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Entry: 3ZDY
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HEADER    CELL ADHESION/IMMUNE SYSTEM/PEPTIDE     03-DEC-12   3ZDY              
TITLE     INTEGRIN ALPHAIIB BETA3 HEADPIECE AND RGD PEPTIDE COMPLEX             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: INTEGRIN ALPHA-IIB;                                        
COMPND   3 CHAIN: A, C;                                                         
COMPND   4 FRAGMENT: RESIDUES 32-488;                                           
COMPND   5 SYNONYM: GPALPHA IIB, GPIIB, PLATELET MEMBRANE GLYCOPROTEIN IIB;     
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: INTEGRIN BETA-3;                                           
COMPND   9 CHAIN: B, D;                                                         
COMPND  10 FRAGMENT: RESIDUES 27-498;                                           
COMPND  11 SYNONYM: PLATELET MEMBRANE GLYCOPROTEIN IIIA, GPIIIA;                
COMPND  12 ENGINEERED: YES;                                                     
COMPND  13 MOL_ID: 3;                                                           
COMPND  14 MOLECULE: 10E5 FAB HEAVY CHAIN;                                      
COMPND  15 CHAIN: E, H;                                                         
COMPND  16 ENGINEERED: YES;                                                     
COMPND  17 MOL_ID: 4;                                                           
COMPND  18 MOLECULE: 10E5 FAB LIGHT CHAIN;                                      
COMPND  19 CHAIN: F, L;                                                         
COMPND  20 ENGINEERED: YES;                                                     
COMPND  21 MOL_ID: 5;                                                           
COMPND  22 MOLECULE: RGD PEPTIDE;                                               
COMPND  23 CHAIN: I, J;                                                         
COMPND  24 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;                               
SOURCE   6 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;                           
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 10029;                                      
SOURCE   8 EXPRESSION_SYSTEM_CELL_LINE: CHO LEC 3.2.1.8;                        
SOURCE   9 EXPRESSION_SYSTEM_VECTOR: PCDNA3.1;                                  
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  12 ORGANISM_COMMON: HUMAN;                                              
SOURCE  13 ORGANISM_TAXID: 9606;                                                
SOURCE  14 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;                               
SOURCE  15 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;                           
SOURCE  16 EXPRESSION_SYSTEM_TAXID: 10029;                                      
SOURCE  17 EXPRESSION_SYSTEM_CELL_LINE: CHO LEC 3.2.1.8;                        
SOURCE  18 EXPRESSION_SYSTEM_VECTOR: PEF1;                                      
SOURCE  19 MOL_ID: 3;                                                           
SOURCE  20 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  21 ORGANISM_COMMON: HOUSE MOUSE;                                        
SOURCE  22 ORGANISM_TAXID: 10090;                                               
SOURCE  23 EXPRESSION_SYSTEM: MUS MUSCULUS;                                     
SOURCE  24 EXPRESSION_SYSTEM_COMMON: HOUSE MOUSE;                               
SOURCE  25 EXPRESSION_SYSTEM_TAXID: 10090;                                      
SOURCE  26 OTHER_DETAILS: HYBRIDOMA;                                            
SOURCE  27 MOL_ID: 4;                                                           
SOURCE  28 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  29 ORGANISM_COMMON: HOUSE MOUSE;                                        
SOURCE  30 ORGANISM_TAXID: 10090;                                               
SOURCE  31 EXPRESSION_SYSTEM: MUS MUSCULUS;                                     
SOURCE  32 EXPRESSION_SYSTEM_COMMON: HOUSE MOUSE;                               
SOURCE  33 EXPRESSION_SYSTEM_TAXID: 10090;                                      
SOURCE  34 OTHER_DETAILS: HYBRIDOMA;                                            
SOURCE  35 MOL_ID: 5;                                                           
SOURCE  36 SYNTHETIC: YES;                                                      
SOURCE  37 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  38 ORGANISM_COMMON: HUMAN;                                              
SOURCE  39 ORGANISM_TAXID: 9606                                                 
KEYWDS    CELL ADHESION-IMMUNE SYSTEM-PEPTIDE COMPLEX, CELL ADHESION            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.H.ZHU,J.Q.ZHU,T.A.SPRINGER                                          
REVDAT   3   25-OCT-17 3ZDY    1       REMARK ATOM                              
REVDAT   2   10-JUL-13 3ZDY    1       JRNL                                     
REVDAT   1   05-JUN-13 3ZDY    0                                                
JRNL        AUTH   J.ZHU,J.ZHU,T.A.SPRINGER                                     
JRNL        TITL   COMPLETE INTEGRIN HEADPIECE OPENING IN EIGHT STEPS.          
JRNL        REF    J.CELL BIOL.                  V. 201  1053 2013              
JRNL        REFN                   ISSN 0021-9525                               
JRNL        PMID   23798730                                                     
JRNL        DOI    10.1083/JCB.201212037                                        
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.45 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE)                               
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.45                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 49.15                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.330                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 146295                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.182                           
REMARK   3   R VALUE            (WORKING SET) : 0.182                           
REMARK   3   FREE R VALUE                     : 0.216                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 0.700                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1015                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 49.1599 -  4.6855    1.00    21384   150  0.1580 0.1784        
REMARK   3     2  4.6855 -  3.7194    1.00    20883   165  0.1463 0.1678        
REMARK   3     3  3.7194 -  3.2494    1.00    20726   150  0.1815 0.2397        
REMARK   3     4  3.2494 -  2.9523    1.00    20660   131  0.2007 0.2560        
REMARK   3     5  2.9523 -  2.7407    1.00    20597   151  0.2308 0.2953        
REMARK   3     6  2.7407 -  2.5792    1.00    20545   132  0.2585 0.3378        
REMARK   3     7  2.5792 -  2.4500    1.00    20485   136  0.2653 0.2858        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.20                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : 0.34                                          
REMARK   3   B_SOL              : 54.51                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.350            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.590           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 45.59                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 77.30                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 5.46540                                              
REMARK   3    B22 (A**2) : 2.20870                                              
REMARK   3    B33 (A**2) : -7.67410                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.005          21810                                  
REMARK   3   ANGLE     :  0.570          29536                                  
REMARK   3   CHIRALITY :  0.038           3278                                  
REMARK   3   PLANARITY :  0.002           3825                                  
REMARK   3   DIHEDRAL  : 12.980           7889                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 20                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN A AND (RESID 1:454 OR RESID 2004:2007)           
REMARK   3    ORIGIN FOR THE GROUP (A):  50.9695  90.4371  54.7385              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2791 T22:  -0.0057                                     
REMARK   3      T33:   0.1522 T12:   0.0046                                     
REMARK   3      T13:   0.0745 T23:   0.0580                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5564 L22:   0.8395                                     
REMARK   3      L33:   0.6508 L12:  -0.0659                                     
REMARK   3      L13:  -0.1099 L23:   0.2607                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0084 S12:  -0.0179 S13:  -0.0403                       
REMARK   3      S21:   0.1082 S22:  -0.0303 S23:   0.0839                       
REMARK   3      S31:   0.1786 S32:  -0.0950 S33:  -0.0215                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN C AND (RESID 1:454 OR RESID 2004:2007)           
REMARK   3    ORIGIN FOR THE GROUP (A):  84.5277  87.1546 119.4334              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2090 T22:   0.2445                                     
REMARK   3      T33:   0.1478 T12:   0.0672                                     
REMARK   3      T13:   0.0787 T23:  -0.0287                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2676 L22:   0.6921                                     
REMARK   3      L33:   1.5431 L12:   0.0308                                     
REMARK   3      L13:  -0.3811 L23:  -0.0437                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0783 S12:   0.0982 S13:  -0.1418                       
REMARK   3      S21:  -0.1477 S22:   0.0549 S23:  -0.1707                       
REMARK   3      S31:   0.3357 S32:   0.4048 S33:   0.0147                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN B AND RESID 1:57                                 
REMARK   3    ORIGIN FOR THE GROUP (A): 123.5684  89.3828  35.1357              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5312 T22:   1.4957                                     
REMARK   3      T33:   0.8316 T12:   0.3502                                     
REMARK   3      T13:  -0.0691 T23:  -0.1934                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.1788 L22:   4.2741                                     
REMARK   3      L33:   1.2173 L12:  -2.0559                                     
REMARK   3      L13:  -1.7819 L23:  -0.3449                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0952 S12:   0.5302 S13:  -0.4902                       
REMARK   3      S21:  -0.1176 S22:  -0.0914 S23:  -1.1286                       
REMARK   3      S31:   0.2311 S32:   0.6025 S33:   0.2722                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN B AND (RESID 58:107 OR RESID 354:432)            
REMARK   3    ORIGIN FOR THE GROUP (A): 101.2858 108.1983  53.4242              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1736 T22:   0.4778                                     
REMARK   3      T33:   0.3818 T12:   0.0569                                     
REMARK   3      T13:  -0.0839 T23:  -0.0800                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.5657 L22:   3.9139                                     
REMARK   3      L33:   7.6004 L12:  -1.1040                                     
REMARK   3      L13:  -2.2314 L23:   3.6251                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0243 S12:  -0.0830 S13:   0.2188                       
REMARK   3      S21:   0.0800 S22:   0.2625 S23:  -0.2378                       
REMARK   3      S31:   0.2292 S32:   0.8065 S33:  -0.1906                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN B AND (RESID 109:352 OR RESID 2001:2003)         
REMARK   3    ORIGIN FOR THE GROUP (A):  67.6653 118.7738  64.3397              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3213 T22:  -0.0550                                     
REMARK   3      T33:   0.1876 T12:   0.0300                                     
REMARK   3      T13:   0.0572 T23:   0.0053                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9336 L22:   1.5891                                     
REMARK   3      L33:   0.6067 L12:   0.2573                                     
REMARK   3      L13:   0.0926 L23:   0.3466                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0239 S12:  -0.0924 S13:   0.1822                       
REMARK   3      S21:   0.1320 S22:   0.0721 S23:  -0.0679                       
REMARK   3      S31:  -0.1828 S32:   0.0647 S33:  -0.0349                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN B AND RESID 433:466                              
REMARK   3    ORIGIN FOR THE GROUP (A): 116.0084  89.9435  19.4222              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5994 T22:   1.6770                                     
REMARK   3      T33:   0.6815 T12:   0.2945                                     
REMARK   3      T13:   0.0982 T23:  -0.1071                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.6671 L22:   4.1397                                     
REMARK   3      L33:   1.0035 L12:   2.2025                                     
REMARK   3      L13:  -1.6341 L23:  -1.2771                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2823 S12:   0.0800 S13:  -0.2975                       
REMARK   3      S21:  -0.7914 S22:   0.0213 S23:  -1.1176                       
REMARK   3      S31:  -0.2614 S32:   0.3885 S33:  -0.3338                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN D AND RESID 1:57                                 
REMARK   3    ORIGIN FOR THE GROUP (A):  15.2712  70.5250 142.7320              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9178 T22:   1.1551                                     
REMARK   3      T33:   0.5692 T12:  -0.5699                                     
REMARK   3      T13:   0.1499 T23:  -0.0904                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.5142 L22:   5.4127                                     
REMARK   3      L33:   2.8230 L12:   2.1569                                     
REMARK   3      L13:  -2.1496 L23:  -1.3391                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4758 S12:  -0.0445 S13:  -0.7126                       
REMARK   3      S21:  -0.1289 S22:   0.0280 S23:   0.6605                       
REMARK   3      S31:   0.8288 S32:  -0.8314 S33:   0.3336                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN D AND (RESID 58:107 OR RESID 354:432)            
REMARK   3    ORIGIN FOR THE GROUP (A):  31.2080  87.4240 117.3885              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3341 T22:   0.6588                                     
REMARK   3      T33:   0.2491 T12:  -0.1923                                     
REMARK   3      T13:  -0.0233 T23:   0.0319                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.7310 L22:   1.9574                                     
REMARK   3      L33:   6.5103 L12:  -0.1030                                     
REMARK   3      L13:  -0.5886 L23:  -1.1688                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1472 S12:   0.5181 S13:  -0.0706                       
REMARK   3      S21:  -0.1276 S22:   0.1056 S23:   0.0683                       
REMARK   3      S31:   0.4874 S32:  -0.9897 S33:   0.0561                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN D AND (RESID 109:352 OR RESID 2001:2003)         
REMARK   3    ORIGIN FOR THE GROUP (A):  60.3590 102.6816 100.6281              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2773 T22:   0.2867                                     
REMARK   3      T33:   0.0852 T12:  -0.0624                                     
REMARK   3      T13:   0.0349 T23:   0.0878                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4381 L22:   0.8591                                     
REMARK   3      L33:   2.3480 L12:  -0.4299                                     
REMARK   3      L13:   0.6057 L23:  -0.2981                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0402 S12:   0.2944 S13:   0.2166                       
REMARK   3      S21:  -0.1672 S22:   0.0666 S23:   0.0297                       
REMARK   3      S31:  -0.1223 S32:  -0.2457 S33:  -0.0590                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: CHAIN D AND RESID 433:471                              
REMARK   3    ORIGIN FOR THE GROUP (A):  21.6242  78.9521 156.6558              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5511 T22:   0.5592                                     
REMARK   3      T33:   0.4943 T12:  -0.2146                                     
REMARK   3      T13:   0.1931 T23:  -0.0991                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.4699 L22:   5.9242                                     
REMARK   3      L33:   5.1612 L12:   2.4387                                     
REMARK   3      L13:  -0.6202 L23:   2.0928                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2507 S12:   0.0607 S13:  -0.5976                       
REMARK   3      S21:   0.2775 S22:   0.0829 S23:   0.3824                       
REMARK   3      S31:   1.0904 S32:  -1.1261 S33:   0.1673                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: CHAIN H AND RESID 1:119                                
REMARK   3    ORIGIN FOR THE GROUP (A):  18.0017  96.5377  83.6955              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5985 T22:   0.5760                                     
REMARK   3      T33:   0.3500 T12:   0.1183                                     
REMARK   3      T13:   0.1976 T23:  -0.0088                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.1097 L22:   0.6893                                     
REMARK   3      L33:   3.8480 L12:   0.7522                                     
REMARK   3      L13:  -2.0113 L23:   0.4278                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2019 S12:  -0.7585 S13:  -0.0633                       
REMARK   3      S21:   0.9085 S22:   0.1329 S23:   0.2585                       
REMARK   3      S31:   0.3731 S32:  -0.1059 S33:   0.1123                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: CHAIN H AND RESID 120:221                              
REMARK   3    ORIGIN FOR THE GROUP (A): -13.7086  80.7099  94.5229              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6047 T22:   0.7888                                     
REMARK   3      T33:   1.3877 T12:   0.1772                                     
REMARK   3      T13:   0.3909 T23:   0.4800                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.4262 L22:   0.0507                                     
REMARK   3      L33:   1.6905 L12:   0.2042                                     
REMARK   3      L13:  -0.8244 L23:  -0.2908                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3839 S12:  -0.6196 S13:  -1.7221                       
REMARK   3      S21:   0.1343 S22:   0.1066 S23:   0.0309                       
REMARK   3      S31:   0.5519 S32:  -0.1822 S33:   0.3190                       
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    SELECTION: CHAIN L AND RESID 1:108                                
REMARK   3    ORIGIN FOR THE GROUP (A):   6.3675  95.6615  65.3048              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2998 T22:   0.6398                                     
REMARK   3      T33:   0.5490 T12:   0.0066                                     
REMARK   3      T13:   0.1457 T23:  -0.1280                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.3251 L22:   0.5392                                     
REMARK   3      L33:   1.2542 L12:   1.0771                                     
REMARK   3      L13:  -0.4050 L23:  -0.5402                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0630 S12:   0.2727 S13:  -0.1215                       
REMARK   3      S21:   0.1489 S22:  -0.2039 S23:   0.8472                       
REMARK   3      S31:   0.1711 S32:  -0.6404 S33:   0.1888                       
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    SELECTION: CHAIN L AND RESID 109:214                              
REMARK   3    ORIGIN FOR THE GROUP (A): -22.0140  92.8721  87.8553              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3406 T22:   0.6800                                     
REMARK   3      T33:   0.8833 T12:   0.1195                                     
REMARK   3      T13:   0.2858 T23:   0.1058                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.5301 L22:   1.3876                                     
REMARK   3      L33:   6.3528 L12:   0.1392                                     
REMARK   3      L13:  -1.2052 L23:   1.1129                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.5161 S12:  -0.2021 S13:  -0.9072                       
REMARK   3      S21:   0.2649 S22:  -0.0077 S23:   0.3613                       
REMARK   3      S31:   0.3217 S32:  -0.3977 S33:   0.3961                       
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    SELECTION: CHAIN E AND RESID 1:119                                
REMARK   3    ORIGIN FOR THE GROUP (A): 114.8122  90.4623  87.2259              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8013 T22:   0.7732                                     
REMARK   3      T33:   0.5082 T12:  -0.1162                                     
REMARK   3      T13:   0.3263 T23:  -0.0451                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.7953 L22:   0.6173                                     
REMARK   3      L33:   7.2664 L12:  -0.4782                                     
REMARK   3      L13:  -1.6696 L23:  -0.1683                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0168 S12:   0.4165 S13:  -0.0626                       
REMARK   3      S21:  -0.7611 S22:  -0.1078 S23:  -0.3280                       
REMARK   3      S31:   1.1432 S32:  -0.2061 S33:   0.1885                       
REMARK   3   TLS GROUP : 16                                                     
REMARK   3    SELECTION: CHAIN E AND RESID 120:221                              
REMARK   3    ORIGIN FOR THE GROUP (A): 150.6850  82.4365  80.5665              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0732 T22:   1.6591                                     
REMARK   3      T33:   0.8706 T12:   0.6266                                     
REMARK   3      T13:   0.2097 T23:   0.0709                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.8510 L22:   2.1404                                     
REMARK   3      L33:   0.6943 L12:   0.5969                                     
REMARK   3      L13:  -0.8879 L23:   0.7319                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1179 S12:   0.5691 S13:  -0.6374                       
REMARK   3      S21:  -0.1466 S22:   0.1743 S23:  -0.9208                       
REMARK   3      S31:   0.6386 S32:   1.6267 S33:  -0.2256                       
REMARK   3   TLS GROUP : 17                                                     
REMARK   3    SELECTION: CHAIN F AND RESID 1:108                                
REMARK   3    ORIGIN FOR THE GROUP (A): 125.6631 100.6998 103.1462              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3518 T22:   0.9748                                     
REMARK   3      T33:   0.9101 T12:  -0.1134                                     
REMARK   3      T13:   0.1729 T23:  -0.0864                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.4042 L22:   0.8613                                     
REMARK   3      L33:   1.3749 L12:   1.3907                                     
REMARK   3      L13:   0.1026 L23:   0.1310                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0181 S12:  -0.1160 S13:   0.7598                       
REMARK   3      S21:  -0.0239 S22:  -0.2527 S23:  -1.0727                       
REMARK   3      S31:  -0.0474 S32:   0.8298 S33:   0.1517                       
REMARK   3   TLS GROUP : 18                                                     
REMARK   3    SELECTION: CHAIN F AND RESID 109:214                              
REMARK   3    ORIGIN FOR THE GROUP (A): 154.4127  98.3190  80.9234              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8422 T22:   2.0081                                     
REMARK   3      T33:   1.2543 T12:   0.0399                                     
REMARK   3      T13:   0.3786 T23:   0.4665                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6253 L22:   2.2149                                     
REMARK   3      L33:   2.7100 L12:   0.1451                                     
REMARK   3      L13:  -1.1502 L23:   0.8709                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1712 S12:   1.0500 S13:   0.1833                       
REMARK   3      S21:  -1.0345 S22:   0.1869 S23:  -0.9760                       
REMARK   3      S31:  -0.6252 S32:   0.5884 S33:  -0.4770                       
REMARK   3   TLS GROUP : 19                                                     
REMARK   3    SELECTION: CHAIN I                                                
REMARK   3    ORIGIN FOR THE GROUP (A):  53.1377 110.2449  75.2552              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5240 T22:   1.1430                                     
REMARK   3      T33:   0.3435 T12:  -0.1788                                     
REMARK   3      T13:   0.0300 T23:  -0.1811                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4903 L22:   0.8696                                     
REMARK   3      L33:   5.7525 L12:  -0.3100                                     
REMARK   3      L13:   1.6069 L23:  -1.1131                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1617 S12:  -0.1603 S13:   0.0104                       
REMARK   3      S21:   0.9887 S22:  -0.0775 S23:   0.0646                       
REMARK   3      S31:  -0.3134 S32:  -0.4684 S33:  -0.0387                       
REMARK   3   TLS GROUP : 20                                                     
REMARK   3    SELECTION: CHAIN J                                                
REMARK   3    ORIGIN FOR THE GROUP (A):  77.7201  94.9508  93.5591              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0885 T22:   1.4236                                     
REMARK   3      T33:   0.5089 T12:  -0.3784                                     
REMARK   3      T13:   0.1534 T23:   0.1259                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.5794 L22:   4.0203                                     
REMARK   3      L33:   5.8162 L12:  -5.2984                                     
REMARK   3      L13:  -6.5994 L23:   4.7624                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4945 S12:   0.7547 S13:   0.3627                       
REMARK   3      S21:  -1.6915 S22:  -0.7173 S23:  -0.6740                       
REMARK   3      S31:   0.5952 S32:   0.2949 S33:   0.2375                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3ZDY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 03-DEC-12.                  
REMARK 100 THE DEPOSITION ID IS D_1290054969.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.9                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 23ID                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97934                            
REMARK 200  MONOCHROMATOR                  : DOUBLE SI CRYSTAL                  
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 146427                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.450                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 6.700                              
REMARK 200  R MERGE                    (I) : 0.20000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.0000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.45                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.51                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 1.39000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.600                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHENIX                                                
REMARK 200 STARTING MODEL: PDB ENTRY 3T3P                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 63.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.35                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 11% PEG 8000, 0.2 M AMMONIUM SULFATE,    
REMARK 280  0.1 M TRIS-HCL, PH 8.9                                              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X+1/2,Y+1/2,-Z                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000      128.88000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       72.62500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000      128.88000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       72.62500            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: PENTAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: PENTAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 13200 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 56980 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -214.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, H, I, L                         
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: PENTAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: PENTAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 12430 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 56970 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -166.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, E, F, J                         
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     LYS A   455                                                      
REMARK 465     ALA A   456                                                      
REMARK 465     SER A   457                                                      
REMARK 465     GLY B     1                                                      
REMARK 465     PRO B     2                                                      
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     VAL C   454                                                      
REMARK 465     LYS C   455                                                      
REMARK 465     ALA C   456                                                      
REMARK 465     SER C   457                                                      
REMARK 465     GLY D     1                                                      
REMARK 465     PRO D     2                                                      
REMARK 465     GLU D   472                                                      
REMARK 465     GLY E   135                                                      
REMARK 465     ASP E   136                                                      
REMARK 465     THR E   137                                                      
REMARK 465     GLY E   220                                                      
REMARK 465     PRO E   221                                                      
REMARK 465     GLY H   135                                                      
REMARK 465     ASP H   136                                                      
REMARK 465     THR H   137                                                      
REMARK 465     GLY H   220                                                      
REMARK 465     PRO H   221                                                      
REMARK 465     PRO J   497                                                      
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     GLU A   61   CD                                                  
REMARK 480     GLU B  174   CG   CD   OE1  OE2                                  
REMARK 480     GLU B  234   CD                                                  
REMARK 480     GLU C   61   CD                                                  
REMARK 480     GLU D  312   CD                                                  
REMARK 480     LYS D  350   CD   CE   NZ                                        
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   N    GLY I   492     O    HOH A  3159              1.99            
REMARK 500   O4   SO4 A  1462     O    HOH A  3331              2.06            
REMARK 500   O    HOH B  3012     O    HOH B  3115              2.06            
REMARK 500   O    HOH B  3137     O    HOH B  3138              2.08            
REMARK 500   O4   SO4 A  1462     O    HOH A  3332              2.08            
REMARK 500   NH1  ARG I   493     O    HOH A  3155              2.09            
REMARK 500   O    HOH A  3036     O    HOH B  3045              2.09            
REMARK 500   O    HOH A  3223     O    HOH A  3224              2.10            
REMARK 500   O    HOH A  3095     O    HOH A  3232              2.11            
REMARK 500   O    HOH A  3036     O    HOH A  3084              2.11            
REMARK 500   OG   SER B   123     O    HOH B  3021              2.12            
REMARK 500   O    HOH A  3331     O    HOH A  3332              2.13            
REMARK 500   NH2  ARG I   493     O    HOH A  3155              2.13            
REMARK 500   O    HOH A  3093     O    HOH A  3230              2.14            
REMARK 500   ND2  ASN D   371     C2   NAG D  3371              2.14            
REMARK 500   O    HOH A  3174     O    HOH A  3175              2.14            
REMARK 500   O    HOH A  3334     O    HOH A  3335              2.14            
REMARK 500   OG   SER A   344     O    HOH A  3265              2.15            
REMARK 500   O    HOH D  3058     O    HOH J  3001              2.15            
REMARK 500   OG1  THR A   413     O    HOH A  3331              2.15            
REMARK 500   O1   SO4 C  1458     O    HOH C  3191              2.15            
REMARK 500   O    HOH B  3107     O    HOH B  3117              2.16            
REMARK 500   O    HOH B  3101     O    HOH B  3102              2.16            
REMARK 500   O    HOH B  3038     O    HOH B  3040              2.17            
REMARK 500   O1   SO4 A  1462     O    HOH A  3332              2.17            
REMARK 500   O    HOH B  3014     O    HOH B  3121              2.17            
REMARK 500   OE1  GLN L    38     O    HOH H  3008              2.18            
REMARK 500   ND2  ASN B   371     C2   NAG B  3371              2.18            
REMARK 500   O    GLY I   492     O    HOH I  3001              2.18            
REMARK 500   OG   SER C   384     O    HOH C  3159              2.18            
REMARK 500   O    HOH C  3047     O    HOH C  3127              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O2   SO4 A  1462     O    HOH C  3163     1554     2.04            
REMARK 500   O2   SO4 A  1462     O    HOH C  3175     1554     2.06            
REMARK 500   O    HOH A  3352     O    HOH C  3174     1554     2.12            
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    SER A  46       37.59    -90.60                                   
REMARK 500    SER A 101     -128.42     51.97                                   
REMARK 500    LYS A 118     -115.00     56.35                                   
REMARK 500    GLU A 123      133.34    101.60                                   
REMARK 500    LEU A 212      -45.33     76.82                                   
REMARK 500    THR A 296      141.96   -177.74                                   
REMARK 500    ASP A 319       35.29     76.94                                   
REMARK 500    PRO B  32      176.25    -51.43                                   
REMARK 500    ASP B  66       51.33   -141.19                                   
REMARK 500    ASP B  76      141.75     63.45                                   
REMARK 500    VAL B 157      -81.93   -128.58                                   
REMARK 500    ASP B 179       41.33    -92.02                                   
REMARK 500    MET B 180       20.64   -149.23                                   
REMARK 500    SER B 213     -155.22   -118.98                                   
REMARK 500    ASP B 241       77.97   -106.38                                   
REMARK 500    LEU B 258      -15.12     94.80                                   
REMARK 500    HIS B 274       33.59   -141.49                                   
REMARK 500    ARG B 352       30.31    -95.22                                   
REMARK 500    LEU B 375     -114.15     50.86                                   
REMARK 500    ASN B 376       76.18   -114.60                                   
REMARK 500    GLN B 440       41.58   -153.88                                   
REMARK 500    SER C 101     -115.75     59.10                                   
REMARK 500    LYS C 118     -106.60     62.92                                   
REMARK 500    GLU C 123      135.92     91.64                                   
REMARK 500    LEU C 212      -36.65     73.45                                   
REMARK 500    THR C 296      144.70   -171.45                                   
REMARK 500    THR D   7       36.11    -87.41                                   
REMARK 500    PHE D  56       76.26   -157.73                                   
REMARK 500    VAL D 157      -75.36   -135.14                                   
REMARK 500    SER D 213     -153.72   -122.87                                   
REMARK 500    ASP D 241       74.49   -111.44                                   
REMARK 500    LEU D 258       -2.96     85.28                                   
REMARK 500    HIS D 274       39.02   -142.72                                   
REMARK 500    ASP D 361       35.30     71.20                                   
REMARK 500    CYS D 374     -118.07    -88.28                                   
REMARK 500    ASN D 376     -157.05     53.30                                   
REMARK 500    ASN D 377       45.55    -95.54                                   
REMARK 500    ASN E  55      -44.91   -138.04                                   
REMARK 500    LYS E  67      -66.71   -106.21                                   
REMARK 500    LEU E 100      -71.57    -93.69                                   
REMARK 500    TYR E 101      -62.79   -108.69                                   
REMARK 500    PRO E 132      172.39    -58.27                                   
REMARK 500    PHE E 152      140.38   -173.82                                   
REMARK 500    PRO E 155     -168.92   -104.45                                   
REMARK 500    SER E 178       75.23     39.28                                   
REMARK 500    ASP E 179       -1.39     71.39                                   
REMARK 500    SER F  30       65.10     36.46                                   
REMARK 500    SER F  31       11.41     54.11                                   
REMARK 500    SER F  43     -159.60    -90.75                                   
REMARK 500    SER F  77       83.48     58.72                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      69 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A2004  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR A 250   O                                                      
REMARK 620 2 THR A 250   OG1  81.3                                              
REMARK 620 3 GLU A 243   OE1  73.3 144.1                                        
REMARK 620 4 GLU A 243   OE2 127.4 138.8  54.6                                  
REMARK 620 5 ASP A 245   OD1 165.5  84.3 118.6  64.1                            
REMARK 620 6 ASP A 247   O    87.5  75.3  78.6  77.2  87.1                      
REMARK 620 7 GLU A 252   OE1 107.6 124.0  88.2  79.1  82.0 156.3                
REMARK 620 8 GLU A 252   OE2  93.9  71.5 134.1 125.7  83.2 146.1  53.1          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A2005  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 297   OD1                                                    
REMARK 620 2 ARG A 303   O    74.7                                              
REMARK 620 3 ASN A 299   OD1  73.9 148.3                                        
REMARK 620 4 ASP A 301   OD1  70.1  85.4  80.1                                  
REMARK 620 5 ASP A 305   OD1 129.7  81.9 122.3 151.5                            
REMARK 620 6 ASP A 305   OD2  84.9  95.4  86.0 153.9  53.4                      
REMARK 620 7 HOH A3252   O   153.2 107.7  98.4  83.4  76.4 120.7                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A2006  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 365   OD1                                                    
REMARK 620 2 ASP A 367   OD1  83.2                                              
REMARK 620 3 ASP A 369   OD1  77.7  83.8                                        
REMARK 620 4 TYR A 371   O    74.6 157.8  90.1                                  
REMARK 620 5 ASP A 373   OD1 135.6 110.2 143.7  87.2                            
REMARK 620 6 ASP A 373   OD2  86.2  90.8 163.5  89.1  52.7                      
REMARK 620 7 HOH A3294   O   152.2 100.7  75.5  98.3  69.1 120.9                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A2007  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN A 430   OD1                                                    
REMARK 620 2 ASP A 426   OD1  87.1                                              
REMARK 620 3 TYR A 432   O    89.4  79.5                                        
REMARK 620 4 ASP A 428   OD1  83.7  71.2 150.2                                  
REMARK 620 5 ASP A 434   OD2 168.6  83.9  95.8  86.8                            
REMARK 620 6 HOH A3342   O    76.9 146.1 129.1  77.4 107.1                      
REMARK 620 7 ASP A 434   OD1 136.7 133.1  84.3 120.0  54.2  74.4                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B2001  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SER B 121   OG                                                     
REMARK 620 2 HOH B3020   O    75.5                                              
REMARK 620 3 HOH B3079   O   160.7  85.2                                        
REMARK 620 4 GLU B 220   OE2 107.2 105.1  78.2                                  
REMARK 620 5 ASP I 495   OD1  90.0 145.2 105.9 109.4                            
REMARK 620 6 HOH B3021   O    92.8  79.6  82.9 160.0  69.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B2002  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH B3023   O                                                      
REMARK 620 2 MET B 335   O    89.3                                              
REMARK 620 3 HOH B3022   O    92.0  72.4                                        
REMARK 620 4 ASP B 126   OD1  81.9 116.9 168.6                                  
REMARK 620 5 SER B 123   O    87.8 161.0  88.9  81.3                            
REMARK 620 6 ASP B 126   OD2  98.1  65.4 136.3  54.6 133.6                      
REMARK 620 7 ASP B 127   OD1 170.5  81.4  83.3 104.1 100.4  79.9                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B2003  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 217   O                                                      
REMARK 620 2 ASP B 158   OD2 163.8                                              
REMARK 620 3 ASP B 217   OD1  73.2  94.1                                        
REMARK 620 4 GLU B 220   OE1  99.3  94.5 169.5                                  
REMARK 620 5 ASN B 215   OD1  85.4 103.5  84.0  88.1                            
REMARK 620 6 PRO B 219   O    88.3  84.7 102.3  84.5 169.4                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA C2004  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP C 247   O                                                      
REMARK 620 2 ASP C 245   OD2 111.4                                              
REMARK 620 3 THR C 250   OG1  76.3  61.9                                        
REMARK 620 4 ASP C 245   OD1  73.6  54.5  87.9                                  
REMARK 620 5 GLU C 243   OE2  60.9 112.0 131.3  59.7                            
REMARK 620 6 THR C 250   O    85.5 132.9  81.9 158.4 114.5                      
REMARK 620 7 GLU C 243   OE1  81.7 155.0 143.1 113.9  54.7  67.0                
REMARK 620 8 GLU C 252   OE2 158.3  55.8  82.0 105.0 137.8  92.4 117.3          
REMARK 620 9 GLU C 252   OE1 145.7  77.5 132.5  87.6  84.9 113.3  80.1  53.9    
REMARK 620 N                    1     2     3     4     5     6     7     8     
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA C2005  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH C3129   O                                                      
REMARK 620 2 ASP C 305   OD2 105.9                                              
REMARK 620 3 ASP C 305   OD1  68.0  53.7                                        
REMARK 620 4 ARG C 303   O   112.9 105.1  86.2                                  
REMARK 620 5 ASP C 301   OD1  84.4 157.0 147.3  89.0                            
REMARK 620 6 ASN C 299   OD1  86.3  78.4 112.2 157.8  81.9                      
REMARK 620 7 ASP C 297   OD1 153.6  89.7 136.9  82.2  74.0  75.9                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA C2006  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP C 373   OD2                                                    
REMARK 620 2 TYR C 371   O    91.5                                              
REMARK 620 3 ASP C 369   OD1 159.2  94.9                                        
REMARK 620 4 ASP C 367   OD1  90.4 162.9  77.8                                  
REMARK 620 5 ASP C 365   OD1  93.8  73.3  69.3  89.6                            
REMARK 620 6 HOH C3154   O   123.4  94.1  75.9  99.1 141.4                      
REMARK 620 7 ASP C 373   OD1  52.9  82.7 147.6 111.8 138.5  72.1                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA C2007  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH C3184   O                                                      
REMARK 620 2 ASP C 434   OD2 115.9                                              
REMARK 620 3 ASP C 434   OD1  73.3  54.8                                        
REMARK 620 4 ASP C 428   OD1  74.0  89.2 109.3                                  
REMARK 620 5 ASP C 426   OD1 139.3  85.2 139.5  71.9                            
REMARK 620 6 TYR C 432   O   135.4  91.6  99.7 144.7  73.0                      
REMARK 620 7 ASN C 430   OD1  75.5 163.3 141.8  82.1  78.5  87.4                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG D2001  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH D3049   O                                                      
REMARK 620 2 SER D 121   OG  151.4                                              
REMARK 620 3 HOH D3016   O    73.0  79.9                                        
REMARK 620 4 HOH D3017   O    78.1 106.5  80.0                                  
REMARK 620 5 GLU D 220   OE2  76.5  96.6  93.9 154.6                            
REMARK 620 6 ASP J 495   OD1  92.8 113.9 165.7  98.4  81.4                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA D2002  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP D 126   OD1                                                    
REMARK 620 2 SER D 123   O    69.3                                              
REMARK 620 3 HOH D3021   O    94.5  81.7                                        
REMARK 620 4 ASP D 127   OD1  89.1 103.0 174.9                                  
REMARK 620 5 ASP D 126   OD2  54.2 121.5  88.5  90.6                            
REMARK 620 6 HOH D3020   O   164.3  95.0  83.5  94.1 141.0                      
REMARK 620 7 MET D 335   O   122.1 168.6  96.9  78.1  69.6  73.6                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA D2003  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP D 158   OD2                                                    
REMARK 620 2 ASP D 217   OD1  91.9                                              
REMARK 620 3 ASN D 215   OD1 113.8  83.6                                        
REMARK 620 4 PRO D 219   O    80.1  98.5 165.9                                  
REMARK 620 5 ASP D 217   O   160.5  71.1  74.8  92.6                            
REMARK 620 6 GLU D 220   OE1 100.4 167.7  92.1  83.0  96.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 2004                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 2005                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 2006                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 2007                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 2001                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 2002                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 2003                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 2004                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 2005                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 2006                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 2007                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG D 2001                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA D 2002                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA D 2003                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 1454                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 1455                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 1467                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 1472                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1455                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1456                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 L 1215                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1457                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 1456                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1458                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1459                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 1468                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1460                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 1469                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 1457                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 L 1216                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 1458                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1461                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1462                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1463                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: Binding site for Mono-Saccharide NAG B3319 bound   
REMARK 800  to ASN B 99                                                         
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: Binding site for Poly-Saccharide residues NAG      
REMARK 800  B3320 through MAN B3323 bound to ASN B 320                          
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: Binding site for Poly-Saccharide residues NAG      
REMARK 800  B3371 through NAG B3372 bound to ASN B 371                          
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: Binding site for Mono-Saccharide NAG D3319 bound   
REMARK 800  to ASN D 99                                                         
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: Binding site for Poly-Saccharide residues NAG      
REMARK 800  D3320 through MAN D3323 bound to ASN D 320                          
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: Binding site for Poly-Saccharide residues NAG      
REMARK 800  D3371 through NAG D3372 bound to ASN D 371                          
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3ZDX   RELATED DB: PDB                                   
REMARK 900 INTEGRIN ALPHAIIB BETA3 HEADPIECE AND RGD PEPTIDE COMPLEX            
REMARK 900 RELATED ID: 3ZDZ   RELATED DB: PDB                                   
REMARK 900 INTEGRIN ALPHAIIB BETA3 HEADPIECE AND RGD PEPTIDE COMPLEX            
REMARK 900 RELATED ID: 3ZE0   RELATED DB: PDB                                   
REMARK 900 INTEGRIN ALPHAIIB BETA3 HEADPIECE AND RGD PEPTIDE COMPLEX            
REMARK 900 RELATED ID: 3ZE1   RELATED DB: PDB                                   
REMARK 900 INTEGRIN ALPHAIIB BETA3 HEADPIECE AND RGD PEPTIDE COMPLEX            
REMARK 900 RELATED ID: 3ZE2   RELATED DB: PDB                                   
REMARK 900 INTEGRIN ALPHAIIB BETA3 HEADPIECE AND RGD PEPTIDE COMPLEX            
DBREF  3ZDY A    1   457  UNP    P08514   ITA2B_HUMAN     32    488             
DBREF  3ZDY B    1   472  UNP    P05106   ITB3_HUMAN      27    498             
DBREF  3ZDY C    1   457  UNP    P08514   ITA2B_HUMAN     32    488             
DBREF  3ZDY D    1   472  UNP    P05106   ITB3_HUMAN      27    498             
DBREF  3ZDY E    1   221  PDB    3ZDY     3ZDY             1    221             
DBREF  3ZDY F    1   214  PDB    3ZDY     3ZDY             1    214             
DBREF  3ZDY H    1   221  PDB    3ZDY     3ZDY             1    221             
DBREF  3ZDY I  492   497  PDB    3ZDY     3ZDY           492    497             
DBREF  3ZDY J  492   497  PDB    3ZDY     3ZDY           492    497             
DBREF  3ZDY L    1   214  PDB    3ZDY     3ZDY             1    214             
SEQRES   1 A  457  LEU ASN LEU ASP PRO VAL GLN LEU THR PHE TYR ALA GLY          
SEQRES   2 A  457  PRO ASN GLY SER GLN PHE GLY PHE SER LEU ASP PHE HIS          
SEQRES   3 A  457  LYS ASP SER HIS GLY ARG VAL ALA ILE VAL VAL GLY ALA          
SEQRES   4 A  457  PRO ARG THR LEU GLY PRO SER GLN GLU GLU THR GLY GLY          
SEQRES   5 A  457  VAL PHE LEU CYS PRO TRP ARG ALA GLU GLY GLY GLN CYS          
SEQRES   6 A  457  PRO SER LEU LEU PHE ASP LEU ARG ASP GLU THR ARG ASN          
SEQRES   7 A  457  VAL GLY SER GLN THR LEU GLN THR PHE LYS ALA ARG GLN          
SEQRES   8 A  457  GLY LEU GLY ALA SER VAL VAL SER TRP SER ASP VAL ILE          
SEQRES   9 A  457  VAL ALA CYS ALA PRO TRP GLN HIS TRP ASN VAL LEU GLU          
SEQRES  10 A  457  LYS THR GLU GLU ALA GLU LYS THR PRO VAL GLY SER CYS          
SEQRES  11 A  457  PHE LEU ALA GLN PRO GLU SER GLY ARG ARG ALA GLU TYR          
SEQRES  12 A  457  SER PRO CYS ARG GLY ASN THR LEU SER ARG ILE TYR VAL          
SEQRES  13 A  457  GLU ASN ASP PHE SER TRP ASP LYS ARG TYR CYS GLU ALA          
SEQRES  14 A  457  GLY PHE SER SER VAL VAL THR GLN ALA GLY GLU LEU VAL          
SEQRES  15 A  457  LEU GLY ALA PRO GLY GLY TYR TYR PHE LEU GLY LEU LEU          
SEQRES  16 A  457  ALA GLN ALA PRO VAL ALA ASP ILE PHE SER SER TYR ARG          
SEQRES  17 A  457  PRO GLY ILE LEU LEU TRP HIS VAL SER SER GLN SER LEU          
SEQRES  18 A  457  SER PHE ASP SER SER ASN PRO GLU TYR PHE ASP GLY TYR          
SEQRES  19 A  457  TRP GLY TYR SER VAL ALA VAL GLY GLU PHE ASP GLY ASP          
SEQRES  20 A  457  LEU ASN THR THR GLU TYR VAL VAL GLY ALA PRO THR TRP          
SEQRES  21 A  457  SER TRP THR LEU GLY ALA VAL GLU ILE LEU ASP SER TYR          
SEQRES  22 A  457  TYR GLN ARG LEU HIS ARG LEU ARG GLY GLU GLN MET ALA          
SEQRES  23 A  457  SER TYR PHE GLY HIS SER VAL ALA VAL THR ASP VAL ASN          
SEQRES  24 A  457  GLY ASP GLY ARG HIS ASP LEU LEU VAL GLY ALA PRO LEU          
SEQRES  25 A  457  TYR MET GLU SER ARG ALA ASP ARG LYS LEU ALA GLU VAL          
SEQRES  26 A  457  GLY ARG VAL TYR LEU PHE LEU GLN PRO ARG GLY PRO HIS          
SEQRES  27 A  457  ALA LEU GLY ALA PRO SER LEU LEU LEU THR GLY THR GLN          
SEQRES  28 A  457  LEU TYR GLY ARG PHE GLY SER ALA ILE ALA PRO LEU GLY          
SEQRES  29 A  457  ASP LEU ASP ARG ASP GLY TYR ASN ASP ILE ALA VAL ALA          
SEQRES  30 A  457  ALA PRO TYR GLY GLY PRO SER GLY ARG GLY GLN VAL LEU          
SEQRES  31 A  457  VAL PHE LEU GLY GLN SER GLU GLY LEU ARG SER ARG PRO          
SEQRES  32 A  457  SER GLN VAL LEU ASP SER PRO PHE PRO THR GLY SER ALA          
SEQRES  33 A  457  PHE GLY PHE SER LEU ARG GLY ALA VAL ASP ILE ASP ASP          
SEQRES  34 A  457  ASN GLY TYR PRO ASP LEU ILE VAL GLY ALA TYR GLY ALA          
SEQRES  35 A  457  ASN GLN VAL ALA VAL TYR ARG ALA GLN PRO VAL VAL LYS          
SEQRES  36 A  457  ALA SER                                                      
SEQRES   1 B  472  GLY PRO ASN ILE CYS THR THR ARG GLY VAL SER SER CYS          
SEQRES   2 B  472  GLN GLN CYS LEU ALA VAL SER PRO MET CYS ALA TRP CYS          
SEQRES   3 B  472  SER ASP GLU ALA LEU PRO LEU GLY SER PRO ARG CYS ASP          
SEQRES   4 B  472  LEU LYS GLU ASN LEU LEU LYS ASP ASN CYS ALA PRO GLU          
SEQRES   5 B  472  SER ILE GLU PHE PRO VAL SER GLU ALA ARG VAL LEU GLU          
SEQRES   6 B  472  ASP ARG PRO LEU SER ASP LYS GLY SER GLY ASP SER SER          
SEQRES   7 B  472  GLN VAL THR GLN VAL SER PRO GLN ARG ILE ALA LEU ARG          
SEQRES   8 B  472  LEU ARG PRO ASP ASP SER LYS ASN PHE SER ILE GLN VAL          
SEQRES   9 B  472  ARG GLN VAL GLU ASP TYR PRO VAL ASP ILE TYR TYR LEU          
SEQRES  10 B  472  MET ASP LEU SER TYR SER MET LYS ASP ASP LEU TRP SER          
SEQRES  11 B  472  ILE GLN ASN LEU GLY THR LYS LEU ALA THR GLN MET ARG          
SEQRES  12 B  472  LYS LEU THR SER ASN LEU ARG ILE GLY PHE GLY ALA PHE          
SEQRES  13 B  472  VAL ASP LYS PRO VAL SER PRO TYR MET TYR ILE SER PRO          
SEQRES  14 B  472  PRO GLU ALA LEU GLU ASN PRO CYS TYR ASP MET LYS THR          
SEQRES  15 B  472  THR CYS LEU PRO MET PHE GLY TYR LYS HIS VAL LEU THR          
SEQRES  16 B  472  LEU THR ASP GLN VAL THR ARG PHE ASN GLU GLU VAL LYS          
SEQRES  17 B  472  LYS GLN SER VAL SER ARG ASN ARG ASP ALA PRO GLU GLY          
SEQRES  18 B  472  GLY PHE ASP ALA ILE MET GLN ALA THR VAL CYS ASP GLU          
SEQRES  19 B  472  LYS ILE GLY TRP ARG ASN ASP ALA SER HIS LEU LEU VAL          
SEQRES  20 B  472  PHE THR THR ASP ALA LYS THR HIS ILE ALA LEU ASP GLY          
SEQRES  21 B  472  ARG LEU ALA GLY ILE VAL GLN PRO ASN ASP GLY GLN CYS          
SEQRES  22 B  472  HIS VAL GLY SER ASP ASN HIS TYR SER ALA SER THR THR          
SEQRES  23 B  472  MET ASP TYR PRO SER LEU GLY LEU MET THR GLU LYS LEU          
SEQRES  24 B  472  SER GLN LYS ASN ILE ASN LEU ILE PHE ALA VAL THR GLU          
SEQRES  25 B  472  ASN VAL VAL ASN LEU TYR GLN ASN TYR SER GLU LEU ILE          
SEQRES  26 B  472  PRO GLY THR THR VAL GLY VAL LEU SER MET ASP SER SER          
SEQRES  27 B  472  ASN VAL LEU GLN LEU ILE VAL ASP ALA TYR GLY LYS ILE          
SEQRES  28 B  472  ARG SER LYS VAL GLU LEU GLU VAL ARG ASP LEU PRO GLU          
SEQRES  29 B  472  GLU LEU SER LEU SER PHE ASN ALA THR CYS LEU ASN ASN          
SEQRES  30 B  472  GLU VAL ILE PRO GLY LEU LYS SER CYS MET GLY LEU LYS          
SEQRES  31 B  472  ILE GLY ASP THR VAL SER PHE SER ILE GLU ALA LYS VAL          
SEQRES  32 B  472  ARG GLY CYS PRO GLN GLU LYS GLU LYS SER PHE THR ILE          
SEQRES  33 B  472  LYS PRO VAL GLY PHE LYS ASP SER LEU ILE VAL GLN VAL          
SEQRES  34 B  472  THR PHE ASP CYS ASP CYS ALA CYS GLN ALA GLN ALA GLU          
SEQRES  35 B  472  PRO ASN SER HIS ARG CYS ASN ASN GLY ASN GLY THR PHE          
SEQRES  36 B  472  GLU CYS GLY VAL CYS ARG CYS GLY PRO GLY TRP LEU GLY          
SEQRES  37 B  472  SER GLN CYS GLU                                              
SEQRES   1 C  457  LEU ASN LEU ASP PRO VAL GLN LEU THR PHE TYR ALA GLY          
SEQRES   2 C  457  PRO ASN GLY SER GLN PHE GLY PHE SER LEU ASP PHE HIS          
SEQRES   3 C  457  LYS ASP SER HIS GLY ARG VAL ALA ILE VAL VAL GLY ALA          
SEQRES   4 C  457  PRO ARG THR LEU GLY PRO SER GLN GLU GLU THR GLY GLY          
SEQRES   5 C  457  VAL PHE LEU CYS PRO TRP ARG ALA GLU GLY GLY GLN CYS          
SEQRES   6 C  457  PRO SER LEU LEU PHE ASP LEU ARG ASP GLU THR ARG ASN          
SEQRES   7 C  457  VAL GLY SER GLN THR LEU GLN THR PHE LYS ALA ARG GLN          
SEQRES   8 C  457  GLY LEU GLY ALA SER VAL VAL SER TRP SER ASP VAL ILE          
SEQRES   9 C  457  VAL ALA CYS ALA PRO TRP GLN HIS TRP ASN VAL LEU GLU          
SEQRES  10 C  457  LYS THR GLU GLU ALA GLU LYS THR PRO VAL GLY SER CYS          
SEQRES  11 C  457  PHE LEU ALA GLN PRO GLU SER GLY ARG ARG ALA GLU TYR          
SEQRES  12 C  457  SER PRO CYS ARG GLY ASN THR LEU SER ARG ILE TYR VAL          
SEQRES  13 C  457  GLU ASN ASP PHE SER TRP ASP LYS ARG TYR CYS GLU ALA          
SEQRES  14 C  457  GLY PHE SER SER VAL VAL THR GLN ALA GLY GLU LEU VAL          
SEQRES  15 C  457  LEU GLY ALA PRO GLY GLY TYR TYR PHE LEU GLY LEU LEU          
SEQRES  16 C  457  ALA GLN ALA PRO VAL ALA ASP ILE PHE SER SER TYR ARG          
SEQRES  17 C  457  PRO GLY ILE LEU LEU TRP HIS VAL SER SER GLN SER LEU          
SEQRES  18 C  457  SER PHE ASP SER SER ASN PRO GLU TYR PHE ASP GLY TYR          
SEQRES  19 C  457  TRP GLY TYR SER VAL ALA VAL GLY GLU PHE ASP GLY ASP          
SEQRES  20 C  457  LEU ASN THR THR GLU TYR VAL VAL GLY ALA PRO THR TRP          
SEQRES  21 C  457  SER TRP THR LEU GLY ALA VAL GLU ILE LEU ASP SER TYR          
SEQRES  22 C  457  TYR GLN ARG LEU HIS ARG LEU ARG GLY GLU GLN MET ALA          
SEQRES  23 C  457  SER TYR PHE GLY HIS SER VAL ALA VAL THR ASP VAL ASN          
SEQRES  24 C  457  GLY ASP GLY ARG HIS ASP LEU LEU VAL GLY ALA PRO LEU          
SEQRES  25 C  457  TYR MET GLU SER ARG ALA ASP ARG LYS LEU ALA GLU VAL          
SEQRES  26 C  457  GLY ARG VAL TYR LEU PHE LEU GLN PRO ARG GLY PRO HIS          
SEQRES  27 C  457  ALA LEU GLY ALA PRO SER LEU LEU LEU THR GLY THR GLN          
SEQRES  28 C  457  LEU TYR GLY ARG PHE GLY SER ALA ILE ALA PRO LEU GLY          
SEQRES  29 C  457  ASP LEU ASP ARG ASP GLY TYR ASN ASP ILE ALA VAL ALA          
SEQRES  30 C  457  ALA PRO TYR GLY GLY PRO SER GLY ARG GLY GLN VAL LEU          
SEQRES  31 C  457  VAL PHE LEU GLY GLN SER GLU GLY LEU ARG SER ARG PRO          
SEQRES  32 C  457  SER GLN VAL LEU ASP SER PRO PHE PRO THR GLY SER ALA          
SEQRES  33 C  457  PHE GLY PHE SER LEU ARG GLY ALA VAL ASP ILE ASP ASP          
SEQRES  34 C  457  ASN GLY TYR PRO ASP LEU ILE VAL GLY ALA TYR GLY ALA          
SEQRES  35 C  457  ASN GLN VAL ALA VAL TYR ARG ALA GLN PRO VAL VAL LYS          
SEQRES  36 C  457  ALA SER                                                      
SEQRES   1 D  472  GLY PRO ASN ILE CYS THR THR ARG GLY VAL SER SER CYS          
SEQRES   2 D  472  GLN GLN CYS LEU ALA VAL SER PRO MET CYS ALA TRP CYS          
SEQRES   3 D  472  SER ASP GLU ALA LEU PRO LEU GLY SER PRO ARG CYS ASP          
SEQRES   4 D  472  LEU LYS GLU ASN LEU LEU LYS ASP ASN CYS ALA PRO GLU          
SEQRES   5 D  472  SER ILE GLU PHE PRO VAL SER GLU ALA ARG VAL LEU GLU          
SEQRES   6 D  472  ASP ARG PRO LEU SER ASP LYS GLY SER GLY ASP SER SER          
SEQRES   7 D  472  GLN VAL THR GLN VAL SER PRO GLN ARG ILE ALA LEU ARG          
SEQRES   8 D  472  LEU ARG PRO ASP ASP SER LYS ASN PHE SER ILE GLN VAL          
SEQRES   9 D  472  ARG GLN VAL GLU ASP TYR PRO VAL ASP ILE TYR TYR LEU          
SEQRES  10 D  472  MET ASP LEU SER TYR SER MET LYS ASP ASP LEU TRP SER          
SEQRES  11 D  472  ILE GLN ASN LEU GLY THR LYS LEU ALA THR GLN MET ARG          
SEQRES  12 D  472  LYS LEU THR SER ASN LEU ARG ILE GLY PHE GLY ALA PHE          
SEQRES  13 D  472  VAL ASP LYS PRO VAL SER PRO TYR MET TYR ILE SER PRO          
SEQRES  14 D  472  PRO GLU ALA LEU GLU ASN PRO CYS TYR ASP MET LYS THR          
SEQRES  15 D  472  THR CYS LEU PRO MET PHE GLY TYR LYS HIS VAL LEU THR          
SEQRES  16 D  472  LEU THR ASP GLN VAL THR ARG PHE ASN GLU GLU VAL LYS          
SEQRES  17 D  472  LYS GLN SER VAL SER ARG ASN ARG ASP ALA PRO GLU GLY          
SEQRES  18 D  472  GLY PHE ASP ALA ILE MET GLN ALA THR VAL CYS ASP GLU          
SEQRES  19 D  472  LYS ILE GLY TRP ARG ASN ASP ALA SER HIS LEU LEU VAL          
SEQRES  20 D  472  PHE THR THR ASP ALA LYS THR HIS ILE ALA LEU ASP GLY          
SEQRES  21 D  472  ARG LEU ALA GLY ILE VAL GLN PRO ASN ASP GLY GLN CYS          
SEQRES  22 D  472  HIS VAL GLY SER ASP ASN HIS TYR SER ALA SER THR THR          
SEQRES  23 D  472  MET ASP TYR PRO SER LEU GLY LEU MET THR GLU LYS LEU          
SEQRES  24 D  472  SER GLN LYS ASN ILE ASN LEU ILE PHE ALA VAL THR GLU          
SEQRES  25 D  472  ASN VAL VAL ASN LEU TYR GLN ASN TYR SER GLU LEU ILE          
SEQRES  26 D  472  PRO GLY THR THR VAL GLY VAL LEU SER MET ASP SER SER          
SEQRES  27 D  472  ASN VAL LEU GLN LEU ILE VAL ASP ALA TYR GLY LYS ILE          
SEQRES  28 D  472  ARG SER LYS VAL GLU LEU GLU VAL ARG ASP LEU PRO GLU          
SEQRES  29 D  472  GLU LEU SER LEU SER PHE ASN ALA THR CYS LEU ASN ASN          
SEQRES  30 D  472  GLU VAL ILE PRO GLY LEU LYS SER CYS MET GLY LEU LYS          
SEQRES  31 D  472  ILE GLY ASP THR VAL SER PHE SER ILE GLU ALA LYS VAL          
SEQRES  32 D  472  ARG GLY CYS PRO GLN GLU LYS GLU LYS SER PHE THR ILE          
SEQRES  33 D  472  LYS PRO VAL GLY PHE LYS ASP SER LEU ILE VAL GLN VAL          
SEQRES  34 D  472  THR PHE ASP CYS ASP CYS ALA CYS GLN ALA GLN ALA GLU          
SEQRES  35 D  472  PRO ASN SER HIS ARG CYS ASN ASN GLY ASN GLY THR PHE          
SEQRES  36 D  472  GLU CYS GLY VAL CYS ARG CYS GLY PRO GLY TRP LEU GLY          
SEQRES  37 D  472  SER GLN CYS GLU                                              
SEQRES   1 E  221  GLU VAL GLN LEU GLN GLN SER GLY ALA GLU LEU VAL LYS          
SEQRES   2 E  221  PRO GLY ALA SER VAL LYS LEU SER CYS THR ALA SER GLY          
SEQRES   3 E  221  PHE ASN ILE LYS ASP THR TYR VAL HIS TRP VAL LYS GLN          
SEQRES   4 E  221  ARG PRO GLU GLN GLY LEU GLU TRP ILE GLY ARG ILE ASP          
SEQRES   5 E  221  PRO ALA ASN GLY TYR THR LYS TYR ASP PRO LYS PHE GLN          
SEQRES   6 E  221  GLY LYS ALA THR ILE THR ALA ASP THR SER SER ASN THR          
SEQRES   7 E  221  ALA TYR LEU GLN LEU SER SER LEU THR SER GLU ASP THR          
SEQRES   8 E  221  ALA VAL TYR TYR CYS VAL ARG PRO LEU TYR ASP TYR TYR          
SEQRES   9 E  221  ALA MET ASP TYR TRP GLY GLN GLY THR SER VAL THR VAL          
SEQRES  10 E  221  SER SER ALA LYS THR THR ALA PRO SER VAL TYR PRO LEU          
SEQRES  11 E  221  ALA PRO VAL CYS GLY ASP THR THR GLY SER SER VAL THR          
SEQRES  12 E  221  LEU GLY CYS LEU VAL LYS GLY TYR PHE PRO GLU PRO VAL          
SEQRES  13 E  221  THR LEU THR TRP ASN SER GLY SER LEU SER SER GLY VAL          
SEQRES  14 E  221  HIS THR PHE PRO ALA VAL LEU GLN SER ASP LEU TYR THR          
SEQRES  15 E  221  LEU SER SER SER VAL THR VAL THR SER SER THR TRP PRO          
SEQRES  16 E  221  SER GLN SER ILE THR CYS ASN VAL ALA HIS PRO ALA SER          
SEQRES  17 E  221  SER THR LYS VAL ASP LYS LYS ILE GLU PRO ARG GLY PRO          
SEQRES   1 F  214  ASP ILE LEU MET THR GLN SER PRO SER SER MET SER VAL          
SEQRES   2 F  214  SER LEU GLY ASP THR VAL SER ILE THR CYS HIS ALA SER          
SEQRES   3 F  214  GLN GLY ILE SER SER ASN ILE GLY TRP LEU GLN GLN LYS          
SEQRES   4 F  214  PRO GLY LYS SER PHE MET GLY LEU ILE TYR TYR GLY THR          
SEQRES   5 F  214  ASN LEU VAL ASP GLY VAL PRO SER ARG PHE SER GLY SER          
SEQRES   6 F  214  GLY SER GLY ALA ASP TYR SER LEU THR ILE SER SER LEU          
SEQRES   7 F  214  ASP SER GLU ASP PHE ALA ASP TYR TYR CYS VAL GLN TYR          
SEQRES   8 F  214  ALA GLN LEU PRO TYR THR PHE GLY GLY GLY THR LYS LEU          
SEQRES   9 F  214  GLU ILE LYS ARG ALA ASP ALA ALA PRO THR VAL SER ILE          
SEQRES  10 F  214  PHE PRO PRO SER SER GLU GLN LEU THR SER GLY GLY ALA          
SEQRES  11 F  214  SER VAL VAL CYS PHE LEU ASN ASN PHE TYR PRO LYS ASP          
SEQRES  12 F  214  ILE ASN VAL LYS TRP LYS ILE ASP GLY SER GLU ARG GLN          
SEQRES  13 F  214  ASN GLY VAL LEU ASN SER TRP THR ASP GLN ASP SER LYS          
SEQRES  14 F  214  ASP SER THR TYR SER MET SER SER THR LEU THR LEU THR          
SEQRES  15 F  214  LYS ASP GLU TYR GLU ARG HIS ASN SER TYR THR CYS GLU          
SEQRES  16 F  214  ALA THR HIS LYS THR SER THR SER PRO ILE VAL LYS SER          
SEQRES  17 F  214  PHE ASN ARG ASN GLU CYS                                      
SEQRES   1 H  221  GLU VAL GLN LEU GLN GLN SER GLY ALA GLU LEU VAL LYS          
SEQRES   2 H  221  PRO GLY ALA SER VAL LYS LEU SER CYS THR ALA SER GLY          
SEQRES   3 H  221  PHE ASN ILE LYS ASP THR TYR VAL HIS TRP VAL LYS GLN          
SEQRES   4 H  221  ARG PRO GLU GLN GLY LEU GLU TRP ILE GLY ARG ILE ASP          
SEQRES   5 H  221  PRO ALA ASN GLY TYR THR LYS TYR ASP PRO LYS PHE GLN          
SEQRES   6 H  221  GLY LYS ALA THR ILE THR ALA ASP THR SER SER ASN THR          
SEQRES   7 H  221  ALA TYR LEU GLN LEU SER SER LEU THR SER GLU ASP THR          
SEQRES   8 H  221  ALA VAL TYR TYR CYS VAL ARG PRO LEU TYR ASP TYR TYR          
SEQRES   9 H  221  ALA MET ASP TYR TRP GLY GLN GLY THR SER VAL THR VAL          
SEQRES  10 H  221  SER SER ALA LYS THR THR ALA PRO SER VAL TYR PRO LEU          
SEQRES  11 H  221  ALA PRO VAL CYS GLY ASP THR THR GLY SER SER VAL THR          
SEQRES  12 H  221  LEU GLY CYS LEU VAL LYS GLY TYR PHE PRO GLU PRO VAL          
SEQRES  13 H  221  THR LEU THR TRP ASN SER GLY SER LEU SER SER GLY VAL          
SEQRES  14 H  221  HIS THR PHE PRO ALA VAL LEU GLN SER ASP LEU TYR THR          
SEQRES  15 H  221  LEU SER SER SER VAL THR VAL THR SER SER THR TRP PRO          
SEQRES  16 H  221  SER GLN SER ILE THR CYS ASN VAL ALA HIS PRO ALA SER          
SEQRES  17 H  221  SER THR LYS VAL ASP LYS LYS ILE GLU PRO ARG GLY PRO          
SEQRES   1 I    6  GLY ARG GLY ASP SER PRO                                      
SEQRES   1 J    6  GLY ARG GLY ASP SER PRO                                      
SEQRES   1 L  214  ASP ILE LEU MET THR GLN SER PRO SER SER MET SER VAL          
SEQRES   2 L  214  SER LEU GLY ASP THR VAL SER ILE THR CYS HIS ALA SER          
SEQRES   3 L  214  GLN GLY ILE SER SER ASN ILE GLY TRP LEU GLN GLN LYS          
SEQRES   4 L  214  PRO GLY LYS SER PHE MET GLY LEU ILE TYR TYR GLY THR          
SEQRES   5 L  214  ASN LEU VAL ASP GLY VAL PRO SER ARG PHE SER GLY SER          
SEQRES   6 L  214  GLY SER GLY ALA ASP TYR SER LEU THR ILE SER SER LEU          
SEQRES   7 L  214  ASP SER GLU ASP PHE ALA ASP TYR TYR CYS VAL GLN TYR          
SEQRES   8 L  214  ALA GLN LEU PRO TYR THR PHE GLY GLY GLY THR LYS LEU          
SEQRES   9 L  214  GLU ILE LYS ARG ALA ASP ALA ALA PRO THR VAL SER ILE          
SEQRES  10 L  214  PHE PRO PRO SER SER GLU GLN LEU THR SER GLY GLY ALA          
SEQRES  11 L  214  SER VAL VAL CYS PHE LEU ASN ASN PHE TYR PRO LYS ASP          
SEQRES  12 L  214  ILE ASN VAL LYS TRP LYS ILE ASP GLY SER GLU ARG GLN          
SEQRES  13 L  214  ASN GLY VAL LEU ASN SER TRP THR ASP GLN ASP SER LYS          
SEQRES  14 L  214  ASP SER THR TYR SER MET SER SER THR LEU THR LEU THR          
SEQRES  15 L  214  LYS ASP GLU TYR GLU ARG HIS ASN SER TYR THR CYS GLU          
SEQRES  16 L  214  ALA THR HIS LYS THR SER THR SER PRO ILE VAL LYS SER          
SEQRES  17 L  214  PHE ASN ARG ASN GLU CYS                                      
MODRES 3ZDY ASN B   99  ASN  GLYCOSYLATION SITE                                 
MODRES 3ZDY ASN B  320  ASN  GLYCOSYLATION SITE                                 
MODRES 3ZDY ASN B  371  ASN  GLYCOSYLATION SITE                                 
MODRES 3ZDY ASN D   99  ASN  GLYCOSYLATION SITE                                 
MODRES 3ZDY ASN D  320  ASN  GLYCOSYLATION SITE                                 
MODRES 3ZDY ASN D  371  ASN  GLYCOSYLATION SITE                                 
HET    SO4  A1455       5                                                       
HET    SO4  A1456       5                                                       
HET    SO4  A1457       5                                                       
HET    SO4  A1458       5                                                       
HET    SO4  A1459       5                                                       
HET    SO4  A1460       5                                                       
HET    SO4  A1461       5                                                       
HET    SO4  A1462       5                                                       
HET    SO4  A1463       5                                                       
HET     CA  A2004       1                                                       
HET     CA  A2005       1                                                       
HET     CA  A2006       1                                                       
HET     CA  A2007       1                                                       
HET    SO4  B1467       5                                                       
HET    SO4  B1468       5                                                       
HET    SO4  B1469       5                                                       
HET     MG  B2001       1                                                       
HET     CA  B2002       1                                                       
HET     CA  B2003       1                                                       
HET    NAG  B3319      27                                                       
HET    NAG  B3320      26                                                       
HET    NAG  B3321      26                                                       
HET    BMA  B3322      20                                                       
HET    MAN  B3323      21                                                       
HET    NAG  B3371      26                                                       
HET    NAG  B3372      27                                                       
HET    SO4  C1454       5                                                       
HET    SO4  C1455       5                                                       
HET    SO4  C1456       5                                                       
HET    SO4  C1457       5                                                       
HET    SO4  C1458       5                                                       
HET     CA  C2004       1                                                       
HET     CA  C2005       1                                                       
HET     CA  C2006       1                                                       
HET     CA  C2007       1                                                       
HET    SO4  D1472       5                                                       
HET     MG  D2001       1                                                       
HET     CA  D2002       1                                                       
HET     CA  D2003       1                                                       
HET    NAG  D3319      27                                                       
HET    NAG  D3320      26                                                       
HET    NAG  D3321      26                                                       
HET    BMA  D3322      20                                                       
HET    MAN  D3323      21                                                       
HET    NAG  D3371      26                                                       
HET    NAG  D3372      27                                                       
HET    SO4  L1215       5                                                       
HET    SO4  L1216       5                                                       
HETNAM     SO4 SULFATE ION                                                      
HETNAM      CA CALCIUM ION                                                      
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     BMA BETA-D-MANNOSE                                                   
HETNAM     MAN ALPHA-D-MANNOSE                                                  
FORMUL  11  SO4    20(O4 S 2-)                                                  
FORMUL  20   CA    12(CA 2+)                                                    
FORMUL  27   MG    2(MG 2+)                                                     
FORMUL  30  NAG    10(C8 H15 N O6)                                              
FORMUL  31  BMA    2(C6 H12 O6)                                                 
FORMUL  31  MAN    2(C6 H12 O6)                                                 
FORMUL  51  HOH   *887(H2 O)                                                    
HELIX    1   1 LEU A  151  ASN A  158  1                                   8    
HELIX    2   2 GLY A  187  LEU A  192  1                                   6    
HELIX    3   3 VAL A  200  TYR A  207  1                                   8    
HELIX    4   4 ASN A  227  PHE A  231  5                                   5    
HELIX    5   5 THR A  259  LEU A  264  1                                   6    
HELIX    6   6 TYR A  440  ALA A  442  5                                   3    
HELIX    7   7 ASN B    3  ARG B    8  1                                   6    
HELIX    8   8 SER B   12  SER B   20  1                                   9    
HELIX    9   9 LYS B   41  LYS B   46  1                                   6    
HELIX   10  10 SER B  121  LYS B  125  5                                   5    
HELIX   11  11 ASP B  126  ILE B  131  1                                   6    
HELIX   12  12 ASN B  133  ARG B  143  1                                  11    
HELIX   13  13 PRO B  170  ASN B  175  1                                   6    
HELIX   14  14 CYS B  177  LYS B  181  5                                   5    
HELIX   15  15 VAL B  200  GLN B  210  1                                  11    
HELIX   16  16 GLY B  221  CYS B  232  1                                  12    
HELIX   17  17 CYS B  232  GLY B  237  1                                   6    
HELIX   18  18 LEU B  258  GLY B  264  5                                   7    
HELIX   19  19 SER B  291  LYS B  302  1                                  12    
HELIX   20  20 VAL B  314  GLU B  323  1                                  10    
HELIX   21  21 ASN B  339  ARG B  352  1                                  14    
HELIX   22  22 CYS B  435  ALA B  441  5                                   7    
HELIX   23  23 LEU C  151  ASN C  158  1                                   8    
HELIX   24  24 GLY C  187  LEU C  192  1                                   6    
HELIX   25  25 VAL C  200  SER C  206  1                                   7    
HELIX   26  26 ASN C  227  PHE C  231  5                                   5    
HELIX   27  27 THR C  259  LEU C  264  1                                   6    
HELIX   28  28 TYR C  440  ALA C  442  5                                   3    
HELIX   29  29 CYS D    5  GLY D    9  5                                   5    
HELIX   30  30 SER D   12  SER D   20  1                                   9    
HELIX   31  31 LEU D   40  ASP D   47  1                                   8    
HELIX   32  32 ALA D   50  GLU D   52  5                                   3    
HELIX   33  33 ASP D   76  VAL D   80  5                                   5    
HELIX   34  34 SER D  121  SER D  123  5                                   3    
HELIX   35  35 MET D  124  ILE D  131  1                                   8    
HELIX   36  36 ASN D  133  ARG D  143  1                                  11    
HELIX   37  37 PRO D  169  ASN D  175  1                                   7    
HELIX   38  38 VAL D  200  GLN D  210  1                                  11    
HELIX   39  39 GLY D  221  CYS D  232  1                                  12    
HELIX   40  40 CYS D  232  GLY D  237  1                                   6    
HELIX   41  41 ASP D  259  GLY D  264  5                                   6    
HELIX   42  42 SER D  291  ASN D  303  1                                  13    
HELIX   43  43 VAL D  314  GLU D  323  1                                  10    
HELIX   44  44 ASN D  339  ARG D  352  1                                  14    
HELIX   45  45 CYS D  435  ALA D  441  5                                   7    
HELIX   46  46 ASN E   28  THR E   32  5                                   5    
HELIX   47  47 PRO E   62  GLN E   65  5                                   4    
HELIX   48  48 THR E   87  THR E   91  5                                   5    
HELIX   49  49 SER E  162  SER E  164  5                                   3    
HELIX   50  50 SER F  121  THR F  126  1                                   6    
HELIX   51  51 LYS F  183  GLU F  187  1                                   5    
HELIX   52  52 ASN H   28  THR H   32  5                                   5    
HELIX   53  53 PRO H   62  PHE H   64  5                                   3    
HELIX   54  54 THR H   74  SER H   76  5                                   3    
HELIX   55  55 THR H   87  THR H   91  5                                   5    
HELIX   56  56 SER L  121  THR L  126  1                                   6    
HELIX   57  57 LYS L  183  GLU L  187  1                                   5    
SHEET    1  AA 4 THR A   9  ALA A  12  0                                        
SHEET    2  AA 4 GLN A 444  TYR A 448 -1  O  VAL A 445   N  TYR A  11           
SHEET    3  AA 4 ASP A 434  ALA A 439 -1  O  LEU A 435   N  TYR A 448           
SHEET    4  AA 4 SER A 420  VAL A 425 -1  O  SER A 420   N  GLY A 438           
SHEET    1  AB 3 LEU A  23  LYS A  27  0                                        
SHEET    2  AB 3 VAL A  33  ALA A  39 -1  O  ALA A  34   N  HIS A  26           
SHEET    3  AB 3 GLY A  52  PRO A  57 -1  O  GLY A  52   N  ALA A  39           
SHEET    1  AC 4 THR A  76  VAL A  79  0                                        
SHEET    2  AC 4 GLN A  82  PHE A  87 -1  O  GLN A  82   N  VAL A  79           
SHEET    3  AC 4 HIS A 112  GLU A 117 -1  O  HIS A 112   N  PHE A  87           
SHEET    4  AC 4 GLU A 120  GLU A 121 -1  O  GLU A 120   N  GLU A 117           
SHEET    1  AD 4 VAL A  97  TRP A 100  0                                        
SHEET    2  AD 4 VAL A 103  ALA A 108 -1  O  VAL A 103   N  TRP A 100           
SHEET    3  AD 4 SER A 129  ALA A 133 -1  O  SER A 129   N  ALA A 108           
SHEET    4  AD 4 ARG A 140  TYR A 143 -1  O  ALA A 141   N  LEU A 132           
SHEET    1  AE 4 SER A 173  VAL A 175  0                                        
SHEET    2  AE 4 GLU A 180  ALA A 185 -1  O  VAL A 182   N  VAL A 174           
SHEET    3  AE 4 LEU A 194  PRO A 199 -1  O  LEU A 194   N  ALA A 185           
SHEET    4  AE 4 SER A 220  LEU A 221 -1  O  SER A 220   N  GLN A 197           
SHEET    1  AF 4 VAL A 239  GLY A 242  0                                        
SHEET    2  AF 4 GLU A 252  ALA A 257 -1  O  GLU A 252   N  GLY A 242           
SHEET    3  AF 4 ALA A 266  LEU A 270 -1  O  ALA A 266   N  ALA A 257           
SHEET    4  AF 4 ARG A 276  ARG A 281 -1  N  LEU A 277   O  ILE A 269           
SHEET    1  AG 4 VAL A 293  THR A 296  0                                        
SHEET    2  AG 4 ASP A 305  ALA A 310 -1  O  ASP A 305   N  THR A 296           
SHEET    3  AG 4 ARG A 327  PHE A 331 -1  O  ARG A 327   N  ALA A 310           
SHEET    4  AG 4 LEU A 345  THR A 348 -1  O  LEU A 345   N  LEU A 330           
SHEET    1  AH 2 MET A 314  ARG A 317  0                                        
SHEET    2  AH 2 LYS A 321  GLU A 324 -1  O  LYS A 321   N  ARG A 317           
SHEET    1  AI 4 ILE A 360  GLY A 364  0                                        
SHEET    2  AI 4 ASP A 373  ALA A 378 -1  O  ASP A 373   N  LEU A 363           
SHEET    3  AI 4 GLN A 388  PHE A 392 -1  O  GLN A 388   N  ALA A 378           
SHEET    4  AI 4 GLN A 405  ASP A 408 -1  O  GLN A 405   N  VAL A 391           
SHEET    1  AJ 2 GLY A 394  GLN A 395  0                                        
SHEET    2  AJ 2 GLY A 398  LEU A 399 -1  O  GLY A 398   N  GLN A 395           
SHEET    1  BA 3 CYS B  38  LEU B  40  0                                        
SHEET    2  BA 3 CYS B  23  CYS B  26 -1  O  ALA B  24   N  ASP B  39           
SHEET    3  BA 3 ILE B  54  GLU B  55 -1  O  GLU B  55   N  TRP B  25           
SHEET    1  BB 6 GLU B  60  GLU B  65  0                                        
SHEET    2  BB 6 ARG B  87  LEU B  92 -1  O  ARG B  87   N  LEU B  64           
SHEET    3  BB 6 LEU B 425  PHE B 431  1  O  ILE B 426   N  ILE B  88           
SHEET    4  BB 6 GLU B 411  PRO B 418 -1  O  LYS B 412   N  VAL B 429           
SHEET    5  BB 6 VAL B 355  ARG B 360 -1  O  GLU B 358   N  LYS B 417           
SHEET    6  BB 6 SER B 385  CYS B 386 -1  O  CYS B 386   N  VAL B 355           
SHEET    1  BC 5 VAL B  83  SER B  84  0                                        
SHEET    2  BC 5 SER B  97  ARG B 105 -1  O  GLN B 103   N  SER B  84           
SHEET    3  BC 5 THR B 394  VAL B 403 -1  O  VAL B 395   N  VAL B 104           
SHEET    4  BC 5 LEU B 366  CYS B 374 -1  O  SER B 367   N  LYS B 402           
SHEET    5  BC 5 GLU B 378  PRO B 381 -1  O  GLU B 378   N  CYS B 374           
SHEET    1  BD 6 TYR B 190  THR B 197  0                                        
SHEET    2  BD 6 LEU B 149  PHE B 156 -1  O  ILE B 151   N  THR B 197           
SHEET    3  BD 6 VAL B 112  ASP B 119  1  O  VAL B 112   N  ARG B 150           
SHEET    4  BD 6 SER B 243  THR B 250  1  O  SER B 243   N  ASP B 113           
SHEET    5  BD 6 ASN B 305  THR B 311  1  O  ASN B 305   N  LEU B 246           
SHEET    6  BD 6 THR B 329  LEU B 333  1  O  THR B 329   N  PHE B 308           
SHEET    1  BE 2 GLY B 453  GLU B 456  0                                        
SHEET    2  BE 2 VAL B 459  CYS B 462 -1  O  VAL B 459   N  GLU B 456           
SHEET    1  CA 4 THR C   9  ALA C  12  0                                        
SHEET    2  CA 4 GLN C 444  TYR C 448 -1  O  VAL C 445   N  TYR C  11           
SHEET    3  CA 4 ASP C 434  ALA C 439 -1  O  LEU C 435   N  TYR C 448           
SHEET    4  CA 4 SER C 420  VAL C 425 -1  O  SER C 420   N  GLY C 438           
SHEET    1  CB 3 LEU C  23  LYS C  27  0                                        
SHEET    2  CB 3 VAL C  33  GLY C  38 -1  O  ALA C  34   N  HIS C  26           
SHEET    3  CB 3 VAL C  53  PRO C  57 -1  O  PHE C  54   N  VAL C  37           
SHEET    1  CC 4 THR C  76  VAL C  79  0                                        
SHEET    2  CC 4 GLN C  82  PHE C  87 -1  O  GLN C  82   N  VAL C  79           
SHEET    3  CC 4 HIS C 112  GLU C 117 -1  O  HIS C 112   N  PHE C  87           
SHEET    4  CC 4 GLU C 120  GLU C 121 -1  O  GLU C 120   N  GLU C 117           
SHEET    1  CD 4 VAL C  97  TRP C 100  0                                        
SHEET    2  CD 4 VAL C 103  ALA C 108 -1  O  VAL C 103   N  TRP C 100           
SHEET    3  CD 4 SER C 129  ALA C 133 -1  O  SER C 129   N  ALA C 108           
SHEET    4  CD 4 ARG C 140  TYR C 143 -1  O  ALA C 141   N  LEU C 132           
SHEET    1  CE 4 SER C 172  VAL C 175  0                                        
SHEET    2  CE 4 GLU C 180  ALA C 185 -1  O  VAL C 182   N  VAL C 174           
SHEET    3  CE 4 LEU C 194  PRO C 199 -1  O  LEU C 194   N  ALA C 185           
SHEET    4  CE 4 SER C 220  LEU C 221 -1  O  SER C 220   N  GLN C 197           
SHEET    1  CF 4 VAL C 239  GLY C 242  0                                        
SHEET    2  CF 4 GLU C 252  ALA C 257 -1  O  GLU C 252   N  GLY C 242           
SHEET    3  CF 4 ALA C 266  LEU C 270 -1  O  ALA C 266   N  ALA C 257           
SHEET    4  CF 4 ARG C 276  ARG C 281 -1  N  LEU C 277   O  ILE C 269           
SHEET    1  CG 4 VAL C 293  THR C 296  0                                        
SHEET    2  CG 4 ASP C 305  ALA C 310 -1  O  ASP C 305   N  THR C 296           
SHEET    3  CG 4 ARG C 327  PHE C 331 -1  O  ARG C 327   N  ALA C 310           
SHEET    4  CG 4 LEU C 345  THR C 348 -1  O  LEU C 345   N  LEU C 330           
SHEET    1  CH 2 MET C 314  ARG C 317  0                                        
SHEET    2  CH 2 LYS C 321  GLU C 324 -1  O  LYS C 321   N  ARG C 317           
SHEET    1  CI 4 ILE C 360  GLY C 364  0                                        
SHEET    2  CI 4 ASP C 373  ALA C 378 -1  O  ASP C 373   N  LEU C 363           
SHEET    3  CI 4 GLN C 388  PHE C 392 -1  O  GLN C 388   N  ALA C 378           
SHEET    4  CI 4 GLN C 405  ASP C 408 -1  O  GLN C 405   N  VAL C 391           
SHEET    1  CJ 2 GLY C 394  GLN C 395  0                                        
SHEET    2  CJ 2 GLY C 398  LEU C 399 -1  O  GLY C 398   N  GLN C 395           
SHEET    1  DA 3 CYS D  38  ASP D  39  0                                        
SHEET    2  DA 3 ALA D  24  CYS D  26 -1  O  ALA D  24   N  ASP D  39           
SHEET    3  DA 3 ILE D  54  GLU D  55 -1  O  GLU D  55   N  TRP D  25           
SHEET    1  DB 6 GLU D  60  GLU D  65  0                                        
SHEET    2  DB 6 ARG D  87  LEU D  92 -1  O  ARG D  87   N  LEU D  64           
SHEET    3  DB 6 LEU D 425  PHE D 431  1  O  ILE D 426   N  ILE D  88           
SHEET    4  DB 6 GLU D 411  PRO D 418 -1  O  LYS D 412   N  VAL D 429           
SHEET    5  DB 6 VAL D 355  ARG D 360 -1  O  GLU D 358   N  LYS D 417           
SHEET    6  DB 6 SER D 385  CYS D 386 -1  O  CYS D 386   N  VAL D 355           
SHEET    1  DC 5 VAL D  83  SER D  84  0                                        
SHEET    2  DC 5 SER D  97  ARG D 105 -1  O  GLN D 103   N  SER D  84           
SHEET    3  DC 5 THR D 394  VAL D 403 -1  O  VAL D 395   N  VAL D 104           
SHEET    4  DC 5 LEU D 366  THR D 373 -1  O  SER D 367   N  LYS D 402           
SHEET    5  DC 5 VAL D 379  PRO D 381 -1  O  ILE D 380   N  ALA D 372           
SHEET    1  DD 6 TYR D 190  THR D 197  0                                        
SHEET    2  DD 6 LEU D 149  PHE D 156 -1  O  ILE D 151   N  THR D 197           
SHEET    3  DD 6 VAL D 112  ASP D 119  1  O  VAL D 112   N  ARG D 150           
SHEET    4  DD 6 SER D 243  THR D 250  1  O  SER D 243   N  ASP D 113           
SHEET    5  DD 6 ASN D 305  THR D 311  1  O  ASN D 305   N  LEU D 246           
SHEET    6  DD 6 THR D 329  LEU D 333  1  O  THR D 329   N  PHE D 308           
SHEET    1  DE 2 GLY D 453  GLU D 456  0                                        
SHEET    2  DE 2 VAL D 459  CYS D 462 -1  O  VAL D 459   N  GLU D 456           
SHEET    1  EA 4 GLN E   3  GLN E   6  0                                        
SHEET    2  EA 4 VAL E  18  SER E  25 -1  O  THR E  23   N  GLN E   5           
SHEET    3  EA 4 THR E  78  LEU E  83 -1  O  ALA E  79   N  CYS E  22           
SHEET    4  EA 4 ALA E  68  ASP E  73 -1  O  THR E  69   N  GLN E  82           
SHEET    1  EB 4 GLU E  10  VAL E  12  0                                        
SHEET    2  EB 4 THR E 113  VAL E 117  1  O  SER E 114   N  GLU E  10           
SHEET    3  EB 4 ALA E  92  ARG E  98 -1  O  ALA E  92   N  VAL E 115           
SHEET    4  EB 4 TYR E 108  TRP E 109 -1  O  TYR E 108   N  ARG E  98           
SHEET    1  EC 6 GLU E  10  VAL E  12  0                                        
SHEET    2  EC 6 THR E 113  VAL E 117  1  O  SER E 114   N  GLU E  10           
SHEET    3  EC 6 ALA E  92  ARG E  98 -1  O  ALA E  92   N  VAL E 115           
SHEET    4  EC 6 VAL E  34  GLN E  39 -1  O  HIS E  35   N  VAL E  97           
SHEET    5  EC 6 LEU E  45  ILE E  51 -1  O  GLU E  46   N  LYS E  38           
SHEET    6  EC 6 THR E  58  TYR E  60 -1  O  LYS E  59   N  ARG E  50           
SHEET    1  ED 2 TYR E 108  TRP E 109  0                                        
SHEET    2  ED 2 ALA E  92  ARG E  98 -1  O  ARG E  98   N  TYR E 108           
SHEET    1  EE 4 SER E 126  LEU E 130  0                                        
SHEET    2  EE 4 SER E 141  TYR E 151 -1  O  GLY E 145   N  LEU E 130           
SHEET    3  EE 4 LEU E 180  THR E 190 -1  O  TYR E 181   N  GLY E 150           
SHEET    4  EE 4 VAL E 175  GLN E 177  1  N  VAL E 175   O  THR E 182           
SHEET    1  EF 4 SER E 126  LEU E 130  0                                        
SHEET    2  EF 4 SER E 141  TYR E 151 -1  O  GLY E 145   N  LEU E 130           
SHEET    3  EF 4 LEU E 180  THR E 190 -1  O  TYR E 181   N  GLY E 150           
SHEET    4  EF 4 VAL E 169  THR E 171 -1  O  HIS E 170   N  SER E 186           
SHEET    1  EG 2 VAL E 175  GLN E 177  0                                        
SHEET    2  EG 2 LEU E 180  THR E 190  1  O  LEU E 180   N  GLN E 177           
SHEET    1  EH 3 THR E 157  TRP E 160  0                                        
SHEET    2  EH 3 THR E 200  ALA E 204 -1  O  ASN E 202   N  THR E 159           
SHEET    3  EH 3 LYS E 211  LYS E 215 -1  O  VAL E 212   N  VAL E 203           
SHEET    1  FA 4 MET F   4  SER F   7  0                                        
SHEET    2  FA 4 VAL F  19  ALA F  25 -1  O  THR F  22   N  SER F   7           
SHEET    3  FA 4 ASP F  70  ILE F  75 -1  O  TYR F  71   N  CYS F  23           
SHEET    4  FA 4 PHE F  62  SER F  67 -1  O  SER F  63   N  THR F  74           
SHEET    1  FB 4 SER F  10  VAL F  13  0                                        
SHEET    2  FB 4 THR F 102  ILE F 106  1  O  LYS F 103   N  MET F  11           
SHEET    3  FB 4 ASP F  85  GLN F  90 -1  O  TYR F  86   N  THR F 102           
SHEET    4  FB 4 THR F  97  PHE F  98 -1  O  THR F  97   N  GLN F  90           
SHEET    1  FC 6 SER F  10  VAL F  13  0                                        
SHEET    2  FC 6 THR F 102  ILE F 106  1  O  LYS F 103   N  MET F  11           
SHEET    3  FC 6 ASP F  85  GLN F  90 -1  O  TYR F  86   N  THR F 102           
SHEET    4  FC 6 ILE F  33  GLN F  38 -1  O  GLY F  34   N  VAL F  89           
SHEET    5  FC 6 PHE F  44  TYR F  49 -1  O  MET F  45   N  GLN F  37           
SHEET    6  FC 6 ASN F  53  LEU F  54 -1  O  ASN F  53   N  TYR F  49           
SHEET    1  FD 2 THR F  97  PHE F  98  0                                        
SHEET    2  FD 2 ASP F  85  GLN F  90 -1  O  GLN F  90   N  THR F  97           
SHEET    1  FE 4 THR F 114  PHE F 118  0                                        
SHEET    2  FE 4 GLY F 129  PHE F 139 -1  O  VAL F 133   N  PHE F 118           
SHEET    3  FE 4 TYR F 173  THR F 182 -1  O  TYR F 173   N  PHE F 139           
SHEET    4  FE 4 VAL F 159  TRP F 163 -1  O  LEU F 160   N  THR F 178           
SHEET    1  FF 4 SER F 153  ARG F 155  0                                        
SHEET    2  FF 4 ASN F 145  ILE F 150 -1  O  TRP F 148   N  ARG F 155           
SHEET    3  FF 4 SER F 191  HIS F 198 -1  O  THR F 193   N  LYS F 149           
SHEET    4  FF 4 SER F 201  ASN F 210 -1  O  SER F 201   N  HIS F 198           
SHEET    1  HA 4 GLN H   3  GLN H   6  0                                        
SHEET    2  HA 4 VAL H  18  SER H  25 -1  O  THR H  23   N  GLN H   5           
SHEET    3  HA 4 THR H  78  LEU H  83 -1  O  ALA H  79   N  CYS H  22           
SHEET    4  HA 4 ALA H  68  ASP H  73 -1  O  THR H  69   N  GLN H  82           
SHEET    1  HB 4 GLU H  10  VAL H  12  0                                        
SHEET    2  HB 4 THR H 113  VAL H 117  1  O  SER H 114   N  GLU H  10           
SHEET    3  HB 4 ALA H  92  ARG H  98 -1  O  ALA H  92   N  VAL H 115           
SHEET    4  HB 4 TYR H 108  TRP H 109 -1  O  TYR H 108   N  ARG H  98           
SHEET    1  HC 6 GLU H  10  VAL H  12  0                                        
SHEET    2  HC 6 THR H 113  VAL H 117  1  O  SER H 114   N  GLU H  10           
SHEET    3  HC 6 ALA H  92  ARG H  98 -1  O  ALA H  92   N  VAL H 115           
SHEET    4  HC 6 VAL H  34  ARG H  40 -1  O  HIS H  35   N  VAL H  97           
SHEET    5  HC 6 GLY H  44  ILE H  51 -1  O  GLY H  44   N  ARG H  40           
SHEET    6  HC 6 THR H  58  TYR H  60 -1  O  LYS H  59   N  ARG H  50           
SHEET    1  HD 2 TYR H 108  TRP H 109  0                                        
SHEET    2  HD 2 ALA H  92  ARG H  98 -1  O  ARG H  98   N  TYR H 108           
SHEET    1  HE 4 SER H 126  LEU H 130  0                                        
SHEET    2  HE 4 SER H 141  TYR H 151 -1  O  GLY H 145   N  LEU H 130           
SHEET    3  HE 4 LEU H 180  THR H 190 -1  O  TYR H 181   N  TYR H 151           
SHEET    4  HE 4 VAL H 175  GLN H 177  1  O  VAL H 175   N  THR H 182           
SHEET    1  HF 4 SER H 126  LEU H 130  0                                        
SHEET    2  HF 4 SER H 141  TYR H 151 -1  O  GLY H 145   N  LEU H 130           
SHEET    3  HF 4 LEU H 180  THR H 190 -1  O  TYR H 181   N  TYR H 151           
SHEET    4  HF 4 VAL H 169  THR H 171 -1  O  HIS H 170   N  SER H 186           
SHEET    1  HG 2 VAL H 175  GLN H 177  0                                        
SHEET    2  HG 2 LEU H 180  THR H 190  1  O  LEU H 180   N  GLN H 177           
SHEET    1  HH 3 THR H 157  TRP H 160  0                                        
SHEET    2  HH 3 THR H 200  HIS H 205 -1  O  ASN H 202   N  THR H 159           
SHEET    3  HH 3 THR H 210  LYS H 215 -1  O  THR H 210   N  HIS H 205           
SHEET    1  LA 4 MET L   4  SER L   7  0                                        
SHEET    2  LA 4 VAL L  19  ALA L  25 -1  O  THR L  22   N  SER L   7           
SHEET    3  LA 4 ASP L  70  ILE L  75 -1  O  TYR L  71   N  CYS L  23           
SHEET    4  LA 4 PHE L  62  SER L  67 -1  O  SER L  63   N  THR L  74           
SHEET    1  LB 4 SER L  10  VAL L  13  0                                        
SHEET    2  LB 4 THR L 102  ILE L 106  1  O  LYS L 103   N  MET L  11           
SHEET    3  LB 4 ASP L  85  GLN L  90 -1  O  TYR L  86   N  THR L 102           
SHEET    4  LB 4 THR L  97  PHE L  98 -1  O  THR L  97   N  GLN L  90           
SHEET    1  LC 6 SER L  10  VAL L  13  0                                        
SHEET    2  LC 6 THR L 102  ILE L 106  1  O  LYS L 103   N  MET L  11           
SHEET    3  LC 6 ASP L  85  GLN L  90 -1  O  TYR L  86   N  THR L 102           
SHEET    4  LC 6 ILE L  33  GLN L  38 -1  O  GLY L  34   N  VAL L  89           
SHEET    5  LC 6 PHE L  44  TYR L  49 -1  O  MET L  45   N  GLN L  37           
SHEET    6  LC 6 ASN L  53  LEU L  54 -1  O  ASN L  53   N  TYR L  49           
SHEET    1  LD 2 THR L  97  PHE L  98  0                                        
SHEET    2  LD 2 ASP L  85  GLN L  90 -1  O  GLN L  90   N  THR L  97           
SHEET    1  LE 4 THR L 114  PHE L 118  0                                        
SHEET    2  LE 4 GLY L 129  PHE L 139 -1  O  VAL L 133   N  PHE L 118           
SHEET    3  LE 4 TYR L 173  THR L 182 -1  O  TYR L 173   N  PHE L 139           
SHEET    4  LE 4 VAL L 159  TRP L 163 -1  O  LEU L 160   N  THR L 178           
SHEET    1  LF 4 SER L 153  ARG L 155  0                                        
SHEET    2  LF 4 ASN L 145  ILE L 150 -1  O  TRP L 148   N  ARG L 155           
SHEET    3  LF 4 SER L 191  HIS L 198 -1  O  THR L 193   N  LYS L 149           
SHEET    4  LF 4 SER L 201  ASN L 210 -1  O  SER L 201   N  HIS L 198           
SSBOND   1 CYS A   56    CYS A   65                          1555   1555  2.04  
SSBOND   2 CYS A  107    CYS A  130                          1555   1555  2.04  
SSBOND   3 CYS A  146    CYS A  167                          1555   1555  2.04  
SSBOND   4 CYS B    5    CYS B   23                          1555   1555  2.03  
SSBOND   5 CYS B   13    CYS B  435                          1555   1555  2.03  
SSBOND   6 CYS B   16    CYS B   38                          1555   1555  2.03  
SSBOND   7 CYS B   26    CYS B   49                          1555   1555  2.03  
SSBOND   8 CYS B  177    CYS B  184                          1555   1555  2.04  
SSBOND   9 CYS B  232    CYS B  273                          1555   1555  2.04  
SSBOND  10 CYS B  374    CYS B  386                          1555   1555  2.03  
SSBOND  11 CYS B  406    CYS B  433                          1555   1555  2.03  
SSBOND  12 CYS B  437    CYS B  457                          1555   1555  2.03  
SSBOND  13 CYS B  448    CYS B  460                          1555   1555  2.03  
SSBOND  14 CYS C   56    CYS C   65                          1555   1555  2.03  
SSBOND  15 CYS C  107    CYS C  130                          1555   1555  2.04  
SSBOND  16 CYS C  146    CYS C  167                          1555   1555  2.03  
SSBOND  17 CYS D    5    CYS D   23                          1555   1555  2.03  
SSBOND  18 CYS D   13    CYS D  435                          1555   1555  2.03  
SSBOND  19 CYS D   16    CYS D   38                          1555   1555  2.03  
SSBOND  20 CYS D   26    CYS D   49                          1555   1555  2.03  
SSBOND  21 CYS D  177    CYS D  184                          1555   1555  2.04  
SSBOND  22 CYS D  232    CYS D  273                          1555   1555  2.04  
SSBOND  23 CYS D  374    CYS D  386                          1555   1555  2.03  
SSBOND  24 CYS D  406    CYS D  433                          1555   1555  2.03  
SSBOND  25 CYS D  437    CYS D  457                          1555   1555  2.03  
SSBOND  26 CYS D  448    CYS D  460                          1555   1555  2.03  
SSBOND  27 CYS D  462    CYS D  471                          1555   1555  2.03  
SSBOND  28 CYS E   22    CYS E   96                          1555   1555  2.03  
SSBOND  29 CYS E  134    CYS F  214                          1555   1555  2.03  
SSBOND  30 CYS E  146    CYS E  201                          1555   1555  2.03  
SSBOND  31 CYS F   23    CYS F   88                          1555   1555  2.04  
SSBOND  32 CYS F  134    CYS F  194                          1555   1555  2.03  
SSBOND  33 CYS H   22    CYS H   96                          1555   1555  2.03  
SSBOND  34 CYS H  134    CYS L  214                          1555   1555  2.03  
SSBOND  35 CYS H  146    CYS H  201                          1555   1555  2.03  
SSBOND  36 CYS L   23    CYS L   88                          1555   1555  2.04  
SSBOND  37 CYS L  134    CYS L  194                          1555   1555  2.03  
LINK        CA    CA A2004                 O   THR A 250     1555   1555  2.36  
LINK        CA    CA A2004                 OG1 THR A 250     1555   1555  2.38  
LINK        CA    CA A2004                 OE1 GLU A 243     1555   1555  2.42  
LINK        CA    CA A2004                 OE2 GLU A 243     1555   1555  2.37  
LINK        CA    CA A2004                 OD1 ASP A 245     1555   1555  2.31  
LINK        CA    CA A2004                 O   ASP A 247     1555   1555  2.35  
LINK        CA    CA A2004                 OE1 GLU A 252     1555   1555  2.47  
LINK        CA    CA A2004                 OE2 GLU A 252     1555   1555  2.43  
LINK        CA    CA A2005                 OD1 ASP A 297     1555   1555  2.36  
LINK        CA    CA A2005                 O   ARG A 303     1555   1555  2.36  
LINK        CA    CA A2005                 OD1 ASN A 299     1555   1555  2.30  
LINK        CA    CA A2005                 OD1 ASP A 301     1555   1555  2.47  
LINK        CA    CA A2005                 OD1 ASP A 305     1555   1555  2.44  
LINK        CA    CA A2005                 OD2 ASP A 305     1555   1555  2.44  
LINK        CA    CA A2005                 O   HOH A3252     1555   1555  2.38  
LINK        CA    CA A2006                 OD1 ASP A 365     1555   1555  2.40  
LINK        CA    CA A2006                 OD1 ASP A 367     1555   1555  2.33  
LINK        CA    CA A2006                 OD1 ASP A 369     1555   1555  2.41  
LINK        CA    CA A2006                 O   TYR A 371     1555   1555  2.27  
LINK        CA    CA A2006                 OD1 ASP A 373     1555   1555  2.47  
LINK        CA    CA A2006                 OD2 ASP A 373     1555   1555  2.46  
LINK        CA    CA A2006                 O   HOH A3294     1555   1555  2.39  
LINK        CA    CA A2007                 OD1 ASN A 430     1555   1555  2.32  
LINK        CA    CA A2007                 OD1 ASP A 426     1555   1555  2.33  
LINK        CA    CA A2007                 O   TYR A 432     1555   1555  2.29  
LINK        CA    CA A2007                 OD1 ASP A 428     1555   1555  2.32  
LINK        CA    CA A2007                 OD2 ASP A 434     1555   1555  2.41  
LINK        CA    CA A2007                 O   HOH A3342     1555   1555  2.42  
LINK        CA    CA A2007                 OD1 ASP A 434     1555   1555  2.40  
LINK         ND2 ASN B  99                 C1  NAG B3319     1555   1555  1.44  
LINK         ND2 ASN B 320                 C1  NAG B3320     1555   1555  1.44  
LINK         ND2 ASN B 371                 C1  NAG B3371     1555   1555  1.44  
LINK        MG    MG B2001                 OG  SER B 121     1555   1555  2.13  
LINK        MG    MG B2001                 O   HOH B3020     1555   1555  2.07  
LINK        MG    MG B2001                 O   HOH B3079     1555   1555  2.09  
LINK        MG    MG B2001                 OE2 GLU B 220     1555   1555  2.10  
LINK        MG    MG B2001                 OD1 ASP I 495     1555   1555  2.07  
LINK        MG    MG B2001                 O   HOH B3021     1555   1555  2.08  
LINK        CA    CA B2002                 O   HOH B3023     1555   1555  2.39  
LINK        CA    CA B2002                 O   MET B 335     1555   1555  2.80  
LINK        CA    CA B2002                 O   HOH B3022     1555   1555  2.40  
LINK        CA    CA B2002                 OD1 ASP B 126     1555   1555  2.38  
LINK        CA    CA B2002                 O   SER B 123     1555   1555  2.52  
LINK        CA    CA B2002                 OD2 ASP B 126     1555   1555  2.41  
LINK        CA    CA B2002                 OD1 ASP B 127     1555   1555  2.39  
LINK        CA    CA B2003                 O   ASP B 217     1555   1555  2.41  
LINK        CA    CA B2003                 OD2 ASP B 158     1555   1555  2.38  
LINK        CA    CA B2003                 OD1 ASP B 217     1555   1555  2.33  
LINK        CA    CA B2003                 OE1 GLU B 220     1555   1555  2.36  
LINK        CA    CA B2003                 OD1 ASN B 215     1555   1555  2.31  
LINK        CA    CA B2003                 O   PRO B 219     1555   1555  2.22  
LINK         O4  NAG B3320                 C1  NAG B3321     1555   1555  1.44  
LINK         O3  BMA B3322                 C1  MAN B3323     1555   1555  1.44  
LINK         C1  BMA B3322                 O4  NAG B3321     1555   1555  1.44  
LINK         O4  NAG B3371                 C1  NAG B3372     1555   1555  1.44  
LINK        CA    CA C2004                 O   ASP C 247     1555   1555  2.35  
LINK        CA    CA C2004                 OD2 ASP C 245     1555   1555  2.40  
LINK        CA    CA C2004                 OG1 THR C 250     1555   1555  2.42  
LINK        CA    CA C2004                 OD1 ASP C 245     1555   1555  2.39  
LINK        CA    CA C2004                 OE2 GLU C 243     1555   1555  2.38  
LINK        CA    CA C2004                 O   THR C 250     1555   1555  2.38  
LINK        CA    CA C2004                 OE1 GLU C 243     1555   1555  2.40  
LINK        CA    CA C2004                 OE2 GLU C 252     1555   1555  2.43  
LINK        CA    CA C2004                 OE1 GLU C 252     1555   1555  2.41  
LINK        CA    CA C2005                 O   HOH C3129     1555   1555  2.39  
LINK        CA    CA C2005                 OD2 ASP C 305     1555   1555  2.45  
LINK        CA    CA C2005                 OD1 ASP C 305     1555   1555  2.40  
LINK        CA    CA C2005                 O   ARG C 303     1555   1555  2.27  
LINK        CA    CA C2005                 OD1 ASP C 301     1555   1555  2.40  
LINK        CA    CA C2005                 OD1 ASN C 299     1555   1555  2.34  
LINK        CA    CA C2005                 OD1 ASP C 297     1555   1555  2.40  
LINK        CA    CA C2006                 OD2 ASP C 373     1555   1555  2.45  
LINK        CA    CA C2006                 O   TYR C 371     1555   1555  2.28  
LINK        CA    CA C2006                 OD1 ASP C 369     1555   1555  2.40  
LINK        CA    CA C2006                 OD1 ASP C 367     1555   1555  2.32  
LINK        CA    CA C2006                 OD1 ASP C 365     1555   1555  2.42  
LINK        CA    CA C2006                 O   HOH C3154     1555   1555  2.37  
LINK        CA    CA C2006                 OD1 ASP C 373     1555   1555  2.46  
LINK        CA    CA C2007                 O   HOH C3184     1555   1555  2.41  
LINK        CA    CA C2007                 OD2 ASP C 434     1555   1555  2.40  
LINK        CA    CA C2007                 OD1 ASP C 434     1555   1555  2.38  
LINK        CA    CA C2007                 OD1 ASP C 428     1555   1555  2.31  
LINK        CA    CA C2007                 OD1 ASP C 426     1555   1555  2.35  
LINK        CA    CA C2007                 O   TYR C 432     1555   1555  2.30  
LINK        CA    CA C2007                 OD1 ASN C 430     1555   1555  2.34  
LINK         ND2 ASN D  99                 C1  NAG D3319     1555   1555  1.44  
LINK         ND2 ASN D 320                 C1  NAG D3320     1555   1555  1.44  
LINK         ND2 ASN D 371                 C1  NAG D3371     1555   1555  1.44  
LINK        MG    MG D2001                 O   HOH D3049     1555   1555  2.08  
LINK        MG    MG D2001                 OG  SER D 121     1555   1555  2.17  
LINK        MG    MG D2001                 O   HOH D3016     1555   1555  2.07  
LINK        MG    MG D2001                 O   HOH D3017     1555   1555  2.08  
LINK        MG    MG D2001                 OE2 GLU D 220     1555   1555  2.09  
LINK        MG    MG D2001                 OD1 ASP J 495     1555   1555  2.07  
LINK        CA    CA D2002                 OD1 ASP D 126     1555   1555  2.38  
LINK        CA    CA D2002                 O   SER D 123     1555   1555  2.45  
LINK        CA    CA D2002                 O   HOH D3021     1555   1555  2.36  
LINK        CA    CA D2002                 OD1 ASP D 127     1555   1555  2.32  
LINK        CA    CA D2002                 OD2 ASP D 126     1555   1555  2.44  
LINK        CA    CA D2002                 O   HOH D3020     1555   1555  2.40  
LINK        CA    CA D2002                 O   MET D 335     1555   1555  2.50  
LINK        CA    CA D2003                 OD2 ASP D 158     1555   1555  2.45  
LINK        CA    CA D2003                 OD1 ASP D 217     1555   1555  2.35  
LINK        CA    CA D2003                 OD1 ASN D 215     1555   1555  2.35  
LINK        CA    CA D2003                 O   PRO D 219     1555   1555  2.26  
LINK        CA    CA D2003                 O   ASP D 217     1555   1555  2.42  
LINK        CA    CA D2003                 OE1 GLU D 220     1555   1555  2.39  
LINK         O4  NAG D3320                 C1  NAG D3321     1555   1555  1.44  
LINK         O3  BMA D3322                 C1  MAN D3323     1555   1555  1.44  
LINK         C1  BMA D3322                 O4  NAG D3321     1555   1555  1.44  
LINK         O4  NAG D3371                 C1  NAG D3372     1555   1555  1.44  
CISPEP   1 SER B   84    PRO B   85          0        -1.66                     
CISPEP   2 SER B  162    PRO B  163          0         4.14                     
CISPEP   3 SER B  168    PRO B  169          0        -3.33                     
CISPEP   4 SER D   84    PRO D   85          0        -2.87                     
CISPEP   5 SER D  162    PRO D  163          0         5.63                     
CISPEP   6 SER D  168    PRO D  169          0        -2.47                     
CISPEP   7 PHE E  152    PRO E  153          0        -3.33                     
CISPEP   8 GLU E  154    PRO E  155          0        -4.78                     
CISPEP   9 TRP E  194    PRO E  195          0         0.14                     
CISPEP  10 SER F    7    PRO F    8          0        -1.85                     
CISPEP  11 LEU F   94    PRO F   95          0         0.59                     
CISPEP  12 TYR F  140    PRO F  141          0         3.18                     
CISPEP  13 PHE H  152    PRO H  153          0        -3.81                     
CISPEP  14 GLU H  154    PRO H  155          0        -2.49                     
CISPEP  15 TRP H  194    PRO H  195          0         1.50                     
CISPEP  16 SER L    7    PRO L    8          0        -2.82                     
CISPEP  17 LEU L   94    PRO L   95          0         0.31                     
CISPEP  18 TYR L  140    PRO L  141          0         0.72                     
SITE     1 AC1  5 GLU A 243  ASP A 245  ASP A 247  THR A 250                    
SITE     2 AC1  5 GLU A 252                                                     
SITE     1 AC2  6 ASP A 297  ASN A 299  ASP A 301  ARG A 303                    
SITE     2 AC2  6 ASP A 305  HOH A3252                                          
SITE     1 AC3  6 ASP A 365  ASP A 367  ASP A 369  TYR A 371                    
SITE     2 AC3  6 ASP A 373  HOH A3294                                          
SITE     1 AC4  6 ASP A 426  ASP A 428  ASN A 430  TYR A 432                    
SITE     2 AC4  6 ASP A 434  HOH A3342                                          
SITE     1 AC5  6 SER B 121  GLU B 220  HOH B3020  HOH B3021                    
SITE     2 AC5  6 HOH B3079  ASP I 495                                          
SITE     1 AC6  6 SER B 123  ASP B 126  ASP B 127  MET B 335                    
SITE     2 AC6  6 HOH B3022  HOH B3023                                          
SITE     1 AC7  5 ASP B 158  ASN B 215  ASP B 217  PRO B 219                    
SITE     2 AC7  5 GLU B 220                                                     
SITE     1 AC8  5 GLU C 243  ASP C 245  ASP C 247  THR C 250                    
SITE     2 AC8  5 GLU C 252                                                     
SITE     1 AC9  6 ASP C 297  ASN C 299  ASP C 301  ARG C 303                    
SITE     2 AC9  6 ASP C 305  HOH C3129                                          
SITE     1 BC1  6 ASP C 365  ASP C 367  ASP C 369  TYR C 371                    
SITE     2 BC1  6 ASP C 373  HOH C3154                                          
SITE     1 BC2  6 ASP C 426  ASP C 428  ASN C 430  TYR C 432                    
SITE     2 BC2  6 ASP C 434  HOH C3184                                          
SITE     1 BC3  6 SER D 121  GLU D 220  HOH D3016  HOH D3017                    
SITE     2 BC3  6 HOH D3049  ASP J 495                                          
SITE     1 BC4  6 SER D 123  ASP D 126  ASP D 127  MET D 335                    
SITE     2 BC4  6 HOH D3020  HOH D3021                                          
SITE     1 BC5  5 ASP D 158  ASN D 215  ASP D 217  PRO D 219                    
SITE     2 BC5  5 GLU D 220                                                     
SITE     1 BC6  4 ARG C 281  GLY C 282  PHE C 331  PRO C 343                    
SITE     1 BC7  5 ASN C 227  TYR C 230  ARG C 276  ARG C 279                    
SITE     2 BC7  5 HOH C3092                                                     
SITE     1 BC8  6 GLN B 106  TYR B 110  SER B 243  ARG B 352                    
SITE     2 BC8  6 GLY B 420  PHE B 421                                          
SITE     1 BC9  6 GLN D 106  TYR D 110  SER D 243  ARG D 352                    
SITE     2 BC9  6 GLY D 420  HOH D3055                                          
SITE     1 CC1  3 TYR A 155  ASN A 158  SER A 161                               
SITE     1 CC2  4 ARG A 279  ARG A 281  HOH A3229  MAN B3323                    
SITE     1 CC3  5 SER L  30  SER L  67  GLY L  68  HOH L3006                    
SITE     2 CC3  5 HOH L3008                                                     
SITE     1 CC4  3 HOH A3352  PHE C  10  GLN C 444                               
SITE     1 CC5  3 ARG C 279  ARG C 281  MAN D3323                               
SITE     1 CC6  5 THR A 296  ASP A 297  HIS A 304  ASN A 372                    
SITE     2 CC6  5 HOH A3353                                                     
SITE     1 CC7  4 TRP A 162  ASP A 224  HOH A3144  HOH A3184                    
SITE     1 CC8  3 GLY B 276  SER B 277  HOH B3112                               
SITE     1 CC9  4 ARG A 400  SER A 401  ARG A 402  HOH A3354                    
SITE     1 DC1  5 ASN B 269  HOH B3106  HOH B3119  HOH B3154                    
SITE     2 DC1  5 HOH B3155                                                     
SITE     1 DC2  3 ILE C 154  ASN C 158  SER C 161                               
SITE     1 DC3  2 GLN L  37  PRO L  59                                          
SITE     1 DC4  3 ALA C  89  HIS C 112  HOH C3191                               
SITE     1 DC5  2 PHE A  10  GLN A 444                                          
SITE     1 DC6  9 ARG A 386  THR A 413  HOH A3331  HOH A3332                    
SITE     2 DC6  9 HOH A3356  ARG C 386  PRO C 412  HOH C3163                    
SITE     3 DC6  9 HOH C3175                                                     
SITE     1 DC7  5 TYR A 230  ARG A 276  ARG A 279  HOH A3185                    
SITE     2 DC7  5 HOH A3194                                                     
SITE     1 DC8  2 ASN B  99  PHE B 100                                          
SITE     1 DC9  6 ARG A 281  SO4 A1456  HOH A3218  ASN B 320                    
SITE     2 DC9  6 HOH B3156  HOH B3157                                          
SITE     1 EC1  5 ASN B 371  PRO B 381  SER B 398  ILE B 399                    
SITE     2 EC1  5 GLU B 400                                                     
SITE     1 EC2  5 ASN D  99  PHE D 100  SER D 101  HOH D3012                    
SITE     2 EC2  5 NAG D3372                                                     
SITE     1 EC3  7 ARG C 281  MET C 285  SO4 C1456  HOH C3109                    
SITE     2 EC3  7 HOH C3114  ASN D 320  HOH D3108                               
SITE     1 EC4  3 ASN D 371  SER D 398  NAG D3319                               
CRYST1  257.760  145.250  106.060  90.00  90.00  90.00 P 21 21 2     8          
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      0.003880  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006885  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009429        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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