GenomeNet

Database: PDB
Entry: 5NEU
LinkDB: 5NEU
Original site: 5NEU 
HEADER    VIRUS                                   11-MAR-17   5NEU              
TITLE     LOCALISED RECONSTRUCTION OF INTEGRIN ALPHA V BETA 6 BOUND TO FOOT AND 
TITLE    2 MOUTH DISEASE VIRUS O1 MANISA - POSE B.                              
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 MUTATION: YES;                                                       
COMPND  10 MOL_ID: 3;                                                           
COMPND  11 MOLECULE: CAPSID PROTEIN;                                            
COMPND  12 CHAIN: 3;                                                            
COMPND  13 ENGINEERED: YES;                                                     
COMPND  14 MOL_ID: 4;                                                           
COMPND  15 MOLECULE: O1 MANISA VP4;                                             
COMPND  16 CHAIN: 4;                                                            
COMPND  17 ENGINEERED: YES;                                                     
COMPND  18 MOL_ID: 5;                                                           
COMPND  19 MOLECULE: INTEGRIN ALPHA-V;                                          
COMPND  20 CHAIN: A;                                                            
COMPND  21 SYNONYM: VITRONECTIN RECEPTOR SUBUNIT ALPHA;                         
COMPND  22 ENGINEERED: YES;                                                     
COMPND  23 MOL_ID: 6;                                                           
COMPND  24 MOLECULE: INTEGRIN BETA-6;                                           
COMPND  25 CHAIN: B;                                                            
COMPND  26 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 5NEU    1       TITLE                                    
REVDAT   3   04-OCT-17 5NEU    1       TITLE                                    
REVDAT   2   30-AUG-17 5NEU    1       REMARK                                   
REVDAT   1   21-JUN-17 5NEU    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.   12.30 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)  : 12.30                          
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 5NEU 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_1200003989.                                   
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 DISEASE VIRUS;     
REMARK 245                                    FOOT-AND-MOUTH DISEASE VIRUS;     
REMARK 245                                    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 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 350   BIOMT1   2  0.500000 -0.809017 -0.309017        0.00000            
REMARK 350   BIOMT2   2  0.809017  0.309017  0.500000        0.00000            
REMARK 350   BIOMT3   2 -0.309017 -0.500000  0.809017        0.00000            
REMARK 350   BIOMT1   3 -0.309017 -0.500000 -0.809017        0.00000            
REMARK 350   BIOMT2   3  0.500000 -0.809017  0.309017        0.00000            
REMARK 350   BIOMT3   3 -0.809017 -0.309017  0.500000        0.00000            
REMARK 350   BIOMT1   4 -0.309017  0.500000 -0.809017        0.00000            
REMARK 350   BIOMT2   4 -0.500000 -0.809017 -0.309017        0.00000            
REMARK 350   BIOMT3   4 -0.809017  0.309017  0.500000        0.00000            
REMARK 350   BIOMT1   5  0.500000  0.809017 -0.309017        0.00000            
REMARK 350   BIOMT2   5 -0.809017  0.309017 -0.500000        0.00000            
REMARK 350   BIOMT3   5 -0.309017  0.500000  0.809017        0.00000            
REMARK 350   BIOMT1   6 -0.809017 -0.309017 -0.500000        0.00000            
REMARK 350   BIOMT2   6 -0.309017 -0.500000  0.809017        0.00000            
REMARK 350   BIOMT3   6 -0.500000  0.809017  0.309017        0.00000            
REMARK 350   BIOMT1   7 -0.500000  0.809017 -0.309017        0.00000            
REMARK 350   BIOMT2   7 -0.809017 -0.309017  0.500000        0.00000            
REMARK 350   BIOMT3   7  0.309017  0.500000  0.809017        0.00000            
REMARK 350   BIOMT1   8  0.500000  0.809017  0.309017        0.00000            
REMARK 350   BIOMT2   8 -0.809017  0.309017  0.500000        0.00000            
REMARK 350   BIOMT3   8  0.309017 -0.500000  0.809017        0.00000            
REMARK 350   BIOMT1   9  0.809017 -0.309017  0.500000        0.00000            
REMARK 350   BIOMT2   9 -0.309017  0.500000  0.809017        0.00000            
REMARK 350   BIOMT3   9 -0.500000 -0.809017  0.309017        0.00000            
REMARK 350   BIOMT1  10  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT2  10  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT3  10 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT1  11 -0.500000  0.809017 -0.309017        0.00000            
REMARK 350   BIOMT2  11  0.809017  0.309017 -0.500000        0.00000            
REMARK 350   BIOMT3  11 -0.309017 -0.500000 -0.809017        0.00000            
REMARK 350   BIOMT1  12  0.500000  0.809017  0.309017        0.00000            
REMARK 350   BIOMT2  12  0.809017 -0.309017 -0.500000        0.00000            
REMARK 350   BIOMT3  12 -0.309017  0.500000 -0.809017        0.00000            
REMARK 350   BIOMT1  13  0.809017 -0.309017  0.500000        0.00000            
REMARK 350   BIOMT2  13  0.309017 -0.500000 -0.809017        0.00000            
REMARK 350   BIOMT3  13  0.500000  0.809017 -0.309017        0.00000            
REMARK 350   BIOMT1  14  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT2  14  0.000000  0.000000 -1.000000        0.00000            
REMARK 350   BIOMT3  14  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT1  15 -0.809017 -0.309017 -0.500000        0.00000            
REMARK 350   BIOMT2  15  0.309017  0.500000 -0.809017        0.00000            
REMARK 350   BIOMT3  15  0.500000 -0.809017 -0.309017        0.00000            
REMARK 350   BIOMT1  16  0.309017 -0.500000  0.809017        0.00000            
REMARK 350   BIOMT2  16 -0.500000 -0.809017 -0.309017        0.00000            
REMARK 350   BIOMT3  16  0.809017 -0.309017 -0.500000        0.00000            
REMARK 350   BIOMT1  17 -0.500000 -0.809017  0.309017        0.00000            
REMARK 350   BIOMT2  17 -0.809017  0.309017 -0.500000        0.00000            
REMARK 350   BIOMT3  17  0.309017 -0.500000 -0.809017        0.00000            
REMARK 350   BIOMT1  18 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2  18  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3  18  0.000000  0.000000 -1.000000        0.00000            
REMARK 350   BIOMT1  19 -0.500000  0.809017  0.309017        0.00000            
REMARK 350   BIOMT2  19  0.809017  0.309017  0.500000        0.00000            
REMARK 350   BIOMT3  19  0.309017  0.500000 -0.809017        0.00000            
REMARK 350   BIOMT1  20  0.309017  0.500000  0.809017        0.00000            
REMARK 350   BIOMT2  20  0.500000 -0.809017  0.309017        0.00000            
REMARK 350   BIOMT3  20  0.809017  0.309017 -0.500000        0.00000            
REMARK 350   BIOMT1  21  0.809017 -0.309017 -0.500000        0.00000            
REMARK 350   BIOMT2  21  0.309017 -0.500000  0.809017        0.00000            
REMARK 350   BIOMT3  21 -0.500000 -0.809017 -0.309017        0.00000            
REMARK 350   BIOMT1  22  0.309017 -0.500000 -0.809017        0.00000            
REMARK 350   BIOMT2  22 -0.500000 -0.809017  0.309017        0.00000            
REMARK 350   BIOMT3  22 -0.809017  0.309017 -0.500000        0.00000            
REMARK 350   BIOMT1  23  0.000000  0.000000 -1.000000        0.00000            
REMARK 350   BIOMT2  23 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT3  23  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT1  24  0.309017  0.500000 -0.809017        0.00000            
REMARK 350   BIOMT2  24 -0.500000  0.809017  0.309017        0.00000            
REMARK 350   BIOMT3  24  0.809017  0.309017  0.500000        0.00000            
REMARK 350   BIOMT1  25  0.809017  0.309017 -0.500000        0.00000            
REMARK 350   BIOMT2  25  0.309017  0.500000  0.809017        0.00000            
REMARK 350   BIOMT3  25  0.500000 -0.809017  0.309017        0.00000            
REMARK 350   BIOMT1  26 -0.309017 -0.500000 -0.809017        0.00000            
REMARK 350   BIOMT2  26 -0.500000  0.809017 -0.309017        0.00000            
REMARK 350   BIOMT3  26  0.809017  0.309017 -0.500000        0.00000            
REMARK 350   BIOMT1  27 -0.309017  0.500000 -0.809017        0.00000            
REMARK 350   BIOMT2  27  0.500000  0.809017  0.309017        0.00000            
REMARK 350   BIOMT3  27  0.809017 -0.309017 -0.500000        0.00000            
REMARK 350   BIOMT1  28  0.500000  0.809017 -0.309017        0.00000            
REMARK 350   BIOMT2  28  0.809017 -0.309017  0.500000        0.00000            
REMARK 350   BIOMT3  28  0.309017 -0.500000 -0.809017        0.00000            
REMARK 350   BIOMT1  29  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2  29  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT3  29  0.000000  0.000000 -1.000000        0.00000            
REMARK 350   BIOMT1  30  0.500000 -0.809017 -0.309017        0.00000            
REMARK 350   BIOMT2  30 -0.809017 -0.309017 -0.500000        0.00000            
REMARK 350   BIOMT3  30  0.309017  0.500000 -0.809017        0.00000            
REMARK 350   BIOMT1  31 -0.500000  0.809017  0.309017        0.00000            
REMARK 350   BIOMT2  31 -0.809017 -0.309017 -0.500000        0.00000            
REMARK 350   BIOMT3  31 -0.309017 -0.500000  0.809017        0.00000            
REMARK 350   BIOMT1  32  0.309017  0.500000  0.809017        0.00000            
REMARK 350   BIOMT2  32 -0.500000  0.809017 -0.309017        0.00000            
REMARK 350   BIOMT3  32 -0.809017 -0.309017  0.500000        0.00000            
REMARK 350   BIOMT1  33  0.309017 -0.500000  0.809017        0.00000            
REMARK 350   BIOMT2  33  0.500000  0.809017  0.309017        0.00000            
REMARK 350   BIOMT3  33 -0.809017  0.309017  0.500000        0.00000            
REMARK 350   BIOMT1  34 -0.500000 -0.809017  0.309017        0.00000            
REMARK 350   BIOMT2  34  0.809017 -0.309017  0.500000        0.00000            
REMARK 350   BIOMT3  34 -0.309017  0.500000  0.809017        0.00000            
REMARK 350   BIOMT1  35 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2  35  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT3  35  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1  36  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT2  36  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT3  36  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT1  37 -0.309017 -0.500000  0.809017        0.00000            
REMARK 350   BIOMT2  37  0.500000 -0.809017 -0.309017        0.00000            
REMARK 350   BIOMT3  37  0.809017  0.309017  0.500000        0.00000            
REMARK 350   BIOMT1  38 -0.809017 -0.309017  0.500000        0.00000            
REMARK 350   BIOMT2  38 -0.309017 -0.500000 -0.809017        0.00000            
REMARK 350   BIOMT3  38  0.500000 -0.809017  0.309017        0.00000            
REMARK 350   BIOMT1  39 -0.809017  0.309017  0.500000        0.00000            
REMARK 350   BIOMT2  39 -0.309017  0.500000 -0.809017        0.00000            
REMARK 350   BIOMT3  39 -0.500000 -0.809017 -0.309017        0.00000            
REMARK 350   BIOMT1  40 -0.309017  0.500000  0.809017        0.00000            
REMARK 350   BIOMT2  40  0.500000  0.809017 -0.309017        0.00000            
REMARK 350   BIOMT3  40 -0.809017  0.309017 -0.500000        0.00000            
REMARK 350   BIOMT1  41  0.809017  0.309017 -0.500000        0.00000            
REMARK 350   BIOMT2  41 -0.309017 -0.500000 -0.809017        0.00000            
REMARK 350   BIOMT3  41 -0.500000  0.809017 -0.309017        0.00000            
REMARK 350   BIOMT1  42  0.809017 -0.309017 -0.500000        0.00000            
REMARK 350   BIOMT2  42 -0.309017  0.500000 -0.809017        0.00000            
REMARK 350   BIOMT3  42  0.500000  0.809017  0.309017        0.00000            
REMARK 350   BIOMT1  43  0.309017 -0.500000 -0.809017        0.00000            
REMARK 350   BIOMT2  43  0.500000  0.809017 -0.309017        0.00000            
REMARK 350   BIOMT3  43  0.809017 -0.309017  0.500000        0.00000            
REMARK 350   BIOMT1  44  0.000000  0.000000 -1.000000        0.00000            
REMARK 350   BIOMT2  44  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT3  44  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT1  45  0.309017  0.500000 -0.809017        0.00000            
REMARK 350   BIOMT2  45  0.500000 -0.809017 -0.309017        0.00000            
REMARK 350   BIOMT3  45 -0.809017 -0.309017 -0.500000        0.00000            
REMARK 350   BIOMT1  46 -0.500000 -0.809017 -0.309017        0.00000            
REMARK 350   BIOMT2  46  0.809017 -0.309017 -0.500000        0.00000            
REMARK 350   BIOMT3  46  0.309017 -0.500000  0.809017        0.00000            
REMARK 350   BIOMT1  47 -0.809017  0.309017 -0.500000        0.00000            
REMARK 350   BIOMT2  47  0.309017 -0.500000 -0.809017        0.00000            
REMARK 350   BIOMT3  47 -0.500000 -0.809017  0.309017        0.00000            
REMARK 350   BIOMT1  48  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT2  48  0.000000  0.000000 -1.000000        0.00000            
REMARK 350   BIOMT3  48 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT1  49  0.809017  0.309017  0.500000        0.00000            
REMARK 350   BIOMT2  49  0.309017  0.500000 -0.809017        0.00000            
REMARK 350   BIOMT3  49 -0.500000  0.809017  0.309017        0.00000            
REMARK 350   BIOMT1  50  0.500000 -0.809017  0.309017        0.00000            
REMARK 350   BIOMT2  50  0.809017  0.309017 -0.500000        0.00000            
REMARK 350   BIOMT3  50  0.309017  0.500000  0.809017        0.00000            
REMARK 350   BIOMT1  51  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT2  51  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT3  51  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT1  52  0.809017  0.309017  0.500000        0.00000            
REMARK 350   BIOMT2  52 -0.309017 -0.500000  0.809017        0.00000            
REMARK 350   BIOMT3  52  0.500000 -0.809017 -0.309017        0.00000            
REMARK 350   BIOMT1  53  0.500000 -0.809017  0.309017        0.00000            
REMARK 350   BIOMT2  53 -0.809017 -0.309017  0.500000        0.00000            
REMARK 350   BIOMT3  53 -0.309017 -0.500000 -0.809017        0.00000            
REMARK 350   BIOMT1  54 -0.500000 -0.809017 -0.309017        0.00000            
REMARK 350   BIOMT2  54 -0.809017  0.309017  0.500000        0.00000            
REMARK 350   BIOMT3  54 -0.309017  0.500000 -0.809017        0.00000            
REMARK 350   BIOMT1  55 -0.809017  0.309017 -0.500000        0.00000            
REMARK 350   BIOMT2  55 -0.309017  0.500000  0.809017        0.00000            
REMARK 350   BIOMT3  55  0.500000  0.809017 -0.309017        0.00000            
REMARK 350   BIOMT1  56 -0.309017 -0.500000  0.809017        0.00000            
REMARK 350   BIOMT2  56 -0.500000  0.809017  0.309017        0.00000            
REMARK 350   BIOMT3  56 -0.809017 -0.309017 -0.500000        0.00000            
REMARK 350   BIOMT1  57 -0.809017 -0.309017  0.500000        0.00000            
REMARK 350   BIOMT2  57  0.309017  0.500000  0.809017        0.00000            
REMARK 350   BIOMT3  57 -0.500000  0.809017 -0.309017        0.00000            
REMARK 350   BIOMT1  58 -0.809017  0.309017  0.500000        0.00000            
REMARK 350   BIOMT2  58  0.309017 -0.500000  0.809017        0.00000            
REMARK 350   BIOMT3  58  0.500000  0.809017  0.309017        0.00000            
REMARK 350   BIOMT1  59 -0.309017  0.500000  0.809017        0.00000            
REMARK 350   BIOMT2  59 -0.500000 -0.809017  0.309017        0.00000            
REMARK 350   BIOMT3  59  0.809017 -0.309017  0.500000        0.00000            
REMARK 350   BIOMT1  60  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT2  60 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT3  60  0.000000 -1.000000  0.000000        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 B    10A                                                     
REMARK 465     GLU B    10B                                                     
REMARK 465     GLN B    26A                                                     
REMARK 465     GLU B    26B                                                     
REMARK 465     ASN B    26C                                                     
REMARK 465     PHE B    26D                                                     
REMARK 465     THR B    26E                                                     
REMARK 465     HIS B    26F                                                     
REMARK 465     PRO B    26G                                                     
REMARK 465     SER B    26H                                                     
REMARK 465     GLY B    26I                                                     
REMARK 465     VAL B    26J                                                     
REMARK 465     GLY B    26K                                                     
REMARK 465     GLU B    26L                                                     
REMARK 465     ALA B    31A                                                     
REMARK 465     ASN B    31B                                                     
REMARK 465     LEU B    31C                                                     
REMARK 465     LEU B    31D                                                     
REMARK 465     ALA B    31E                                                     
REMARK 465     LYS B    31F                                                     
REMARK 465     GLY B    31G                                                     
REMARK 465     GLU B   507A                                                     
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   O    SER 1     3     OD1  ASN 3   152              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   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   O    SER 1     3     CG   ASN 3   152              1.17            
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   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   O    VAL 1   141     ND2  ASN 1   143              1.52            
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 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   CZ   ARG 1   200     CA   ALA 3    82              1.66            
REMARK 500   O    ARG 1    26     CG   GLU 3   210              1.67            
REMARK 500   NH1  ARG 1   200     CA   ALA 3    83              1.69            
REMARK 500   C    SER 1     3     OD1  ASN 3   152              1.70            
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   NE2  GLN 2   139     N    PHE 3    90              1.78            
REMARK 500   NH1  ARG 1   200     C    ALA 3    82              1.78            
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   NH2  ARG 1   200     C    ALA 3    82              1.86            
REMARK 500   O    SER 1     3     ND2  ASN 3   152              1.86            
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      94 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    PHE 1 163   CA  -  C   -  N   ANGL. DEV. = -16.9 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    SER 1 134       70.53     57.20                                   
REMARK 500    THR 1 140     -156.80    -63.29                                   
REMARK 500    ASN 1 143      142.27     77.08                                   
REMARK 500    VAL 1 144     -101.77   -152.96                                   
REMARK 500    ASP 1 147      -38.41   -133.75                                   
REMARK 500    GLN 1 153       47.43   -102.07                                   
REMARK 500    THR 1 161       43.01    -89.68                                   
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    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    SER A  63      -86.28     56.08                                   
REMARK 500    PHE A  72      -94.73    -72.02                                   
REMARK 500    ALA A  74       37.58    -90.87                                   
REMARK 500    TYR A  80      -63.36   -136.68                                   
REMARK 500    ALA A  81     -101.12    -82.99                                   
REMARK 500    GLN A 102      -93.11     56.45                                   
REMARK 500    LEU A 111       37.30    -85.14                                   
REMARK 500    GLU A 121     -156.30   -134.98                                   
REMARK 500    ARG A 122       85.04   -159.16                                   
REMARK 500    ARG A 143       87.29   -158.79                                   
REMARK 500    SER A 144     -129.49   -158.07                                   
REMARK 500    ILE A 147     -147.19   -125.45                                   
REMARK 500    ALA A 149     -105.67     57.62                                   
REMARK 500    THR A 164     -156.55    -99.18                                   
REMARK 500    PHE A 177       79.71     56.92                                   
REMARK 500    GLN A 180      -70.29    -79.98                                   
REMARK 500    ASN A 205      -76.74    -75.35                                   
REMARK 500    ARG A 211     -152.04    -89.11                                   
REMARK 500    ALA A 213     -132.91   -131.74                                   
REMARK 500    GLN A 214     -145.61    -88.25                                   
REMARK 500    ASN A 232      -20.30   -144.16                                   
REMARK 500    ASP A 234      -13.22   -153.39                                   
REMARK 500    ARG A 245       69.86   -111.18                                   
REMARK 500    ALA A 247       89.78     57.20                                   
REMARK 500    ARG A 248       52.35     38.04                                   
REMARK 500    THR A 249       73.88     54.78                                   
REMARK 500    LEU A 250      -59.58   -123.71                                   
REMARK 500    LYS A 259      -46.15   -130.62                                   
REMARK 500    MET A 261       85.50     57.26                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     106 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY                                       
REMARK 500                                                                      
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY                       
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER                 
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;                     
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;                            
REMARK 500 I=INSERTION CODE).                                                   
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        ANGLE                                           
REMARK 500    PHE 1 163         13.76                                           
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                              MG 12001  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP 1 147   OD1                                                    
REMARK 620 2 ASP B 102   OD2 117.4                                              
REMARK 620 3 SER B 104   OG   72.7  73.7                                        
REMARK 620 4 GLU B 202   OE2  59.7  93.4 117.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B 602  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 109   O                                                      
REMARK 620 2 ASP B 110   OD1 107.5                                              
REMARK 620 3 LYS B 317   O   153.4  84.7                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B 601  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU B 141   OE1                                                    
REMARK 620 2 ASP B 199   OD1 123.1                                              
REMARK 620 3 ASP B 199   OD2  91.3  43.7                                        
REMARK 620 4 PRO B 201   O    87.6  92.1  59.1                                  
REMARK 620 5 GLU B 202   OE1  83.6 151.8 157.3  98.4                            
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 MG 1 2001                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA B 601                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA B 602                  
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-3635   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  5NEU 1    1   208  UNP    Q6PMW3   Q6PMW3_9PICO   725    932             
DBREF  5NEU 2    1   218  UNP    Q6PMW3   Q6PMW3_9PICO   287    504             
DBREF1 5NEU 3    1   220  UNP                  A0A1C6ZW60_9PICO                 
DBREF2 5NEU 3     A0A1C6ZW60                        304         523             
DBREF  5NEU 4    1    85  UNP    E1ACS1   E1ACS1_9PICO   202    286             
DBREF  5NEU A    1   594  UNP    P06756   ITAV_HUMAN      31    624             
DBREF  5NEU B    5   539  UNP    P18564   ITB6_HUMAN      22    491             
SEQADV 5NEU TYR 2   93  UNP  Q6PMW3    SER   379 ENGINEERED MUTATION            
SEQADV 5NEU THR 3  168  UNP  A0A1C6ZW6 ALA   471 CONFLICT                       
SEQADV 5NEU VAL 3  174  UNP  A0A1C6ZW6 ALA   477 CONFLICT                       
SEQADV 5NEU     A       UNP  P06756    ALA    60 DELETION                       
SEQADV 5NEU     A       UNP  P06756    SER    61 DELETION                       
SEQADV 5NEU CYS A  400  UNP  P06756    MET   430 CONFLICT                       
SEQADV 5NEU     A       UNP  P06756    GLN   534 DELETION                       
SEQADV 5NEU     A       UNP  P06756    LYS   535 DELETION                       
SEQADV 5NEU CYS B  249  UNP  P18564    ILE   287 CONFLICT                       
SEQADV 5NEU ASN B  517  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 HIS 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  590  PHE ASN LEU ASP VAL ASP SER PRO ALA GLU TYR SER GLY          
SEQRES   2 A  590  PRO GLU GLY SER TYR PHE GLY PHE ALA VAL ASP PHE PHE          
SEQRES   3 A  590  VAL PRO SER SER ARG MET PHE LEU LEU VAL GLY ALA PRO          
SEQRES   4 A  590  LYS ALA ASN THR THR GLN PRO GLY ILE VAL GLU GLY GLY          
SEQRES   5 A  590  GLN VAL LEU LYS CYS ASP TRP SER SER THR ARG ARG CYS          
SEQRES   6 A  590  GLN PRO ILE GLU PHE ASP ALA THR GLY ASN ARG ASP TYR          
SEQRES   7 A  590  ALA LYS ASP ASP PRO LEU GLU PHE LYS SER HIS GLN TRP          
SEQRES   8 A  590  PHE GLY ALA SER VAL ARG SER LYS GLN ASP LYS ILE LEU          
SEQRES   9 A  590  ALA CYS ALA PRO LEU TYR HIS TRP ARG THR GLU MET LYS          
SEQRES  10 A  590  GLN GLU ARG GLU PRO VAL GLY THR CYS PHE LEU GLN ASP          
SEQRES  11 A  590  GLY THR LYS THR VAL GLU TYR ALA PRO CYS ARG SER GLN          
SEQRES  12 A  590  ASP ILE ASP ALA ASP GLY GLN GLY PHE CYS GLN GLY GLY          
SEQRES  13 A  590  PHE SER ILE ASP PHE THR LYS ALA ASP ARG VAL LEU LEU          
SEQRES  14 A  590  GLY GLY PRO GLY SER PHE TYR TRP GLN GLY GLN LEU ILE          
SEQRES  15 A  590  SER ASP GLN VAL ALA GLU ILE VAL SER LYS TYR ASP PRO          
SEQRES  16 A  590  ASN VAL TYR SER ILE LYS TYR ASN ASN GLN LEU ALA THR          
SEQRES  17 A  590  ARG THR ALA GLN ALA ILE PHE ASP ASP SER TYR LEU GLY          
SEQRES  18 A  590  TYR SER VAL ALA VAL GLY ASP PHE ASN GLY ASP GLY ILE          
SEQRES  19 A  590  ASP ASP PHE VAL SER GLY VAL PRO ARG ALA ALA ARG THR          
SEQRES  20 A  590  LEU GLY MET VAL TYR ILE TYR ASP GLY LYS ASN MET SER          
SEQRES  21 A  590  SER LEU TYR ASN PHE THR GLY GLU GLN MET ALA ALA TYR          
SEQRES  22 A  590  PHE GLY PHE SER VAL ALA ALA THR ASP ILE ASN GLY ASP          
SEQRES  23 A  590  ASP TYR ALA ASP VAL PHE ILE GLY ALA PRO LEU PHE MET          
SEQRES  24 A  590  ASP ARG GLY SER ASP GLY LYS LEU GLN GLU VAL GLY GLN          
SEQRES  25 A  590  VAL SER VAL SER LEU GLN ARG ALA SER GLY ASP PHE GLN          
SEQRES  26 A  590  THR THR LYS LEU ASN GLY PHE GLU VAL PHE ALA ARG PHE          
SEQRES  27 A  590  GLY SER ALA ILE ALA PRO LEU GLY ASP LEU ASP GLN ASP          
SEQRES  28 A  590  GLY PHE ASN ASP ILE ALA ILE ALA ALA PRO TYR GLY GLY          
SEQRES  29 A  590  GLU ASP LYS LYS GLY ILE VAL TYR ILE PHE ASN GLY ARG          
SEQRES  30 A  590  SER THR GLY LEU ASN ALA VAL PRO SER GLN ILE LEU GLU          
SEQRES  31 A  590  GLY GLN TRP ALA ALA ARG SER CYS PRO PRO SER PHE GLY          
SEQRES  32 A  590  TYR SER MET LYS GLY ALA THR ASP ILE ASP LYS ASN GLY          
SEQRES  33 A  590  TYR PRO ASP LEU ILE VAL GLY ALA PHE GLY VAL ASP ARG          
SEQRES  34 A  590  ALA ILE LEU TYR ARG ALA ARG PRO VAL ILE THR VAL ASN          
SEQRES  35 A  590  ALA GLY LEU GLU VAL TYR PRO SER ILE LEU ASN GLN ASP          
SEQRES  36 A  590  ASN LYS THR CYS SER LEU PRO GLY THR ALA LEU LYS VAL          
SEQRES  37 A  590  SER CYS PHE ASN VAL ARG PHE CYS LEU LYS ALA ASP GLY          
SEQRES  38 A  590  LYS GLY VAL LEU PRO ARG LYS LEU ASN PHE GLN VAL GLU          
SEQRES  39 A  590  LEU LEU LEU ASP LYS LEU LYS GLY ALA ILE ARG ARG ALA          
SEQRES  40 A  590  LEU PHE LEU TYR SER ARG SER PRO SER HIS SER LYS ASN          
SEQRES  41 A  590  MET THR ILE SER ARG GLY GLY LEU MET GLN CYS GLU GLU          
SEQRES  42 A  590  LEU ILE ALA TYR LEU ARG ASP GLU SER GLU PHE ARG ASP          
SEQRES  43 A  590  LYS LEU THR PRO ILE THR ILE PHE MET GLU TYR ARG LEU          
SEQRES  44 A  590  ASP TYR ARG THR ALA ALA ASP THR THR GLY LEU GLN PRO          
SEQRES  45 A  590  ILE LEU ASN GLN PHE THR PRO ALA ASN ILE SER ARG GLN          
SEQRES  46 A  590  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     MG  12001       1                                                       
HET     CA  B 601       1                                                       
HET     CA  B 602       1                                                       
HETNAM      MG MAGNESIUM ION                                                    
HETNAM      CA CALCIUM ION                                                      
FORMUL   7   MG    MG 2+                                                        
FORMUL   8   CA    2(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 ALA 2   56  GLU 2   59  5                                   4    
HELIX    6 AA6 GLY 2   89  ASP 2   96  1                                   8    
HELIX    7 AA7 ARG 2  135  PHE 2  143  5                                   9    
HELIX    8 AA8 ASN 3   43  CYS 3   51  1                                   9    
HELIX    9 AA9 PHE 3   90  ALA 3   95  1                                   6    
HELIX   10 AB1 GLU 3  137  CYS 3  142  5                                   6    
HELIX   11 AB2 TRP 4   67  SER 4   74  1                                   8    
HELIX   12 AB3 GLY A  175  GLN A  180  1                                   6    
HELIX   13 AB4 VAL A  188  TYR A  195  1                                   8    
HELIX   14 AB5 GLY A  366  LYS A  370  5                                   5    
HELIX   15 AB6 CYS B   12  GLY B   19  1                                   8    
HELIX   16 AB7 SER B  104  ASP B  109  5                                   6    
HELIX   17 AB8 ASP B  110  LYS B  115  1                                   6    
HELIX   18 AB9 LEU B  117  THR B  129  1                                  13    
HELIX   19 AC1 THR B  151  ALA B  156  1                                   6    
HELIX   20 AC2 ALA B  182  GLN B  192  1                                  11    
HELIX   21 AC3 GLY B  204  ALA B  211  1                                   8    
HELIX   22 AC4 PHE B  238  GLY B  246  5                                   9    
HELIX   23 AC5 TYR B  263  VAL B  268  5                                   6    
HELIX   24 AC6 THR B  273  ASN B  284  1                                  12    
HELIX   25 AC7 GLU B  295  ILE B  307  1                                  13    
HELIX   26 AC8 ASN B  321  LEU B  333  1                                  13    
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 3 ALA A   9  SER A  12  0                                        
SHEET    2 AB3 3 ARG A 431  TYR A 435 -1  O  LEU A 434   N  ALA A   9           
SHEET    3 AB3 3 LEU A 422  ALA A 426 -1  N  LEU A 422   O  TYR A 435           
SHEET    1 AB4 4 VAL A  23  PHE A  26  0                                        
SHEET    2 AB4 4 PHE A  35  ALA A  40 -1  O  PHE A  35   N  PHE A  26           
SHEET    3 AB4 4 GLN A  55  ASP A  60 -1  O  LEU A  57   N  VAL A  38           
SHEET    4 AB4 4 ARG A  66  ILE A  70 -1  O  GLN A  68   N  LYS A  58           
SHEET    1 AB5 3 GLU A  87  PHE A  88  0                                        
SHEET    2 AB5 3 HIS A 113  TRP A 114 -1  O  HIS A 113   N  PHE A  88           
SHEET    3 AB5 3 GLU A 123  PRO A 124 -1  O  GLU A 123   N  TRP A 114           
SHEET    1 AB6 4 SER A  97  LYS A 101  0                                        
SHEET    2 AB6 4 LYS A 104  ALA A 109 -1  O  LYS A 104   N  LYS A 101           
SHEET    3 AB6 4 THR A 127  ASP A 132 -1  O  PHE A 129   N  ALA A 107           
SHEET    4 AB6 4 LYS A 135  TYR A 139 -1  O  VAL A 137   N  LEU A 130           
SHEET    1 AB7 3 ASP A 162  PHE A 163  0                                        
SHEET    2 AB7 3 ARG A 168  LEU A 170 -1  O  LEU A 170   N  ASP A 162           
SHEET    3 AB7 3 SER A 185  GLN A 187 -1  O  ASP A 186   N  VAL A 169           
SHEET    1 AB8 4 VAL A 226  ALA A 227  0                                        
SHEET    2 AB8 4 PHE A 239  VAL A 243 -1  O  VAL A 240   N  ALA A 227           
SHEET    3 AB8 4 MET A 252  TYR A 256 -1  O  TYR A 256   N  PHE A 239           
SHEET    4 AB8 4 SER A 263  ASN A 266 -1  O  LEU A 264   N  ILE A 255           
SHEET    1 AB9 4 ALA A 282  THR A 283  0                                        
SHEET    2 AB9 4 ASP A 292  ILE A 295 -1  O  ASP A 292   N  THR A 283           
SHEET    3 AB9 4 GLN A 314  LEU A 319 -1  O  SER A 316   N  ILE A 295           
SHEET    4 AB9 4 GLN A 327  ASN A 332 -1  O  LEU A 331   N  VAL A 315           
SHEET    1 AC1 2 MET A 301  ASP A 302  0                                        
SHEET    2 AC1 2 GLN A 310  GLU A 311 -1  O  GLN A 310   N  ASP A 302           
SHEET    1 AC2 3 ALA A 343  GLY A 348  0                                        
SHEET    2 AC2 3 ASP A 357  ALA A 362 -1  O  ALA A 359   N  ALA A 345           
SHEET    3 AC2 3 ILE A 372  PHE A 376 -1  O  ILE A 372   N  ALA A 362           
SHEET    1 AC3 4 LEU A 447  TYR A 450  0                                        
SHEET    2 AC3 4 CYS A 472  ASP A 482 -1  O  ARG A 476   N  GLU A 448           
SHEET    3 AC3 4 GLN A 534  LEU A 542 -1  O  ALA A 540   N  PHE A 473           
SHEET    4 AC3 4 ALA A 511  PHE A 513 -1  N  LEU A 512   O  TYR A 541           
SHEET    1 AC4 4 LEU A 447  TYR A 450  0                                        
SHEET    2 AC4 4 CYS A 472  ASP A 482 -1  O  ARG A 476   N  GLU A 448           
SHEET    3 AC4 4 VAL A 440  ASN A 444 -1  N  ASN A 444   O  LYS A 480           
SHEET    4 AC4 4 ILE A 577  LEU A 578  1  O  ILE A 577   N  ILE A 441           
SHEET    1 AC5 4 HIS A 521  ILE A 527  0                                        
SHEET    2 AC5 4 LEU A 491  LEU A 498 -1  N  LEU A 497   O  HIS A 521           
SHEET    3 AC5 4 ILE A 557  LEU A 563 -1  O  GLU A 560   N  GLU A 496           
SHEET    4 AC5 4 ASN A 585  ARG A 588 -1  O  ILE A 586   N  MET A 559           
SHEET    1 AC6 2 ALA B  23  TRP B  24  0                                        
SHEET    2 AC6 2 CYS B  28  ASP B  29 -1  O  ASP B  29   N  ALA B  23           
SHEET    1 AC7 5 GLN B  43  ILE B  46  0                                        
SHEET    2 AC7 5 SER B  70  LYS B  74 -1  O  LYS B  74   N  GLN B  43           
SHEET    3 AC7 5 GLU B 494  VAL B 497  1  O  LEU B 496   N  LEU B  73           
SHEET    4 AC7 5 ARG B 480  PRO B 486 -1  N  ILE B 482   O  LEU B 495           
SHEET    5 AC7 5 LEU B 426  LEU B 429 -1  N  LEU B 429   O  ILE B 483           
SHEET    1 AC8 2 ALA B  80  THR B  82  0                                        
SHEET    2 AC8 2 THR B 469  ASN B 471 -1  O  VAL B 470   N  GLN B  81           
SHEET    1 AC9 2 VAL B  85  HIS B  86  0                                        
SHEET    2 AC9 2 SER B 465  PHE B 466 -1  O  PHE B 466   N  VAL B  85           
SHEET    1 AD1 3 PHE B 132  LEU B 134  0                                        
SHEET    2 AD1 3 VAL B  95  ASP B 102  1  N  VAL B  95   O  ARG B 133           
SHEET    3 AD1 3 SER B 138  PHE B 139  1  O  PHE B 139   N  MET B 101           
SHEET    1 AD2 5 PHE B 132  LEU B 134  0                                        
SHEET    2 AD2 5 VAL B  95  ASP B 102  1  N  VAL B  95   O  ARG B 133           
SHEET    3 AD2 5 LEU B 225  VAL B 231  1  O  LEU B 225   N  ASP B  96           
SHEET    4 AD2 5 LEU B 287  ALA B 291  1  O  ILE B 289   N  LEU B 228           
SHEET    5 AD2 5 ALA B 310  THR B 311  1  O  THR B 311   N  PHE B 290           
SHEET    1 AD3 2 ALA B 441  ILE B 442  0                                        
SHEET    2 AD3 2 LEU B 448  PHE B 449 -1  O  PHE B 449   N  ALA B 441           
SHEET    1 AD4 2 GLY B 520  GLN B 523  0                                        
SHEET    2 AD4 2 VAL B 526  CYS B 529 -1  O  VAL B 526   N  GLN B 523           
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  249                          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   22                          1555   1555  2.03  
SSBOND   8 CYS B   12    CYS B  503                          1555   1555  2.03  
SSBOND   9 CYS B   15    CYS B   28                          1555   1555  2.03  
SSBOND  10 CYS B   25    CYS B   32                          1555   1555  2.03  
SSBOND  11 CYS B  159    CYS B  166                          1555   1555  2.03  
SSBOND  12 CYS B  214    CYS B  255                          1555   1555  2.03  
SSBOND  13 CYS B  443    CYS B  455                          1555   1555  2.03  
SSBOND  14 CYS B  475    CYS B  501                          1555   1555  2.03  
SSBOND  15 CYS B  505    CYS B  524                          1555   1555  2.03  
SSBOND  16 CYS B  515    CYS B  527                          1555   1555  2.03  
SSBOND  17 CYS B  529    CYS B  538                          1555   1555  2.03  
LINK         OD1 ASP 1 147                MG    MG 12001     1555   1555  2.76  
LINK         OD2 ASP B 102                MG    MG 12001     1555   1555  2.70  
LINK         OG  SER B 104                MG    MG 12001     1555   1555  2.28  
LINK         O   ASP B 109                CA    CA B 602     1555   1555  3.14  
LINK         OD1 ASP B 110                CA    CA B 602     1555   1555  2.65  
LINK         OE1 GLU B 141                CA    CA B 601     1555   1555  2.61  
LINK         OD1 ASP B 199                CA    CA B 601     1555   1555  2.61  
LINK         OD2 ASP B 199                CA    CA B 601     1555   1555  3.14  
LINK         O   PRO B 201                CA    CA B 601     1555   1555  2.71  
LINK         OE1 GLU B 202                CA    CA B 601     1555   1555  2.63  
LINK         OE2 GLU B 202                MG    MG 12001     1555   1555  2.96  
LINK         O   LYS B 317                CA    CA B 602     1555   1555  2.57  
CISPEP   1 ALA 1  110    PRO 1  111          0        -5.74                     
CISPEP   2 ASN 1  131    GLY 1  132          0        -0.17                     
CISPEP   3 TYR 1  136    GLY 1  137          0         0.05                     
CISPEP   4 GLY 1  137    ASP 1  138          0         0.04                     
CISPEP   5 ALA 1  142    ASN 1  143          0        -0.04                     
CISPEP   6 VAL 1  144    ARG 1  145          0         3.49                     
CISPEP   7 LEU 2   83    PRO 2   84          0         2.95                     
CISPEP   8 TYR A  450    PRO A  451          0        -0.12                     
CISPEP   9 ALA B   67    PRO B   68          0        -1.40                     
CISPEP  10 SER B  145    PRO B  146          0         1.48                     
SITE     1 AC1  5 ASP 1 147  ASP B 102  SER B 104  GLU B 202                    
SITE     2 AC1  5 ALA B 234                                                     
SITE     1 AC2  5 GLU B 141  ASN B 197  ASP B 199  PRO B 201                    
SITE     2 AC2  5 GLU B 202                                                     
SITE     1 AC3  4 ASP B 109  ASP B 110  LYS B 317  ASP B 318                    
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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