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Database: PDB
Entry: 4O02
LinkDB: 4O02
Original site: 4O02 
HEADER    PROTEIN BINDING                         13-DEC-13   4O02              
TITLE     ALPHAVBETA3 INTEGRIN IN COMPLEX WITH MONOCLONAL ANTIBODY FAB FRAGMENT.
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: INTEGRIN ALPHA-V;                                          
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: VITRONECTIN RECEPTOR SUBUNIT ALPHA;                         
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: INTEGRIN BETA-3;                                           
COMPND   8 CHAIN: B;                                                            
COMPND   9 SYNONYM: PLATELET MEMBRANE GLYCOPROTEIN IIIA, GPIIIA;                
COMPND  10 ENGINEERED: YES;                                                     
COMPND  11 MOL_ID: 3;                                                           
COMPND  12 MOLECULE: 17E6 LIGHT CHAIN;                                          
COMPND  13 CHAIN: L;                                                            
COMPND  14 MOL_ID: 4;                                                           
COMPND  15 MOLECULE: 17E6 HEAVY CHAIN;                                          
COMPND  16 CHAIN: H                                                             
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: ITGAV, MSK8, VNRA;                                             
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  10 ORGANISM_COMMON: HUMAN;                                              
SOURCE  11 ORGANISM_TAXID: 9606;                                                
SOURCE  12 GENE: ITGB3, GP3A;                                                   
SOURCE  13 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE  15 MOL_ID: 3;                                                           
SOURCE  16 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  17 ORGANISM_TAXID: 10090;                                               
SOURCE  18 MOL_ID: 4;                                                           
SOURCE  19 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  20 ORGANISM_TAXID: 10090                                                
KEYWDS    PROTEIN BINDING                                                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    B.MAHALINGAM,J.VAN AGTHOVEN,J.XIONG,M.A.ARNAOUT                       
REVDAT   2   25-FEB-15 4O02    1       JRNL   REMARK                            
REVDAT   1   02-APR-14 4O02    0                                                
JRNL        AUTH   B.MAHALINGAM,J.F.VAN AGTHOVEN,J.P.XIONG,J.L.ALONSO,          
JRNL        AUTH 2 B.D.ADAIR,X.RUI,S.ANAND,M.MEHRBOD,M.R.MOFRAD,C.BURGER,       
JRNL        AUTH 3 S.L.GOODMAN,M.A.ARNAOUT                                      
JRNL        TITL   ATOMIC BASIS FOR THE SPECIES-SPECIFIC INHIBITION OF ALPHA V  
JRNL        TITL 2 INTEGRINS BY MONOCLONAL ANTIBODY 17E6 IS REVEALED BY THE     
JRNL        TITL 3 CRYSTAL STRUCTURE OF ALPHA V BETA 3 ECTODOMAIN-17E6 FAB      
JRNL        TITL 4 COMPLEX.                                                     
JRNL        REF    J.BIOL.CHEM.                  V. 289 13801 2014              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   24692540                                                     
JRNL        DOI    10.1074/JBC.M113.546929                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.8.2_1309)                   
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 49.86                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 87.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 31286                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.250                           
REMARK   3   R VALUE            (WORKING SET) : 0.246                           
REMARK   3   FREE R VALUE                     : 0.312                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.990                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1562                            
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 49.8665 -  8.0083    0.98     3236   167  0.2234 0.2884        
REMARK   3     2  8.0083 -  6.3606    1.00     3147   156  0.2826 0.3395        
REMARK   3     3  6.3606 -  5.5578    1.00     3085   167  0.2648 0.3483        
REMARK   3     4  5.5578 -  5.0502    1.00     3071   167  0.2369 0.2912        
REMARK   3     5  5.0502 -  4.6885    0.99     3035   144  0.2126 0.2913        
REMARK   3     6  4.6885 -  4.4122    0.96     2945   152  0.2161 0.2812        
REMARK   3     7  4.4122 -  4.1914    0.91     2774   162  0.2405 0.3236        
REMARK   3     8  4.1914 -  4.0090    0.85     2572   146  0.2704 0.3191        
REMARK   3     9  4.0090 -  3.8547    0.74     2236   115  0.2805 0.3220        
REMARK   3    10  3.8547 -  3.7218    0.65     1988    99  0.3107 0.3729        
REMARK   3    11  3.7218 -  3.6054    0.54     1635    87  0.3249 0.3724        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.530            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 33.920           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 112.00                         
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  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      :  0.008          13859                                  
REMARK   3   ANGLE     :  1.374          18980                                  
REMARK   3   CHIRALITY :  0.051           2252                                  
REMARK   3   PLANARITY :  0.007           2573                                  
REMARK   3   DIHEDRAL  : 14.889           4259                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 20                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: chain 'B' and (resid 1 through 121 )                   
REMARK   3    ORIGIN FOR THE GROUP (A): -84.5908  56.9412 -19.8699              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9356 T22:   0.8230                                     
REMARK   3      T33:   2.1034 T12:  -0.1459                                     
REMARK   3      T13:   0.2458 T23:   0.1094                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.6461 L22:   2.8360                                     
REMARK   3      L33:   4.2343 L12:   1.7337                                     
REMARK   3      L13:   3.0601 L23:   0.9286                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2277 S12:   0.1657 S13:   0.4345                       
REMARK   3      S21:  -1.4185 S22:  -0.1278 S23:   0.2979                       
REMARK   3      S31:  -0.3427 S32:  -1.1654 S33:   0.3980                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: chain 'B' and (resid 122 through 304 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -50.5424  59.6160  11.0595              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4657 T22:   0.5496                                     
REMARK   3      T33:   1.3110 T12:   0.0289                                     
REMARK   3      T13:   0.0820 T23:  -0.0925                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4706 L22:   6.9430                                     
REMARK   3      L33:   3.7438 L12:  -0.5236                                     
REMARK   3      L13:   0.3406 L23:  -1.4404                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1598 S12:  -0.3475 S13:   0.9342                       
REMARK   3      S21:   0.6820 S22:   0.1247 S23:  -0.5987                       
REMARK   3      S31:  -0.4239 S32:   0.1464 S33:  -0.0040                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: chain 'B' and (resid 305 through 441 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -65.5307  59.1636 -11.9175              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7333 T22:   0.5782                                     
REMARK   3      T33:   1.5301 T12:   0.1778                                     
REMARK   3      T13:   0.2453 T23:   0.0807                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.4415 L22:   2.1412                                     
REMARK   3      L33:   2.9640 L12:   1.0464                                     
REMARK   3      L13:   2.5053 L23:   0.7664                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1564 S12:   0.5185 S13:   0.4953                       
REMARK   3      S21:  -0.1381 S22:  -0.3592 S23:   0.4683                       
REMARK   3      S31:   0.0461 S32:  -0.1032 S33:   0.1589                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: chain 'B' and (resid 442 through 657 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -72.0152  44.9878 -30.2976              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.4726 T22:   1.9123                                     
REMARK   3      T33:   1.6412 T12:   0.3479                                     
REMARK   3      T13:  -0.0671 T23:   0.1202                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.2971 L22:   1.5918                                     
REMARK   3      L33:   3.4068 L12:   2.2277                                     
REMARK   3      L13:   1.3421 L23:   1.1976                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1879 S12:   0.2225 S13:   0.2384                       
REMARK   3      S21:  -0.2272 S22:  -0.0206 S23:   0.2279                       
REMARK   3      S31:   0.0095 S32:   0.6688 S33:  -0.1902                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: chain 'B' and (resid 658 through 687 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -40.3572  79.1169 -28.7975              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   4.2168 T22:   3.6505                                     
REMARK   3      T33:   3.1122 T12:  -0.5533                                     
REMARK   3      T13:   0.0735 T23:   1.8162                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4268 L22:   3.6710                                     
REMARK   3      L33:   5.5863 L12:   1.2377                                     
REMARK   3      L13:  -1.5300 L23:  -4.5341                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1671 S12:  -1.6700 S13:  -2.1312                       
REMARK   3      S21:   1.1889 S22:  -0.2196 S23:   0.3032                       
REMARK   3      S31:   2.7815 S32:  -0.3906 S33:   0.3688                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: chain 'A' and (resid 1 through 214 )                   
REMARK   3    ORIGIN FOR THE GROUP (A): -42.7428  25.0434  17.5967              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5332 T22:   0.6366                                     
REMARK   3      T33:   0.5891 T12:  -0.0172                                     
REMARK   3      T13:   0.0113 T23:   0.0506                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.0444 L22:   3.8382                                     
REMARK   3      L33:   4.3084 L12:  -1.5466                                     
REMARK   3      L13:   1.5119 L23:  -0.7170                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1571 S12:  -0.8492 S13:  -0.5204                       
REMARK   3      S21:   0.1555 S22:  -0.1097 S23:   0.6030                       
REMARK   3      S31:   0.3985 S32:  -0.0178 S33:  -0.0092                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: chain 'A' and (resid 215 through 403 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -51.1012  29.5331  -4.6392              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8262 T22:   0.5745                                     
REMARK   3      T33:   0.9045 T12:   0.0130                                     
REMARK   3      T13:  -0.2144 T23:   0.1211                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.9222 L22:   4.1025                                     
REMARK   3      L33:   5.4858 L12:   1.3432                                     
REMARK   3      L13:   0.6973 L23:  -0.6631                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3591 S12:   0.6035 S13:  -0.7171                       
REMARK   3      S21:  -0.9746 S22:   0.5387 S23:   0.6779                       
REMARK   3      S31:   0.6866 S32:  -0.5054 S33:  -0.8600                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: chain 'A' and (resid 404 through 533 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -77.5031   5.6917 -11.7723              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   2.0150 T22:   1.1110                                     
REMARK   3      T33:   2.1995 T12:  -0.0358                                     
REMARK   3      T13:  -1.0334 T23:   0.1708                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.6641 L22:   0.7842                                     
REMARK   3      L33:   3.3217 L12:   1.5824                                     
REMARK   3      L13:   2.4003 L23:   1.5689                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2640 S12:   0.2500 S13:  -1.3230                       
REMARK   3      S21:  -1.7146 S22:  -0.0084 S23:   1.0723                       
REMARK   3      S31:   0.2311 S32:  -0.6311 S33:  -0.2074                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: chain 'A' and (resid 534 through 622 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -78.1372   8.4029 -27.8464              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   2.1100 T22:   0.9690                                     
REMARK   3      T33:   2.6647 T12:   0.0880                                     
REMARK   3      T13:  -0.5505 T23:  -0.0253                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7135 L22:   1.8456                                     
REMARK   3      L33:   5.3322 L12:   1.5146                                     
REMARK   3      L13:  -0.0472 L23:  -2.1621                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3438 S12:   0.1917 S13:  -0.0674                       
REMARK   3      S21:  -1.1722 S22:   0.5005 S23:   0.9155                       
REMARK   3      S31:   1.8196 S32:  -0.4331 S33:  -0.7982                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: chain 'A' and (resid 623 through 742 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -65.0469  18.9114 -42.1338              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   2.7212 T22:   1.3731                                     
REMARK   3      T33:   2.0989 T12:   0.2606                                     
REMARK   3      T13:  -0.4254 T23:  -0.1041                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.5043 L22:   5.1758                                     
REMARK   3      L33:   3.4912 L12:   1.0898                                     
REMARK   3      L13:  -0.0121 L23:  -0.1873                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0976 S12:  -0.3932 S13:  -0.3149                       
REMARK   3      S21:  -1.2221 S22:   0.7286 S23:  -1.1716                       
REMARK   3      S31:   1.7202 S32:   0.1687 S33:  -0.6552                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: chain 'A' and (resid 743 through 953 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -26.9213  58.8388 -41.7315              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.9530 T22:   2.5370                                     
REMARK   3      T33:   2.5170 T12:  -0.0215                                     
REMARK   3      T13:   0.6351 T23:   0.0699                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.2386 L22:   4.7236                                     
REMARK   3      L33:   0.2131 L12:   1.4345                                     
REMARK   3      L13:   0.9201 L23:   0.0331                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.5780 S12:   0.1064 S13:  -0.7854                       
REMARK   3      S21:  -1.3716 S22:   0.2333 S23:  -2.3322                       
REMARK   3      S31:   0.1024 S32:   0.4951 S33:   0.3793                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: chain 'L' and (resid 1 through 32 )                    
REMARK   3    ORIGIN FOR THE GROUP (A):  -9.7180  23.7676  40.8371              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9264 T22:   1.5728                                     
REMARK   3      T33:   0.8993 T12:  -0.1851                                     
REMARK   3      T13:  -0.3485 T23:   0.0886                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.3250 L22:   5.3840                                     
REMARK   3      L33:   4.0639 L12:  -2.2949                                     
REMARK   3      L13:   0.0084 L23:   0.0223                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -1.2646 S12:  -1.4496 S13:   0.9884                       
REMARK   3      S21:   1.4213 S22:   0.0555 S23:  -0.6805                       
REMARK   3      S31:  -0.1184 S32:   0.3303 S33:   1.1766                       
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    SELECTION: chain 'L' and (resid 33 through 61 )                   
REMARK   3    ORIGIN FOR THE GROUP (A): -14.2590  18.2086  29.7929              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8022 T22:   1.0568                                     
REMARK   3      T33:   1.2658 T12:   0.2397                                     
REMARK   3      T13:   0.2907 T23:  -0.2826                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.9754 L22:   7.5961                                     
REMARK   3      L33:   1.6084 L12:  -2.2665                                     
REMARK   3      L13:   0.6076 L23:  -0.0005                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2231 S12:   1.2723 S13:  -1.3087                       
REMARK   3      S21:  -0.5518 S22:  -0.4324 S23:   0.5704                       
REMARK   3      S31:   0.4259 S32:   0.4007 S33:   0.1464                       
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    SELECTION: chain 'L' and (resid 62 through 102 )                  
REMARK   3    ORIGIN FOR THE GROUP (A): -11.6633  21.7086  35.5388              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5295 T22:   1.2966                                     
REMARK   3      T33:   0.7002 T12:  -0.0174                                     
REMARK   3      T13:  -0.0367 T23:  -0.0477                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.3141 L22:   7.7402                                     
REMARK   3      L33:   5.2222 L12:  -0.7989                                     
REMARK   3      L13:  -0.5155 L23:  -1.2103                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2536 S12:  -1.8548 S13:  -0.3247                       
REMARK   3      S21:   0.3078 S22:   0.2106 S23:   0.5129                       
REMARK   3      S31:  -0.4579 S32:  -0.3771 S33:  -0.0461                       
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    SELECTION: chain 'L' and (resid 103 through 120 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  13.9310   7.5083  36.5198              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6555 T22:   1.8609                                     
REMARK   3      T33:   2.4265 T12:   0.0489                                     
REMARK   3      T13:  -0.0244 T23:   0.4642                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.4932 L22:   0.3366                                     
REMARK   3      L33:   0.3786 L12:   1.0051                                     
REMARK   3      L13:   1.1519 L23:   0.3481                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3293 S12:  -0.2312 S13:  -1.2696                       
REMARK   3      S21:   0.0186 S22:  -0.5518 S23:  -1.5163                       
REMARK   3      S31:   0.5475 S32:   0.1684 S33:   0.2245                       
REMARK   3   TLS GROUP : 16                                                     
REMARK   3    SELECTION: chain 'L' and (resid 121 through 173 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  20.6178  14.8377  32.7426              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8822 T22:   2.1986                                     
REMARK   3      T33:   1.7444 T12:  -0.0275                                     
REMARK   3      T13:  -0.1542 T23:  -0.0193                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.8478 L22:   6.3526                                     
REMARK   3      L33:   5.4382 L12:  -1.0034                                     
REMARK   3      L13:   1.8566 L23:   1.1332                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2749 S12:   0.5084 S13:   0.5540                       
REMARK   3      S21:  -0.2310 S22:   0.2433 S23:  -1.9407                       
REMARK   3      S31:  -0.3160 S32:   3.0080 S33:  -0.1098                       
REMARK   3   TLS GROUP : 17                                                     
REMARK   3    SELECTION: chain 'L' and (resid 174 through 214 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  30.0585  15.0830  35.8210              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0639 T22:   2.8708                                     
REMARK   3      T33:   1.8495 T12:  -0.1373                                     
REMARK   3      T13:  -0.1533 T23:  -0.0953                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.4414 L22:   7.0884                                     
REMARK   3      L33:   1.6880 L12:   0.3783                                     
REMARK   3      L13:   1.2028 L23:  -1.7924                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1504 S12:  -1.0590 S13:   0.3867                       
REMARK   3      S21:   0.7289 S22:  -0.8928 S23:  -2.5891                       
REMARK   3      S31:  -0.4210 S32:   0.3731 S33:   1.1357                       
REMARK   3   TLS GROUP : 18                                                     
REMARK   3    SELECTION: chain 'H' and (resid 1 through 98 )                    
REMARK   3    ORIGIN FOR THE GROUP (A):  -7.7132  32.5180  16.1715              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7757 T22:   1.0659                                     
REMARK   3      T33:   1.6423 T12:   0.0484                                     
REMARK   3      T13:   0.1662 T23:   0.3098                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0940 L22:   4.2105                                     
REMARK   3      L33:   5.4783 L12:  -0.3752                                     
REMARK   3      L13:   0.4969 L23:  -1.4869                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4010 S12:   0.8968 S13:   0.5170                       
REMARK   3      S21:  -0.0855 S22:  -0.8959 S23:  -1.7248                       
REMARK   3      S31:  -0.3161 S32:   1.4638 S33:   0.4863                       
REMARK   3   TLS GROUP : 19                                                     
REMARK   3    SELECTION: chain 'H' and (resid 99 through 150 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  10.6449  17.5576  21.2372              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9177 T22:   2.5127                                     
REMARK   3      T33:   2.2967 T12:   0.6134                                     
REMARK   3      T13:   0.4226 T23:   0.0832                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.1270 L22:   3.6930                                     
REMARK   3      L33:   1.5418 L12:  -1.8595                                     
REMARK   3      L13:  -0.7203 L23:  -0.3365                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4882 S12:  -0.4507 S13:   0.5718                       
REMARK   3      S21:  -0.3251 S22:   0.2215 S23:  -2.1925                       
REMARK   3      S31:   0.7870 S32:   1.9619 S33:   0.2327                       
REMARK   3   TLS GROUP : 20                                                     
REMARK   3    SELECTION: chain 'H' and (resid 151 through 218 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  20.1143   9.1275  18.1597              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.2667 T22:   2.5027                                     
REMARK   3      T33:   1.7470 T12:   0.5272                                     
REMARK   3      T13:   0.2578 T23:  -0.2027                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.0173 L22:   2.6216                                     
REMARK   3      L33:   4.6763 L12:   3.0861                                     
REMARK   3      L13:  -0.2612 L23:   0.8928                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.9593 S12:   0.4343 S13:  -0.6590                       
REMARK   3      S21:  -0.3025 S22:   1.0036 S23:  -0.1067                       
REMARK   3      S31:   1.2224 S32:   1.1170 S33:  -0.0452                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: RAMACHANDRAN RESTRAINS                    
REMARK   4                                                                      
REMARK   4 4O02 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-JAN-14.                  
REMARK 100 THE RCSB ID CODE IS RCSB083871.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : 5.6                                
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 19-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97857                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 31351                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 31351.000                          
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 87.9                               
REMARK 200  DATA REDUNDANCY                : 3.800                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.13100                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.3000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.73                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 55.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.80                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.86600                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 62.46                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.28                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 13.5% PEG 4000, PH 5.6, VAPOR            
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 298K                           
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       55.23200            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000      133.49400            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       55.23200            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000      133.49400            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, L, H                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     LYS A   834                                                      
REMARK 465     ILE A   835                                                      
REMARK 465     SER A   836                                                      
REMARK 465     SER A   837                                                      
REMARK 465     LEU A   838                                                      
REMARK 465     GLN A   839                                                      
REMARK 465     THR A   840                                                      
REMARK 465     THR A   841                                                      
REMARK 465     GLU A   842                                                      
REMARK 465     LYS A   843                                                      
REMARK 465     ASN A   844                                                      
REMARK 465     ASP A   845                                                      
REMARK 465     THR A   846                                                      
REMARK 465     VAL A   847                                                      
REMARK 465     ALA A   848                                                      
REMARK 465     GLY A   849                                                      
REMARK 465     GLN A   850                                                      
REMARK 465     GLY A   851                                                      
REMARK 465     GLU A   852                                                      
REMARK 465     ARG A   853                                                      
REMARK 465     ASP A   854                                                      
REMARK 465     HIS A   855                                                      
REMARK 465     LEU A   856                                                      
REMARK 465     ILE A   857                                                      
REMARK 465     THR A   858                                                      
REMARK 465     LYS A   859                                                      
REMARK 465     ARG A   860                                                      
REMARK 465     ASP A   861                                                      
REMARK 465     LEU A   862                                                      
REMARK 465     ALA A   863                                                      
REMARK 465     LEU A   864                                                      
REMARK 465     SER A   865                                                      
REMARK 465     GLU A   866                                                      
REMARK 465     GLY A   867                                                      
REMARK 465     ASP A   868                                                      
REMARK 465     ILE A   869                                                      
REMARK 465     HIS A   870                                                      
REMARK 465     THR A   871                                                      
REMARK 465     GLY A   954                                                      
REMARK 465     ILE A   955                                                      
REMARK 465     GLN A   956                                                      
REMARK 465     PRO A   957                                                      
REMARK 465     ALA A   958                                                      
REMARK 465     PRO A   959                                                      
REMARK 465     MET A   960                                                      
REMARK 465     PRO A   961                                                      
REMARK 465     VAL A   962                                                      
REMARK 465     PRO B   688                                                      
REMARK 465     LYS B   689                                                      
REMARK 465     GLY B   690                                                      
REMARK 465     PRO B   691                                                      
REMARK 465     ASP B   692                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     VAL A   5    CG1  CG2                                            
REMARK 470     GLU A  10    CG   CD   OE1  OE2                                  
REMARK 470     SER A  31    OG                                                  
REMARK 470     SER A  32    OG                                                  
REMARK 470     ARG A  33    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU A  37    CG   CD1  CD2                                       
REMARK 470     ILE A  50    CG1  CG2  CD1                                       
REMARK 470     VAL A  56    CG1  CG2                                            
REMARK 470     LYS A  58    CG   CD   CE   NZ                                   
REMARK 470     ARG A  66    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN A  68    CG   CD   OE1  NE2                                  
REMARK 470     GLU A  71    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 104    CG   CD   CE   NZ                                   
REMARK 470     THR A 116    OG1  CG2                                            
REMARK 470     LYS A 119    CG   CD   CE   NZ                                   
REMARK 470     GLU A 121    CG   CD   OE1  OE2                                  
REMARK 470     VAL A 125    CG1  CG2                                            
REMARK 470     LEU A 130    CG   CD1  CD2                                       
REMARK 470     VAL A 137    CG1  CG2                                            
REMARK 470     SER A 160    OG                                                  
REMARK 470     LYS A 165    CG   CD   CE   NZ                                   
REMARK 470     ARG A 211    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     SER A 225    OG                                                  
REMARK 470     VAL A 228    CG1  CG2                                            
REMARK 470     ASP A 234    CG   OD1  OD2                                       
REMARK 470     ILE A 236    CG1  CG2  CD1                                       
REMARK 470     VAL A 240    CG1  CG2                                            
REMARK 470     SER A 241    OG                                                  
REMARK 470     VAL A 243    CG1  CG2                                            
REMARK 470     ARG A 248    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 259    CG   CD   CE   NZ                                   
REMARK 470     SER A 262    OG                                                  
REMARK 470     VAL A 280    CG1  CG2                                            
REMARK 470     ILE A 285    CG1  CG2  CD1                                       
REMARK 470     VAL A 293    CG1  CG2                                            
REMARK 470     ILE A 295    CG1  CG2  CD1                                       
REMARK 470     LYS A 308    CG   CD   CE   NZ                                   
REMARK 470     VAL A 312    CG1  CG2                                            
REMARK 470     SER A 318    OG                                                  
REMARK 470     ARG A 321    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     SER A 323    OG                                                  
REMARK 470     ASP A 325    CG   OD1  OD2                                       
REMARK 470     GLN A 327    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 330    CG   CD   CE   NZ                                   
REMARK 470     LEU A 350    CG   CD1  CD2                                       
REMARK 470     LYS A 369    CG   CD   CE   NZ                                   
REMARK 470     LYS A 370    CG   CD   CE   NZ                                   
REMARK 470     ARG A 379    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU A 383    CG   CD1  CD2                                       
REMARK 470     ILE A 390    CG1  CG2  CD1                                       
REMARK 470     LEU A 391    CG   CD1  CD2                                       
REMARK 470     GLN A 394    CG   CD   OE1  NE2                                  
REMARK 470     ARG A 398    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 409    CG   CD   CE   NZ                                   
REMARK 470     THR A 412    OG1  CG2                                            
REMARK 470     ILE A 414    CG1  CG2  CD1                                       
REMARK 470     LYS A 416    CG   CD   CE   NZ                                   
REMARK 470     LEU A 422    CG   CD1  CD2                                       
REMARK 470     VAL A 424    CG1  CG2                                            
REMARK 470     VAL A 429    CG1  CG2                                            
REMARK 470     ARG A 436    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU A 447    CG   CD1  CD2                                       
REMARK 470     GLU A 448    CG   CD   OE1  OE2                                  
REMARK 470     VAL A 449    CG1  CG2                                            
REMARK 470     TYR A 450    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     PRO A 451    CG   CD                                             
REMARK 470     SER A 452    OG                                                  
REMARK 470     ILE A 453    CG1  CG2  CD1                                       
REMARK 470     LEU A 454    CG   CD1  CD2                                       
REMARK 470     ASN A 455    CG   OD1  ND2                                       
REMARK 470     GLN A 456    CG   CD   OE1  NE2                                  
REMARK 470     ASP A 457    CG   OD1  OD2                                       
REMARK 470     ASN A 458    CG   OD1  ND2                                       
REMARK 470     THR A 460    OG1  CG2                                            
REMARK 470     CYS A 461    SG                                                  
REMARK 470     SER A 462    OG                                                  
REMARK 470     LEU A 463    CG   CD1  CD2                                       
REMARK 470     PRO A 464    CG   CD                                             
REMARK 470     THR A 466    OG1  CG2                                            
REMARK 470     LEU A 468    CG   CD1  CD2                                       
REMARK 470     LYS A 469    CG   CD   CE   NZ                                   
REMARK 470     VAL A 470    CG1  CG2                                            
REMARK 470     SER A 471    OG                                                  
REMARK 470     PHE A 473    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ASN A 474    CG   OD1  ND2                                       
REMARK 470     VAL A 475    CG1  CG2                                            
REMARK 470     ARG A 476    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU A 479    CG   CD1  CD2                                       
REMARK 470     LYS A 480    CG   CD   CE   NZ                                   
REMARK 470     ASP A 482    CG   OD1  OD2                                       
REMARK 470     LEU A 487    CG   CD1  CD2                                       
REMARK 470     ARG A 489    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 490    CG   CD   CE   NZ                                   
REMARK 470     LEU A 491    CG   CD1  CD2                                       
REMARK 470     GLN A 494    CG   CD   OE1  NE2                                  
REMARK 470     VAL A 495    CG1  CG2                                            
REMARK 470     LEU A 497    CG   CD1  CD2                                       
REMARK 470     LEU A 498    CG   CD1  CD2                                       
REMARK 470     LEU A 499    CG   CD1  CD2                                       
REMARK 470     LYS A 501    CG   CD   CE   NZ                                   
REMARK 470     LEU A 502    CG   CD1  CD2                                       
REMARK 470     LYS A 503    CG   CD   CE   NZ                                   
REMARK 470     GLN A 504    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 505    CG   CD   CE   NZ                                   
REMARK 470     ILE A 508    CG1  CG2  CD1                                       
REMARK 470     ARG A 509    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 510    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU A 512    CG   CD1  CD2                                       
REMARK 470     PHE A 513    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LEU A 514    CG   CD1  CD2                                       
REMARK 470     TYR A 515    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     SER A 516    OG                                                  
REMARK 470     SER A 518    OG                                                  
REMARK 470     PRO A 519    CG   CD                                             
REMARK 470     HIS A 521    CG   ND1  CD2  CE1  NE2                             
REMARK 470     SER A 522    OG                                                  
REMARK 470     LYS A 523    CG   CD   CE   NZ                                   
REMARK 470     ILE A 527    CG1  CG2  CD1                                       
REMARK 470     ARG A 529    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU A 532    CG   CD1  CD2                                       
REMARK 470     GLU A 537    CG   CD   OE1  OE2                                  
REMARK 470     LEU A 538    CG   CD1  CD2                                       
REMARK 470     ILE A 539    CG1  CG2  CD1                                       
REMARK 470     TYR A 541    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LEU A 542    CG   CD1  CD2                                       
REMARK 470     ARG A 543    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP A 544    CG   OD1  OD2                                       
REMARK 470     GLU A 545    CG   CD   OE1  OE2                                  
REMARK 470     SER A 546    OG                                                  
REMARK 470     GLU A 547    CG   CD   OE1  OE2                                  
REMARK 470     PHE A 548    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ARG A 549    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP A 550    CG   OD1  OD2                                       
REMARK 470     LYS A 551    CG   CD   CE   NZ                                   
REMARK 470     LEU A 552    CG   CD1  CD2                                       
REMARK 470     THR A 553    OG1  CG2                                            
REMARK 470     THR A 556    OG1  CG2                                            
REMARK 470     MET A 559    CG   SD   CE                                        
REMARK 470     THR A 567    OG1  CG2                                            
REMARK 470     THR A 571    OG1  CG2                                            
REMARK 470     THR A 572    OG1  CG2                                            
REMARK 470     LEU A 574    CG   CD1  CD2                                       
REMARK 470     GLN A 575    CG   CD   OE1  NE2                                  
REMARK 470     GLN A 580    CG   CD   OE1  NE2                                  
REMARK 470     PHE A 581    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     THR A 582    OG1  CG2                                            
REMARK 470     PRO A 583    CG   CD                                             
REMARK 470     ILE A 586    CG1  CG2  CD1                                       
REMARK 470     SER A 587    OG                                                  
REMARK 470     ARG A 588    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     HIS A 591    CG   ND1  CD2  CE1  NE2                             
REMARK 470     ILE A 592    CG1  CG2  CD1                                       
REMARK 470     LEU A 593    CG   CD1  CD2                                       
REMARK 470     LEU A 594    CG   CD1  CD2                                       
REMARK 470     ASP A 595    CG   OD1  OD2                                       
REMARK 470     ASN A 600    CG   OD1  ND2                                       
REMARK 470     VAL A 601    CG1  CG2                                            
REMARK 470     LYS A 603    CG   CD   CE   NZ                                   
REMARK 470     LYS A 605    CG   CD   CE   NZ                                   
REMARK 470     GLU A 607    CG   CD   OE1  OE2                                  
REMARK 470     SER A 609    OG                                                  
REMARK 470     SER A 612    OG                                                  
REMARK 470     LYS A 615    CG   CD   CE   NZ                                   
REMARK 470     LYS A 616    CG   CD   CE   NZ                                   
REMARK 470     ILE A 617    CG1  CG2  CD1                                       
REMARK 470     TYR A 618    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ASP A 621    CG   OD1  OD2                                       
REMARK 470     ASP A 622    CG   OD1  OD2                                       
REMARK 470     ASN A 623    CG   OD1  ND2                                       
REMARK 470     LEU A 625    CG   CD1  CD2                                       
REMARK 470     THR A 626    OG1  CG2                                            
REMARK 470     LEU A 627    CG   CD1  CD2                                       
REMARK 470     ILE A 628    CG1  CG2  CD1                                       
REMARK 470     VAL A 629    CG1  CG2                                            
REMARK 470     LYS A 630    CG   CD   CE   NZ                                   
REMARK 470     GLN A 632    CG   CD   OE1  NE2                                  
REMARK 470     GLU A 636    CG   CD   OE1  OE2                                  
REMARK 470     LEU A 643    CG   CD1  CD2                                       
REMARK 470     ILE A 644    CG1  CG2  CD1                                       
REMARK 470     VAL A 645    CG1  CG2                                            
REMARK 470     ILE A 647    CG1  CG2  CD1                                       
REMARK 470     LEU A 649    CG   CD1  CD2                                       
REMARK 470     PHE A 653    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ILE A 654    CG1  CG2  CD1                                       
REMARK 470     VAL A 656    CG1  CG2                                            
REMARK 470     ARG A 658    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASN A 659    CG   OD1  ND2                                       
REMARK 470     LEU A 663    CG   CD1  CD2                                       
REMARK 470     ARG A 665    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU A 666    CG   CD1  CD2                                       
REMARK 470     SER A 667    OG                                                  
REMARK 470     LYS A 671    CG   CD   CE   NZ                                   
REMARK 470     ASN A 674    CG   OD1  ND2                                       
REMARK 470     THR A 676    OG1  CG2                                            
REMARK 470     ARG A 677    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN A 678    CG   CD   OE1  NE2                                  
REMARK 470     VAL A 679    CG1  CG2                                            
REMARK 470     VAL A 680    CG1  CG2                                            
REMARK 470     ASP A 682    CG   OD1  OD2                                       
REMARK 470     LEU A 683    CG   CD1  CD2                                       
REMARK 470     ASN A 685    CG   OD1  ND2                                       
REMARK 470     MET A 687    CG   SD   CE                                        
REMARK 470     LYS A 688    CG   CD   CE   NZ                                   
REMARK 470     THR A 691    OG1  CG2                                            
REMARK 470     GLN A 692    CG   CD   OE1  NE2                                  
REMARK 470     LEU A 693    CG   CD1  CD2                                       
REMARK 470     LEU A 694    CG   CD1  CD2                                       
REMARK 470     LEU A 697    CG   CD1  CD2                                       
REMARK 470     ARG A 698    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     PHE A 699    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     HIS A 702    CG   ND1  CD2  CE1  NE2                             
REMARK 470     GLN A 703    CG   CD   OE1  NE2                                  
REMARK 470     GLN A 704    CG   CD   OE1  NE2                                  
REMARK 470     SER A 705    OG                                                  
REMARK 470     MET A 707    CG   SD   CE                                        
REMARK 470     ASP A 708    CG   OD1  OD2                                       
REMARK 470     THR A 709    OG1  CG2                                            
REMARK 470     SER A 710    OG                                                  
REMARK 470     VAL A 711    CG1  CG2                                            
REMARK 470     LYS A 712    CG   CD   CE   NZ                                   
REMARK 470     PHE A 713    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LEU A 715    CG   CD1  CD2                                       
REMARK 470     GLN A 716    CG   CD   OE1  NE2                                  
REMARK 470     ILE A 717    CG1  CG2  CD1                                       
REMARK 470     GLN A 718    CG   CD   OE1  NE2                                  
REMARK 470     PHE A 723    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ASP A 724    CG   OD1  OD2                                       
REMARK 470     LYS A 725    CG   CD   CE   NZ                                   
REMARK 470     VAL A 729    CG1  CG2                                            
REMARK 470     VAL A 730    CG1  CG2                                            
REMARK 470     SER A 731    OG                                                  
REMARK 470     HIS A 732    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LYS A 733    CG   CD   CE   NZ                                   
REMARK 470     VAL A 734    CG1  CG2                                            
REMARK 470     ASP A 735    CG   OD1  OD2                                       
REMARK 470     LEU A 736    CG   CD1  CD2                                       
REMARK 470     VAL A 738    CG1  CG2                                            
REMARK 470     LEU A 739    CG   CD1  CD2                                       
REMARK 470     VAL A 742    CG1  CG2                                            
REMARK 470     GLU A 743    CG   CD   OE1  OE2                                  
REMARK 470     ILE A 744    CG1  CG2  CD1                                       
REMARK 470     ARG A 745    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     VAL A 747    CG1  CG2                                            
REMARK 470     SER A 749    OG                                                  
REMARK 470     ASP A 751    CG   OD1  OD2                                       
REMARK 470     VAL A 753    CG1  CG2                                            
REMARK 470     PHE A 754    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LEU A 755    CG   CD1  CD2                                       
REMARK 470     PRO A 756    CG   CD                                             
REMARK 470     ILE A 757    CG1  CG2  CD1                                       
REMARK 470     GLU A 761    CG   CD   OE1  OE2                                  
REMARK 470     HIS A 762    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LYS A 763    CG   CD   CE   NZ                                   
REMARK 470     ASN A 765    CG   OD1  ND2                                       
REMARK 470     GLU A 767    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 769    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 770    CG   CD   OE1  OE2                                  
REMARK 470     ASP A 771    CG   OD1  OD2                                       
REMARK 470     VAL A 772    CG1  CG2                                            
REMARK 470     PRO A 774    CG   CD                                             
REMARK 470     VAL A 775    CG1  CG2                                            
REMARK 470     VAL A 776    CG1  CG2                                            
REMARK 470     GLN A 777    CG   CD   OE1  NE2                                  
REMARK 470     HIS A 778    CG   ND1  CD2  CE1  NE2                             
REMARK 470     ILE A 779    CG1  CG2  CD1                                       
REMARK 470     TYR A 780    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     GLU A 781    CG   CD   OE1  OE2                                  
REMARK 470     LEU A 782    CG   CD1  CD2                                       
REMARK 470     ARG A 783    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASN A 784    CG   OD1  ND2                                       
REMARK 470     ASN A 785    CG   OD1  ND2                                       
REMARK 470     PRO A 787    CG   CD                                             
REMARK 470     SER A 788    OG                                                  
REMARK 470     PHE A 790    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LYS A 792    CG   CD   CE   NZ                                   
REMARK 470     MET A 794    CG   SD   CE                                        
REMARK 470     LEU A 795    CG   CD1  CD2                                       
REMARK 470     HIS A 796    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LEU A 797    CG   CD1  CD2                                       
REMARK 470     TRP A 799    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP A 799    CZ3  CH2                                            
REMARK 470     PRO A 800    CG   CD                                             
REMARK 470     TYR A 801    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LYS A 802    CG   CD   CE   NZ                                   
REMARK 470     TYR A 803    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ASN A 804    CG   OD1  ND2                                       
REMARK 470     ASN A 805    CG   OD1  ND2                                       
REMARK 470     ASN A 806    CG   OD1  ND2                                       
REMARK 470     THR A 807    OG1  CG2                                            
REMARK 470     LEU A 808    CG   CD1  CD2                                       
REMARK 470     LEU A 809    CG   CD1  CD2                                       
REMARK 470     TYR A 810    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ILE A 811    CG1  CG2  CD1                                       
REMARK 470     LEU A 812    CG   CD1  CD2                                       
REMARK 470     HIS A 813    CG   ND1  CD2  CE1  NE2                             
REMARK 470     TYR A 814    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ASP A 815    CG   OD1  OD2                                       
REMARK 470     MET A 820    CG   SD   CE                                        
REMARK 470     ASN A 821    CG   OD1  ND2                                       
REMARK 470     CYS A 822    SG                                                  
REMARK 470     THR A 823    OG1  CG2                                            
REMARK 470     SER A 824    OG                                                  
REMARK 470     ASP A 825    CG   OD1  OD2                                       
REMARK 470     MET A 826    CG   SD   CE                                        
REMARK 470     ILE A 828    CG1  CG2  CD1                                       
REMARK 470     ASN A 829    CG   OD1  ND2                                       
REMARK 470     LEU A 831    CG   CD1  CD2                                       
REMARK 470     ARG A 832    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ILE A 833    CG1  CG2  CD1                                       
REMARK 470     CYS A 874    SG                                                  
REMARK 470     VAL A 876    CG1  CG2                                            
REMARK 470     GLN A 878    CG   CD   OE1  NE2                                  
REMARK 470     CYS A 879    SG                                                  
REMARK 470     LEU A 880    CG   CD1  CD2                                       
REMARK 470     LYS A 881    CG   CD   CE   NZ                                   
REMARK 470     ILE A 882    CG1  CG2  CD1                                       
REMARK 470     VAL A 883    CG1  CG2                                            
REMARK 470     CYS A 884    SG                                                  
REMARK 470     GLN A 885    CG   CD   OE1  NE2                                  
REMARK 470     VAL A 886    CG1  CG2                                            
REMARK 470     ARG A 888    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU A 889    CG   CD1  CD2                                       
REMARK 470     ASP A 890    CG   OD1  OD2                                       
REMARK 470     ARG A 891    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 893    CG   CD   CE   NZ                                   
REMARK 470     SER A 894    OG                                                  
REMARK 470     ILE A 896    CG1  CG2  CD1                                       
REMARK 470     LEU A 897    CG   CD1  CD2                                       
REMARK 470     TYR A 898    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     VAL A 899    CG1  CG2                                            
REMARK 470     LYS A 900    CG   CD   CE   NZ                                   
REMARK 470     SER A 901    OG                                                  
REMARK 470     LEU A 902    CG   CD1  CD2                                       
REMARK 470     LEU A 903    CG   CD1  CD2                                       
REMARK 470     TRP A 904    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP A 904    CZ3  CH2                                            
REMARK 470     THR A 905    OG1  CG2                                            
REMARK 470     GLU A 906    CG   CD   OE1  OE2                                  
REMARK 470     THR A 907    OG1  CG2                                            
REMARK 470     PHE A 908    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     MET A 909    CG   SD   CE                                        
REMARK 470     ASN A 910    CG   OD1  ND2                                       
REMARK 470     LYS A 911    CG   CD   CE   NZ                                   
REMARK 470     ASN A 913    CG   OD1  ND2                                       
REMARK 470     GLN A 914    CG   CD   OE1  NE2                                  
REMARK 470     ASN A 915    CG   OD1  ND2                                       
REMARK 470     HIS A 916    CG   ND1  CD2  CE1  NE2                             
REMARK 470     SER A 917    OG                                                  
REMARK 470     SER A 919    OG                                                  
REMARK 470     LEU A 920    CG   CD1  CD2                                       
REMARK 470     LYS A 921    CG   CD   CE   NZ                                   
REMARK 470     SER A 922    OG                                                  
REMARK 470     SER A 925    OG                                                  
REMARK 470     PHE A 926    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ASN A 927    CG   OD1  ND2                                       
REMARK 470     VAL A 928    CG1  CG2                                            
REMARK 470     ILE A 929    CG1  CG2  CD1                                       
REMARK 470     GLU A 930    CG   CD   OE1  OE2                                  
REMARK 470     PHE A 931    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     PRO A 932    CG   CD                                             
REMARK 470     TYR A 933    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LYS A 934    CG   CD   CE   NZ                                   
REMARK 470     ASN A 935    CG   OD1  ND2                                       
REMARK 470     LEU A 936    CG   CD1  CD2                                       
REMARK 470     PRO A 937    CG   CD                                             
REMARK 470     ILE A 938    CG1  CG2  CD1                                       
REMARK 470     GLU A 939    CG   CD   OE1  OE2                                  
REMARK 470     THR A 942    OG1  CG2                                            
REMARK 470     SER A 944    OG                                                  
REMARK 470     THR A 945    OG1  CG2                                            
REMARK 470     LEU A 946    CG   CD1  CD2                                       
REMARK 470     VAL A 947    CG1  CG2                                            
REMARK 470     THR A 948    OG1  CG2                                            
REMARK 470     THR A 949    OG1  CG2                                            
REMARK 470     ASN A 950    CG   OD1  ND2                                       
REMARK 470     VAL A 951    CG1  CG2                                            
REMARK 470     THR A 952    OG1  CG2                                            
REMARK 470     TRP A 953    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP A 953    CZ3  CH2                                            
REMARK 470     ILE B   4    CG1  CG2  CD1                                       
REMARK 470     THR B   7    OG1  CG2                                            
REMARK 470     ARG B   8    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     SER B  11    OG                                                  
REMARK 470     SER B  12    OG                                                  
REMARK 470     GLN B  14    CG   CD   OE1  NE2                                  
REMARK 470     GLN B  15    CG   CD   OE1  NE2                                  
REMARK 470     LEU B  17    CG   CD1  CD2                                       
REMARK 470     VAL B  19    CG1  CG2                                            
REMARK 470     ASP B  28    CG   OD1  OD2                                       
REMARK 470     GLU B  29    CG   CD   OE1  OE2                                  
REMARK 470     LEU B  33    CG   CD1  CD2                                       
REMARK 470     SER B  35    OG                                                  
REMARK 470     PRO B  36    CG   CD                                             
REMARK 470     ARG B  37    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP B  39    CG   OD1  OD2                                       
REMARK 470     LEU B  40    CG   CD1  CD2                                       
REMARK 470     LYS B  41    CG   CD   CE   NZ                                   
REMARK 470     GLU B  42    CG   CD   OE1  OE2                                  
REMARK 470     ASN B  43    CG   OD1  ND2                                       
REMARK 470     LEU B  44    CG   CD1  CD2                                       
REMARK 470     LEU B  45    CG   CD1  CD2                                       
REMARK 470     LYS B  46    CG   CD   CE   NZ                                   
REMARK 470     GLU B  52    CG   CD   OE1  OE2                                  
REMARK 470     ILE B  54    CG1  CG2  CD1                                       
REMARK 470     GLU B  55    CG   CD   OE1  OE2                                  
REMARK 470     PHE B  56    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     VAL B  58    CG1  CG2                                            
REMARK 470     GLU B  60    CG   CD   OE1  OE2                                  
REMARK 470     ARG B  62    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     VAL B  63    CG1  CG2                                            
REMARK 470     LYS B  72    CG   CD   CE   NZ                                   
REMARK 470     ASP B  76    CG   OD1  OD2                                       
REMARK 470     SER B  77    OG                                                  
REMARK 470     THR B  81    OG1  CG2                                            
REMARK 470     GLN B  82    CG   CD   OE1  NE2                                  
REMARK 470     VAL B  83    CG1  CG2                                            
REMARK 470     SER B  84    OG                                                  
REMARK 470     LEU B  90    CG   CD1  CD2                                       
REMARK 470     ARG B  91    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU B  92    CG   CD1  CD2                                       
REMARK 470     ARG B  93    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     SER B  97    OG                                                  
REMARK 470     LYS B  98    CG   CD   CE   NZ                                   
REMARK 470     SER B 101    OG                                                  
REMARK 470     GLN B 103    CG   CD   OE1  NE2                                  
REMARK 470     VAL B 104    CG1  CG2                                            
REMARK 470     VAL B 107    CG1  CG2                                            
REMARK 470     VAL B 112    CG1  CG2                                            
REMARK 470     LEU B 117    CG   CD1  CD2                                       
REMARK 470     LYS B 125    CG   CD   CE   NZ                                   
REMARK 470     LEU B 128    CG   CD1  CD2                                       
REMARK 470     LYS B 137    CG   CD   CE   NZ                                   
REMARK 470     THR B 146    OG1  CG2                                            
REMARK 470     ASN B 148    CG   OD1  ND2                                       
REMARK 470     LEU B 149    CG   CD1  CD2                                       
REMARK 470     ARG B 150    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     VAL B 157    CG1  CG2                                            
REMARK 470     ASP B 179    CG   OD1  OD2                                       
REMARK 470     LYS B 181    CG   CD   CE   NZ                                   
REMARK 470     THR B 182    OG1  CG2                                            
REMARK 470     THR B 183    OG1  CG2                                            
REMARK 470     LEU B 185    CG   CD1  CD2                                       
REMARK 470     LYS B 191    CG   CD   CE   NZ                                   
REMARK 470     ASP B 198    CG   OD1  OD2                                       
REMARK 470     LYS B 208    CG   CD   CE   NZ                                   
REMARK 470     SER B 211    OG                                                  
REMARK 470     VAL B 212    CG1  CG2                                            
REMARK 470     ASN B 215    CG   OD1  ND2                                       
REMARK 470     ARG B 216    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ILE B 226    CG1  CG2  CD1                                       
REMARK 470     VAL B 231    CG1  CG2                                            
REMARK 470     LYS B 235    CG   CD   CE   NZ                                   
REMARK 470     LYS B 253    CG   CD   CE   NZ                                   
REMARK 470     VAL B 266    CG1  CG2                                            
REMARK 470     GLN B 267    CG   CD   OE1  NE2                                  
REMARK 470     GLN B 272    CG   CD   OE1  NE2                                  
REMARK 470     VAL B 275    CG1  CG2                                            
REMARK 470     SER B 282    OG                                                  
REMARK 470     THR B 286    OG1  CG2                                            
REMARK 470     LEU B 292    CG   CD1  CD2                                       
REMARK 470     LYS B 302    CG   CD   CE   NZ                                   
REMARK 470     ILE B 307    CG1  CG2  CD1                                       
REMARK 470     VAL B 310    CG1  CG2                                            
REMARK 470     GLU B 312    CG   CD   OE1  OE2                                  
REMARK 470     VAL B 314    CG1  CG2                                            
REMARK 470     GLU B 323    CG   CD   OE1  OE2                                  
REMARK 470     LEU B 324    CG   CD1  CD2                                       
REMARK 470     THR B 328    OG1  CG2                                            
REMARK 470     VAL B 330    CG1  CG2                                            
REMARK 470     SER B 337    OG                                                  
REMARK 470     LYS B 350    CG   CD   CE   NZ                                   
REMARK 470     SER B 353    OG                                                  
REMARK 470     LYS B 354    CG   CD   CE   NZ                                   
REMARK 470     GLU B 356    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 358    CG   CD   OE1  OE2                                  
REMARK 470     VAL B 359    CG1  CG2                                            
REMARK 470     ARG B 360    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B 365    CG   CD   OE1  OE2                                  
REMARK 470     SER B 367    OG                                                  
REMARK 470     LEU B 368    CG   CD1  CD2                                       
REMARK 470     SER B 369    OG                                                  
REMARK 470     LEU B 375    CG   CD1  CD2                                       
REMARK 470     ASN B 376    CG   OD1  ND2                                       
REMARK 470     GLU B 378    CG   CD   OE1  OE2                                  
REMARK 470     ILE B 380    CG1  CG2  CD1                                       
REMARK 470     LEU B 383    CG   CD1  CD2                                       
REMARK 470     LYS B 384    CG   CD   CE   NZ                                   
REMARK 470     SER B 385    OG                                                  
REMARK 470     MET B 387    CG   SD   CE                                        
REMARK 470     LYS B 390    CG   CD   CE   NZ                                   
REMARK 470     ASP B 393    CG   OD1  OD2                                       
REMARK 470     THR B 394    OG1  CG2                                            
REMARK 470     VAL B 395    CG1  CG2                                            
REMARK 470     LYS B 402    CG   CD   CE   NZ                                   
REMARK 470     VAL B 403    CG1  CG2                                            
REMARK 470     ARG B 404    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B 409    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 412    CG   CD   CE   NZ                                   
REMARK 470     THR B 415    OG1  CG2                                            
REMARK 470     VAL B 419    CG1  CG2                                            
REMARK 470     LYS B 422    CG   CD   CE   NZ                                   
REMARK 470     SER B 424    OG                                                  
REMARK 470     VAL B 427    CG1  CG2                                            
REMARK 470     VAL B 429    CG1  CG2                                            
REMARK 470     GLN B 438    CG   CD   OE1  NE2                                  
REMARK 470     GLN B 440    CG   CD   OE1  NE2                                  
REMARK 470     GLU B 442    CG   CD   OE1  OE2                                  
REMARK 470     ASN B 444    CG   OD1  ND2                                       
REMARK 470     HIS B 446    CG   ND1  CD2  CE1  NE2                             
REMARK 470     ARG B 447    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASN B 449    CG   OD1  ND2                                       
REMARK 470     ASN B 450    CG   OD1  ND2                                       
REMARK 470     ASN B 452    CG   OD1  ND2                                       
REMARK 470     THR B 454    OG1  CG2                                            
REMARK 470     GLU B 456    CG   CD   OE1  OE2                                  
REMARK 470     VAL B 459    CG1  CG2                                            
REMARK 470     ARG B 461    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     PRO B 464    CG   CD                                             
REMARK 470     TRP B 466    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP B 466    CZ3  CH2                                            
REMARK 470     LEU B 467    CG   CD1  CD2                                       
REMARK 470     GLN B 470    CG   CD   OE1  NE2                                  
REMARK 470     GLU B 472    CG   CD   OE1  OE2                                  
REMARK 470     SER B 474    OG                                                  
REMARK 470     GLU B 475    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 476    CG   CD   OE1  OE2                                  
REMARK 470     ASP B 477    CG   OD1  OD2                                       
REMARK 470     TYR B 478    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ARG B 479    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN B 482    CG   CD   OE1  NE2                                  
REMARK 470     GLN B 483    CG   CD   OE1  NE2                                  
REMARK 470     ASP B 484    CG   OD1  OD2                                       
REMARK 470     GLU B 485    CG   CD   OE1  OE2                                  
REMARK 470     SER B 487    OG                                                  
REMARK 470     ARG B 489    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B 490    CG   CD   OE1  OE2                                  
REMARK 470     VAL B 494    CG1  CG2                                            
REMARK 470     ARG B 498    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B 500    CG   CD   OE1  OE2                                  
REMARK 470     LEU B 502    CG   CD1  CD2                                       
REMARK 470     CYS B 503    SG                                                  
REMARK 470     GLN B 505    CG   CD   OE1  NE2                                  
REMARK 470     VAL B 507    CG1  CG2                                            
REMARK 470     SER B 510    OG                                                  
REMARK 470     SER B 511    OG                                                  
REMARK 470     ASP B 512    CG   OD1  OD2                                       
REMARK 470     LYS B 515    CG   CD   CE   NZ                                   
REMARK 470     ILE B 516    CG1  CG2  CD1                                       
REMARK 470     THR B 517    OG1  CG2                                            
REMARK 470     LYS B 519    CG   CD   CE   NZ                                   
REMARK 470     GLU B 522    CG   CD   OE1  OE2                                  
REMARK 470     ASP B 524    CG   OD1  OD2                                       
REMARK 470     PHE B 526    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     SER B 527    OG                                                  
REMARK 470     VAL B 529    CG1  CG2                                            
REMARK 470     ARG B 530    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 532    CG   CD   CE   NZ                                   
REMARK 470     MET B 535    CG   SD   CE                                        
REMARK 470     SER B 537    OG                                                  
REMARK 470     HIS B 539    CG   ND1  CD2  CE1  NE2                             
REMARK 470     GLN B 541    CG   CD   OE1  NE2                                  
REMARK 470     SER B 543    OG                                                  
REMARK 470     ASP B 546    CG   OD1  OD2                                       
REMARK 470     LEU B 548    CG   CD1  CD2                                       
REMARK 470     SER B 551    OG                                                  
REMARK 470     ASP B 552    CG   OD1  OD2                                       
REMARK 470     THR B 554    OG1  CG2                                            
REMARK 470     TYR B 556    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     TYR B 557    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     THR B 561    OG1  CG2                                            
REMARK 470     THR B 562    OG1  CG2                                            
REMARK 470     ARG B 563    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     THR B 564    OG1  CG2                                            
REMARK 470     ASP B 565    CG   OD1  OD2                                       
REMARK 470     SER B 569    OG                                                  
REMARK 470     SER B 570    OG                                                  
REMARK 470     LEU B 573    CG   CD1  CD2                                       
REMARK 470     LEU B 574    CG   CD1  CD2                                       
REMARK 470     ARG B 578    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 580    CG   CD   CE   NZ                                   
REMARK 470     GLU B 582    CG   CD   OE1  OE2                                  
REMARK 470     VAL B 587    CG1  CG2                                            
REMARK 470     GLN B 590    CG   CD   OE1  NE2                                  
REMARK 470     SER B 593    OG                                                  
REMARK 470     GLU B 599    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 600    CG   CD   CE   NZ                                   
REMARK 470     THR B 603    OG1  CG2                                            
REMARK 470     ASP B 606    CG   OD1  OD2                                       
REMARK 470     THR B 609    OG1  CG2                                            
REMARK 470     PHE B 610    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LYS B 611    CG   CD   CE   NZ                                   
REMARK 470     LYS B 612    CG   CD   CE   NZ                                   
REMARK 470     GLU B 613    CG   CD   OE1  OE2                                  
REMARK 470     VAL B 615    CG1  CG2                                            
REMARK 470     GLU B 616    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 618    CG   CD   CE   NZ                                   
REMARK 470     LYS B 619    CG   CD   CE   NZ                                   
REMARK 470     PHE B 620    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ASP B 621    CG   OD1  OD2                                       
REMARK 470     ARG B 622    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU B 625    CG   CD1  CD2                                       
REMARK 470     HIS B 626    CG   ND1  CD2  CE1  NE2                             
REMARK 470     ASP B 627    CG   OD1  OD2                                       
REMARK 470     GLU B 628    CG   CD   OE1  OE2                                  
REMARK 470     ASN B 629    CG   OD1  ND2                                       
REMARK 470     THR B 630    OG1  CG2                                            
REMARK 470     ARG B 633    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     TYR B 634    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ARG B 636    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP B 637    CG   OD1  OD2                                       
REMARK 470     GLU B 638    CG   CD   OE1  OE2                                  
REMARK 470     ILE B 639    CG1  CG2  CD1                                       
REMARK 470     GLU B 640    CG   CD   OE1  OE2                                  
REMARK 470     SER B 641    OG                                                  
REMARK 470     VAL B 642    CG1  CG2                                            
REMARK 470     LYS B 643    CG   CD   CE   NZ                                   
REMARK 470     GLU B 644    CG   CD   OE1  OE2                                  
REMARK 470     LEU B 645    CG   CD1  CD2                                       
REMARK 470     LYS B 646    CG   CD   CE   NZ                                   
REMARK 470     ASP B 647    CG   OD1  OD2                                       
REMARK 470     THR B 648    OG1  CG2                                            
REMARK 470     LYS B 650    CG   CD   CE   NZ                                   
REMARK 470     ASP B 651    CG   OD1  OD2                                       
REMARK 470     VAL B 653    CG1  CG2                                            
REMARK 470     ASN B 654    CG   OD1  ND2                                       
REMARK 470     THR B 656    OG1  CG2                                            
REMARK 470     TYR B 657    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LYS B 658    CG   CD   CE   NZ                                   
REMARK 470     ASN B 659    CG   OD1  ND2                                       
REMARK 470     GLU B 660    CG   CD   OE1  OE2                                  
REMARK 470     ASP B 661    CG   OD1  OD2                                       
REMARK 470     ASP B 662    CG   OD1  OD2                                       
REMARK 470     CYS B 663    SG                                                  
REMARK 470     VAL B 664    CG1  CG2                                            
REMARK 470     VAL B 665    CG1  CG2                                            
REMARK 470     ARG B 666    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     PHE B 667    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     GLN B 668    CG   CD   OE1  NE2                                  
REMARK 470     TYR B 669    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     TYR B 670    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     GLU B 671    CG   CD   OE1  OE2                                  
REMARK 470     ASP B 672    CG   OD1  OD2                                       
REMARK 470     SER B 673    OG                                                  
REMARK 470     SER B 674    OG                                                  
REMARK 470     LYS B 676    CG   CD   CE   NZ                                   
REMARK 470     SER B 677    OG                                                  
REMARK 470     ILE B 678    CG1  CG2  CD1                                       
REMARK 470     LEU B 679    CG   CD1  CD2                                       
REMARK 470     TYR B 680    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     VAL B 681    CG1  CG2                                            
REMARK 470     VAL B 682    CG1  CG2                                            
REMARK 470     GLU B 683    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 684    CG   CD   OE1  OE2                                  
REMARK 470     PRO B 685    CG   CD                                             
REMARK 470     GLU B 686    CG   CD   OE1  OE2                                  
REMARK 470     CYS B 687    SG                                                  
REMARK 470     ILE L   2    CG1  CG2  CD1                                       
REMARK 470     GLN L   3    CG   CD   OE1  NE2                                  
REMARK 470     LEU L  11    CG   CD1  CD2                                       
REMARK 470     LEU L  15    CG   CD1  CD2                                       
REMARK 470     VAL L  19    CG1  CG2                                            
REMARK 470     LEU L  33    CG   CD1  CD2                                       
REMARK 470     SER L  34    OG                                                  
REMARK 470     LYS L  39    CG   CD   CE   NZ                                   
REMARK 470     VAL L  44    CG1  CG2                                            
REMARK 470     LYS L  45    CG   CD   CE   NZ                                   
REMARK 470     THR L  51    OG1  CG2                                            
REMARK 470     SER L  52    OG                                                  
REMARK 470     LYS L  53    CG   CD   CE   NZ                                   
REMARK 470     SER L  63    OG                                                  
REMARK 470     ILE L  83    CG1  CG2  CD1                                       
REMARK 470     LYS L 103    CG   CD   CE   NZ                                   
REMARK 470     VAL L 104    CG1  CG2                                            
REMARK 470     GLU L 105    CG   CD   OE1  OE2                                  
REMARK 470     ARG L 107    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     THR L 114    OG1  CG2                                            
REMARK 470     SER L 116    OG                                                  
REMARK 470     ILE L 117    CG1  CG2  CD1                                       
REMARK 470     PHE L 118    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     PRO L 119    CG   CD                                             
REMARK 470     SER L 121    OG                                                  
REMARK 470     SER L 122    OG                                                  
REMARK 470     GLU L 123    CG   CD   OE1  OE2                                  
REMARK 470     GLN L 124    CG   CD   OE1  NE2                                  
REMARK 470     LEU L 125    CG   CD1  CD2                                       
REMARK 470     THR L 126    OG1  CG2                                            
REMARK 470     SER L 127    OG                                                  
REMARK 470     SER L 131    OG                                                  
REMARK 470     VAL L 132    CG1  CG2                                            
REMARK 470     VAL L 133    CG1  CG2                                            
REMARK 470     PHE L 135    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LEU L 136    CG   CD1  CD2                                       
REMARK 470     LYS L 142    CG   CD   CE   NZ                                   
REMARK 470     ILE L 144    CG1  CG2  CD1                                       
REMARK 470     VAL L 146    CG1  CG2                                            
REMARK 470     LYS L 147    CG   CD   CE   NZ                                   
REMARK 470     LYS L 149    CG   CD   CE   NZ                                   
REMARK 470     ILE L 150    CG1  CG2  CD1                                       
REMARK 470     GLU L 154    CG   CD   OE1  OE2                                  
REMARK 470     ARG L 155    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN L 156    CG   CD   OE1  NE2                                  
REMARK 470     THR L 164    OG1  CG2                                            
REMARK 470     ASP L 165    CG   OD1  OD2                                       
REMARK 470     ASP L 167    CG   OD1  OD2                                       
REMARK 470     LYS L 169    CG   CD   CE   NZ                                   
REMARK 470     MET L 175    CG   SD   CE                                        
REMARK 470     SER L 177    OG                                                  
REMARK 470     LEU L 181    CG   CD1  CD2                                       
REMARK 470     ASP L 184    CG   OD1  OD2                                       
REMARK 470     TYR L 186    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     GLU L 187    CG   CD   OE1  OE2                                  
REMARK 470     ARG L 188    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASN L 190    CG   OD1  ND2                                       
REMARK 470     THR L 197    OG1  CG2                                            
REMARK 470     LYS L 199    CG   CD   CE   NZ                                   
REMARK 470     ILE L 205    CG1  CG2  CD1                                       
REMARK 470     LYS L 207    CG   CD   CE   NZ                                   
REMARK 470     SER L 208    OG                                                  
REMARK 470     PHE L 209    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ASN L 210    CG   OD1  ND2                                       
REMARK 470     ARG L 211    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU L 213    CG   CD   OE1  OE2                                  
REMARK 470     CYS L 214    SG                                                  
REMARK 470     GLN H   5    CG   CD   OE1  NE2                                  
REMARK 470     SER H   7    OG                                                  
REMARK 470     LEU H  11    CG   CD1  CD2                                       
REMARK 470     VAL H  18    CG1  CG2                                            
REMARK 470     LYS H  19    CG   CD   CE   NZ                                   
REMARK 470     SER H  21    OG                                                  
REMARK 470     LYS H  23    CG   CD   CE   NZ                                   
REMARK 470     SER H  30    OG                                                  
REMARK 470     LYS H  38    CG   CD   CE   NZ                                   
REMARK 470     ARG H  40    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU H  45    CG   CD1  CD2                                       
REMARK 470     GLU H  46    CG   CD   OE1  OE2                                  
REMARK 470     ILE H  48    CG1  CG2  CD1                                       
REMARK 470     ILE H  51    CG1  CG2  CD1                                       
REMARK 470     ILE H  63    CG1  CG2  CD1                                       
REMARK 470     LYS H  67    CG   CD   CE   NZ                                   
REMARK 470     THR H  71    OG1  CG2                                            
REMARK 470     MET H  81    CG   SD   CE                                        
REMARK 470     SER H  84    OG                                                  
REMARK 470     LEU H  86    CG   CD1  CD2                                       
REMARK 470     VAL H  93    CG1  CG2                                            
REMARK 470     SER H  98    OG                                                  
REMARK 470     SER H 113    OG                                                  
REMARK 470     VAL H 114    CG1  CG2                                            
REMARK 470     LYS H 120    CG   CD   CE   NZ                                   
REMARK 470     THR H 122    OG1  CG2                                            
REMARK 470     PRO H 124    CG   CD                                             
REMARK 470     SER H 125    OG                                                  
REMARK 470     VAL H 126    CG1  CG2                                            
REMARK 470     PRO H 128    CG   CD                                             
REMARK 470     LEU H 129    CG   CD1  CD2                                       
REMARK 470     PRO H 131    CG   CD                                             
REMARK 470     VAL H 132    CG1  CG2                                            
REMARK 470     CYS H 133    SG                                                  
REMARK 470     ASP H 135    CG   OD1  OD2                                       
REMARK 470     SER H 140    OG                                                  
REMARK 470     VAL H 141    CG1  CG2                                            
REMARK 470     THR H 142    OG1  CG2                                            
REMARK 470     LEU H 143    CG   CD1  CD2                                       
REMARK 470     LEU H 146    CG   CD1  CD2                                       
REMARK 470     VAL H 147    CG1  CG2                                            
REMARK 470     PRO H 152    CG   CD                                             
REMARK 470     GLU H 153    CG   CD   OE1  OE2                                  
REMARK 470     VAL H 155    CG1  CG2                                            
REMARK 470     THR H 156    OG1  CG2                                            
REMARK 470     LEU H 157    CG   CD1  CD2                                       
REMARK 470     THR H 158    OG1  CG2                                            
REMARK 470     ASN H 160    CG   OD1  ND2                                       
REMARK 470     SER H 161    OG                                                  
REMARK 470     SER H 163    OG                                                  
REMARK 470     LEU H 164    CG   CD1  CD2                                       
REMARK 470     SER H 165    OG                                                  
REMARK 470     VAL H 168    CG1  CG2                                            
REMARK 470     HIS H 169    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LEU H 175    CG   CD1  CD2                                       
REMARK 470     LEU H 179    CG   CD1  CD2                                       
REMARK 470     SER H 183    OG                                                  
REMARK 470     THR H 187    OG1  CG2                                            
REMARK 470     VAL H 188    CG1  CG2                                            
REMARK 470     THR H 189    OG1  CG2                                            
REMARK 470     SER H 191    OG                                                  
REMARK 470     THR H 192    OG1  CG2                                            
REMARK 470     SER H 195    OG                                                  
REMARK 470     GLN H 196    CG   CD   OE1  NE2                                  
REMARK 470     SER H 197    OG                                                  
REMARK 470     ILE H 198    CG1  CG2  CD1                                       
REMARK 470     ASN H 201    CG   OD1  ND2                                       
REMARK 470     VAL H 202    CG1  CG2                                            
REMARK 470     HIS H 204    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LYS H 210    CG   CD   CE   NZ                                   
REMARK 470     VAL H 211    CG1  CG2                                            
REMARK 470     LYS H 214    CG   CD   CE   NZ                                   
REMARK 470     ILE H 215    CG1  CG2  CD1                                       
REMARK 470     GLU H 216    CG   CD   OE1  OE2                                  
REMARK 470     PRO H 217    CG   CD                                             
REMARK 470     ARG H 218    CG   CD   NE   CZ   NH1  NH2                        
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    ALA A  30      -74.06    -81.63                                   
REMARK 500    SER A  63     -136.31     59.51                                   
REMARK 500    ARG A  66     -148.07     62.41                                   
REMARK 500    GLN A 102     -128.31     55.03                                   
REMARK 500    ASP A 132      -80.31   -152.86                                   
REMARK 500    THR A 134      -77.76   -125.71                                   
REMARK 500    LYS A 135      118.96     35.75                                   
REMARK 500    ASP A 148     -178.40    175.08                                   
REMARK 500    ALA A 166     -167.09    -75.69                                   
REMARK 500    PHE A 231      -59.55   -129.81                                   
REMARK 500    ASP A 234     -162.25   -124.83                                   
REMARK 500    LEU A 264      -63.24   -104.36                                   
REMARK 500    SER A 305     -113.32     48.90                                   
REMARK 500    ARG A 339       71.50     55.07                                   
REMARK 500    GLN A 394      -60.40   -104.14                                   
REMARK 500    ALA A 396      -71.22    -74.61                                   
REMARK 500    ARG A 398      -70.37   -129.95                                   
REMARK 500    SER A 399      -72.45   -115.01                                   
REMARK 500    ALA A 411       -4.02     69.63                                   
REMARK 500    ILE A 453      163.18    173.13                                   
REMARK 500    THR A 460      -67.94   -132.64                                   
REMARK 500    LEU A 463      138.40   -175.13                                   
REMARK 500    PRO A 488       65.66    -63.79                                   
REMARK 500    ARG A 489     -113.24     56.71                                   
REMARK 500    ASP A 500      -75.69   -101.21                                   
REMARK 500    LYS A 501      -46.39     73.87                                   
REMARK 500    LYS A 503     -164.16   -170.37                                   
REMARK 500    GLN A 504      -15.07     77.29                                   
REMARK 500    ALA A 507     -131.88     59.17                                   
REMARK 500    TYR A 515      -66.45   -125.52                                   
REMARK 500    LYS A 523      108.82   -161.53                                   
REMARK 500    ARG A 529     -145.15     54.57                                   
REMARK 500    LEU A 532       72.97     48.80                                   
REMARK 500    GLU A 545     -113.29     52.27                                   
REMARK 500    GLU A 547      -14.57     77.63                                   
REMARK 500    ASP A 550     -147.67     52.50                                   
REMARK 500    LYS A 551      173.61    171.37                                   
REMARK 500    ILE A 555       92.12     59.20                                   
REMARK 500    THR A 572      -75.96    -99.83                                   
REMARK 500    GLN A 580      -72.73    -57.77                                   
REMARK 500    ASP A 595     -147.73     57.19                                   
REMARK 500    CYS A 596      -17.18     64.38                                   
REMARK 500    ASP A 599      -53.56   -144.31                                   
REMARK 500    ASN A 600       -2.51     91.60                                   
REMARK 500    ASP A 613      -63.13   -105.96                                   
REMARK 500    GLN A 614      -54.43   -128.07                                   
REMARK 500    LYS A 615       84.92     63.23                                   
REMARK 500    ILE A 619        1.65     83.80                                   
REMARK 500    ALA A 651      152.29    176.29                                   
REMARK 500    ASN A 659      -70.52   -126.10                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     166 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 THR A  134     LYS A  135                  140.80                    
REMARK 500 THR A  768     GLU A  769                 -149.16                    
REMARK 500 ARG B    8     GLY B    9                 -148.63                    
REMARK 500 ALA B   50     PRO B   51                  120.79                    
REMARK 500 SER B   53     ILE B   54                  149.95                    
REMARK 500 ALA B  624     LEU B  625                  138.44                    
REMARK 500 PHE L   94     PRO L   95                 -106.29                    
REMARK 500 TYR L  140     PRO L  141                 -114.64                    
REMARK 500 SER L  168     LYS L  169                 -142.02                    
REMARK 500 SER H  139     SER H  140                 -146.15                    
REMARK 500 PHE H  151     PRO H  152                  118.44                    
REMARK 500 ASP H  178     LEU H  179                  146.88                    
REMARK 500 LEU H  179     TYR H  180                  141.52                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN A1026  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 292   OD1                                                    
REMARK 620 2 ASP A 292   OD2  60.9                                              
REMARK 620 3 ASN A 286   OD1 116.0  88.5                                        
REMARK 620 4 ASP A 288   OD1 152.4 146.6  72.8                                  
REMARK 620 5 ASP A 284   OD1 135.4  77.5  75.4  71.2                            
REMARK 620 6 TYR A 290   O    90.9  97.2 151.4  87.9  78.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN A1028  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 TYR A 419   O                                                      
REMARK 620 2 ASP A 413   OD1  79.8                                              
REMARK 620 3 ASN A 417   OD1  81.9  88.9                                        
REMARK 620 4 ASP A 421   OD2 111.5 132.7 137.1                                  
REMARK 620 5 ASP A 421   OD1  93.4  75.0 163.8  59.0                            
REMARK 620 6 ASP A 415   OD1 154.4  80.6  81.5  93.9  97.2                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN B 707  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SER B 123   O                                                      
REMARK 620 2 ASP B 127   OD1 101.5                                              
REMARK 620 3 ASP B 126   OD1 109.4 117.5                                        
REMARK 620 4 ASP B 126   OD2  93.9  64.3  60.7                                  
REMARK 620 5 MET B 335   O   161.6  84.5  82.3 104.4                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN A1027  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 349   OD2                                                    
REMARK 620 2 ASP A 353   OD2  68.6                                              
REMARK 620 3 ASP A 357   OD2 136.7 146.1                                        
REMARK 620 4 PHE A 355   O    78.9  84.7  80.9                                  
REMARK 620 5 ASP A 357   OD1  90.0 153.8  60.0 106.6                            
REMARK 620 6 ASP A 351   OD2  75.2  71.1 129.4 149.5  89.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN A1025  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN A 232   OD1                                                    
REMARK 620 2 ASN A 232   O    46.5                                              
REMARK 620 3 ASP A 234   O   115.3  85.7                                        
REMARK 620 4 ASP A 230   OD2 139.4  99.9  75.8                                  
REMARK 620 5 ASP A 238   OD2 109.6 117.0 132.8  60.4                            
REMARK 620 6 ASP A 238   OD1  77.8 119.5 148.8 113.8  54.8                      
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 NAG A 1001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 1002                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA A 1003                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 1004                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA A 1005                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 1006                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 1007                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 1008                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA A 1009                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 1010                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 1011                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA A 1012                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 1013                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 1014                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 1015                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 1016                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 1017                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 1018                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 1019                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 1020                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA A 1021                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 1022                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 1023                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 1024                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 1025                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 1026                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 1027                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 1028                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO3 A 1029                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO3 A 1030                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 701                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 702                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 703                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 704                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 705                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 706                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN B 707                  
DBREF  4O02 A    1   962  UNP    P06756   ITAV_HUMAN      31    992             
DBREF  4O02 B    1   692  UNP    P05106   ITB3_HUMAN      27    718             
DBREF  4O02 L    1   214  PDB    4O02     4O02             1    214             
DBREF  4O02 H    1   218  PDB    4O02     4O02             1    218             
SEQRES   1 A  962  PHE ASN LEU ASP VAL ASP SER PRO ALA GLU TYR SER GLY          
SEQRES   2 A  962  PRO GLU GLY SER TYR PHE GLY PHE ALA VAL ASP PHE PHE          
SEQRES   3 A  962  VAL PRO SER ALA SER SER ARG MET PHE LEU LEU VAL GLY          
SEQRES   4 A  962  ALA PRO LYS ALA ASN THR THR GLN PRO GLY ILE VAL GLU          
SEQRES   5 A  962  GLY GLY GLN VAL LEU LYS CYS ASP TRP SER SER THR ARG          
SEQRES   6 A  962  ARG CYS GLN PRO ILE GLU PHE ASP ALA THR GLY ASN ARG          
SEQRES   7 A  962  ASP TYR ALA LYS ASP ASP PRO LEU GLU PHE LYS SER HIS          
SEQRES   8 A  962  GLN TRP PHE GLY ALA SER VAL ARG SER LYS GLN ASP LYS          
SEQRES   9 A  962  ILE LEU ALA CYS ALA PRO LEU TYR HIS TRP ARG THR GLU          
SEQRES  10 A  962  MET LYS GLN GLU ARG GLU PRO VAL GLY THR CYS PHE LEU          
SEQRES  11 A  962  GLN ASP GLY THR LYS THR VAL GLU TYR ALA PRO CYS ARG          
SEQRES  12 A  962  SER GLN ASP ILE ASP ALA ASP GLY GLN GLY PHE CYS GLN          
SEQRES  13 A  962  GLY GLY PHE SER ILE ASP PHE THR LYS ALA ASP ARG VAL          
SEQRES  14 A  962  LEU LEU GLY GLY PRO GLY SER PHE TYR TRP GLN GLY GLN          
SEQRES  15 A  962  LEU ILE SER ASP GLN VAL ALA GLU ILE VAL SER LYS TYR          
SEQRES  16 A  962  ASP PRO ASN VAL TYR SER ILE LYS TYR ASN ASN GLN LEU          
SEQRES  17 A  962  ALA THR ARG THR ALA GLN ALA ILE PHE ASP ASP SER TYR          
SEQRES  18 A  962  LEU GLY TYR SER VAL ALA VAL GLY ASP PHE ASN GLY ASP          
SEQRES  19 A  962  GLY ILE ASP ASP PHE VAL SER GLY VAL PRO ARG ALA ALA          
SEQRES  20 A  962  ARG THR LEU GLY MET VAL TYR ILE TYR ASP GLY LYS ASN          
SEQRES  21 A  962  MET SER SER LEU TYR ASN PHE THR GLY GLU GLN MET ALA          
SEQRES  22 A  962  ALA TYR PHE GLY PHE SER VAL ALA ALA THR ASP ILE ASN          
SEQRES  23 A  962  GLY ASP ASP TYR ALA ASP VAL PHE ILE GLY ALA PRO LEU          
SEQRES  24 A  962  PHE MET ASP ARG GLY SER ASP GLY LYS LEU GLN GLU VAL          
SEQRES  25 A  962  GLY GLN VAL SER VAL SER LEU GLN ARG ALA SER GLY ASP          
SEQRES  26 A  962  PHE GLN THR THR LYS LEU ASN GLY PHE GLU VAL PHE ALA          
SEQRES  27 A  962  ARG PHE GLY SER ALA ILE ALA PRO LEU GLY ASP LEU ASP          
SEQRES  28 A  962  GLN ASP GLY PHE ASN ASP ILE ALA ILE ALA ALA PRO TYR          
SEQRES  29 A  962  GLY GLY GLU ASP LYS LYS GLY ILE VAL TYR ILE PHE ASN          
SEQRES  30 A  962  GLY ARG SER THR GLY LEU ASN ALA VAL PRO SER GLN ILE          
SEQRES  31 A  962  LEU GLU GLY GLN TRP ALA ALA ARG SER MET PRO PRO SER          
SEQRES  32 A  962  PHE GLY TYR SER MET LYS GLY ALA THR ASP ILE ASP LYS          
SEQRES  33 A  962  ASN GLY TYR PRO ASP LEU ILE VAL GLY ALA PHE GLY VAL          
SEQRES  34 A  962  ASP ARG ALA ILE LEU TYR ARG ALA ARG PRO VAL ILE THR          
SEQRES  35 A  962  VAL ASN ALA GLY LEU GLU VAL TYR PRO SER ILE LEU ASN          
SEQRES  36 A  962  GLN ASP ASN LYS THR CYS SER LEU PRO GLY THR ALA LEU          
SEQRES  37 A  962  LYS VAL SER CYS PHE ASN VAL ARG PHE CYS LEU LYS ALA          
SEQRES  38 A  962  ASP GLY LYS GLY VAL LEU PRO ARG LYS LEU ASN PHE GLN          
SEQRES  39 A  962  VAL GLU LEU LEU LEU ASP LYS LEU LYS GLN LYS GLY ALA          
SEQRES  40 A  962  ILE ARG ARG ALA LEU PHE LEU TYR SER ARG SER PRO SER          
SEQRES  41 A  962  HIS SER LYS ASN MET THR ILE SER ARG GLY GLY LEU MET          
SEQRES  42 A  962  GLN CYS GLU GLU LEU ILE ALA TYR LEU ARG ASP GLU SER          
SEQRES  43 A  962  GLU PHE ARG ASP LYS LEU THR PRO ILE THR ILE PHE MET          
SEQRES  44 A  962  GLU TYR ARG LEU ASP TYR ARG THR ALA ALA ASP THR THR          
SEQRES  45 A  962  GLY LEU GLN PRO ILE LEU ASN GLN PHE THR PRO ALA ASN          
SEQRES  46 A  962  ILE SER ARG GLN ALA HIS ILE LEU LEU ASP CYS GLY GLU          
SEQRES  47 A  962  ASP ASN VAL CYS LYS PRO LYS LEU GLU VAL SER VAL ASP          
SEQRES  48 A  962  SER ASP GLN LYS LYS ILE TYR ILE GLY ASP ASP ASN PRO          
SEQRES  49 A  962  LEU THR LEU ILE VAL LYS ALA GLN ASN GLN GLY GLU GLY          
SEQRES  50 A  962  ALA TYR GLU ALA GLU LEU ILE VAL SER ILE PRO LEU GLN          
SEQRES  51 A  962  ALA ASP PHE ILE GLY VAL VAL ARG ASN ASN GLU ALA LEU          
SEQRES  52 A  962  ALA ARG LEU SER CYS ALA PHE LYS THR GLU ASN GLN THR          
SEQRES  53 A  962  ARG GLN VAL VAL CYS ASP LEU GLY ASN PRO MET LYS ALA          
SEQRES  54 A  962  GLY THR GLN LEU LEU ALA GLY LEU ARG PHE SER VAL HIS          
SEQRES  55 A  962  GLN GLN SER GLU MET ASP THR SER VAL LYS PHE ASP LEU          
SEQRES  56 A  962  GLN ILE GLN SER SER ASN LEU PHE ASP LYS VAL SER PRO          
SEQRES  57 A  962  VAL VAL SER HIS LYS VAL ASP LEU ALA VAL LEU ALA ALA          
SEQRES  58 A  962  VAL GLU ILE ARG GLY VAL SER SER PRO ASP HIS VAL PHE          
SEQRES  59 A  962  LEU PRO ILE PRO ASN TRP GLU HIS LYS GLU ASN PRO GLU          
SEQRES  60 A  962  THR GLU GLU ASP VAL GLY PRO VAL VAL GLN HIS ILE TYR          
SEQRES  61 A  962  GLU LEU ARG ASN ASN GLY PRO SER SER PHE SER LYS ALA          
SEQRES  62 A  962  MET LEU HIS LEU GLN TRP PRO TYR LYS TYR ASN ASN ASN          
SEQRES  63 A  962  THR LEU LEU TYR ILE LEU HIS TYR ASP ILE ASP GLY PRO          
SEQRES  64 A  962  MET ASN CYS THR SER ASP MET GLU ILE ASN PRO LEU ARG          
SEQRES  65 A  962  ILE LYS ILE SER SER LEU GLN THR THR GLU LYS ASN ASP          
SEQRES  66 A  962  THR VAL ALA GLY GLN GLY GLU ARG ASP HIS LEU ILE THR          
SEQRES  67 A  962  LYS ARG ASP LEU ALA LEU SER GLU GLY ASP ILE HIS THR          
SEQRES  68 A  962  LEU GLY CYS GLY VAL ALA GLN CYS LEU LYS ILE VAL CYS          
SEQRES  69 A  962  GLN VAL GLY ARG LEU ASP ARG GLY LYS SER ALA ILE LEU          
SEQRES  70 A  962  TYR VAL LYS SER LEU LEU TRP THR GLU THR PHE MET ASN          
SEQRES  71 A  962  LYS GLU ASN GLN ASN HIS SER TYR SER LEU LYS SER SER          
SEQRES  72 A  962  ALA SER PHE ASN VAL ILE GLU PHE PRO TYR LYS ASN LEU          
SEQRES  73 A  962  PRO ILE GLU ASP ILE THR ASN SER THR LEU VAL THR THR          
SEQRES  74 A  962  ASN VAL THR TRP GLY ILE GLN PRO ALA PRO MET PRO VAL          
SEQRES   1 B  692  GLY PRO ASN ILE CYS THR THR ARG GLY VAL SER SER CYS          
SEQRES   2 B  692  GLN GLN CYS LEU ALA VAL SER PRO MET CYS ALA TRP CYS          
SEQRES   3 B  692  SER ASP GLU ALA LEU PRO LEU GLY SER PRO ARG CYS ASP          
SEQRES   4 B  692  LEU LYS GLU ASN LEU LEU LYS ASP ASN CYS ALA PRO GLU          
SEQRES   5 B  692  SER ILE GLU PHE PRO VAL SER GLU ALA ARG VAL LEU GLU          
SEQRES   6 B  692  ASP ARG PRO LEU SER ASP LYS GLY SER GLY ASP SER SER          
SEQRES   7 B  692  GLN VAL THR GLN VAL SER PRO GLN ARG ILE ALA LEU ARG          
SEQRES   8 B  692  LEU ARG PRO ASP ASP SER LYS ASN PHE SER ILE GLN VAL          
SEQRES   9 B  692  ARG GLN VAL GLU ASP TYR PRO VAL ASP ILE TYR TYR LEU          
SEQRES  10 B  692  MET ASP LEU SER TYR SER MET LYS ASP ASP LEU TRP SER          
SEQRES  11 B  692  ILE GLN ASN LEU GLY THR LYS LEU ALA THR GLN MET ARG          
SEQRES  12 B  692  LYS LEU THR SER ASN LEU ARG ILE GLY PHE GLY ALA PHE          
SEQRES  13 B  692  VAL ASP LYS PRO VAL SER PRO TYR MET TYR ILE SER PRO          
SEQRES  14 B  692  PRO GLU ALA LEU GLU ASN PRO CYS TYR ASP MET LYS THR          
SEQRES  15 B  692  THR CYS LEU PRO MET PHE GLY TYR LYS HIS VAL LEU THR          
SEQRES  16 B  692  LEU THR ASP GLN VAL THR ARG PHE ASN GLU GLU VAL LYS          
SEQRES  17 B  692  LYS GLN SER VAL SER ARG ASN ARG ASP ALA PRO GLU GLY          
SEQRES  18 B  692  GLY PHE ASP ALA ILE MET GLN ALA THR VAL CYS ASP GLU          
SEQRES  19 B  692  LYS ILE GLY TRP ARG ASN ASP ALA SER HIS LEU LEU VAL          
SEQRES  20 B  692  PHE THR THR ASP ALA LYS THR HIS ILE ALA LEU ASP GLY          
SEQRES  21 B  692  ARG LEU ALA GLY ILE VAL GLN PRO ASN ASP GLY GLN CYS          
SEQRES  22 B  692  HIS VAL GLY SER ASP ASN HIS TYR SER ALA SER THR THR          
SEQRES  23 B  692  MET ASP TYR PRO SER LEU GLY LEU MET THR GLU LYS LEU          
SEQRES  24 B  692  SER GLN LYS ASN ILE ASN LEU ILE PHE ALA VAL THR GLU          
SEQRES  25 B  692  ASN VAL VAL ASN LEU TYR GLN ASN TYR SER GLU LEU ILE          
SEQRES  26 B  692  PRO GLY THR THR VAL GLY VAL LEU SER MET ASP SER SER          
SEQRES  27 B  692  ASN VAL LEU GLN LEU ILE VAL ASP ALA TYR GLY LYS ILE          
SEQRES  28 B  692  ARG SER LYS VAL GLU LEU GLU VAL ARG ASP LEU PRO GLU          
SEQRES  29 B  692  GLU LEU SER LEU SER PHE ASN ALA THR CYS LEU ASN ASN          
SEQRES  30 B  692  GLU VAL ILE PRO GLY LEU LYS SER CYS MET GLY LEU LYS          
SEQRES  31 B  692  ILE GLY ASP THR VAL SER PHE SER ILE GLU ALA LYS VAL          
SEQRES  32 B  692  ARG GLY CYS PRO GLN GLU LYS GLU LYS SER PHE THR ILE          
SEQRES  33 B  692  LYS PRO VAL GLY PHE LYS ASP SER LEU ILE VAL GLN VAL          
SEQRES  34 B  692  THR PHE ASP CYS ASP CYS ALA CYS GLN ALA GLN ALA GLU          
SEQRES  35 B  692  PRO ASN SER HIS ARG CYS ASN ASN GLY ASN GLY THR PHE          
SEQRES  36 B  692  GLU CYS GLY VAL CYS ARG CYS GLY PRO GLY TRP LEU GLY          
SEQRES  37 B  692  SER GLN CYS GLU CYS SER GLU GLU ASP TYR ARG PRO SER          
SEQRES  38 B  692  GLN GLN ASP GLU CYS SER PRO ARG GLU GLY GLN PRO VAL          
SEQRES  39 B  692  CYS SER GLN ARG GLY GLU CYS LEU CYS GLY GLN CYS VAL          
SEQRES  40 B  692  CYS HIS SER SER ASP PHE GLY LYS ILE THR GLY LYS TYR          
SEQRES  41 B  692  CYS GLU CYS ASP ASP PHE SER CYS VAL ARG TYR LYS GLY          
SEQRES  42 B  692  GLU MET CYS SER GLY HIS GLY GLN CYS SER CYS GLY ASP          
SEQRES  43 B  692  CYS LEU CYS ASP SER ASP TRP THR GLY TYR TYR CYS ASN          
SEQRES  44 B  692  CYS THR THR ARG THR ASP THR CYS MET SER SER ASN GLY          
SEQRES  45 B  692  LEU LEU CYS SER GLY ARG GLY LYS CYS GLU CYS GLY SER          
SEQRES  46 B  692  CYS VAL CYS ILE GLN PRO GLY SER TYR GLY ASP THR CYS          
SEQRES  47 B  692  GLU LYS CYS PRO THR CYS PRO ASP ALA CYS THR PHE LYS          
SEQRES  48 B  692  LYS GLU CYS VAL GLU CYS LYS LYS PHE ASP ARG GLY ALA          
SEQRES  49 B  692  LEU HIS ASP GLU ASN THR CYS ASN ARG TYR CYS ARG ASP          
SEQRES  50 B  692  GLU ILE GLU SER VAL LYS GLU LEU LYS ASP THR GLY LYS          
SEQRES  51 B  692  ASP ALA VAL ASN CYS THR TYR LYS ASN GLU ASP ASP CYS          
SEQRES  52 B  692  VAL VAL ARG PHE GLN TYR TYR GLU ASP SER SER GLY LYS          
SEQRES  53 B  692  SER ILE LEU TYR VAL VAL GLU GLU PRO GLU CYS PRO LYS          
SEQRES  54 B  692  GLY PRO ASP                                                  
SEQRES   1 L  214  ASP ILE GLN MET THR GLN THR THR SER SER LEU SER ALA          
SEQRES   2 L  214  SER LEU GLY ASP ARG VAL ILE ILE SER CYS ARG ALA SER          
SEQRES   3 L  214  GLN ASP ILE SER ASN TYR LEU SER TRP TYR GLN GLN LYS          
SEQRES   4 L  214  PRO ASP GLY THR VAL LYS LEU LEU ILE PHE TYR THR SER          
SEQRES   5 L  214  LYS LEU HIS SER GLY VAL PRO SER ARG PHE SER GLY SER          
SEQRES   6 L  214  GLY SER GLY THR ASP TYR SER LEU THR ILE SER ASN LEU          
SEQRES   7 L  214  ASP GLN GLU ASP ILE ALA THR TYR PHE CYS GLN GLN GLY          
SEQRES   8 L  214  ASN THR PHE PRO TYR THR PHE GLY GLY GLY THR LYS VAL          
SEQRES   9 L  214  GLU MET ARG 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                                      
SEQRES   1 H  218  GLN VAL GLN LEU GLN GLN SER GLY ALA GLU LEU ALA GLU          
SEQRES   2 H  218  PRO GLY ALA SER VAL LYS MET SER CYS LYS ALA SER GLY          
SEQRES   3 H  218  TYR THR PHE SER SER PHE TRP MET HIS TRP VAL LYS GLN          
SEQRES   4 H  218  ARG PRO GLY GLN GLY LEU GLU TRP ILE GLY TYR ILE ASN          
SEQRES   5 H  218  PRO ARG SER GLY TYR THR GLU CYS ASN GLU ILE PHE ARG          
SEQRES   6 H  218  ASP LYS ALA THR MET THR ALA ASP THR SER SER SER THR          
SEQRES   7 H  218  ALA TYR MET GLN LEU SER GLY LEU THR SER GLU ASP SER          
SEQRES   8 H  218  ALA VAL TYR TYR CYS ALA SER PHE LEU GLY ARG GLY ALA          
SEQRES   9 H  218  MET ASP TYR TRP GLY GLN GLY THR SER VAL THR VAL SER          
SEQRES  10 H  218  SER ALA LYS THR THR ALA PRO SER VAL TYR PRO LEU ALA          
SEQRES  11 H  218  PRO VAL CYS GLY ASP THR THR GLY SER SER VAL THR LEU          
SEQRES  12 H  218  GLY CYS LEU VAL LYS GLY TYR PHE PRO GLU PRO VAL THR          
SEQRES  13 H  218  LEU THR TRP ASN SER GLY SER LEU SER ALA GLY VAL HIS          
SEQRES  14 H  218  THR PHE PRO ALA VAL LEU GLN SER ASP LEU TYR THR LEU          
SEQRES  15 H  218  SER SER SER VAL THR VAL THR SER SER THR TRP PRO SER          
SEQRES  16 H  218  GLN SER ILE THR CYS ASN VAL ALA HIS PRO ALA SER SER          
SEQRES  17 H  218  THR LYS VAL ASP LYS LYS ILE GLU PRO ARG                      
MODRES 4O02 ASN B  371  ASN  GLYCOSYLATION SITE                                 
MODRES 4O02 ASN A  524  ASN  GLYCOSYLATION SITE                                 
MODRES 4O02 ASN B  559  ASN  GLYCOSYLATION SITE                                 
MODRES 4O02 ASN B   99  ASN  GLYCOSYLATION SITE                                 
MODRES 4O02 ASN A   44  ASN  GLYCOSYLATION SITE                                 
MODRES 4O02 ASN A  260  ASN  GLYCOSYLATION SITE                                 
MODRES 4O02 ASN A  943  ASN  GLYCOSYLATION SITE                                 
MODRES 4O02 ASN B  320  ASN  GLYCOSYLATION SITE                                 
MODRES 4O02 ASN A  585  ASN  GLYCOSYLATION SITE                                 
MODRES 4O02 ASN A  266  ASN  GLYCOSYLATION SITE                                 
HET    NAG  A1001      14                                                       
HET    NAG  A1002      14                                                       
HET    BMA  A1003      11                                                       
HET    MAN  A1004      11                                                       
HET    BMA  A1005      11                                                       
HET    MAN  A1006      11                                                       
HET    NAG  A1007      14                                                       
HET    NAG  A1008      14                                                       
HET    BMA  A1009      11                                                       
HET    NAG  A1010      14                                                       
HET    NAG  A1011      14                                                       
HET    BMA  A1012      11                                                       
HET    MAN  A1013      11                                                       
HET    MAN  A1014      11                                                       
HET    MAN  A1015      11                                                       
HET    NAG  A1016      14                                                       
HET    NAG  A1017      14                                                       
HET    NAG  A1018      14                                                       
HET    NAG  A1019      14                                                       
HET    NAG  A1020      14                                                       
HET    BMA  A1021      11                                                       
HET    MAN  A1022      11                                                       
HET    MAN  A1023      11                                                       
HET    MAN  A1024      11                                                       
HET     MN  A1025       1                                                       
HET     MN  A1026       1                                                       
HET     MN  A1027       1                                                       
HET     MN  A1028       1                                                       
HET    NO3  A1029       4                                                       
HET    NO3  A1030       4                                                       
HET    NAG  B 701      14                                                       
HET    NAG  B 702      14                                                       
HET    NAG  B 703      14                                                       
HET    NAG  B 704      14                                                       
HET    NAG  B 705      14                                                       
HET    NAG  B 706      14                                                       
HET     MN  B 707       1                                                       
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     BMA BETA-D-MANNOSE                                                   
HETNAM     MAN ALPHA-D-MANNOSE                                                  
HETNAM      MN MANGANESE (II) ION                                               
HETNAM     NO3 NITRATE ION                                                      
FORMUL   5  NAG    17(C8 H15 N O6)                                              
FORMUL   5  BMA    5(C6 H12 O6)                                                 
FORMUL   5  MAN    8(C6 H12 O6)                                                 
FORMUL  11   MN    5(MN 2+)                                                     
FORMUL  15  NO3    2(N O3 1-)                                                   
HELIX    1   1 GLY A  175  GLN A  180  1                                   6    
HELIX    2   2 GLN A  187  TYR A  195  1                                   9    
HELIX    3   3 GLN A  214  ASP A  218  5                                   5    
HELIX    4   4 ARG A  245  LEU A  250  1                                   6    
HELIX    5   5 GLY A  366  LYS A  370  5                                   5    
HELIX    6   6 PHE A  427  VAL A  429  5                                   3    
HELIX    7   7 THR A  768  GLY A  773  1                                   6    
HELIX    8   8 SER B   12  SER B   20  1                                   9    
HELIX    9   9 GLU B   42  ASP B   47  1                                   6    
HELIX   10  10 SER B  121  LYS B  125  5                                   5    
HELIX   11  11 ASP B  126  GLN B  132  1                                   7    
HELIX   12  12 ASN B  133  ARG B  143  1                                  11    
HELIX   13  13 PRO B  170  GLU B  174  5                                   5    
HELIX   14  14 VAL B  200  LYS B  208  1                                   9    
HELIX   15  15 GLY B  221  CYS B  232  1                                  12    
HELIX   16  16 LEU B  258  LEU B  262  5                                   5    
HELIX   17  17 SER B  291  LYS B  302  1                                  12    
HELIX   18  18 VAL B  314  ILE B  325  1                                  12    
HELIX   19  19 ASN B  339  ARG B  352  1                                  14    
HELIX   20  20 LEU B  574  GLY B  577  5                                   4    
HELIX   21  21 ALA B  607  ASP B  621  1                                  15    
HELIX   22  22 ASP L   79  ILE L   83  5                                   5    
HELIX   23  23 THR L  182  HIS L  189  1                                   8    
HELIX   24  24 THR H   28  PHE H   32  5                                   5    
HELIX   25  25 THR H   87  SER H   91  5                                   5    
HELIX   26  26 SER H  161  SER H  163  5                                   3    
SHEET    1   A 4 ALA A   9  SER A  12  0                                        
SHEET    2   A 4 ARG A 431  TYR A 435 -1  O  ALA A 432   N  TYR A  11           
SHEET    3   A 4 LEU A 422  ALA A 426 -1  N  VAL A 424   O  ILE A 433           
SHEET    4   A 4 SER A 407  LYS A 409 -1  N  LYS A 409   O  ILE A 423           
SHEET    1   B 4 VAL A  23  PHE A  26  0                                        
SHEET    2   B 4 PHE A  35  ALA A  40 -1  O  LEU A  37   N  ASP A  24           
SHEET    3   B 4 GLN A  55  ASP A  60 -1  O  CYS A  59   N  LEU A  36           
SHEET    4   B 4 CYS A  67  PRO A  69 -1  O  GLN A  68   N  LYS A  58           
SHEET    1   C 2 ASP A  79  ALA A  81  0                                        
SHEET    2   C 2 ASP A  84  PRO A  85 -1  O  ASP A  84   N  ALA A  81           
SHEET    1   D 3 GLU A  87  PHE A  88  0                                        
SHEET    2   D 3 HIS A 113  ARG A 115 -1  O  HIS A 113   N  PHE A  88           
SHEET    3   D 3 ARG A 122  GLU A 123 -1  O  GLU A 123   N  TRP A 114           
SHEET    1   E 4 VAL A  98  LYS A 101  0                                        
SHEET    2   E 4 LYS A 104  ALA A 109 -1  O  LEU A 106   N  ARG A  99           
SHEET    3   E 4 THR A 127  GLN A 131 -1  O  THR A 127   N  ALA A 109           
SHEET    4   E 4 THR A 136  TYR A 139 -1  O  VAL A 137   N  LEU A 130           
SHEET    1   F 4 SER A 160  PHE A 163  0                                        
SHEET    2   F 4 VAL A 169  GLY A 173 -1  O  GLY A 172   N  SER A 160           
SHEET    3   F 4 GLN A 182  ASP A 186 -1  O  ASP A 186   N  VAL A 169           
SHEET    4   F 4 LEU A 208  ALA A 209 -1  O  LEU A 208   N  SER A 185           
SHEET    1   G 4 VAL A 226  GLY A 229  0                                        
SHEET    2   G 4 ASP A 238  VAL A 243 -1  O  VAL A 240   N  ALA A 227           
SHEET    3   G 4 MET A 252  TYR A 256 -1  O  TYR A 256   N  PHE A 239           
SHEET    4   G 4 SER A 263  THR A 268 -1  O  LEU A 264   N  ILE A 255           
SHEET    1   H 4 VAL A 280  THR A 283  0                                        
SHEET    2   H 4 ASP A 292  ALA A 297 -1  O  ASP A 292   N  THR A 283           
SHEET    3   H 4 GLN A 314  LEU A 319 -1  O  GLN A 314   N  ALA A 297           
SHEET    4   H 4 GLN A 327  ASN A 332 -1  O  THR A 329   N  VAL A 317           
SHEET    1   I 2 MET A 301  ASP A 302  0                                        
SHEET    2   I 2 GLN A 310  GLU A 311 -1  O  GLN A 310   N  ASP A 302           
SHEET    1   J 4 ILE A 344  GLY A 348  0                                        
SHEET    2   J 4 ASP A 357  ALA A 362 -1  O  ASP A 357   N  GLY A 348           
SHEET    3   J 4 ILE A 372  PHE A 376 -1  O  PHE A 376   N  ILE A 358           
SHEET    4   J 4 GLN A 389  GLU A 392 -1  O  LEU A 391   N  VAL A 373           
SHEET    1   K 5 ALA A 511  PHE A 513  0                                        
SHEET    2   K 5 GLN A 534  LEU A 542 -1  O  TYR A 541   N  LEU A 512           
SHEET    3   K 5 CYS A 472  ASP A 482 -1  N  PHE A 473   O  ALA A 540           
SHEET    4   K 5 VAL A 440  VAL A 449 -1  N  THR A 442   O  ASP A 482           
SHEET    5   K 5 ILE A 577  LEU A 578  1  O  ILE A 577   N  ILE A 441           
SHEET    1   L 4 SER A 520  ILE A 527  0                                        
SHEET    2   L 4 LEU A 491  LEU A 498 -1  N  LEU A 497   O  HIS A 521           
SHEET    3   L 4 ILE A 557  LEU A 563 -1  O  GLU A 560   N  GLU A 496           
SHEET    4   L 4 ASN A 585  ARG A 588 -1  O  ARG A 588   N  ILE A 557           
SHEET    1   M 4 LEU A 606  ASP A 611  0                                        
SHEET    2   M 4 ASN A 623  ASN A 633 -1  O  LYS A 630   N  SER A 609           
SHEET    3   M 4 GLN A 692  VAL A 701 -1  O  ALA A 695   N  VAL A 629           
SHEET    4   M 4 ASP A 652  VAL A 656 -1  N  ASP A 652   O  SER A 700           
SHEET    1   N 4 GLN A 678  ASP A 682  0                                        
SHEET    2   N 4 GLU A 642  SER A 646 -1  N  VAL A 645   O  VAL A 679           
SHEET    3   N 4 PHE A 713  GLN A 718 -1  O  GLN A 716   N  ILE A 644           
SHEET    4   N 4 VAL A 730  HIS A 732 -1  O  VAL A 730   N  LEU A 715           
SHEET    1   O 4 ALA A 741  SER A 748  0                                        
SHEET    2   O 4 VAL A 775  ASN A 785 -1  O  GLU A 781   N  ARG A 745           
SHEET    3   O 4 LYS A 893  LEU A 903 -1  O  SER A 901   N  VAL A 776           
SHEET    4   O 4 LEU A 809  TYR A 814 -1  N  TYR A 810   O  LEU A 902           
SHEET    1   P 6 HIS A 752  VAL A 753  0                                        
SHEET    2   P 6 THR A 942  VAL A 951  1  O  ASN A 950   N  VAL A 753           
SHEET    3   P 6 TYR A 918  ILE A 929 -1  N  SER A 922   O  VAL A 947           
SHEET    4   P 6 LYS A 792  GLN A 798 -1  N  LYS A 792   O  ILE A 929           
SHEET    5   P 6 ILE A 882  VAL A 886 -1  O  ILE A 882   N  LEU A 797           
SHEET    6   P 6 MET A 820  THR A 823 -1  N  ASN A 821   O  GLN A 885           
SHEET    1   Q 6 GLU B  60  GLU B  65  0                                        
SHEET    2   Q 6 ARG B  87  LEU B  92 -1  O  ARG B  91   N  GLU B  60           
SHEET    3   Q 6 LEU B 425  PHE B 431  1  O  THR B 430   N  LEU B  90           
SHEET    4   Q 6 LYS B 412  PRO B 418 -1  N  ILE B 416   O  LEU B 425           
SHEET    5   Q 6 LYS B 354  ARG B 360 -1  N  GLU B 358   O  LYS B 417           
SHEET    6   Q 6 SER B 385  MET B 387 -1  O  CYS B 386   N  VAL B 355           
SHEET    1   R 4 SER B  97  ARG B 105  0                                        
SHEET    2   R 4 THR B 394  VAL B 403 -1  O  VAL B 395   N  VAL B 104           
SHEET    3   R 4 LEU B 366  LEU B 375 -1  N  SER B 369   O  GLU B 400           
SHEET    4   R 4 GLU B 378  PRO B 381 -1  O  GLU B 378   N  LEU B 375           
SHEET    1   S 6 TYR B 190  THR B 197  0                                        
SHEET    2   S 6 LEU B 149  PHE B 156 -1  N  ILE B 151   O  THR B 197           
SHEET    3   S 6 VAL B 112  ASP B 119  1  N  TYR B 116   O  GLY B 152           
SHEET    4   S 6 SER B 243  THR B 250  1  O  SER B 243   N  ASP B 113           
SHEET    5   S 6 ASN B 305  VAL B 310  1  O  ALA B 309   N  PHE B 248           
SHEET    6   S 6 THR B 329  VAL B 332  1  O  THR B 329   N  PHE B 308           
SHEET    1   T 2 GLU B 500  LEU B 502  0                                        
SHEET    2   T 2 GLN B 505  VAL B 507 -1  O  VAL B 507   N  GLU B 500           
SHEET    1   U 2 GLY B 540  SER B 543  0                                        
SHEET    2   U 2 ASP B 546  CYS B 549 -1  O  ASP B 546   N  SER B 543           
SHEET    1   V 2 TRP B 553  THR B 554  0                                        
SHEET    2   V 2 CYS B 560  THR B 561 -1  O  CYS B 560   N  THR B 554           
SHEET    1   W 2 GLY B 579  CYS B 581  0                                        
SHEET    2   W 2 CYS B 586  CYS B 588 -1  O  VAL B 587   N  LYS B 580           
SHEET    1   X 3 VAL B 653  THR B 656  0                                        
SHEET    2   X 3 ARG B 666  TYR B 669 -1  O  PHE B 667   N  CYS B 655           
SHEET    3   X 3 LEU B 679  VAL B 681 -1  O  TYR B 680   N  GLN B 668           
SHEET    1   Y 4 MET L   4  THR L   5  0                                        
SHEET    2   Y 4 VAL L  19  ALA L  25 -1  O  ARG L  24   N  THR L   5           
SHEET    3   Y 4 ASP L  70  ILE L  75 -1  O  TYR L  71   N  CYS L  23           
SHEET    4   Y 4 PHE L  62  GLY L  66 -1  N  SER L  63   O  THR L  74           
SHEET    1   Z 5 SER L  10  ALA L  13  0                                        
SHEET    2   Z 5 THR L 102  MET L 106  1  O  GLU L 105   N  LEU L  11           
SHEET    3   Z 5 THR L  85  GLN L  90 -1  N  TYR L  86   O  THR L 102           
SHEET    4   Z 5 LEU L  33  LYS L  39 -1  N  TYR L  36   O  PHE L  87           
SHEET    5   Z 5 GLY L  42  ILE L  48 -1  O  LYS L  45   N  GLN L  37           
SHEET    1  AA 4 SER L  10  ALA L  13  0                                        
SHEET    2  AA 4 THR L 102  MET L 106  1  O  GLU L 105   N  LEU L  11           
SHEET    3  AA 4 THR L  85  GLN L  90 -1  N  TYR L  86   O  THR L 102           
SHEET    4  AA 4 THR L  97  PHE L  98 -1  O  THR L  97   N  GLN L  90           
SHEET    1  AB 4 THR L 114  SER L 116  0                                        
SHEET    2  AB 4 VAL L 133  PHE L 139 -1  O  ASN L 137   N  THR L 114           
SHEET    3  AB 4 TYR L 173  LEU L 179 -1  O  TYR L 173   N  PHE L 139           
SHEET    4  AB 4 VAL L 159  THR L 164 -1  N  SER L 162   O  SER L 176           
SHEET    1  AC 4 SER L 153  GLU L 154  0                                        
SHEET    2  AC 4 ASN L 145  ILE L 150 -1  N  ILE L 150   O  SER L 153           
SHEET    3  AC 4 SER L 191  THR L 197 -1  O  THR L 197   N  ASN L 145           
SHEET    4  AC 4 ILE L 205  ASN L 210 -1  O  LYS L 207   N  CYS L 194           
SHEET    1  AD 4 GLN H   3  GLN H   6  0                                        
SHEET    2  AD 4 SER H  17  SER H  25 -1  O  SER H  25   N  GLN H   3           
SHEET    3  AD 4 THR H  78  SER H  84 -1  O  LEU H  83   N  VAL H  18           
SHEET    4  AD 4 ALA H  68  ASP H  73 -1  N  ASP H  73   O  THR H  78           
SHEET    1  AE 6 GLU H  10  LEU H  11  0                                        
SHEET    2  AE 6 THR H 112  THR H 115  1  O  SER H 113   N  GLU H  10           
SHEET    3  AE 6 ALA H  92  PHE H  99 -1  N  TYR H  94   O  THR H 112           
SHEET    4  AE 6 MET H  34  GLN H  39 -1  N  VAL H  37   O  TYR H  95           
SHEET    5  AE 6 LEU H  45  ILE H  51 -1  O  GLU H  46   N  LYS H  38           
SHEET    6  AE 6 THR H  58  CYS H  60 -1  O  GLU H  59   N  TYR H  50           
SHEET    1  AF 4 GLU H  10  LEU H  11  0                                        
SHEET    2  AF 4 THR H 112  THR H 115  1  O  SER H 113   N  GLU H  10           
SHEET    3  AF 4 ALA H  92  PHE H  99 -1  N  TYR H  94   O  THR H 112           
SHEET    4  AF 4 MET H 105  TRP H 108 -1  O  TYR H 107   N  SER H  98           
SHEET    1  AG 4 TYR H 127  LEU H 129  0                                        
SHEET    2  AG 4 SER H 140  TYR H 150 -1  O  GLY H 144   N  LEU H 129           
SHEET    3  AG 4 SER H 184  THR H 189 -1  O  VAL H 188   N  VAL H 141           
SHEET    4  AG 4 VAL H 168  THR H 170 -1  N  HIS H 169   O  SER H 185           
SHEET    1  AH 3 TYR H 127  LEU H 129  0                                        
SHEET    2  AH 3 SER H 140  TYR H 150 -1  O  GLY H 144   N  LEU H 129           
SHEET    3  AH 3 TYR H 180  LEU H 182 -1  O  LEU H 182   N  VAL H 147           
SHEET    1  AI 3 THR H 156  TRP H 159  0                                        
SHEET    2  AI 3 THR H 199  ALA H 203 -1  O  ASN H 201   N  THR H 158           
SHEET    3  AI 3 LYS H 210  LYS H 214 -1  O  LYS H 213   N  CYS H 200           
SSBOND   1 CYS A   59    CYS A   67                          1555   1555  2.03  
SSBOND   2 CYS A  108    CYS A  128                          1555   1555  2.03  
SSBOND   3 CYS A  142    CYS A  155                          1555   1555  2.02  
SSBOND   4 CYS A  478    CYS A  535                          1555   1555  2.03  
SSBOND   5 CYS A  596    CYS A  602                          1555   1555  2.03  
SSBOND   6 CYS A  668    CYS A  681                          1555   1555  2.03  
SSBOND   7 CYS B    5    CYS B   23                          1555   1555  2.03  
SSBOND   8 CYS B   13    CYS B  435                          1555   1555  2.03  
SSBOND   9 CYS B   16    CYS B   38                          1555   1555  2.03  
SSBOND  10 CYS B   26    CYS B   49                          1555   1555  2.03  
SSBOND  11 CYS B  177    CYS B  184                          1555   1555  2.04  
SSBOND  12 CYS B  232    CYS B  273                          1555   1555  2.03  
SSBOND  13 CYS B  374    CYS B  386                          1555   1555  2.03  
SSBOND  14 CYS B  406    CYS B  433                          1555   1555  2.03  
SSBOND  15 CYS B  437    CYS B  457                          1555   1555  2.03  
SSBOND  16 CYS B  448    CYS B  460                          1555   1555  2.04  
SSBOND  17 CYS B  462    CYS B  471                          1555   1555  2.03  
SSBOND  18 CYS B  486    CYS B  501                          1555   1555  2.04  
SSBOND  19 CYS B  495    CYS B  506                          1555   1555  2.08  
SSBOND  20 CYS B  508    CYS B  521                          1555   1555  2.03  
SSBOND  21 CYS B  523    CYS B  544                          1555   1555  2.03  
SSBOND  22 CYS B  528    CYS B  542                          1555   1555  2.03  
SSBOND  23 CYS B  536    CYS B  547                          1555   1555  2.03  
SSBOND  24 CYS B  549    CYS B  558                          1555   1555  2.03  
SSBOND  25 CYS B  560    CYS B  583                          1555   1555  2.03  
SSBOND  26 CYS B  567    CYS B  581                          1555   1555  2.03  
SSBOND  27 CYS B  575    CYS B  586                          1555   1555  2.03  
SSBOND  28 CYS B  588    CYS B  598                          1555   1555  2.03  
SSBOND  29 CYS B  601    CYS B  604                          1555   1555  2.03  
SSBOND  30 CYS B  608    CYS B  655                          1555   1555  2.03  
SSBOND  31 CYS B  614    CYS B  635                          1555   1555  2.04  
SSBOND  32 CYS B  617    CYS B  631                          1555   1555  2.05  
SSBOND  33 CYS L   23    CYS L   88                          1555   1555  2.04  
SSBOND  34 CYS L  134    CYS L  194                          1555   1555  2.03  
SSBOND  35 CYS H   22    CYS H   96                          1555   1555  2.03  
SSBOND  36 CYS H  145    CYS H  200                          1555   1555  2.03  
LINK         ND2 ASN B 371                 C1  NAG B 704     1555   1555  1.43  
LINK         O6  BMA A1003                 C1  MAN A1004     1555   1555  1.43  
LINK         O4  NAG A1019                 C1  NAG A1020     1555   1555  1.45  
LINK         O4  NAG A1011                 C1  BMA A1012     1555   1555  1.44  
LINK         O4  NAG B 704                 C1  NAG B 705     1555   1555  1.44  
LINK         O4  NAG A1010                 C1  NAG A1011     1555   1555  1.44  
LINK         ND2 ASN A 524                 C1  NAG A1016     1555   1555  1.45  
LINK         ND2 ASN B 559                 C1  NAG B 706     1555   1555  1.44  
LINK         ND2 ASN B  99                 C1  NAG B 701     1555   1555  1.43  
LINK         ND2 ASN A  44                 C1  NAG A1001     1555   1555  1.44  
LINK         O4  NAG A1007                 C1  NAG A1008     1555   1555  1.44  
LINK         O4  NAG A1008                 C1  BMA A1009     1555   1555  1.44  
LINK         O6  BMA A1012                 C1  MAN A1013     1555   1555  1.44  
LINK         ND2 ASN A 260                 C1  NAG A1007     1555   1555  1.44  
LINK         ND2 ASN A 943                 C1  NAG A1019     1555   1555  1.45  
LINK         O4  NAG A1001                 C1  NAG A1002     1555   1555  1.44  
LINK         O3  BMA A1003                 C1  MAN A1006     1555   1555  1.44  
LINK         O3  BMA A1012                 C1  MAN A1015     1555   1555  1.44  
LINK         ND2 ASN B 320                 C1  NAG B 702     1555   1555  1.45  
LINK         O4  MAN A1004                 C1  BMA A1005     1555   1555  1.44  
LINK         O3  MAN A1023                 C1  MAN A1024     1555   1555  1.45  
LINK         ND2 ASN A 585                 C1  NAG A1017     1555   1555  1.45  
LINK         O3  BMA A1021                 C1  MAN A1022     1555   1555  1.45  
LINK         O3  MAN A1013                 C1  MAN A1014     1555   1555  1.45  
LINK         O4  NAG A1017                 C1  NAG A1018     1555   1555  1.44  
LINK         O4  NAG A1020                 C1  BMA A1021     1555   1555  1.45  
LINK         O4  NAG B 702                 C1  NAG B 703     1555   1555  1.44  
LINK         ND2 ASN A 266                 C1  NAG A1010     1555   1555  1.43  
LINK         O3  MAN A1022                 C1  MAN A1023     1555   1555  1.46  
LINK         O4  NAG A1002                 C1  BMA A1003     1555   1555  1.45  
LINK         OD1 ASP A 292                MN    MN A1026     1555   1555  2.16  
LINK         O   TYR A 419                MN    MN A1028     1555   1555  2.09  
LINK         O   SER B 123                MN    MN B 707     1555   1555  2.21  
LINK         OD1 ASP A 413                MN    MN A1028     1555   1555  2.18  
LINK         OD2 ASP A 349                MN    MN A1027     1555   1555  2.16  
LINK         OD2 ASP A 353                MN    MN A1027     1555   1555  2.26  
LINK         OD2 ASP A 292                MN    MN A1026     1555   1555  2.16  
LINK         OD1 ASN A 417                MN    MN A1028     1555   1555  2.23  
LINK         OD1 ASN A 286                MN    MN A1026     1555   1555  2.22  
LINK         OD1 ASN A 232                MN    MN A1025     1555   1555  2.18  
LINK         O   ASN A 232                MN    MN A1025     1555   1555  2.29  
LINK         OD1 ASP A 288                MN    MN A1026     1555   1555  2.16  
LINK         OD2 ASP A 357                MN    MN A1027     1555   1555  2.19  
LINK         O   PHE A 355                MN    MN A1027     1555   1555  2.33  
LINK         OD2 ASP A 421                MN    MN A1028     1555   1555  2.19  
LINK         O   ASP A 234                MN    MN A1025     1555   1555  2.37  
LINK         OD2 ASP A 230                MN    MN A1025     1555   1555  2.13  
LINK         OD2 ASP A 238                MN    MN A1025     1555   1555  2.30  
LINK         OD1 ASP A 238                MN    MN A1025     1555   1555  2.32  
LINK         OD1 ASP A 284                MN    MN A1026     1555   1555  2.15  
LINK         O   TYR A 290                MN    MN A1026     1555   1555  2.18  
LINK         OD1 ASP A 357                MN    MN A1027     1555   1555  2.18  
LINK         OD2 ASP A 351                MN    MN A1027     1555   1555  2.16  
LINK         OD1 ASP A 421                MN    MN A1028     1555   1555  2.21  
LINK         OD1 ASP A 415                MN    MN A1028     1555   1555  2.18  
LINK         OD1 ASP B 127                MN    MN B 707     1555   1555  2.21  
LINK         OD1 ASP B 126                MN    MN B 707     1555   1555  2.21  
LINK         OD2 ASP B 126                MN    MN B 707     1555   1555  2.10  
LINK         O   MET B 335                MN    MN B 707     1555   1555  2.31  
SITE     1 AC1  6 GLU A  15  GLY A  16  LYS A  42  ASN A  44                    
SITE     2 AC1  6 GLU A  52  NAG A1002                                          
SITE     1 AC2  2 NAG A1001  BMA A1003                                          
SITE     1 AC3  3 NAG A1002  MAN A1004  MAN A1006                               
SITE     1 AC4  2 BMA A1003  BMA A1005                                          
SITE     1 AC5  2 MAN A1004  MAN A1024                                          
SITE     1 AC6  1 BMA A1003                                                     
SITE     1 AC7  3 ASP A 257  ASN A 260  NAG A1008                               
SITE     1 AC8  2 NAG A1007  BMA A1009                                          
SITE     1 AC9  1 NAG A1008                                                     
SITE     1 BC1  6 PHE A 217  TYR A 254  SER A 263  LEU A 264                    
SITE     2 BC1  6 ASN A 266  NAG A1011                                          
SITE     1 BC2  3 PHE A 217  NAG A1010  BMA A1012                               
SITE     1 BC3  4 GLN A 214  NAG A1011  MAN A1013  MAN A1015                    
SITE     1 BC4  2 BMA A1012  MAN A1014                                          
SITE     1 BC5  2 GLN A 214  MAN A1013                                          
SITE     1 BC6  1 BMA A1012                                                     
SITE     1 BC7  3 ASN A 492  ASN A 524  THR A 526                               
SITE     1 BC8  5 GLU A 560  ALA A 584  ASN A 585  NAG A1018                    
SITE     2 BC8  5 ASP B 512                                                     
SITE     1 BC9  1 NAG A1017                                                     
SITE     1 CC1  3 ASN A 943  SER A 944  NAG A1020                               
SITE     1 CC2  2 NAG A1019  BMA A1021                                          
SITE     1 CC3  2 NAG A1020  MAN A1022                                          
SITE     1 CC4  2 BMA A1021  MAN A1023                                          
SITE     1 CC5  2 MAN A1022  MAN A1024                                          
SITE     1 CC6  2 BMA A1005  MAN A1023                                          
SITE     1 CC7  5 ASP A 230  ASN A 232  ASP A 234  ILE A 236                    
SITE     2 CC7  5 ASP A 238                                                     
SITE     1 CC8  5 ASP A 284  ASN A 286  ASP A 288  TYR A 290                    
SITE     2 CC8  5 ASP A 292                                                     
SITE     1 CC9  5 ASP A 349  ASP A 351  ASP A 353  PHE A 355                    
SITE     2 CC9  5 ASP A 357                                                     
SITE     1 DC1  5 ASP A 413  ASP A 415  ASN A 417  TYR A 419                    
SITE     2 DC1  5 ASP A 421                                                     
SITE     1 DC2  3 ILE A 202  LYS A 203  TYR H 107                               
SITE     1 DC3  6 PRO A 141  ILE A 202  GLN A 207  THR H  28                    
SITE     2 DC3  6 SER H  31  PHE H  32                                          
SITE     1 DC4  3 ASN B  99  PHE B 100  NAG B 705                               
SITE     1 DC5  4 ARG A 248  ASN B 316  ASN B 320  NAG B 703                    
SITE     1 DC6  1 NAG B 702                                                     
SITE     1 DC7  5 ASN B 371  SER B 398  ILE B 399  GLU B 400                    
SITE     2 DC7  5 NAG B 705                                                     
SITE     1 DC8  3 GLU B 400  NAG B 701  NAG B 704                               
SITE     1 DC9  3 ARG B 530  TYR B 531  ASN B 559                               
SITE     1 EC1  4 SER B 123  ASP B 126  ASP B 127  MET B 335                    
CRYST1  110.464  266.988  102.163  90.00  90.00  90.00 P 21 21 2     4          
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      0.009053  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.003745  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009788        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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