GenomeNet

Database: PDB
Entry: 1M1X
LinkDB: 1M1X
Original site: 1M1X 
HEADER    CELL ADHESION                           20-JUN-02   1M1X              
TITLE     CRYSTAL STRUCTURE OF THE EXTRACELLULAR SEGMENT OF INTEGRIN ALPHA      
TITLE    2 VBETA3 BOUND TO MN2+                                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: INTEGRIN ALPHA-V;                                          
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: RESIDUES 31-987;                                           
COMPND   5 SYNONYM: VITRONECTIN RECEPTOR ALPHA SUBUNIT, CD51 ANTIGEN;           
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: INTEGRIN BETA-3;                                           
COMPND   9 CHAIN: B;                                                            
COMPND  10 FRAGMENT: RESIDUES 27-718;                                           
COMPND  11 SYNONYM: PLATELET MEMBRANE GLYCOPROTEIN IIIA, GPIIIA, CD61 ANTIGEN;  
COMPND  12 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 CELL_LINE: SF9;                                                      
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  12 ORGANISM_COMMON: HUMAN;                                              
SOURCE  13 ORGANISM_TAXID: 9606;                                                
SOURCE  14 CELL_LINE: SF9;                                                      
SOURCE  15 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE  16 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE  18 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS                           
KEYWDS    GENU, HYBRID DOMAIN, BETA-TAIL DOMAIN, PSI DOMAIN, EGF DOMAIN, MIDAS, 
KEYWDS   2 ADMIDAS, CAGE MOTIF, PROPELLER, A-DOMAIN, THIGH DOMAIN, CALF DOMAIN, 
KEYWDS   3 CELL ADHESION                                                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.-P.XIONG,T.STEHLE,R.ZHANG,A.JOACHIMIAK,M.FRECH,S.L.GOODMAN,         
AUTHOR   2 M.A.ARNAOUT                                                          
REVDAT   4   13-JUL-11 1M1X    1       VERSN                                    
REVDAT   3   24-FEB-09 1M1X    1       VERSN                                    
REVDAT   2   01-APR-03 1M1X    1       JRNL                                     
REVDAT   1   14-AUG-02 1M1X    0                                                
JRNL        AUTH   J.P.XIONG,T.STEHLE,R.ZHANG,A.JOACHIMIAK,M.FRECH,S.L.GOODMAN, 
JRNL        AUTH 2 M.A.ARNAOUT                                                  
JRNL        TITL   CRYSTAL STRUCTURE OF THE EXTRACELLULAR SEGMENT OF INTEGRIN   
JRNL        TITL 2 ALPHA VBETA3 IN COMPLEX WITH AN ARG-GLY-ASP LIGAND.          
JRNL        REF    SCIENCE                       V. 296   151 2002              
JRNL        REFN                   ISSN 0036-8075                               
JRNL        PMID   11884718                                                     
JRNL        DOI    10.1126/SCIENCE.1069040                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR 3.851                                         
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 43401                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : SAME AS IN WILD TYPE            
REMARK   3                                      STRUCTURE, PDB ENTRY 1JV2       
REMARK   3   R VALUE            (WORKING SET) : 0.244                           
REMARK   3   FREE R VALUE                     : 0.323                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 2125                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 11398                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 258                                     
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) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.010                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.69                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1M1X COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 31-JUL-02.                  
REMARK 100 THE RCSB ID CODE IS RCSB016496.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 24-JUN-01                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 19-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0332                             
REMARK 200  MONOCHROMATOR                  : UNDULATOR                          
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : CUSTOM-MADE                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 44739                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.4                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.40                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 86.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS            
REMARK 200 SOFTWARE USED: X-PLOR                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 70.51                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.17                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG, MES, MN, PH 6.0, VAPOR DIFFUSION,   
REMARK 280  HANGING DROP, TEMPERATURE 278K                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+1/3                                           
REMARK 290       6555   -X,-X+Y,-Z+2/3                                          
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      206.86667            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      103.43333            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000      103.43333            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000      206.86667            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 11420 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 64840 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 8.0 KCAL/MOL                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLN A   839                                                      
REMARK 465     THR A   840                                                      
REMARK 465     THR A   841                                                      
REMARK 465     GLU A   842                                                      
REMARK 465     LYS A   843                                                      
REMARK 465     ASN A   844                                                      
REMARK 465     ASP A   845                                                      
REMARK 465     THR A   846                                                      
REMARK 465     VAL A   847                                                      
REMARK 465     ALA A   848                                                      
REMARK 465     GLY A   849                                                      
REMARK 465     GLN A   850                                                      
REMARK 465     GLY A   851                                                      
REMARK 465     GLU A   852                                                      
REMARK 465     ARG A   853                                                      
REMARK 465     ASP A   854                                                      
REMARK 465     HIS A   855                                                      
REMARK 465     LEU A   856                                                      
REMARK 465     ILE A   857                                                      
REMARK 465     THR A   858                                                      
REMARK 465     LYS A   859                                                      
REMARK 465     ARG A   860                                                      
REMARK 465     ASP A   861                                                      
REMARK 465     LEU A   862                                                      
REMARK 465     ALA A   863                                                      
REMARK 465     LEU A   864                                                      
REMARK 465     SER A   865                                                      
REMARK 465     GLU A   866                                                      
REMARK 465     GLY A   867                                                      
REMARK 465     PRO A   957                                                      
REMARK 465     GLY B     1                                                      
REMARK 465     PRO B     2                                                      
REMARK 465     ASN B     3                                                      
REMARK 465     ILE B     4                                                      
REMARK 465     CYS B     5                                                      
REMARK 465     THR B     6                                                      
REMARK 465     THR B     7                                                      
REMARK 465     ARG B     8                                                      
REMARK 465     GLY B     9                                                      
REMARK 465     VAL B    10                                                      
REMARK 465     SER B    11                                                      
REMARK 465     SER B    12                                                      
REMARK 465     CYS B    13                                                      
REMARK 465     GLN B    14                                                      
REMARK 465     GLN B    15                                                      
REMARK 465     CYS B    16                                                      
REMARK 465     LEU B    17                                                      
REMARK 465     ALA B    18                                                      
REMARK 465     VAL B    19                                                      
REMARK 465     SER B    20                                                      
REMARK 465     PRO B    21                                                      
REMARK 465     MET B    22                                                      
REMARK 465     CYS B    23                                                      
REMARK 465     ALA B    24                                                      
REMARK 465     TRP B    25                                                      
REMARK 465     CYS B    26                                                      
REMARK 465     SER B    27                                                      
REMARK 465     ASP B    28                                                      
REMARK 465     GLU B    29                                                      
REMARK 465     ALA B    30                                                      
REMARK 465     LEU B    31                                                      
REMARK 465     PRO B    32                                                      
REMARK 465     LEU B    33                                                      
REMARK 465     GLY B    34                                                      
REMARK 465     SER B    35                                                      
REMARK 465     PRO B    36                                                      
REMARK 465     ARG B    37                                                      
REMARK 465     CYS B    38                                                      
REMARK 465     ASP B    39                                                      
REMARK 465     LEU B    40                                                      
REMARK 465     LYS B    41                                                      
REMARK 465     GLU B    42                                                      
REMARK 465     ASN B    43                                                      
REMARK 465     LEU B    44                                                      
REMARK 465     LEU B    45                                                      
REMARK 465     LYS B    46                                                      
REMARK 465     ASP B    47                                                      
REMARK 465     ASN B    48                                                      
REMARK 465     CYS B    49                                                      
REMARK 465     ALA B    50                                                      
REMARK 465     PRO B    51                                                      
REMARK 465     GLU B    52                                                      
REMARK 465     SER B    53                                                      
REMARK 465     ILE B    54                                                      
REMARK 465     CYS B   435                                                      
REMARK 465     ALA B   436                                                      
REMARK 465     CYS B   437                                                      
REMARK 465     GLN B   438                                                      
REMARK 465     ALA B   439                                                      
REMARK 465     GLN B   440                                                      
REMARK 465     ALA B   441                                                      
REMARK 465     GLU B   442                                                      
REMARK 465     PRO B   443                                                      
REMARK 465     ASN B   444                                                      
REMARK 465     SER B   445                                                      
REMARK 465     HIS B   446                                                      
REMARK 465     ARG B   447                                                      
REMARK 465     CYS B   448                                                      
REMARK 465     ASN B   449                                                      
REMARK 465     ASN B   450                                                      
REMARK 465     GLY B   451                                                      
REMARK 465     ASN B   452                                                      
REMARK 465     GLY B   453                                                      
REMARK 465     THR B   454                                                      
REMARK 465     PHE B   455                                                      
REMARK 465     GLU B   456                                                      
REMARK 465     CYS B   457                                                      
REMARK 465     GLY B   458                                                      
REMARK 465     VAL B   459                                                      
REMARK 465     CYS B   460                                                      
REMARK 465     ARG B   461                                                      
REMARK 465     CYS B   462                                                      
REMARK 465     GLY B   463                                                      
REMARK 465     PRO B   464                                                      
REMARK 465     GLY B   465                                                      
REMARK 465     TRP B   466                                                      
REMARK 465     LEU B   467                                                      
REMARK 465     GLY B   468                                                      
REMARK 465     SER B   469                                                      
REMARK 465     GLN B   470                                                      
REMARK 465     CYS B   471                                                      
REMARK 465     GLU B   472                                                      
REMARK 465     CYS B   473                                                      
REMARK 465     SER B   474                                                      
REMARK 465     GLU B   475                                                      
REMARK 465     GLU B   476                                                      
REMARK 465     ASP B   477                                                      
REMARK 465     TYR B   478                                                      
REMARK 465     ARG B   479                                                      
REMARK 465     PRO B   480                                                      
REMARK 465     SER B   481                                                      
REMARK 465     GLN B   482                                                      
REMARK 465     GLN B   483                                                      
REMARK 465     ASP B   484                                                      
REMARK 465     GLU B   485                                                      
REMARK 465     CYS B   486                                                      
REMARK 465     SER B   487                                                      
REMARK 465     PRO B   488                                                      
REMARK 465     ARG B   489                                                      
REMARK 465     GLU B   490                                                      
REMARK 465     GLY B   491                                                      
REMARK 465     GLN B   492                                                      
REMARK 465     PRO B   493                                                      
REMARK 465     VAL B   494                                                      
REMARK 465     CYS B   495                                                      
REMARK 465     SER B   496                                                      
REMARK 465     GLN B   497                                                      
REMARK 465     ARG B   498                                                      
REMARK 465     GLY B   499                                                      
REMARK 465     GLU B   500                                                      
REMARK 465     CYS B   501                                                      
REMARK 465     LEU B   502                                                      
REMARK 465     CYS B   503                                                      
REMARK 465     GLY B   504                                                      
REMARK 465     GLN B   505                                                      
REMARK 465     CYS B   506                                                      
REMARK 465     VAL B   507                                                      
REMARK 465     CYS B   508                                                      
REMARK 465     HIS B   509                                                      
REMARK 465     SER B   510                                                      
REMARK 465     SER B   511                                                      
REMARK 465     ASP B   512                                                      
REMARK 465     PHE B   513                                                      
REMARK 465     GLY B   514                                                      
REMARK 465     LYS B   515                                                      
REMARK 465     ILE B   516                                                      
REMARK 465     THR B   517                                                      
REMARK 465     GLY B   518                                                      
REMARK 465     LYS B   519                                                      
REMARK 465     TYR B   520                                                      
REMARK 465     CYS B   521                                                      
REMARK 465     GLU B   522                                                      
REMARK 465     CYS B   523                                                      
REMARK 465     ASP B   524                                                      
REMARK 465     ASP B   525                                                      
REMARK 465     PHE B   526                                                      
REMARK 465     SER B   527                                                      
REMARK 465     CYS B   528                                                      
REMARK 465     VAL B   529                                                      
REMARK 465     ARG B   530                                                      
REMARK 465     TYR B   531                                                      
REMARK 465     PRO B   691                                                      
REMARK 465     ASP B   692                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    PRO A 363   C   -  N   -  CA  ANGL. DEV. =   9.8 DEGREES          
REMARK 500    PRO A 451   C   -  N   -  CA  ANGL. DEV. = -10.3 DEGREES          
REMARK 500    PRO A 451   C   -  N   -  CD  ANGL. DEV. =  13.1 DEGREES          
REMARK 500    PRO A 750   C   -  N   -  CA  ANGL. DEV. =  -9.5 DEGREES          
REMARK 500    LEU A 880   N   -  CA  -  C   ANGL. DEV. = -17.2 DEGREES          
REMARK 500    GLU A 912   N   -  CA  -  C   ANGL. DEV. =  21.9 DEGREES          
REMARK 500    PRO B 170   C   -  N   -  CA  ANGL. DEV. =  -9.4 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    GLU A  15      101.83    -58.65                                   
REMARK 500    SER A  62       43.85    -62.63                                   
REMARK 500    SER A  63       29.81     43.61                                   
REMARK 500    PRO A  69     -165.60    -40.43                                   
REMARK 500    GLU A  71       83.66    -66.84                                   
REMARK 500    LYS A  82      -91.27    -50.65                                   
REMARK 500    ASP A  83       51.58   -100.72                                   
REMARK 500    LYS A 101     -120.14   -137.92                                   
REMARK 500    ASP A 103      -24.68     76.09                                   
REMARK 500    PRO A 110       -1.34    -57.00                                   
REMARK 500    MET A 118      -65.54    -90.40                                   
REMARK 500    ARG A 122       68.37   -152.91                                   
REMARK 500    ASP A 132       80.83   -158.72                                   
REMARK 500    ILE A 147     -163.55   -122.72                                   
REMARK 500    ASP A 148      175.28     64.84                                   
REMARK 500    ASP A 162      146.18   -179.26                                   
REMARK 500    ALA A 166       23.00    -79.85                                   
REMARK 500    ASP A 167       79.32     48.67                                   
REMARK 500    PHE A 177     -135.82     66.63                                   
REMARK 500    TRP A 179       25.83     43.48                                   
REMARK 500    ALA A 189      -26.66     69.11                                   
REMARK 500    LYS A 194      -11.57   -176.15                                   
REMARK 500    PRO A 197       -7.03    -57.96                                   
REMARK 500    SER A 201      -74.38   -166.63                                   
REMARK 500    ILE A 202      110.42     55.06                                   
REMARK 500    VAL A 243       75.36   -110.12                                   
REMARK 500    ALA A 247     -123.28     59.46                                   
REMARK 500    ARG A 248       62.45   -119.23                                   
REMARK 500    LYS A 259      -41.99   -130.55                                   
REMARK 500    MET A 261       25.47     81.19                                   
REMARK 500    LEU A 264      -76.00    -90.55                                   
REMARK 500    PHE A 276       94.32    -62.48                                   
REMARK 500    ASN A 286       46.41   -142.58                                   
REMARK 500    ASP A 288       20.33   -142.02                                   
REMARK 500    ASP A 289       70.22     36.22                                   
REMARK 500    PRO A 298      -16.80    -49.60                                   
REMARK 500    GLN A 327       72.69   -118.21                                   
REMARK 500    THR A 329     -169.80   -112.15                                   
REMARK 500    PHE A 337      -23.22     85.96                                   
REMARK 500    PHE A 340      -59.81   -121.45                                   
REMARK 500    ALA A 343      101.55   -164.44                                   
REMARK 500    ASP A 349       66.07   -158.51                                   
REMARK 500    LEU A 350      -60.96    -27.68                                   
REMARK 500    GLN A 352       85.83     63.19                                   
REMARK 500    ASP A 353       14.55   -140.37                                   
REMARK 500    ILE A 358      145.06   -172.34                                   
REMARK 500    ASN A 384       98.90    -68.35                                   
REMARK 500    ALA A 385       -4.09    -55.19                                   
REMARK 500    GLN A 389      154.25    178.33                                   
REMARK 500    SER A 399       -7.50   -147.00                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     218 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    TYR B 625         0.07    SIDE CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    THR A 460        24.6      L          L   OUTSIDE RANGE           
REMARK 500    GLU A 598        21.1      L          L   OUTSIDE RANGE           
REMARK 500    ASP A 611        24.8      L          L   OUTSIDE RANGE           
REMARK 500    GLN A 703        22.2      L          L   OUTSIDE RANGE           
REMARK 500    GLU A 912        19.6      L          L   OUTSIDE RANGE           
REMARK 500    SER B 162        23.4      L          L   OUTSIDE RANGE           
REMARK 500    ASN B 377        24.2      L          L   OUTSIDE RANGE           
REMARK 500    CYS B 544        24.6      L          L   OUTSIDE RANGE           
REMARK 500    GLN B 590        23.5      L          L   OUTSIDE RANGE           
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                              MN A4004  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 238   OD1                                                    
REMARK 620 2 ILE A 236   O    69.0                                              
REMARK 620 3 ASP A 230   OD2  94.9  85.6                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN A4005  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN A 286   ND2                                                    
REMARK 620 2 ASP A 288   OD2  63.9                                              
REMARK 620 3 TYR A 290   O   130.3 128.1                                        
REMARK 620 4 ASP A 284   OD2  77.6  66.9  69.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN A4006  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 357   OD1                                                    
REMARK 620 2 ASP A 353   OD2 132.1                                              
REMARK 620 3 PHE A 355   O    77.6  82.3                                        
REMARK 620 4 ASP A 351   OD2  81.8  65.3 110.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN A4007  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 TYR A 419   O                                                      
REMARK 620 2 ASP A 421   OD1  94.8                                              
REMARK 620 3 ASP A 415   OD2 133.8 111.7                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN A4008  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 636   OE2                                                    
REMARK 620 2 VAL A 601   O    93.0                                              
REMARK 620 3 ASP A 599   OD1 115.7 113.0                                        
REMARK 620 4 ASP A 599   OD2 116.0  63.8  49.2                                  
REMARK 620 5 GLU A 636   OE1  49.5  93.0 151.9 153.8                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN B4002  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 127   OD1                                                    
REMARK 620 2 SER B 123   O   103.2                                              
REMARK 620 N                    1                                               
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 2044                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 2045                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 2260                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 2266                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 2267                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 2458                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 2585                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 2586                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 2943                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NDG A 2944                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 2950                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 2951                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 3320                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 3371                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 3559                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NDG B 3560                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 3654                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NDG B 3655                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN B 4002                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 4004                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 4005                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 4006                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 4007                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 4008                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1JV2   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE EXTRACELLULAR SEGMENT OF INTEGRIN           
REMARK 900 ALPHAVBETA3                                                          
REMARK 900 RELATED ID: 1M1U   RELATED DB: PDB                                   
REMARK 900 AN ISOLEUCINE-BASED ALLOSTERIC SWITCH CONTROLS AFFINITY AND          
REMARK 900 SHAPE SHIFTING IN INTEGRIN CD11B A-DOMAIN                            
DBREF  1M1X A    1   957  GB     14743192 XP_002379       31    987             
DBREF  1M1X B    1   692  UNP    P05106   ITB3_HUMAN      27    718             
SEQRES   1 A  957  PHE ASN LEU ASP VAL ASP SER PRO ALA GLU TYR SER GLY          
SEQRES   2 A  957  PRO GLU GLY SER TYR PHE GLY PHE ALA VAL ASP PHE PHE          
SEQRES   3 A  957  VAL PRO SER ALA SER SER ARG MET PHE LEU LEU VAL GLY          
SEQRES   4 A  957  ALA PRO LYS ALA ASN THR THR GLN PRO GLY ILE VAL GLU          
SEQRES   5 A  957  GLY GLY GLN VAL LEU LYS CYS ASP TRP SER SER THR ARG          
SEQRES   6 A  957  ARG CYS GLN PRO ILE GLU PHE ASP ALA THR GLY ASN ARG          
SEQRES   7 A  957  ASP TYR ALA LYS ASP ASP PRO LEU GLU PHE LYS SER HIS          
SEQRES   8 A  957  GLN TRP PHE GLY ALA SER VAL ARG SER LYS GLN ASP LYS          
SEQRES   9 A  957  ILE LEU ALA CYS ALA PRO LEU TYR HIS TRP ARG THR GLU          
SEQRES  10 A  957  MET LYS GLN GLU ARG GLU PRO VAL GLY THR CYS PHE LEU          
SEQRES  11 A  957  GLN ASP GLY THR LYS THR VAL GLU TYR ALA PRO CYS ARG          
SEQRES  12 A  957  SER GLN ASP ILE ASP ALA ASP GLY GLN GLY PHE CYS GLN          
SEQRES  13 A  957  GLY GLY PHE SER ILE ASP PHE THR LYS ALA ASP ARG VAL          
SEQRES  14 A  957  LEU LEU GLY GLY PRO GLY SER PHE TYR TRP GLN GLY GLN          
SEQRES  15 A  957  LEU ILE SER ASP GLN VAL ALA GLU ILE VAL SER LYS TYR          
SEQRES  16 A  957  ASP PRO ASN VAL TYR SER ILE LYS TYR ASN ASN GLN LEU          
SEQRES  17 A  957  ALA THR ARG THR ALA GLN ALA ILE PHE ASP ASP SER TYR          
SEQRES  18 A  957  LEU GLY TYR SER VAL ALA VAL GLY ASP PHE ASN GLY ASP          
SEQRES  19 A  957  GLY ILE ASP ASP PHE VAL SER GLY VAL PRO ARG ALA ALA          
SEQRES  20 A  957  ARG THR LEU GLY MET VAL TYR ILE TYR ASP GLY LYS ASN          
SEQRES  21 A  957  MET SER SER LEU TYR ASN PHE THR GLY GLU GLN MET ALA          
SEQRES  22 A  957  ALA TYR PHE GLY PHE SER VAL ALA ALA THR ASP ILE ASN          
SEQRES  23 A  957  GLY ASP ASP TYR ALA ASP VAL PHE ILE GLY ALA PRO LEU          
SEQRES  24 A  957  PHE MET ASP ARG GLY SER ASP GLY LYS LEU GLN GLU VAL          
SEQRES  25 A  957  GLY GLN VAL SER VAL SER LEU GLN ARG ALA SER GLY ASP          
SEQRES  26 A  957  PHE GLN THR THR LYS LEU ASN GLY PHE GLU VAL PHE ALA          
SEQRES  27 A  957  ARG PHE GLY SER ALA ILE ALA PRO LEU GLY ASP LEU ASP          
SEQRES  28 A  957  GLN ASP GLY PHE ASN ASP ILE ALA ILE ALA ALA PRO TYR          
SEQRES  29 A  957  GLY GLY GLU ASP LYS LYS GLY ILE VAL TYR ILE PHE ASN          
SEQRES  30 A  957  GLY ARG SER THR GLY LEU ASN ALA VAL PRO SER GLN ILE          
SEQRES  31 A  957  LEU GLU GLY GLN TRP ALA ALA ARG SER MET PRO PRO SER          
SEQRES  32 A  957  PHE GLY TYR SER MET LYS GLY ALA THR ASP ILE ASP LYS          
SEQRES  33 A  957  ASN GLY TYR PRO ASP LEU ILE VAL GLY ALA PHE GLY VAL          
SEQRES  34 A  957  ASP ARG ALA ILE LEU TYR ARG ALA ARG PRO VAL ILE THR          
SEQRES  35 A  957  VAL ASN ALA GLY LEU GLU VAL TYR PRO SER ILE LEU ASN          
SEQRES  36 A  957  GLN ASP ASN LYS THR CYS SER LEU PRO GLY THR ALA LEU          
SEQRES  37 A  957  LYS VAL SER CYS PHE ASN VAL ARG PHE CYS LEU LYS ALA          
SEQRES  38 A  957  ASP GLY LYS GLY VAL LEU PRO ARG LYS LEU ASN PHE GLN          
SEQRES  39 A  957  VAL GLU LEU LEU LEU ASP LYS LEU LYS GLN LYS GLY ALA          
SEQRES  40 A  957  ILE ARG ARG ALA LEU PHE LEU TYR SER ARG SER PRO SER          
SEQRES  41 A  957  HIS SER LYS ASN MET THR ILE SER ARG GLY GLY LEU MET          
SEQRES  42 A  957  GLN CYS GLU GLU LEU ILE ALA TYR LEU ARG ASP GLU SER          
SEQRES  43 A  957  GLU PHE ARG ASP LYS LEU THR PRO ILE THR ILE PHE MET          
SEQRES  44 A  957  GLU TYR ARG LEU ASP TYR ARG THR ALA ALA ASP THR THR          
SEQRES  45 A  957  GLY LEU GLN PRO ILE LEU ASN GLN PHE THR PRO ALA ASN          
SEQRES  46 A  957  ILE SER ARG GLN ALA HIS ILE LEU LEU ASP CYS GLY GLU          
SEQRES  47 A  957  ASP ASN VAL CYS LYS PRO LYS LEU GLU VAL SER VAL ASP          
SEQRES  48 A  957  SER ASP GLN LYS LYS ILE TYR ILE GLY ASP ASP ASN PRO          
SEQRES  49 A  957  LEU THR LEU ILE VAL LYS ALA GLN ASN GLN GLY GLU GLY          
SEQRES  50 A  957  ALA TYR GLU ALA GLU LEU ILE VAL SER ILE PRO LEU GLN          
SEQRES  51 A  957  ALA ASP PHE ILE GLY VAL VAL ARG ASN ASN GLU ALA LEU          
SEQRES  52 A  957  ALA ARG LEU SER CYS ALA PHE LYS THR GLU ASN GLN THR          
SEQRES  53 A  957  ARG GLN VAL VAL CYS ASP LEU GLY ASN PRO MET LYS ALA          
SEQRES  54 A  957  GLY THR GLN LEU LEU ALA GLY LEU ARG PHE SER VAL HIS          
SEQRES  55 A  957  GLN GLN SER GLU MET ASP THR SER VAL LYS PHE ASP LEU          
SEQRES  56 A  957  GLN ILE GLN SER SER ASN LEU PHE ASP LYS VAL SER PRO          
SEQRES  57 A  957  VAL VAL SER HIS LYS VAL ASP LEU ALA VAL LEU ALA ALA          
SEQRES  58 A  957  VAL GLU ILE ARG GLY VAL SER SER PRO ASP HIS VAL PHE          
SEQRES  59 A  957  LEU PRO ILE PRO ASN TRP GLU HIS LYS GLU ASN PRO GLU          
SEQRES  60 A  957  THR GLU GLU ASP VAL GLY PRO VAL VAL GLN HIS ILE TYR          
SEQRES  61 A  957  GLU LEU ARG ASN ASN GLY PRO SER SER PHE SER LYS ALA          
SEQRES  62 A  957  MET LEU HIS LEU GLN TRP PRO TYR LYS TYR ASN ASN ASN          
SEQRES  63 A  957  THR LEU LEU TYR ILE LEU HIS TYR ASP ILE ASP GLY PRO          
SEQRES  64 A  957  MET ASN CYS THR SER ASP MET GLU ILE ASN PRO LEU ARG          
SEQRES  65 A  957  ILE LYS ILE SER SER LEU GLN THR THR GLU LYS ASN ASP          
SEQRES  66 A  957  THR VAL ALA GLY GLN GLY GLU ARG ASP HIS LEU ILE THR          
SEQRES  67 A  957  LYS ARG ASP LEU ALA LEU SER GLU GLY ASP ILE HIS THR          
SEQRES  68 A  957  LEU GLY CYS GLY VAL ALA GLN CYS LEU LYS ILE VAL CYS          
SEQRES  69 A  957  GLN VAL GLY ARG LEU ASP ARG GLY LYS SER ALA ILE LEU          
SEQRES  70 A  957  TYR VAL LYS SER LEU LEU TRP THR GLU THR PHE MET ASN          
SEQRES  71 A  957  LYS GLU ASN GLN ASN HIS SER TYR SER LEU LYS SER SER          
SEQRES  72 A  957  ALA SER PHE ASN VAL ILE GLU PHE PRO TYR LYS ASN LEU          
SEQRES  73 A  957  PRO ILE GLU ASP ILE THR ASN SER THR LEU VAL THR THR          
SEQRES  74 A  957  ASN VAL THR TRP GLY ILE GLN PRO                              
SEQRES   1 B  692  GLY PRO ASN ILE CYS THR THR ARG GLY VAL SER SER CYS          
SEQRES   2 B  692  GLN GLN CYS LEU ALA VAL SER PRO MET CYS ALA TRP CYS          
SEQRES   3 B  692  SER ASP GLU ALA LEU PRO LEU GLY SER PRO ARG CYS ASP          
SEQRES   4 B  692  LEU LYS GLU ASN LEU LEU LYS ASP ASN CYS ALA PRO GLU          
SEQRES   5 B  692  SER ILE GLU PHE PRO VAL SER GLU ALA ARG VAL LEU GLU          
SEQRES   6 B  692  ASP ARG PRO LEU SER ASP LYS GLY SER GLY ASP SER SER          
SEQRES   7 B  692  GLN VAL THR GLN VAL SER PRO GLN ARG ILE ALA LEU ARG          
SEQRES   8 B  692  LEU ARG PRO ASP ASP SER LYS ASN PHE SER ILE GLN VAL          
SEQRES   9 B  692  ARG GLN VAL GLU ASP TYR PRO VAL ASP ILE TYR TYR LEU          
SEQRES  10 B  692  MET ASP LEU SER TYR SER MET LYS ASP ASP LEU TRP SER          
SEQRES  11 B  692  ILE GLN ASN LEU GLY THR LYS LEU ALA THR GLN MET ARG          
SEQRES  12 B  692  LYS LEU THR SER ASN LEU ARG ILE GLY PHE GLY ALA PHE          
SEQRES  13 B  692  VAL ASP LYS PRO VAL SER PRO TYR MET TYR ILE SER PRO          
SEQRES  14 B  692  PRO GLU ALA LEU GLU ASN PRO CYS TYR ASP MET LYS THR          
SEQRES  15 B  692  THR CYS LEU PRO MET PHE GLY TYR LYS HIS VAL LEU THR          
SEQRES  16 B  692  LEU THR ASP GLN VAL THR ARG PHE ASN GLU GLU VAL LYS          
SEQRES  17 B  692  LYS GLN SER VAL SER ARG ASN ARG ASP ALA PRO GLU GLY          
SEQRES  18 B  692  GLY PHE ASP ALA ILE MET GLN ALA THR VAL CYS ASP GLU          
SEQRES  19 B  692  LYS ILE GLY TRP ARG ASN ASP ALA SER HIS LEU LEU VAL          
SEQRES  20 B  692  PHE THR THR ASP ALA LYS THR HIS ILE ALA LEU ASP GLY          
SEQRES  21 B  692  ARG LEU ALA GLY ILE VAL GLN PRO ASN ASP GLY GLN CYS          
SEQRES  22 B  692  HIS VAL GLY SER ASP ASN HIS TYR SER ALA SER THR THR          
SEQRES  23 B  692  MET ASP TYR PRO SER LEU GLY LEU MET THR GLU LYS LEU          
SEQRES  24 B  692  SER GLN LYS ASN ILE ASN LEU ILE PHE ALA VAL THR GLU          
SEQRES  25 B  692  ASN VAL VAL ASN LEU TYR GLN ASN TYR SER GLU LEU ILE          
SEQRES  26 B  692  PRO GLY THR THR VAL GLY VAL LEU SER MET ASP SER SER          
SEQRES  27 B  692  ASN VAL LEU GLN LEU ILE VAL ASP ALA TYR GLY LYS ILE          
SEQRES  28 B  692  ARG SER LYS VAL GLU LEU GLU VAL ARG ASP LEU PRO GLU          
SEQRES  29 B  692  GLU LEU SER LEU SER PHE ASN ALA THR CYS LEU ASN ASN          
SEQRES  30 B  692  GLU VAL ILE PRO GLY LEU LYS SER CYS MET GLY LEU LYS          
SEQRES  31 B  692  ILE GLY ASP THR VAL SER PHE SER ILE GLU ALA LYS VAL          
SEQRES  32 B  692  ARG GLY CYS PRO GLN GLU LYS GLU LYS SER PHE THR ILE          
SEQRES  33 B  692  LYS PRO VAL GLY PHE LYS ASP SER LEU ILE VAL GLN VAL          
SEQRES  34 B  692  THR PHE ASP CYS ASP CYS ALA CYS GLN ALA GLN ALA GLU          
SEQRES  35 B  692  PRO ASN SER HIS ARG CYS ASN ASN GLY ASN GLY THR PHE          
SEQRES  36 B  692  GLU CYS GLY VAL CYS ARG CYS GLY PRO GLY TRP LEU GLY          
SEQRES  37 B  692  SER GLN CYS GLU CYS SER GLU GLU ASP TYR ARG PRO SER          
SEQRES  38 B  692  GLN GLN ASP GLU CYS SER PRO ARG GLU GLY GLN PRO VAL          
SEQRES  39 B  692  CYS SER GLN ARG GLY GLU CYS LEU CYS GLY GLN CYS VAL          
SEQRES  40 B  692  CYS HIS SER SER ASP PHE GLY LYS ILE THR GLY LYS TYR          
SEQRES  41 B  692  CYS GLU CYS ASP ASP PHE SER CYS VAL ARG TYR LYS GLY          
SEQRES  42 B  692  GLU MET CYS SER GLY HIS GLY GLN CYS SER CYS GLY ASP          
SEQRES  43 B  692  CYS LEU CYS ASP SER ASP TRP THR GLY TYR TYR CYS ASN          
SEQRES  44 B  692  CYS THR THR ARG THR ASP THR CYS MET SER SER ASN GLY          
SEQRES  45 B  692  LEU LEU CYS SER GLY ARG GLY LYS CYS GLU CYS GLY SER          
SEQRES  46 B  692  CYS VAL CYS ILE GLN PRO GLY SER TYR GLY ASP THR CYS          
SEQRES  47 B  692  GLU LYS CYS PRO THR CYS PRO ASP ALA CYS THR PHE LYS          
SEQRES  48 B  692  LYS GLU CYS VAL GLU CYS LYS LYS PHE ASP ARG GLU PRO          
SEQRES  49 B  692  TYR MET THR GLU ASN THR CYS ASN ARG TYR CYS ARG ASP          
SEQRES  50 B  692  GLU ILE GLU SER VAL LYS GLU LEU LYS ASP THR GLY LYS          
SEQRES  51 B  692  ASP ALA VAL ASN CYS THR TYR LYS ASN GLU ASP ASP CYS          
SEQRES  52 B  692  VAL VAL ARG PHE GLN TYR TYR GLU ASP SER SER GLY LYS          
SEQRES  53 B  692  SER ILE LEU TYR VAL VAL GLU GLU PRO GLU CYS PRO LYS          
SEQRES  54 B  692  GLY PRO ASP                                                  
MODRES 1M1X ASN A   44  ASN  GLYCOSYLATION SITE                                 
MODRES 1M1X ASN A  260  ASN  GLYCOSYLATION SITE                                 
MODRES 1M1X ASN A  266  ASN  GLYCOSYLATION SITE                                 
MODRES 1M1X ASN A  458  ASN  GLYCOSYLATION SITE                                 
MODRES 1M1X ASN A  585  ASN  GLYCOSYLATION SITE                                 
MODRES 1M1X ASN A  943  ASN  GLYCOSYLATION SITE                                 
MODRES 1M1X ASN A  950  ASN  GLYCOSYLATION SITE                                 
MODRES 1M1X ASN B  320  ASN  GLYCOSYLATION SITE                                 
MODRES 1M1X ASN B  371  ASN  GLYCOSYLATION SITE                                 
MODRES 1M1X ASN B  559  ASN  GLYCOSYLATION SITE                                 
MODRES 1M1X ASN B  654  ASN  GLYCOSYLATION SITE                                 
HET    NAG  A2044      14                                                       
HET    NAG  A2045      14                                                       
HET    NAG  A2260      14                                                       
HET    NAG  A2266      14                                                       
HET    NAG  A2267      14                                                       
HET    NAG  A2458      14                                                       
HET    NAG  A2585      14                                                       
HET    NAG  A2586      14                                                       
HET    NAG  A2943      14                                                       
HET    NDG  A2944      14                                                       
HET    NAG  A2950      14                                                       
HET    NAG  A2951      14                                                       
HET    NAG  B3320      14                                                       
HET    NAG  B3371      14                                                       
HET    NAG  B3559      14                                                       
HET    NDG  B3560      14                                                       
HET    NAG  B3654      14                                                       
HET    NDG  B3655      14                                                       
HET     MN  B4002       1                                                       
HET     MN  A4004       1                                                       
HET     MN  A4005       1                                                       
HET     MN  A4006       1                                                       
HET     MN  A4007       1                                                       
HET     MN  A4008       1                                                       
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     NDG 2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE                        
HETNAM      MN MANGANESE (II) ION                                               
FORMUL   3  NAG    15(C8 H15 N O6)                                              
FORMUL   8  NDG    3(C8 H15 N O6)                                               
FORMUL  14   MN    6(MN 2+)                                                     
HELIX    1   1 GLY A  175  GLN A  180  1                                   6    
HELIX    2   2 GLN A  214  ASP A  218  5                                   5    
HELIX    3   3 ARG A  245  LEU A  250  1                                   6    
HELIX    4   4 GLY A  366  LYS A  370  5                                   5    
HELIX    5   5 ASP A  544  PHE A  548  5                                   5    
HELIX    6   6 THR A  768  GLY A  773  1                                   6    
HELIX    7   7 LYS B  125  TRP B  129  5                                   5    
HELIX    8   8 GLY B  135  ARG B  143  1                                   9    
HELIX    9   9 PRO B  170  GLU B  174  5                                   5    
HELIX   10  10 THR B  201  GLN B  210  1                                  10    
HELIX   11  11 GLY B  222  CYS B  232  1                                  11    
HELIX   12  12 CYS B  232  GLY B  237  1                                   6    
HELIX   13  13 LEU B  258  LEU B  262  5                                   5    
HELIX   14  14 TYR B  281  THR B  285  5                                   5    
HELIX   15  15 SER B  291  LYS B  302  1                                  12    
HELIX   16  16 VAL B  314  TYR B  321  1                                   8    
HELIX   17  17 LEU B  343  ARG B  352  1                                  10    
HELIX   18  18 THR B  564  MET B  568  5                                   5    
HELIX   19  19 LEU B  573  GLY B  577  5                                   5    
HELIX   20  20 ASP B  606  LYS B  611  1                                   6    
HELIX   21  21 LYS B  611  LYS B  619  1                                   9    
SHEET    1   A 4 ALA A   9  SER A  12  0                                        
SHEET    2   A 4 ARG A 431  ARG A 436 -1  O  LEU A 434   N  ALA A   9           
SHEET    3   A 4 ASP A 421  ALA A 426 -1  N  LEU A 422   O  TYR A 435           
SHEET    4   A 4 SER A 407  LYS A 409 -1  N  LYS A 409   O  ILE A 423           
SHEET    1   B 4 VAL A  23  PHE A  26  0                                        
SHEET    2   B 4 PHE A  35  GLY A  39 -1  O  PHE A  35   N  PHE A  26           
SHEET    3   B 4 VAL A  56  ASP A  60 -1  O  LEU A  57   N  VAL A  38           
SHEET    4   B 4 CYS A  67  PRO A  69 -1  O  GLN A  68   N  LYS A  58           
SHEET    1   C 2 ASP A  79  ALA A  81  0                                        
SHEET    2   C 2 ASP A  84  PRO A  85 -1  O  ASP A  84   N  ALA A  81           
SHEET    1   D 3 GLU A  87  PHE A  88  0                                        
SHEET    2   D 3 HIS A 113  TRP A 114 -1  O  HIS A 113   N  PHE A  88           
SHEET    3   D 3 GLU A 123  PRO A 124 -1  O  GLU A 123   N  TRP A 114           
SHEET    1   E 4 SER A  97  SER A 100  0                                        
SHEET    2   E 4 LYS A 104  ALA A 109 -1  O  LEU A 106   N  ARG A  99           
SHEET    3   E 4 THR A 127  ASP A 132 -1  O  THR A 127   N  ALA A 109           
SHEET    4   E 4 LYS A 135  TYR A 139 -1  O  VAL A 137   N  LEU A 130           
SHEET    1   F 4 ILE A 161  THR A 164  0                                        
SHEET    2   F 4 ARG A 168  GLY A 172 -1  O  LEU A 170   N  ASP A 162           
SHEET    3   F 4 LEU A 183  GLN A 187 -1  O  ASP A 186   N  VAL A 169           
SHEET    4   F 4 LEU A 208  ALA A 209 -1  O  LEU A 208   N  SER A 185           
SHEET    1   G 4 SER A 225  GLY A 229  0                                        
SHEET    2   G 4 ASP A 238  VAL A 243 -1  O  ASP A 238   N  GLY A 229           
SHEET    3   G 4 MET A 252  TYR A 256 -1  O  MET A 252   N  VAL A 243           
SHEET    4   G 4 SER A 263  THR A 268 -1  O  PHE A 267   N  VAL A 253           
SHEET    1   H 4 VAL A 280  THR A 283  0                                        
SHEET    2   H 4 ASP A 292  ALA A 297 -1  O  ASP A 292   N  THR A 283           
SHEET    3   H 4 GLN A 314  GLN A 320 -1  O  SER A 316   N  ILE A 295           
SHEET    4   H 4 PHE A 326  ASN A 332 -1  O  LEU A 331   N  VAL A 315           
SHEET    1   I 2 MET A 301  ARG A 303  0                                        
SHEET    2   I 2 LEU A 309  GLU A 311 -1  O  GLN A 310   N  ASP A 302           
SHEET    1   J 4 ILE A 344  ALA A 345  0                                        
SHEET    2   J 4 ASP A 357  ALA A 362 -1  O  ALA A 359   N  ALA A 345           
SHEET    3   J 4 ILE A 372  ARG A 379 -1  O  PHE A 376   N  ILE A 358           
SHEET    4   J 4 GLY A 382  LEU A 383 -1  O  GLY A 382   N  ARG A 379           
SHEET    1   K 4 ILE A 344  ALA A 345  0                                        
SHEET    2   K 4 ASP A 357  ALA A 362 -1  O  ALA A 359   N  ALA A 345           
SHEET    3   K 4 ILE A 372  ARG A 379 -1  O  PHE A 376   N  ILE A 358           
SHEET    4   K 4 ILE A 390  GLU A 392 -1  O  LEU A 391   N  VAL A 373           
SHEET    1   L 2 VAL A 440  ILE A 441  0                                        
SHEET    2   L 2 ILE A 577  LEU A 578  1  O  ILE A 577   N  ILE A 441           
SHEET    1   M 4 ALA A 511  PHE A 513  0                                        
SHEET    2   M 4 GLN A 534  LEU A 542 -1  O  TYR A 541   N  LEU A 512           
SHEET    3   M 4 CYS A 472  ALA A 481 -1  N  PHE A 473   O  ALA A 540           
SHEET    4   M 4 VAL A 443  ALA A 445 -1  N  ASN A 444   O  LYS A 480           
SHEET    1   N 4 ALA A 511  PHE A 513  0                                        
SHEET    2   N 4 GLN A 534  LEU A 542 -1  O  TYR A 541   N  LEU A 512           
SHEET    3   N 4 CYS A 472  ALA A 481 -1  N  PHE A 473   O  ALA A 540           
SHEET    4   N 4 GLU A 448  VAL A 449 -1  N  GLU A 448   O  ARG A 476           
SHEET    1   O 4 SER A 520  LYS A 523  0                                        
SHEET    2   O 4 VAL A 495  LEU A 499 -1  N  LEU A 497   O  HIS A 521           
SHEET    3   O 4 ILE A 555  GLU A 560 -1  O  PHE A 558   N  LEU A 498           
SHEET    4   O 4 ILE A 586  ALA A 590 -1  O  ILE A 586   N  MET A 559           
SHEET    1   P 4 LEU A 606  GLU A 607  0                                        
SHEET    2   P 4 ASN A 623  ASN A 633 -1  O  GLN A 632   N  GLU A 607           
SHEET    3   P 4 GLN A 692  VAL A 701 -1  O  LEU A 693   N  ALA A 631           
SHEET    4   P 4 PHE A 653  GLY A 655 -1  N  GLY A 655   O  ARG A 698           
SHEET    1   Q 3 LYS A 616  TYR A 618  0                                        
SHEET    2   Q 3 VAL A 730  ALA A 737  1  O  ALA A 737   N  ILE A 617           
SHEET    3   Q 3 SER A 710  LEU A 715 -1  N  LEU A 715   O  VAL A 730           
SHEET    1   R 3 GLU A 642  SER A 646  0                                        
SHEET    2   R 3 ARG A 677  ASP A 682 -1  O  VAL A 679   N  VAL A 645           
SHEET    3   R 3 ALA A 669  THR A 672 -1  N  LYS A 671   O  GLN A 678           
SHEET    1   S 4 VAL A 742  SER A 748  0                                        
SHEET    2   S 4 GLN A 777  ASN A 784 -1  O  GLU A 781   N  ARG A 745           
SHEET    3   S 4 LYS A 893  LYS A 900 -1  O  ALA A 895   N  LEU A 782           
SHEET    4   S 4 HIS A 813  ASP A 817 -1  N  ASP A 815   O  TYR A 898           
SHEET    1   T 5 HIS A 752  PHE A 754  0                                        
SHEET    2   T 5 ILE A 941  THR A 952  1  O  ASN A 950   N  VAL A 753           
SHEET    3   T 5 SER A 917  GLU A 930 -1  N  VAL A 928   O  ILE A 941           
SHEET    4   T 5 LYS A 792  TYR A 803 -1  N  HIS A 796   O  SER A 925           
SHEET    5   T 5 ASN A 806  THR A 807 -1  O  ASN A 806   N  TYR A 803           
SHEET    1   U 6 HIS A 752  PHE A 754  0                                        
SHEET    2   U 6 ILE A 941  THR A 952  1  O  ASN A 950   N  VAL A 753           
SHEET    3   U 6 SER A 917  GLU A 930 -1  N  VAL A 928   O  ILE A 941           
SHEET    4   U 6 LYS A 792  TYR A 803 -1  N  HIS A 796   O  SER A 925           
SHEET    5   U 6 GLN A 878  VAL A 886 -1  O  CYS A 884   N  LEU A 795           
SHEET    6   U 6 MET A 820  SER A 824 -1  N  ASN A 821   O  GLN A 885           
SHEET    1   V 6 ARG B  62  LEU B  64  0                                        
SHEET    2   V 6 ARG B  87  ILE B  88 -1  O  ARG B  87   N  LEU B  64           
SHEET    3   V 6 LEU B 425  GLN B 428  1  O  GLN B 428   N  ILE B  88           
SHEET    4   V 6 SER B 413  PRO B 418 -1  N  ILE B 416   O  LEU B 425           
SHEET    5   V 6 LYS B 354  GLU B 358 -1  N  GLU B 358   O  LYS B 417           
SHEET    6   V 6 SER B 385  MET B 387 -1  O  CYS B 386   N  VAL B 355           
SHEET    1   W 2 ARG B  91  LEU B  92  0                                        
SHEET    2   W 2 THR B 430  PHE B 431  1  O  THR B 430   N  LEU B  92           
SHEET    1   X 3 SER B  97  ASN B  99  0                                        
SHEET    2   X 3 GLU B 400  VAL B 403 -1  O  ALA B 401   N  LYS B  98           
SHEET    3   X 3 LEU B 366  SER B 369 -1  N  SER B 367   O  LYS B 402           
SHEET    1   Y 4 ILE B 102  ARG B 105  0                                        
SHEET    2   Y 4 THR B 394  PHE B 397 -1  O  VAL B 395   N  VAL B 104           
SHEET    3   Y 4 ASN B 371  THR B 373 -1  N  THR B 373   O  SER B 396           
SHEET    4   Y 4 VAL B 379  PRO B 381 -1  O  ILE B 380   N  ALA B 372           
SHEET    1   Z 6 TYR B 190  LYS B 191  0                                        
SHEET    2   Z 6 LEU B 149  PHE B 156 -1  N  ALA B 155   O  LYS B 191           
SHEET    3   Z 6 VAL B 112  ASP B 119  1  N  TYR B 116   O  GLY B 154           
SHEET    4   Z 6 SER B 243  THR B 250  1  O  THR B 249   N  LEU B 117           
SHEET    5   Z 6 LEU B 306  THR B 311  1  O  ILE B 307   N  PHE B 248           
SHEET    6   Z 6 THR B 329  LEU B 333  1  O  THR B 329   N  PHE B 308           
SHEET    1  AA 2 TRP B 553  THR B 554  0                                        
SHEET    2  AA 2 CYS B 560  THR B 561 -1  O  CYS B 560   N  THR B 554           
SHEET    1  AB 2 GLY B 579  CYS B 581  0                                        
SHEET    2  AB 2 CYS B 586  CYS B 588 -1  O  VAL B 587   N  LYS B 580           
SHEET    1  AC 3 VAL B 653  ASN B 659  0                                        
SHEET    2  AC 3 CYS B 663  TYR B 669 -1  O  VAL B 665   N  TYR B 657           
SHEET    3  AC 3 VAL B 682  GLU B 686 -1  O  VAL B 682   N  ARG B 666           
SSBOND   1 CYS A   59    CYS A   67                          1555   1555  2.07  
SSBOND   2 CYS A  108    CYS A  128                          1555   1555  2.03  
SSBOND   3 CYS A  142    CYS A  155                          1555   1555  2.03  
SSBOND   4 CYS A  461    CYS A  472                          1555   1555  2.08  
SSBOND   5 CYS A  478    CYS A  535                          1555   1555  2.03  
SSBOND   6 CYS A  596    CYS A  602                          1555   1555  2.07  
SSBOND   7 CYS A  668    CYS A  681                          1555   1555  2.03  
SSBOND   8 CYS A  822    CYS A  884                          1555   1555  2.02  
SSBOND   9 CYS A  874    CYS A  879                          1555   1555  2.02  
SSBOND  10 CYS B  177    CYS B  184                          1555   1555  2.04  
SSBOND  11 CYS B  232    CYS B  273                          1555   1555  2.04  
SSBOND  12 CYS B  374    CYS B  386                          1555   1555  2.02  
SSBOND  13 CYS B  406    CYS B  433                          1555   1555  2.03  
SSBOND  14 CYS B  536    CYS B  544                          1555   1555  2.04  
SSBOND  15 CYS B  542    CYS B  547                          1555   1555  2.03  
SSBOND  16 CYS B  549    CYS B  558                          1555   1555  2.03  
SSBOND  17 CYS B  560    CYS B  583                          1555   1555  2.03  
SSBOND  18 CYS B  567    CYS B  581                          1555   1555  2.02  
SSBOND  19 CYS B  575    CYS B  586                          1555   1555  2.02  
SSBOND  20 CYS B  588    CYS B  598                          1555   1555  2.03  
SSBOND  21 CYS B  601    CYS B  604                          1555   1555  2.03  
SSBOND  22 CYS B  608    CYS B  655                          1555   1555  2.02  
SSBOND  23 CYS B  614    CYS B  635                          1555   1555  2.03  
SSBOND  24 CYS B  617    CYS B  631                          1555   1555  2.02  
SSBOND  25 CYS B  663    CYS B  687                          1555   1555  2.03  
LINK         ND2 ASN A  44                 C1  NAG A2044     1555   1555  1.45  
LINK         ND2 ASN A 260                 C1  NAG A2260     1555   1555  1.46  
LINK         ND2 ASN A 266                 C1  NAG A2266     1555   1555  1.44  
LINK         ND2 ASN A 458                 C1  NAG A2458     1555   1555  1.45  
LINK         ND2 ASN A 585                 C1  NAG A2585     1555   1555  1.45  
LINK         ND2 ASN A 943                 C1  NAG A2943     1555   1555  1.45  
LINK         ND2 ASN A 950                 C1  NAG A2950     1555   1555  1.45  
LINK         O4  NAG A2044                 C1  NAG A2045     1555   1555  1.39  
LINK         O4  NAG A2266                 C1  NAG A2267     1555   1555  1.41  
LINK         O4  NAG A2585                 C1  NAG A2586     1555   1555  1.39  
LINK         O4  NAG A2943                 C1  NDG A2944     1555   1555  1.39  
LINK         O4  NAG A2950                 C1  NAG A2951     1555   1555  1.40  
LINK         O4  NAG B3559                 C1  NDG B3560     1555   1555  1.40  
LINK         O4  NAG B3654                 C1  NDG B3655     1555   1555  1.39  
LINK         ND2 ASN B 320                 C1  NAG B3320     1555   1555  1.45  
LINK         ND2 ASN B 371                 C1  NAG B3371     1555   1555  1.46  
LINK         ND2 ASN B 559                 C1  NAG B3559     1555   1555  1.45  
LINK         ND2 ASN B 654                 C1  NAG B3654     1555   1555  1.45  
LINK        MN    MN A4004                 OD1 ASP A 238     1555   1555  2.39  
LINK        MN    MN A4004                 O   ILE A 236     1555   1555  2.42  
LINK        MN    MN A4004                 OD2 ASP A 230     1555   1555  2.70  
LINK        MN    MN A4005                 ND2 ASN A 286     1555   1555  2.55  
LINK        MN    MN A4005                 OD2 ASP A 288     1555   1555  2.59  
LINK        MN    MN A4005                 O   TYR A 290     1555   1555  2.36  
LINK        MN    MN A4005                 OD2 ASP A 284     1555   1555  2.30  
LINK        MN    MN A4006                 OD1 ASP A 357     1555   1555  2.77  
LINK        MN    MN A4006                 OD2 ASP A 353     1555   1555  2.66  
LINK        MN    MN A4006                 O   PHE A 355     1555   1555  2.41  
LINK        MN    MN A4006                 OD2 ASP A 351     1555   1555  2.73  
LINK        MN    MN A4007                 O   TYR A 419     1555   1555  2.43  
LINK        MN    MN A4007                 OD1 ASP A 421     1555   1555  2.75  
LINK        MN    MN A4007                 OD2 ASP A 415     1555   1555  2.56  
LINK        MN    MN A4008                 OE2 GLU A 636     1555   1555  2.55  
LINK        MN    MN A4008                 O   VAL A 601     1555   1555  2.28  
LINK        MN    MN A4008                 OD1 ASP A 599     1555   1555  2.70  
LINK        MN    MN A4008                 OD2 ASP A 599     1555   1555  2.54  
LINK        MN    MN A4008                 OE1 GLU A 636     1555   1555  2.69  
LINK        MN    MN B4002                 OD1 ASP B 127     1555   1555  1.93  
LINK        MN    MN B4002                 O   SER B 123     1555   1555  2.54  
SITE     1 AC1  6 GLY A  16  LYS A  42  ASN A  44  VAL A  51                    
SITE     2 AC1  6 GLU A  52  NAG A2045                                          
SITE     1 AC2  2 HIS A  91  NAG A2044                                          
SITE     1 AC3  1 ASN A 260                                                     
SITE     1 AC4  6 PHE A 217  TYR A 254  SER A 263  LEU A 264                    
SITE     2 AC4  6 ASN A 266  NAG A2267                                          
SITE     1 AC5  4 ALA A 213  GLN A 214  PHE A 217  NAG A2266                    
SITE     1 AC6  7 PRO A 451  LEU A 454  ASN A 455  ASN A 458                    
SITE     2 AC6  7 THR A 460  SER A 471  CYS A 472                               
SITE     1 AC7  3 GLU A 560  ASN A 585  NAG A2586                               
SITE     1 AC8  1 NAG A2585                                                     
SITE     1 AC9  3 THR A 942  ASN A 943  NDG A2944                               
SITE     1 BC1  1 NAG A2943                                                     
SITE     1 BC2  4 ASP A 751  THR A 948  ASN A 950  NAG A2951                    
SITE     1 BC3  1 NAG A2950                                                     
SITE     1 BC4  3 ARG A 248  ASN B 316  ASN B 320                               
SITE     1 BC5  2 ASN B 371  GLU B 400                                          
SITE     1 BC6  3 TYR B 557  ASN B 559  NDG B3560                               
SITE     1 BC7  3 PRO A 624  ILE A 654  NAG B3559                               
SITE     1 BC8  8 ASP B 647  THR B 648  GLY B 649  LYS B 650                    
SITE     2 BC8  8 ALA B 652  ASN B 654  ARG B 666  NDG B3655                    
SITE     1 BC9  5 LYS B 646  ASP B 647  THR B 648  LYS B 650                    
SITE     2 BC9  5 NAG B3654                                                     
SITE     1 CC1  5 SER B 123  MET B 124  ASP B 126  ASP B 127                    
SITE     2 CC1  5 MET B 335                                                     
SITE     1 CC2  5 ASP A 230  ASN A 232  ASP A 234  ILE A 236                    
SITE     2 CC2  5 ASP A 238                                                     
SITE     1 CC3  5 ASP A 284  ASN A 286  ASP A 288  TYR A 290                    
SITE     2 CC3  5 ASP A 292                                                     
SITE     1 CC4  5 ASP A 349  ASP A 351  ASP A 353  PHE A 355                    
SITE     2 CC4  5 ASP A 357                                                     
SITE     1 CC5  6 ASP A 413  ASP A 415  ASN A 417  TYR A 419                    
SITE     2 CC5  6 PRO A 420  ASP A 421                                          
SITE     1 CC6  4 GLY A 597  ASP A 599  VAL A 601  GLU A 636                    
CRYST1  130.400  130.400  310.300  90.00  90.00 120.00 P 32 2 1      6          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.007669  0.004428  0.000000        0.00000                         
SCALE2      0.000000  0.008855  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003223        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system