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Database: PDB
Entry: 4QU4
LinkDB: 4QU4
Original site: 4QU4 
HEADER    HYDROLASE                               10-JUL-14   4QU4              
TITLE     IMPROVED REFINEMENT OF THE MTR4 APO CRYSTAL STRUCTURE                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ATP-DEPENDENT RNA HELICASE DOB1;                           
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: MRNA TRANSPORT REGULATOR MTR4;                              
COMPND   5 EC: 3.6.4.13;                                                        
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;                       
SOURCE   3 ORGANISM_COMMON: BAKER'S YEAST;                                      
SOURCE   4 ORGANISM_TAXID: 4932;                                                
SOURCE   5 GENE: DOB1, J1158, MTR4, MTR4/YJL050W, YJL050W;                      
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21-CODONPLUS(DE3)-RIL;                   
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET151 DIRECTIONAL TOPO                   
KEYWDS    REC-A FOLD, WINGED-HELIX-TURN-HELIX, ANTIPARALLEL-COILED-COIL, DSHCT  
KEYWDS   2 DOMAIN, HELICASE, NUCLEOTIDE BINDING, PHOSPHOPROTEIN, RRNA           
KEYWDS   3 PROCESSING, TRAMP, ATP BINDING, NUCLEUS, HYDROLASE                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.J.JOHNSON,L.L.TAYLOR                                                
REVDAT   3   28-FEB-24 4QU4    1       REMARK SEQADV                            
REVDAT   2   14-JAN-15 4QU4    1       JRNL                                     
REVDAT   1   03-DEC-14 4QU4    0                                                
SPRSDE     03-DEC-14 4QU4      3L9O                                             
JRNL        AUTH   L.L.TAYLOR,R.N.JACKSON,M.REXHEPAJ,A.K.KING,L.K.LOTT,         
JRNL        AUTH 2 A.VAN HOOF,S.J.JOHNSON                                       
JRNL        TITL   THE MTR4 RATCHET HELIX AND ARCH DOMAIN BOTH FUNCTION TO      
JRNL        TITL 2 PROMOTE RNA UNWINDING.                                       
JRNL        REF    NUCLEIC ACIDS RES.            V.  42 13861 2014              
JRNL        REFN                   ISSN 0305-1048                               
JRNL        PMID   25414331                                                     
JRNL        DOI    10.1093/NAR/GKU1208                                          
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   R.N.JACKSON,A.A.KLAUER,B.J.HINTZE,H.ROBINSON,A.VAN HOOF,     
REMARK   1  AUTH 2 S.J.JOHNSON                                                  
REMARK   1  TITL   THE CRYSTAL STRUCTURE OF MTR4 REVEALS A NOVEL ARCH DOMAIN    
REMARK   1  TITL 2 REQUIRED FOR RRNA PROCESSING.                                
REMARK   1  REF    EMBO J.                       V.  29  2205 2010              
REMARK   1  REFN                   ISSN 0261-4189                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.39 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.9_1692)                     
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) : 3.39                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 28.76                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 93.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 26095                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.250                           
REMARK   3   R VALUE            (WORKING SET) : 0.248                           
REMARK   3   FREE R VALUE                     : 0.299                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.860                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1268                            
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 28.7583 -  7.0255    1.00     3068   173  0.1983 0.2499        
REMARK   3     2  7.0255 -  5.5898    1.00     2973   155  0.3124 0.3368        
REMARK   3     3  5.5898 -  4.8871    1.00     2951   143  0.2519 0.3305        
REMARK   3     4  4.8871 -  4.4420    1.00     2913   149  0.2219 0.2987        
REMARK   3     5  4.4420 -  4.1246    1.00     2943   138  0.2485 0.3043        
REMARK   3     6  4.1246 -  3.8821    1.00     2888   137  0.2930 0.3167        
REMARK   3     7  3.8821 -  3.6881    0.99     2881   154  0.3206 0.3833        
REMARK   3     8  3.6881 -  3.5278    0.85     2464   123  0.3423 0.4255        
REMARK   3     9  3.5278 -  3.3920    0.60     1746    96  0.3539 0.3918        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.530            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 38.780           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 137.4                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 164.4                          
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           6789                                  
REMARK   3   ANGLE     :  1.463           9265                                  
REMARK   3   CHIRALITY :  0.052           1123                                  
REMARK   3   PLANARITY :  0.007           1196                                  
REMARK   3   DIHEDRAL  : 14.952           2290                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 10                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 79:122)                             
REMARK   3    ORIGIN FOR THE GROUP (A): 121.4053  54.1914  81.9824              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.4882 T22:   1.6363                                     
REMARK   3      T33:   1.8414 T12:  -0.5718                                     
REMARK   3      T13:   0.2647 T23:  -0.3716                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4901 L22:   0.7245                                     
REMARK   3      L33:   1.4770 L12:  -1.0626                                     
REMARK   3      L13:   1.5118 L23:  -1.0392                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4911 S12:  -0.5364 S13:   0.5464                       
REMARK   3      S21:   0.8397 S22:   0.5707 S23:  -1.0894                       
REMARK   3      S31:   0.8878 S32:   0.6098 S33:  -0.0000                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 123:321)                            
REMARK   3    ORIGIN FOR THE GROUP (A): 117.5086  51.8302  55.8376              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8181 T22:   1.1179                                     
REMARK   3      T33:   1.4826 T12:  -0.1393                                     
REMARK   3      T13:   0.2657 T23:  -0.3027                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.9461 L22:   4.4006                                     
REMARK   3      L33:   6.6049 L12:   2.7957                                     
REMARK   3      L13:   3.1836 L23:  -0.7880                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0764 S12:  -0.4919 S13:   0.7772                       
REMARK   3      S21:   0.0887 S22:  -0.4164 S23:   0.3407                       
REMARK   3      S31:   0.2770 S32:  -0.3368 S33:  -0.0001                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 322:415)                            
REMARK   3    ORIGIN FOR THE GROUP (A): 101.9349  64.1837  87.3387              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.5352 T22:   1.5788                                     
REMARK   3      T33:   1.3137 T12:  -0.3586                                     
REMARK   3      T13:   0.1014 T23:  -0.3172                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.6638 L22:   5.4108                                     
REMARK   3      L33:   3.2597 L12:   0.7969                                     
REMARK   3      L13:  -1.4461 L23:   1.6121                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0921 S12:  -0.7313 S13:   0.6103                       
REMARK   3      S21:  -0.6695 S22:   0.8091 S23:  -0.7377                       
REMARK   3      S31:  -0.2863 S32:   0.6662 S33:  -0.0000                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 416:496)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  95.3732  79.6656  66.3684              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   4.9842 T22:   1.0150                                     
REMARK   3      T33:   1.6650 T12:   0.0373                                     
REMARK   3      T13:  -0.2247 T23:  -0.0151                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2277 L22:   0.7423                                     
REMARK   3      L33:   1.4946 L12:   0.1277                                     
REMARK   3      L13:  -0.0808 L23:   0.1020                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1456 S12:  -0.1949 S13:   0.3534                       
REMARK   3      S21:  -1.9922 S22:  -0.5973 S23:   0.0948                       
REMARK   3      S31:  -2.5728 S32:  -0.9086 S33:  -0.1419                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 497:599)                            
REMARK   3    ORIGIN FOR THE GROUP (A): 100.1560  55.5452  71.3988              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.8011 T22:   1.5463                                     
REMARK   3      T33:   1.4673 T12:  -0.4140                                     
REMARK   3      T13:   0.1673 T23:  -0.1893                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0902 L22:   3.3927                                     
REMARK   3      L33:   6.2213 L12:   0.2529                                     
REMARK   3      L13:   1.2392 L23:   4.6278                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.6396 S12:   0.2996 S13:   0.2742                       
REMARK   3      S21:  -1.5229 S22:   0.6201 S23:  -0.0506                       
REMARK   3      S31:  -1.4309 S32:   0.3780 S33:  -0.0004                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 600:661)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  90.4966  22.5567  70.4676              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.5943 T22:   1.7975                                     
REMARK   3      T33:   1.5463 T12:   0.0425                                     
REMARK   3      T13:   0.2550 T23:   0.0688                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0427 L22:   2.6099                                     
REMARK   3      L33:   1.7790 L12:   1.7733                                     
REMARK   3      L13:  -0.8313 L23:  -1.5578                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3803 S12:  -0.8651 S13:  -0.5577                       
REMARK   3      S21:  -0.5251 S22:   0.0030 S23:  -0.7333                       
REMARK   3      S31:   0.1924 S32:   0.9719 S33:  -0.0000                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 662:780)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  71.4543  44.5331  82.5487              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.3807 T22:   1.5862                                     
REMARK   3      T33:   1.4364 T12:   0.3554                                     
REMARK   3      T13:   0.0293 T23:  -0.0746                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.5218 L22:   3.0745                                     
REMARK   3      L33:   3.8979 L12:   1.6466                                     
REMARK   3      L13:   1.8740 L23:   0.6717                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3039 S12:  -0.5016 S13:  -0.1094                       
REMARK   3      S21:   0.3716 S22:   0.0191 S23:   0.0622                       
REMARK   3      S31:   0.4900 S32:   0.4328 S33:  -0.0000                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 781:877)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  72.6577  25.5875  83.1105              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.6927 T22:   1.5141                                     
REMARK   3      T33:   1.5345 T12:  -0.0018                                     
REMARK   3      T13:   0.0756 T23:   0.1765                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4806 L22:   3.5586                                     
REMARK   3      L33:   2.1061 L12:  -1.1511                                     
REMARK   3      L13:  -0.7719 L23:   0.1584                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0988 S12:  -0.5361 S13:   0.0787                       
REMARK   3      S21:  -0.1549 S22:   0.0281 S23:   0.3412                       
REMARK   3      S31:  -0.2593 S32:   0.3228 S33:   0.0000                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 878:995)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  82.7170  46.1998  43.0707              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   2.3586 T22:   2.3193                                     
REMARK   3      T33:   1.8799 T12:  -0.1513                                     
REMARK   3      T13:  -0.2126 T23:  -0.0516                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8322 L22:   2.2311                                     
REMARK   3      L33:  -0.0238 L12:  -0.7501                                     
REMARK   3      L13:   0.2044 L23:  -0.2693                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.5877 S12:   0.1623 S13:   0.0311                       
REMARK   3      S21:  -1.6456 S22:   0.1160 S23:   1.1313                       
REMARK   3      S31:  -0.7490 S32:  -0.6646 S33:  -0.0001                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: (CHAIN A AND RESID 996:1072)                           
REMARK   3    ORIGIN FOR THE GROUP (A):  85.9075  67.1731  45.1656              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   3.5475 T22:   2.5358                                     
REMARK   3      T33:   1.5350 T12:   0.3674                                     
REMARK   3      T13:  -0.2059 T23:   0.2104                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0882 L22:   0.0394                                     
REMARK   3      L33:   0.5071 L12:  -0.1273                                     
REMARK   3      L13:  -0.5264 L23:   0.2121                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4152 S12:  -0.2002 S13:   0.6948                       
REMARK   3      S21:   0.2790 S22:  -0.6791 S23:   0.0441                       
REMARK   3      S31:  -1.0321 S32:  -0.9230 S33:  -0.0180                       
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 4QU4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-JUL-14.                  
REMARK 100 THE DEPOSITION ID IS D_1000086515.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 19-JAN-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 190                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X29A                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9793                             
REMARK 200  MONOCHROMATOR                  : SI(111)                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 26177                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.389                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.0                               
REMARK 200  DATA REDUNDANCY                : 10.00                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.39                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.52                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 59.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.80                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.49400                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.900                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: SOLVE                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 68.38                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.89                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.4 M AMMONIUM DIHYDROGEN PHOSPHATE,     
REMARK 280  0.1 M TRIS, PH 8.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE      
REMARK 280  277K                                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+2/3                                           
REMARK 290       6555   -X,-X+Y,-Z+1/3                                          
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       63.64967            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      127.29933            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000      127.29933            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       63.64967            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: 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 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   -34                                                      
REMARK 465     HIS A   -33                                                      
REMARK 465     HIS A   -32                                                      
REMARK 465     HIS A   -31                                                      
REMARK 465     HIS A   -30                                                      
REMARK 465     HIS A   -29                                                      
REMARK 465     HIS A   -28                                                      
REMARK 465     GLY A   -27                                                      
REMARK 465     LYS A   -26                                                      
REMARK 465     PRO A   -25                                                      
REMARK 465     ILE A   -24                                                      
REMARK 465     PRO A   -23                                                      
REMARK 465     ASN A   -22                                                      
REMARK 465     PRO A   -21                                                      
REMARK 465     LEU A   -20                                                      
REMARK 465     LEU A   -19                                                      
REMARK 465     GLY A   -18                                                      
REMARK 465     LEU A   -17                                                      
REMARK 465     ASP A   -16                                                      
REMARK 465     SER A   -15                                                      
REMARK 465     THR A   -14                                                      
REMARK 465     GLU A   -13                                                      
REMARK 465     ASN A   -12                                                      
REMARK 465     LEU A   -11                                                      
REMARK 465     TYR A   -10                                                      
REMARK 465     PHE A    -9                                                      
REMARK 465     GLN A    -8                                                      
REMARK 465     GLY A    -7                                                      
REMARK 465     ILE A    -6                                                      
REMARK 465     ASP A    -5                                                      
REMARK 465     PRO A    -4                                                      
REMARK 465     PHE A    -3                                                      
REMARK 465     THR A    -2                                                      
REMARK 465     GLU A    -1                                                      
REMARK 465     PHE A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     ASP A     2                                                      
REMARK 465     SER A     3                                                      
REMARK 465     THR A     4                                                      
REMARK 465     ASP A     5                                                      
REMARK 465     LEU A     6                                                      
REMARK 465     PHE A     7                                                      
REMARK 465     ASP A     8                                                      
REMARK 465     VAL A     9                                                      
REMARK 465     PHE A    10                                                      
REMARK 465     GLU A    11                                                      
REMARK 465     GLU A    12                                                      
REMARK 465     THR A    13                                                      
REMARK 465     PRO A    14                                                      
REMARK 465     VAL A    15                                                      
REMARK 465     GLU A    16                                                      
REMARK 465     LEU A    17                                                      
REMARK 465     PRO A    18                                                      
REMARK 465     THR A    19                                                      
REMARK 465     ASP A    20                                                      
REMARK 465     SER A    21                                                      
REMARK 465     ASN A    22                                                      
REMARK 465     GLY A    23                                                      
REMARK 465     GLU A    24                                                      
REMARK 465     LYS A    25                                                      
REMARK 465     ASN A    26                                                      
REMARK 465     ALA A    27                                                      
REMARK 465     ASP A    28                                                      
REMARK 465     THR A    29                                                      
REMARK 465     ASN A    30                                                      
REMARK 465     VAL A    31                                                      
REMARK 465     GLY A    32                                                      
REMARK 465     ASP A    33                                                      
REMARK 465     THR A    34                                                      
REMARK 465     PRO A    35                                                      
REMARK 465     ASP A    36                                                      
REMARK 465     HIS A    37                                                      
REMARK 465     THR A    38                                                      
REMARK 465     GLN A    39                                                      
REMARK 465     ASP A    40                                                      
REMARK 465     LYS A    41                                                      
REMARK 465     LYS A    42                                                      
REMARK 465     HIS A    43                                                      
REMARK 465     GLY A    44                                                      
REMARK 465     LEU A    45                                                      
REMARK 465     GLU A    46                                                      
REMARK 465     GLU A    47                                                      
REMARK 465     GLU A    48                                                      
REMARK 465     LYS A    49                                                      
REMARK 465     GLU A    50                                                      
REMARK 465     GLU A    51                                                      
REMARK 465     HIS A    52                                                      
REMARK 465     GLU A    53                                                      
REMARK 465     GLU A    54                                                      
REMARK 465     ASN A    55                                                      
REMARK 465     ASN A    56                                                      
REMARK 465     SER A    57                                                      
REMARK 465     GLU A    58                                                      
REMARK 465     ASN A    59                                                      
REMARK 465     LYS A    60                                                      
REMARK 465     LYS A    61                                                      
REMARK 465     ILE A    62                                                      
REMARK 465     LYS A    63                                                      
REMARK 465     SER A    64                                                      
REMARK 465     ASN A    65                                                      
REMARK 465     LYS A    66                                                      
REMARK 465     SER A    67                                                      
REMARK 465     LYS A    68                                                      
REMARK 465     THR A    69                                                      
REMARK 465     GLU A    70                                                      
REMARK 465     ASP A    71                                                      
REMARK 465     LYS A    72                                                      
REMARK 465     ASN A    73                                                      
REMARK 465     LYS A    74                                                      
REMARK 465     LYS A    75                                                      
REMARK 465     VAL A    76                                                      
REMARK 465     VAL A    77                                                      
REMARK 465     VAL A    78                                                      
REMARK 465     ASP A    94                                                      
REMARK 465     SER A   361                                                      
REMARK 465     ASN A   362                                                      
REMARK 465     GLN A   363                                                      
REMARK 465     ILE A   364                                                      
REMARK 465     GLY A   365                                                      
REMARK 465     ASP A   366                                                      
REMARK 465     ASP A   367                                                      
REMARK 465     PRO A   368                                                      
REMARK 465     ASN A   369                                                      
REMARK 465     SER A   370                                                      
REMARK 465     THR A   371                                                      
REMARK 465     ASP A   372                                                      
REMARK 465     SER A   373                                                      
REMARK 465     ARG A   374                                                      
REMARK 465     GLY A   375                                                      
REMARK 465     LYS A   376                                                      
REMARK 465     LYS A   377                                                      
REMARK 465     GLY A   378                                                      
REMARK 465     GLN A   379                                                      
REMARK 465     THR A   380                                                      
REMARK 465     TYR A   381                                                      
REMARK 465     LYS A   382                                                      
REMARK 465     GLY A   383                                                      
REMARK 465     GLY A   384                                                      
REMARK 465     SER A   385                                                      
REMARK 465     ALA A   386                                                      
REMARK 465     LYS A   387                                                      
REMARK 465     GLY A   388                                                      
REMARK 465     ASP A   389                                                      
REMARK 465     SER A   873                                                      
REMARK 465     GLN A   874                                                      
REMARK 465     PHE A   943                                                      
REMARK 465     ALA A   944                                                      
REMARK 465     PHE A   945                                                      
REMARK 465     GLN A   946                                                      
REMARK 465     GLU A   947                                                      
REMARK 465     ARG A   948                                                      
REMARK 465     CYS A   949                                                      
REMARK 465     LYS A   950                                                      
REMARK 465     GLU A   951                                                      
REMARK 465     ALA A   952                                                      
REMARK 465     PRO A   953                                                      
REMARK 465     ARG A   954                                                      
REMARK 465     LEU A   955                                                      
REMARK 465     LYS A   956                                                      
REMARK 465     PRO A   957                                                      
REMARK 465     GLU A   958                                                      
REMARK 465     ALA A  1008                                                      
REMARK 465     VAL A  1039                                                      
REMARK 465     ASN A  1043                                                      
REMARK 465     GLY A  1046                                                      
REMARK 465     LEU A  1073                                                      
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     GLU A  86    CG   CD   OE1  OE2                                  
REMARK 470     ARG A  91    CD   NE   CZ   NH1  NH2                             
REMARK 470     LYS A  97    CG   CD   CE   NZ                                   
REMARK 470     LEU A  99    CG   CD1  CD2                                       
REMARK 470     GLU A 103    CG   CD   OE1  OE2                                  
REMARK 470     LEU A 105    CG   CD1  CD2                                       
REMARK 470     GLN A 106    CG   CD   OE1  NE2                                  
REMARK 470     GLU A 108    OE1                                                 
REMARK 470     LYS A 112    CD   CE   NZ                                        
REMARK 470     ARG A 114    CD   NE   CZ   NH1  NH2                             
REMARK 470     GLN A 118    CD   OE1  NE2                                       
REMARK 470     ARG A 120    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 136    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 138    CD   CE   NZ                                        
REMARK 470     ARG A 163    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 177    CG   CD   CE   NZ                                   
REMARK 470     LYS A 190    CD   CE   NZ                                        
REMARK 470     LYS A 192    CD   CE   NZ                                        
REMARK 470     ARG A 194    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ILE A 201    CG1  CD1                                            
REMARK 470     LYS A 202    CD   CE   NZ                                        
REMARK 470     ARG A 210    CD   NE   CZ   NH1  NH2                             
REMARK 470     ILE A 226    CG1  CG2  CD1                                       
REMARK 470     ASP A 231    CG   OD1  OD2                                       
REMARK 470     GLU A 240    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 248    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 254    CD   NE   CZ   NH1  NH2                             
REMARK 470     GLU A 255    CD   OE1  OE2                                       
REMARK 470     LYS A 270    CD   CE   NZ                                        
REMARK 470     ARG A 272    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 278    CD   OE1  OE2                                       
REMARK 470     LYS A 286    CD   CE   NZ                                        
REMARK 470     ILE A 296    CG1  CG2  CD1                                       
REMARK 470     GLU A 301    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 304    CD   OE1  OE2                                       
REMARK 470     LYS A 308    CG   CD   CE   NZ                                   
REMARK 470     ASN A 320    OD1  ND2                                            
REMARK 470     HIS A 334    CG   ND1  CD2  CE1  NE2                             
REMARK 470     ASP A 343    CG   OD1  OD2                                       
REMARK 470     LYS A 345    CD   CE   NZ                                        
REMARK 470     LYS A 355    CD   CE   NZ                                        
REMARK 470     LYS A 391    CD   CE   NZ                                        
REMARK 470     LYS A 396    CG   CD   CE   NZ                                   
REMARK 470     LYS A 399    CD   CE   NZ                                        
REMARK 470     LYS A 403    CD   CE   NZ                                        
REMARK 470     LYS A 404    CD   CE   NZ                                        
REMARK 470     LYS A 405    CG   CD   CE   NZ                                   
REMARK 470     ASN A 407    CG   OD1  ND2                                       
REMARK 470     ILE A 410    CG1  CG2  CD1                                       
REMARK 470     GLU A 420    CG   CD   OE1  OE2                                  
REMARK 470     LEU A 422    CG   CD1  CD2                                       
REMARK 470     LEU A 424    CG   CD1  CD2                                       
REMARK 470     LYS A 425    CD   CE   NZ                                        
REMARK 470     MET A 426    SD   CE                                             
REMARK 470     LYS A 428    CD   CE   NZ                                        
REMARK 470     LEU A 429    CD1  CD2                                            
REMARK 470     PHE A 431    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ASN A 432    CG   OD1  ND2                                       
REMARK 470     ASP A 435    CG   OD1  OD2                                       
REMARK 470     GLU A 436    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 438    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 442    CG   CD   CE   NZ                                   
REMARK 470     PHE A 444    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     GLU A 453    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 456    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 457    CG   CD   OE1  OE2                                  
REMARK 470     LEU A 458    CG   CD1  CD2                                       
REMARK 470     GLN A 460    CG   CD   OE1  NE2                                  
REMARK 470     ILE A 461    CG1  CG2  CD1                                       
REMARK 470     LYS A 462    CG   CD   CE   NZ                                   
REMARK 470     ILE A 464    CG1  CG2  CD1                                       
REMARK 470     PRO A 466    O                                                   
REMARK 470     LEU A 467    CD1  CD2                                            
REMARK 470     ARG A 469    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 470    NE   CZ   NH1  NH2                                  
REMARK 470     ILE A 474    CG1  CG2  CD1                                       
REMARK 470     HIS A 476    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LYS A 484    CG   CD   CE   NZ                                   
REMARK 470     GLU A 488    CG   CD   OE1  OE2                                  
REMARK 470     PHE A 491    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     GLN A 492    CD   OE1  NE2                                       
REMARK 470     GLU A 493    CG   CD   OE1  OE2                                  
REMARK 470     PHE A 495    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LYS A 497    CG   CD   CE   NZ                                   
REMARK 470     PHE A 500    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     THR A 502    OG1                                                 
REMARK 470     GLU A 503    CG   CD   OE1  OE2                                  
REMARK 470     ILE A 507    CG1  CG2  CD1                                       
REMARK 470     LYS A 514    CD   CE   NZ                                        
REMARK 470     LYS A 523    CD   CE   NZ                                        
REMARK 470     TRP A 524    CD1  CD2  NE1  CE2  CE3  CZ2  CZ3                   
REMARK 470     TRP A 524    CH2                                                 
REMARK 470     GLN A 527    CD   OE1  NE2                                       
REMARK 470     PHE A 529    CD1  CE1  CE2  CZ                                   
REMARK 470     ARG A 530    CD   NE   CZ   NH1  NH2                             
REMARK 470     GLN A 539    CG   CD   OE1  NE2                                  
REMARK 470     ARG A 543    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 547    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 561    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 562    CD   CE   NZ                                        
REMARK 470     LYS A 569    CD   CE   NZ                                        
REMARK 470     PHE A 583    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LEU A 585    CD1  CD2                                            
REMARK 470     ASN A 588    CG   OD1  ND2                                       
REMARK 470     ARG A 595    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 606    CD   OE1  OE2                                       
REMARK 470     GLN A 611    CD   OE1  NE2                                       
REMARK 470     LYS A 623    CD   CE   NZ                                        
REMARK 470     LYS A 624    CD   CE   NZ                                        
REMARK 470     LEU A 628    CD1  CD2                                            
REMARK 470     LYS A 629    CG   CD   CE   NZ                                   
REMARK 470     LYS A 630    CD   CE   NZ                                        
REMARK 470     PHE A 632    CD1  CE1  CE2  CZ                                   
REMARK 470     ILE A 635    CD1                                                 
REMARK 470     GLU A 636    CG   CD   OE1  OE2                                  
REMARK 470     ASP A 639    OD1  OD2                                            
REMARK 470     GLU A 640    CD   OE1  OE2                                       
REMARK 470     GLU A 641    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 644    CD   CE   NZ                                        
REMARK 470     GLU A 650    CD   OE1  OE2                                       
REMARK 470     LYS A 654    CD   CE   NZ                                        
REMARK 470     GLU A 681    CD   OE1  OE2                                       
REMARK 470     LYS A 687    CE   NZ                                             
REMARK 470     LYS A 700    CD   CE   NZ                                        
REMARK 470     ILE A 702    CG1  CG2  CD1                                       
REMARK 470     LYS A 704    CG   CD   CE   NZ                                   
REMARK 470     ARG A 705    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     SER A 708    OG                                                  
REMARK 470     LYS A 736    CG   CD   CE   NZ                                   
REMARK 470     GLU A 744    CD   OE1  OE2                                       
REMARK 470     ARG A 747    CD   NE   CZ   NH1  NH2                             
REMARK 470     GLU A 751    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 754    CG   CD   CE   NZ                                   
REMARK 470     LEU A 764    CD1  CD2                                            
REMARK 470     ASP A 765    OD1  OD2                                            
REMARK 470     LYS A 768    CD   CE   NZ                                        
REMARK 470     LYS A 779    CG   CD   CE   NZ                                   
REMARK 470     ASP A 780    CG   OD1  OD2                                       
REMARK 470     ARG A 782    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN A 786    CD   OE1  NE2                                       
REMARK 470     LYS A 787    CE   NZ                                             
REMARK 470     LYS A 792    CD   CE   NZ                                        
REMARK 470     ARG A 795    CD   NE   CZ   NH1  NH2                             
REMARK 470     ARG A 799    CD   NE   CZ   NH1  NH2                             
REMARK 470     ARG A 800    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP A 803    CG   OD1  OD2                                       
REMARK 470     LYS A 812    CD   CE   NZ                                        
REMARK 470     GLU A 817    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 819    CD   OE1  OE2                                       
REMARK 470     ASP A 820    CG   OD1  OD2                                       
REMARK 470     LEU A 822    CD1                                                 
REMARK 470     LYS A 823    CG   CD   CE   NZ                                   
REMARK 470     LYS A 826    CD   CE   NZ                                        
REMARK 470     LYS A 834    CD   CE   NZ                                        
REMARK 470     ASN A 842    CG   OD1  ND2                                       
REMARK 470     GLU A 847    OE1  OE2                                            
REMARK 470     GLU A 848    CD   OE1  OE2                                       
REMARK 470     LYS A 852    CD   CE   NZ                                        
REMARK 470     ARG A 855    NE   CZ   NH1  NH2                                  
REMARK 470     LYS A 856    CD   CE   NZ                                        
REMARK 470     LYS A 864    CG   CD   CE   NZ                                   
REMARK 470     GLN A 865    CD   NE2                                            
REMARK 470     LEU A 866    CD1  CD2                                            
REMARK 470     LYS A 867    CD   CE   NZ                                        
REMARK 470     LYS A 869    CE   NZ                                             
REMARK 470     VAL A 876    CG1  CG2                                            
REMARK 470     GLN A 878    CD   OE1  NE2                                       
REMARK 470     ARG A 883    CD   NE   CZ   NH1  NH2                             
REMARK 470     ARG A 885    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 887    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 891    NE   CZ   NH1  NH2                                  
REMARK 470     LEU A 892    CG   CD1  CD2                                       
REMARK 470     PHE A 894    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ASP A 899    OD1  OD2                                            
REMARK 470     ILE A 900    CD1                                                 
REMARK 470     ILE A 901    CG1  CG2  CD1                                       
REMARK 470     GLU A 902    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 904    CG   CD   CE   NZ                                   
REMARK 470     ARG A 906    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     VAL A 907    CG1  CG2                                            
REMARK 470     CYS A 909    SG                                                  
REMARK 470     LEU A 917    CG   CD1  CD2                                       
REMARK 470     ASN A 927    CG   OD1  ND2                                       
REMARK 470     PHE A 928    CD1  CD2  CE1  CE2  CZ                              
REMARK 470     GLU A 930    CD   OE1  OE2                                       
REMARK 470     LEU A 931    CG   CD1  CD2                                       
REMARK 470     LYS A 932    CD   CE   NZ                                        
REMARK 470     GLU A 934    CG   CD   OE1  OE2                                  
REMARK 470     GLN A 935    CG   CD   OE1  NE2                                  
REMARK 470     LEU A 959    CD1  CD2                                            
REMARK 470     GLU A 961    CD   OE1  OE2                                       
REMARK 470     LEU A 963    CG   CD1  CD2                                       
REMARK 470     LYS A 964    CG   CD   CE   NZ                                   
REMARK 470     ARG A 967    CD   NE   CZ   NH1  NH2                             
REMARK 470     GLU A 968    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 972    CG   CD   CE   NZ                                   
REMARK 470     LYS A 975    CG   CD   CE   NZ                                   
REMARK 470     LYS A 978    CD   CE   NZ                                        
REMARK 470     ASP A 979    OD1  OD2                                            
REMARK 470     LYS A 981    CD   CE   NZ                                        
REMARK 470     GLU A 983    CD   OE1  OE2                                       
REMARK 470     VAL A 985    CG1  CG2                                            
REMARK 470     GLU A 986    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 987    CG   CD   CE   NZ                                   
REMARK 470     ASP A 988    CG   OD1  OD2                                       
REMARK 470     TYR A 989    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     GLU A 991    CD   OE1  OE2                                       
REMARK 470     ARG A 994    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     HIS A 995    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LEU A 997    CG   CD1  CD2                                       
REMARK 470     GLU A 999    CD   OE1  OE2                                       
REMARK 470     VAL A1000    CG1  CG2                                            
REMARK 470     TYR A1002    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     GLU A1003    CG   CD   OE1  OE2                                  
REMARK 470     TRP A1004    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP A1004    CZ3  CH2                                            
REMARK 470     CYS A1005    CB   SG                                             
REMARK 470     ARG A1006    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     THR A1009    OG1  CG2                                            
REMARK 470     PHE A1010    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     THR A1011    OG1  CG2                                            
REMARK 470     GLN A1012    CG   CD   OE1  NE2                                  
REMARK 470     ILE A1013    CB   CG1  CG2  CD1                                  
REMARK 470     LYS A1015    CD   CE   NZ                                        
REMARK 470     MET A1016    CG   SD   CE                                        
REMARK 470     ASP A1018    CG   OD1  OD2                                       
REMARK 470     VAL A1019    CG1  CG2                                            
REMARK 470     TYR A1020    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     GLU A1021    CD   OE1  OE2                                       
REMARK 470     ILE A1025    CD1                                                 
REMARK 470     ARG A1026    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     MET A1027    SD   CE                                             
REMARK 470     PHE A1028    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LYS A1029    NZ                                                  
REMARK 470     ARG A1030    CZ   NH1  NH2                                       
REMARK 470     GLU A1032    CG   CD   OE1  OE2                                  
REMARK 470     LEU A1034    CG   CD1  CD2                                       
REMARK 470     LYS A1036    CG   CD   CE   NZ                                   
REMARK 470     ILE A1045    CG1  CG2  CD1                                       
REMARK 470     LYS A1051    CG   CD   CE   NZ                                   
REMARK 470     GLU A1052    CG   CD   OE1  OE2                                  
REMARK 470     LYS A1053    CG   CD   CE   NZ                                   
REMARK 470     MET A1054    CG   SD   CE                                        
REMARK 470     GLU A1055    CD   OE1  OE2                                       
REMARK 470     LEU A1058    CG   CD1  CD2                                       
REMARK 470     LYS A1059    CG   CD   CE   NZ                                   
REMARK 470     LEU A1060    CG   CD1  CD2                                       
REMARK 470     ILE A1061    CD1                                                 
REMARK 470     ARG A1063    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   OE1  GLU A   910     OG   SER A   913              2.09            
REMARK 500   O    GLU A   986     N    ASP A   988              2.15            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    LEU A 735   CA  -  CB  -  CG  ANGL. DEV. =  17.4 DEGREES          
REMARK 500    LEU A 775   CA  -  CB  -  CG  ANGL. DEV. =  17.6 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    GLU A 142      108.27    -59.39                                   
REMARK 500    ALA A 143      -76.98    -56.76                                   
REMARK 500    THR A 173       60.12    -63.48                                   
REMARK 500    ASN A 229       77.13     18.72                                   
REMARK 500    ARG A 248     -141.32    -79.24                                   
REMARK 500    SER A 250       82.67    -52.69                                   
REMARK 500    MET A 253      -41.73    -10.21                                   
REMARK 500    GLU A 271      -98.86    -90.68                                   
REMARK 500    ARG A 272       -9.95    -46.42                                   
REMARK 500    LEU A 283      150.58    -23.52                                   
REMARK 500    ASP A 285      -14.95    -40.75                                   
REMARK 500    PRO A 297      -75.72    -55.93                                   
REMARK 500    SER A 311       78.78     17.63                                   
REMARK 500    PRO A 323       98.49    -59.11                                   
REMARK 500    THR A 324      101.61     73.41                                   
REMARK 500    ASP A 336      -39.22   -154.33                                   
REMARK 500    LEU A 340      104.61    -53.85                                   
REMARK 500    LYS A 345      -50.37   -133.39                                   
REMARK 500    ARG A 349       70.14    -69.66                                   
REMARK 500    SER A 359       29.17    -76.45                                   
REMARK 500    TYR A 406       71.02   -104.77                                   
REMARK 500    LEU A 429      -96.64    -71.99                                   
REMARK 500    ASP A 430       40.85    -64.53                                   
REMARK 500    ASN A 432     -155.13    -68.73                                   
REMARK 500    GLU A 438       30.91    -69.07                                   
REMARK 500    ALA A 439      -27.23   -164.13                                   
REMARK 500    ASN A 446       19.90    -62.69                                   
REMARK 500    ALA A 447      -70.95   -146.37                                   
REMARK 500    GLU A 457     -133.73    -91.50                                   
REMARK 500    LEU A 458      166.67     62.19                                   
REMARK 500    PRO A 459       42.54    -69.47                                   
REMARK 500    GLN A 460      -65.71    -93.56                                   
REMARK 500    HIS A 463     -137.99     55.09                                   
REMARK 500    ILE A 464      -60.71     50.83                                   
REMARK 500    HIS A 476     -127.55     14.97                                   
REMARK 500    LEU A 479     -137.42    -75.51                                   
REMARK 500    SER A 506        8.80    -55.29                                   
REMARK 500    ALA A 513     -112.85   -138.49                                   
REMARK 500    LYS A 514      -56.41     54.47                                   
REMARK 500    ASP A 525       62.46   -173.68                                   
REMARK 500    MET A 558      106.06    -51.65                                   
REMARK 500    ASP A 560       28.05   -170.00                                   
REMARK 500    ASN A 588       19.61    -52.33                                   
REMARK 500    MET A 589      -36.98   -135.46                                   
REMARK 500    ARG A 595      -81.96    -58.52                                   
REMARK 500    GLU A 602      -17.79    -42.50                                   
REMARK 500    PHE A 673     -153.16    -88.18                                   
REMARK 500    PRO A 743      151.04    -44.35                                   
REMARK 500    GLU A 751      106.95    -54.86                                   
REMARK 500    ASN A 772       42.15    -90.22                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      93 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 HIS A  334     GLY A  335                  149.91                    
REMARK 500 TYR A  406     ASN A  407                 -137.89                    
REMARK 500 HIS A  476     SER A  477                 -131.85                    
REMARK 500 GLN A  527     GLN A  528                  147.02                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 1101                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 1102                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 1103                
DBREF  4QU4 A    1  1073  UNP    P47047   MTR4_YEAST       1   1073             
SEQADV 4QU4 MET A  -34  UNP  P47047              EXPRESSION TAG                 
SEQADV 4QU4 HIS A  -33  UNP  P47047              EXPRESSION TAG                 
SEQADV 4QU4 HIS A  -32  UNP  P47047              EXPRESSION TAG                 
SEQADV 4QU4 HIS A  -31  UNP  P47047              EXPRESSION TAG                 
SEQADV 4QU4 HIS A  -30  UNP  P47047              EXPRESSION TAG                 
SEQADV 4QU4 HIS A  -29  UNP  P47047              EXPRESSION TAG                 
SEQADV 4QU4 HIS A  -28  UNP  P47047              EXPRESSION TAG                 
SEQADV 4QU4 GLY A  -27  UNP  P47047              EXPRESSION TAG                 
SEQADV 4QU4 LYS A  -26  UNP  P47047              EXPRESSION TAG                 
SEQADV 4QU4 PRO A  -25  UNP  P47047              EXPRESSION TAG                 
SEQADV 4QU4 ILE A  -24  UNP  P47047              EXPRESSION TAG                 
SEQADV 4QU4 PRO A  -23  UNP  P47047              EXPRESSION TAG                 
SEQADV 4QU4 ASN A  -22  UNP  P47047              EXPRESSION TAG                 
SEQADV 4QU4 PRO A  -21  UNP  P47047              EXPRESSION TAG                 
SEQADV 4QU4 LEU A  -20  UNP  P47047              EXPRESSION TAG                 
SEQADV 4QU4 LEU A  -19  UNP  P47047              EXPRESSION TAG                 
SEQADV 4QU4 GLY A  -18  UNP  P47047              EXPRESSION TAG                 
SEQADV 4QU4 LEU A  -17  UNP  P47047              EXPRESSION TAG                 
SEQADV 4QU4 ASP A  -16  UNP  P47047              EXPRESSION TAG                 
SEQADV 4QU4 SER A  -15  UNP  P47047              EXPRESSION TAG                 
SEQADV 4QU4 THR A  -14  UNP  P47047              EXPRESSION TAG                 
SEQADV 4QU4 GLU A  -13  UNP  P47047              EXPRESSION TAG                 
SEQADV 4QU4 ASN A  -12  UNP  P47047              EXPRESSION TAG                 
SEQADV 4QU4 LEU A  -11  UNP  P47047              EXPRESSION TAG                 
SEQADV 4QU4 TYR A  -10  UNP  P47047              EXPRESSION TAG                 
SEQADV 4QU4 PHE A   -9  UNP  P47047              EXPRESSION TAG                 
SEQADV 4QU4 GLN A   -8  UNP  P47047              EXPRESSION TAG                 
SEQADV 4QU4 GLY A   -7  UNP  P47047              EXPRESSION TAG                 
SEQADV 4QU4 ILE A   -6  UNP  P47047              EXPRESSION TAG                 
SEQADV 4QU4 ASP A   -5  UNP  P47047              EXPRESSION TAG                 
SEQADV 4QU4 PRO A   -4  UNP  P47047              EXPRESSION TAG                 
SEQADV 4QU4 PHE A   -3  UNP  P47047              EXPRESSION TAG                 
SEQADV 4QU4 THR A   -2  UNP  P47047              EXPRESSION TAG                 
SEQADV 4QU4 GLU A   -1  UNP  P47047              EXPRESSION TAG                 
SEQADV 4QU4 PHE A    0  UNP  P47047              EXPRESSION TAG                 
SEQRES   1 A 1108  MET HIS HIS HIS HIS HIS HIS GLY LYS PRO ILE PRO ASN          
SEQRES   2 A 1108  PRO LEU LEU GLY LEU ASP SER THR GLU ASN LEU TYR PHE          
SEQRES   3 A 1108  GLN GLY ILE ASP PRO PHE THR GLU PHE MET ASP SER THR          
SEQRES   4 A 1108  ASP LEU PHE ASP VAL PHE GLU GLU THR PRO VAL GLU LEU          
SEQRES   5 A 1108  PRO THR ASP SER ASN GLY GLU LYS ASN ALA ASP THR ASN          
SEQRES   6 A 1108  VAL GLY ASP THR PRO ASP HIS THR GLN ASP LYS LYS HIS          
SEQRES   7 A 1108  GLY LEU GLU GLU GLU LYS GLU GLU HIS GLU GLU ASN ASN          
SEQRES   8 A 1108  SER GLU ASN LYS LYS ILE LYS SER ASN LYS SER LYS THR          
SEQRES   9 A 1108  GLU ASP LYS ASN LYS LYS VAL VAL VAL PRO VAL LEU ALA          
SEQRES  10 A 1108  ASP SER PHE GLU GLN GLU ALA SER ARG GLU VAL ASP ALA          
SEQRES  11 A 1108  SER LYS GLY LEU THR ASN SER GLU THR LEU GLN VAL GLU          
SEQRES  12 A 1108  GLN ASP GLY LYS VAL ARG LEU SER HIS GLN VAL ARG HIS          
SEQRES  13 A 1108  GLN VAL ALA LEU PRO PRO ASN TYR ASP TYR THR PRO ILE          
SEQRES  14 A 1108  ALA GLU HIS LYS ARG VAL ASN GLU ALA ARG THR TYR PRO          
SEQRES  15 A 1108  PHE THR LEU ASP PRO PHE GLN ASP THR ALA ILE SER CYS          
SEQRES  16 A 1108  ILE ASP ARG GLY GLU SER VAL LEU VAL SER ALA HIS THR          
SEQRES  17 A 1108  SER ALA GLY LYS THR VAL VAL ALA GLU TYR ALA ILE ALA          
SEQRES  18 A 1108  GLN SER LEU LYS ASN LYS GLN ARG VAL ILE TYR THR SER          
SEQRES  19 A 1108  PRO ILE LYS ALA LEU SER ASN GLN LYS TYR ARG GLU LEU          
SEQRES  20 A 1108  LEU ALA GLU PHE GLY ASP VAL GLY LEU MET THR GLY ASP          
SEQRES  21 A 1108  ILE THR ILE ASN PRO ASP ALA GLY CYS LEU VAL MET THR          
SEQRES  22 A 1108  THR GLU ILE LEU ARG SER MET LEU TYR ARG GLY SER GLU          
SEQRES  23 A 1108  VAL MET ARG GLU VAL ALA TRP VAL ILE PHE ASP GLU VAL          
SEQRES  24 A 1108  HIS TYR MET ARG ASP LYS GLU ARG GLY VAL VAL TRP GLU          
SEQRES  25 A 1108  GLU THR ILE ILE LEU LEU PRO ASP LYS VAL ARG TYR VAL          
SEQRES  26 A 1108  PHE LEU SER ALA THR ILE PRO ASN ALA MET GLU PHE ALA          
SEQRES  27 A 1108  GLU TRP ILE CYS LYS ILE HIS SER GLN PRO CYS HIS ILE          
SEQRES  28 A 1108  VAL TYR THR ASN PHE ARG PRO THR PRO LEU GLN HIS TYR          
SEQRES  29 A 1108  LEU PHE PRO ALA HIS GLY ASP GLY ILE TYR LEU VAL VAL          
SEQRES  30 A 1108  ASP GLU LYS SER THR PHE ARG GLU GLU ASN PHE GLN LYS          
SEQRES  31 A 1108  ALA MET ALA SER ILE SER ASN GLN ILE GLY ASP ASP PRO          
SEQRES  32 A 1108  ASN SER THR ASP SER ARG GLY LYS LYS GLY GLN THR TYR          
SEQRES  33 A 1108  LYS GLY GLY SER ALA LYS GLY ASP ALA LYS GLY ASP ILE          
SEQRES  34 A 1108  TYR LYS ILE VAL LYS MET ILE TRP LYS LYS LYS TYR ASN          
SEQRES  35 A 1108  PRO VAL ILE VAL PHE SER PHE SER LYS ARG ASP CYS GLU          
SEQRES  36 A 1108  GLU LEU ALA LEU LYS MET SER LYS LEU ASP PHE ASN SER          
SEQRES  37 A 1108  ASP ASP GLU LYS GLU ALA LEU THR LYS ILE PHE ASN ASN          
SEQRES  38 A 1108  ALA ILE ALA LEU LEU PRO GLU THR ASP ARG GLU LEU PRO          
SEQRES  39 A 1108  GLN ILE LYS HIS ILE LEU PRO LEU LEU ARG ARG GLY ILE          
SEQRES  40 A 1108  GLY ILE HIS HIS SER GLY LEU LEU PRO ILE LEU LYS GLU          
SEQRES  41 A 1108  VAL ILE GLU ILE LEU PHE GLN GLU GLY PHE LEU LYS VAL          
SEQRES  42 A 1108  LEU PHE ALA THR GLU THR PHE SER ILE GLY LEU ASN MET          
SEQRES  43 A 1108  PRO ALA LYS THR VAL VAL PHE THR SER VAL ARG LYS TRP          
SEQRES  44 A 1108  ASP GLY GLN GLN PHE ARG TRP VAL SER GLY GLY GLU TYR          
SEQRES  45 A 1108  ILE GLN MET SER GLY ARG ALA GLY ARG ARG GLY LEU ASP          
SEQRES  46 A 1108  ASP ARG GLY ILE VAL ILE MET MET ILE ASP GLU LYS MET          
SEQRES  47 A 1108  GLU PRO GLN VAL ALA LYS GLY MET VAL LYS GLY GLN ALA          
SEQRES  48 A 1108  ASP ARG LEU ASP SER ALA PHE HIS LEU GLY TYR ASN MET          
SEQRES  49 A 1108  ILE LEU ASN LEU MET ARG VAL GLU GLY ILE SER PRO GLU          
SEQRES  50 A 1108  PHE MET LEU GLU HIS SER PHE PHE GLN PHE GLN ASN VAL          
SEQRES  51 A 1108  ILE SER VAL PRO VAL MET GLU LYS LYS LEU ALA GLU LEU          
SEQRES  52 A 1108  LYS LYS ASP PHE ASP GLY ILE GLU VAL GLU ASP GLU GLU          
SEQRES  53 A 1108  ASN VAL LYS GLU TYR HIS GLU ILE GLU GLN ALA ILE LYS          
SEQRES  54 A 1108  GLY TYR ARG GLU ASP VAL ARG GLN VAL VAL THR HIS PRO          
SEQRES  55 A 1108  ALA ASN ALA LEU SER PHE LEU GLN PRO GLY ARG LEU VAL          
SEQRES  56 A 1108  GLU ILE SER VAL ASN GLY LYS ASP ASN TYR GLY TRP GLY          
SEQRES  57 A 1108  ALA VAL VAL ASP PHE ALA LYS ARG ILE ASN LYS ARG ASN          
SEQRES  58 A 1108  PRO SER ALA VAL TYR THR ASP HIS GLU SER TYR ILE VAL          
SEQRES  59 A 1108  ASN VAL VAL VAL ASN THR MET TYR ILE ASP SER PRO VAL          
SEQRES  60 A 1108  ASN LEU LEU LYS PRO PHE ASN PRO THR LEU PRO GLU GLY          
SEQRES  61 A 1108  ILE ARG PRO ALA GLU GLU GLY GLU LYS SER ILE CYS ALA          
SEQRES  62 A 1108  VAL ILE PRO ILE THR LEU ASP SER ILE LYS SER ILE GLY          
SEQRES  63 A 1108  ASN LEU ARG LEU TYR MET PRO LYS ASP ILE ARG ALA SER          
SEQRES  64 A 1108  GLY GLN LYS GLU THR VAL GLY LYS SER LEU ARG GLU VAL          
SEQRES  65 A 1108  ASN ARG ARG PHE PRO ASP GLY ILE PRO VAL LEU ASP PRO          
SEQRES  66 A 1108  VAL LYS ASN MET LYS ILE GLU ASP GLU ASP PHE LEU LYS          
SEQRES  67 A 1108  LEU MET LYS LYS ILE ASP VAL LEU ASN THR LYS LEU SER          
SEQRES  68 A 1108  SER ASN PRO LEU THR ASN SER MET ARG LEU GLU GLU LEU          
SEQRES  69 A 1108  TYR GLY LYS TYR SER ARG LYS HIS ASP LEU HIS GLU ASP          
SEQRES  70 A 1108  MET LYS GLN LEU LYS ARG LYS ILE SER GLU SER GLN ALA          
SEQRES  71 A 1108  VAL ILE GLN LEU ASP ASP LEU ARG ARG ARG LYS ARG VAL          
SEQRES  72 A 1108  LEU ARG ARG LEU GLY PHE CYS THR PRO ASN ASP ILE ILE          
SEQRES  73 A 1108  GLU LEU LYS GLY ARG VAL ALA CYS GLU ILE SER SER GLY          
SEQRES  74 A 1108  ASP GLU LEU LEU LEU THR GLU LEU ILE PHE ASN GLY ASN          
SEQRES  75 A 1108  PHE ASN GLU LEU LYS PRO GLU GLN ALA ALA ALA LEU LEU          
SEQRES  76 A 1108  SER CYS PHE ALA PHE GLN GLU ARG CYS LYS GLU ALA PRO          
SEQRES  77 A 1108  ARG LEU LYS PRO GLU LEU ALA GLU PRO LEU LYS ALA MET          
SEQRES  78 A 1108  ARG GLU ILE ALA ALA LYS ILE ALA LYS ILE MET LYS ASP          
SEQRES  79 A 1108  SER LYS ILE GLU VAL VAL GLU LYS ASP TYR VAL GLU SER          
SEQRES  80 A 1108  PHE ARG HIS GLU LEU MET GLU VAL VAL TYR GLU TRP CYS          
SEQRES  81 A 1108  ARG GLY ALA THR PHE THR GLN ILE CYS LYS MET THR ASP          
SEQRES  82 A 1108  VAL TYR GLU GLY SER LEU ILE ARG MET PHE LYS ARG LEU          
SEQRES  83 A 1108  GLU GLU LEU VAL LYS GLU LEU VAL ASP VAL ALA ASN THR          
SEQRES  84 A 1108  ILE GLY ASN SER SER LEU LYS GLU LYS MET GLU ALA VAL          
SEQRES  85 A 1108  LEU LYS LEU ILE HIS ARG ASP ILE VAL SER ALA GLY SER          
SEQRES  86 A 1108  LEU TYR LEU                                                  
HET    PO4  A1101       5                                                       
HET    PO4  A1102       5                                                       
HET    PO4  A1103       5                                                       
HETNAM     PO4 PHOSPHATE ION                                                    
FORMUL   2  PO4    3(O4 P 3-)                                                   
HELIX    1   1 ASP A  151  GLY A  164  1                                  14    
HELIX    2   2 GLY A  176  ASN A  191  1                                  16    
HELIX    3   3 ILE A  201  GLY A  217  1                                  17    
HELIX    4   4 THR A  239  ARG A  248  1                                  10    
HELIX    5   5 GLU A  251  ARG A  254  5                                   4    
HELIX    6   6 VAL A  264  ASP A  269  5                                   6    
HELIX    7   7 ARG A  272  LEU A  283  1                                  12    
HELIX    8   8 ALA A  299  HIS A  310  1                                  12    
HELIX    9   9 ARG A  349  SER A  359  1                                  11    
HELIX   10  10 LYS A  391  LYS A  404  1                                  14    
HELIX   11  11 SER A  415  LYS A  425  1                                  11    
HELIX   12  12 GLU A  436  ALA A  449  1                                  14    
HELIX   13  13 GLU A  453  ARG A  456  5                                   4    
HELIX   14  14 GLU A  457  LYS A  462  1                                   6    
HELIX   15  15 ILE A  464  ARG A  469  1                                   6    
HELIX   16  16 ILE A  482  GLU A  493  1                                  12    
HELIX   17  17 SER A  533  GLY A  542  1                                  10    
HELIX   18  18 GLU A  564  LYS A  573  1                                  10    
HELIX   19  19 GLY A  586  VAL A  596  1                                  11    
HELIX   20  20 SER A  600  GLU A  606  1                                   7    
HELIX   21  21 SER A  608  ASP A  633  1                                  26    
HELIX   22  22 ASP A  639  THR A  665  1                                  27    
HELIX   23  23 ASN A  669  PHE A  673  5                                   5    
HELIX   24  24 ASN A  685  LYS A  687  5                                   3    
HELIX   25  25 PRO A  731  LEU A  735  5                                   5    
HELIX   26  26 GLY A  785  PHE A  801  1                                  17    
HELIX   27  27 ASP A  818  SER A  837  1                                  20    
HELIX   28  28 ARG A  845  ILE A  870  1                                  26    
HELIX   29  29 GLN A  878  ARG A  891  1                                  14    
HELIX   30  30 ASP A  915  PHE A  924  1                                  10    
HELIX   31  31 ALA A  936  SER A  941  1                                   6    
HELIX   32  32 LEU A  963  SER A  980  1                                  18    
HELIX   33  33 GLU A  999  CYS A 1005  1                                   7    
HELIX   34  34 PHE A 1010  CYS A 1014  1                                   5    
HELIX   35  35 SER A 1023  LYS A 1036  1                                  14    
HELIX   36  36 SER A 1048  ARG A 1063  1                                  16    
HELIX   37  37 ASP A 1064  VAL A 1066  5                                   3    
SHEET    1   A10 VAL A  80  VAL A  93  0                                        
SHEET    2   A10 VAL A 113  LEU A 125 -1  O  HIS A 117   N  ALA A  89           
SHEET    3   A10 CYS A 314  THR A 319 -1  O  TYR A 318   N  ARG A 120           
SHEET    4   A10 SER A 166  SER A 170  1  N  LEU A 168   O  HIS A 315           
SHEET    5   A10 ARG A 288  SER A 293  1  O  SER A 293   N  VAL A 169           
SHEET    6   A10 VAL A 256  ASP A 262  1  N  VAL A 259   O  ARG A 288           
SHEET    7   A10 ARG A 194  SER A 199  1  N  ARG A 194   O  ALA A 257           
SHEET    8   A10 CYS A 234  THR A 238  1  O  LEU A 235   N  TYR A 197           
SHEET    9   A10 VAL A 219  MET A 222  1  N  GLY A 220   O  VAL A 236           
SHEET   10   A10 THR A 227  ILE A 228 -1  O  ILE A 228   N  LEU A 221           
SHEET    1   B 7 TYR A 339  VAL A 342  0                                        
SHEET    2   B 7 LEU A 326  PHE A 331 -1  N  HIS A 328   O  VAL A 341           
SHEET    3   B 7 GLY A 553  MET A 558  1  O  VAL A 555   N  TYR A 329           
SHEET    4   B 7 THR A 515  PHE A 518  1  N  VAL A 516   O  ILE A 554           
SHEET    5   B 7 VAL A 409  ILE A 410  1  N  ILE A 410   O  THR A 515           
SHEET    6   B 7 VAL A 498  ALA A 501  1  O  LEU A 499   N  VAL A 409           
SHEET    7   B 7 ILE A 472  HIS A 475  1  N  GLY A 473   O  PHE A 500           
SHEET    1   C 2 ARG A 522  LYS A 523  0                                        
SHEET    2   C 2 ARG A 530  TRP A 531 -1  O  ARG A 530   N  LYS A 523           
SHEET    1   D 5 SER A 755  THR A 763  0                                        
SHEET    2   D 5 TYR A 717  TYR A 727 -1  N  VAL A 719   O  ILE A 762           
SHEET    3   D 5 ASP A 688  LYS A 700 -1  N  ALA A 694   O  VAL A 722           
SHEET    4   D 5 ARG A 678  VAL A 684 -1  N  ARG A 678   O  VAL A 695           
SHEET    5   D 5 ILE A 767  ARG A 774 -1  O  SER A 769   N  GLU A 681           
CISPEP   1 LYS A  345    SER A  346          0         7.09                     
CISPEP   2 ILE A  507    GLY A  508          0         4.72                     
CISPEP   3 GLY A  526    GLN A  527          0       -10.86                     
SITE     1 AC1  3 GLU A 263  TYR A 266  GLY A 508                               
SITE     1 AC2  5 LYS A 416  HIS A 476  SER A 477  THR A 502                    
SITE     2 AC2  5 THR A 504                                                     
SITE     1 AC3  1 LYS A 827                                                     
CRYST1  133.516  133.516  190.949  90.00  90.00 120.00 P 31 2 1      6          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.007490  0.004324  0.000000        0.00000                         
SCALE2      0.000000  0.008648  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005237        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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