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Entry: 5XAM
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HEADER    MEMBRANE PROTEIN                        14-MAR-17   5XAM              
TITLE     CRYSTAL STRUCTURE OF SECDF IN I FORM AT 4 A RESOLUTION                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROTEIN TRANSLOCASE SUBUNIT SECD;                          
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: UNP RESIDUES 28-768;                                       
COMPND   5 SYNONYM: PROTEIN-EXPORT MEMBRANE PROTEIN SECF;                       
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: DEINOCOCCUS RADIODURANS STR. R1;                
SOURCE   3 ORGANISM_TAXID: 243230;                                              
SOURCE   4 STRAIN: R1;                                                          
SOURCE   5 GENE: SECD, SECF, DR_1822;                                           
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: C41(DE3);                                  
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET28                                     
KEYWDS    MEMBRANE PROTEIN, ALFA HELICAL, SEC TRANSLOCON                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    T.TSUKAZAKI,Y.TANAKA,A.FURUKWA                                        
REVDAT   5   11-NOV-20 5XAM    1       REMARK                                   
REVDAT   4   14-OCT-20 5XAM    1       SOURCE                                   
REVDAT   3   22-MAY-19 5XAM    1       TITLE                                    
REVDAT   2   04-OCT-17 5XAM    1       REMARK                                   
REVDAT   1   17-MAY-17 5XAM    0                                                
JRNL        AUTH   A.FURUKAWA,K.YOSHIKAIE,T.MORI,H.MORI,Y.V.MORIMOTO,Y.SUGANO,  
JRNL        AUTH 2 S.IWAKI,T.MINAMINO,Y.SUGITA,Y.TANAKA,T.TSUKAZAKI             
JRNL        TITL   TUNNEL FORMATION INFERRED FROM THE I-FORM STRUCTURES OF THE  
JRNL        TITL 2 PROTON-DRIVEN PROTEIN SECRETION MOTOR SECDF                  
JRNL        REF    CELL REP                      V.  19   895 2017              
JRNL        REFN                   ESSN 2211-1247                               
JRNL        PMID   28467902                                                     
JRNL        DOI    10.1016/J.CELREP.2017.04.030                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    4.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.10.1_2155                                   
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 : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 4.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 47.99                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.330                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 17102                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.340                           
REMARK   3   R VALUE            (WORKING SET) : 0.333                           
REMARK   3   FREE R VALUE                     : 0.402                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.000                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 1711                            
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 47.9888 -  9.1384    0.99     1397   153  0.2095 0.2974        
REMARK   3     2  9.1384 -  7.2615    1.00     1343   154  0.3004 0.3973        
REMARK   3     3  7.2615 -  6.3460    1.00     1327   153  0.3972 0.4359        
REMARK   3     4  6.3460 -  5.7668    1.00     1330   148  0.4141 0.4403        
REMARK   3     5  5.7668 -  5.3541    1.00     1333   139  0.4057 0.3976        
REMARK   3     6  5.3541 -  5.0387    1.00     1308   151  0.3913 0.4336        
REMARK   3     7  5.0387 -  4.7866    0.99     1290   138  0.4124 0.4691        
REMARK   3     8  4.7866 -  4.5784    1.00     1332   152  0.4505 0.5016        
REMARK   3     9  4.5784 -  4.4023    0.79     1047   112  0.4977 0.5751        
REMARK   3    10  4.4023 -  4.2505    0.92     1187   150  0.4698 0.5154        
REMARK   3    11  4.2505 -  4.1177    0.94     1247   123  0.3947 0.4411        
REMARK   3    12  4.1177 -  4.0000    0.96     1250   138  0.3740 0.4885        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
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)     : 1.070            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 51.950           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 149.4                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 242.3                          
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      :  0.003           9997                                  
REMARK   3   ANGLE     :  0.708          13699                                  
REMARK   3   CHIRALITY :  0.042           1789                                  
REMARK   3   PLANARITY :  0.006           1716                                  
REMARK   3   DIHEDRAL  : 13.235           5864                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 17                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 29 THROUGH 110 )                  
REMARK   3    ORIGIN FOR THE GROUP (A): -11.6396   3.6477  38.6215              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4516 T22:   1.8819                                     
REMARK   3      T33:   2.4495 T12:   0.3137                                     
REMARK   3      T13:   0.4193 T23:  -0.0537                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3296 L22:   3.3316                                     
REMARK   3      L33:   7.9068 L12:   1.1335                                     
REMARK   3      L13:  -1.9438 L23:   3.2583                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1157 S12:  -0.9338 S13:   0.6600                       
REMARK   3      S21:  -0.8355 S22:  -0.0189 S23:  -1.2986                       
REMARK   3      S31:  -0.9636 S32:   1.4420 S33:  -0.1872                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 111 THROUGH 270 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -5.4274  -6.8130   0.7564              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.5479 T22:   1.6217                                     
REMARK   3      T33:   1.9013 T12:   0.0955                                     
REMARK   3      T13:   0.4483 T23:   0.2161                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.6903 L22:   3.3544                                     
REMARK   3      L33:   6.7738 L12:   1.2402                                     
REMARK   3      L13:   0.4869 L23:  -1.2707                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1875 S12:   1.2723 S13:   0.7421                       
REMARK   3      S21:  -1.0797 S22:  -0.0457 S23:  -0.6221                       
REMARK   3      S31:   1.5962 S32:   1.6219 S33:   0.0987                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 271 THROUGH 380 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -20.2531  -6.3199  51.6767              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6051 T22:   1.0826                                     
REMARK   3      T33:   1.5462 T12:   0.0757                                     
REMARK   3      T13:  -0.0799 T23:  -0.4025                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.8852 L22:   1.8466                                     
REMARK   3      L33:   9.1516 L12:  -2.7895                                     
REMARK   3      L13:  -1.6172 L23:  -0.8319                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3120 S12:  -0.3039 S13:  -1.3220                       
REMARK   3      S21:   0.2740 S22:  -0.0745 S23:  -0.4201                       
REMARK   3      S31:  -0.1438 S32:  -0.6038 S33:   0.4443                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 381 THROUGH 513 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -16.5653 -13.4908  60.7545              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0764 T22:   1.5819                                     
REMARK   3      T33:   2.0871 T12:   0.1164                                     
REMARK   3      T13:  -0.1322 T23:  -0.2081                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1577 L22:   3.6398                                     
REMARK   3      L33:   2.5720 L12:  -1.9358                                     
REMARK   3      L13:   2.2620 L23:  -2.4618                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.8498 S12:   0.4442 S13:  -1.0164                       
REMARK   3      S21:   0.9023 S22:   0.0107 S23:  -0.5321                       
REMARK   3      S31:   1.0289 S32:   0.8749 S33:  -0.3343                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 514 THROUGH 548 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -28.3254 -28.1342  25.6804              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.3499 T22:   3.2236                                     
REMARK   3      T33:   1.3629 T12:  -1.8275                                     
REMARK   3      T13:  -1.5444 T23:  -2.0892                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.5140 L22:   3.4636                                     
REMARK   3      L33:   9.7112 L12:  -0.4992                                     
REMARK   3      L13:  -4.8755 L23:  -2.3681                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   1.7542 S12:   1.0961 S13:  -0.0976                       
REMARK   3      S21:   0.2968 S22:   1.3205 S23:  -0.0518                       
REMARK   3      S31:   2.6583 S32:   1.5263 S33:   2.1820                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 549 THROUGH 644 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -12.1809 -22.9215  42.2291              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7066 T22:   2.6762                                     
REMARK   3      T33:   1.9503 T12:   0.4343                                     
REMARK   3      T13:  -0.3372 T23:  -0.6592                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1043 L22:   4.0617                                     
REMARK   3      L33:   6.7176 L12:   0.8629                                     
REMARK   3      L13:  -1.0900 L23:  -0.8123                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.9917 S12:   1.2997 S13:  -1.6362                       
REMARK   3      S21:   0.3460 S22:  -0.8191 S23:  -0.5192                       
REMARK   3      S31:   1.0265 S32:   1.4444 S33:   0.2449                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 645 THROUGH 758 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -16.1253 -22.8903  65.4240              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7543 T22:   1.3747                                     
REMARK   3      T33:   1.4439 T12:  -0.1158                                     
REMARK   3      T13:  -0.1376 T23:   0.0642                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0612 L22:   4.9613                                     
REMARK   3      L33:   7.6484 L12:   0.4581                                     
REMARK   3      L13:   0.1384 L23:   2.2686                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2930 S12:   0.3304 S13:   0.6984                       
REMARK   3      S21:   1.2636 S22:  -0.5451 S23:  -0.6975                       
REMARK   3      S31:   2.4176 S32:   0.7784 S33:  -0.8419                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 31 THROUGH 69 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  23.4046  -1.1809  49.9323              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   2.0996 T22:  -0.4697                                     
REMARK   3      T33:   2.4686 T12:  -1.8123                                     
REMARK   3      T13:   1.0476 T23:   0.2790                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.6257 L22:   2.0227                                     
REMARK   3      L33:   6.8718 L12:  -3.3274                                     
REMARK   3      L13:  -2.2871 L23:  -0.1811                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   1.5854 S12:   1.7354 S13:   0.7630                       
REMARK   3      S21:  -4.5341 S22:  -1.5349 S23:  -1.3992                       
REMARK   3      S31:  -0.5244 S32:  -0.2550 S33:   0.5557                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 70 THROUGH 128 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  36.5301 -18.6973  24.7963              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   3.1299 T22:   1.2994                                     
REMARK   3      T33:   2.2716 T12:   1.4763                                     
REMARK   3      T13:   2.9419 T23:  -0.7229                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.2246 L22:   3.9555                                     
REMARK   3      L33:   2.4816 L12:  -0.9947                                     
REMARK   3      L13:  -2.8744 L23:  -0.2673                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.8352 S12:   0.2281 S13:   0.5796                       
REMARK   3      S21:  -2.9394 S22:  -1.4098 S23:  -4.4347                       
REMARK   3      S31:  -0.6862 S32:   0.5172 S33:  -0.4106                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 129 THROUGH 164 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  31.3433 -23.3297   5.1684              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.1247 T22:   2.0589                                     
REMARK   3      T33:   3.0938 T12:   0.2226                                     
REMARK   3      T13:   0.6510 T23:   0.9232                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.6086 L22:   2.1819                                     
REMARK   3      L33:   0.4020 L12:   0.8959                                     
REMARK   3      L13:   1.0113 L23:  -0.1931                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -1.1667 S12:   0.6198 S13:  -0.7662                       
REMARK   3      S21:  -1.3416 S22:  -0.2715 S23:  -0.7225                       
REMARK   3      S31:  -0.7059 S32:   1.8194 S33:   0.1081                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 165 THROUGH 230 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  37.8156 -14.5920  -6.4467              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   2.6340 T22:   4.7639                                     
REMARK   3      T33:   2.1542 T12:   0.6187                                     
REMARK   3      T13:  -0.7074 T23:   1.5898                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4329 L22:   9.8039                                     
REMARK   3      L33:   7.0940 L12:  -0.5195                                     
REMARK   3      L13:  -0.8356 L23:   6.1079                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0561 S12:   2.2791 S13:   1.3776                       
REMARK   3      S21:  -0.5739 S22:   1.5743 S23:  -1.1667                       
REMARK   3      S31:  -1.7649 S32:   3.0038 S33:   1.7670                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 231 THROUGH 288 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  32.7109 -21.9571   7.9904              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   2.3324 T22:   4.6303                                     
REMARK   3      T33:   2.7161 T12:   1.6473                                     
REMARK   3      T13:   1.4100 T23:   0.9553                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1449 L22:   4.5103                                     
REMARK   3      L33:   1.0323 L12:   2.2329                                     
REMARK   3      L13:   1.1127 L23:   2.1502                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -2.5575 S12:   0.4297 S13:   0.9859                       
REMARK   3      S21:  -0.9471 S22:   0.3035 S23:   0.4656                       
REMARK   3      S31:   1.7688 S32:   0.7014 S33:   0.1440                       
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 289 THROUGH 408 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  22.9785 -18.9602  61.7711              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.5789 T22:   0.6969                                     
REMARK   3      T33:   0.9536 T12:  -0.0997                                     
REMARK   3      T13:   0.2679 T23:  -0.7336                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.0488 L22:   5.1812                                     
REMARK   3      L33:   4.5421 L12:  -2.1735                                     
REMARK   3      L13:   0.6335 L23:  -3.6381                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -1.1424 S12:  -0.4284 S13:   0.4472                       
REMARK   3      S21:   1.6823 S22:   0.0319 S23:  -0.8407                       
REMARK   3      S31:  -0.4303 S32:  -0.9126 S33:   0.5813                       
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 409 THROUGH 520 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  25.1789 -30.4618  57.0263              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.1597 T22:   0.8055                                     
REMARK   3      T33:   1.2319 T12:  -0.4161                                     
REMARK   3      T13:   0.0315 T23:  -0.2747                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4300 L22:   3.5433                                     
REMARK   3      L33:   3.9610 L12:  -0.0440                                     
REMARK   3      L13:   1.9755 L23:  -3.4463                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.5959 S12:   0.6761 S13:  -0.1536                       
REMARK   3      S21:   0.2243 S22:  -1.4362 S23:   0.2150                       
REMARK   3      S31:   0.6040 S32:  -1.5432 S33:   0.2995                       
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 521 THROUGH 569 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  19.1972 -40.1081  23.9586              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   2.5402 T22:   1.7574                                     
REMARK   3      T33:   1.2458 T12:  -0.4170                                     
REMARK   3      T13:  -1.0995 T23:   1.0905                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1468 L22:   2.3732                                     
REMARK   3      L33:   3.8637 L12:  -1.0466                                     
REMARK   3      L13:  -2.6098 L23:   2.4720                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.5003 S12:  -0.9025 S13:  -0.6108                       
REMARK   3      S21:   1.9475 S22:  -0.4168 S23:  -0.1274                       
REMARK   3      S31:   1.6111 S32:   0.9619 S33:  -2.8514                       
REMARK   3   TLS GROUP : 16                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 570 THROUGH 617 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  33.1790 -33.6885  38.8827              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -1.7083 T22:   3.7251                                     
REMARK   3      T33:   1.0323 T12:  -0.8352                                     
REMARK   3      T13:   0.5162 T23:   0.5978                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.1141 L22:   1.5356                                     
REMARK   3      L33:   4.1136 L12:   0.6386                                     
REMARK   3      L13:   5.7888 L23:   0.9858                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1147 S12:   1.4937 S13:   0.3985                       
REMARK   3      S21:  -1.9075 S22:   0.2166 S23:   0.9522                       
REMARK   3      S31:   0.1119 S32:   0.5260 S33:   0.3207                       
REMARK   3   TLS GROUP : 17                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 618 THROUGH 754 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  29.0209 -36.6101  64.0466              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5330 T22:   0.8378                                     
REMARK   3      T33:   1.0070 T12:   0.4631                                     
REMARK   3      T13:  -0.2446 T23:   0.0497                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.6157 L22:   5.9734                                     
REMARK   3      L33:   3.6909 L12:   0.7285                                     
REMARK   3      L13:   0.1802 L23:  -0.1250                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2880 S12:  -0.3323 S13:  -0.5918                       
REMARK   3      S21:   0.5984 S22:  -0.0610 S23:   0.3933                       
REMARK   3      S31:   0.7601 S32:   1.5502 S33:  -0.4515                       
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 5XAM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 17-MAR-17.                  
REMARK 100 THE DEPOSITION ID IS D_1300003190.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 30-OCT-16                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6                                  
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SPRING-8                           
REMARK 200  BEAMLINE                       : BL32XU                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1                                  
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS EIGER X 9M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL                                
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 17534                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 4.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 36.0                               
REMARK 200  DATA REDUNDANCY                : 2.500                              
REMARK 200  R MERGE                    (I) : 0.15600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 2.9000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 4.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 4.07                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 14.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.10                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.82100                            
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, PHASER                                        
REMARK 200 STARTING MODEL: 3AQP                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 61.62                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.20                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 38% PEG 200, NH4-CITRATE, PH 6,          
REMARK 280  LIPIDIC CUBIC PHASE, TEMPERATURE 298K                               
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,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       31.13000            
REMARK 290   SMTRY3   2  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: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
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: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A    27                                                      
REMARK 465     SER A    28                                                      
REMARK 465     ASN A   227                                                      
REMARK 465     ARG A   228                                                      
REMARK 465     GLN A   542                                                      
REMARK 465     ASN A   759                                                      
REMARK 465     ARG A   760                                                      
REMARK 465     ALA A   761                                                      
REMARK 465     ALA A   762                                                      
REMARK 465     LYS A   763                                                      
REMARK 465     PRO A   764                                                      
REMARK 465     VAL A   765                                                      
REMARK 465     THR A   766                                                      
REMARK 465     ASN A   767                                                      
REMARK 465     SER A   768                                                      
REMARK 465     HIS A   769                                                      
REMARK 465     HIS A   770                                                      
REMARK 465     HIS A   771                                                      
REMARK 465     HIS A   772                                                      
REMARK 465     HIS A   773                                                      
REMARK 465     HIS A   774                                                      
REMARK 465     HIS A   775                                                      
REMARK 465     HIS A   776                                                      
REMARK 465     MET B    27                                                      
REMARK 465     SER B    28                                                      
REMARK 465     ARG B    29                                                      
REMARK 465     PRO B    30                                                      
REMARK 465     THR B    92                                                      
REMARK 465     ARG B    93                                                      
REMARK 465     ASN B   169                                                      
REMARK 465     PRO B   170                                                      
REMARK 465     ARG B   171                                                      
REMARK 465     SER B   172                                                      
REMARK 465     SER B   173                                                      
REMARK 465     GLY B   174                                                      
REMARK 465     TYR B   175                                                      
REMARK 465     THR B   176                                                      
REMARK 465     LEU B   177                                                      
REMARK 465     ALA B   178                                                      
REMARK 465     GLN B   179                                                      
REMARK 465     LEU B   180                                                      
REMARK 465     ALA B   191                                                      
REMARK 465     ASP B   192                                                      
REMARK 465     ALA B   193                                                      
REMARK 465     THR B   194                                                      
REMARK 465     SER B   195                                                      
REMARK 465     GLY B   196                                                      
REMARK 465     THR B   197                                                      
REMARK 465     THR B   243                                                      
REMARK 465     ILE B   244                                                      
REMARK 465     ASN B   245                                                      
REMARK 465     GLN B   246                                                      
REMARK 465     ARG B   247                                                      
REMARK 465     LEU B   248                                                      
REMARK 465     PHE B   249                                                      
REMARK 465     ARG B   250                                                      
REMARK 465     ASP B   251                                                      
REMARK 465     ILE B   252                                                      
REMARK 465     GLN B   253                                                      
REMARK 465     ILE B   254                                                      
REMARK 465     SER B   255                                                      
REMARK 465     GLY B   256                                                      
REMARK 465     ILE B   541                                                      
REMARK 465     GLN B   542                                                      
REMARK 465     ARG B   543                                                      
REMARK 465     ASP B   544                                                      
REMARK 465     THR B   545                                                      
REMARK 465     TRP B   755                                                      
REMARK 465     ARG B   756                                                      
REMARK 465     ASP B   757                                                      
REMARK 465     LYS B   758                                                      
REMARK 465     ASN B   759                                                      
REMARK 465     ARG B   760                                                      
REMARK 465     ALA B   761                                                      
REMARK 465     ALA B   762                                                      
REMARK 465     LYS B   763                                                      
REMARK 465     PRO B   764                                                      
REMARK 465     VAL B   765                                                      
REMARK 465     THR B   766                                                      
REMARK 465     ASN B   767                                                      
REMARK 465     SER B   768                                                      
REMARK 465     HIS B   769                                                      
REMARK 465     HIS B   770                                                      
REMARK 465     HIS B   771                                                      
REMARK 465     HIS B   772                                                      
REMARK 465     HIS B   773                                                      
REMARK 465     HIS B   774                                                      
REMARK 465     HIS B   775                                                      
REMARK 465     HIS B   776                                                      
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     ARG A  29    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     TRP A  50    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP A  50    CZ3  CH2                                            
REMARK 470     ARG A  51    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A  56    CG   CD   CE   NZ                                   
REMARK 470     TRP A  60    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP A  60    CZ3  CH2                                            
REMARK 470     TRP A  63    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP A  63    CZ3  CH2                                            
REMARK 470     TYR A  67    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     MET A  70    CG   SD   CE                                        
REMARK 470     ASP A  75    CG   OD1  OD2                                       
REMARK 470     LYS A  77    CG   CD   CE   NZ                                   
REMARK 470     ARG A  81    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A  83    CG   CD   OE1  OE2                                  
REMARK 470     GLU A  87    CG   CD   OE1  OE2                                  
REMARK 470     ARG A  93    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A  95    CG   CD   OE1  OE2                                  
REMARK 470     ARG A  98    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 100    CG   CD   CE   NZ                                   
REMARK 470     ARG A 106    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 114    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 123    CG   CD   CE   NZ                                   
REMARK 470     ARG A 124    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 128    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 141    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN A 145    CG   CD   OE1  NE2                                  
REMARK 470     ARG A 149    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 151    CG   CD   OE1  OE2                                  
REMARK 470     PHE A 152    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ARG A 153    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 160    CG   CD   CE   NZ                                   
REMARK 470     ASP A 162    CG   OD1  OD2                                       
REMARK 470     ARG A 166    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 167    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 168    CG   CD   CE   NZ                                   
REMARK 470     ARG A 171    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     TYR A 175    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     GLN A 179    CG   CD   OE1  NE2                                  
REMARK 470     GLU A 188    CG   CD   OE1  OE2                                  
REMARK 470     GLN A 199    CG   CD   OE1  NE2                                  
REMARK 470     GLN A 203    CG   CD   OE1  NE2                                  
REMARK 470     PHE A 208    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LYS A 209    CG   CD   CE   NZ                                   
REMARK 470     LYS A 216    CG   CD   CE   NZ                                   
REMARK 470     PHE A 218    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     PHE A 221    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LYS A 224    CG   CD   CE   NZ                                   
REMARK 470     MET A 230    CG   SD   CE                                        
REMARK 470     GLN A 237    CG   CD   OE1  NE2                                  
REMARK 470     GLN A 239    CG   CD   OE1  NE2                                  
REMARK 470     ASN A 245    CG   OD1  ND2                                       
REMARK 470     GLN A 246    CG   CD   OE1  NE2                                  
REMARK 470     ARG A 247    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     PHE A 249    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ARG A 250    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP A 251    CG   OD1  OD2                                       
REMARK 470     GLN A 253    CG   CD   OE1  NE2                                  
REMARK 470     PHE A 258    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     GLU A 261    CG   CD   OE1  OE2                                  
REMARK 470     GLN A 265    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 271    CG   CD   CE   NZ                                   
REMARK 470     LYS A 278    CG   CD   CE   NZ                                   
REMARK 470     ARG A 285    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     PHE A 311    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     MET A 313    CG   SD   CE                                        
REMARK 470     TYR A 317    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     TRP A 321    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP A 321    CZ3  CH2                                            
REMARK 470     PHE A 322    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ARG A 373    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 382    CG   CD   CE   NZ                                   
REMARK 470     PHE A 424    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ASN A 456    CG   OD1  ND2                                       
REMARK 470     MET A 457    CG   SD   CE                                        
REMARK 470     GLN A 461    CG   CD   OE1  NE2                                  
REMARK 470     TRP A 462    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP A 462    CZ3  CH2                                            
REMARK 470     LYS A 464    CG   CD   CE   NZ                                   
REMARK 470     HIS A 465    CG   ND1  CD2  CE1  NE2                             
REMARK 470     HIS A 467    CG   ND1  CD2  CE1  NE2                             
REMARK 470     ASP A 469    CG   OD1  OD2                                       
REMARK 470     PHE A 470    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LYS A 475    CG   CD   CE   NZ                                   
REMARK 470     ASP A 514    CG   OD1  OD2                                       
REMARK 470     GLU A 520    CG   CD   OE1  OE2                                  
REMARK 470     GLN A 521    CG   CD   OE1  NE2                                  
REMARK 470     ARG A 523    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASN A 524    CG   OD1  ND2                                       
REMARK 470     LYS A 533    CG   CD   CE   NZ                                   
REMARK 470     GLN A 537    CG   CD   OE1  NE2                                  
REMARK 470     ARG A 543    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP A 544    CG   OD1  OD2                                       
REMARK 470     GLN A 549    CG   CD   OE1  NE2                                  
REMARK 470     GLN A 550    CG   CD   OE1  NE2                                  
REMARK 470     GLN A 552    CG   CD   OE1  NE2                                  
REMARK 470     ASN A 553    CG   OD1  ND2                                       
REMARK 470     PHE A 554    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LYS A 557    CG   CD   CE   NZ                                   
REMARK 470     GLU A 560    CG   CD   OE1  OE2                                  
REMARK 470     GLN A 580    CG   CD   OE1  NE2                                  
REMARK 470     GLU A 585    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 598    CG   CD   CE   NZ                                   
REMARK 470     TYR A 686    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ARG A 687    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 700    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     TRP B  63    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP B  63    CZ3  CH2                                            
REMARK 470     TYR B  67    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     GLN B  68    CG   CD   OE1  NE2                                  
REMARK 470     PHE B  69    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ARG B  81    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B  83    CG   CD   OE1  OE2                                  
REMARK 470     GLU B  95    CG   CD   OE1  OE2                                  
REMARK 470     ARG B  98    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B 106    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B 124    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B 139    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B 141    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN B 145    CG   CD   OE1  NE2                                  
REMARK 470     GLN B 146    CG   CD   OE1  NE2                                  
REMARK 470     ARG B 149    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B 151    CG   CD   OE1  OE2                                  
REMARK 470     PHE B 152    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ARG B 153    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASN B 156    CG   OD1  ND2                                       
REMARK 470     ASP B 158    CG   OD1  OD2                                       
REMARK 470     LYS B 160    CG   CD   CE   NZ                                   
REMARK 470     ASP B 162    CG   OD1  OD2                                       
REMARK 470     ARG B 166    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B 167    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 168    CG   CD   CE   NZ                                   
REMARK 470     GLU B 188    CG   CD   OE1  OE2                                  
REMARK 470     ASP B 198    CG   OD1  OD2                                       
REMARK 470     GLN B 199    CG   CD   OE1  NE2                                  
REMARK 470     ARG B 200    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN B 203    CG   CD   OE1  NE2                                  
REMARK 470     TRP B 204    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP B 204    CZ3  CH2                                            
REMARK 470     ASN B 207    CG   OD1  ND2                                       
REMARK 470     PHE B 208    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LYS B 209    CG   CD   CE   NZ                                   
REMARK 470     ASP B 212    CG   OD1  OD2                                       
REMARK 470     LYS B 216    CG   CD   CE   NZ                                   
REMARK 470     PHE B 218    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ASP B 220    CG   OD1  OD2                                       
REMARK 470     PHE B 221    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LYS B 224    CG   CD   CE   NZ                                   
REMARK 470     ASN B 227    CG   OD1  ND2                                       
REMARK 470     ARG B 228    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     MET B 230    CG   SD   CE                                        
REMARK 470     ASP B 236    CG   OD1  OD2                                       
REMARK 470     GLN B 237    CG   CD   OE1  NE2                                  
REMARK 470     GLN B 239    CG   CD   OE1  NE2                                  
REMARK 470     ASN B 257    CG   OD1  ND2                                       
REMARK 470     PHE B 258    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     GLU B 261    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 262    CG   CD   OE1  OE2                                  
REMARK 470     GLN B 265    CG   CD   OE1  NE2                                  
REMARK 470     LYS B 271    CG   CD   CE   NZ                                   
REMARK 470     ARG B 285    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     TYR B 318    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ARG B 380    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 382    CG   CD   CE   NZ                                   
REMARK 470     HIS B 406    CG   ND1  CD2  CE1  NE2                             
REMARK 470     PHE B 424    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ARG B 453    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     TYR B 499    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ARG B 617    CG   CD   NE   CZ   NH1  NH2                        
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   OD1  ASP B   401     OH   TYR B   613              2.13            
REMARK 500   O    VAL A   368     N    GLU A   372              2.13            
REMARK 500   OD1  ASP A   666     OG   SER A   741              2.14            
REMARK 500   O    THR A   396     N    LEU A   400              2.16            
REMARK 500   OG1  THR A   186     OG1  THR A   189              2.17            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    ARG A  51   C     PRO A  52   N       0.139                       
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    TRP A  60      -63.59   -124.12                                   
REMARK 500    TRP A  63       70.53   -152.59                                   
REMARK 500    GLU A  87      -71.92    -56.43                                   
REMARK 500    GLU A 114       72.86     57.48                                   
REMARK 500    ALA A 148       69.26     61.22                                   
REMARK 500    ARG A 166      -56.24   -137.74                                   
REMARK 500    SER A 173       61.30     61.33                                   
REMARK 500    LEU A 180       70.45     55.36                                   
REMARK 500    VAL A 184      -72.00   -126.97                                   
REMARK 500    PHE A 344      -71.16    -71.87                                   
REMARK 500    THR A 396      -70.06    -45.37                                   
REMARK 500    THR A 418     -175.58    -68.77                                   
REMARK 500    PHE A 446      -73.96    -49.20                                   
REMARK 500    PRO A 473       21.45    -72.92                                   
REMARK 500    LEU A 480      -72.06    -66.42                                   
REMARK 500    LEU A 483       10.43    -68.82                                   
REMARK 500    ARG A 512       23.87   -149.29                                   
REMARK 500    PRO A 559      172.00    -59.89                                   
REMARK 500    ASN A 562     -178.16    -69.85                                   
REMARK 500    GLN A 578        9.03     96.66                                   
REMARK 500    GLU A 585      125.10   -173.86                                   
REMARK 500    ARG A 617       51.99   -142.06                                   
REMARK 500    ASN A 677       37.87    -79.81                                   
REMARK 500    SER A 699      -70.61    -87.03                                   
REMARK 500    PRO A 721      -70.46    -67.61                                   
REMARK 500    LEU A 728      -73.28    -65.64                                   
REMARK 500    ALA B 109        5.67    -68.16                                   
REMARK 500    GLU B 114       68.06     66.98                                   
REMARK 500    ALA B 148       40.09   -108.38                                   
REMARK 500    GLU B 151      110.62   -168.13                                   
REMARK 500    ARG B 153      135.16    175.58                                   
REMARK 500    SER B 157       31.77   -141.19                                   
REMARK 500    LEU B 229       78.75     59.82                                   
REMARK 500    ASP B 235       48.08     34.85                                   
REMARK 500    TYR B 416       29.30   -147.13                                   
REMARK 500    ALA B 420      -84.15    -73.53                                   
REMARK 500    TRP B 445      -74.21    -68.33                                   
REMARK 500    ASN B 498     -128.75     61.38                                   
REMARK 500    TYR B 499     -149.88     70.76                                   
REMARK 500    VAL B 501       29.94     47.21                                   
REMARK 500    ASP B 502      -73.68   -145.58                                   
REMARK 500    PRO B 559     -168.46    -71.38                                   
REMARK 500    LEU B 561      149.03   -174.12                                   
REMARK 500    LEU B 582      -34.43   -141.73                                   
REMARK 500    LEU B 723      -75.15    -65.73                                   
REMARK 500    ARG B 724       27.96    -73.89                                   
REMARK 500    ILE B 744      -57.30   -132.42                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3AQP   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5XAN   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5XAP   RELATED DB: PDB                                   
DBREF  5XAM A   28   768  UNP    Q9RTE3   Q9RTE3_DEIRA    28    768             
DBREF  5XAM B   28   768  UNP    Q9RTE3   Q9RTE3_DEIRA    28    768             
SEQADV 5XAM MET A   27  UNP  Q9RTE3              EXPRESSION TAG                 
SEQADV 5XAM HIS A  769  UNP  Q9RTE3              EXPRESSION TAG                 
SEQADV 5XAM HIS A  770  UNP  Q9RTE3              EXPRESSION TAG                 
SEQADV 5XAM HIS A  771  UNP  Q9RTE3              EXPRESSION TAG                 
SEQADV 5XAM HIS A  772  UNP  Q9RTE3              EXPRESSION TAG                 
SEQADV 5XAM HIS A  773  UNP  Q9RTE3              EXPRESSION TAG                 
SEQADV 5XAM HIS A  774  UNP  Q9RTE3              EXPRESSION TAG                 
SEQADV 5XAM HIS A  775  UNP  Q9RTE3              EXPRESSION TAG                 
SEQADV 5XAM HIS A  776  UNP  Q9RTE3              EXPRESSION TAG                 
SEQADV 5XAM MET B   27  UNP  Q9RTE3              EXPRESSION TAG                 
SEQADV 5XAM HIS B  769  UNP  Q9RTE3              EXPRESSION TAG                 
SEQADV 5XAM HIS B  770  UNP  Q9RTE3              EXPRESSION TAG                 
SEQADV 5XAM HIS B  771  UNP  Q9RTE3              EXPRESSION TAG                 
SEQADV 5XAM HIS B  772  UNP  Q9RTE3              EXPRESSION TAG                 
SEQADV 5XAM HIS B  773  UNP  Q9RTE3              EXPRESSION TAG                 
SEQADV 5XAM HIS B  774  UNP  Q9RTE3              EXPRESSION TAG                 
SEQADV 5XAM HIS B  775  UNP  Q9RTE3              EXPRESSION TAG                 
SEQADV 5XAM HIS B  776  UNP  Q9RTE3              EXPRESSION TAG                 
SEQRES   1 A  750  MET SER ARG PRO ASN PRO TRP THR ALA LEU LEU LEU LEU          
SEQRES   2 A  750  LEU THR LEU LEU GLY SER LEU LEU TYR ILE TRP ARG PRO          
SEQRES   3 A  750  TRP GLU HIS LYS ASN ASP PRO TRP SER LEU TRP ASN ASP          
SEQRES   4 A  750  GLN TYR GLN PHE MET THR LEU GLY LEU ASP LEU LYS GLY          
SEQRES   5 A  750  GLY LEU ARG ILE GLU LEU ALA PRO GLU SER GLY THR ALA          
SEQRES   6 A  750  THR ARG ASP GLU LEU ASP ARG VAL LYS THR VAL ILE GLU          
SEQRES   7 A  750  ASN ARG ILE ASN ALA LEU GLY VAL ALA GLU PRO THR VAL          
SEQRES   8 A  750  THR VAL SER GLY GLY LYS ARG VAL VAL VAL GLU ILE PRO          
SEQRES   9 A  750  GLY ALA THR PRO ALA VAL GLN ASP ARG ALA ARG SER ILE          
SEQRES  10 A  750  ILE GLN GLN THR ALA ARG LEU GLU PHE ARG ILE VAL ASN          
SEQRES  11 A  750  SER ASP ALA LYS PRO ASP PRO ALA VAL ARG GLU LYS ASN          
SEQRES  12 A  750  PRO ARG SER SER GLY TYR THR LEU ALA GLN LEU GLY PRO          
SEQRES  13 A  750  VAL VAL ALA THR GLY GLU THR ILE ALA ASP ALA THR SER          
SEQRES  14 A  750  GLY THR ASP GLN ARG SER GLY GLN TRP VAL VAL ASN PHE          
SEQRES  15 A  750  LYS THR THR ASP ALA GLY ALA LYS THR PHE GLY ASP PHE          
SEQRES  16 A  750  THR GLY LYS ASN VAL ASN ARG LEU MET ALA VAL VAL LEU          
SEQRES  17 A  750  ASP ASP GLN ILE GLN SER VAL ALA THR ILE ASN GLN ARG          
SEQRES  18 A  750  LEU PHE ARG ASP ILE GLN ILE SER GLY ASN PHE THR PRO          
SEQRES  19 A  750  GLU GLU ALA SER GLN LEU ALA LEU VAL LEU LYS SER GLY          
SEQRES  20 A  750  ALA LEU PRO ILE LYS ILE VAL THR ALA ALA GLU ARG SER          
SEQRES  21 A  750  ILE GLY PRO SER LEU GLY ALA ASP ALA ILE ARG SER GLY          
SEQRES  22 A  750  ALA ILE ALA ALA LEU VAL GLY ILE GLY LEU VAL PHE VAL          
SEQRES  23 A  750  MET LEU PHE ALA TYR TYR GLY LEU TRP PHE GLY LEU VAL          
SEQRES  24 A  750  GLY ALA LEU GLY LEU LEU PHE SER SER ILE ILE ILE LEU          
SEQRES  25 A  750  GLY ILE LEU GLY GLY PHE GLY ALA THR LEU THR LEU PRO          
SEQRES  26 A  750  GLY ILE ALA GLY LEU VAL LEU THR ILE GLY ALA ALA VAL          
SEQRES  27 A  750  ASP GLY ASN VAL ILE SER PHE GLU ARG ILE LYS GLU GLU          
SEQRES  28 A  750  LEU ALA ARG GLY LYS GLY ILE LYS ASN ALA ILE GLY ALA          
SEQRES  29 A  750  GLY TYR GLU HIS SER THR ALA ALA ILE LEU ASP VAL ASN          
SEQRES  30 A  750  ALA SER HIS LEU LEU SER ALA LEU ALA LEU TYR ASN TYR          
SEQRES  31 A  750  SER THR GLY ALA VAL LYS GLY PHE ALA VAL THR LEU ILE          
SEQRES  32 A  750  ILE GLY VAL ILE ALA SER THR PHE SER ASN LEU VAL PHE          
SEQRES  33 A  750  ALA LYS TRP PHE MET GLN TRP LEU ALA GLN ARG ARG PRO          
SEQRES  34 A  750  ASN MET SER ALA PRO GLN TRP ILE LYS HIS THR HIS PHE          
SEQRES  35 A  750  ASP PHE MET LYS PRO ALA LYS VAL ILE THR THR LEU SER          
SEQRES  36 A  750  VAL LEU LEU ALA LEU ALA GLY ALA ALA LEU VAL ALA THR          
SEQRES  37 A  750  ARG GLY LEU ASN TYR GLY VAL ASP PHE ALA PRO GLY THR          
SEQRES  38 A  750  THR LEU THR ALA ARG VAL ASP ARG GLN VAL THR THR GLU          
SEQRES  39 A  750  GLN LEU ARG ASN SER VAL ILE GLY ALA GLY VAL SER LYS          
SEQRES  40 A  750  VAL THR GLY GLN SER ALA THR ILE GLN ARG ASP THR THR          
SEQRES  41 A  750  PRO GLY GLN GLN GLY GLN ASN PHE THR VAL LYS VAL PRO          
SEQRES  42 A  750  GLU LEU ASN ASP ALA GLU VAL LYS GLN ILE GLY ALA ALA          
SEQRES  43 A  750  ILE GLY LYS LEU PRO GLN GLY GLN VAL LEU ALA SER GLU          
SEQRES  44 A  750  THR VAL GLY PRO ALA VAL GLY LYS GLU LEU THR GLN LYS          
SEQRES  45 A  750  THR ILE TYR ALA VAL LEU LEU GLY LEU GLY LEU ILE LEU          
SEQRES  46 A  750  VAL TYR VAL GLY PHE ARG PHE ASP PHE ILE MET GLY LEU          
SEQRES  47 A  750  GLY SER ILE ILE ALA ALA ILE HIS ASP VAL ALA ILE ALA          
SEQRES  48 A  750  MET GLY LEU PHE SER LEU LEU GLY LEU GLU PHE THR VAL          
SEQRES  49 A  750  ALA SER VAL ALA ALA LEU LEU THR LEU ILE GLY TYR SER          
SEQRES  50 A  750  LEU ASN ASP SER ILE ILE VAL SER ASP ARG ILE ARG GLU          
SEQRES  51 A  750  ASN MET LYS THR MET ARG GLY HIS SER TYR ARG GLU ILE          
SEQRES  52 A  750  VAL ASN ALA ALA ILE ASN GLN THR LEU SER ARG THR VAL          
SEQRES  53 A  750  MET THR SER VAL SER THR MET LEU PRO LEU ILE SER LEU          
SEQRES  54 A  750  LEU ILE PHE GLY GLY PRO VAL LEU ARG ASP PHE SER LEU          
SEQRES  55 A  750  ILE LEU LEU VAL GLY ILE LEU VAL GLY THR TYR SER SER          
SEQRES  56 A  750  ILE TYR ILE VAL ALA PRO LEU VAL VAL TYR PHE GLU GLU          
SEQRES  57 A  750  TRP ARG ASP LYS ASN ARG ALA ALA LYS PRO VAL THR ASN          
SEQRES  58 A  750  SER HIS HIS HIS HIS HIS HIS HIS HIS                          
SEQRES   1 B  750  MET SER ARG PRO ASN PRO TRP THR ALA LEU LEU LEU LEU          
SEQRES   2 B  750  LEU THR LEU LEU GLY SER LEU LEU TYR ILE TRP ARG PRO          
SEQRES   3 B  750  TRP GLU HIS LYS ASN ASP PRO TRP SER LEU TRP ASN ASP          
SEQRES   4 B  750  GLN TYR GLN PHE MET THR LEU GLY LEU ASP LEU LYS GLY          
SEQRES   5 B  750  GLY LEU ARG ILE GLU LEU ALA PRO GLU SER GLY THR ALA          
SEQRES   6 B  750  THR ARG ASP GLU LEU ASP ARG VAL LYS THR VAL ILE GLU          
SEQRES   7 B  750  ASN ARG ILE ASN ALA LEU GLY VAL ALA GLU PRO THR VAL          
SEQRES   8 B  750  THR VAL SER GLY GLY LYS ARG VAL VAL VAL GLU ILE PRO          
SEQRES   9 B  750  GLY ALA THR PRO ALA VAL GLN ASP ARG ALA ARG SER ILE          
SEQRES  10 B  750  ILE GLN GLN THR ALA ARG LEU GLU PHE ARG ILE VAL ASN          
SEQRES  11 B  750  SER ASP ALA LYS PRO ASP PRO ALA VAL ARG GLU LYS ASN          
SEQRES  12 B  750  PRO ARG SER SER GLY TYR THR LEU ALA GLN LEU GLY PRO          
SEQRES  13 B  750  VAL VAL ALA THR GLY GLU THR ILE ALA ASP ALA THR SER          
SEQRES  14 B  750  GLY THR ASP GLN ARG SER GLY GLN TRP VAL VAL ASN PHE          
SEQRES  15 B  750  LYS THR THR ASP ALA GLY ALA LYS THR PHE GLY ASP PHE          
SEQRES  16 B  750  THR GLY LYS ASN VAL ASN ARG LEU MET ALA VAL VAL LEU          
SEQRES  17 B  750  ASP ASP GLN ILE GLN SER VAL ALA THR ILE ASN GLN ARG          
SEQRES  18 B  750  LEU PHE ARG ASP ILE GLN ILE SER GLY ASN PHE THR PRO          
SEQRES  19 B  750  GLU GLU ALA SER GLN LEU ALA LEU VAL LEU LYS SER GLY          
SEQRES  20 B  750  ALA LEU PRO ILE LYS ILE VAL THR ALA ALA GLU ARG SER          
SEQRES  21 B  750  ILE GLY PRO SER LEU GLY ALA ASP ALA ILE ARG SER GLY          
SEQRES  22 B  750  ALA ILE ALA ALA LEU VAL GLY ILE GLY LEU VAL PHE VAL          
SEQRES  23 B  750  MET LEU PHE ALA TYR TYR GLY LEU TRP PHE GLY LEU VAL          
SEQRES  24 B  750  GLY ALA LEU GLY LEU LEU PHE SER SER ILE ILE ILE LEU          
SEQRES  25 B  750  GLY ILE LEU GLY GLY PHE GLY ALA THR LEU THR LEU PRO          
SEQRES  26 B  750  GLY ILE ALA GLY LEU VAL LEU THR ILE GLY ALA ALA VAL          
SEQRES  27 B  750  ASP GLY ASN VAL ILE SER PHE GLU ARG ILE LYS GLU GLU          
SEQRES  28 B  750  LEU ALA ARG GLY LYS GLY ILE LYS ASN ALA ILE GLY ALA          
SEQRES  29 B  750  GLY TYR GLU HIS SER THR ALA ALA ILE LEU ASP VAL ASN          
SEQRES  30 B  750  ALA SER HIS LEU LEU SER ALA LEU ALA LEU TYR ASN TYR          
SEQRES  31 B  750  SER THR GLY ALA VAL LYS GLY PHE ALA VAL THR LEU ILE          
SEQRES  32 B  750  ILE GLY VAL ILE ALA SER THR PHE SER ASN LEU VAL PHE          
SEQRES  33 B  750  ALA LYS TRP PHE MET GLN TRP LEU ALA GLN ARG ARG PRO          
SEQRES  34 B  750  ASN MET SER ALA PRO GLN TRP ILE LYS HIS THR HIS PHE          
SEQRES  35 B  750  ASP PHE MET LYS PRO ALA LYS VAL ILE THR THR LEU SER          
SEQRES  36 B  750  VAL LEU LEU ALA LEU ALA GLY ALA ALA LEU VAL ALA THR          
SEQRES  37 B  750  ARG GLY LEU ASN TYR GLY VAL ASP PHE ALA PRO GLY THR          
SEQRES  38 B  750  THR LEU THR ALA ARG VAL ASP ARG GLN VAL THR THR GLU          
SEQRES  39 B  750  GLN LEU ARG ASN SER VAL ILE GLY ALA GLY VAL SER LYS          
SEQRES  40 B  750  VAL THR GLY GLN SER ALA THR ILE GLN ARG ASP THR THR          
SEQRES  41 B  750  PRO GLY GLN GLN GLY GLN ASN PHE THR VAL LYS VAL PRO          
SEQRES  42 B  750  GLU LEU ASN ASP ALA GLU VAL LYS GLN ILE GLY ALA ALA          
SEQRES  43 B  750  ILE GLY LYS LEU PRO GLN GLY GLN VAL LEU ALA SER GLU          
SEQRES  44 B  750  THR VAL GLY PRO ALA VAL GLY LYS GLU LEU THR GLN LYS          
SEQRES  45 B  750  THR ILE TYR ALA VAL LEU LEU GLY LEU GLY LEU ILE LEU          
SEQRES  46 B  750  VAL TYR VAL GLY PHE ARG PHE ASP PHE ILE MET GLY LEU          
SEQRES  47 B  750  GLY SER ILE ILE ALA ALA ILE HIS ASP VAL ALA ILE ALA          
SEQRES  48 B  750  MET GLY LEU PHE SER LEU LEU GLY LEU GLU PHE THR VAL          
SEQRES  49 B  750  ALA SER VAL ALA ALA LEU LEU THR LEU ILE GLY TYR SER          
SEQRES  50 B  750  LEU ASN ASP SER ILE ILE VAL SER ASP ARG ILE ARG GLU          
SEQRES  51 B  750  ASN MET LYS THR MET ARG GLY HIS SER TYR ARG GLU ILE          
SEQRES  52 B  750  VAL ASN ALA ALA ILE ASN GLN THR LEU SER ARG THR VAL          
SEQRES  53 B  750  MET THR SER VAL SER THR MET LEU PRO LEU ILE SER LEU          
SEQRES  54 B  750  LEU ILE PHE GLY GLY PRO VAL LEU ARG ASP PHE SER LEU          
SEQRES  55 B  750  ILE LEU LEU VAL GLY ILE LEU VAL GLY THR TYR SER SER          
SEQRES  56 B  750  ILE TYR ILE VAL ALA PRO LEU VAL VAL TYR PHE GLU GLU          
SEQRES  57 B  750  TRP ARG ASP LYS ASN ARG ALA ALA LYS PRO VAL THR ASN          
SEQRES  58 B  750  SER HIS HIS HIS HIS HIS HIS HIS HIS                          
HELIX    1 AA1 ASN A   31  TRP A   50  1                                  20    
HELIX    2 AA2 THR A   92  GLY A  111  1                                  20    
HELIX    3 AA3 THR A  133  GLN A  145  1                                  13    
HELIX    4 AA4 THR A  211  GLY A  223  1                                  13    
HELIX    5 AA5 THR A  259  LYS A  271  1                                  13    
HELIX    6 AA6 GLY A  288  TYR A  318  1                                  31    
HELIX    7 AA7 GLY A  319  PHE A  344  1                                  26    
HELIX    8 AA8 PRO A  351  GLY A  381  1                                  31    
HELIX    9 AA9 GLY A  383  ALA A  412  1                                  30    
HELIX   10 AB1 THR A  418  SER A  438  1                                  21    
HELIX   11 AB2 VAL A  441  ARG A  453  1                                  13    
HELIX   12 AB3 PRO A  473  THR A  494  1                                  22    
HELIX   13 AB4 THR A  519  GLY A  528  1                                  10    
HELIX   14 AB5 ASN A  562  GLY A  570  1                                   9    
HELIX   15 AB6 GLY A  570  LYS A  575  1                                   6    
HELIX   16 AB7 GLY A  588  VAL A  614  1                                  27    
HELIX   17 AB8 ASP A  619  GLY A  645  1                                  27    
HELIX   18 AB9 THR A  649  ARG A  675  1                                  27    
HELIX   19 AC1 GLU A  676  LYS A  679  5                                   4    
HELIX   20 AC2 ILE A  689  PHE A  718  1                                  30    
HELIX   21 AC3 GLY A  720  LYS A  758  1                                  39    
HELIX   22 AC4 TRP B   33  TRP B   50  1                                  18    
HELIX   23 AC5 GLU B   95  ILE B  107  1                                  13    
HELIX   24 AC6 THR B  133  GLN B  145  1                                  13    
HELIX   25 AC7 ALA B  213  PHE B  221  1                                   9    
HELIX   26 AC8 THR B  259  LYS B  271  1                                  13    
HELIX   27 AC9 GLY B  288  VAL B  305  1                                  18    
HELIX   28 AD1 LEU B  309  TYR B  317  1                                   9    
HELIX   29 AD2 PHE B  322  GLY B  343  1                                  22    
HELIX   30 AD3 THR B  349  GLU B  376  1                                  28    
HELIX   31 AD4 GLU B  377  ALA B  379  5                                   3    
HELIX   32 AD5 ILE B  384  SER B  409  1                                  26    
HELIX   33 AD6 ALA B  410  ASN B  415  1                                   6    
HELIX   34 AD7 ALA B  420  VAL B  441  1                                  22    
HELIX   35 AD8 VAL B  441  ARG B  454  1                                  14    
HELIX   36 AD9 PRO B  473  GLY B  496  1                                  24    
HELIX   37 AE1 GLU B  520  GLY B  528  1                                   9    
HELIX   38 AE2 GLU B  565  GLY B  570  1                                   6    
HELIX   39 AE3 ALA B  572  LEU B  576  5                                   5    
HELIX   40 AE4 GLY B  588  PHE B  618  1                                  31    
HELIX   41 AE5 ASP B  619  GLY B  645  1                                  27    
HELIX   42 AE6 THR B  649  LEU B  664  1                                  16    
HELIX   43 AE7 LEU B  664  MET B  681  1                                  18    
HELIX   44 AE8 ARG B  687  GLN B  696  1                                  10    
HELIX   45 AE9 GLN B  696  SER B  714  1                                  19    
HELIX   46 AF1 VAL B  722  ILE B  742  1                                  21    
HELIX   47 AF2 ILE B  744  GLU B  754  1                                  11    
SHEET    1 AA1 2 ALA A  85  PRO A  86  0                                        
SHEET    2 AA1 2 ILE A 279  VAL A 280 -1  O  VAL A 280   N  ALA A  85           
SHEET    1 AA2 2 THR A 116  SER A 120  0                                        
SHEET    2 AA2 2 ARG A 124  GLU A 128 -1  O  VAL A 126   N  THR A 118           
SHEET    1 AA3 3 ARG A 153  ILE A 154  0                                        
SHEET    2 AA3 3 MET A 230  LEU A 234 -1  O  ALA A 231   N  ARG A 153           
SHEET    3 AA3 3 GLN A 237  ALA A 242 -1  O  GLN A 237   N  LEU A 234           
SHEET    1 AA4 2 ALA A 193  THR A 194  0                                        
SHEET    2 AA4 2 ASN A 207  PHE A 208 -1  O  ASN A 207   N  THR A 194           
SHEET    1 AA5 3 PHE A 554  THR A 555  0                                        
SHEET    2 AA5 3 THR A 508  ALA A 511 -1  N  ALA A 511   O  PHE A 554           
SHEET    3 AA5 3 SER A 584  GLU A 585 -1  O  GLU A 585   N  THR A 508           
SHEET    1 AA6 6 VAL B 125  GLU B 128  0                                        
SHEET    2 AA6 6 ARG B  81  PRO B  86 -1  N  ILE B  82   O  VAL B 127           
SHEET    3 AA6 6 ILE B 279  SER B 286 -1  O  ALA B 283   N  GLU B  83           
SHEET    4 AA6 6 GLN B 580  GLU B 585 -1  O  SER B 584   N  SER B 286           
SHEET    5 AA6 6 THR B 507  VAL B 513 -1  N  ARG B 512   O  GLN B 580           
SHEET    6 AA6 6 GLN B 552  VAL B 558 -1  O  GLN B 552   N  VAL B 513           
SHEET    1 AA7 2 VAL B 232  VAL B 233  0                                        
SHEET    2 AA7 2 ILE B 238  GLN B 239 -1  O  GLN B 239   N  VAL B 232           
CRYST1   93.320   62.260  181.710  90.00 101.71  90.00 P 1 21 1      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      0.010716  0.000000  0.002221        0.00000                         
SCALE2      0.000000  0.016062  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005620        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system