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Database: PDB
Entry: 4PLN
LinkDB: 4PLN
Original site: 4PLN 
HEADER    PROTEIN BINDING                         18-MAY-14   4PLN              
TITLE     CRYSTAL STRUCTURE OF CHICKEN NETRIN-1 (LN-LE3) COMPLEXED WITH MOUSE   
TITLE    2 NEOGENIN (FN4-5)                                                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: NETRIN-1;                                                  
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: LN-LE3 (UNP RESIDUES 26-457);                              
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: NEOGENIN;                                                  
COMPND   8 CHAIN: C, D;                                                         
COMPND   9 FRAGMENT: FN4-5 (UNP RESIDUES 765-964)                               
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: HOMO SAPIENS;                                     
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  10 ORGANISM_COMMON: MOUSE;                                              
SOURCE  11 ORGANISM_TAXID: 10090                                                
KEYWDS    ELONGATED, CYSTEINE RICH, GLYCOPROTEIN, COMPLEX, PROTEIN BINDING      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.XU,D.B.NIKOLOV                                                      
REVDAT   4   27-SEP-17 4PLN    1       COMPND SOURCE JRNL   REMARK              
REVDAT   3   25-FEB-15 4PLN    1       REMARK                                   
REVDAT   2   25-JUN-14 4PLN    1       JRNL                                     
REVDAT   1   18-JUN-14 4PLN    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.    3.20 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) : 3.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 49.95                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.360                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 40730                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.198                           
REMARK   3   R VALUE            (WORKING SET) : 0.196                           
REMARK   3   FREE R VALUE                     : 0.240                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.910                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2000                            
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 49.9552 -  7.6847    0.98     2847   148  0.1931 0.2168        
REMARK   3     2  7.6847 -  6.1031    0.97     2765   142  0.1911 0.2097        
REMARK   3     3  6.1031 -  5.3326    0.99     2829   146  0.1705 0.2222        
REMARK   3     4  5.3326 -  4.8455    0.96     2737   142  0.1547 0.1912        
REMARK   3     5  4.8455 -  4.4984    0.98     2760   142  0.1387 0.1785        
REMARK   3     6  4.4984 -  4.2333    0.99     2831   146  0.1535 0.1963        
REMARK   3     7  4.2333 -  4.0214    0.99     2775   144  0.1728 0.1976        
REMARK   3     8  4.0214 -  3.8464    0.99     2822   145  0.1981 0.2323        
REMARK   3     9  3.8464 -  3.6984    0.95     2683   139  0.2105 0.3002        
REMARK   3    10  3.6984 -  3.5708    0.98     2787   144  0.2297 0.2837        
REMARK   3    11  3.5708 -  3.4592    0.98     2771   143  0.2463 0.3129        
REMARK   3    12  3.4592 -  3.3603    0.98     2782   143  0.2595 0.3020        
REMARK   3    13  3.3603 -  3.2719    0.98     2802   145  0.2849 0.3886        
REMARK   3    14  3.2719 -  3.2000    0.90     2539   131  0.3266 0.3685        
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)     : 0.450            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.810           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 60.75                          
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      :  0.007          10116                                  
REMARK   3   ANGLE     :  1.173          13705                                  
REMARK   3   CHIRALITY :  0.048           1490                                  
REMARK   3   PLANARITY :  0.007           1787                                  
REMARK   3   DIHEDRAL  : 14.374           3731                                  
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 : 2                                           
REMARK   3   NCS GROUP : 1                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN A                                     
REMARK   3     SELECTION          : CHAIN B                                     
REMARK   3     ATOM PAIRS NUMBER  : 3663                                        
REMARK   3     RMSD               : NULL                                        
REMARK   3   NCS GROUP : 2                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN C                                     
REMARK   3     SELECTION          : CHAIN D                                     
REMARK   3     ATOM PAIRS NUMBER  : 1795                                        
REMARK   3     RMSD               : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4PLN 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_1000201636.                                   
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                             : 7.0                                
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 : HKL                                
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 40756                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.200                              
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     (%) : 97.8                               
REMARK 200  DATA REDUNDANCY                : 3.800                              
REMARK 200  R MERGE                    (I) : 0.20000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 2.6000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.31                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.89600                            
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   (%): 72.55                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.48                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M HEPES PH 7.0, 12% PEG3350, VAPOR    
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 298K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,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        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       65.10550            
REMARK 290   SMTRY3   2  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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 9100 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 62650 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -38.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D                            
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 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     PRO A   457                                                      
REMARK 465     GLY B    26                                                      
REMARK 465     TYR B    27                                                      
REMARK 465     PRO B    28                                                      
REMARK 465     GLY B    29                                                      
REMARK 465     LEU B    30                                                      
REMARK 465     ASN B    31                                                      
REMARK 465     MET B    32                                                      
REMARK 465     PHE B    33                                                      
REMARK 465     ALA B    34                                                      
REMARK 465     VAL B    35                                                      
REMARK 465     GLN B    36                                                      
REMARK 465     THR B    37                                                      
REMARK 465     ALA B    38                                                      
REMARK 465     GLN B    39                                                      
REMARK 465     PRO B   457                                                      
REMARK 465     GLY D   967                                                      
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 470     SER B 108    OG                                                  
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    ASP B   100     N    LYS B   102              1.70            
REMARK 500   NZ   LYS B   142     OE2  GLU B   316              1.98            
REMARK 500   OE2  GLU B    84     NH1  ARG B   213              2.06            
REMARK 500   ND2  ASN B   118     C2   NAG B   502              2.10            
REMARK 500   NH2  ARG A   374     OE2  GLU B    46              2.12            
REMARK 500   O    GLU A   200     NH1  ARG A   228              2.12            
REMARK 500   ND2  ASN B   133     C2   NAG B   503              2.14            
REMARK 500   ND2  ASN A   133     C2   NAG A   503              2.15            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   OE1  GLN D   924     O7   NAG A   501     2545     1.84            
REMARK 500   OE2  GLU B   268     NE   ARG C   951     2645     2.17            
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 101   C   -  N   -  CD  ANGL. DEV. =  12.9 DEGREES          
REMARK 500    PRO B  75   C   -  N   -  CA  ANGL. DEV. = -15.1 DEGREES          
REMARK 500    PRO B 101   C   -  N   -  CD  ANGL. DEV. = -21.0 DEGREES          
REMARK 500    PRO D 832   C   -  N   -  CD  ANGL. DEV. =  13.7 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    HIS A  47      154.49    179.93                                   
REMARK 500    ALA A  98       -2.57    -49.18                                   
REMARK 500    PRO A 101       11.62    -66.99                                   
REMARK 500    PRO A 107       36.19    -79.02                                   
REMARK 500    PRO A 131       32.29    -87.63                                   
REMARK 500    PHE A 176      -60.42   -105.40                                   
REMARK 500    MET A 186      -63.54    -99.18                                   
REMARK 500    SER A 191     -168.27    -77.50                                   
REMARK 500    HIS A 209       18.46     58.37                                   
REMARK 500    ALA A 334       -7.95     69.73                                   
REMARK 500    ARG A 335      -64.81   -101.72                                   
REMARK 500    ASN A 376       -0.64     69.00                                   
REMARK 500    ASP B  45     -177.42    -64.99                                   
REMARK 500    HIS B  47      154.43    178.58                                   
REMARK 500    ALA B  98       25.74    -70.68                                   
REMARK 500    PRO B 101      -14.91    -24.93                                   
REMARK 500    TYR B 127       77.00     50.11                                   
REMARK 500    PHE B 176      -60.80   -106.42                                   
REMARK 500    MET B 186      -64.15    -98.39                                   
REMARK 500    SER B 191     -169.65    -77.11                                   
REMARK 500    ASP B 265      -70.07    -56.89                                   
REMARK 500    PHE B 323       -6.71     65.30                                   
REMARK 500    ALA B 334       -8.00     69.75                                   
REMARK 500    ARG B 335      -64.29   -103.14                                   
REMARK 500    ASN B 376       -0.78     69.59                                   
REMARK 500    VAL C 782      -72.92    -58.01                                   
REMARK 500    SER C 810      139.92   -175.54                                   
REMARK 500    PRO C 811       46.39    -87.26                                   
REMARK 500    THR C 901      -69.42   -122.63                                   
REMARK 500    THR C 933      -76.80   -105.26                                   
REMARK 500    SER C 966       -1.54     68.49                                   
REMARK 500    SER D 810      138.93   -176.10                                   
REMARK 500    PRO D 811       46.82    -86.90                                   
REMARK 500    THR D 901      -70.84   -123.09                                   
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 ASP A  211     VAL A  212                  145.84                    
REMARK 500 GLU A  264     ASP A  265                  137.80                    
REMARK 500 LYS B   74     PRO B   75                  145.19                    
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 504  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 PHE A 109   O                                                      
REMARK 620 2 ASP A 112   OD1  79.8                                              
REMARK 620 3 THR A 120   O    62.1 113.6                                        
REMARK 620 4 THR A 120   OG1  84.6  64.9  59.7                                  
REMARK 620 5 SER A 279   O    64.7 135.0  74.1 132.8                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B 504  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 PHE B 109   O                                                      
REMARK 620 2 ASP B 112   OD1  68.1                                              
REMARK 620 3 THR B 120   O    69.2 114.7                                        
REMARK 620 4 THR B 120   OG1  84.8  67.3  61.8                                  
REMARK 620 5 SER B 279   O    76.7 137.0  72.2 133.9                            
REMARK 620 N                    1     2     3     4                             
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 CA B 504                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
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: AC4                                                 
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: AC5                                                 
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 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 501 bound   
REMARK 800  to ASN B 97                                                         
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 502 bound   
REMARK 800  to ASN B 118                                                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 503 bound   
REMARK 800  to ASN B 133                                                        
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4PLM   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4PLO   RELATED DB: PDB                                   
DBREF  4PLN A   26   457  UNP    Q90922   NET1_CHICK      26    457             
DBREF  4PLN B   26   457  UNP    Q90922   NET1_CHICK      26    457             
DBREF  4PLN C  765   964  UNP    P97798   NEO1_MOUSE     765    964             
DBREF  4PLN D  765   964  UNP    P97798   NEO1_MOUSE     765    964             
SEQADV 4PLN GLY C  763  UNP  P97798              EXPRESSION TAG                 
SEQADV 4PLN SER C  764  UNP  P97798              EXPRESSION TAG                 
SEQADV 4PLN GLN C  924  UNP  P97798    ASN   924 ENGINEERED MUTATION            
SEQADV 4PLN ALA C  965  UNP  P97798              EXPRESSION TAG                 
SEQADV 4PLN SER C  966  UNP  P97798              EXPRESSION TAG                 
SEQADV 4PLN GLY C  967  UNP  P97798              EXPRESSION TAG                 
SEQADV 4PLN GLY D  763  UNP  P97798              EXPRESSION TAG                 
SEQADV 4PLN SER D  764  UNP  P97798              EXPRESSION TAG                 
SEQADV 4PLN GLN D  924  UNP  P97798    ASN   924 ENGINEERED MUTATION            
SEQADV 4PLN ALA D  965  UNP  P97798              EXPRESSION TAG                 
SEQADV 4PLN SER D  966  UNP  P97798              EXPRESSION TAG                 
SEQADV 4PLN GLY D  967  UNP  P97798              EXPRESSION TAG                 
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                                                  
SEQRES   1 B  432  GLY TYR PRO GLY LEU ASN MET PHE ALA VAL GLN THR ALA          
SEQRES   2 B  432  GLN PRO ASP PRO CYS TYR ASP GLU HIS GLY LEU PRO ARG          
SEQRES   3 B  432  ARG CYS ILE PRO ASP PHE VAL ASN SER ALA PHE GLY LYS          
SEQRES   4 B  432  GLU VAL LYS VAL SER SER THR CYS GLY LYS PRO PRO SER          
SEQRES   5 B  432  ARG TYR CYS VAL VAL THR GLU LYS GLY GLU GLU GLN VAL          
SEQRES   6 B  432  ARG SER CYS HIS LEU CYS ASN ALA SER ASP PRO LYS ARG          
SEQRES   7 B  432  ALA HIS PRO PRO SER PHE LEU THR ASP LEU ASN ASN PRO          
SEQRES   8 B  432  HIS ASN LEU THR CYS TRP GLN SER ASP SER TYR VAL GLN          
SEQRES   9 B  432  TYR PRO HIS ASN VAL THR LEU THR LEU SER LEU GLY LYS          
SEQRES  10 B  432  LYS PHE GLU VAL THR TYR VAL SER LEU GLN PHE CYS SER          
SEQRES  11 B  432  PRO ARG PRO GLU SER MET ALA ILE TYR LYS SER MET ASP          
SEQRES  12 B  432  TYR GLY LYS THR TRP VAL PRO PHE GLN PHE TYR SER THR          
SEQRES  13 B  432  GLN CYS ARG LYS MET TYR ASN LYS PRO SER ARG ALA ALA          
SEQRES  14 B  432  ILE THR LYS GLN ASN GLU GLN GLU ALA ILE CYS THR ASP          
SEQRES  15 B  432  SER HIS THR ASP VAL ARG PRO LEU SER GLY GLY LEU ILE          
SEQRES  16 B  432  ALA PHE SER THR LEU ASP GLY ARG PRO THR ALA HIS ASP          
SEQRES  17 B  432  PHE ASP ASN SER PRO VAL LEU GLN ASP TRP VAL THR ALA          
SEQRES  18 B  432  THR ASP ILE LYS VAL THR PHE SER ARG LEU HIS THR PHE          
SEQRES  19 B  432  GLY ASP GLU ASN GLU ASP ASP SER GLU LEU ALA ARG ASP          
SEQRES  20 B  432  SER TYR PHE TYR ALA VAL SER ASP LEU GLN VAL GLY GLY          
SEQRES  21 B  432  ARG CYS LYS CYS ASN GLY HIS ALA SER ARG CYS VAL ARG          
SEQRES  22 B  432  ASP ARG ASP ASP ASN LEU VAL CYS ASP CYS LYS HIS ASN          
SEQRES  23 B  432  THR ALA GLY PRO GLU CYS ASP ARG CYS LYS PRO PHE HIS          
SEQRES  24 B  432  TYR ASP ARG PRO TRP GLN ARG ALA THR ALA ARG GLU ALA          
SEQRES  25 B  432  ASN GLU CYS VAL ALA CYS ASN CYS ASN LEU HIS ALA ARG          
SEQRES  26 B  432  ARG CYS ARG PHE ASN MET GLU LEU TYR LYS LEU SER GLY          
SEQRES  27 B  432  ARG LYS SER GLY GLY VAL CYS LEU ASN CYS ARG HIS ASN          
SEQRES  28 B  432  THR ALA GLY ARG HIS CYS HIS TYR CYS LYS GLU GLY PHE          
SEQRES  29 B  432  TYR ARG ASP LEU SER LYS PRO ILE SER HIS ARG LYS ALA          
SEQRES  30 B  432  CYS LYS GLU CYS ASP CYS HIS PRO VAL GLY ALA ALA GLY          
SEQRES  31 B  432  GLN THR CYS ASN GLN THR THR GLY GLN CYS PRO CYS LYS          
SEQRES  32 B  432  ASP GLY VAL THR GLY ILE THR CYS ASN ARG CYS ALA LYS          
SEQRES  33 B  432  GLY TYR GLN GLN SER ARG SER PRO ILE ALA PRO CYS ILE          
SEQRES  34 B  432  LYS ILE PRO                                                  
SEQRES   1 C  205  GLY SER ASP GLU THR ARG VAL PRO GLU VAL PRO SER SER          
SEQRES   2 C  205  LEU HIS VAL ARG PRO LEU VAL THR SER ILE VAL VAL SER          
SEQRES   3 C  205  TRP THR PRO PRO GLU ASN GLN ASN ILE VAL VAL ARG GLY          
SEQRES   4 C  205  TYR ALA ILE GLY TYR GLY ILE GLY SER PRO HIS ALA GLN          
SEQRES   5 C  205  THR ILE LYS VAL ASP TYR LYS GLN ARG TYR TYR THR ILE          
SEQRES   6 C  205  GLU ASN LEU ASP PRO SER SER HIS TYR VAL ILE THR LEU          
SEQRES   7 C  205  LYS ALA PHE ASN ASN VAL GLY GLU GLY ILE PRO LEU TYR          
SEQRES   8 C  205  GLU SER ALA VAL THR ARG PRO HIS THR VAL PRO ASP PRO          
SEQRES   9 C  205  THR PRO MET MET PRO PRO VAL GLY VAL GLN ALA SER ILE          
SEQRES  10 C  205  LEU SER HIS ASP THR ILE ARG ILE THR TRP ALA ASP ASN          
SEQRES  11 C  205  SER LEU PRO LYS HIS GLN LYS ILE THR ASP SER ARG TYR          
SEQRES  12 C  205  TYR THR VAL ARG TRP LYS THR ASN ILE PRO ALA ASN THR          
SEQRES  13 C  205  LYS TYR LYS ASN ALA GLN ALA THR THR LEU SER TYR LEU          
SEQRES  14 C  205  VAL THR GLY LEU LYS PRO ASN THR LEU TYR GLU PHE SER          
SEQRES  15 C  205  VAL MET VAL THR LYS GLY ARG ARG SER SER THR TRP SER          
SEQRES  16 C  205  MET THR ALA HIS GLY ALA THR ALA SER GLY                      
SEQRES   1 D  205  GLY SER ASP GLU THR ARG VAL PRO GLU VAL PRO SER SER          
SEQRES   2 D  205  LEU HIS VAL ARG PRO LEU VAL THR SER ILE VAL VAL SER          
SEQRES   3 D  205  TRP THR PRO PRO GLU ASN GLN ASN ILE VAL VAL ARG GLY          
SEQRES   4 D  205  TYR ALA ILE GLY TYR GLY ILE GLY SER PRO HIS ALA GLN          
SEQRES   5 D  205  THR ILE LYS VAL ASP TYR LYS GLN ARG TYR TYR THR ILE          
SEQRES   6 D  205  GLU ASN LEU ASP PRO SER SER HIS TYR VAL ILE THR LEU          
SEQRES   7 D  205  LYS ALA PHE ASN ASN VAL GLY GLU GLY ILE PRO LEU TYR          
SEQRES   8 D  205  GLU SER ALA VAL THR ARG PRO HIS THR VAL PRO ASP PRO          
SEQRES   9 D  205  THR PRO MET MET PRO PRO VAL GLY VAL GLN ALA SER ILE          
SEQRES  10 D  205  LEU SER HIS ASP THR ILE ARG ILE THR TRP ALA ASP ASN          
SEQRES  11 D  205  SER LEU PRO LYS HIS GLN LYS ILE THR ASP SER ARG TYR          
SEQRES  12 D  205  TYR THR VAL ARG TRP LYS THR ASN ILE PRO ALA ASN THR          
SEQRES  13 D  205  LYS TYR LYS ASN ALA GLN ALA THR THR LEU SER TYR LEU          
SEQRES  14 D  205  VAL THR GLY LEU LYS PRO ASN THR LEU TYR GLU PHE SER          
SEQRES  15 D  205  VAL MET VAL THR LYS GLY ARG ARG SER SER THR TRP SER          
SEQRES  16 D  205  MET THR ALA HIS GLY ALA THR ALA SER GLY                      
HET    NAG  A 501      14                                                       
HET    NAG  A 502      14                                                       
HET    NAG  A 503      14                                                       
HET     CA  A 504       1                                                       
HET    NAG  B 501      14                                                       
HET    NAG  B 502      14                                                       
HET    NAG  B 503      14                                                       
HET     CA  B 504       1                                                       
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM      CA CALCIUM ION                                                      
FORMUL   5  NAG    6(C8 H15 N O6)                                               
FORMUL   8   CA    2(CA 2+)                                                     
HELIX    1 AA1 GLN A  182  ASN A  188  1                                   7    
HELIX    2 AA2 THR A  230  ASN A  236  5                                   7    
HELIX    3 AA3 SER A  237  VAL A  244  1                                   8    
HELIX    4 AA4 SER A  267  ASP A  272  1                                   6    
HELIX    5 AA5 ASN A  355  SER A  362  1                                   8    
HELIX    6 AA6 PRO B  107  ASP B  112  1                                   6    
HELIX    7 AA7 GLN B  182  ASN B  188  1                                   7    
HELIX    8 AA8 THR B  230  ASN B  236  5                                   7    
HELIX    9 AA9 SER B  237  VAL B  244  1                                   8    
HELIX   10 AB1 SER B  267  ASP B  272  1                                   6    
HELIX   11 AB2 ASN B  355  SER B  362  1                                   8    
SHEET    1 AA1 3 PHE A  57  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 6 ALA A 277  CYS A 287  0                                        
SHEET    2 AA2 6 VAL A 134  PHE A 153 -1  N  SER A 150   O  GLN A 282           
SHEET    3 AA2 6 THR A 245  ARG A 255 -1  O  ILE A 249   N  LEU A 138           
SHEET    4 AA2 6 SER A 160  SER A 166 -1  N  SER A 166   O  THR A 247           
SHEET    5 AA2 6 VAL A 174  SER A 180 -1  O  PHE A 176   N  ILE A 163           
SHEET    6 AA2 6 CYS A 205  THR A 206  1  O  THR A 206   N  PHE A 178           
SHEET    1 AA3 3 LYS A  67  VAL A  68  0                                        
SHEET    2 AA3 3 VAL A 134  PHE A 153 -1  O  THR A 137   N  LYS A  67           
SHEET    3 AA3 3 LEU A 219  SER A 223 -1  O  PHE A 222   N  VAL A 149           
SHEET    1 AA4 2 SER A  77  GLU A  84  0                                        
SHEET    2 AA4 2 GLN A  89  CYS A  96 -1  O  HIS A  94   N  TYR A  79           
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 CYS A 352  PHE A 354  0                                        
SHEET    2 AA7 2 GLY A 368  CYS A 370 -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           
SHEET    1 AB3 3 PHE B  57  ASN B  59  0                                        
SHEET    2 AB3 3 ALA B 277  CYS B 287 -1  O  GLY B 285   N  VAL B  58           
SHEET    3 AB3 3 TRP B 122  GLN B 123 -1  N  TRP B 122   O  VAL B 278           
SHEET    1 AB4 6 ALA B 277  CYS B 287  0                                        
SHEET    2 AB4 6 VAL B 134  PHE B 153 -1  N  GLN B 152   O  SER B 279           
SHEET    3 AB4 6 THR B 245  ARG B 255 -1  O  ILE B 249   N  LEU B 138           
SHEET    4 AB4 6 SER B 160  SER B 166 -1  N  SER B 166   O  THR B 247           
SHEET    5 AB4 6 VAL B 174  SER B 180 -1  O  PHE B 176   N  ILE B 163           
SHEET    6 AB4 6 CYS B 205  THR B 206  1  O  THR B 206   N  SER B 180           
SHEET    1 AB5 3 LYS B  67  VAL B  68  0                                        
SHEET    2 AB5 3 VAL B 134  PHE B 153 -1  O  THR B 137   N  LYS B  67           
SHEET    3 AB5 3 LEU B 219  SER B 223 -1  O  PHE B 222   N  VAL B 149           
SHEET    1 AB6 2 SER B  77  LYS B  85  0                                        
SHEET    2 AB6 2 GLU B  88  CYS B  96 -1  O  HIS B  94   N  TYR B  79           
SHEET    1 AB7 2 CYS B 296  ARG B 298  0                                        
SHEET    2 AB7 2 LEU B 304  CYS B 306 -1  O  VAL B 305   N  VAL B 297           
SHEET    1 AB8 2 THR B 312  ALA B 313  0                                        
SHEET    2 AB8 2 ARG B 319  CYS B 320 -1  O  ARG B 319   N  ALA B 313           
SHEET    1 AB9 2 CYS B 352  PHE B 354  0                                        
SHEET    2 AB9 2 GLY B 368  CYS B 370 -1  O  VAL B 369   N  ARG B 353           
SHEET    1 AC1 2 THR B 377  ALA B 378  0                                        
SHEET    2 AC1 2 TYR B 384  CYS B 385 -1  O  TYR B 384   N  ALA B 378           
SHEET    1 AC2 2 PHE B 389  ARG B 391  0                                        
SHEET    2 AC2 2 CYS B 403  GLU B 405 -1  O  LYS B 404   N  TYR B 390           
SHEET    1 AC3 2 VAL B 431  THR B 432  0                                        
SHEET    2 AC3 2 ARG B 438  CYS B 439 -1  O  ARG B 438   N  THR B 432           
SHEET    1 AC4 2 TYR B 443  GLN B 445  0                                        
SHEET    2 AC4 2 CYS B 453  LYS B 455 -1  O  ILE B 454   N  GLN B 444           
SHEET    1 AC5 3 PRO C 773  PRO C 780  0                                        
SHEET    2 AC5 3 ILE C 785  PRO C 792 -1  O  VAL C 786   N  ARG C 779           
SHEET    3 AC5 3 TYR C 824  ILE C 827 -1  O  TYR C 825   N  VAL C 787           
SHEET    1 AC6 4 GLN C 814  ASP C 819  0                                        
SHEET    2 AC6 4 GLY C 801  ILE C 808 -1  N  ILE C 804   O  ILE C 816           
SHEET    3 AC6 4 HIS C 835  ASN C 844 -1  O  LYS C 841   N  ALA C 803           
SHEET    4 AC6 4 GLY C 847  GLU C 848 -1  O  GLY C 847   N  ASN C 844           
SHEET    1 AC7 4 GLN C 814  ASP C 819  0                                        
SHEET    2 AC7 4 GLY C 801  ILE C 808 -1  N  ILE C 804   O  ILE C 816           
SHEET    3 AC7 4 HIS C 835  ASN C 844 -1  O  LYS C 841   N  ALA C 803           
SHEET    4 AC7 4 LEU C 852  VAL C 857 -1  O  ALA C 856   N  TYR C 836           
SHEET    1 AC8 3 VAL C 873  ILE C 879  0                                        
SHEET    2 AC8 3 ILE C 885  ALA C 890 -1  O  ARG C 886   N  SER C 878           
SHEET    3 AC8 3 SER C 929  VAL C 932 -1  O  TYR C 930   N  ILE C 887           
SHEET    1 AC9 4 LYS C 921  ALA C 925  0                                        
SHEET    2 AC9 4 ARG C 904  THR C 912 -1  N  VAL C 908   O  ALA C 923           
SHEET    3 AC9 4 LEU C 940  LYS C 949 -1  O  GLU C 942   N  LYS C 911           
SHEET    4 AC9 4 ARG C 952  SER C 953 -1  O  ARG C 952   N  LYS C 949           
SHEET    1 AD1 4 LYS C 921  ALA C 925  0                                        
SHEET    2 AD1 4 ARG C 904  THR C 912 -1  N  VAL C 908   O  ALA C 923           
SHEET    3 AD1 4 LEU C 940  LYS C 949 -1  O  GLU C 942   N  LYS C 911           
SHEET    4 AD1 4 ALA C 960  ALA C 963 -1  O  ALA C 960   N  PHE C 943           
SHEET    1 AD2 3 SER D 775  PRO D 780  0                                        
SHEET    2 AD2 3 ILE D 785  THR D 790 -1  O  SER D 788   N  HIS D 777           
SHEET    3 AD2 3 TYR D 824  ILE D 827 -1  O  TYR D 825   N  VAL D 787           
SHEET    1 AD3 4 GLN D 814  ASP D 819  0                                        
SHEET    2 AD3 4 GLY D 801  ILE D 808 -1  N  ILE D 804   O  ILE D 816           
SHEET    3 AD3 4 HIS D 835  ASN D 844 -1  O  LYS D 841   N  ALA D 803           
SHEET    4 AD3 4 GLY D 847  GLU D 848 -1  O  GLY D 847   N  ASN D 844           
SHEET    1 AD4 4 GLN D 814  ASP D 819  0                                        
SHEET    2 AD4 4 GLY D 801  ILE D 808 -1  N  ILE D 804   O  ILE D 816           
SHEET    3 AD4 4 HIS D 835  ASN D 844 -1  O  LYS D 841   N  ALA D 803           
SHEET    4 AD4 4 LEU D 852  VAL D 857 -1  O  ALA D 856   N  TYR D 836           
SHEET    1 AD5 3 VAL D 873  ILE D 879  0                                        
SHEET    2 AD5 3 ILE D 885  ALA D 890 -1  O  THR D 888   N  GLN D 876           
SHEET    3 AD5 3 SER D 929  VAL D 932 -1  O  VAL D 932   N  ILE D 885           
SHEET    1 AD6 4 LYS D 921  ALA D 925  0                                        
SHEET    2 AD6 4 ARG D 904  THR D 912 -1  N  VAL D 908   O  ALA D 923           
SHEET    3 AD6 4 LEU D 940  LYS D 949 -1  O  GLU D 942   N  LYS D 911           
SHEET    4 AD6 4 ARG D 952  SER D 953 -1  O  ARG D 952   N  LYS D 949           
SHEET    1 AD7 4 LYS D 921  ALA D 925  0                                        
SHEET    2 AD7 4 ARG D 904  THR D 912 -1  N  VAL D 908   O  ALA D 923           
SHEET    3 AD7 4 LEU D 940  LYS D 949 -1  O  GLU D 942   N  LYS D 911           
SHEET    4 AD7 4 ALA D 960  ALA D 963 -1  O  ALA D 960   N  PHE D 943           
SSBOND   1 CYS A   43    CYS A   53                          1555   1555  2.05  
SSBOND   2 CYS A   72    CYS A   96                          1555   1555  2.03  
SSBOND   3 CYS A   80    CYS A   93                          1555   1555  2.04  
SSBOND   4 CYS A  121    CYS A  154                          1555   1555  2.03  
SSBOND   5 CYS A  183    CYS A  205                          1555   1555  2.05  
SSBOND   6 CYS A  287    CYS A  296                          1555   1555  2.04  
SSBOND   7 CYS A  289    CYS A  306                          1555   1555  2.04  
SSBOND   8 CYS A  308    CYS A  317                          1555   1555  2.04  
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  2.01  
SSBOND  12 CYS A  373    CYS A  382                          1555   1555  2.04  
SSBOND  13 CYS A  385    CYS A  403                          1555   1555  2.04  
SSBOND  14 CYS A  406    CYS A  418                          1555   1555  2.05  
SSBOND  15 CYS A  408    CYS A  425                          1555   1555  2.05  
SSBOND  16 CYS A  427    CYS A  436                          1555   1555  2.04  
SSBOND  17 CYS A  439    CYS A  453                          1555   1555  2.03  
SSBOND  18 CYS B   43    CYS B   53                          1555   1555  1.99  
SSBOND  19 CYS B   72    CYS B   96                          1555   1555  2.04  
SSBOND  20 CYS B   80    CYS B   93                          1555   1555  2.05  
SSBOND  21 CYS B  121    CYS B  154                          1555   1555  2.04  
SSBOND  22 CYS B  183    CYS B  205                          1555   1555  2.05  
SSBOND  23 CYS B  287    CYS B  296                          1555   1555  2.04  
SSBOND  24 CYS B  289    CYS B  306                          1555   1555  1.97  
SSBOND  25 CYS B  308    CYS B  317                          1555   1555  1.97  
SSBOND  26 CYS B  320    CYS B  340                          1555   1555  2.01  
SSBOND  27 CYS B  343    CYS B  352                          1555   1555  2.05  
SSBOND  28 CYS B  345    CYS B  370                          1555   1555  2.02  
SSBOND  29 CYS B  373    CYS B  382                          1555   1555  2.03  
SSBOND  30 CYS B  385    CYS B  403                          1555   1555  2.04  
SSBOND  31 CYS B  406    CYS B  418                          1555   1555  2.04  
SSBOND  32 CYS B  408    CYS B  425                          1555   1555  2.04  
SSBOND  33 CYS B  427    CYS B  436                          1555   1555  2.04  
SSBOND  34 CYS B  439    CYS B  453                          1555   1555  2.04  
LINK         ND2 ASN A  97                 C1  NAG A 501     1555   1555  1.48  
LINK         O   PHE A 109                CA    CA A 504     1555   1555  2.87  
LINK         OD1 ASP A 112                CA    CA A 504     1555   1555  2.41  
LINK         ND2 ASN A 118                 C1  NAG A 502     1555   1555  1.45  
LINK         O   THR A 120                CA    CA A 504     1555   1555  2.86  
LINK         OG1 THR A 120                CA    CA A 504     1555   1555  2.87  
LINK         ND2 ASN A 133                 C1  NAG A 503     1555   1555  1.44  
LINK         O   SER A 279                CA    CA A 504     1555   1555  2.33  
LINK         ND2 ASN B  97                 C1  NAG B 501     1555   1555  1.43  
LINK         O   PHE B 109                CA    CA B 504     1555   1555  2.60  
LINK         OD1 ASP B 112                CA    CA B 504     1555   1555  2.39  
LINK         ND2 ASN B 118                 C1  NAG B 502     1555   1555  1.45  
LINK         O   THR B 120                CA    CA B 504     1555   1555  2.74  
LINK         OG1 THR B 120                CA    CA B 504     1555   1555  2.42  
LINK         ND2 ASN B 133                 C1  NAG B 503     1555   1555  1.44  
LINK         O   SER B 279                CA    CA B 504     1555   1555  2.39  
CISPEP   1 HIS A   47    GLY A   48          0       -26.06                     
CISPEP   2 LYS A   74    PRO A   75          0        -3.34                     
CISPEP   3 TYR A  130    PRO A  131          0         1.43                     
CISPEP   4 VAL A  212    ARG A  213          0        15.75                     
CISPEP   5 ARG A  213    PRO A  214          0         4.88                     
CISPEP   6 HIS B   47    GLY B   48          0       -25.31                     
CISPEP   7 TYR B  130    PRO B  131          0         5.77                     
CISPEP   8 ARG B  213    PRO B  214          0        -0.06                     
CISPEP   9 ILE C  914    PRO C  915          0         2.98                     
CISPEP  10 PRO D  864    ASP D  865          0         4.53                     
CISPEP  11 ILE D  914    PRO D  915          0         4.82                     
SITE     1 AC1  4 PHE A 109  ASP A 112  THR A 120  SER A 279                    
SITE     1 AC2  4 PHE B 109  ASP B 112  THR B 120  SER B 279                    
SITE     1 AC3  2 ASN A  97  SER A  99                                          
SITE     1 AC4  3 PRO A 101  ASN A 118  LEU A 119                               
SITE     1 AC5  3 PRO A 131  ASN A 133  SER A 254                               
SITE     1 AC6  5 PRO B  76  LEU B  95  ASN B  97  SER B  99                    
SITE     2 AC6  5 ASP B 100                                                     
SITE     1 AC7  4 PRO B 101  PHE B 109  ASN B 118  LEU B 119                    
SITE     1 AC8  4 PRO B 131  HIS B 132  ASN B 133  SER B 254                    
CRYST1   79.070  130.211  126.037  90.00  99.98  90.00 P 1 21 1      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      0.012647  0.000000  0.002225        0.00000                         
SCALE2      0.000000  0.007680  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008056        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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