A   603     O    HOH A   624              2.07            
REMARK 500   ND2  ASN A   118     C2   NAG A   502              2.11            
REMARK 500   NE2  HIS A   324     O    HOH A   601              2.13            
REMARK 500   OH   TYR A   127     O    HOH A   602              2.17            
REMARK 500   NH2  ARG A   192     OD1  ASP A   207              2.18            
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    GLN A 129      158.62    173.61                                   
REMARK 500    HIS A 132      134.00    155.60                                   
REMARK 500    SER A 254      -89.84   -103.99                                   
REMARK 500    ASP A 266     -120.49     50.30                                   
REMARK 500    PHE A 323       -1.88     69.07                                   
REMARK 500    LYS A 365      -62.88   -101.46                                   
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 GLU A   84     LYS A   85                  148.47                    
REMARK 500 LYS A   85     GLY A   86                 -147.69                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 681        DISTANCE =  7.02 ANGSTROMS                       
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 504  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 PHE A 109   O                                                      
REMARK 620 2 ASP A 112   OD1  69.8                                              
REMARK 620 3 THR A 120   O    83.8 125.3                                        
REMARK 620 4 THR A 120   OG1 118.4  77.6  74.4                                  
REMARK 620 5 SER A 279   O    77.0 134.5  79.2 147.2                            
REMARK 620 6 HOH A 656   O   170.2 119.9  89.9  66.6  94.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 504                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 505                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 506                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 507                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
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: AC6                                                 
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: AC7                                                 
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: 4PLN   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4PLO   RELATED DB: PDB                                   
DBREF  4PLM A   26   457  UNP    Q90922   NET1_CHICK      26    457             
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     CA  A 504       1                                                       
HET     CL  A 505       1                                                       
HET     CL  A 506       1                                                       
HET     MG  A 507       1                                                       
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM      CA CALCIUM ION                                                      
HETNAM      CL CHLORIDE ION                                                     
HETNAM      MG MAGNESIUM ION                                                    
FORMUL   2  NAG    3(C8 H15 N O6)                                               
FORMUL   5   CA    CA 2+                                                        
FORMUL   6   CL    2(CL 1-)                                                     
FORMUL   8   MG    MG 2+                                                        
FORMUL   9  HOH   *82(H2 O)                                                     
HELIX    1 AA1 ASP A  100  ALA A  104  5                                   5    
HELIX    2 AA2 PRO A  106  LEU A  110  5                                   5    
HELIX    3 AA3 GLN A  182  ASN A  188  1                                   7    
HELIX    4 AA4 THR A  230  ASN A  236  5                                   7    
HELIX    5 AA5 SER A  237  VAL A  244  1                                   8    
HELIX    6 AA6 ASN A  355  SER A  362  1                                   8    
SHEET    1 AA1 3 VAL A  58  ASN A  59  0                                        
SHEET    2 AA1 3 ALA A 277  CYS A 287 -1  O  GLY A 285   N  VAL A  58           
SHEET    3 AA1 3 TRP A 122  GLN A 123 -1  N  TRP A 122   O  VAL A 278           
SHEET    1 AA2 3 LYS A  67  VAL A  68  0                                        
SHEET    2 AA2 3 VAL A 134  PHE A 153 -1  O  THR A 137   N  LYS A  67           
SHEET    3 AA2 3 GLY A 218  SER A 223 -1  O  PHE A 222   N  VAL A 149           
SHEET    1 AA3 6 ALA A 277  CYS A 287  0                                        
SHEET    2 AA3 6 VAL A 134  PHE A 153 -1  N  SER A 150   O  GLN A 282           
SHEET    3 AA3 6 THR A 245  PHE A 253 -1  O  ALA A 246   N  PHE A 144           
SHEET    4 AA3 6 SER A 160  SER A 166 -1  N  SER A 166   O  THR A 247           
SHEET    5 AA3 6 VAL A 174  SER A 180 -1  O  PHE A 176   N  ILE A 163           
SHEET    6 AA3 6 CYS A 205  THR A 206  1  O  THR A 206   N  SER A 180           
SHEET    1 AA4 2 SER A  77  LYS A  85  0                                        
SHEET    2 AA4 2 GLU A  88  CYS A  96 -1  O  GLU A  88   N  LYS A  85           
SHEET    1 AA5 2 CYS A 296  ARG A 298  0                                        
SHEET    2 AA5 2 LEU A 304  CYS A 306 -1  O  VAL A 305   N  VAL A 297           
SHEET    1 AA6 2 THR A 312  ALA A 313  0                                        
SHEET    2 AA6 2 ARG A 319  CYS A 320 -1  O  ARG A 319   N  ALA A 313           
SHEET    1 AA7 2 ARG A 351  PHE A 354  0                                        
SHEET    2 AA7 2 GLY A 368  LEU A 371 -1  O  VAL A 369   N  ARG A 353           
SHEET    1 AA8 2 THR A 377  ALA A 378  0                                        
SHEET    2 AA8 2 TYR A 384  CYS A 385 -1  O  TYR A 384   N  ALA A 378           
SHEET    1 AA9 2 PHE A 389  ARG A 391  0                                        
SHEET    2 AA9 2 CYS A 403  GLU A 405 -1  O  LYS A 404   N  TYR A 390           
SHEET    1 AB1 2 VAL A 431  THR A 432  0                                        
SHEET    2 AB1 2 ARG A 438  CYS A 439 -1  O  ARG A 438   N  THR A 432           
SHEET    1 AB2 2 TYR A 443  GLN A 445  0                                        
SHEET    2 AB2 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  2.04  
SSBOND   2 CYS A   72    CYS A   96                          1555   1555  2.01  
SSBOND   3 CYS A   80    CYS A   93                          1555   1555  2.03  
SSBOND   4 CYS A  121    CYS A  154                          1555   1555  2.02  
SSBOND   5 CYS A  183    CYS A  205                          1555   1555  2.04  
SSBOND   6 CYS A  287    CYS A  296                          1555   1555  2.04  
SSBOND   7 CYS A  289    CYS A  306                          1555   1555  2.03  
SSBOND   8 CYS A  308    CYS A  317                          1555   1555  2.03  
SSBOND   9 CYS A  320    CYS A  340                          1555   1555  2.04  
SSBOND  10 CYS A  343    CYS A  352                          1555   1555  2.03  
SSBOND  11 CYS A  345    CYS A  370                          1555   1555  2.04  
SSBOND  12 CYS A  373    CYS A  382                          1555   1555  2.04  
SSBOND  13 CYS A  385    CYS A  403                          1555   1555  2.02  
SSBOND  14 CYS A  406    CYS A  418                          1555   1555  2.03  
SSBOND  15 CYS A  408    CYS A  425                          1555   1555  2.02  
SSBOND  16 CYS A  427    CYS A  436                          1555   1555  2.02  
SSBOND  17 CYS A  439    CYS A  453                          1555   1555  2.04  
LINK         ND2 ASN A  97                 C1  NAG A 501     1555   1555  1.46  
LINK         O   PHE A 109                CA    CA A 504     1555   1555  2.39  
LINK         OD1 ASP A 112                CA    CA A 504     1555   1555  2.42  
LINK         ND2 ASN A 118                 C1  NAG A 502     1555   1555  1.44  
LINK         O   THR A 120                CA    CA A 504     1555   1555  2.56  
LINK         OG1 THR A 120                CA    CA A 504     1555   1555  2.92  
LINK         OE1 GLN A 123                MG    MG A 507     1555   1555  2.90  
LINK         ND2 ASN A 133                 C1  NAG A 503     1555   1555  1.45  
LINK         O   SER A 279                CA    CA A 504     1555   1555  2.30  
LINK        CA    CA A 504                 O   HOH A 656     1555   1555  2.38  
CISPEP   1 LYS A   74    PRO A   75          0         3.58                     
CISPEP   2 TYR A  130    PRO A  131          0        -9.34                     
CISPEP   3 VAL A  212    ARG A  213          0         4.89                     
CISPEP   4 ARG A  213    PRO A  214          0        -3.86                     
CISPEP   5 GLY A  260    ASP A  261          0       -20.19                     
SITE     1 AC1  5 PHE A 109  ASP A 112  THR A 120  SER A 279                    
SITE     2 AC1  5 HOH A 656                                                     
SITE     1 AC2  2 ARG A 157  LEU A 393                                          
SITE     1 AC3  3 HIS A 105  CYS A 121   MG A 507                               
SITE     1 AC4  2 GLN A 123   CL A 506                                          
SITE     1 AC5  3 ASN A  97  SER A  99  HOH A 679                               
SITE     1 AC6  1 ASN A 118                                                     
SITE     1 AC7  1 ASN A 133                                                     
CRYST1   62.627   62.627  269.788  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      0.015968  0.009219  0.000000        0.00000                         
SCALE2      0.000000  0.018438  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003707        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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