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Database: PDB
Entry: 4GBX
LinkDB: 4GBX
Original site: 4GBX 
HEADER    IMMUNE SYSTEM                           28-JUL-12   4GBX              
TITLE     CRYSTAL STRUCTURE OF AN IMMUNE COMPLEX AT PH 6.5                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HLA CLASS II HISTOCOMPATIBILITY ANTIGEN, DM ALPHA CHAIN;   
COMPND   3 CHAIN: C;                                                            
COMPND   4 SYNONYM: MHC CLASS II ANTIGEN DMA, REALLY INTERESTING NEW GENE 6     
COMPND   5 PROTEIN;                                                             
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES;                                                       
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: HLA CLASS II HISTOCOMPATIBILITY ANTIGEN, DM BETA CHAIN;    
COMPND  10 CHAIN: D;                                                            
COMPND  11 SYNONYM: MHC CLASS II ANTIGEN DMB, REALLY INTERESTING NEW GENE 7     
COMPND  12 PROTEIN;                                                             
COMPND  13 ENGINEERED: YES;                                                     
COMPND  14 MUTATION: YES;                                                       
COMPND  15 MOL_ID: 3;                                                           
COMPND  16 MOLECULE: HLA CLASS II HISTOCOMPATIBILITY ANTIGEN, DR ALPHA CHAIN;   
COMPND  17 CHAIN: A;                                                            
COMPND  18 SYNONYM: MHC CLASS II ANTIGEN DRA;                                   
COMPND  19 ENGINEERED: YES;                                                     
COMPND  20 MUTATION: YES;                                                       
COMPND  21 MOL_ID: 4;                                                           
COMPND  22 MOLECULE: HLA CLASS II HISTOCOMPATIBILITY ANTIGEN, DRB1-1 BETA CHAIN;
COMPND  23 CHAIN: B;                                                            
COMPND  24 SYNONYM: MHC CLASS II ANTIGEN DRB1*1, DR-1, DR1;                     
COMPND  25 ENGINEERED: YES;                                                     
COMPND  26 MUTATION: YES;                                                       
COMPND  27 MOL_ID: 5;                                                           
COMPND  28 MOLECULE: SYNTHETIC PEPTIDE;                                         
COMPND  29 CHAIN: E;                                                            
COMPND  30 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: ALPHA CHAIN, DMA, HLA-DM, HLA-DMA, MHC CLASS II MOLECULE,      
SOURCE   6 RING6;                                                               
SOURCE   7 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;                               
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 10029;                                      
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: LEC3.2.8.1;                                
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: PEE14.1;                                  
SOURCE  12 MOL_ID: 2;                                                           
SOURCE  13 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  14 ORGANISM_COMMON: HUMAN;                                              
SOURCE  15 ORGANISM_TAXID: 9606;                                                
SOURCE  16 GENE: BETA CHAIN, DMB, HLA-DMB, MHC CLASS II MOLECULE HLA-DM, RING7; 
SOURCE  17 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;                               
SOURCE  18 EXPRESSION_SYSTEM_TAXID: 10029;                                      
SOURCE  19 EXPRESSION_SYSTEM_STRAIN: LEC3.2.8.1;                                
SOURCE  20 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  21 EXPRESSION_SYSTEM_PLASMID: PEE14.1;                                  
SOURCE  22 MOL_ID: 3;                                                           
SOURCE  23 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  24 ORGANISM_COMMON: HUMAN;                                              
SOURCE  25 ORGANISM_TAXID: 9606;                                                
SOURCE  26 GENE: ALPHA CHAIN, HLA-DR1, HLA-DRA, HLA-DRA1, MHC CLASS II          
SOURCE  27 MOLECULE;                                                            
SOURCE  28 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE  29 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE  30 MOL_ID: 4;                                                           
SOURCE  31 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  32 ORGANISM_COMMON: HUMAN;                                              
SOURCE  33 ORGANISM_TAXID: 9606;                                                
SOURCE  34 GENE: BETA CHAIN, HLA-DR1, HLA-DRB1, MHC CLASS II MOLECULE;          
SOURCE  35 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE  36 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE  37 MOL_ID: 5;                                                           
SOURCE  38 SYNTHETIC: YES;                                                      
SOURCE  39 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;                            
SOURCE  40 ORGANISM_COMMON: SYNTHETIC CONSTRUCT;                                
SOURCE  41 ORGANISM_TAXID: 32630                                                
KEYWDS    IMMUNE COMPLEX, PEPTIDE LOADING, PEPTIDE EDITING, ANTIGEN             
KEYWDS   2 PRESENTATION, IMMUNE SYSTEM                                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.K.SETHI,W.POS,K.W.WUCHERPFENNIG                                     
REVDAT   3   29-JUL-20 4GBX    1       COMPND REMARK SEQADV HETNAM              
REVDAT   3 2                   1       LINK   SITE                              
REVDAT   2   15-NOV-17 4GBX    1       REMARK                                   
REVDAT   1   16-JAN-13 4GBX    0                                                
JRNL        AUTH   W.POS,D.K.SETHI,M.J.CALL,M.S.SCHULZE,A.K.ANDERS,J.PYRDOL,    
JRNL        AUTH 2 K.W.WUCHERPFENNIG                                            
JRNL        TITL   CRYSTAL STRUCTURE OF THE HLA-DM-HLA-DR1 COMPLEX DEFINES      
JRNL        TITL 2 MECHANISMS FOR RAPID PEPTIDE SELECTION.                      
JRNL        REF    CELL(CAMBRIDGE,MASS.)         V. 151  1557 2012              
JRNL        REFN                   ISSN 0092-8674                               
JRNL        PMID   23260142                                                     
JRNL        DOI    10.1016/J.CELL.2012.11.025                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.8_1065                                      
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 36.99                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.360                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 24550                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.200                           
REMARK   3   R VALUE            (WORKING SET) : 0.198                           
REMARK   3   FREE R VALUE                     : 0.250                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1227                            
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 36.9936 -  6.2315    0.98     2691   160  0.2030 0.2508        
REMARK   3     2  6.2315 -  4.9499    0.99     2616   143  0.1906 0.2338        
REMARK   3     3  4.9499 -  4.3253    1.00     2609   137  0.1492 0.1970        
REMARK   3     4  4.3253 -  3.9303    1.00     2593   129  0.1772 0.2291        
REMARK   3     5  3.9303 -  3.6489    1.00     2578   137  0.2101 0.2789        
REMARK   3     6  3.6489 -  3.4339    1.00     2594   106  0.2036 0.2963        
REMARK   3     7  3.4339 -  3.2621    1.00     2562   128  0.2229 0.2897        
REMARK   3     8  3.2621 -  3.1201    1.00     2563   146  0.2667 0.2862        
REMARK   3     9  3.1201 -  3.0001    1.00     2517   141  0.3113 0.3513        
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)     : 0.390            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.850           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 70.32                          
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      :  0.010           6323                                  
REMARK   3   ANGLE     :  1.295           8612                                  
REMARK   3   CHIRALITY :  0.087            939                                  
REMARK   3   PLANARITY :  0.007           1120                                  
REMARK   3   DIHEDRAL  : 16.830           2269                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 25                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 12 THROUGH 37 )                   
REMARK   3    ORIGIN FOR THE GROUP (A): -57.3588  12.0208  13.2840              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.2116 T22:   0.5822                                     
REMARK   3      T33:   1.1091 T12:   0.4933                                     
REMARK   3      T13:  -0.1332 T23:  -0.1950                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4725 L22:   0.5339                                     
REMARK   3      L33:   0.8619 L12:  -0.2209                                     
REMARK   3      L13:  -0.3280 L23:  -0.3722                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3064 S12:  -0.2421 S13:   0.6189                       
REMARK   3      S21:   0.6483 S22:   0.1879 S23:   0.5803                       
REMARK   3      S31:  -0.6608 S32:  -0.1190 S33:   0.0784                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 38 THROUGH 54 )                   
REMARK   3    ORIGIN FOR THE GROUP (A): -65.1056  13.4398  17.8295              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.3306 T22:   1.1434                                     
REMARK   3      T33:   1.1682 T12:   0.5559                                     
REMARK   3      T13:  -0.0860 T23:  -0.3919                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3075 L22:   1.0192                                     
REMARK   3      L33:   1.0574 L12:  -0.5595                                     
REMARK   3      L13:   0.5243 L23:  -0.9898                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0018 S12:   0.1667 S13:   0.1025                       
REMARK   3      S21:   0.2448 S22:   0.2689 S23:   0.2790                       
REMARK   3      S31:  -0.2337 S32:  -0.1609 S33:  -0.2983                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 55 THROUGH 69 )                   
REMARK   3    ORIGIN FOR THE GROUP (A): -65.2016  19.0638  24.1041              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.2046 T22:   1.0250                                     
REMARK   3      T33:   1.4391 T12:   0.3685                                     
REMARK   3      T13:  -0.1384 T23:  -0.2498                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2073 L22:   2.4148                                     
REMARK   3      L33:   0.8046 L12:  -0.6830                                     
REMARK   3      L13:   0.4044 L23:  -1.3975                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.8427 S12:   0.1533 S13:   0.3061                       
REMARK   3      S21:   0.9483 S22:   0.6094 S23:   0.0189                       
REMARK   3      S31:  -0.2574 S32:   0.2880 S33:  -0.6249                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 70 THROUGH 130 )                  
REMARK   3    ORIGIN FOR THE GROUP (A): -60.0225   1.3947  12.3894              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5796 T22:   0.6914                                     
REMARK   3      T33:   0.8283 T12:   0.3421                                     
REMARK   3      T13:  -0.0094 T23:  -0.1340                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8457 L22:   1.3731                                     
REMARK   3      L33:   0.4192 L12:  -0.4754                                     
REMARK   3      L13:   0.0968 L23:   0.1356                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2410 S12:  -0.2936 S13:   0.7339                       
REMARK   3      S21:   0.1909 S22:  -0.0664 S23:   0.3924                       
REMARK   3      S31:  -0.5062 S32:  -0.8202 S33:  -0.0126                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 131 THROUGH 142 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -67.1955 -12.3916  24.9462              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7154 T22:   0.7623                                     
REMARK   3      T33:   0.6381 T12:   0.1156                                     
REMARK   3      T13:   0.2893 T23:  -0.2639                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.4144 L22:   1.8614                                     
REMARK   3      L33:   1.3995 L12:   1.4419                                     
REMARK   3      L13:   1.1957 L23:  -0.6080                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1956 S12:  -1.0395 S13:   0.1220                       
REMARK   3      S21:  -0.1969 S22:  -0.0565 S23:  -0.1459                       
REMARK   3      S31:  -0.3135 S32:  -0.5949 S33:   0.1167                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 143 THROUGH 162 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -60.2948   2.2041  18.6938              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6501 T22:   0.7613                                     
REMARK   3      T33:   0.7371 T12:   0.3345                                     
REMARK   3      T13:   0.0527 T23:  -0.0381                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2524 L22:   1.9660                                     
REMARK   3      L33:   1.0504 L12:   1.2335                                     
REMARK   3      L13:   0.7885 L23:   0.7749                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.8988 S12:  -0.6552 S13:   0.2288                       
REMARK   3      S21:   0.6202 S22:   0.2557 S23:   0.1076                       
REMARK   3      S31:  -0.5880 S32:  -0.2241 S33:   0.1761                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 163 THROUGH 202 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -59.3138 -10.2817  27.7109              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4696 T22:   0.7771                                     
REMARK   3      T33:   0.6018 T12:   0.1733                                     
REMARK   3      T13:   0.1398 T23:  -0.1410                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0697 L22:   1.3033                                     
REMARK   3      L33:   2.9484 L12:   0.2325                                     
REMARK   3      L13:   1.0863 L23:   0.0493                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0830 S12:  -0.8845 S13:   0.4608                       
REMARK   3      S21:   0.2310 S22:  -0.0264 S23:   0.2059                       
REMARK   3      S31:   0.3392 S32:  -1.2370 S33:  -0.0417                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 3 THROUGH 14 )                    
REMARK   3    ORIGIN FOR THE GROUP (A): -54.3710  12.9236   8.3687              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.2695 T22:   0.6486                                     
REMARK   3      T33:   1.0294 T12:   0.2829                                     
REMARK   3      T13:  -0.2910 T23:  -0.1916                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2723 L22:   0.1652                                     
REMARK   3      L33:   0.1243 L12:   0.1959                                     
REMARK   3      L13:  -0.1903 L23:  -0.1324                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2651 S12:  -0.1784 S13:   0.5988                       
REMARK   3      S21:   0.5183 S22:  -0.0031 S23:  -0.6361                       
REMARK   3      S31:  -0.3258 S32:   0.0624 S33:   0.1454                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 15 THROUGH 28 )                   
REMARK   3    ORIGIN FOR THE GROUP (A): -49.4334  20.3955  10.6683              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.9697 T22:   0.2154                                     
REMARK   3      T33:   1.2188 T12:   0.0252                                     
REMARK   3      T13:  -0.4970 T23:  -0.2133                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  -0.0020 L22:   0.4145                                     
REMARK   3      L33:   0.2154 L12:   0.0723                                     
REMARK   3      L13:  -0.0439 L23:  -0.3001                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3596 S12:  -0.1652 S13:   1.0352                       
REMARK   3      S21:   0.3039 S22:  -0.3223 S23:  -0.2263                       
REMARK   3      S31:  -0.9072 S32:  -0.1007 S33:   0.4523                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 29 THROUGH 38 )                   
REMARK   3    ORIGIN FOR THE GROUP (A): -50.3056  12.5228   0.2704              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.2550 T22:   0.6031                                     
REMARK   3      T33:   0.8826 T12:   0.1370                                     
REMARK   3      T13:  -0.0256 T23:   0.0839                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.4964 L22:   1.3276                                     
REMARK   3      L33:   1.3990 L12:   2.1529                                     
REMARK   3      L13:   0.0761 L23:  -0.0129                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1035 S12:   0.3168 S13:   0.2712                       
REMARK   3      S21:   0.1408 S22:   0.1684 S23:   0.1451                       
REMARK   3      S31:  -1.4216 S32:  -0.2006 S33:  -0.0381                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 39 THROUGH 65 )                   
REMARK   3    ORIGIN FOR THE GROUP (A): -50.3891  16.7006  -6.4171              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.6598 T22:   0.8674                                     
REMARK   3      T33:   1.3601 T12:  -0.0686                                     
REMARK   3      T13:  -0.1623 T23:   0.3403                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1792 L22:   1.7275                                     
REMARK   3      L33:   1.8471 L12:   1.3700                                     
REMARK   3      L13:   0.2896 L23:   0.8403                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0090 S12:   0.6897 S13:   0.5031                       
REMARK   3      S21:   0.1307 S22:   0.2321 S23:  -0.7991                       
REMARK   3      S31:  -0.2887 S32:  -0.1896 S33:  -0.5676                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 66 THROUGH 91 )                   
REMARK   3    ORIGIN FOR THE GROUP (A): -55.0981  26.3620  12.8083              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.7251 T22:   0.6481                                     
REMARK   3      T33:   1.6807 T12:   0.3125                                     
REMARK   3      T13:   0.1147 T23:  -0.0102                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0777 L22:   0.0064                                     
REMARK   3      L33:   0.0125 L12:  -0.0243                                     
REMARK   3      L13:   0.0341 L23:  -0.0074                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2534 S12:  -0.0623 S13:   0.9083                       
REMARK   3      S21:   1.1773 S22:   0.1043 S23:  -0.2525                       
REMARK   3      S31:  -0.0126 S32:   0.1177 S33:   0.4115                       
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 92 THROUGH 119 )                  
REMARK   3    ORIGIN FOR THE GROUP (A): -43.2496  -4.7582  39.1748              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8163 T22:   0.7798                                     
REMARK   3      T33:   0.7087 T12:   0.2248                                     
REMARK   3      T13:  -0.1252 T23:  -0.3836                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3507 L22:   1.0186                                     
REMARK   3      L33:   1.5522 L12:   0.3109                                     
REMARK   3      L13:  -0.7179 L23:  -0.4260                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2130 S12:  -0.4982 S13:   0.4347                       
REMARK   3      S21:   0.6664 S22:  -0.1078 S23:   0.4134                       
REMARK   3      S31:  -0.4818 S32:   0.0315 S33:   0.3761                       
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 120 THROUGH 143 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -37.9724   1.7505  38.4501              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0010 T22:   0.7272                                     
REMARK   3      T33:   0.8485 T12:  -0.0418                                     
REMARK   3      T13:  -0.1346 T23:  -0.2849                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9142 L22:   1.0021                                     
REMARK   3      L33:   0.9453 L12:  -0.6928                                     
REMARK   3      L13:   0.6134 L23:  -0.3907                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0264 S12:   0.0481 S13:   0.4191                       
REMARK   3      S21:  -0.2956 S22:  -0.0162 S23:  -0.0983                       
REMARK   3      S31:  -0.3882 S32:   0.5520 S33:  -0.0611                       
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 144 THROUGH 157 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -49.4172   3.3027  28.3110              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7642 T22:   0.5219                                     
REMARK   3      T33:   0.8625 T12:   0.1715                                     
REMARK   3      T13:   0.1953 T23:  -0.4529                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2029 L22:   4.3848                                     
REMARK   3      L33:   3.9058 L12:   1.3502                                     
REMARK   3      L13:   0.1240 L23:  -0.4507                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.6581 S12:  -0.3744 S13:   0.4666                       
REMARK   3      S21:  -0.1546 S22:   0.2116 S23:   0.5171                       
REMARK   3      S31:  -0.0638 S32:   0.4861 S33:  -0.0070                       
REMARK   3   TLS GROUP : 16                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 158 THROUGH 177 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -36.2669  -6.0806  45.1304              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.1621 T22:   0.7797                                     
REMARK   3      T33:   0.5210 T12:   0.2788                                     
REMARK   3      T13:  -0.1017 T23:  -0.5411                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.4419 L22:   1.8162                                     
REMARK   3      L33:   2.2543 L12:   0.1464                                     
REMARK   3      L13:   0.8729 L23:   1.2525                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3802 S12:  -0.5305 S13:   0.1350                       
REMARK   3      S21:   0.7585 S22:  -0.0196 S23:  -0.1319                       
REMARK   3      S31:  -0.4744 S32:   0.3269 S33:  -0.2949                       
REMARK   3   TLS GROUP : 17                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 178 THROUGH 193 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -41.6171   3.9959  45.9340              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.3966 T22:   0.9310                                     
REMARK   3      T33:   0.8619 T12:   0.4061                                     
REMARK   3      T13:  -0.1897 T23:  -0.7102                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4239 L22:   1.6215                                     
REMARK   3      L33:   1.4604 L12:  -0.8653                                     
REMARK   3      L13:   0.8363 L23:  -0.3156                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2831 S12:  -0.5798 S13:   0.6719                       
REMARK   3      S21:   0.5704 S22:   0.0112 S23:  -0.0047                       
REMARK   3      S31:   0.0121 S32:   0.0782 S33:  -0.1775                       
REMARK   3   TLS GROUP : 18                                                     
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 3 THROUGH 45 )                    
REMARK   3    ORIGIN FOR THE GROUP (A): -46.2275 -13.1716  -1.6973              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2948 T22:   0.3199                                     
REMARK   3      T33:   0.4582 T12:   0.0206                                     
REMARK   3      T13:  -0.0330 T23:   0.0352                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2182 L22:   1.9953                                     
REMARK   3      L33:   2.0287 L12:   0.3184                                     
REMARK   3      L13:  -0.6229 L23:  -0.1285                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1716 S12:   0.2724 S13:   0.4560                       
REMARK   3      S21:   0.0245 S22:   0.0786 S23:   0.0578                       
REMARK   3      S31:  -0.1329 S32:  -0.2394 S33:   0.1278                       
REMARK   3   TLS GROUP : 19                                                     
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 46 THROUGH 58 )                   
REMARK   3    ORIGIN FOR THE GROUP (A): -45.9742  -1.2785   3.6464              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8852 T22:   0.1910                                     
REMARK   3      T33:   1.2346 T12:  -0.1900                                     
REMARK   3      T13:  -0.1875 T23:   0.0083                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5846 L22:   0.1616                                     
REMARK   3      L33:   2.6534 L12:  -0.2914                                     
REMARK   3      L13:   1.1778 L23:  -0.6465                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3106 S12:  -0.0753 S13:   0.9729                       
REMARK   3      S21:  -0.5635 S22:  -0.1997 S23:   0.2486                       
REMARK   3      S31:  -0.8805 S32:  -0.1021 S33:   0.2245                       
REMARK   3   TLS GROUP : 20                                                     
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 59 THROUGH 154 )                  
REMARK   3    ORIGIN FOR THE GROUP (A): -49.7612 -23.9534   3.0823              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2123 T22:   0.3951                                     
REMARK   3      T33:   0.3028 T12:   0.0099                                     
REMARK   3      T13:  -0.0456 T23:   0.0376                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7120 L22:   1.1619                                     
REMARK   3      L33:   1.7948 L12:   0.0209                                     
REMARK   3      L13:  -0.7969 L23:   0.2742                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0708 S12:   0.1411 S13:   0.3090                       
REMARK   3      S21:   0.0344 S22:   0.0684 S23:   0.0667                       
REMARK   3      S31:   0.0601 S32:  -0.0937 S33:   0.0144                       
REMARK   3   TLS GROUP : 21                                                     
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 155 THROUGH 182 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -54.9050 -33.2905  13.5626              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3875 T22:   0.4671                                     
REMARK   3      T33:   0.3856 T12:  -0.1114                                     
REMARK   3      T13:   0.0457 T23:   0.0467                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9140 L22:   1.7159                                     
REMARK   3      L33:   6.5355 L12:   0.2316                                     
REMARK   3      L13:  -1.0285 L23:   1.9773                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1351 S12:  -0.1906 S13:  -0.2586                       
REMARK   3      S21:   0.3773 S22:   0.0375 S23:  -0.0758                       
REMARK   3      S31:   0.8634 S32:  -0.6821 S33:  -0.1210                       
REMARK   3   TLS GROUP : 22                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID -5 THROUGH 32 )                   
REMARK   3    ORIGIN FOR THE GROUP (A): -40.7443 -20.3999  -8.4580              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2816 T22:   0.3870                                     
REMARK   3      T33:   0.3361 T12:  -0.0431                                     
REMARK   3      T13:   0.0275 T23:   0.0319                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.6249 L22:   2.0519                                     
REMARK   3      L33:   2.1965 L12:   1.4222                                     
REMARK   3      L13:   1.8487 L23:   1.8496                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0356 S12:   0.2369 S13:   0.1772                       
REMARK   3      S21:   0.1870 S22:  -0.0257 S23:   0.0230                       
REMARK   3      S31:  -0.0616 S32:   0.2300 S33:  -0.0007                       
REMARK   3   TLS GROUP : 23                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 33 THROUGH 122 )                  
REMARK   3    ORIGIN FOR THE GROUP (A): -33.3798 -14.4841  -2.3340              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3345 T22:   0.3967                                     
REMARK   3      T33:   0.4444 T12:  -0.1337                                     
REMARK   3      T13:  -0.0029 T23:   0.0612                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6752 L22:   0.2745                                     
REMARK   3      L33:   2.9536 L12:  -0.6405                                     
REMARK   3      L13:  -0.2169 L23:   0.0720                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0217 S12:   0.3674 S13:   0.3858                       
REMARK   3      S21:  -0.0847 S22:  -0.0354 S23:  -0.2038                       
REMARK   3      S31:  -0.3799 S32:   0.2469 S33:   0.0639                       
REMARK   3   TLS GROUP : 24                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 123 THROUGH 190 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -30.1004 -24.3689  26.4315              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4458 T22:   0.4369                                     
REMARK   3      T33:   0.3847 T12:   0.1141                                     
REMARK   3      T13:  -0.0371 T23:  -0.0725                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3582 L22:   1.1324                                     
REMARK   3      L33:   2.3923 L12:   0.2653                                     
REMARK   3      L13:   0.0257 L23:   1.0498                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1694 S12:  -0.2569 S13:  -0.0044                       
REMARK   3      S21:   0.6530 S22:   0.1783 S23:  -0.1159                       
REMARK   3      S31:   0.3322 S32:   0.6716 S33:  -0.0285                       
REMARK   3   TLS GROUP : 25                                                     
REMARK   3    SELECTION: CHAIN 'E' AND (RESID 84 THROUGH 93 )                   
REMARK   3    ORIGIN FOR THE GROUP (A): -41.1958  -9.1352 -16.2979              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3780 T22:   0.7789                                     
REMARK   3      T33:   0.7923 T12:  -0.1606                                     
REMARK   3      T13:  -0.0689 T23:   0.0815                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3628 L22:   1.1996                                     
REMARK   3      L33:   1.8222 L12:  -0.6023                                     
REMARK   3      L13:   0.0268 L23:  -1.3853                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4075 S12:   0.1375 S13:  -0.1205                       
REMARK   3      S21:   0.2034 S22:  -0.1106 S23:  -0.2699                       
REMARK   3      S31:  -0.4061 S32:  -0.1190 S33:   0.5898                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4GBX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-JUL-12.                  
REMARK 100 THE DEPOSITION ID IS D_1000073991.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 19-APR-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 24-ID-E                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.978                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 27191                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.500                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY                : 3.600                              
REMARK 200  R MERGE                    (I) : 0.07000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.00                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.87500                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: 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   (%): 62.01                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.24                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M MES, 6% PEG 20000, VAPOR            
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 291K, PH 6.5                   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
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       33.08350            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       71.55350            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       63.01600            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       71.55350            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       33.08350            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       63.01600            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 5570 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 19280 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -33.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 7300 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 18770 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -25.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, E                               
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     VAL C     1                                                      
REMARK 465     PRO C     2                                                      
REMARK 465     GLU C     3                                                      
REMARK 465     ALA C     4                                                      
REMARK 465     PRO C     5                                                      
REMARK 465     THR C     6                                                      
REMARK 465     PRO C     7                                                      
REMARK 465     MET C     8                                                      
REMARK 465     TRP C     9                                                      
REMARK 465     PRO C    10                                                      
REMARK 465     ASP C    11                                                      
REMARK 465     VAL C   201                                                      
REMARK 465     PRO C   202                                                      
REMARK 465     ARG C   203                                                      
REMARK 465     GLY D     1                                                      
REMARK 465     GLY D     2                                                      
REMARK 465     GLY D   194                                                      
REMARK 465     CYS D   195                                                      
REMARK 465     LEU D   196                                                      
REMARK 465     VAL D   197                                                      
REMARK 465     PRO D   198                                                      
REMARK 465     ARG D   199                                                      
REMARK 465     ILE A     1                                                      
REMARK 465     LYS A     2                                                      
REMARK 465     PRO A   183                                                      
REMARK 465     SER A   184                                                      
REMARK 465     PRO A   185                                                      
REMARK 465     LEU A   186                                                      
REMARK 465     PRO A   187                                                      
REMARK 465     GLU A   188                                                      
REMARK 465     THR A   189                                                      
REMARK 465     THR A   190                                                      
REMARK 465     GLU A   191                                                      
REMARK 465     LYS B   105                                                      
REMARK 465     THR B   106                                                      
REMARK 465     GLN B   107                                                      
REMARK 465     PRO B   108                                                      
REMARK 465     LEU B   109                                                      
REMARK 465     GLN B   110                                                      
REMARK 465     HIS B   111                                                      
REMARK 465     ARG B   191                                                      
REMARK 465     SER B   192                                                      
REMARK 465     SER B   193                                                      
REMARK 465     GLY B   194                                                      
REMARK 465     GLY B   195                                                      
REMARK 465     GLY B   196                                                      
REMARK 465     SER B   197                                                      
REMARK 465     LEU B   198                                                      
REMARK 465     PRO B   199                                                      
REMARK 465     ALA B   200                                                      
REMARK 465     THR B   201                                                      
REMARK 465     GLY B   202                                                      
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     GLN C  14    CG   CD   OE1  NE2                                  
REMARK 470     LEU C  56    CG   CD1  CD2                                       
REMARK 470     GLN C  64    CG   CD   OE1  NE2                                  
REMARK 470     PHE C 145    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ASP D  15    CG   OD1  OD2                                       
REMARK 470     LYS D  20    CG   CD   CE   NZ                                   
REMARK 470     ASN D  74    CG   OD1  ND2                                       
REMARK 470     LYS B  65    CG   CD   CE   NZ                                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   ND2  ASN A   118     O5   NAG A   201              2.00            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   NZ   LYS C    89     O    GLY D   169     2354     2.17            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ARG C  55     -143.18    -74.01                                   
REMARK 500    LEU C  56       79.37   -114.82                                   
REMARK 500    PRO C  57       61.11   -115.09                                   
REMARK 500    GLU C  58       44.84     39.89                                   
REMARK 500    ALA C  60       86.36     53.62                                   
REMARK 500    ALA C  63     -131.97     55.83                                   
REMARK 500    ASP C  68       84.78   -150.53                                   
REMARK 500    ASP C 183       20.26   -153.49                                   
REMARK 500    LEU D  33      -61.03   -102.77                                   
REMARK 500    MET D  43       58.18    -96.40                                   
REMARK 500    GLU D  47     -139.02     50.13                                   
REMARK 500    LEU D  62      157.89     80.34                                   
REMARK 500    ASN D  63       -8.00     67.53                                   
REMARK 500    MET D  69      -18.00    -41.79                                   
REMARK 500    THR D 158     -178.79   -178.23                                   
REMARK 500    GLU D 177       73.51   -111.94                                   
REMARK 500    ASP A  27       15.41     51.09                                   
REMARK 500    ARG A 100       -4.17     80.57                                   
REMARK 500    PRO A 115       72.19    -65.23                                   
REMARK 500    ASN A 124       73.63     42.55                                   
REMARK 500    GLN B  -2      -88.75   -123.12                                   
REMARK 500    ASN B  19       73.30     41.92                                   
REMARK 500    ASN B  33     -105.41     51.99                                   
REMARK 500    VAL B  85      -71.14    -61.50                                   
REMARK 500    TRP B 153       34.89     80.22                                   
REMARK 500    HIS B 177      142.26   -170.53                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  4GBX C    1   199  UNP    P28067   DMA_HUMAN       27    225             
DBREF  4GBX D    1   193  UNP    P28068   DMB_HUMAN       19    211             
DBREF  4GBX A    1   191  UNP    P01903   DRA_HUMAN       26    216             
DBREF  4GBX B    1   191  UNP    P04229   2B11_HUMAN      30    220             
DBREF  4GBX E   84    93  PDB    4GBX     4GBX            84     93             
SEQADV 4GBX GLN C  136  UNP  P28067    HIS   162 VARIANT                        
SEQADV 4GBX HIS C  137  UNP  P28067    ASP   163 VARIANT                        
SEQADV 4GBX ASP C  165  UNP  P28067    ASN   191 ENGINEERED MUTATION            
SEQADV 4GBX LEU C  200  UNP  P28067              EXPRESSION TAG                 
SEQADV 4GBX VAL C  201  UNP  P28067              EXPRESSION TAG                 
SEQADV 4GBX PRO C  202  UNP  P28067              EXPRESSION TAG                 
SEQADV 4GBX ARG C  203  UNP  P28067              EXPRESSION TAG                 
SEQADV 4GBX SER D   46  UNP  P28068    CYS    64 ENGINEERED MUTATION            
SEQADV 4GBX ASP D   92  UNP  P28068    ASN   110 ENGINEERED MUTATION            
SEQADV 4GBX GLY D  194  UNP  P28068              EXPRESSION TAG                 
SEQADV 4GBX CYS D  195  UNP  P28068              EXPRESSION TAG                 
SEQADV 4GBX LEU D  196  UNP  P28068              EXPRESSION TAG                 
SEQADV 4GBX VAL D  197  UNP  P28068              EXPRESSION TAG                 
SEQADV 4GBX PRO D  198  UNP  P28068              EXPRESSION TAG                 
SEQADV 4GBX ARG D  199  UNP  P28068              EXPRESSION TAG                 
SEQADV 4GBX CYS A   65  UNP  P01903    VAL    90 ENGINEERED MUTATION            
SEQADV 4GBX VAL B   -5  UNP  P04229              EXPRESSION TAG                 
SEQADV 4GBX LEU B   -4  UNP  P04229              EXPRESSION TAG                 
SEQADV 4GBX PHE B   -3  UNP  P04229              EXPRESSION TAG                 
SEQADV 4GBX GLN B   -2  UNP  P04229              EXPRESSION TAG                 
SEQADV 4GBX GLY B   -1  UNP  P04229              EXPRESSION TAG                 
SEQADV 4GBX PRO B    0  UNP  P04229              EXPRESSION TAG                 
SEQADV 4GBX SER B   30  UNP  P04229    CYS    59 ENGINEERED MUTATION            
SEQADV 4GBX SER B  192  UNP  P04229              EXPRESSION TAG                 
SEQADV 4GBX SER B  193  UNP  P04229              EXPRESSION TAG                 
SEQADV 4GBX GLY B  194  UNP  P04229              EXPRESSION TAG                 
SEQADV 4GBX GLY B  195  UNP  P04229              EXPRESSION TAG                 
SEQADV 4GBX GLY B  196  UNP  P04229              EXPRESSION TAG                 
SEQADV 4GBX SER B  197  UNP  P04229              EXPRESSION TAG                 
SEQADV 4GBX LEU B  198  UNP  P04229              EXPRESSION TAG                 
SEQADV 4GBX PRO B  199  UNP  P04229              EXPRESSION TAG                 
SEQADV 4GBX ALA B  200  UNP  P04229              EXPRESSION TAG                 
SEQADV 4GBX THR B  201  UNP  P04229              EXPRESSION TAG                 
SEQADV 4GBX GLY B  202  UNP  P04229              EXPRESSION TAG                 
SEQRES   1 C  203  VAL PRO GLU ALA PRO THR PRO MET TRP PRO ASP ASP LEU          
SEQRES   2 C  203  GLN ASN HIS THR PHE LEU HIS THR VAL TYR CYS GLN ASP          
SEQRES   3 C  203  GLY SER PRO SER VAL GLY LEU SER GLU ALA TYR ASP GLU          
SEQRES   4 C  203  ASP GLN LEU PHE PHE PHE ASP PHE SER GLN ASN THR ARG          
SEQRES   5 C  203  VAL PRO ARG LEU PRO GLU PHE ALA ASP TRP ALA GLN GLU          
SEQRES   6 C  203  GLN GLY ASP ALA PRO ALA ILE LEU PHE ASP LYS GLU PHE          
SEQRES   7 C  203  CYS GLU TRP MET ILE GLN GLN ILE GLY PRO LYS LEU ASP          
SEQRES   8 C  203  GLY LYS ILE PRO VAL SER ARG GLY PHE PRO ILE ALA GLU          
SEQRES   9 C  203  VAL PHE THR LEU LYS PRO LEU GLU PHE GLY LYS PRO ASN          
SEQRES  10 C  203  THR LEU VAL CYS PHE VAL SER ASN LEU PHE PRO PRO MET          
SEQRES  11 C  203  LEU THR VAL ASN TRP GLN HIS HIS SER VAL PRO VAL GLU          
SEQRES  12 C  203  GLY PHE GLY PRO THR PHE VAL SER ALA VAL ASP GLY LEU          
SEQRES  13 C  203  SER PHE GLN ALA PHE SER TYR LEU ASP PHE THR PRO GLU          
SEQRES  14 C  203  PRO SER ASP ILE PHE SER CYS ILE VAL THR HIS GLU ILE          
SEQRES  15 C  203  ASP ARG TYR THR ALA ILE ALA TYR TRP VAL PRO ARG ASN          
SEQRES  16 C  203  ALA LEU PRO SER LEU VAL PRO ARG                              
SEQRES   1 D  199  GLY GLY PHE VAL ALA HIS VAL GLU SER THR CYS LEU LEU          
SEQRES   2 D  199  ASP ASP ALA GLY THR PRO LYS ASP PHE THR TYR CYS ILE          
SEQRES   3 D  199  SER PHE ASN LYS ASP LEU LEU THR CYS TRP ASP PRO GLU          
SEQRES   4 D  199  GLU ASN LYS MET ALA PRO SER GLU PHE GLY VAL LEU ASN          
SEQRES   5 D  199  SER LEU ALA ASN VAL LEU SER GLN HIS LEU ASN GLN LYS          
SEQRES   6 D  199  ASP THR LEU MET GLN ARG LEU ARG ASN GLY LEU GLN ASN          
SEQRES   7 D  199  CYS ALA THR HIS THR GLN PRO PHE TRP GLY SER LEU THR          
SEQRES   8 D  199  ASP ARG THR ARG PRO PRO SER VAL GLN VAL ALA LYS THR          
SEQRES   9 D  199  THR PRO PHE ASN THR ARG GLU PRO VAL MET LEU ALA CYS          
SEQRES  10 D  199  TYR VAL TRP GLY PHE TYR PRO ALA GLU VAL THR ILE THR          
SEQRES  11 D  199  TRP ARG LYS ASN GLY LYS LEU VAL MET PRO HIS SER SER          
SEQRES  12 D  199  ALA HIS LYS THR ALA GLN PRO ASN GLY ASP TRP THR TYR          
SEQRES  13 D  199  GLN THR LEU SER HIS LEU ALA LEU THR PRO SER TYR GLY          
SEQRES  14 D  199  ASP THR TYR THR CYS VAL VAL GLU HIS ILE GLY ALA PRO          
SEQRES  15 D  199  GLU PRO ILE LEU ARG ASP TRP THR PRO GLY LEU GLY CYS          
SEQRES  16 D  199  LEU VAL PRO ARG                                              
SEQRES   1 A  191  ILE LYS GLU GLU HIS VAL ILE ILE GLN ALA GLU PHE TYR          
SEQRES   2 A  191  LEU ASN PRO ASP GLN SER GLY GLU PHE MET PHE ASP PHE          
SEQRES   3 A  191  ASP GLY ASP GLU ILE PHE HIS VAL ASP MET ALA LYS LYS          
SEQRES   4 A  191  GLU THR VAL TRP ARG LEU GLU GLU PHE GLY ARG PHE ALA          
SEQRES   5 A  191  SER PHE GLU ALA GLN GLY ALA LEU ALA ASN ILE ALA CYS          
SEQRES   6 A  191  ASP LYS ALA ASN LEU GLU ILE MET THR LYS ARG SER ASN          
SEQRES   7 A  191  TYR THR PRO ILE THR ASN VAL PRO PRO GLU VAL THR VAL          
SEQRES   8 A  191  LEU THR ASN SER PRO VAL GLU LEU ARG GLU PRO ASN VAL          
SEQRES   9 A  191  LEU ILE CYS PHE ILE ASP LYS PHE THR PRO PRO VAL VAL          
SEQRES  10 A  191  ASN VAL THR TRP LEU ARG ASN GLY LYS PRO VAL THR THR          
SEQRES  11 A  191  GLY VAL SER GLU THR VAL PHE LEU PRO ARG GLU ASP HIS          
SEQRES  12 A  191  LEU PHE ARG LYS PHE HIS TYR LEU PRO PHE LEU PRO SER          
SEQRES  13 A  191  THR GLU ASP VAL TYR ASP CYS ARG VAL GLU HIS TRP GLY          
SEQRES  14 A  191  LEU ASP GLU PRO LEU LEU LYS HIS TRP GLU PHE ASP ALA          
SEQRES  15 A  191  PRO SER PRO LEU PRO GLU THR THR GLU                          
SEQRES   1 B  208  VAL LEU PHE GLN GLY PRO GLY ASP THR ARG PRO ARG PHE          
SEQRES   2 B  208  LEU TRP GLN LEU LYS PHE GLU CYS HIS PHE PHE ASN GLY          
SEQRES   3 B  208  THR GLU ARG VAL ARG LEU LEU GLU ARG SER ILE TYR ASN          
SEQRES   4 B  208  GLN GLU GLU SER VAL ARG PHE ASP SER ASP VAL GLY GLU          
SEQRES   5 B  208  TYR ARG ALA VAL THR GLU LEU GLY ARG PRO ASP ALA GLU          
SEQRES   6 B  208  TYR TRP ASN SER GLN LYS ASP LEU LEU GLU GLN ARG ARG          
SEQRES   7 B  208  ALA ALA VAL ASP THR TYR CYS ARG HIS ASN TYR GLY VAL          
SEQRES   8 B  208  GLY GLU SER PHE THR VAL GLN ARG ARG VAL GLU PRO LYS          
SEQRES   9 B  208  VAL THR VAL TYR PRO SER LYS THR GLN PRO LEU GLN HIS          
SEQRES  10 B  208  HIS ASN LEU LEU VAL CYS SER VAL SER GLY PHE TYR PRO          
SEQRES  11 B  208  GLY SER ILE GLU VAL ARG TRP PHE ARG ASN GLY GLN GLU          
SEQRES  12 B  208  GLU LYS ALA GLY VAL VAL SER THR GLY LEU ILE GLN ASN          
SEQRES  13 B  208  GLY ASP TRP THR PHE GLN THR LEU VAL MET LEU GLU THR          
SEQRES  14 B  208  VAL PRO ARG SER GLY GLU VAL TYR THR CYS GLN VAL GLU          
SEQRES  15 B  208  HIS PRO SER VAL THR SER PRO LEU THR VAL GLU TRP ARG          
SEQRES  16 B  208  ALA ARG SER SER GLY GLY GLY SER LEU PRO ALA THR GLY          
SEQRES   1 E   10  GLY LYS GLN ASN CYS LEU LYS LEU ALA THR                      
MODRES 4GBX ASN A   78  ASN  GLYCOSYLATION SITE                                 
MODRES 4GBX ASN C   15  ASN  GLYCOSYLATION SITE                                 
MODRES 4GBX ASN A  118  ASN  GLYCOSYLATION SITE                                 
HET    NAG  C 301      14                                                       
HET    NAG  A 201      14                                                       
HET    NAG  A 202      14                                                       
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
FORMUL   6  NAG    3(C8 H15 N O6)                                               
FORMUL   9  HOH   *56(H2 O)                                                     
HELIX    1   1 ASP C   68  ILE C   86  1                                  19    
HELIX    2   2 ILE C   86  ASP C   91  1                                   6    
HELIX    3   3 LEU D   51  HIS D   61  1                                  11    
HELIX    4   4 LYS D   65  GLY D   75  1                                  11    
HELIX    5   5 GLY D   75  ARG D   93  1                                  19    
HELIX    6   6 LEU A   45  GLN A   57  1                                  13    
HELIX    7   7 GLY A   58  SER A   77  1                                  20    
HELIX    8   8 THR B   51  LEU B   53  5                                   3    
HELIX    9   9 GLY B   54  GLN B   64  1                                  11    
HELIX   10  10 GLN B   64  TYR B   78  1                                  15    
HELIX   11  11 TYR B   78  GLY B   86  1                                   9    
HELIX   12  12 GLY B   86  VAL B   91  1                                   6    
SHEET    1   A 7 THR C  51  PRO C  54  0                                        
SHEET    2   A 7 ASP C  40  ASP C  46 -1  N  PHE C  44   O  VAL C  53           
SHEET    3   A 7 VAL C  31  TYR C  37 -1  N  LEU C  33   O  PHE C  45           
SHEET    4   A 7 THR C  17  GLN C  25 -1  N  THR C  21   O  SER C  34           
SHEET    5   A 7 VAL D   4  LEU D  13 -1  O  ALA D   5   N  CYS C  24           
SHEET    6   A 7 PRO D  19  PHE D  28 -1  O  LYS D  20   N  LEU D  12           
SHEET    7   A 7 LEU D  32  THR D  34 -1  O  THR D  34   N  ILE D  26           
SHEET    1   B 9 VAL C  96  SER C  97  0                                        
SHEET    2   B 9 GLU A  40  TRP A  43  1  O  THR A  41   N  VAL C  96           
SHEET    3   B 9 ASP A  29  ASP A  35 -1  N  HIS A  33   O  VAL A  42           
SHEET    4   B 9 SER A  19  PHE A  26 -1  N  PHE A  26   O  ASP A  29           
SHEET    5   B 9 HIS A   5  ASN A  15 -1  N  ALA A  10   O  MET A  23           
SHEET    6   B 9 PHE B   7  PHE B  18 -1  O  CYS B  15   N  ILE A   7           
SHEET    7   B 9 ARG B  23  TYR B  32 -1  O  LEU B  27   N  GLU B  14           
SHEET    8   B 9 GLU B  35  ASP B  41 -1  O  GLU B  35   N  TYR B  32           
SHEET    9   B 9 TYR B  47  ALA B  49 -1  O  ARG B  48   N  ARG B  39           
SHEET    1   C 4 ILE C 102  THR C 107  0                                        
SHEET    2   C 4 ASN C 117  LEU C 126 -1  O  SER C 124   N  ILE C 102           
SHEET    3   C 4 SER C 157  PHE C 166 -1  O  PHE C 166   N  ASN C 117           
SHEET    4   C 4 PHE C 145  VAL C 153 -1  N  SER C 151   O  GLN C 159           
SHEET    1   D 4 VAL C 140  VAL C 142  0                                        
SHEET    2   D 4 LEU C 131  HIS C 137 -1  N  TRP C 135   O  VAL C 142           
SHEET    3   D 4 PHE C 174  HIS C 180 -1  O  ILE C 177   N  ASN C 134           
SHEET    4   D 4 THR C 186  TRP C 191 -1  O  ALA C 189   N  CYS C 176           
SHEET    1   E 4 SER D  98  LYS D 103  0                                        
SHEET    2   E 4 VAL D 113  PHE D 122 -1  O  ALA D 116   N  ALA D 102           
SHEET    3   E 4 TYR D 156  LEU D 164 -1  O  SER D 160   N  CYS D 117           
SHEET    4   E 4 GLN D 149  PRO D 150 -1  N  GLN D 149   O  GLN D 157           
SHEET    1   F 4 LYS D 136  VAL D 138  0                                        
SHEET    2   F 4 ILE D 129  LYS D 133 -1  N  LYS D 133   O  LYS D 136           
SHEET    3   F 4 TYR D 172  VAL D 176 -1  O  THR D 173   N  ARG D 132           
SHEET    4   F 4 ILE D 185  TRP D 189 -1  O  TRP D 189   N  TYR D 172           
SHEET    1   G 4 GLU A  88  THR A  93  0                                        
SHEET    2   G 4 ASN A 103  PHE A 112 -1  O  ILE A 106   N  LEU A  92           
SHEET    3   G 4 PHE A 145  PHE A 153 -1  O  LEU A 151   N  LEU A 105           
SHEET    4   G 4 SER A 133  GLU A 134 -1  N  SER A 133   O  TYR A 150           
SHEET    1   H 4 GLU A  88  THR A  93  0                                        
SHEET    2   H 4 ASN A 103  PHE A 112 -1  O  ILE A 106   N  LEU A  92           
SHEET    3   H 4 PHE A 145  PHE A 153 -1  O  LEU A 151   N  LEU A 105           
SHEET    4   H 4 LEU A 138  PRO A 139 -1  N  LEU A 138   O  ARG A 146           
SHEET    1   I 4 LYS A 126  PRO A 127  0                                        
SHEET    2   I 4 ASN A 118  ARG A 123 -1  N  ARG A 123   O  LYS A 126           
SHEET    3   I 4 TYR A 161  GLU A 166 -1  O  ARG A 164   N  THR A 120           
SHEET    4   I 4 LEU A 174  TRP A 178 -1  O  TRP A 178   N  TYR A 161           
SHEET    1   J 4 LYS B  98  PRO B 103  0                                        
SHEET    2   J 4 ASN B 113  PHE B 122 -1  O  VAL B 116   N  TYR B 102           
SHEET    3   J 4 PHE B 155  THR B 163 -1  O  VAL B 159   N  CYS B 117           
SHEET    4   J 4 VAL B 142  SER B 144 -1  N  VAL B 143   O  MET B 160           
SHEET    1   K 4 LYS B  98  PRO B 103  0                                        
SHEET    2   K 4 ASN B 113  PHE B 122 -1  O  VAL B 116   N  TYR B 102           
SHEET    3   K 4 PHE B 155  THR B 163 -1  O  VAL B 159   N  CYS B 117           
SHEET    4   K 4 ILE B 148  GLN B 149 -1  N  ILE B 148   O  GLN B 156           
SHEET    1   L 4 GLN B 136  GLU B 138  0                                        
SHEET    2   L 4 GLU B 128  ARG B 133 -1  N  ARG B 133   O  GLN B 136           
SHEET    3   L 4 VAL B 170  GLU B 176 -1  O  THR B 172   N  PHE B 132           
SHEET    4   L 4 LEU B 184  ARG B 189 -1  O  LEU B 184   N  VAL B 175           
SSBOND   1 CYS C   24    CYS C   79                          1555   1555  2.03  
SSBOND   2 CYS C  121    CYS C  176                          1555   1555  2.02  
SSBOND   3 CYS D   11    CYS D   79                          1555   1555  2.03  
SSBOND   4 CYS D   25    CYS D   35                          1555   1555  2.01  
SSBOND   5 CYS D  117    CYS D  174                          1555   1555  2.02  
SSBOND   6 CYS A   65    CYS E   88                          1555   1555  2.06  
SSBOND   7 CYS A  107    CYS A  163                          1555   1555  2.06  
SSBOND   8 CYS B   15    CYS B   79                          1555   1555  2.06  
SSBOND   9 CYS B  117    CYS B  173                          1555   1555  2.04  
LINK         ND2 ASN C  15                 C1  NAG C 301     1555   1555  1.50  
LINK         ND2 ASN A  78                 C1  NAG A 202     1555   1555  1.50  
LINK         ND2 ASN A 118                 C1  NAG A 201     1555   1555  1.54  
CISPEP   1 SER C   28    PRO C   29          0        -1.40                     
CISPEP   2 PHE C  127    PRO C  128          0         0.95                     
CISPEP   3 TYR D  123    PRO D  124          0        -3.10                     
CISPEP   4 ASN A   15    PRO A   16          0        -0.45                     
CISPEP   5 GLN A   57    GLY A   58          0        -3.59                     
CISPEP   6 THR A  113    PRO A  114          0        -5.53                     
CISPEP   7 TYR B  123    PRO B  124          0         9.43                     
CRYST1   66.167  126.032  143.107  90.00  90.00  90.00 P 21 21 21    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      0.015113  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007934  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006988        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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