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Database: PDB
Entry: 3VI3
LinkDB: 3VI3
Original site: 3VI3 
HEADER    CELL ADHESION/IMMUNE SYSTEM             21-SEP-11   3VI3              
TITLE     CRYSTAL STRUCTURE OF ALPHA5BETA1 INTEGRIN HEADPIECE (LIGAND-FREE FORM)
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: INTEGRIN ALPHA-5;                                          
COMPND   3 CHAIN: A, C;                                                         
COMPND   4 FRAGMENT: UNP RESIDUES 42-664;                                       
COMPND   5 SYNONYM: CD49 ANTIGEN-LIKE FAMILY MEMBER E, FIBRONECTIN RECEPTOR     
COMPND   6 SUBUNIT ALPHA, INTEGRIN ALPHA-F, VLA-5, INTEGRIN ALPHA-5 HEAVY CHAIN,
COMPND   7 INTEGRIN ALPHA-5 LIGHT CHAIN;                                        
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MOL_ID: 2;                                                           
COMPND  10 MOLECULE: INTEGRIN BETA-1;                                           
COMPND  11 CHAIN: B, D;                                                         
COMPND  12 FRAGMENT: UNP RESIDUES 21-465;                                       
COMPND  13 SYNONYM: FIBRONECTIN RECEPTOR SUBUNIT BETA, VLA-4 SUBUNIT BETA;      
COMPND  14 ENGINEERED: YES;                                                     
COMPND  15 MOL_ID: 3;                                                           
COMPND  16 MOLECULE: SG/19 FAB FRAGMENT (LIGHT CHAIN);                          
COMPND  17 CHAIN: L, E;                                                         
COMPND  18 ENGINEERED: YES;                                                     
COMPND  19 MOL_ID: 4;                                                           
COMPND  20 MOLECULE: SG/19 FAB FRAGMENT (HEAVY CHAIN);                          
COMPND  21 CHAIN: H, F;                                                         
COMPND  22 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: FNRA, ITGA5;                                                   
SOURCE   6 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;                               
SOURCE   7 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;                           
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 10029;                                      
SOURCE   9 EXPRESSION_SYSTEM_CELL: CHO-LEC3.2.8.1 CELL;                         
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  12 ORGANISM_COMMON: HUMAN;                                              
SOURCE  13 ORGANISM_TAXID: 9606;                                                
SOURCE  14 GENE: FNRB, ITGB1, MDF2, MSK12;                                      
SOURCE  15 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;                               
SOURCE  16 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;                           
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 10029;                                      
SOURCE  18 EXPRESSION_SYSTEM_CELL: CHO-LEC3.2.8.1 CELL;                         
SOURCE  19 MOL_ID: 3;                                                           
SOURCE  20 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  21 ORGANISM_COMMON: MOUSE;                                              
SOURCE  22 ORGANISM_TAXID: 10090;                                               
SOURCE  23 EXPRESSION_SYSTEM: MUS MUSCULUS;                                     
SOURCE  24 EXPRESSION_SYSTEM_COMMON: MOUSE;                                     
SOURCE  25 EXPRESSION_SYSTEM_TAXID: 10090;                                      
SOURCE  26 EXPRESSION_SYSTEM_CELL: HYBRIDOMA;                                   
SOURCE  27 MOL_ID: 4;                                                           
SOURCE  28 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  29 ORGANISM_COMMON: MOUSE;                                              
SOURCE  30 ORGANISM_TAXID: 10090;                                               
SOURCE  31 EXPRESSION_SYSTEM: MUS MUSCULUS;                                     
SOURCE  32 EXPRESSION_SYSTEM_COMMON: MOUSE;                                     
SOURCE  33 EXPRESSION_SYSTEM_TAXID: 10090;                                      
SOURCE  34 EXPRESSION_SYSTEM_CELL: HYBRIDOMA                                    
KEYWDS    BETA PROPELLER FOLD, ROSSMANN FOLD, BETA SANDWICH, FIBRONECTIN        
KEYWDS   2 RECEPTOR, CELL ADHESION-IMMUNE SYSTEM COMPLEX                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.NAGAE,T.NOGI,J.TAKAGI                                               
REVDAT   4   22-NOV-17 3VI3    1       REMARK                                   
REVDAT   3   12-NOV-14 3VI3    1       KEYWDS                                   
REVDAT   2   18-APR-12 3VI3    1       JRNL                                     
REVDAT   1   22-FEB-12 3VI3    0                                                
JRNL        AUTH   M.NAGAE,S.RE,E.MIHARA,T.NOGI,Y.SUGITA,J.TAKAGI               
JRNL        TITL   CRYSTAL STRUCTURE OF ALPHA5BETA1 INTEGRIN ECTODOMAIN: ATOMIC 
JRNL        TITL 2 DETAILS OF THE FIBRONECTIN RECEPTOR                          
JRNL        REF    J.CELL BIOL.                  V. 197   131 2012              
JRNL        REFN                   ISSN 0021-9525                               
JRNL        PMID   22451694                                                     
JRNL        DOI    10.1083/JCB.201111077                                        
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.6.0117                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 100.00                         
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 85066                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.210                           
REMARK   3   R VALUE            (WORKING SET) : 0.207                           
REMARK   3   FREE R VALUE                     : 0.267                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 4480                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.90                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.98                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 6256                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.38                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3290                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 316                          
REMARK   3   BIN FREE R VALUE                    : 0.3820                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 22435                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 368                                     
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 71.74                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.25000                                              
REMARK   3    B22 (A**2) : -0.18000                                             
REMARK   3    B33 (A**2) : -4.81000                                             
REMARK   3    B12 (A**2) : -0.99000                                             
REMARK   3    B13 (A**2) : 5.47000                                              
REMARK   3    B23 (A**2) : 1.39000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.409         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.335         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 17.896        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.940                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.899                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 23435 ; 0.007 ; 0.020       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 31789 ; 1.262 ; 1.978       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  2911 ; 6.649 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   996 ;36.030 ;24.458       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  3703 ;18.426 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):   112 ;19.543 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  3550 ; 0.086 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 17752 ; 0.004 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3VI3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 30-SEP-11.                  
REMARK 100 THE DEPOSITION ID IS D_1000095071.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 19-APR-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 90                                 
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : PHOTON FACTORY                     
REMARK 200  BEAMLINE                       : BL-17A                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9                                
REMARK 200  MONOCHROMATOR                  : SI(111)                            
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 270                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 90446                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 116.390                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.8                               
REMARK 200  DATA REDUNDANCY                : 2.600                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.06100                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.00                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.60                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.46200                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.100                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 61.13                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.16                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M BIS-TRIS (PH6.5), 20%(W/V)          
REMARK 280  PEG8000, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K            
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, E, F                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, L, H                            
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     LEU A   602                                                      
REMARK 465     ASP A   603                                                      
REMARK 465     CYS A   604                                                      
REMARK 465     GLY A   605                                                      
REMARK 465     GLU A   606                                                      
REMARK 465     ASP A   607                                                      
REMARK 465     ASN A   608                                                      
REMARK 465     ILE A   609                                                      
REMARK 465     CYS A   610                                                      
REMARK 465     VAL A   611                                                      
REMARK 465     PRO A   612                                                      
REMARK 465     ASP A   613                                                      
REMARK 465     LEU A   614                                                      
REMARK 465     GLN A   615                                                      
REMARK 465     LEU A   616                                                      
REMARK 465     GLU A   617                                                      
REMARK 465     VAL A   618                                                      
REMARK 465     PHE A   619                                                      
REMARK 465     GLY A   620                                                      
REMARK 465     GLU A   621                                                      
REMARK 465     GLN A   622                                                      
REMARK 465     ASN A   623                                                      
REMARK 465     GLY A   624                                                      
REMARK 465     GLY A   625                                                      
REMARK 465     LEU A   626                                                      
REMARK 465     GLU A   627                                                      
REMARK 465     ASN A   628                                                      
REMARK 465     LEU A   629                                                      
REMARK 465     TYR A   630                                                      
REMARK 465     PHE A   631                                                      
REMARK 465     GLN A   632                                                      
REMARK 465     GLN B     1                                                      
REMARK 465     THR B     2                                                      
REMARK 465     ASP B     3                                                      
REMARK 465     GLU B     4                                                      
REMARK 465     ASN B     5                                                      
REMARK 465     ASN B    30                                                      
REMARK 465     SER B    31                                                      
REMARK 465     THR B    32                                                      
REMARK 465     PHE B    33                                                      
REMARK 465     LEU B    34                                                      
REMARK 465     GLN B    35                                                      
REMARK 465     GLU B    36                                                      
REMARK 465     GLY B    37                                                      
REMARK 465     MET B    38                                                      
REMARK 465     PRO B    39                                                      
REMARK 465     THR B    40                                                      
REMARK 465     SER B    41                                                      
REMARK 465     ALA B    42                                                      
REMARK 465     GLY B   446                                                      
REMARK 465     GLY B   447                                                      
REMARK 465     LEU B   448                                                      
REMARK 465     GLU B   449                                                      
REMARK 465     ASN B   450                                                      
REMARK 465     LEU B   451                                                      
REMARK 465     TYR B   452                                                      
REMARK 465     PHE B   453                                                      
REMARK 465     GLN B   454                                                      
REMARK 465     LYS C   513                                                      
REMARK 465     GLY C   514                                                      
REMARK 465     GLY C   515                                                      
REMARK 465     VAL C   516                                                      
REMARK 465     ARG C   517                                                      
REMARK 465     SER C   554                                                      
REMARK 465     GLU C   555                                                      
REMARK 465     PHE C   556                                                      
REMARK 465     ARG C   557                                                      
REMARK 465     ASP C   558                                                      
REMARK 465     LYS C   559                                                      
REMARK 465     LEU C   601                                                      
REMARK 465     LEU C   602                                                      
REMARK 465     ASP C   603                                                      
REMARK 465     CYS C   604                                                      
REMARK 465     GLY C   605                                                      
REMARK 465     GLU C   606                                                      
REMARK 465     ASP C   607                                                      
REMARK 465     ASN C   608                                                      
REMARK 465     ILE C   609                                                      
REMARK 465     CYS C   610                                                      
REMARK 465     VAL C   611                                                      
REMARK 465     PRO C   612                                                      
REMARK 465     ASP C   613                                                      
REMARK 465     LEU C   614                                                      
REMARK 465     GLN C   615                                                      
REMARK 465     LEU C   616                                                      
REMARK 465     GLU C   617                                                      
REMARK 465     VAL C   618                                                      
REMARK 465     PHE C   619                                                      
REMARK 465     GLY C   620                                                      
REMARK 465     GLU C   621                                                      
REMARK 465     GLN C   622                                                      
REMARK 465     ASN C   623                                                      
REMARK 465     GLY C   624                                                      
REMARK 465     GLY C   625                                                      
REMARK 465     LEU C   626                                                      
REMARK 465     GLU C   627                                                      
REMARK 465     ASN C   628                                                      
REMARK 465     LEU C   629                                                      
REMARK 465     TYR C   630                                                      
REMARK 465     PHE C   631                                                      
REMARK 465     GLN C   632                                                      
REMARK 465     GLN D     1                                                      
REMARK 465     THR D     2                                                      
REMARK 465     ASP D     3                                                      
REMARK 465     GLU D     4                                                      
REMARK 465     LEU D    34                                                      
REMARK 465     GLN D    35                                                      
REMARK 465     GLU D    36                                                      
REMARK 465     GLY D    37                                                      
REMARK 465     MET D    38                                                      
REMARK 465     PRO D    39                                                      
REMARK 465     THR D    40                                                      
REMARK 465     SER D    41                                                      
REMARK 465     ALA D    42                                                      
REMARK 465     GLY D   446                                                      
REMARK 465     GLY D   447                                                      
REMARK 465     LEU D   448                                                      
REMARK 465     GLU D   449                                                      
REMARK 465     ASN D   450                                                      
REMARK 465     LEU D   451                                                      
REMARK 465     TYR D   452                                                      
REMARK 465     PHE D   453                                                      
REMARK 465     GLN D   454                                                      
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   ND2  ASN C   256     C2   NAG C  2008              1.82            
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    LEU L  94   CA  -  CB  -  CG  ANGL. DEV. =  13.9 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    GLN A  51       64.95     37.50                                   
REMARK 500    PRO A  64      -71.64    -64.72                                   
REMARK 500    GLN A  66      -71.38    -74.28                                   
REMARK 500    ARG A  78      138.94    -37.75                                   
REMARK 500    SER A  85      -46.88   -143.20                                   
REMARK 500    SER A  86      -78.33     36.80                                   
REMARK 500    GLU A  90       -1.74   -144.54                                   
REMARK 500    LYS A 125     -128.74   -106.23                                   
REMARK 500    ASP A 140       68.78     39.51                                   
REMARK 500    SER A 153     -162.09   -127.00                                   
REMARK 500    LEU A 212      107.33    -56.53                                   
REMARK 500    ASP A 243     -153.16    -74.21                                   
REMARK 500    THR A 258       -5.48     66.44                                   
REMARK 500    ILE A 270      108.56    -39.86                                   
REMARK 500    ALA A 282        4.80     56.08                                   
REMARK 500    TYR A 284       45.90    -93.01                                   
REMARK 500    ARG A 350       93.28    -53.09                                   
REMARK 500    PRO A 374       -1.48    -53.85                                   
REMARK 500    ASP A 432     -169.24   -125.64                                   
REMARK 500    LEU A 474      -89.06   -144.00                                   
REMARK 500    GLN A 512       22.03    -72.35                                   
REMARK 500    GLU A 541      103.78    -59.16                                   
REMARK 500    ASN A 552       68.33    -67.55                                   
REMARK 500    SER A 554       35.86    -94.12                                   
REMARK 500    LEU A 560      -73.20    -73.53                                   
REMARK 500    PRO A 573       35.26    -77.89                                   
REMARK 500    ALA A 575       50.53     36.28                                   
REMARK 500    ASP A 578     -109.35   -104.98                                   
REMARK 500    LYS B   9     -152.02    -82.57                                   
REMARK 500    ALA B  10       89.51    -66.98                                   
REMARK 500    LYS B  13     -149.99   -143.72                                   
REMARK 500    SER B  14     -102.80    -86.95                                   
REMARK 500    CYS B  15      -72.85   -115.83                                   
REMARK 500    CYS B  25      118.67    -37.61                                   
REMARK 500    ASP B  45      -62.71   -123.46                                   
REMARK 500    GLU B  48       20.35    -78.96                                   
REMARK 500    PRO B  57       46.74    -69.68                                   
REMARK 500    ASN B  62       89.18   -155.40                                   
REMARK 500    ASN B  72       57.87   -158.84                                   
REMARK 500    ARG B  78       35.94    -95.63                                   
REMARK 500    VAL B 168      -73.27   -129.05                                   
REMARK 500    THR B 171       54.26    -92.82                                   
REMARK 500    CYS B 187     -160.37   -112.77                                   
REMARK 500    SER B 222     -155.49   -117.57                                   
REMARK 500    VAL B 250     -169.37   -119.47                                   
REMARK 500    ALA B 265      133.74    -39.31                                   
REMARK 500    VAL B 274      -13.43   -141.55                                   
REMARK 500    ASN B 277      134.78    -38.18                                   
REMARK 500    HIS B 282       51.12   -141.88                                   
REMARK 500    PRO B 416     -102.34    -96.06                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     150 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 PHE C  155     SER C  156                 -146.52                    
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 B2003  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU B 229   OE1                                                    
REMARK 620 2 SER B 132   OG   94.7                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG D2003  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU D 229   OE1                                                    
REMARK 620 2 SER D 132   OG   90.3                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A2004  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 TYR A 430   O                                                      
REMARK 620 2 ASP A 426   OD1 167.1                                              
REMARK 620 3 ASP A 424   OD1  79.9  87.9                                        
REMARK 620 4 ASP A 432   OD2  79.5 109.7 112.6                                  
REMARK 620 5 ASN A 428   OD1 102.0  73.7  92.0 155.1                            
REMARK 620 6 ASP A 432   OD1  93.8  86.3  70.5  48.0 154.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A2003  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 TYR A 366   O                                                      
REMARK 620 2 ASP A 364   OD2  99.8                                              
REMARK 620 3 ASP A 362   OD1 159.1  83.8                                        
REMARK 620 4 ASP A 368   OD2  75.3 154.4 109.9                                  
REMARK 620 5 ASP A 360   OD2  73.2  71.8  88.6 128.2                            
REMARK 620 6 ASP A 368   OD1 104.7 152.3  68.7  48.3 103.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA C2004  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 TYR C 430   O                                                      
REMARK 620 2 ASP C 426   OD1 165.6                                              
REMARK 620 3 ASN C 428   OD1  85.0 106.1                                        
REMARK 620 4 ASP C 432   OD2  77.3  89.0 121.0                                  
REMARK 620 5 ASP C 424   OD1  78.0 106.6 106.8 123.0                            
REMARK 620 6 ASP C 432   OD1  93.8  73.3 167.6  46.9  85.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA C2003  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 TYR C 366   O                                                      
REMARK 620 2 ASP C 362   OD1 171.2                                              
REMARK 620 3 ASP C 364   OD2  80.8  92.1                                        
REMARK 620 4 ASP C 368   OD2  71.5 117.3 127.7                                  
REMARK 620 5 ASP C 360   OD2  73.6  99.8  77.8 131.1                            
REMARK 620 6 ASP C 368   OD1 107.3  80.3 169.4  51.9 110.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA D2002  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 PRO D 228   O                                                      
REMARK 620 2 ASN D 224   OD1 170.4                                              
REMARK 620 3 GLU D 169   OE1  74.8  99.6                                        
REMARK 620 4 ASP D 226   O    98.0  83.0 150.1                                  
REMARK 620 5 ASP D 226   OD1  88.5  82.9  81.3  69.3                            
REMARK 620 6 GLU D 229   OE2  88.9 100.4 108.6 100.1 168.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B2002  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN B 224   OD1                                                    
REMARK 620 2 GLU B 169   OE1  84.0                                              
REMARK 620 3 PRO B 228   O   163.3  79.4                                        
REMARK 620 4 ASP B 226   O    91.6 153.2 104.0                                  
REMARK 620 5 GLU B 229   OE2  85.7 103.3  96.2 102.8                            
REMARK 620 6 ASP B 226   OD1  93.1  81.3  86.3  72.5 175.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A2001  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SER A 241   OG                                                     
REMARK 620 2 THR A 245   O   175.1                                              
REMARK 620 3 ASP A 243   OD1  98.9  84.1                                        
REMARK 620 4 ASP A 247   OD2  85.4  93.0 160.8                                  
REMARK 620 5 GLU A 239   OE2  81.3 102.5  92.1  69.9                            
REMARK 620 6 ASP A 247   OD1  75.7  99.8 150.0  49.2 115.6                      
REMARK 620 7 GLU A 239   OE1 125.8  58.1  84.5  77.9  44.6 122.9                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA C2001  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SER C 241   OG                                                     
REMARK 620 2 THR C 245   O   164.7                                              
REMARK 620 3 ASP C 243   OD1  62.4 102.6                                        
REMARK 620 4 GLU C 239   OE2  70.1 117.6  97.3                                  
REMARK 620 5 ASP C 247   OD2  83.7 110.3 144.6  79.2                            
REMARK 620 6 GLU C 239   OE1 120.5  69.2 122.5  50.5  82.4                      
REMARK 620 7 ASP C 247   OD1  80.7 103.8 112.0 121.9  47.9 125.3                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA C2002  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN C 295   OD1                                                    
REMARK 620 2 LEU C 299   O   146.0                                              
REMARK 620 3 ASP C 293   OD2  72.4  74.0                                        
REMARK 620 4 ASP C 301   OD1 118.9  84.8 125.2                                  
REMARK 620 5 ASP C 297   OD1  80.2  90.7  82.0 149.3                            
REMARK 620 6 ASP C 301   OD2  87.6  90.5  78.9  50.9 159.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A2002  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 297   OD1                                                    
REMARK 620 2 ASN A 295   OD1  66.1                                              
REMARK 620 3 ASP A 293   OD2  83.4  91.2                                        
REMARK 620 4 LEU A 299   O   116.4 145.4  56.6                                  
REMARK 620 5 ASP A 301   OD1 156.5 100.9 117.5  85.6                            
REMARK 620 6 ASP A 301   OD2 133.3  69.6  83.5  92.3  47.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B2001  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 138   OD1                                                    
REMARK 620 2 ASP B 137   OD2  68.4                                              
REMARK 620 3 SER B 134   O    89.2  72.7                                        
REMARK 620 4 ALA B 342   O    74.7 100.0 163.9                                  
REMARK 620 5 ASP B 137   OD1 103.2  55.9 115.8  68.5                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA D2001  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP D 137   OD1                                                    
REMARK 620 2 ASP D 138   OD1  84.9                                              
REMARK 620 3 ALA D 342   O    68.7  71.3                                        
REMARK 620 4 SER D 134   O   125.4  96.8 161.7                                  
REMARK 620 5 ASP D 137   OD2  55.7  69.5 113.0  73.8                            
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 CA A 2001                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 2002                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 2003                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 2004                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 2005                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 2006                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 2007                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 2008                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 2009                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 2010                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA A 2011                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 2012                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 2013                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 2014                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 2015                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 2001                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 2002                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 2003                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 2004                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 2005                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 2006                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 2001                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 2002                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 2003                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 2004                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 2005                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 2006                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 2007                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 2008                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 2009                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 2010                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 2011                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA C 2012                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN C 2013                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN C 2014                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN C 2015                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 2016                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA D 2001                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA D 2002                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG D 2003                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 2004                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3VI4   RELATED DB: PDB                                   
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 1. THE SEQUENCE CONFLICTS OF ENTITY 2 (INTEGRIN BETA-1) ARE BASED    
REMARK 999 ON REFERENCE 1 OF DATABASE UNIPROTKB/SWISS-PROT P05556 (ITB1_HUMAN)  
REMARK 999 . 2. THE SEQUENCE OF SG/19 LIGHT CHAIN HAS BEEN DEPOSITED TO EMBL    
REMARK 999 WITH ACCESSION NUMBER HE578878, AND SG/19 HEAVY CHAIN SG/19 HAS      
REMARK 999 BEEN DEPOSITED TO EMBL WITH ACCESSION NUMBER HE578877.               
DBREF  3VI3 A    1   623  UNP    P08648   ITA5_HUMAN      42    664             
DBREF  3VI3 B    1   445  UNP    P05556   ITB1_HUMAN      21    465             
DBREF  3VI3 C    1   623  UNP    P08648   ITA5_HUMAN      42    664             
DBREF  3VI3 D    1   445  UNP    P05556   ITB1_HUMAN      21    465             
DBREF  3VI3 L    1   219  PDB    3VI3     3VI3             1    219             
DBREF  3VI3 E    1   219  PDB    3VI3     3VI3             1    219             
DBREF  3VI3 H    1   218  PDB    3VI3     3VI3             1    218             
DBREF  3VI3 F    1   218  PDB    3VI3     3VI3             1    218             
SEQADV 3VI3 GLY A  624  UNP  P08648              EXPRESSION TAG                 
SEQADV 3VI3 GLY A  625  UNP  P08648              EXPRESSION TAG                 
SEQADV 3VI3 LEU A  626  UNP  P08648              EXPRESSION TAG                 
SEQADV 3VI3 GLU A  627  UNP  P08648              EXPRESSION TAG                 
SEQADV 3VI3 ASN A  628  UNP  P08648              EXPRESSION TAG                 
SEQADV 3VI3 LEU A  629  UNP  P08648              EXPRESSION TAG                 
SEQADV 3VI3 TYR A  630  UNP  P08648              EXPRESSION TAG                 
SEQADV 3VI3 PHE A  631  UNP  P08648              EXPRESSION TAG                 
SEQADV 3VI3 GLN A  632  UNP  P08648              EXPRESSION TAG                 
SEQADV 3VI3 HIS B   92  UNP  P05556    THR   112 SEE REMARK 999                 
SEQADV 3VI3 THR B  195  UNP  P05556    SER   215 SEE REMARK 999                 
SEQADV 3VI3 GLY B  446  UNP  P05556              EXPRESSION TAG                 
SEQADV 3VI3 GLY B  447  UNP  P05556              EXPRESSION TAG                 
SEQADV 3VI3 LEU B  448  UNP  P05556              EXPRESSION TAG                 
SEQADV 3VI3 GLU B  449  UNP  P05556              EXPRESSION TAG                 
SEQADV 3VI3 ASN B  450  UNP  P05556              EXPRESSION TAG                 
SEQADV 3VI3 LEU B  451  UNP  P05556              EXPRESSION TAG                 
SEQADV 3VI3 TYR B  452  UNP  P05556              EXPRESSION TAG                 
SEQADV 3VI3 PHE B  453  UNP  P05556              EXPRESSION TAG                 
SEQADV 3VI3 GLN B  454  UNP  P05556              EXPRESSION TAG                 
SEQADV 3VI3 GLY C  624  UNP  P08648              EXPRESSION TAG                 
SEQADV 3VI3 GLY C  625  UNP  P08648              EXPRESSION TAG                 
SEQADV 3VI3 LEU C  626  UNP  P08648              EXPRESSION TAG                 
SEQADV 3VI3 GLU C  627  UNP  P08648              EXPRESSION TAG                 
SEQADV 3VI3 ASN C  628  UNP  P08648              EXPRESSION TAG                 
SEQADV 3VI3 LEU C  629  UNP  P08648              EXPRESSION TAG                 
SEQADV 3VI3 TYR C  630  UNP  P08648              EXPRESSION TAG                 
SEQADV 3VI3 PHE C  631  UNP  P08648              EXPRESSION TAG                 
SEQADV 3VI3 GLN C  632  UNP  P08648              EXPRESSION TAG                 
SEQADV 3VI3 HIS D   92  UNP  P05556    THR   112 SEE REMARK 999                 
SEQADV 3VI3 THR D  195  UNP  P05556    SER   215 SEE REMARK 999                 
SEQADV 3VI3 GLY D  446  UNP  P05556              EXPRESSION TAG                 
SEQADV 3VI3 GLY D  447  UNP  P05556              EXPRESSION TAG                 
SEQADV 3VI3 LEU D  448  UNP  P05556              EXPRESSION TAG                 
SEQADV 3VI3 GLU D  449  UNP  P05556              EXPRESSION TAG                 
SEQADV 3VI3 ASN D  450  UNP  P05556              EXPRESSION TAG                 
SEQADV 3VI3 LEU D  451  UNP  P05556              EXPRESSION TAG                 
SEQADV 3VI3 TYR D  452  UNP  P05556              EXPRESSION TAG                 
SEQADV 3VI3 PHE D  453  UNP  P05556              EXPRESSION TAG                 
SEQADV 3VI3 GLN D  454  UNP  P05556              EXPRESSION TAG                 
SEQRES   1 A  632  PHE ASN LEU ASP ALA GLU ALA PRO ALA VAL LEU SER GLY          
SEQRES   2 A  632  PRO PRO GLY SER PHE PHE GLY PHE SER VAL GLU PHE TYR          
SEQRES   3 A  632  ARG PRO GLY THR ASP GLY VAL SER VAL LEU VAL GLY ALA          
SEQRES   4 A  632  PRO LYS ALA ASN THR SER GLN PRO GLY VAL LEU GLN GLY          
SEQRES   5 A  632  GLY ALA VAL TYR LEU CYS PRO TRP GLY ALA SER PRO THR          
SEQRES   6 A  632  GLN CYS THR PRO ILE GLU PHE ASP SER LYS GLY SER ARG          
SEQRES   7 A  632  LEU LEU GLU SER SER LEU SER SER SER GLU GLY GLU GLU          
SEQRES   8 A  632  PRO VAL GLU TYR LYS SER LEU GLN TRP PHE GLY ALA THR          
SEQRES   9 A  632  VAL ARG ALA HIS GLY SER SER ILE LEU ALA CYS ALA PRO          
SEQRES  10 A  632  LEU TYR SER TRP ARG THR GLU LYS GLU PRO LEU SER ASP          
SEQRES  11 A  632  PRO VAL GLY THR CYS TYR LEU SER THR ASP ASN PHE THR          
SEQRES  12 A  632  ARG ILE LEU GLU TYR ALA PRO CYS ARG SER ASP PHE SER          
SEQRES  13 A  632  TRP ALA ALA GLY GLN GLY TYR CYS GLN GLY GLY PHE SER          
SEQRES  14 A  632  ALA GLU PHE THR LYS THR GLY ARG VAL VAL LEU GLY GLY          
SEQRES  15 A  632  PRO GLY SER TYR PHE TRP GLN GLY GLN ILE LEU SER ALA          
SEQRES  16 A  632  THR GLN GLU GLN ILE ALA GLU SER TYR TYR PRO GLU TYR          
SEQRES  17 A  632  LEU ILE ASN LEU VAL GLN GLY GLN LEU GLN THR ARG GLN          
SEQRES  18 A  632  ALA SER SER ILE TYR ASP ASP SER TYR LEU GLY TYR SER          
SEQRES  19 A  632  VAL ALA VAL GLY GLU PHE SER GLY ASP ASP THR GLU ASP          
SEQRES  20 A  632  PHE VAL ALA GLY VAL PRO LYS GLY ASN LEU THR TYR GLY          
SEQRES  21 A  632  TYR VAL THR ILE LEU ASN GLY SER ASP ILE ARG SER LEU          
SEQRES  22 A  632  TYR ASN PHE SER GLY GLU GLN MET ALA SER TYR PHE GLY          
SEQRES  23 A  632  TYR ALA VAL ALA ALA THR ASP VAL ASN GLY ASP GLY LEU          
SEQRES  24 A  632  ASP ASP LEU LEU VAL GLY ALA PRO LEU LEU MET ASP ARG          
SEQRES  25 A  632  THR PRO ASP GLY ARG PRO GLN GLU VAL GLY ARG VAL TYR          
SEQRES  26 A  632  VAL TYR LEU GLN HIS PRO ALA GLY ILE GLU PRO THR PRO          
SEQRES  27 A  632  THR LEU THR LEU THR GLY HIS ASP GLU PHE GLY ARG PHE          
SEQRES  28 A  632  GLY SER SER LEU THR PRO LEU GLY ASP LEU ASP GLN ASP          
SEQRES  29 A  632  GLY TYR ASN ASP VAL ALA ILE GLY ALA PRO PHE GLY GLY          
SEQRES  30 A  632  GLU THR GLN GLN GLY VAL VAL PHE VAL PHE PRO GLY GLY          
SEQRES  31 A  632  PRO GLY GLY LEU GLY SER LYS PRO SER GLN VAL LEU GLN          
SEQRES  32 A  632  PRO LEU TRP ALA ALA SER HIS THR PRO ASP PHE PHE GLY          
SEQRES  33 A  632  SER ALA LEU ARG GLY GLY ARG ASP LEU ASP GLY ASN GLY          
SEQRES  34 A  632  TYR PRO ASP LEU ILE VAL GLY SER PHE GLY VAL ASP LYS          
SEQRES  35 A  632  ALA VAL VAL TYR ARG GLY ARG PRO ILE VAL SER ALA SER          
SEQRES  36 A  632  ALA SER LEU THR ILE PHE PRO ALA MET PHE ASN PRO GLU          
SEQRES  37 A  632  GLU ARG SER CYS SER LEU GLU GLY ASN PRO VAL ALA CYS          
SEQRES  38 A  632  ILE ASN LEU SER PHE CYS LEU ASN ALA SER GLY LYS HIS          
SEQRES  39 A  632  VAL ALA ASP SER ILE GLY PHE THR VAL GLU LEU GLN LEU          
SEQRES  40 A  632  ASP TRP GLN LYS GLN LYS GLY GLY VAL ARG ARG ALA LEU          
SEQRES  41 A  632  PHE LEU ALA SER ARG GLN ALA THR LEU THR GLN THR LEU          
SEQRES  42 A  632  LEU ILE GLN ASN GLY ALA ARG GLU ASP CYS ARG GLU MET          
SEQRES  43 A  632  LYS ILE TYR LEU ARG ASN GLU SER GLU PHE ARG ASP LYS          
SEQRES  44 A  632  LEU SER PRO ILE HIS ILE ALA LEU ASN PHE SER LEU ASP          
SEQRES  45 A  632  PRO GLN ALA PRO VAL ASP SER HIS GLY LEU ARG PRO ALA          
SEQRES  46 A  632  LEU HIS TYR GLN SER LYS SER ARG ILE GLU ASP LYS ALA          
SEQRES  47 A  632  GLN ILE LEU LEU ASP CYS GLY GLU ASP ASN ILE CYS VAL          
SEQRES  48 A  632  PRO ASP LEU GLN LEU GLU VAL PHE GLY GLU GLN ASN GLY          
SEQRES  49 A  632  GLY LEU GLU ASN LEU TYR PHE GLN                              
SEQRES   1 B  454  GLN THR ASP GLU ASN ARG CYS LEU LYS ALA ASN ALA LYS          
SEQRES   2 B  454  SER CYS GLY GLU CYS ILE GLN ALA GLY PRO ASN CYS GLY          
SEQRES   3 B  454  TRP CYS THR ASN SER THR PHE LEU GLN GLU GLY MET PRO          
SEQRES   4 B  454  THR SER ALA ARG CYS ASP ASP LEU GLU ALA LEU LYS LYS          
SEQRES   5 B  454  LYS GLY CYS PRO PRO ASP ASP ILE GLU ASN PRO ARG GLY          
SEQRES   6 B  454  SER LYS ASP ILE LYS LYS ASN LYS ASN VAL THR ASN ARG          
SEQRES   7 B  454  SER LYS GLY THR ALA GLU LYS LEU LYS PRO GLU ASP ILE          
SEQRES   8 B  454  HIS GLN ILE GLN PRO GLN GLN LEU VAL LEU ARG LEU ARG          
SEQRES   9 B  454  SER GLY GLU PRO GLN THR PHE THR LEU LYS PHE LYS ARG          
SEQRES  10 B  454  ALA GLU ASP TYR PRO ILE ASP LEU TYR TYR LEU MET ASP          
SEQRES  11 B  454  LEU SER TYR SER MET LYS ASP ASP LEU GLU ASN VAL LYS          
SEQRES  12 B  454  SER LEU GLY THR ASP LEU MET ASN GLU MET ARG ARG ILE          
SEQRES  13 B  454  THR SER ASP PHE ARG ILE GLY PHE GLY SER PHE VAL GLU          
SEQRES  14 B  454  LYS THR VAL MET PRO TYR ILE SER THR THR PRO ALA LYS          
SEQRES  15 B  454  LEU ARG ASN PRO CYS THR SER GLU GLN ASN CYS THR THR          
SEQRES  16 B  454  PRO PHE SER TYR LYS ASN VAL LEU SER LEU THR ASN LYS          
SEQRES  17 B  454  GLY GLU VAL PHE ASN GLU LEU VAL GLY LYS GLN ARG ILE          
SEQRES  18 B  454  SER GLY ASN LEU ASP SER PRO GLU GLY GLY PHE ASP ALA          
SEQRES  19 B  454  ILE MET GLN VAL ALA VAL CYS GLY SER LEU ILE GLY TRP          
SEQRES  20 B  454  ARG ASN VAL THR ARG LEU LEU VAL PHE SER THR ASP ALA          
SEQRES  21 B  454  GLY PHE HIS PHE ALA GLY ASP GLY LYS LEU GLY GLY ILE          
SEQRES  22 B  454  VAL LEU PRO ASN ASP GLY GLN CYS HIS LEU GLU ASN ASN          
SEQRES  23 B  454  MET TYR THR MET SER HIS TYR TYR ASP TYR PRO SER ILE          
SEQRES  24 B  454  ALA HIS LEU VAL GLN LYS LEU SER GLU ASN ASN ILE GLN          
SEQRES  25 B  454  THR ILE PHE ALA VAL THR GLU GLU PHE GLN PRO VAL TYR          
SEQRES  26 B  454  LYS GLU LEU LYS ASN LEU ILE PRO LYS SER ALA VAL GLY          
SEQRES  27 B  454  THR LEU SER ALA ASN SER SER ASN VAL ILE GLN LEU ILE          
SEQRES  28 B  454  ILE ASP ALA TYR ASN SER LEU SER SER GLU VAL ILE LEU          
SEQRES  29 B  454  GLU ASN GLY LYS LEU SER GLU GLY VAL THR ILE SER TYR          
SEQRES  30 B  454  LYS SER TYR CYS LYS ASN GLY VAL ASN GLY THR GLY GLU          
SEQRES  31 B  454  ASN GLY ARG LYS CYS SER ASN ILE SER ILE GLY ASP GLU          
SEQRES  32 B  454  VAL GLN PHE GLU ILE SER ILE THR SER ASN LYS CYS PRO          
SEQRES  33 B  454  LYS LYS ASP SER ASP SER PHE LYS ILE ARG PRO LEU GLY          
SEQRES  34 B  454  PHE THR GLU GLU VAL GLU VAL ILE LEU GLN TYR ILE CYS          
SEQRES  35 B  454  GLU CYS GLU GLY GLY LEU GLU ASN LEU TYR PHE GLN              
SEQRES   1 C  632  PHE ASN LEU ASP ALA GLU ALA PRO ALA VAL LEU SER GLY          
SEQRES   2 C  632  PRO PRO GLY SER PHE PHE GLY PHE SER VAL GLU PHE TYR          
SEQRES   3 C  632  ARG PRO GLY THR ASP GLY VAL SER VAL LEU VAL GLY ALA          
SEQRES   4 C  632  PRO LYS ALA ASN THR SER GLN PRO GLY VAL LEU GLN GLY          
SEQRES   5 C  632  GLY ALA VAL TYR LEU CYS PRO TRP GLY ALA SER PRO THR          
SEQRES   6 C  632  GLN CYS THR PRO ILE GLU PHE ASP SER LYS GLY SER ARG          
SEQRES   7 C  632  LEU LEU GLU SER SER LEU SER SER SER GLU GLY GLU GLU          
SEQRES   8 C  632  PRO VAL GLU TYR LYS SER LEU GLN TRP PHE GLY ALA THR          
SEQRES   9 C  632  VAL ARG ALA HIS GLY SER SER ILE LEU ALA CYS ALA PRO          
SEQRES  10 C  632  LEU TYR SER TRP ARG THR GLU LYS GLU PRO LEU SER ASP          
SEQRES  11 C  632  PRO VAL GLY THR CYS TYR LEU SER THR ASP ASN PHE THR          
SEQRES  12 C  632  ARG ILE LEU GLU TYR ALA PRO CYS ARG SER ASP PHE SER          
SEQRES  13 C  632  TRP ALA ALA GLY GLN GLY TYR CYS GLN GLY GLY PHE SER          
SEQRES  14 C  632  ALA GLU PHE THR LYS THR GLY ARG VAL VAL LEU GLY GLY          
SEQRES  15 C  632  PRO GLY SER TYR PHE TRP GLN GLY GLN ILE LEU SER ALA          
SEQRES  16 C  632  THR GLN GLU GLN ILE ALA GLU SER TYR TYR PRO GLU TYR          
SEQRES  17 C  632  LEU ILE ASN LEU VAL GLN GLY GLN LEU GLN THR ARG GLN          
SEQRES  18 C  632  ALA SER SER ILE TYR ASP ASP SER TYR LEU GLY TYR SER          
SEQRES  19 C  632  VAL ALA VAL GLY GLU PHE SER GLY ASP ASP THR GLU ASP          
SEQRES  20 C  632  PHE VAL ALA GLY VAL PRO LYS GLY ASN LEU THR TYR GLY          
SEQRES  21 C  632  TYR VAL THR ILE LEU ASN GLY SER ASP ILE ARG SER LEU          
SEQRES  22 C  632  TYR ASN PHE SER GLY GLU GLN MET ALA SER TYR PHE GLY          
SEQRES  23 C  632  TYR ALA VAL ALA ALA THR ASP VAL ASN GLY ASP GLY LEU          
SEQRES  24 C  632  ASP ASP LEU LEU VAL GLY ALA PRO LEU LEU MET ASP ARG          
SEQRES  25 C  632  THR PRO ASP GLY ARG PRO GLN GLU VAL GLY ARG VAL TYR          
SEQRES  26 C  632  VAL TYR LEU GLN HIS PRO ALA GLY ILE GLU PRO THR PRO          
SEQRES  27 C  632  THR LEU THR LEU THR GLY HIS ASP GLU PHE GLY ARG PHE          
SEQRES  28 C  632  GLY SER SER LEU THR PRO LEU GLY ASP LEU ASP GLN ASP          
SEQRES  29 C  632  GLY TYR ASN ASP VAL ALA ILE GLY ALA PRO PHE GLY GLY          
SEQRES  30 C  632  GLU THR GLN GLN GLY VAL VAL PHE VAL PHE PRO GLY GLY          
SEQRES  31 C  632  PRO GLY GLY LEU GLY SER LYS PRO SER GLN VAL LEU GLN          
SEQRES  32 C  632  PRO LEU TRP ALA ALA SER HIS THR PRO ASP PHE PHE GLY          
SEQRES  33 C  632  SER ALA LEU ARG GLY GLY ARG ASP LEU ASP GLY ASN GLY          
SEQRES  34 C  632  TYR PRO ASP LEU ILE VAL GLY SER PHE GLY VAL ASP LYS          
SEQRES  35 C  632  ALA VAL VAL TYR ARG GLY ARG PRO ILE VAL SER ALA SER          
SEQRES  36 C  632  ALA SER LEU THR ILE PHE PRO ALA MET PHE ASN PRO GLU          
SEQRES  37 C  632  GLU ARG SER CYS SER LEU GLU GLY ASN PRO VAL ALA CYS          
SEQRES  38 C  632  ILE ASN LEU SER PHE CYS LEU ASN ALA SER GLY LYS HIS          
SEQRES  39 C  632  VAL ALA ASP SER ILE GLY PHE THR VAL GLU LEU GLN LEU          
SEQRES  40 C  632  ASP TRP GLN LYS GLN LYS GLY GLY VAL ARG ARG ALA LEU          
SEQRES  41 C  632  PHE LEU ALA SER ARG GLN ALA THR LEU THR GLN THR LEU          
SEQRES  42 C  632  LEU ILE GLN ASN GLY ALA ARG GLU ASP CYS ARG GLU MET          
SEQRES  43 C  632  LYS ILE TYR LEU ARG ASN GLU SER GLU PHE ARG ASP LYS          
SEQRES  44 C  632  LEU SER PRO ILE HIS ILE ALA LEU ASN PHE SER LEU ASP          
SEQRES  45 C  632  PRO GLN ALA PRO VAL ASP SER HIS GLY LEU ARG PRO ALA          
SEQRES  46 C  632  LEU HIS TYR GLN SER LYS SER ARG ILE GLU ASP LYS ALA          
SEQRES  47 C  632  GLN ILE LEU LEU ASP CYS GLY GLU ASP ASN ILE CYS VAL          
SEQRES  48 C  632  PRO ASP LEU GLN LEU GLU VAL PHE GLY GLU GLN ASN GLY          
SEQRES  49 C  632  GLY LEU GLU ASN LEU TYR PHE GLN                              
SEQRES   1 D  454  GLN THR ASP GLU ASN ARG CYS LEU LYS ALA ASN ALA LYS          
SEQRES   2 D  454  SER CYS GLY GLU CYS ILE GLN ALA GLY PRO ASN CYS GLY          
SEQRES   3 D  454  TRP CYS THR ASN SER THR PHE LEU GLN GLU GLY MET PRO          
SEQRES   4 D  454  THR SER ALA ARG CYS ASP ASP LEU GLU ALA LEU LYS LYS          
SEQRES   5 D  454  LYS GLY CYS PRO PRO ASP ASP ILE GLU ASN PRO ARG GLY          
SEQRES   6 D  454  SER LYS ASP ILE LYS LYS ASN LYS ASN VAL THR ASN ARG          
SEQRES   7 D  454  SER LYS GLY THR ALA GLU LYS LEU LYS PRO GLU ASP ILE          
SEQRES   8 D  454  HIS GLN ILE GLN PRO GLN GLN LEU VAL LEU ARG LEU ARG          
SEQRES   9 D  454  SER GLY GLU PRO GLN THR PHE THR LEU LYS PHE LYS ARG          
SEQRES  10 D  454  ALA GLU ASP TYR PRO ILE ASP LEU TYR TYR LEU MET ASP          
SEQRES  11 D  454  LEU SER TYR SER MET LYS ASP ASP LEU GLU ASN VAL LYS          
SEQRES  12 D  454  SER LEU GLY THR ASP LEU MET ASN GLU MET ARG ARG ILE          
SEQRES  13 D  454  THR SER ASP PHE ARG ILE GLY PHE GLY SER PHE VAL GLU          
SEQRES  14 D  454  LYS THR VAL MET PRO TYR ILE SER THR THR PRO ALA LYS          
SEQRES  15 D  454  LEU ARG ASN PRO CYS THR SER GLU GLN ASN CYS THR THR          
SEQRES  16 D  454  PRO PHE SER TYR LYS ASN VAL LEU SER LEU THR ASN LYS          
SEQRES  17 D  454  GLY GLU VAL PHE ASN GLU LEU VAL GLY LYS GLN ARG ILE          
SEQRES  18 D  454  SER GLY ASN LEU ASP SER PRO GLU GLY GLY PHE ASP ALA          
SEQRES  19 D  454  ILE MET GLN VAL ALA VAL CYS GLY SER LEU ILE GLY TRP          
SEQRES  20 D  454  ARG ASN VAL THR ARG LEU LEU VAL PHE SER THR ASP ALA          
SEQRES  21 D  454  GLY PHE HIS PHE ALA GLY ASP GLY LYS LEU GLY GLY ILE          
SEQRES  22 D  454  VAL LEU PRO ASN ASP GLY GLN CYS HIS LEU GLU ASN ASN          
SEQRES  23 D  454  MET TYR THR MET SER HIS TYR TYR ASP TYR PRO SER ILE          
SEQRES  24 D  454  ALA HIS LEU VAL GLN LYS LEU SER GLU ASN ASN ILE GLN          
SEQRES  25 D  454  THR ILE PHE ALA VAL THR GLU GLU PHE GLN PRO VAL TYR          
SEQRES  26 D  454  LYS GLU LEU LYS ASN LEU ILE PRO LYS SER ALA VAL GLY          
SEQRES  27 D  454  THR LEU SER ALA ASN SER SER ASN VAL ILE GLN LEU ILE          
SEQRES  28 D  454  ILE ASP ALA TYR ASN SER LEU SER SER GLU VAL ILE LEU          
SEQRES  29 D  454  GLU ASN GLY LYS LEU SER GLU GLY VAL THR ILE SER TYR          
SEQRES  30 D  454  LYS SER TYR CYS LYS ASN GLY VAL ASN GLY THR GLY GLU          
SEQRES  31 D  454  ASN GLY ARG LYS CYS SER ASN ILE SER ILE GLY ASP GLU          
SEQRES  32 D  454  VAL GLN PHE GLU ILE SER ILE THR SER ASN LYS CYS PRO          
SEQRES  33 D  454  LYS LYS ASP SER ASP SER PHE LYS ILE ARG PRO LEU GLY          
SEQRES  34 D  454  PHE THR GLU GLU VAL GLU VAL ILE LEU GLN TYR ILE CYS          
SEQRES  35 D  454  GLU CYS GLU GLY GLY LEU GLU ASN LEU TYR PHE GLN              
SEQRES   1 L  219  ASP ILE VAL MET THR GLN ALA THR PRO SER ILE PRO VAL          
SEQRES   2 L  219  THR PRO GLY GLU SER VAL SER ILE SER CYS ARG SER ASN          
SEQRES   3 L  219  LYS SER LEU LEU HIS SER ASN GLY ASN THR TYR LEU TYR          
SEQRES   4 L  219  TRP PHE LEU GLN ARG PRO GLY GLN SER PRO ARG LEU LEU          
SEQRES   5 L  219  ILE PHE ARG MET SER ASN LEU ALA SER GLY VAL PRO ASP          
SEQRES   6 L  219  ARG PHE SER GLY SER GLY SER GLY THR ALA PHE THR LEU          
SEQRES   7 L  219  ARG ILE SER ARG VAL GLU ALA ALA ASP VAL GLY ILE TYR          
SEQRES   8 L  219  PHE CYS LEU GLN HIS LEU GLU TYR PRO PHE THR PHE GLY          
SEQRES   9 L  219  ALA GLY THR LYS LEU GLU LEU LYS ARG ALA ASP ALA ALA          
SEQRES  10 L  219  PRO THR VAL SER ILE PHE PRO PRO SER SER GLU GLN LEU          
SEQRES  11 L  219  THR SER GLY GLY ALA SER VAL VAL CYS PHE LEU ASN ASN          
SEQRES  12 L  219  PHE TYR PRO LYS ASP ILE ASN VAL LYS TRP LYS ILE ASP          
SEQRES  13 L  219  GLY SER GLU ARG GLN ASN GLY VAL LEU ASN SER TRP THR          
SEQRES  14 L  219  ASP GLN ASP SER LYS ASP SER THR TYR SER MET SER SER          
SEQRES  15 L  219  THR LEU THR LEU THR LYS ASP GLU TYR GLU ARG HIS ASN          
SEQRES  16 L  219  SER TYR THR CYS GLU ALA THR HIS LYS THR SER THR SER          
SEQRES  17 L  219  PRO ILE VAL LYS SER PHE ASN ARG ASN GLU CYS                  
SEQRES   1 H  218  GLN VAL HIS LEU GLN GLN SER GLY ALA GLU LEU MET LYS          
SEQRES   2 H  218  PRO GLY ALA SER VAL LYS ILE SER CYS LYS ALA THR GLY          
SEQRES   3 H  218  TYR THR PHE THR SER TYR TRP ILE GLU TRP VAL LYS GLN          
SEQRES   4 H  218  ARG PRO GLY HIS GLY LEU GLU TRP LEU GLY GLU ILE LEU          
SEQRES   5 H  218  PRO GLY SER GLY TYR ILE HIS TYR ASN GLU LYS PHE LYS          
SEQRES   6 H  218  GLY LYS ALA THR PHE THR THR ASP THR SER SER ASN THR          
SEQRES   7 H  218  ALA TYR MET GLN LEU SER SER LEU THR SER GLU ASP SER          
SEQRES   8 H  218  ALA VAL TYR TYR CYS SER ARG ALA LEU ALA LEU TYR ALA          
SEQRES   9 H  218  MET ASP TYR TRP GLY GLN GLY THR SER VAL THR VAL SER          
SEQRES  10 H  218  SER ALA LYS THR THR PRO PRO SER VAL TYR PRO LEU ALA          
SEQRES  11 H  218  PRO GLY SER ALA ALA GLN THR ASN SER MET VAL THR LEU          
SEQRES  12 H  218  GLY CYS LEU VAL LYS GLY TYR PHE PRO GLU PRO VAL THR          
SEQRES  13 H  218  VAL THR TRP ASN SER GLY SER LEU SER SER GLY VAL HIS          
SEQRES  14 H  218  THR PHE PRO ALA VAL LEU GLN SER ASP LEU TYR THR LEU          
SEQRES  15 H  218  SER SER SER VAL THR VAL PRO SER SER THR TRP PRO SER          
SEQRES  16 H  218  GLU THR VAL THR CYS ASN VAL ALA HIS PRO ALA SER SER          
SEQRES  17 H  218  THR LYS VAL ASP LYS LYS ILE VAL PRO ARG                      
SEQRES   1 E  219  ASP ILE VAL MET THR GLN ALA THR PRO SER ILE PRO VAL          
SEQRES   2 E  219  THR PRO GLY GLU SER VAL SER ILE SER CYS ARG SER ASN          
SEQRES   3 E  219  LYS SER LEU LEU HIS SER ASN GLY ASN THR TYR LEU TYR          
SEQRES   4 E  219  TRP PHE LEU GLN ARG PRO GLY GLN SER PRO ARG LEU LEU          
SEQRES   5 E  219  ILE PHE ARG MET SER ASN LEU ALA SER GLY VAL PRO ASP          
SEQRES   6 E  219  ARG PHE SER GLY SER GLY SER GLY THR ALA PHE THR LEU          
SEQRES   7 E  219  ARG ILE SER ARG VAL GLU ALA ALA ASP VAL GLY ILE TYR          
SEQRES   8 E  219  PHE CYS LEU GLN HIS LEU GLU TYR PRO PHE THR PHE GLY          
SEQRES   9 E  219  ALA GLY THR LYS LEU GLU LEU LYS ARG ALA ASP ALA ALA          
SEQRES  10 E  219  PRO THR VAL SER ILE PHE PRO PRO SER SER GLU GLN LEU          
SEQRES  11 E  219  THR SER GLY GLY ALA SER VAL VAL CYS PHE LEU ASN ASN          
SEQRES  12 E  219  PHE TYR PRO LYS ASP ILE ASN VAL LYS TRP LYS ILE ASP          
SEQRES  13 E  219  GLY SER GLU ARG GLN ASN GLY VAL LEU ASN SER TRP THR          
SEQRES  14 E  219  ASP GLN ASP SER LYS ASP SER THR TYR SER MET SER SER          
SEQRES  15 E  219  THR LEU THR LEU THR LYS ASP GLU TYR GLU ARG HIS ASN          
SEQRES  16 E  219  SER TYR THR CYS GLU ALA THR HIS LYS THR SER THR SER          
SEQRES  17 E  219  PRO ILE VAL LYS SER PHE ASN ARG ASN GLU CYS                  
SEQRES   1 F  218  GLN VAL HIS LEU GLN GLN SER GLY ALA GLU LEU MET LYS          
SEQRES   2 F  218  PRO GLY ALA SER VAL LYS ILE SER CYS LYS ALA THR GLY          
SEQRES   3 F  218  TYR THR PHE THR SER TYR TRP ILE GLU TRP VAL LYS GLN          
SEQRES   4 F  218  ARG PRO GLY HIS GLY LEU GLU TRP LEU GLY GLU ILE LEU          
SEQRES   5 F  218  PRO GLY SER GLY TYR ILE HIS TYR ASN GLU LYS PHE LYS          
SEQRES   6 F  218  GLY LYS ALA THR PHE THR THR ASP THR SER SER ASN THR          
SEQRES   7 F  218  ALA TYR MET GLN LEU SER SER LEU THR SER GLU ASP SER          
SEQRES   8 F  218  ALA VAL TYR TYR CYS SER ARG ALA LEU ALA LEU TYR ALA          
SEQRES   9 F  218  MET ASP TYR TRP GLY GLN GLY THR SER VAL THR VAL SER          
SEQRES  10 F  218  SER ALA LYS THR THR PRO PRO SER VAL TYR PRO LEU ALA          
SEQRES  11 F  218  PRO GLY SER ALA ALA GLN THR ASN SER MET VAL THR LEU          
SEQRES  12 F  218  GLY CYS LEU VAL LYS GLY TYR PHE PRO GLU PRO VAL THR          
SEQRES  13 F  218  VAL THR TRP ASN SER GLY SER LEU SER SER GLY VAL HIS          
SEQRES  14 F  218  THR PHE PRO ALA VAL LEU GLN SER ASP LEU TYR THR LEU          
SEQRES  15 F  218  SER SER SER VAL THR VAL PRO SER SER THR TRP PRO SER          
SEQRES  16 F  218  GLU THR VAL THR CYS ASN VAL ALA HIS PRO ALA SER SER          
SEQRES  17 F  218  THR LYS VAL ASP LYS LYS ILE VAL PRO ARG                      
MODRES 3VI3 ASN A  275  ASN  GLYCOSYLATION SITE                                 
MODRES 3VI3 ASN C  275  ASN  GLYCOSYLATION SITE                                 
MODRES 3VI3 ASN A  266  ASN  GLYCOSYLATION SITE                                 
MODRES 3VI3 ASN B  249  ASN  GLYCOSYLATION SITE                                 
MODRES 3VI3 ASN A  256  ASN  GLYCOSYLATION SITE                                 
MODRES 3VI3 ASN B  386  ASN  GLYCOSYLATION SITE                                 
MODRES 3VI3 ASN D  386  ASN  GLYCOSYLATION SITE                                 
MODRES 3VI3 ASN A   43  ASN  GLYCOSYLATION SITE                                 
MODRES 3VI3 ASN C   43  ASN  GLYCOSYLATION SITE                                 
MODRES 3VI3 ASN C  568  ASN  GLYCOSYLATION SITE                                 
MODRES 3VI3 ASN C  266  ASN  GLYCOSYLATION SITE                                 
MODRES 3VI3 ASN A  568  ASN  GLYCOSYLATION SITE                                 
MODRES 3VI3 ASN C  256  ASN  GLYCOSYLATION SITE                                 
MODRES 3VI3 ASN A  141  ASN  GLYCOSYLATION SITE                                 
MODRES 3VI3 ASN C  141  ASN  GLYCOSYLATION SITE                                 
HET     CA  A2001       1                                                       
HET     CA  A2002       1                                                       
HET     CA  A2003       1                                                       
HET     CA  A2004       1                                                       
HET    NAG  A2005      14                                                       
HET    NAG  A2006      14                                                       
HET    NAG  A2007      14                                                       
HET    NAG  A2008      14                                                       
HET    NAG  A2009      14                                                       
HET    NAG  A2010      14                                                       
HET    BMA  A2011      11                                                       
HET    MAN  A2012      11                                                       
HET    MAN  A2013      11                                                       
HET    MAN  A2014      11                                                       
HET    NAG  A2015      14                                                       
HET     CA  B2001       1                                                       
HET     CA  B2002       1                                                       
HET     MG  B2003       1                                                       
HET    NAG  B2004      14                                                       
HET    NAG  B2005      14                                                       
HET    NAG  B2006      14                                                       
HET     CA  C2001       1                                                       
HET     CA  C2002       1                                                       
HET     CA  C2003       1                                                       
HET     CA  C2004       1                                                       
HET    NAG  C2005      14                                                       
HET    NAG  C2006      14                                                       
HET    NAG  C2007      14                                                       
HET    NAG  C2008      14                                                       
HET    NAG  C2009      14                                                       
HET    NAG  C2010      14                                                       
HET    NAG  C2011      14                                                       
HET    BMA  C2012      11                                                       
HET    MAN  C2013      11                                                       
HET    MAN  C2014      11                                                       
HET    MAN  C2015      11                                                       
HET    NAG  C2016      14                                                       
HET     CA  D2001       1                                                       
HET     CA  D2002       1                                                       
HET     MG  D2003       1                                                       
HET    NAG  D2004      14                                                       
HETNAM      CA CALCIUM ION                                                      
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     BMA BETA-D-MANNOSE                                                   
HETNAM     MAN ALPHA-D-MANNOSE                                                  
HETNAM      MG MAGNESIUM ION                                                    
FORMUL   9   CA    12(CA 2+)                                                    
FORMUL  13  NAG    19(C8 H15 N O6)                                              
FORMUL  17  BMA    2(C6 H12 O6)                                                 
FORMUL  17  MAN    6(C6 H12 O6)                                                 
FORMUL  21   MG    2(MG 2+)                                                     
HELIX    1   1 GLY A  184  GLN A  189  1                                   6    
HELIX    2   2 THR A  196  TYR A  204  1                                   9    
HELIX    3   3 SER A  223  ASP A  227  5                                   5    
HELIX    4   4 ARG A  350  SER A  353  5                                   4    
HELIX    5   5 PHE A  438  VAL A  440  5                                   3    
HELIX    6   6 ASP B   46  LYS B   51  1                                   6    
HELIX    7   7 SER B  132  SER B  134  5                                   3    
HELIX    8   8 MET B  135  LYS B  143  1                                   9    
HELIX    9   9 SER B  144  ARG B  154  1                                  11    
HELIX   10  10 LYS B  208  GLY B  217  1                                  10    
HELIX   11  11 GLY B  230  CYS B  241  1                                  12    
HELIX   12  12 CYS B  241  GLY B  246  1                                   6    
HELIX   13  13 GLY B  268  GLY B  272  5                                   5    
HELIX   14  14 SER B  298  ASN B  309  1                                  12    
HELIX   15  15 PHE B  321  ILE B  332  1                                  12    
HELIX   16  16 ASN B  346  SER B  360  1                                  15    
HELIX   17  17 LYS B  382  GLY B  384  5                                   3    
HELIX   18  18 GLU B  390  GLY B  392  5                                   3    
HELIX   19  19 LEU C   80  LEU C   84  5                                   5    
HELIX   20  20 GLY C  184  GLN C  189  1                                   6    
HELIX   21  21 THR C  196  TYR C  204  1                                   9    
HELIX   22  22 SER C  223  ASP C  227  5                                   5    
HELIX   23  23 PHE C  438  VAL C  440  5                                   3    
HELIX   24  24 CYS D   15  GLN D   20  1                                   6    
HELIX   25  25 LEU D   47  LYS D   52  1                                   6    
HELIX   26  26 SER D  132  SER D  134  5                                   3    
HELIX   27  27 MET D  135  LEU D  145  1                                  11    
HELIX   28  28 THR D  147  ARG D  155  1                                   9    
HELIX   29  29 THR D  179  ASN D  185  1                                   7    
HELIX   30  30 LYS D  208  GLY D  217  1                                  10    
HELIX   31  31 GLY D  230  CYS D  241  1                                  12    
HELIX   32  32 CYS D  241  GLY D  246  1                                   6    
HELIX   33  33 GLY D  266  GLY D  272  5                                   7    
HELIX   34  34 SER D  298  ASN D  309  1                                  12    
HELIX   35  35 PHE D  321  ILE D  332  1                                  12    
HELIX   36  36 ASN D  346  SER D  360  1                                  15    
HELIX   37  37 THR D  388  GLY D  392  5                                   5    
HELIX   38  38 GLU L   84  VAL L   88  5                                   5    
HELIX   39  39 SER L  126  GLY L  133  1                                   8    
HELIX   40  40 LYS L  188  GLU L  192  1                                   5    
HELIX   41  41 THR H   28  TYR H   32  5                                   5    
HELIX   42  42 GLU H   62  LYS H   65  5                                   4    
HELIX   43  43 THR H   74  SER H   76  5                                   3    
HELIX   44  44 THR H   87  SER H   91  5                                   5    
HELIX   45  45 SER H  161  SER H  163  5                                   3    
HELIX   46  46 PRO H  189  TRP H  193  5                                   5    
HELIX   47  47 PRO H  205  SER H  208  5                                   4    
HELIX   48  48 GLU E   84  VAL E   88  5                                   5    
HELIX   49  49 SER E  126  SER E  132  1                                   7    
HELIX   50  50 LYS E  188  GLU E  192  1                                   5    
HELIX   51  51 THR F   28  TYR F   32  5                                   5    
HELIX   52  52 GLU F   62  LYS F   65  5                                   4    
HELIX   53  53 THR F   74  SER F   76  5                                   3    
HELIX   54  54 THR F   87  SER F   91  5                                   5    
HELIX   55  55 SER F  161  SER F  163  5                                   3    
HELIX   56  56 SER F  191  TRP F  193  5                                   3    
HELIX   57  57 PRO F  205  SER F  208  5                                   4    
SHEET    1   A 4 ALA A   9  SER A  12  0                                        
SHEET    2   A 4 LYS A 442  TYR A 446 -1  O  VAL A 445   N  ALA A   9           
SHEET    3   A 4 LEU A 433  SER A 437 -1  N  LEU A 433   O  TYR A 446           
SHEET    4   A 4 LEU A 419  GLY A 421 -1  N  ARG A 420   O  ILE A 434           
SHEET    1   B 4 VAL A  23  TYR A  26  0                                        
SHEET    2   B 4 SER A  34  ALA A  39 -1  O  LEU A  36   N  GLU A  24           
SHEET    3   B 4 ALA A  54  PRO A  59 -1  O  TYR A  56   N  VAL A  37           
SHEET    4   B 4 THR A  68  ILE A  70 -1  O  ILE A  70   N  VAL A  55           
SHEET    1   C 2 GLU A  94  TYR A  95  0                                        
SHEET    2   C 2 SER A 120  TRP A 121 -1  O  SER A 120   N  TYR A  95           
SHEET    1   D 4 VAL A 105  HIS A 108  0                                        
SHEET    2   D 4 SER A 111  ALA A 116 -1  O  LEU A 113   N  ARG A 106           
SHEET    3   D 4 THR A 134  THR A 139 -1  O  THR A 134   N  ALA A 116           
SHEET    4   D 4 ARG A 144  TYR A 148 -1  O  LEU A 146   N  LEU A 137           
SHEET    1   E 4 ALA A 170  PHE A 172  0                                        
SHEET    2   E 4 VAL A 178  GLY A 182 -1  O  VAL A 179   N  GLU A 171           
SHEET    3   E 4 GLN A 191  ALA A 195 -1  O  LEU A 193   N  LEU A 180           
SHEET    4   E 4 LEU A 217  GLN A 218 -1  O  LEU A 217   N  SER A 194           
SHEET    1   F 4 VAL A 235  GLY A 238  0                                        
SHEET    2   F 4 ASP A 247  ASN A 256 -1  O  VAL A 249   N  ALA A 236           
SHEET    3   F 4 TYR A 259  LEU A 265 -1  O  LEU A 265   N  PHE A 248           
SHEET    4   F 4 SER A 272  SER A 277 -1  O  LEU A 273   N  ILE A 264           
SHEET    1   G 4 VAL A 289  THR A 292  0                                        
SHEET    2   G 4 ASP A 301  ALA A 306 -1  O  LEU A 303   N  ALA A 290           
SHEET    3   G 4 ARG A 323  TYR A 327 -1  O  TYR A 325   N  VAL A 304           
SHEET    4   G 4 LEU A 340  THR A 343 -1  O  LEU A 340   N  VAL A 326           
SHEET    1   H 2 MET A 310  ARG A 312  0                                        
SHEET    2   H 2 PRO A 318  GLU A 320 -1  O  GLN A 319   N  ASP A 311           
SHEET    1   I 4 SER A 354  GLY A 359  0                                        
SHEET    2   I 4 ASP A 368  ALA A 373 -1  O  ASP A 368   N  GLY A 359           
SHEET    3   I 4 VAL A 383  PHE A 387 -1  O  PHE A 385   N  ILE A 371           
SHEET    4   I 4 GLN A 400  LEU A 402 -1  O  LEU A 402   N  VAL A 384           
SHEET    1   J 2 GLY A 389  GLY A 390  0                                        
SHEET    2   J 2 GLY A 393  LEU A 394 -1  O  GLY A 393   N  GLY A 390           
SHEET    1   K 5 ALA A 519  PHE A 521  0                                        
SHEET    2   K 5 ASP A 542  LEU A 550 -1  O  TYR A 549   N  LEU A 520           
SHEET    3   K 5 CYS A 481  SER A 491 -1  N  ILE A 482   O  ILE A 548           
SHEET    4   K 5 ILE A 451  ILE A 460 -1  N  SER A 453   O  SER A 491           
SHEET    5   K 5 ALA A 585  LEU A 586  1  O  ALA A 585   N  VAL A 452           
SHEET    1   L 5 MET A 464  PHE A 465  0                                        
SHEET    2   L 5 ARG A 593  ILE A 600  1  O  GLN A 599   N  PHE A 465           
SHEET    3   L 5 ILE A 563  LEU A 571 -1  N  ILE A 565   O  ASP A 596           
SHEET    4   L 5 SER A 498  LEU A 507 -1  N  GLU A 504   O  ASN A 568           
SHEET    5   L 5 THR A 528  GLN A 536 -1  O  ILE A 535   N  ILE A 499           
SHEET    1   M 2 CYS A 472  SER A 473  0                                        
SHEET    2   M 2 PRO A 478  VAL A 479 -1  O  VAL A 479   N  CYS A 472           
SHEET    1   N 6 SER B  66  LYS B  71  0                                        
SHEET    2   N 6 GLN B  98  LEU B 103 -1  O  GLN B  98   N  LYS B  71           
SHEET    3   N 6 VAL B 434  TYR B 440  1  O  ILE B 437   N  LEU B 101           
SHEET    4   N 6 SER B 420  PRO B 427 -1  N  ILE B 425   O  VAL B 434           
SHEET    5   N 6 VAL B 362  ASN B 366 -1  N  GLU B 365   O  ARG B 426           
SHEET    6   N 6 LYS B 394  CYS B 395 -1  O  CYS B 395   N  VAL B 362           
SHEET    1   O 5 ILE B  94  GLN B  95  0                                        
SHEET    2   O 5 PHE B 111  LYS B 116 -1  O  LYS B 114   N  GLN B  95           
SHEET    3   O 5 GLU B 403  SER B 412 -1  O  VAL B 404   N  PHE B 115           
SHEET    4   O 5 VAL B 373  TYR B 380 -1  N  LYS B 378   O  GLU B 407           
SHEET    5   O 5 ASN B 386  THR B 388 -1  O  GLY B 387   N  SER B 379           
SHEET    1   P 6 TYR B 199  THR B 206  0                                        
SHEET    2   P 6 PHE B 160  PHE B 167 -1  N  ILE B 162   O  THR B 206           
SHEET    3   P 6 ILE B 123  ASP B 130  1  N  TYR B 127   O  GLY B 165           
SHEET    4   P 6 THR B 251  THR B 258  1  O  LEU B 253   N  TYR B 126           
SHEET    5   P 6 ILE B 311  THR B 318  1  O  ILE B 314   N  LEU B 254           
SHEET    6   P 6 SER B 335  LEU B 340  1  O  ALA B 336   N  PHE B 315           
SHEET    1   Q 2 LEU B 283  GLU B 284  0                                        
SHEET    2   Q 2 MET B 287  TYR B 288 -1  O  MET B 287   N  GLU B 284           
SHEET    1   R 4 ALA C   9  SER C  12  0                                        
SHEET    2   R 4 LYS C 442  TYR C 446 -1  O  ALA C 443   N  LEU C  11           
SHEET    3   R 4 ASP C 432  SER C 437 -1  N  LEU C 433   O  TYR C 446           
SHEET    4   R 4 LEU C 419  ARG C 423 -1  N  ARG C 420   O  ILE C 434           
SHEET    1   S 4 VAL C  23  TYR C  26  0                                        
SHEET    2   S 4 SER C  34  ALA C  39 -1  O  LEU C  36   N  GLU C  24           
SHEET    3   S 4 ALA C  54  PRO C  59 -1  O  CYS C  58   N  VAL C  35           
SHEET    4   S 4 THR C  68  PRO C  69 -1  O  THR C  68   N  LEU C  57           
SHEET    1   T 2 GLU C  94  TYR C  95  0                                        
SHEET    2   T 2 SER C 120  TRP C 121 -1  O  SER C 120   N  TYR C  95           
SHEET    1   U 4 VAL C 105  HIS C 108  0                                        
SHEET    2   U 4 SER C 111  ALA C 116 -1  O  LEU C 113   N  ARG C 106           
SHEET    3   U 4 THR C 134  SER C 138 -1  O  THR C 134   N  ALA C 116           
SHEET    4   U 4 ILE C 145  TYR C 148 -1  O  LEU C 146   N  LEU C 137           
SHEET    1   V 4 SER C 169  PHE C 172  0                                        
SHEET    2   V 4 VAL C 178  GLY C 182 -1  O  GLY C 181   N  SER C 169           
SHEET    3   V 4 GLN C 191  ALA C 195 -1  O  ALA C 195   N  VAL C 178           
SHEET    4   V 4 LEU C 217  GLN C 218 -1  O  LEU C 217   N  SER C 194           
SHEET    1   W 4 VAL C 235  GLY C 238  0                                        
SHEET    2   W 4 ASP C 247  VAL C 252 -1  O  ASP C 247   N  GLY C 238           
SHEET    3   W 4 TYR C 261  LEU C 265 -1  O  LEU C 265   N  PHE C 248           
SHEET    4   W 4 SER C 272  SER C 277 -1  O  LEU C 273   N  ILE C 264           
SHEET    1   X 4 VAL C 289  THR C 292  0                                        
SHEET    2   X 4 ASP C 301  ALA C 306 -1  O  LEU C 303   N  ALA C 290           
SHEET    3   X 4 ARG C 323  TYR C 327 -1  O  ARG C 323   N  ALA C 306           
SHEET    4   X 4 LEU C 340  THR C 343 -1  O  LEU C 340   N  VAL C 326           
SHEET    1   Y 2 MET C 310  ARG C 312  0                                        
SHEET    2   Y 2 PRO C 318  GLU C 320 -1  O  GLN C 319   N  ASP C 311           
SHEET    1   Z 2 GLN C 329  HIS C 330  0                                        
SHEET    2   Z 2 GLY C 333  ILE C 334 -1  O  GLY C 333   N  HIS C 330           
SHEET    1  AA 4 SER C 354  GLY C 359  0                                        
SHEET    2  AA 4 ASP C 368  ALA C 373 -1  O  ASP C 368   N  GLY C 359           
SHEET    3  AA 4 VAL C 383  PHE C 387 -1  O  PHE C 387   N  VAL C 369           
SHEET    4  AA 4 GLN C 400  LEU C 402 -1  O  LEU C 402   N  VAL C 384           
SHEET    1  AB 2 ILE C 451  VAL C 452  0                                        
SHEET    2  AB 2 ALA C 585  LEU C 586  1  O  ALA C 585   N  VAL C 452           
SHEET    1  AC 3 SER C 455  ALA C 456  0                                        
SHEET    2  AC 3 CYS C 481  ASN C 489 -1  O  ASN C 489   N  SER C 455           
SHEET    3  AC 3 THR C 459  ILE C 460 -1  N  THR C 459   O  SER C 485           
SHEET    1  AD 4 SER C 455  ALA C 456  0                                        
SHEET    2  AD 4 CYS C 481  ASN C 489 -1  O  ASN C 489   N  SER C 455           
SHEET    3  AD 4 ASP C 542  LEU C 550 -1  O  MET C 546   N  LEU C 484           
SHEET    4  AD 4 ALA C 519  PHE C 521 -1  N  LEU C 520   O  TYR C 549           
SHEET    1  AE 4 THR C 528  ILE C 535  0                                        
SHEET    2  AE 4 ILE C 499  GLN C 506 -1  N  ILE C 499   O  ILE C 535           
SHEET    3  AE 4 ALA C 566  LEU C 571 -1  O  SER C 570   N  THR C 502           
SHEET    4  AE 4 ARG C 593  ILE C 594 -1  O  ILE C 594   N  LEU C 567           
SHEET    1  AF 2 TRP D  27  CYS D  28  0                                        
SHEET    2  AF 2 ILE D  60  GLU D  61 -1  O  GLU D  61   N  TRP D  27           
SHEET    1  AG 6 SER D  66  LYS D  71  0                                        
SHEET    2  AG 6 GLN D  98  ARG D 104 -1  O  VAL D 100   N  ASP D  68           
SHEET    3  AG 6 VAL D 434  ILE D 441  1  O  ILE D 437   N  LEU D 101           
SHEET    4  AG 6 ASP D 421  PRO D 427 -1  N  ASP D 421   O  LEU D 438           
SHEET    5  AG 6 VAL D 362  ASN D 366 -1  N  GLU D 365   O  ARG D 426           
SHEET    6  AG 6 LYS D 394  CYS D 395 -1  O  CYS D 395   N  VAL D 362           
SHEET    1  AH 5 ILE D  94  GLN D  95  0                                        
SHEET    2  AH 5 GLN D 109  LYS D 116 -1  O  LYS D 114   N  GLN D  95           
SHEET    3  AH 5 GLU D 403  THR D 411 -1  O  VAL D 404   N  PHE D 115           
SHEET    4  AH 5 THR D 374  TYR D 380 -1  N  THR D 374   O  THR D 411           
SHEET    5  AH 5 ASN D 386  GLY D 387 -1  O  GLY D 387   N  SER D 379           
SHEET    1  AI 6 TYR D 199  THR D 206  0                                        
SHEET    2  AI 6 PHE D 160  PHE D 167 -1  N  ILE D 162   O  THR D 206           
SHEET    3  AI 6 ILE D 123  ASP D 130  1  N  MET D 129   O  GLY D 165           
SHEET    4  AI 6 THR D 251  THR D 258  1  O  VAL D 255   N  TYR D 126           
SHEET    5  AI 6 ILE D 311  THR D 318  1  O  ILE D 314   N  LEU D 254           
SHEET    6  AI 6 SER D 335  LEU D 340  1  O  ALA D 336   N  PHE D 315           
SHEET    1  AJ 4 MET L   4  THR L   5  0                                        
SHEET    2  AJ 4 SER L  22  SER L  25 -1  O  ARG L  24   N  THR L   5           
SHEET    3  AJ 4 ALA L  75  ILE L  80 -1  O  PHE L  76   N  CYS L  23           
SHEET    4  AJ 4 PHE L  67  GLY L  71 -1  N  SER L  68   O  ARG L  79           
SHEET    1  AK 6 SER L  10  VAL L  13  0                                        
SHEET    2  AK 6 THR L 107  LEU L 111  1  O  LYS L 108   N  ILE L  11           
SHEET    3  AK 6 GLY L  89  GLN L  95 -1  N  TYR L  91   O  THR L 107           
SHEET    4  AK 6 LEU L  38  GLN L  43 -1  N  GLN L  43   O  ILE L  90           
SHEET    5  AK 6 ARG L  50  PHE L  54 -1  O  LEU L  52   N  TRP L  40           
SHEET    6  AK 6 ASN L  58  LEU L  59 -1  O  ASN L  58   N  PHE L  54           
SHEET    1  AL 4 SER L  10  VAL L  13  0                                        
SHEET    2  AL 4 THR L 107  LEU L 111  1  O  LYS L 108   N  ILE L  11           
SHEET    3  AL 4 GLY L  89  GLN L  95 -1  N  TYR L  91   O  THR L 107           
SHEET    4  AL 4 THR L 102  PHE L 103 -1  O  THR L 102   N  GLN L  95           
SHEET    1  AM 4 THR L 119  PHE L 123  0                                        
SHEET    2  AM 4 GLY L 134  PHE L 144 -1  O  VAL L 138   N  PHE L 123           
SHEET    3  AM 4 TYR L 178  THR L 187 -1  O  LEU L 186   N  ALA L 135           
SHEET    4  AM 4 VAL L 164  TRP L 168 -1  N  SER L 167   O  SER L 181           
SHEET    1  AN 4 SER L 158  GLU L 159  0                                        
SHEET    2  AN 4 ASN L 150  ILE L 155 -1  N  ILE L 155   O  SER L 158           
SHEET    3  AN 4 SER L 196  THR L 202 -1  O  THR L 198   N  LYS L 154           
SHEET    4  AN 4 ILE L 210  ASN L 215 -1  O  PHE L 214   N  TYR L 197           
SHEET    1  AO 4 HIS H   3  GLN H   6  0                                        
SHEET    2  AO 4 VAL H  18  THR H  25 -1  O  THR H  25   N  HIS H   3           
SHEET    3  AO 4 THR H  78  LEU H  83 -1  O  ALA H  79   N  CYS H  22           
SHEET    4  AO 4 ALA H  68  ASP H  73 -1  N  THR H  71   O  TYR H  80           
SHEET    1  AP 6 GLU H  10  MET H  12  0                                        
SHEET    2  AP 6 THR H 112  VAL H 116  1  O  THR H 115   N  GLU H  10           
SHEET    3  AP 6 ALA H  92  LEU H 100 -1  N  ALA H  92   O  VAL H 114           
SHEET    4  AP 6 TRP H  33  GLN H  39 -1  N  GLU H  35   O  SER H  97           
SHEET    5  AP 6 GLU H  46  ILE H  51 -1  O  GLU H  46   N  LYS H  38           
SHEET    6  AP 6 ILE H  58  TYR H  60 -1  O  HIS H  59   N  GLU H  50           
SHEET    1  AQ 4 GLU H  10  MET H  12  0                                        
SHEET    2  AQ 4 THR H 112  VAL H 116  1  O  THR H 115   N  GLU H  10           
SHEET    3  AQ 4 ALA H  92  LEU H 100 -1  N  ALA H  92   O  VAL H 114           
SHEET    4  AQ 4 TYR H 103  TRP H 108 -1  O  MET H 105   N  ARG H  98           
SHEET    1  AR 4 SER H 125  LEU H 129  0                                        
SHEET    2  AR 4 LEU H 143  TYR H 150 -1  O  LEU H 146   N  TYR H 127           
SHEET    3  AR 4 TYR H 180  VAL H 186 -1  O  TYR H 180   N  TYR H 150           
SHEET    4  AR 4 VAL H 168  THR H 170 -1  N  HIS H 169   O  SER H 185           
SHEET    1  AS 4 SER H 125  LEU H 129  0                                        
SHEET    2  AS 4 LEU H 143  TYR H 150 -1  O  LEU H 146   N  TYR H 127           
SHEET    3  AS 4 TYR H 180  VAL H 186 -1  O  TYR H 180   N  TYR H 150           
SHEET    4  AS 4 VAL H 174  LEU H 175 -1  N  VAL H 174   O  THR H 181           
SHEET    1  AT 3 THR H 156  TRP H 159  0                                        
SHEET    2  AT 3 THR H 199  HIS H 204 -1  O  ASN H 201   N  THR H 158           
SHEET    3  AT 3 THR H 209  LYS H 214 -1  O  THR H 209   N  HIS H 204           
SHEET    1  AU 4 MET E   4  THR E   5  0                                        
SHEET    2  AU 4 VAL E  19  SER E  25 -1  O  ARG E  24   N  THR E   5           
SHEET    3  AU 4 ALA E  75  ILE E  80 -1  O  PHE E  76   N  CYS E  23           
SHEET    4  AU 4 PHE E  67  GLY E  71 -1  N  SER E  68   O  ARG E  79           
SHEET    1  AV 6 SER E  10  VAL E  13  0                                        
SHEET    2  AV 6 THR E 107  LEU E 111  1  O  GLU E 110   N  VAL E  13           
SHEET    3  AV 6 GLY E  89  GLN E  95 -1  N  TYR E  91   O  THR E 107           
SHEET    4  AV 6 LEU E  38  GLN E  43 -1  N  PHE E  41   O  PHE E  92           
SHEET    5  AV 6 ARG E  50  PHE E  54 -1  O  LEU E  52   N  TRP E  40           
SHEET    6  AV 6 ASN E  58  LEU E  59 -1  O  ASN E  58   N  PHE E  54           
SHEET    1  AW 4 SER E  10  VAL E  13  0                                        
SHEET    2  AW 4 THR E 107  LEU E 111  1  O  GLU E 110   N  VAL E  13           
SHEET    3  AW 4 GLY E  89  GLN E  95 -1  N  TYR E  91   O  THR E 107           
SHEET    4  AW 4 THR E 102  PHE E 103 -1  O  THR E 102   N  GLN E  95           
SHEET    1  AX 4 THR E 119  PHE E 123  0                                        
SHEET    2  AX 4 GLY E 134  PHE E 144 -1  O  PHE E 140   N  SER E 121           
SHEET    3  AX 4 TYR E 178  THR E 187 -1  O  TYR E 178   N  PHE E 144           
SHEET    4  AX 4 VAL E 164  TRP E 168 -1  N  LEU E 165   O  THR E 183           
SHEET    1  AY 4 SER E 158  ARG E 160  0                                        
SHEET    2  AY 4 ILE E 149  ILE E 155 -1  N  ILE E 155   O  SER E 158           
SHEET    3  AY 4 SER E 196  HIS E 203 -1  O  GLU E 200   N  LYS E 152           
SHEET    4  AY 4 ILE E 210  ASN E 215 -1  O  PHE E 214   N  TYR E 197           
SHEET    1  AZ 4 HIS F   3  GLN F   6  0                                        
SHEET    2  AZ 4 SER F  17  THR F  25 -1  O  LYS F  23   N  GLN F   5           
SHEET    3  AZ 4 THR F  78  SER F  84 -1  O  LEU F  83   N  VAL F  18           
SHEET    4  AZ 4 ALA F  68  ASP F  73 -1  N  THR F  71   O  TYR F  80           
SHEET    1  BA 6 GLU F  10  MET F  12  0                                        
SHEET    2  BA 6 THR F 112  VAL F 116  1  O  SER F 113   N  GLU F  10           
SHEET    3  BA 6 ALA F  92  LEU F 100 -1  N  ALA F  92   O  VAL F 114           
SHEET    4  BA 6 TRP F  33  GLN F  39 -1  N  VAL F  37   O  TYR F  95           
SHEET    5  BA 6 LEU F  45  LEU F  52 -1  O  LEU F  48   N  TRP F  36           
SHEET    6  BA 6 TYR F  57  TYR F  60 -1  O  HIS F  59   N  GLU F  50           
SHEET    1  BB 4 GLU F  10  MET F  12  0                                        
SHEET    2  BB 4 THR F 112  VAL F 116  1  O  SER F 113   N  GLU F  10           
SHEET    3  BB 4 ALA F  92  LEU F 100 -1  N  ALA F  92   O  VAL F 114           
SHEET    4  BB 4 TYR F 103  TRP F 108 -1  O  MET F 105   N  ARG F  98           
SHEET    1  BC 4 SER F 125  LEU F 129  0                                        
SHEET    2  BC 4 MET F 140  TYR F 150 -1  O  LEU F 146   N  TYR F 127           
SHEET    3  BC 4 TYR F 180  PRO F 189 -1  O  TYR F 180   N  TYR F 150           
SHEET    4  BC 4 VAL F 168  THR F 170 -1  N  HIS F 169   O  SER F 185           
SHEET    1  BD 4 SER F 125  LEU F 129  0                                        
SHEET    2  BD 4 MET F 140  TYR F 150 -1  O  LEU F 146   N  TYR F 127           
SHEET    3  BD 4 TYR F 180  PRO F 189 -1  O  TYR F 180   N  TYR F 150           
SHEET    4  BD 4 VAL F 174  LEU F 175 -1  N  VAL F 174   O  THR F 181           
SHEET    1  BE 3 THR F 156  TRP F 159  0                                        
SHEET    2  BE 3 THR F 199  HIS F 204 -1  O  ASN F 201   N  THR F 158           
SHEET    3  BE 3 THR F 209  LYS F 214 -1  O  LYS F 213   N  CYS F 200           
SSBOND   1 CYS A   58    CYS A   67                          1555   1555  2.04  
SSBOND   2 CYS A  115    CYS A  135                          1555   1555  2.07  
SSBOND   3 CYS A  151    CYS A  164                          1555   1555  2.04  
SSBOND   4 CYS A  472    CYS A  481                          1555   1555  2.04  
SSBOND   5 CYS A  487    CYS A  543                          1555   1555  2.05  
SSBOND   6 CYS B    7    CYS B   25                          1555   1555  2.04  
SSBOND   7 CYS B   15    CYS B  444                          1555   1555  2.04  
SSBOND   8 CYS B   18    CYS B   44                          1555   1555  2.04  
SSBOND   9 CYS B   28    CYS B   55                          1555   1555  2.03  
SSBOND  10 CYS B  187    CYS B  193                          1555   1555  2.04  
SSBOND  11 CYS B  241    CYS B  281                          1555   1555  2.04  
SSBOND  12 CYS B  381    CYS B  395                          1555   1555  2.04  
SSBOND  13 CYS B  415    CYS B  442                          1555   1555  2.04  
SSBOND  14 CYS C   58    CYS C   67                          1555   1555  2.05  
SSBOND  15 CYS C  115    CYS C  135                          1555   1555  2.08  
SSBOND  16 CYS C  151    CYS C  164                          1555   1555  2.05  
SSBOND  17 CYS C  472    CYS C  481                          1555   1555  2.04  
SSBOND  18 CYS C  487    CYS C  543                          1555   1555  2.04  
SSBOND  19 CYS D    7    CYS D   25                          1555   1555  2.03  
SSBOND  20 CYS D   15    CYS D  444                          1555   1555  2.04  
SSBOND  21 CYS D   18    CYS D   44                          1555   1555  2.04  
SSBOND  22 CYS D   28    CYS D   55                          1555   1555  2.03  
SSBOND  23 CYS D  187    CYS D  193                          1555   1555  2.05  
SSBOND  24 CYS D  241    CYS D  281                          1555   1555  2.07  
SSBOND  25 CYS D  381    CYS D  395                          1555   1555  2.06  
SSBOND  26 CYS D  415    CYS D  442                          1555   1555  2.04  
SSBOND  27 CYS L   23    CYS L   93                          1555   1555  2.07  
SSBOND  28 CYS L  139    CYS L  199                          1555   1555  2.06  
SSBOND  29 CYS H   22    CYS H   96                          1555   1555  2.04  
SSBOND  30 CYS H  145    CYS H  200                          1555   1555  2.01  
SSBOND  31 CYS E   23    CYS E   93                          1555   1555  2.05  
SSBOND  32 CYS E  139    CYS E  199                          1555   1555  2.04  
SSBOND  33 CYS F   22    CYS F   96                          1555   1555  2.04  
SSBOND  34 CYS F  145    CYS F  200                          1555   1555  2.03  
LINK         ND2 ASN A 275                 C1  NAG A2009     1555   1555  1.43  
LINK         O6  BMA C2012                 C1  MAN C2014     1555   1555  1.43  
LINK         O4  NAG A2009                 C1  NAG A2010     1555   1555  1.43  
LINK         ND2 ASN C 275                 C1  NAG C2010     1555   1555  1.43  
LINK         O4  NAG C2010                 C1  NAG C2011     1555   1555  1.44  
LINK         ND2 ASN A 266                 C1  NAG A2008     1555   1555  1.44  
LINK         ND2 ASN B 249                 C1  NAG B2004     1555   1555  1.44  
LINK         O4  NAG A2010                 C1  BMA A2011     1555   1555  1.44  
LINK         ND2 ASN A 256                 C1  NAG A2007     1555   1555  1.44  
LINK         ND2 ASN B 386                 C1  NAG B2005     1555   1555  1.44  
LINK         ND2 ASN D 386                 C1  NAG D2004     1555   1555  1.44  
LINK         ND2 ASN A  43                 C1  NAG A2005     1555   1555  1.44  
LINK         ND2 ASN C  43                 C1  NAG C2005     1555   1555  1.44  
LINK         O3  BMA C2012                 C1  MAN C2013     1555   1555  1.44  
LINK         O3  BMA A2011                 C1  MAN A2012     1555   1555  1.44  
LINK         O4  NAG C2011                 C1  BMA C2012     1555   1555  1.44  
LINK         ND2 ASN C 568                 C1  NAG C2016     1555   1555  1.44  
LINK         ND2 ASN C 266                 C1  NAG C2009     1555   1555  1.44  
LINK         O3  MAN A2013                 C1  MAN A2014     1555   1555  1.44  
LINK         O4  NAG C2005                 C1  NAG C2006     1555   1555  1.44  
LINK         O6  BMA A2011                 C1  MAN A2013     1555   1555  1.45  
LINK         ND2 ASN A 568                 C1  NAG A2015     1555   1555  1.45  
LINK         ND2 ASN C 256                 C1  NAG C2008     1555   1555  1.45  
LINK         ND2 ASN A 141                 C1  NAG A2006     1555   1555  1.45  
LINK         O4  NAG B2005                 C1  NAG B2006     1555   1555  1.45  
LINK         ND2 ASN C 141                 C1  NAG C2007     1555   1555  1.45  
LINK         O3  MAN C2014                 C1  MAN C2015     1555   1555  1.45  
LINK         OE1 GLU B 229                MG    MG B2003     1555   1555  1.92  
LINK         OE1 GLU D 229                MG    MG D2003     1555   1555  1.92  
LINK         OG  SER B 132                MG    MG B2003     1555   1555  2.08  
LINK         OG  SER D 132                MG    MG D2003     1555   1555  2.08  
LINK         O   TYR A 430                CA    CA A2004     1555   1555  2.22  
LINK         O   TYR A 366                CA    CA A2003     1555   1555  2.31  
LINK         O   TYR C 430                CA    CA C2004     1555   1555  2.31  
LINK         OD2 ASP A 364                CA    CA A2003     1555   1555  2.31  
LINK         OD1 ASP A 426                CA    CA A2004     1555   1555  2.31  
LINK         O   TYR C 366                CA    CA C2003     1555   1555  2.31  
LINK         O   PRO D 228                CA    CA D2002     1555   1555  2.31  
LINK         OD1 ASN D 224                CA    CA D2002     1555   1555  2.31  
LINK         OD1 ASN B 224                CA    CA B2002     1555   1555  2.32  
LINK         OD1 ASP C 362                CA    CA C2003     1555   1555  2.32  
LINK         OE1 GLU B 169                CA    CA B2002     1555   1555  2.32  
LINK         OD1 ASP A 362                CA    CA A2003     1555   1555  2.32  
LINK         OG  SER A 241                CA    CA A2001     1555   1555  2.32  
LINK         OG  SER C 241                CA    CA C2001     1555   1555  2.32  
LINK         OE1 GLU D 169                CA    CA D2002     1555   1555  2.32  
LINK         OD2 ASP A 368                CA    CA A2003     1555   1555  2.32  
LINK         OD1 ASN C 295                CA    CA C2002     1555   1555  2.32  
LINK         O   PRO B 228                CA    CA B2002     1555   1555  2.32  
LINK         OD1 ASP A 297                CA    CA A2002     1555   1555  2.32  
LINK         OD1 ASN A 295                CA    CA A2002     1555   1555  2.32  
LINK         O   THR A 245                CA    CA A2001     1555   1555  2.32  
LINK         OD2 ASP C 364                CA    CA C2003     1555   1555  2.32  
LINK         OD1 ASP A 243                CA    CA A2001     1555   1555  2.32  
LINK         OD2 ASP C 368                CA    CA C2003     1555   1555  2.32  
LINK         OD1 ASP C 426                CA    CA C2004     1555   1555  2.32  
LINK         OD1 ASP A 424                CA    CA A2004     1555   1555  2.32  
LINK         O   THR C 245                CA    CA C2001     1555   1555  2.32  
LINK         O   LEU C 299                CA    CA C2002     1555   1555  2.32  
LINK         OD1 ASP B 138                CA    CA B2001     1555   1555  2.32  
LINK         OD1 ASN C 428                CA    CA C2004     1555   1555  2.32  
LINK         OD2 ASP C 293                CA    CA C2002     1555   1555  2.32  
LINK         OD2 ASP C 360                CA    CA C2003     1555   1555  2.32  
LINK         OD2 ASP A 432                CA    CA A2004     1555   1555  2.32  
LINK         OD1 ASP C 301                CA    CA C2002     1555   1555  2.32  
LINK         O   ASP D 226                CA    CA D2002     1555   1555  2.33  
LINK         O   ASP B 226                CA    CA B2002     1555   1555  2.33  
LINK         OD1 ASP C 243                CA    CA C2001     1555   1555  2.33  
LINK         OD2 ASP B 137                CA    CA B2001     1555   1555  2.33  
LINK         OD1 ASP D 137                CA    CA D2001     1555   1555  2.33  
LINK         OD2 ASP A 293                CA    CA A2002     1555   1555  2.33  
LINK         OE2 GLU B 229                CA    CA B2002     1555   1555  2.33  
LINK         O   LEU A 299                CA    CA A2002     1555   1555  2.33  
LINK         OD2 ASP A 247                CA    CA A2001     1555   1555  2.33  
LINK         OE2 GLU C 239                CA    CA C2001     1555   1555  2.33  
LINK         OE2 GLU A 239                CA    CA A2001     1555   1555  2.33  
LINK         OD2 ASP A 360                CA    CA A2003     1555   1555  2.33  
LINK         OD1 ASP C 297                CA    CA C2002     1555   1555  2.33  
LINK         OD1 ASP D 226                CA    CA D2002     1555   1555  2.33  
LINK         OE2 GLU D 229                CA    CA D2002     1555   1555  2.33  
LINK         OD2 ASP C 247                CA    CA C2001     1555   1555  2.33  
LINK         O   SER B 134                CA    CA B2001     1555   1555  2.33  
LINK         OD1 ASP A 301                CA    CA A2002     1555   1555  2.33  
LINK         OD1 ASN A 428                CA    CA A2004     1555   1555  2.33  
LINK         O   ALA B 342                CA    CA B2001     1555   1555  2.33  
LINK         OD1 ASP D 138                CA    CA D2001     1555   1555  2.33  
LINK         O   ALA D 342                CA    CA D2001     1555   1555  2.33  
LINK         OD2 ASP C 432                CA    CA C2004     1555   1555  2.33  
LINK         O   SER D 134                CA    CA D2001     1555   1555  2.33  
LINK         OD2 ASP D 137                CA    CA D2001     1555   1555  2.33  
LINK         OD1 ASP B 137                CA    CA B2001     1555   1555  2.34  
LINK         OD1 ASP B 226                CA    CA B2002     1555   1555  2.34  
LINK         OD1 ASP C 424                CA    CA C2004     1555   1555  2.34  
LINK         OD1 ASP C 368                CA    CA C2003     1555   1555  2.64  
LINK         OE1 GLU C 239                CA    CA C2001     1555   1555  2.74  
LINK         OD2 ASP C 301                CA    CA C2002     1555   1555  2.74  
LINK         OD1 ASP A 247                CA    CA A2001     1555   1555  2.84  
LINK         OD1 ASP A 368                CA    CA A2003     1555   1555  2.89  
LINK         OD1 ASP C 247                CA    CA C2001     1555   1555  2.92  
LINK         OD1 ASP A 432                CA    CA A2004     1555   1555  2.92  
LINK         OD1 ASP C 432                CA    CA C2004     1555   1555  2.96  
LINK         OD2 ASP A 301                CA    CA A2002     1555   1555  2.99  
LINK         OE1 GLU A 239                CA    CA A2001     1555   1555  3.12  
CISPEP   1 GLN B   95    PRO B   96          0         1.65                     
CISPEP   2 MET B  173    PRO B  174          0         2.77                     
CISPEP   3 GLN D   95    PRO D   96          0        -8.89                     
CISPEP   4 MET D  173    PRO D  174          0         7.52                     
CISPEP   5 TYR L   99    PRO L  100          0        -6.14                     
CISPEP   6 TYR L  145    PRO L  146          0         2.83                     
CISPEP   7 PHE H  151    PRO H  152          0        -5.43                     
CISPEP   8 GLU H  153    PRO H  154          0         1.01                     
CISPEP   9 TRP H  193    PRO H  194          0         6.78                     
CISPEP  10 TYR E   99    PRO E  100          0        -1.74                     
CISPEP  11 TYR E  145    PRO E  146          0         2.72                     
CISPEP  12 PHE F  151    PRO F  152          0        -3.37                     
CISPEP  13 GLU F  153    PRO F  154          0        12.99                     
CISPEP  14 TRP F  193    PRO F  194          0         3.97                     
SITE     1 AC1  5 GLU A 239  SER A 241  ASP A 243  THR A 245                    
SITE     2 AC1  5 ASP A 247                                                     
SITE     1 AC2  5 ASP A 293  ASN A 295  ASP A 297  LEU A 299                    
SITE     2 AC2  5 ASP A 301                                                     
SITE     1 AC3  5 ASP A 360  ASP A 362  ASP A 364  TYR A 366                    
SITE     2 AC3  5 ASP A 368                                                     
SITE     1 AC4  5 ASP A 424  ASP A 426  ASN A 428  TYR A 430                    
SITE     2 AC4  5 ASP A 432                                                     
SITE     1 AC5  5 PRO A  15  GLY A  16  LYS A  41  ASN A  43                    
SITE     2 AC5  5 GLN A  51                                                     
SITE     1 AC6  2 PRO A  28  ASN A 141                                          
SITE     1 AC7  2 ASN A 256  SER A 277                                          
SITE     1 AC8  4 SER A 241  ASN A 266  SER A 268  ASP A 269                    
SITE     1 AC9  5 TYR A 261  SER A 272  LEU A 273  ASN A 275                    
SITE     2 AC9  5 NAG A2010                                                     
SITE     1 BC1  4 ALA A 222  TYR A 226  NAG A2009  BMA A2011                    
SITE     1 BC2  3 NAG A2010  MAN A2012  MAN A2013                               
SITE     1 BC3  1 BMA A2011                                                     
SITE     1 BC4  2 BMA A2011  MAN A2014                                          
SITE     1 BC5  4 GLN A 221  ALA A 222  SER A 223  MAN A2013                    
SITE     1 BC6  5 THR A 502  GLU A 504  ASN A 568  PHE A 569                    
SITE     2 BC6  5 SER A 570                                                     
SITE     1 BC7  4 SER B 134  ASP B 137  ASP B 138  ALA B 342                    
SITE     1 BC8  6 GLU B 169  ASN B 224  ASP B 226  SER B 227                    
SITE     2 BC8  6 PRO B 228  GLU B 229                                          
SITE     1 BC9  2 SER B 132  GLU B 229                                          
SITE     1 CC1  1 ASN B 249                                                     
SITE     1 CC2  4 TYR B 380  GLY B 384  ASN B 386  NAG B2006                    
SITE     1 CC3  1 NAG B2005                                                     
SITE     1 CC4  5 GLU C 239  SER C 241  ASP C 243  THR C 245                    
SITE     2 CC4  5 ASP C 247                                                     
SITE     1 CC5  5 ASP C 293  ASN C 295  ASP C 297  LEU C 299                    
SITE     2 CC5  5 ASP C 301                                                     
SITE     1 CC6  5 ASP C 360  ASP C 362  ASP C 364  TYR C 366                    
SITE     2 CC6  5 ASP C 368                                                     
SITE     1 CC7  5 ASP C 424  ASP C 426  ASN C 428  TYR C 430                    
SITE     2 CC7  5 ASP C 432                                                     
SITE     1 CC8  5 GLY C  16  LYS C  41  ASN C  43  GLN C  51                    
SITE     2 CC8  5 NAG C2006                                                     
SITE     1 CC9  1 NAG C2005                                                     
SITE     1 DC1  3 ASP C  31  ASN C 141  PHE C 142                               
SITE     1 DC2  3 ASN C 256  TYR C 259  SER C 277                               
SITE     1 DC3  4 ASN C 266  SER C 268  ASP C 269  LEU C 273                    
SITE     1 DC4  6 TYR C 226  TYR C 261  SER C 272  LEU C 273                    
SITE     2 DC4  6 ASN C 275  NAG C2011                                          
SITE     1 DC5  4 ALA C 222  TYR C 226  NAG C2010  BMA C2012                    
SITE     1 DC6  3 NAG C2011  MAN C2013  MAN C2014                               
SITE     1 DC7  1 BMA C2012                                                     
SITE     1 DC8  4 ARG C 220  GLN C 221  BMA C2012  MAN C2015                    
SITE     1 DC9  3 ALA C 222  SER C 223  MAN C2014                               
SITE     1 EC1  5 GLU C 504  ASN C 568  PHE C 569  SER C 570                    
SITE     2 EC1  5 ARG C 593                                                     
SITE     1 EC2  4 SER D 134  ASP D 137  ASP D 138  ALA D 342                    
SITE     1 EC3  5 GLU D 169  ASN D 224  ASP D 226  PRO D 228                    
SITE     2 EC3  5 GLU D 229                                                     
SITE     1 EC4  2 SER D 132  GLU D 229                                          
SITE     1 EC5  3 TYR D 380  GLY D 384  ASN D 386                               
CRYST1   92.956  102.805  125.079  76.10  70.19  71.28 P 1           2          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.010758 -0.003645 -0.003374        0.00000                         
SCALE2      0.000000  0.010270 -0.001532        0.00000                         
SCALE3      0.000000  0.000000  0.008592        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system