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Database: PDB
Entry: 5NET
LinkDB: 5NET
Original site: 5NET 
HEADER    VIRUS                                   11-MAR-17   5NET              
TITLE     LOCALISED RECONSTRUCTION OF INTEGRIN ALPHA V BETA 6 BOUND TO FOOT AND 
TITLE    2 MOUTH DISEASE VIRUS O1 MANISA - POSE A.                              
CAVEAT     5NET    ILE A 147 HAS WRONG CHIRALITY AT ATOM CA MAN A 606 HAS WRONG 
CAVEAT   2 5NET    CHIRALITY AT ATOM C1 MAN A 613 HAS WRONG CHIRALITY AT ATOM   
CAVEAT   3 5NET    C1 NAG B 501 HAS WRONG CHIRALITY AT ATOM C1                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: O1 MANISA VP1;                                             
COMPND   3 CHAIN: 1;                                                            
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MOL_ID: 2;                                                           
COMPND   6 MOLECULE: O1 MANISA VP2;                                             
COMPND   7 CHAIN: 2;                                                            
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MOL_ID: 3;                                                           
COMPND  10 MOLECULE: O1 MANISA VP3;                                             
COMPND  11 CHAIN: 3;                                                            
COMPND  12 ENGINEERED: YES;                                                     
COMPND  13 MOL_ID: 4;                                                           
COMPND  14 MOLECULE: O1 MANISA VP4;                                             
COMPND  15 CHAIN: 4;                                                            
COMPND  16 ENGINEERED: YES;                                                     
COMPND  17 MOL_ID: 5;                                                           
COMPND  18 MOLECULE: INTEGRIN ALPHA-V;                                          
COMPND  19 CHAIN: A;                                                            
COMPND  20 SYNONYM: VITRONECTIN RECEPTOR SUBUNIT ALPHA;                         
COMPND  21 ENGINEERED: YES;                                                     
COMPND  22 MOL_ID: 6;                                                           
COMPND  23 MOLECULE: INTEGRIN BETA-6;                                           
COMPND  24 CHAIN: B;                                                            
COMPND  25 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: FOOT-AND-MOUTH DISEASE VIRUS;                   
SOURCE   3 ORGANISM_TAXID: 12110;                                               
SOURCE   4 EXPRESSION_SYSTEM: CRICETINAE GEN. SP.;                              
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 36483;                                      
SOURCE   6 MOL_ID: 2;                                                           
SOURCE   7 ORGANISM_SCIENTIFIC: FOOT-AND-MOUTH DISEASE VIRUS;                   
SOURCE   8 ORGANISM_TAXID: 12110;                                               
SOURCE   9 EXPRESSION_SYSTEM: CRICETINAE GEN. SP.;                              
SOURCE  10 EXPRESSION_SYSTEM_TAXID: 36483;                                      
SOURCE  11 MOL_ID: 3;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: FOOT-AND-MOUTH DISEASE VIRUS;                   
SOURCE  13 ORGANISM_TAXID: 12110;                                               
SOURCE  14 EXPRESSION_SYSTEM: CRICETINAE GEN. SP.;                              
SOURCE  15 EXPRESSION_SYSTEM_TAXID: 36483;                                      
SOURCE  16 MOL_ID: 4;                                                           
SOURCE  17 ORGANISM_SCIENTIFIC: FOOT-AND-MOUTH DISEASE VIRUS;                   
SOURCE  18 ORGANISM_TAXID: 12110;                                               
SOURCE  19 EXPRESSION_SYSTEM: CRICETINAE GEN. SP.;                              
SOURCE  20 EXPRESSION_SYSTEM_TAXID: 36483;                                      
SOURCE  21 MOL_ID: 5;                                                           
SOURCE  22 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  23 ORGANISM_COMMON: HUMAN;                                              
SOURCE  24 ORGANISM_TAXID: 9606;                                                
SOURCE  25 GENE: ITGAV, MSK8, VNRA;                                             
SOURCE  26 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE  27 EXPRESSION_SYSTEM_COMMON: HUMAN;                                     
SOURCE  28 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE  29 EXPRESSION_SYSTEM_CELL_LINE: HEK293S;                                
SOURCE  30 MOL_ID: 6;                                                           
SOURCE  31 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  32 ORGANISM_COMMON: HUMAN;                                              
SOURCE  33 ORGANISM_TAXID: 9606;                                                
SOURCE  34 GENE: ITGB6;                                                         
SOURCE  35 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE  36 EXPRESSION_SYSTEM_COMMON: HUMAN;                                     
SOURCE  37 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE  38 EXPRESSION_SYSTEM_CELL_LINE: HEK293S                                 
KEYWDS    FOOT AND MOUTH DISEASE VIRUS, FMDV, VIRUS, OPANASIA, VIRUS-RECEPTOR,  
KEYWDS   2 COMPLEX                                                              
EXPDTA    ELECTRON MICROSCOPY                                                   
AUTHOR    A.KOTECHA,D.STUART                                                    
REVDAT   4   28-MAR-18 5NET    1       TITLE                                    
REVDAT   3   04-OCT-17 5NET    1       TITLE                                    
REVDAT   2   30-AUG-17 5NET    1       REMARK                                   
REVDAT   1   21-JUN-17 5NET    0                                                
JRNL        AUTH   A.KOTECHA,Q.WANG,X.DONG,S.L.ILCA,M.ONDIVIELA,R.ZIHE,J.SEAGO, 
JRNL        AUTH 2 B.CHARLESTON,E.E.FRY,N.G.A.ABRESCIA,T.A.SPRINGER,            
JRNL        AUTH 3 J.T.HUISKONEN,D.I.STUART                                     
JRNL        TITL   RULES OF ENGAGEMENT BETWEEN ALPHA V BETA 6 INTEGRIN AND      
JRNL        TITL 2 FOOT-AND-MOUTH DISEASE VIRUS.                                
JRNL        REF    NAT COMMUN                    V.   8 15408 2017              
JRNL        REFN                   ESSN 2041-1723                               
JRNL        PMID   28534487                                                     
JRNL        DOI    10.1038/NCOMMS15408                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    8.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   SOFTWARE PACKAGES      : SERIALEM, CTFFIND, UCSF CHIMERA,          
REMARK   3                            PHENIX, RELION, RELION, RELION, RELION    
REMARK   3   RECONSTRUCTION SCHEMA  : BACK PROJECTION                           
REMARK   3                                                                      
REMARK   3 EM MAP-MODEL FITTING AND REFINEMENT                                  
REMARK   3   PDB ENTRY                    : NULL                                
REMARK   3   REFINEMENT SPACE             : REAL                                
REMARK   3   REFINEMENT PROTOCOL          : RIGID BODY FIT                      
REMARK   3   REFINEMENT TARGET            : CROSS-CORRELATION COEFFICIENT       
REMARK   3   OVERALL ANISOTROPIC B VALUE  : 120.000                             
REMARK   3                                                                      
REMARK   3 FITTING PROCEDURE : NULL                                             
REMARK   3                                                                      
REMARK   3 EM IMAGE RECONSTRUCTION STATISTICS                                   
REMARK   3   NOMINAL PIXEL SIZE (ANGSTROMS)    : NULL                           
REMARK   3   ACTUAL PIXEL SIZE  (ANGSTROMS)    : NULL                           
REMARK   3   EFFECTIVE RESOLUTION (ANGSTROMS)  : 8.600                          
REMARK   3   NUMBER OF PARTICLES               : 13483                          
REMARK   3   CTF CORRECTION METHOD             : PHASE FLIPPING AND AMPLITUDE   
REMARK   3                                       CORRECTION                     
REMARK   3                                                                      
REMARK   3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL                    
REMARK   3                                                                      
REMARK   3 OTHER DETAILS: NULL                                                  
REMARK   4                                                                      
REMARK   4 5NET COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 13-MAR-17.                  
REMARK 100 THE DEPOSITION ID IS D_1200003987.                                   
REMARK 245                                                                      
REMARK 245 EXPERIMENTAL DETAILS                                                 
REMARK 245   RECONSTRUCTION METHOD          : SINGLE PARTICLE                   
REMARK 245   SPECIMEN TYPE                  : NULL                              
REMARK 245                                                                      
REMARK 245 ELECTRON MICROSCOPE SAMPLE                                           
REMARK 245   SAMPLE TYPE                    : PARTICLE                          
REMARK 245   PARTICLE TYPE                  : POINT                             
REMARK 245   NAME OF SAMPLE                 : FOOT AND MOUTH VIRUS AND          
REMARK 245                                    INTEGRIN; FOOT-AND-MOUTH          
REMARK 245                                    DISEASE VIRUS; INTEGRIN           
REMARK 245   SAMPLE CONCENTRATION (MG ML-1) : 0.50                              
REMARK 245   SAMPLE SUPPORT DETAILS         : NULL                              
REMARK 245   SAMPLE VITRIFICATION DETAILS   : NULL                              
REMARK 245   SAMPLE BUFFER                  : NULL                              
REMARK 245   PH                             : 8.00                              
REMARK 245   SAMPLE DETAILS                 : NULL                              
REMARK 245                                                                      
REMARK 245 DATA ACQUISITION                                                     
REMARK 245   DATE OF EXPERIMENT                : NULL                           
REMARK 245   NUMBER OF MICROGRAPHS-IMAGES      : 360                            
REMARK 245   TEMPERATURE (KELVIN)              : NULL                           
REMARK 245   MICROSCOPE MODEL                  : FEI POLARA 300                 
REMARK 245   DETECTOR TYPE                     : GATAN K2 SUMMIT (4K X 4K)      
REMARK 245   MINIMUM DEFOCUS (NM)              : 1000.00                        
REMARK 245   MAXIMUM DEFOCUS (NM)              : 4000.00                        
REMARK 245   MINIMUM TILT ANGLE (DEGREES)      : NULL                           
REMARK 245   MAXIMUM TILT ANGLE (DEGREES)      : NULL                           
REMARK 245   NOMINAL CS                        : 2.00                           
REMARK 245   IMAGING MODE                      : BRIGHT FIELD                   
REMARK 245   ELECTRON DOSE (ELECTRONS NM**-2)  : 18.00                          
REMARK 245   ILLUMINATION MODE                 : FLOOD BEAM                     
REMARK 245   NOMINAL MAGNIFICATION             : 160000                         
REMARK 245   CALIBRATED MAGNIFICATION          : 37037                          
REMARK 245   SOURCE                            : FIELD EMISSION GUN             
REMARK 245   ACCELERATION VOLTAGE (KV)         : 300                            
REMARK 245   IMAGING DETAILS                   : NULL                           
REMARK 247                                                                      
REMARK 247 ELECTRON MICROSCOPY                                                  
REMARK 247  THE COORDINATES IN THIS ENTRY WERE GENERATED FROM ELECTRON          
REMARK 247  MICROSCOPY DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE              
REMARK 247  THAT CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES           
REMARK 247  ON THESE RECORDS ARE MEANINGLESS EXCEPT FOR THE CALCULATION         
REMARK 247  OF THE STRUCTURE FACTORS.                                           
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 300 THE ASSEMBLY REPRESENTED IN THIS ENTRY HAS REGULAR                   
REMARK 300 ICOSAHEDRAL POINT SYMMETRY (SCHOENFLIES SYMBOL = I).                 
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: HEXAMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 26880 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 75960 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -56.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 1, 2, 3, 4, A, B                      
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     ASP 2     1                                                      
REMARK 465     LYS 2     2                                                      
REMARK 465     LYS 2     3                                                      
REMARK 465     THR 2     4                                                      
REMARK 465     GLU 2     5                                                      
REMARK 465     GLU 2     6                                                      
REMARK 465     THR 2     7                                                      
REMARK 465     THR 2     8                                                      
REMARK 465     LEU 2     9                                                      
REMARK 465     LEU 2    10                                                      
REMARK 465     GLU 2    11                                                      
REMARK 465     GLY 4     1                                                      
REMARK 465     ALA 4     2                                                      
REMARK 465     GLY 4     3                                                      
REMARK 465     GLN 4     4                                                      
REMARK 465     SER 4     5                                                      
REMARK 465     SER 4     6                                                      
REMARK 465     PRO 4     7                                                      
REMARK 465     ALA 4     8                                                      
REMARK 465     THR 4     9                                                      
REMARK 465     GLY 4    10                                                      
REMARK 465     SER 4    11                                                      
REMARK 465     GLN 4    12                                                      
REMARK 465     ASN 4    13                                                      
REMARK 465     GLN 4    14                                                      
REMARK 465     ASP 4    40                                                      
REMARK 465     ASN 4    41                                                      
REMARK 465     ALA 4    42                                                      
REMARK 465     THR 4    43                                                      
REMARK 465     SER 4    44                                                      
REMARK 465     GLY 4    45                                                      
REMARK 465     GLY 4    46                                                      
REMARK 465     SER 4    47                                                      
REMARK 465     ASN 4    48                                                      
REMARK 465     GLU 4    49                                                      
REMARK 465     GLY 4    50                                                      
REMARK 465     SER 4    51                                                      
REMARK 465     THR 4    52                                                      
REMARK 465     ASP 4    53                                                      
REMARK 465     THR 4    54                                                      
REMARK 465     THR 4    55                                                      
REMARK 465     SER 4    56                                                      
REMARK 465     THR 4    57                                                      
REMARK 465     HIS 4    58                                                      
REMARK 465     THR 4    59                                                      
REMARK 465     THR 4    60                                                      
REMARK 465     ASN 4    61                                                      
REMARK 465     THR 4    62                                                      
REMARK 465     GLN 4    63                                                      
REMARK 465     ASN 4    64                                                      
REMARK 465     ASN 4    65                                                      
REMARK 465     ALA A    30                                                      
REMARK 465     SER A    31                                                      
REMARK 465     LEU A   264                                                      
REMARK 465     GLN A   504                                                      
REMARK 465     LYS A   505                                                      
REMARK 465     ALA B    11                                                      
REMARK 465     GLU B    12                                                      
REMARK 465     GLN B    28A                                                     
REMARK 465     GLU B    28B                                                     
REMARK 465     ASN B    28C                                                     
REMARK 465     PHE B    28D                                                     
REMARK 465     THR B    28E                                                     
REMARK 465     HIS B    28F                                                     
REMARK 465     PRO B    28G                                                     
REMARK 465     SER B    28H                                                     
REMARK 465     GLY B    28I                                                     
REMARK 465     VAL B    28J                                                     
REMARK 465     GLY B    28K                                                     
REMARK 465     GLU B    28L                                                     
REMARK 465     ALA B    43                                                      
REMARK 465     ASN B    44                                                      
REMARK 465     LEU B    45                                                      
REMARK 465     LEU B    46                                                      
REMARK 465     ALA B    47                                                      
REMARK 465     LYS B    48                                                      
REMARK 465     GLY B    49                                                      
REMARK 465     GLU B   439                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   N    ARG 1   200     NZ   LYS 3    84              0.48            
REMARK 500   O    ARG 1    26     CD   GLU 3   210              0.50            
REMARK 500   C    GLN 1   203     CG2  VAL 3   174              0.55            
REMARK 500   NZ   LYS 1   202     N    VAL 3   174              0.56            
REMARK 500   C    ARG 1    26     OE2  GLU 3   210              0.68            
REMARK 500   C    ALA 1   199     CE   LYS 3    84              0.68            
REMARK 500   CE   LYS 1   202     C    ASP 3   173              0.71            
REMARK 500   CD   LYS 1   202     O    ASP 3   173              0.79            
REMARK 500   CZ   ARG 1   200     N    ALA 3    83              0.79            
REMARK 500   CZ   ARG 1   200     C    ALA 3    82              0.90            
REMARK 500   CE   LYS 1   202     O    ASP 3   173              0.94            
REMARK 500   C    ALA 1   199     NZ   LYS 3    84              0.94            
REMARK 500   O    ARG 1    26     OE2  GLU 3   210              0.95            
REMARK 500   NH2  ARG B    74     O    SER B   144              0.96            
REMARK 500   NH1  ARG 1   200     N    ALA 3    83              1.03            
REMARK 500   NE   ARG 1   200     C    ALA 3    82              1.04            
REMARK 500   NH2  ARG 1   200     N    ALA 3    82              1.05            
REMARK 500   O    ALA 1   199     CE   LYS 3    84              1.07            
REMARK 500   O    GLN 1   203     CG2  VAL 3   174              1.12            
REMARK 500   CZ   ARG B    74     O    SER B   144              1.22            
REMARK 500   NH2  ARG 1   200     CA   ALA 3    82              1.23            
REMARK 500   N    LYS 1   204     CG2  VAL 3   174              1.29            
REMARK 500   CE1  PHE 3    30     CE   MET 4    34              1.31            
REMARK 500   N    ARG 1    27     OE2  GLU 3   210              1.34            
REMARK 500   NZ   LYS 1   202     CA   VAL 3   174              1.34            
REMARK 500   C    ARG 1    26     CD   GLU 3   210              1.34            
REMARK 500   CA   ASP B   110     CB   SER B   148              1.40            
REMARK 500   NE   ARG 1   200     N    ALA 3    83              1.40            
REMARK 500   N    ARG 1    26     OE1  GLU 3   210              1.43            
REMARK 500   O    THR 1    30     OD1  ASN 3    43              1.44            
REMARK 500   NZ   LYS 1   202     C    ASP 3   173              1.50            
REMARK 500   CD   LYS 1   202     C    ASP 3   173              1.57            
REMARK 500   CE   LYS 1   202     N    VAL 3   174              1.57            
REMARK 500   NH2  ARG B    74     C    SER B   144              1.57            
REMARK 500   NH2  ARG 1   200     C    LEU 3    81              1.59            
REMARK 500   O    ARG 1    26     OE1  GLU 3   210              1.60            
REMARK 500   NE   ARG 1   200     O    ALA 3    82              1.63            
REMARK 500   O    GLY 1   137     CD2  LEU 2    80              1.64            
REMARK 500   CZ   ARG 1   200     CA   ALA 3    82              1.66            
REMARK 500   O    ARG 1    26     CG   GLU 3   210              1.67            
REMARK 500   OD1  ASN A   585     C1   NAG A   615              1.69            
REMARK 500   NH1  ARG 1   200     CA   ALA 3    83              1.69            
REMARK 500   CA   ALA 1   199     CE   LYS 3    84              1.70            
REMARK 500   OE1  GLU 1   184     NH1  ARG 3    34              1.75            
REMARK 500   N    ARG 1   200     CE   LYS 3    84              1.75            
REMARK 500   CA   ARG 1   200     NZ   LYS 3    84              1.76            
REMARK 500   NH1  ARG 1   200     C    ALA 3    82              1.78            
REMARK 500   ND2  ASN A   585     C1   NAG A   615              1.79            
REMARK 500   CD   ARG 1   200     O    ALA 3    82              1.83            
REMARK 500   NH1  ARG 1   200     O    ALA 3    83              1.83            
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     110 CLOSE CONTACTS                                
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    ILE A 147   CB  -  CA  -  C   ANGL. DEV. = -23.9 DEGREES          
REMARK 500    ILE A 147   N   -  CA  -  C   ANGL. DEV. =  50.7 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    LEU 1  51       56.05    -93.23                                   
REMARK 500    PRO 1 104       83.07    -69.09                                   
REMARK 500    ASN 1 133       62.83   -151.87                                   
REMARK 500    ASN 1 143      -62.53   -127.69                                   
REMARK 500    THR 1 161       -8.43    -53.74                                   
REMARK 500    CYS 1 187       77.71     54.66                                   
REMARK 500    HIS 1 201       93.79    -69.49                                   
REMARK 500    TYR 2  36      -12.70     70.24                                   
REMARK 500    ALA 2  37      148.70   -175.32                                   
REMARK 500    LEU 2  51       31.56    -95.16                                   
REMARK 500    GLN 2 139       44.47   -107.73                                   
REMARK 500    ASN 2 190     -166.33   -128.68                                   
REMARK 500    ASN 2 207       65.43     36.39                                   
REMARK 500    ASN 3 179       73.02     58.43                                   
REMARK 500    LEU 3 213       76.28     59.74                                   
REMARK 500    MET 4  27      -81.22    -64.01                                   
REMARK 500    GLN 4  28      -24.37   -148.02                                   
REMARK 500    LEU 4  79     -169.58   -127.06                                   
REMARK 500    PRO A  28     -138.43    -87.81                                   
REMARK 500    PRO A  48      109.12    -53.92                                   
REMARK 500    SER A  63     -117.31     59.49                                   
REMARK 500    ARG A  65       59.13   -103.08                                   
REMARK 500    GLN A 102     -111.37     58.95                                   
REMARK 500    MET A 118      -98.22   -120.25                                   
REMARK 500    THR A 136      110.29   -160.92                                   
REMARK 500    ALA A 149      -61.05     65.22                                   
REMARK 500    ASN A 206       60.14   -108.65                                   
REMARK 500    ASN A 260       15.44   -146.61                                   
REMARK 500    ARG A 398      -54.67   -125.82                                   
REMARK 500    SER A 399      -60.39   -145.54                                   
REMARK 500    TYR A 515       41.60    -81.75                                   
REMARK 500    SER A 516      -22.52   -166.49                                   
REMARK 500    SER A 546       41.54    -95.82                                   
REMARK 500    THR A 571      -81.82     53.55                                   
REMARK 500    PRO A 576      170.90    -59.83                                   
REMARK 500    PHE A 581        8.89     58.16                                   
REMARK 500    LEU B   8       86.19     60.53                                   
REMARK 500    ASP B  40     -157.63   -140.52                                   
REMARK 500    SER B 124       -2.02   -165.25                                   
REMARK 500    GLU B 134       54.05   -143.06                                   
REMARK 500    VAL B 158      -76.00   -135.98                                   
REMARK 500    CYS B 177       51.21   -106.18                                   
REMARK 500    PRO B 181       86.99    -57.71                                   
REMARK 500    ASP B 199       86.65    -65.20                                   
REMARK 500    ASN B 215     -162.76   -165.79                                   
REMARK 500    ILE B 216      -77.66    -96.16                                   
REMARK 500    MET B 258       30.97    -90.37                                   
REMARK 500    HIS B 274       42.19   -145.01                                   
REMARK 500    ASP B 276     -171.83    -69.56                                   
REMARK 500    GLN B 314      -18.12   -148.89                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      57 RAMACHANDRAN OUTLIERS.                        
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 TYR 1  136     GLY 1  137                  -48.70                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     MAN 3  301                                                       
REMARK 610     MAN 3  302                                                       
REMARK 610     NAG A  601                                                       
REMARK 610     NAG A  604                                                       
REMARK 610     MAN A  607                                                       
REMARK 610     MAN A  608                                                       
REMARK 610     NAG A  614                                                       
REMARK 610     NAG A  615                                                       
REMARK 610     NAG B  502                                                       
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 621  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 230   OD1                                                    
REMARK 620 2 ASN A 232   OD1  73.6                                              
REMARK 620 3 ASP A 234   OD1  75.0  63.6                                        
REMARK 620 4 ILE A 236   O    70.5 142.7  96.9                                  
REMARK 620 5 ASP A 238   OD1 128.3 116.0 156.5  94.6                            
REMARK 620 6 ASP A 238   OD2  80.3  81.9 141.9 101.7  53.8                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 622  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 284   OD1                                                    
REMARK 620 2 ASN A 286   OD1  78.4                                              
REMARK 620 3 ASP A 288   OD1  62.3  69.9                                        
REMARK 620 4 TYR A 290   O    69.9 146.3 103.5                                  
REMARK 620 5 ASP A 292   OD1 130.2 112.3 167.3  81.5                            
REMARK 620 6 ASP A 292   OD2  86.6  73.6 135.7  93.0  54.4                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 620  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 349   OD1                                                    
REMARK 620 2 ASP A 351   OD1  83.2                                              
REMARK 620 3 ASP A 353   OD1  74.8  80.4                                        
REMARK 620 4 PHE A 355   O    71.2 154.3  90.7                                  
REMARK 620 5 ASP A 357   OD1 147.1 109.7 135.9  93.5                            
REMARK 620 6 ASP A 357   OD2 108.3  67.5 146.8 122.1  54.8                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 619  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 415   OD1                                                    
REMARK 620 2 ASP A 415   OD2  48.0                                              
REMARK 620 3 ASN A 417   OD1  80.2  91.9                                        
REMARK 620 4 TYR A 419   O   109.4 152.8  66.5                                  
REMARK 620 5 ASP A 421   OD1 101.0 101.3 163.3  97.8                            
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 NAG A 614                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 619                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 620                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 621                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 622                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A    
REMARK 800  610 through MAN A 613 bound to ASN A 458                            
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 501 bound   
REMARK 800  to ASN B 77                                                         
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A    
REMARK 800  601 through MAN A 603                                               
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A    
REMARK 800  604 through MAN A 606                                               
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A    
REMARK 800  615 through MAN A 618                                               
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: EMD-3631   RELATED DB: EMDB                              
REMARK 900 ICOSAHEDRAL RECONSTRUCTION OF FMDV O1 MANISA AND INTEGRIN ALPHA V    
REMARK 900 BETA 6 COMPLEX                                                       
REMARK 900 RELATED ID: EMD-3634   RELATED DB: EMDB                              
REMARK 900 LOCALISED RECONSTRUCTION OF ALPHA V BETA 6 BOUND TO FOOT AND MOUTH   
REMARK 900 DISEASE VIRUS O PANASIA - POSE A                                     
DBREF  5NET 1    1   208  UNP    Q6PMW3   Q6PMW3_9PICO   725    932             
DBREF  5NET 2    1   218  UNP    Q6PMW3   Q6PMW3_9PICO   287    504             
DBREF  5NET 3    1   220  UNP    Q80B23   Q80B23_9PICO   505    724             
DBREF  5NET 4    1    85  UNP    E1ACS1   E1ACS1_9PICO   202    286             
DBREF  5NET A    1   594  UNP    P06756   ITAV_HUMAN      31    624             
DBREF  5NET B    5   471  UNP    P18564   ITB6_HUMAN      22    491             
SEQADV 5NET TYR 2   93  UNP  Q6PMW3    SER   379 CONFLICT                       
SEQADV 5NET ARG 3   56  UNP  Q80B23    HIS   560 CONFLICT                       
SEQADV 5NET THR 3  168  UNP  Q80B23    ALA   672 CONFLICT                       
SEQADV 5NET CYS A  400  UNP  P06756    MET   430 CONFLICT                       
SEQADV 5NET CYS B  267  UNP  P18564    ILE   287 CONFLICT                       
SEQADV 5NET ASN B  449  UNP  P18564    HIS   469 CONFLICT                       
SEQRES   1 1  208  THR THR SER ALA GLY GLU SER ALA ASP PRO VAL THR ALA          
SEQRES   2 1  208  THR VAL GLU ASN TYR GLY GLY GLU THR GLN VAL GLN ARG          
SEQRES   3 1  208  ARG GLN HIS THR ASP VAL SER PHE ILE LEU ASP ARG PHE          
SEQRES   4 1  208  VAL LYS VAL THR PRO LYS ASP GLN ILE ASN VAL LEU ASP          
SEQRES   5 1  208  LEU MET GLN THR PRO ALA HIS THR LEU VAL GLY ALA LEU          
SEQRES   6 1  208  LEU ARG THR ALA THR TYR TYR PHE ALA ASP LEU GLU VAL          
SEQRES   7 1  208  ALA VAL LYS HIS GLU GLY ASN LEU THR TRP VAL PRO ASN          
SEQRES   8 1  208  GLY ALA PRO GLU ALA ALA LEU ASP ASN THR THR ASN PRO          
SEQRES   9 1  208  THR ALA TYR HIS LYS ALA PRO LEU THR ARG LEU ALA LEU          
SEQRES  10 1  208  PRO TYR THR ALA PRO HIS ARG VAL LEU ALA THR VAL TYR          
SEQRES  11 1  208  ASN GLY ASN SER LYS TYR GLY ASP GLY THR VAL ALA ASN          
SEQRES  12 1  208  VAL ARG GLY ASP LEU GLN VAL LEU ALA GLN LYS ALA ALA          
SEQRES  13 1  208  ARG ALA LEU PRO THR SER PHE ASN TYR GLY ALA ILE LYS          
SEQRES  14 1  208  ALA THR ARG VAL THR GLU LEU LEU TYR ARG MET LYS ARG          
SEQRES  15 1  208  ALA GLU THR TYR CYS PRO ARG PRO LEU LEU ALA ILE HIS          
SEQRES  16 1  208  PRO ASP GLN ALA ARG HIS LYS GLN LYS ILE VAL ALA PRO          
SEQRES   1 2  218  ASP LYS LYS THR GLU GLU THR THR LEU LEU GLU ASP ARG          
SEQRES   2 2  218  ILE LEU THR THR ARG ASN GLY HIS THR THR SER THR THR          
SEQRES   3 2  218  GLN SER SER VAL GLY VAL THR TYR GLY TYR ALA THR ALA          
SEQRES   4 2  218  GLU ASP PHE VAL SER GLY PRO ASN THR SER GLY LEU GLU          
SEQRES   5 2  218  THR ARG VAL ALA GLN ALA GLU ARG PHE PHE LYS THR HIS          
SEQRES   6 2  218  LEU PHE ASP TRP VAL THR SER ASP PRO PHE GLY ARG CYS          
SEQRES   7 2  218  HIS LEU LEU GLU LEU PRO THR ASP HIS LYS GLY VAL TYR          
SEQRES   8 2  218  GLY TYR LEU THR ASP SER TYR ALA TYR MET ARG ASN GLY          
SEQRES   9 2  218  TRP ASP VAL GLU VAL THR ALA VAL GLY ASN GLN PHE ASN          
SEQRES  10 2  218  GLY GLY CYS LEU LEU VAL ALA MET VAL PRO GLU LEU CYS          
SEQRES  11 2  218  SER ILE GLN LYS ARG GLU LEU TYR GLN LEU THR LEU PHE          
SEQRES  12 2  218  PRO HIS GLN PHE ILE ASN PRO ARG THR ASN MET THR ALA          
SEQRES  13 2  218  HIS ILE THR VAL PRO PHE VAL GLY VAL ASN ARG TYR ASP          
SEQRES  14 2  218  GLN TYR LYS VAL HIS LYS PRO TRP THR LEU VAL VAL MET          
SEQRES  15 2  218  VAL VAL ALA PRO LEU THR VAL ASN SER GLU GLY ALA PRO          
SEQRES  16 2  218  GLN ILE LYS VAL TYR ALA ASN ILE ALA PRO THR ASN VAL          
SEQRES  17 2  218  HIS VAL ALA GLY GLU PHE PRO SER LYS GLU                      
SEQRES   1 3  220  GLY ILE PHE PRO VAL ALA CYS SER ASP GLY TYR GLY GLY          
SEQRES   2 3  220  LEU VAL THR THR ASP PRO LYS THR ALA ASP PRO ALA TYR          
SEQRES   3 3  220  GLY LYS VAL PHE ASN PRO PRO ARG ASN MET LEU PRO GLY          
SEQRES   4 3  220  ARG PHE THR ASN PHE LEU ASP VAL ALA GLU ALA CYS PRO          
SEQRES   5 3  220  THR PHE LEU ARG PHE GLU GLY ASP VAL PRO TYR VAL THR          
SEQRES   6 3  220  THR LYS THR ASP SER ASP ARG VAL LEU ALA GLN PHE ASP          
SEQRES   7 3  220  LEU SER LEU ALA ALA LYS HIS MET SER ASN THR PHE LEU          
SEQRES   8 3  220  ALA GLY LEU ALA GLN TYR TYR THR GLN TYR SER GLY THR          
SEQRES   9 3  220  ILE ASN LEU HIS PHE MET PHE THR GLY PRO THR ASP ALA          
SEQRES  10 3  220  LYS ALA ARG TYR MET ILE ALA TYR ALA PRO PRO GLY MET          
SEQRES  11 3  220  GLU PRO PRO LYS THR PRO GLU ALA ALA ALA HIS CYS ILE          
SEQRES  12 3  220  HIS ALA GLU TRP ASP THR GLY LEU ASN SER LYS PHE THR          
SEQRES  13 3  220  PHE SER ILE PRO TYR LEU SER ALA ALA ASP TYR THR TYR          
SEQRES  14 3  220  THR ALA SER ASP VAL ALA GLU THR THR ASN VAL GLN GLY          
SEQRES  15 3  220  TRP VAL CYS LEU PHE GLN ILE THR HIS GLY LYS ALA ASP          
SEQRES  16 3  220  GLY ASP ALA LEU VAL VAL LEU ALA SER ALA GLY LYS ASP          
SEQRES  17 3  220  PHE GLU LEU ARG LEU PRO VAL ASP ALA ARG THR GLN              
SEQRES   1 4   85  GLY ALA GLY GLN SER SER PRO ALA THR GLY SER GLN ASN          
SEQRES   2 4   85  GLN SER GLY ASN THR GLY SER ILE ILE ASN ASN TYR TYR          
SEQRES   3 4   85  MET GLN GLN TYR GLN ASN SER MET ASP THR GLN LEU GLY          
SEQRES   4 4   85  ASP ASN ALA THR SER GLY GLY SER ASN GLU GLY SER THR          
SEQRES   5 4   85  ASP THR THR SER THR HIS THR THR ASN THR GLN ASN ASN          
SEQRES   6 4   85  ASP TRP PHE SER LYS LEU ALA SER SER ALA PHE SER GLY          
SEQRES   7 4   85  LEU PHE GLY ALA LEU LEU ALA                                  
SEQRES   1 A  594  PHE ASN LEU ASP VAL ASP SER PRO ALA GLU TYR SER GLY          
SEQRES   2 A  594  PRO GLU GLY SER TYR PHE GLY PHE ALA VAL ASP PHE PHE          
SEQRES   3 A  594  VAL PRO SER ALA SER SER ARG MET PHE LEU LEU VAL GLY          
SEQRES   4 A  594  ALA PRO LYS ALA ASN THR THR GLN PRO GLY ILE VAL GLU          
SEQRES   5 A  594  GLY GLY GLN VAL LEU LYS CYS ASP TRP SER SER THR ARG          
SEQRES   6 A  594  ARG CYS GLN PRO ILE GLU PHE ASP ALA THR GLY ASN ARG          
SEQRES   7 A  594  ASP TYR ALA LYS ASP ASP PRO LEU GLU PHE LYS SER HIS          
SEQRES   8 A  594  GLN TRP PHE GLY ALA SER VAL ARG SER LYS GLN ASP LYS          
SEQRES   9 A  594  ILE LEU ALA CYS ALA PRO LEU TYR HIS TRP ARG THR GLU          
SEQRES  10 A  594  MET LYS GLN GLU ARG GLU PRO VAL GLY THR CYS PHE LEU          
SEQRES  11 A  594  GLN ASP GLY THR LYS THR VAL GLU TYR ALA PRO CYS ARG          
SEQRES  12 A  594  SER GLN ASP ILE ASP ALA ASP GLY GLN GLY PHE CYS GLN          
SEQRES  13 A  594  GLY GLY PHE SER ILE ASP PHE THR LYS ALA ASP ARG VAL          
SEQRES  14 A  594  LEU LEU GLY GLY PRO GLY SER PHE TYR TRP GLN GLY GLN          
SEQRES  15 A  594  LEU ILE SER ASP GLN VAL ALA GLU ILE VAL SER LYS TYR          
SEQRES  16 A  594  ASP PRO ASN VAL TYR SER ILE LYS TYR ASN ASN GLN LEU          
SEQRES  17 A  594  ALA THR ARG THR ALA GLN ALA ILE PHE ASP ASP SER TYR          
SEQRES  18 A  594  LEU GLY TYR SER VAL ALA VAL GLY ASP PHE ASN GLY ASP          
SEQRES  19 A  594  GLY ILE ASP ASP PHE VAL SER GLY VAL PRO ARG ALA ALA          
SEQRES  20 A  594  ARG THR LEU GLY MET VAL TYR ILE TYR ASP GLY LYS ASN          
SEQRES  21 A  594  MET SER SER LEU TYR ASN PHE THR GLY GLU GLN MET ALA          
SEQRES  22 A  594  ALA TYR PHE GLY PHE SER VAL ALA ALA THR ASP ILE ASN          
SEQRES  23 A  594  GLY ASP ASP TYR ALA ASP VAL PHE ILE GLY ALA PRO LEU          
SEQRES  24 A  594  PHE MET ASP ARG GLY SER ASP GLY LYS LEU GLN GLU VAL          
SEQRES  25 A  594  GLY GLN VAL SER VAL SER LEU GLN ARG ALA SER GLY ASP          
SEQRES  26 A  594  PHE GLN THR THR LYS LEU ASN GLY PHE GLU VAL PHE ALA          
SEQRES  27 A  594  ARG PHE GLY SER ALA ILE ALA PRO LEU GLY ASP LEU ASP          
SEQRES  28 A  594  GLN ASP GLY PHE ASN ASP ILE ALA ILE ALA ALA PRO TYR          
SEQRES  29 A  594  GLY GLY GLU ASP LYS LYS GLY ILE VAL TYR ILE PHE ASN          
SEQRES  30 A  594  GLY ARG SER THR GLY LEU ASN ALA VAL PRO SER GLN ILE          
SEQRES  31 A  594  LEU GLU GLY GLN TRP ALA ALA ARG SER CYS PRO PRO SER          
SEQRES  32 A  594  PHE GLY TYR SER MET LYS GLY ALA THR ASP ILE ASP LYS          
SEQRES  33 A  594  ASN GLY TYR PRO ASP LEU ILE VAL GLY ALA PHE GLY VAL          
SEQRES  34 A  594  ASP ARG ALA ILE LEU TYR ARG ALA ARG PRO VAL ILE THR          
SEQRES  35 A  594  VAL ASN ALA GLY LEU GLU VAL TYR PRO SER ILE LEU ASN          
SEQRES  36 A  594  GLN ASP ASN LYS THR CYS SER LEU PRO GLY THR ALA LEU          
SEQRES  37 A  594  LYS VAL SER CYS PHE ASN VAL ARG PHE CYS LEU LYS ALA          
SEQRES  38 A  594  ASP GLY LYS GLY VAL LEU PRO ARG LYS LEU ASN PHE GLN          
SEQRES  39 A  594  VAL GLU LEU LEU LEU ASP LYS LEU LYS GLN LYS GLY ALA          
SEQRES  40 A  594  ILE ARG ARG ALA LEU PHE LEU TYR SER ARG SER PRO SER          
SEQRES  41 A  594  HIS SER LYS ASN MET THR ILE SER ARG GLY GLY LEU MET          
SEQRES  42 A  594  GLN CYS GLU GLU LEU ILE ALA TYR LEU ARG ASP GLU SER          
SEQRES  43 A  594  GLU PHE ARG ASP LYS LEU THR PRO ILE THR ILE PHE MET          
SEQRES  44 A  594  GLU TYR ARG LEU ASP TYR ARG THR ALA ALA ASP THR THR          
SEQRES  45 A  594  GLY LEU GLN PRO ILE LEU ASN GLN PHE THR PRO ALA ASN          
SEQRES  46 A  594  ILE SER ARG GLN ALA HIS ILE LEU LEU                          
SEQRES   1 B  470  GLY CYS ALA LEU GLY GLY ALA GLU THR CYS GLU ASP CYS          
SEQRES   2 B  470  LEU LEU ILE GLY PRO GLN CYS ALA TRP CYS ALA GLN GLU          
SEQRES   3 B  470  ASN PHE THR HIS PRO SER GLY VAL GLY GLU ARG CYS ASP          
SEQRES   4 B  470  THR PRO ALA ASN LEU LEU ALA LYS GLY CYS GLN LEU ASN          
SEQRES   5 B  470  PHE ILE GLU ASN PRO VAL SER GLN VAL GLU ILE LEU LYS          
SEQRES   6 B  470  ASN LYS PRO LEU SER VAL GLY ARG GLN LYS ASN SER SER          
SEQRES   7 B  470  ASP ILE VAL GLN ILE ALA PRO GLN SER LEU ILE LEU LYS          
SEQRES   8 B  470  LEU ARG PRO GLY GLY ALA GLN THR LEU GLN VAL HIS VAL          
SEQRES   9 B  470  ARG GLN THR GLU ASP TYR PRO VAL ASP LEU TYR TYR LEU          
SEQRES  10 B  470  MET ASP LEU SER ALA SER MET ASP ASP ASP LEU ASN THR          
SEQRES  11 B  470  ILE LYS GLU LEU GLY SER ARG LEU SER LYS GLU MET SER          
SEQRES  12 B  470  LYS LEU THR SER ASN PHE ARG LEU GLY PHE GLY SER PHE          
SEQRES  13 B  470  VAL GLU LYS PRO VAL SER PRO PHE VAL LYS THR THR PRO          
SEQRES  14 B  470  GLU GLU ILE ALA ASN PRO CYS SER SER ILE PRO TYR PHE          
SEQRES  15 B  470  CYS LEU PRO THR PHE GLY PHE LYS HIS ILE LEU PRO LEU          
SEQRES  16 B  470  THR ASN ASP ALA GLU ARG PHE ASN GLU ILE VAL LYS ASN          
SEQRES  17 B  470  GLN LYS ILE SER ALA ASN ILE ASP THR PRO GLU GLY GLY          
SEQRES  18 B  470  PHE ASP ALA ILE MET GLN ALA ALA VAL CYS LYS GLU LYS          
SEQRES  19 B  470  ILE GLY TRP ARG ASN ASP SER LEU HIS LEU LEU VAL PHE          
SEQRES  20 B  470  VAL SER ASP ALA ASP SER HIS PHE GLY MET ASP SER LYS          
SEQRES  21 B  470  LEU ALA GLY ILE VAL CYS PRO ASN ASP GLY LEU CYS HIS          
SEQRES  22 B  470  LEU ASP SER LYS ASN GLU TYR SER MET SER THR VAL LEU          
SEQRES  23 B  470  GLU TYR PRO THR ILE GLY GLN LEU ILE ASP LYS LEU VAL          
SEQRES  24 B  470  GLN ASN ASN VAL LEU LEU ILE PHE ALA VAL THR GLN GLU          
SEQRES  25 B  470  GLN VAL HIS LEU TYR GLU ASN TYR ALA LYS LEU ILE PRO          
SEQRES  26 B  470  GLY ALA THR VAL GLY LEU LEU GLN LYS ASP SER GLY ASN          
SEQRES  27 B  470  ILE LEU GLN LEU ILE ILE SER ALA TYR GLU GLU LEU ARG          
SEQRES  28 B  470  SER GLU VAL GLU LEU GLU VAL LEU GLY ASP THR GLU GLY          
SEQRES  29 B  470  LEU ASN LEU SER PHE THR ALA ILE CYS ASN ASN GLY THR          
SEQRES  30 B  470  LEU PHE GLN HIS GLN LYS LYS CYS SER HIS MET LYS VAL          
SEQRES  31 B  470  GLY ASP THR ALA SER PHE SER VAL THR VAL ASN ILE PRO          
SEQRES  32 B  470  HIS CYS GLU ARG ARG SER ARG HIS ILE ILE ILE LYS PRO          
SEQRES  33 B  470  VAL GLY LEU GLY ASP ALA LEU GLU LEU LEU VAL SER PRO          
SEQRES  34 B  470  GLU CYS ASN CYS ASP CYS GLN LYS GLU VAL GLU VAL ASN          
SEQRES  35 B  470  SER SER LYS CYS HIS ASN GLY ASN GLY SER PHE GLN CYS          
SEQRES  36 B  470  GLY VAL CYS ALA CYS HIS PRO GLY HIS MET GLY PRO ARG          
SEQRES  37 B  470  CYS GLU                                                      
HET    MAN  3 301      11                                                       
HET    MAN  3 302      11                                                       
HET    NAG  A 601      14                                                       
HET    NAG  A 602      14                                                       
HET    MAN  A 603      12                                                       
HET    NAG  A 604      14                                                       
HET    NAG  A 605      14                                                       
HET    MAN  A 606      11                                                       
HET    MAN  A 607      11                                                       
HET    MAN  A 608      11                                                       
HET    MAN  A 609      11                                                       
HET    NAG  A 610      14                                                       
HET    NAG  A 611      14                                                       
HET    MAN  A 612      11                                                       
HET    MAN  A 613      11                                                       
HET    NAG  A 614      14                                                       
HET    NAG  A 615      14                                                       
HET    NAG  A 616      14                                                       
HET    MAN  A 617      12                                                       
HET    MAN  A 618      12                                                       
HET     CA  A 619       1                                                       
HET     CA  A 620       1                                                       
HET     CA  A 621       1                                                       
HET     CA  A 622       1                                                       
HET    NAG  B 501      14                                                       
HET    NAG  B 502      14                                                       
HETNAM     MAN ALPHA-D-MANNOSE                                                  
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM      CA CALCIUM ION                                                      
FORMUL   7  MAN    11(C6 H12 O6)                                                
FORMUL   9  NAG    11(C8 H15 N O6)                                              
FORMUL  16   CA    4(CA 2+)                                                     
HELIX    1 AA1 THR 1   14  GLY 1   19  5                                   6    
HELIX    2 AA2 ASP 1   52  THR 1   56  5                                   5    
HELIX    3 AA3 THR 1   60  LEU 1   65  1                                   6    
HELIX    4 AA4 PRO 1   94  ASP 1   99  5                                   6    
HELIX    5 AA5 LEU 1  148  GLN 1  153  1                                   6    
HELIX    6 AA6 LYS 1  154  ARG 1  157  5                                   4    
HELIX    7 AA7 ALA 2   56  GLU 2   59  5                                   4    
HELIX    8 AA8 GLY 2   89  ASP 2   96  1                                   8    
HELIX    9 AA9 ARG 2  135  PHE 2  143  5                                   9    
HELIX   10 AB1 ASN 3   43  CYS 3   51  1                                   9    
HELIX   11 AB2 PHE 3   90  ALA 3   95  1                                   6    
HELIX   12 AB3 GLU 3  137  CYS 3  142  5                                   6    
HELIX   13 AB4 TRP 4   67  SER 4   74  1                                   8    
HELIX   14 AB5 GLY A  175  GLN A  180  1                                   6    
HELIX   15 AB6 VAL A  188  LYS A  194  1                                   7    
HELIX   16 AB7 GLN A  214  ASP A  218  5                                   5    
HELIX   17 AB8 ARG A  245  LEU A  250  1                                   6    
HELIX   18 AB9 GLY A  366  LYS A  370  5                                   5    
HELIX   19 AC1 PHE A  427  VAL A  429  5                                   3    
HELIX   20 AC2 ASP A  544  PHE A  548  5                                   5    
HELIX   21 AC3 ASP A  564  ALA A  569  1                                   6    
HELIX   22 AC4 CYS B   14  ILE B   20  1                                   7    
HELIX   23 AC5 ASN B   77  ILE B   81  5                                   5    
HELIX   24 AC6 ASP B  127  THR B  131  5                                   5    
HELIX   25 AC7 LEU B  135  LYS B  145  1                                  11    
HELIX   26 AC8 THR B  169  ASN B  175  1                                   7    
HELIX   27 AC9 ASP B  199  GLN B  210  1                                  12    
HELIX   28 AD1 GLY B  221  CYS B  232  1                                  12    
HELIX   29 AD2 CYS B  232  GLY B  237  1                                   6    
HELIX   30 AD3 PHE B  256  GLY B  264  5                                   9    
HELIX   31 AD4 TYR B  281  VAL B  286  5                                   6    
HELIX   32 AD5 THR B  291  ASN B  302  1                                  12    
HELIX   33 AD6 GLN B  314  ILE B  325  1                                  12    
HELIX   34 AD7 ASN B  339  LEU B  351  1                                  13    
HELIX   35 AD8 CYS B  434  LYS B  438  5                                   5    
SHEET    1 AA1 5 THR 1   2  SER 1   3  0                                        
SHEET    2 AA1 5 LYS 3 154  ILE 3 159 -1  O  LYS 3 154   N  SER 1   3           
SHEET    3 AA1 5 ILE 3 105  PHE 3 111 -1  N  PHE 3 109   O  PHE 3 155           
SHEET    4 AA1 5 ALA 3 198  ALA 3 205 -1  O  LEU 3 202   N  HIS 3 108           
SHEET    5 AA1 5 THR 3  53  PHE 3  54 -1  N  THR 3  53   O  ALA 3 203           
SHEET    1 AA2 5 THR 1   2  SER 1   3  0                                        
SHEET    2 AA2 5 LYS 3 154  ILE 3 159 -1  O  LYS 3 154   N  SER 1   3           
SHEET    3 AA2 5 ILE 3 105  PHE 3 111 -1  N  PHE 3 109   O  PHE 3 155           
SHEET    4 AA2 5 ALA 3 198  ALA 3 205 -1  O  LEU 3 202   N  HIS 3 108           
SHEET    5 AA2 5 TYR 3  63  THR 3  65 -1  N  VAL 3  64   O  LEU 3 199           
SHEET    1 AA3 4 VAL 1  40  VAL 1  42  0                                        
SHEET    2 AA3 4 ARG 1 172  PRO 1 188 -1  O  TYR 1 178   N  VAL 1  40           
SHEET    3 AA3 4 ALA 1  69  GLU 1  83 -1  N  PHE 1  73   O  GLU 1 184           
SHEET    4 AA3 4 LEU 1 126  ALA 1 127 -1  O  LEU 1 126   N  TYR 1  72           
SHEET    1 AA4 4 THR 1 113  ALA 1 116  0                                        
SHEET    2 AA4 4 ALA 1  69  GLU 1  83 -1  N  VAL 1  80   O  THR 1 113           
SHEET    3 AA4 4 ARG 1 172  PRO 1 188 -1  O  GLU 1 184   N  PHE 1  73           
SHEET    4 AA4 4 ARG 3  40  PHE 3  41 -1  O  PHE 3  41   N  THR 1 185           
SHEET    1 AA5 4 ILE 1  48  VAL 1  50  0                                        
SHEET    2 AA5 4 ALA 1 167  LYS 1 169 -1  O  ILE 1 168   N  ASN 1  49           
SHEET    3 AA5 4 LEU 1  86  VAL 1  89 -1  N  THR 1  87   O  LYS 1 169           
SHEET    4 AA5 4 THR 1 105  ALA 1 106 -1  O  ALA 1 106   N  LEU 1  86           
SHEET    1 AA6 2 THR 2  16  ASN 2  19  0                                        
SHEET    2 AA6 2 THR 2  22  THR 2  25 -1  O  SER 2  24   N  THR 2  17           
SHEET    1 AA7 5 VAL 2  32  TYR 2  34  0                                        
SHEET    2 AA7 5 THR 2 155  VAL 2 160  1  O  THR 2 159   N  THR 2  33           
SHEET    3 AA7 5 TYR 2  98  ALA 2 111 -1  N  TRP 2 105   O  VAL 2 160           
SHEET    4 AA7 5 PRO 2 205  GLU 2 213 -1  O  GLY 2 212   N  ALA 2  99           
SHEET    5 AA7 5 GLU 2  52  ARG 2  54 -1  N  THR 2  53   O  VAL 2 210           
SHEET    1 AA8 5 VAL 2  32  TYR 2  34  0                                        
SHEET    2 AA8 5 THR 2 155  VAL 2 160  1  O  THR 2 159   N  THR 2  33           
SHEET    3 AA8 5 TYR 2  98  ALA 2 111 -1  N  TRP 2 105   O  VAL 2 160           
SHEET    4 AA8 5 ILE 2 197  ILE 2 203 -1  O  TYR 2 200   N  THR 2 110           
SHEET    5 AA8 5 PHE 2  62  TRP 2  69 -1  N  PHE 2  67   O  VAL 2 199           
SHEET    1 AA9 4 HIS 2  79  LEU 2  83  0                                        
SHEET    2 AA9 4 TRP 2 177  ALA 2 185 -1  O  LEU 2 179   N  LEU 2  81           
SHEET    3 AA9 4 CYS 2 120  PRO 2 127 -1  N  ALA 2 124   O  VAL 2 180           
SHEET    4 AA9 4 HIS 2 145  ILE 2 148 -1  O  ILE 2 148   N  LEU 2 121           
SHEET    1 AB1 4 VAL 3  73  ASP 3  78  0                                        
SHEET    2 AB1 4 TRP 3 183  GLY 3 192 -1  O  LEU 3 186   N  ALA 3  75           
SHEET    3 AB1 4 LYS 3 118  ALA 3 126 -1  N  LYS 3 118   O  GLY 3 192           
SHEET    4 AB1 4 ALA 3 145  ASP 3 148 -1  O  TRP 3 147   N  TYR 3 121           
SHEET    1 AB2 3 THR 3 168  TYR 3 169  0                                        
SHEET    2 AB2 3 TYR 3  98  SER 3 102 -1  N  TYR 3 101   O  THR 3 168           
SHEET    3 AB2 3 GLU 3 210  PRO 3 214 -1  O  GLU 3 210   N  SER 3 102           
SHEET    1 AB3 4 ALA A   9  SER A  12  0                                        
SHEET    2 AB3 4 ARG A 431  TYR A 435 -1  O  LEU A 434   N  ALA A   9           
SHEET    3 AB3 4 ASP A 421  ALA A 426 -1  N  VAL A 424   O  ILE A 433           
SHEET    4 AB3 4 SER A 407  THR A 412 -1  N  LYS A 409   O  ILE A 423           
SHEET    1 AB4 4 VAL A  23  PHE A  26  0                                        
SHEET    2 AB4 4 PHE A  35  ALA A  40 -1  O  LEU A  37   N  ASP A  24           
SHEET    3 AB4 4 GLN A  55  ASP A  60 -1  O  CYS A  59   N  LEU A  36           
SHEET    4 AB4 4 CYS A  67  ILE A  70 -1  O  GLN A  68   N  LYS A  58           
SHEET    1 AB5 2 ASP A  79  ALA A  81  0                                        
SHEET    2 AB5 2 ASP A  84  PRO A  85 -1  O  ASP A  84   N  TYR A  80           
SHEET    1 AB6 2 GLU A  87  PHE A  88  0                                        
SHEET    2 AB6 2 HIS A 113  TRP A 114 -1  O  HIS A 113   N  PHE A  88           
SHEET    1 AB7 4 VAL A  98  LYS A 101  0                                        
SHEET    2 AB7 4 LYS A 104  ALA A 109 -1  O  LEU A 106   N  ARG A  99           
SHEET    3 AB7 4 THR A 127  ASP A 132 -1  O  THR A 127   N  ALA A 109           
SHEET    4 AB7 4 LYS A 135  TYR A 139 -1  O  VAL A 137   N  LEU A 130           
SHEET    1 AB8 4 ILE A 161  PHE A 163  0                                        
SHEET    2 AB8 4 ARG A 168  GLY A 173 -1  O  LEU A 170   N  ASP A 162           
SHEET    3 AB8 4 GLN A 182  GLN A 187 -1  O  ASP A 186   N  VAL A 169           
SHEET    4 AB8 4 GLN A 207  ALA A 209 -1  O  LEU A 208   N  SER A 185           
SHEET    1 AB9 4 VAL A 226  GLY A 229  0                                        
SHEET    2 AB9 4 ASP A 238  VAL A 243 -1  O  ASP A 238   N  GLY A 229           
SHEET    3 AB9 4 MET A 252  TYR A 256 -1  O  MET A 252   N  VAL A 243           
SHEET    4 AB9 4 ASN A 266  THR A 268 -1  O  PHE A 267   N  VAL A 253           
SHEET    1 AC1 4 VAL A 280  THR A 283  0                                        
SHEET    2 AC1 4 ASP A 292  ALA A 297 -1  O  PHE A 294   N  ALA A 281           
SHEET    3 AC1 4 GLN A 314  GLN A 320 -1  O  SER A 318   N  VAL A 293           
SHEET    4 AC1 4 PHE A 326  ASN A 332 -1  O  THR A 329   N  VAL A 317           
SHEET    1 AC2 2 MET A 301  ARG A 303  0                                        
SHEET    2 AC2 2 LEU A 309  GLU A 311 -1  O  GLN A 310   N  ASP A 302           
SHEET    1 AC3 4 ILE A 344  GLY A 348  0                                        
SHEET    2 AC3 4 ASP A 357  ALA A 362 -1  O  ASP A 357   N  GLY A 348           
SHEET    3 AC3 4 ILE A 372  ASN A 377 -1  O  TYR A 374   N  ILE A 360           
SHEET    4 AC3 4 GLN A 389  GLU A 392 -1  O  LEU A 391   N  VAL A 373           
SHEET    1 AC4 3 ALA A 481  ASP A 482  0                                        
SHEET    2 AC4 3 VAL A 440  VAL A 443 -1  N  THR A 442   O  ASP A 482           
SHEET    3 AC4 3 ILE A 577  LEU A 578  1  O  ILE A 577   N  ILE A 441           
SHEET    1 AC5 4 GLY A 446  TYR A 450  0                                        
SHEET    2 AC5 4 CYS A 472  LEU A 479 -1  O  ARG A 476   N  GLU A 448           
SHEET    3 AC5 4 GLN A 534  LEU A 542 -1  O  ALA A 540   N  PHE A 473           
SHEET    4 AC5 4 ALA A 511  PHE A 513 -1  N  LEU A 512   O  TYR A 541           
SHEET    1 AC6 5 ILE A 453  LEU A 454  0                                        
SHEET    2 AC6 5 ASN A 585  ILE A 592  1  O  HIS A 591   N  LEU A 454           
SHEET    3 AC6 5 ILE A 555  LEU A 563 -1  N  ILE A 557   O  ARG A 588           
SHEET    4 AC6 5 LYS A 490  LEU A 499 -1  N  GLU A 496   O  GLU A 560           
SHEET    5 AC6 5 SER A 520  SER A 528 -1  O  MET A 525   N  PHE A 493           
SHEET    1 AC7 3 CYS B  39  ASP B  40  0                                        
SHEET    2 AC7 3 ALA B  25  CYS B  27 -1  N  ALA B  25   O  ASP B  40           
SHEET    3 AC7 3 ILE B  55  GLU B  56 -1  O  GLU B  56   N  TRP B  26           
SHEET    1 AC8 6 GLN B  61  LYS B  66  0                                        
SHEET    2 AC8 6 SER B  88  LEU B  93 -1  O  ILE B  90   N  GLU B  63           
SHEET    3 AC8 6 LEU B 424  PRO B 430  1  O  LEU B 427   N  LEU B  91           
SHEET    4 AC8 6 ARG B 411  PRO B 417 -1  N  ILE B 415   O  LEU B 424           
SHEET    5 AC8 6 VAL B 355  LEU B 360 -1  N  LEU B 360   O  ILE B 414           
SHEET    6 AC8 6 LYS B 385  CYS B 386 -1  O  CYS B 386   N  VAL B 355           
SHEET    1 AC9 5 ILE B  84  ALA B  85  0                                        
SHEET    2 AC9 5 GLN B  99  ARG B 106 -1  O  HIS B 104   N  ALA B  85           
SHEET    3 AC9 5 THR B 394  ASN B 402 -1  O  VAL B 399   N  LEU B 101           
SHEET    4 AC9 5 ASN B 367  ILE B 373 -1  N  ASN B 367   O  ASN B 402           
SHEET    5 AC9 5 LEU B 379  GLN B 381 -1  O  PHE B 380   N  ALA B 372           
SHEET    1 AD1 6 PHE B 190  THR B 197  0                                        
SHEET    2 AD1 6 PHE B 150  PHE B 157 -1  N  PHE B 154   O  LEU B 194           
SHEET    3 AD1 6 VAL B 113  ASP B 120  1  N  LEU B 115   O  GLY B 153           
SHEET    4 AD1 6 LEU B 243  SER B 250  1  O  LEU B 245   N  ASP B 114           
SHEET    5 AD1 6 LEU B 305  THR B 311  1  O  LEU B 305   N  HIS B 244           
SHEET    6 AD1 6 THR B 329  LEU B 333  1  O  LEU B 333   N  VAL B 310           
SHEET    1 AD2 2 GLY B 452  GLN B 455  0                                        
SHEET    2 AD2 2 VAL B 458  CYS B 461 -1  O  ALA B 460   N  SER B 453           
SSBOND   1 CYS A   59    CYS A   67                          1555   1555  2.03  
SSBOND   2 CYS A  108    CYS A  128                          1555   1555  2.03  
SSBOND   3 CYS A  142    CYS A  155                          1555   1555  2.03  
SSBOND   4 CYS A  400    CYS B  267                          1555   1555  2.03  
SSBOND   5 CYS A  461    CYS A  472                          1555   1555  2.03  
SSBOND   6 CYS A  478    CYS A  535                          1555   1555  2.03  
SSBOND   7 CYS B    6    CYS B   24                          1555   1555  2.03  
SSBOND   8 CYS B   14    CYS B  434                          1555   1555  2.03  
SSBOND   9 CYS B   17    CYS B   39                          1555   1555  2.03  
SSBOND  10 CYS B   27    CYS B   50                          1555   1555  2.03  
SSBOND  11 CYS B  177    CYS B  184                          1555   1555  2.03  
SSBOND  12 CYS B  232    CYS B  273                          1555   1555  2.03  
SSBOND  13 CYS B  374    CYS B  386                          1555   1555  2.03  
SSBOND  14 CYS B  406    CYS B  432                          1555   1555  2.03  
SSBOND  15 CYS B  436    CYS B  456                          1555   1555  2.03  
SSBOND  16 CYS B  447    CYS B  459                          1555   1555  2.03  
SSBOND  17 CYS B  461    CYS B  470                          1555   1555  2.03  
LINK         OD1 ASP A 230                CA    CA A 621     1555   1555  2.50  
LINK         OD1 ASN A 232                CA    CA A 621     1555   1555  2.38  
LINK         OD1 ASP A 234                CA    CA A 621     1555   1555  2.41  
LINK         O   ILE A 236                CA    CA A 621     1555   1555  2.46  
LINK         OD1 ASP A 238                CA    CA A 621     1555   1555  2.36  
LINK         OD2 ASP A 238                CA    CA A 621     1555   1555  2.47  
LINK         OD1 ASP A 284                CA    CA A 622     1555   1555  2.43  
LINK         OD1 ASN A 286                CA    CA A 622     1555   1555  2.35  
LINK         OD1 ASP A 288                CA    CA A 622     1555   1555  2.36  
LINK         O   TYR A 290                CA    CA A 622     1555   1555  2.32  
LINK         OD1 ASP A 292                CA    CA A 622     1555   1555  2.36  
LINK         OD2 ASP A 292                CA    CA A 622     1555   1555  2.44  
LINK         OD1 ASP A 349                CA    CA A 620     1555   1555  2.42  
LINK         OD1 ASP A 351                CA    CA A 620     1555   1555  2.32  
LINK         OD1 ASP A 353                CA    CA A 620     1555   1555  2.31  
LINK         O   PHE A 355                CA    CA A 620     1555   1555  2.21  
LINK         OD1 ASP A 357                CA    CA A 620     1555   1555  2.37  
LINK         OD2 ASP A 357                CA    CA A 620     1555   1555  2.40  
LINK         OD1 ASP A 415                CA    CA A 619     1555   1555  2.32  
LINK         OD2 ASP A 415                CA    CA A 619     1555   1555  2.91  
LINK         OD1 ASN A 417                CA    CA A 619     1555   1555  2.37  
LINK         O   TYR A 419                CA    CA A 619     1555   1555  2.43  
LINK         OD1 ASP A 421                CA    CA A 619     1555   1555  2.35  
LINK         ND2 ASN A 458                 C1  NAG A 610     1555   1555  1.29  
LINK         ND2 ASN B  77                 C1  NAG B 501     1555   1555  1.44  
LINK         O4  NAG A 601                 C1  NAG A 602     1555   1555  1.44  
LINK         O4  NAG A 602                 C1  MAN A 603     1555   1555  1.43  
LINK         O4  NAG A 604                 C1  NAG A 605     1555   1555  1.36  
LINK         O4  NAG A 605                 C1  MAN A 606     1555   1555  1.38  
LINK         O2  MAN A 608                 C1  MAN A 609     1555   1555  1.30  
LINK         O4  NAG A 610                 C1  NAG A 611     1555   1555  1.33  
LINK         O4  NAG A 611                 C1  MAN A 612     1555   1555  1.44  
LINK         O3  MAN A 612                 C1  MAN A 613     1555   1555  1.44  
LINK         O4  NAG A 615                 C1  NAG A 616     1555   1555  1.44  
LINK         O4  NAG A 616                 C1  MAN A 617     1555   1555  1.45  
LINK         O4  MAN A 617                 C1  MAN A 618     1555   1555  1.45  
CISPEP   1 ALA 1  110    PRO 1  111          0        -5.74                     
CISPEP   2 LEU 2   83    PRO 2   84          0         2.95                     
CISPEP   3 TYR A  450    PRO A  451          0        -2.43                     
CISPEP   4 ALA B   85    PRO B   86          0        -1.84                     
CISPEP   5 SER B  163    PRO B  164          0         5.63                     
SITE     1 AC1  3 GLN A 494  SER A 522  ASN A 524                               
SITE     1 AC2  5 ASP A 415  ASN A 417  TYR A 419  ASP A 421                    
SITE     2 AC2  5 ALA A 437                                                     
SITE     1 AC3  5 ASP A 349  ASP A 351  ASP A 353  PHE A 355                    
SITE     2 AC3  5 ASP A 357                                                     
SITE     1 AC4  5 ASP A 230  ASN A 232  ASP A 234  ILE A 236                    
SITE     2 AC4  5 ASP A 238                                                     
SITE     1 AC5  5 ASP A 284  ASN A 286  ASP A 288  TYR A 290                    
SITE     2 AC5  5 ASP A 292                                                     
SITE     1 AC6  6 TYR A 450  ASN A 455  ASN A 458  THR A 460                    
SITE     2 AC6  6 CYS A 472  ASN A 474                                          
SITE     1 AC7  3 ASN B  77  SER B  79  ASP B  80                               
SITE     1 AC8  2 ASN A 232  SER A 262                                          
SITE     1 AC9  2 ASN A 232  NAG A 601                                          
SITE     1 AD1  4 PHE A 558  PRO A 583  ALA A 584  ASN A 585                    
CRYST1    1.000    1.000    1.000  90.00  90.00  90.00 P 1                      
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      1.000000  0.000000  0.000000        0.00000                         
SCALE2      0.000000  1.000000  0.000000        0.00000                         
SCALE3      0.000000  0.000000  1.000000        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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