GenomeNet

Database: PDB
Entry: 5XAP
LinkDB: 5XAP
Original site: 5XAP 
HEADER    MEMBRANE PROTEIN                        14-MAR-17   5XAP              
TITLE     CRYSTAL STRUCTURE OF SECDF IN I FORM (C2 SPACE GROUP)                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROTEIN TRANSLOCASE SUBUNIT SECD;                          
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 28-768;                                       
COMPND   5 SYNONYM: PROTEIN-EXPORT MEMBRANE PROTEIN SECF;                       
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: DEINOCOCCUS RADIODURANS STR. R1;                
SOURCE   3 ORGANISM_TAXID: 243230;                                              
SOURCE   4 STRAIN: R1;                                                          
SOURCE   5 GENE: SECD, SECF, DR_1822;                                           
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: C41(DE3);                                  
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET28                                     
KEYWDS    MEMBRANE PROTEIN, ALFA HELICAL, SEC TRANSLOCON                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    T.TSUKAZAKI,Y.TANAKA,A.FURUKWA                                        
REVDAT   5   11-NOV-20 5XAP    1       REMARK                                   
REVDAT   4   14-OCT-20 5XAP    1       SOURCE                                   
REVDAT   3   22-MAY-19 5XAP    1       TITLE                                    
REVDAT   2   04-OCT-17 5XAP    1       REMARK                                   
REVDAT   1   17-MAY-17 5XAP    0                                                
JRNL        AUTH   A.FURUKAWA,K.YOSHIKAIE,T.MORI,H.MORI,Y.V.MORIMOTO,Y.SUGANO,  
JRNL        AUTH 2 S.IWAKI,T.MINAMINO,Y.SUGITA,Y.TANAKA,T.TSUKAZAKI             
JRNL        TITL   TUNNEL FORMATION INFERRED FROM THE I-FORM STRUCTURES OF THE  
JRNL        TITL 2 PROTON-DRIVEN PROTEIN SECRETION MOTOR SECDF                  
JRNL        REF    CELL REP                      V.  19   895 2017              
JRNL        REFN                   ESSN 2211-1247                               
JRNL        PMID   28467902                                                     
JRNL        DOI    10.1016/J.CELREP.2017.04.030                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.61 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (1.10.1_2155: ???)                            
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.61                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 49.14                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 28635                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.207                           
REMARK   3   R VALUE            (WORKING SET) : 0.203                           
REMARK   3   FREE R VALUE                     : 0.258                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 6.990                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2002                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 49.1438 -  6.2732    0.99     1998   156  0.1687 0.1946        
REMARK   3     2  6.2732 -  4.9808    1.00     1952   144  0.2185 0.2480        
REMARK   3     3  4.9808 -  4.3516    0.88     1707   129  0.1927 0.2643        
REMARK   3     4  4.3516 -  3.9539    1.00     1966   148  0.1951 0.2575        
REMARK   3     5  3.9539 -  3.6706    1.00     1900   143  0.1956 0.2414        
REMARK   3     6  3.6706 -  3.4543    1.00     1968   144  0.2007 0.2662        
REMARK   3     7  3.4543 -  3.2813    1.00     1926   160  0.2172 0.2699        
REMARK   3     8  3.2813 -  3.1385    1.00     1926   129  0.2176 0.2892        
REMARK   3     9  3.1385 -  3.0177    1.00     1924   144  0.2189 0.3049        
REMARK   3    10  3.0177 -  2.9136    1.00     1936   150  0.2229 0.2856        
REMARK   3    11  2.9136 -  2.8225    1.00     1916   149  0.2219 0.2980        
REMARK   3    12  2.8225 -  2.7418    1.00     1931   137  0.2290 0.2819        
REMARK   3    13  2.7418 -  2.6697    1.00     1892   144  0.2297 0.2804        
REMARK   3    14  2.6697 -  2.6045    0.87     1691   125  0.2237 0.3209        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.290            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.330           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 42.74                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 49.33                          
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           5771                                  
REMARK   3   ANGLE     :  1.046           7806                                  
REMARK   3   CHIRALITY :  0.054            927                                  
REMARK   3   PLANARITY :  0.006            983                                  
REMARK   3   DIHEDRAL  : 19.021           3445                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 5                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 29 THROUGH 92 )                   
REMARK   3    ORIGIN FOR THE GROUP (A): -38.2035 -23.4364  25.6404              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3188 T22:   0.2626                                     
REMARK   3      T33:   0.2850 T12:   0.0473                                     
REMARK   3      T13:  -0.0578 T23:   0.0107                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.3399 L22:   2.2180                                     
REMARK   3      L33:   2.5668 L12:   2.7692                                     
REMARK   3      L13:  -3.0783 L23:  -1.9399                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2408 S12:  -0.0949 S13:   0.1873                       
REMARK   3      S21:   0.1621 S22:  -0.2231 S23:   0.1873                       
REMARK   3      S31:  -0.0448 S32:   0.3827 S33:  -0.0335                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 93 THROUGH 288 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):   1.9275 -19.8108  17.4617              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3492 T22:   0.4061                                     
REMARK   3      T33:   0.2168 T12:   0.0550                                     
REMARK   3      T13:   0.0133 T23:  -0.0403                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.5813 L22:   1.2695                                     
REMARK   3      L33:  -0.1025 L12:  -2.3434                                     
REMARK   3      L13:   0.9682 L23:  -0.3978                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0879 S12:  -0.0944 S13:   0.0606                       
REMARK   3      S21:  -0.0791 S22:  -0.0453 S23:   0.0768                       
REMARK   3      S31:  -0.0172 S32:   0.0717 S33:  -0.0401                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 289 THROUGH 518 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -54.0098  -8.4741  18.6490              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2267 T22:   0.1883                                     
REMARK   3      T33:   0.2262 T12:   0.0088                                     
REMARK   3      T13:  -0.0065 T23:  -0.0432                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8217 L22:   1.0176                                     
REMARK   3      L33:   1.1447 L12:  -0.0971                                     
REMARK   3      L13:  -0.3889 L23:  -0.2115                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0310 S12:  -0.1350 S13:  -0.0849                       
REMARK   3      S21:  -0.0416 S22:   0.0083 S23:   0.0099                       
REMARK   3      S31:   0.0422 S32:   0.0080 S33:  -0.0261                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 519 THROUGH 562 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -21.3968   8.9019  18.9005              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4268 T22:   0.4282                                     
REMARK   3      T33:   0.8135 T12:  -0.0614                                     
REMARK   3      T13:   0.0614 T23:  -0.0692                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.9332 L22:   3.0830                                     
REMARK   3      L33:   8.4220 L12:   0.0473                                     
REMARK   3      L13:   2.7215 L23:   2.6967                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2967 S12:  -0.6864 S13:   1.2991                       
REMARK   3      S21:  -0.0896 S22:   0.1477 S23:  -0.5737                       
REMARK   3      S31:  -0.8969 S32:  -0.1412 S33:  -0.2496                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 563 THROUGH 760 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -50.6313  -1.0374   7.4151              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2633 T22:   0.1619                                     
REMARK   3      T33:   0.2892 T12:  -0.0137                                     
REMARK   3      T13:   0.0576 T23:   0.0335                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.5114 L22:   1.0963                                     
REMARK   3      L33:   1.1493 L12:  -0.4634                                     
REMARK   3      L13:  -0.4616 L23:  -0.0471                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0119 S12:   0.2952 S13:   0.4040                       
REMARK   3      S21:  -0.0648 S22:   0.0248 S23:  -0.0004                       
REMARK   3      S31:  -0.0322 S32:  -0.0779 S33:   0.0207                       
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 5XAP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 17-MAR-17.                  
REMARK 100 THE DEPOSITION ID IS D_1300003195.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 20-MAY-16                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.9                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SPRING-8                           
REMARK 200  BEAMLINE                       : BL32XU                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1                                  
REMARK 200  MONOCHROMATOR                  : ??                                 
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS EIGER X 9M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL                                
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 28645                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.0                               
REMARK 200  DATA REDUNDANCY                : 10.20                              
REMARK 200  R MERGE                    (I) : 0.22300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 4.0000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.64                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.83300                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 3AQP                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 59.69                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.05                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 41% PEG 200, 100MM NA-CITRATE, 100MM     
REMARK 280  NH4NO3, PH 5.9, LIPIDIC CUBIC PHASE, TEMPERATURE 298K               
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000      104.13250            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       34.90350            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000      104.13250            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       34.90350            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
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    27                                                      
REMARK 465     SER A    28                                                      
REMARK 465     ALA A   761                                                      
REMARK 465     ALA A   762                                                      
REMARK 465     LYS A   763                                                      
REMARK 465     PRO A   764                                                      
REMARK 465     VAL A   765                                                      
REMARK 465     THR A   766                                                      
REMARK 465     ASN A   767                                                      
REMARK 465     SER A   768                                                      
REMARK 465     HIS A   769                                                      
REMARK 465     HIS A   770                                                      
REMARK 465     HIS A   771                                                      
REMARK 465     HIS A   772                                                      
REMARK 465     HIS A   773                                                      
REMARK 465     HIS A   774                                                      
REMARK 465     HIS A   775                                                      
REMARK 465     HIS A   776                                                      
REMARK 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   520     NH2  ARG A   523              2.08            
REMARK 500   NE2  GLN A   145     OG1  THR A   281              2.13            
REMARK 500   NH2  ARG A   149     OD2  ASP A   236              2.13            
REMARK 500   OD1  ASP A   365     O    HOH A   901              2.13            
REMARK 500   NH1  ARG A   543     OE1  GLN A   552              2.15            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    PHE A 208   CB    PHE A 208   CG     -0.124                       
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    ARG A 760   NE  -  CZ  -  NH2 ANGL. DEV. =   3.0 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    ARG A  51       62.24     39.08                                   
REMARK 500    ALA A 148       52.46     70.16                                   
REMARK 500    ASN A 227       -9.54     89.32                                   
REMARK 500    ASN A 227       -9.13     89.32                                   
REMARK 500    ASP A 235       51.81     39.07                                   
REMARK 500    PHE A 249      -85.07   -130.17                                   
REMARK 500    HIS A 465       39.39    -99.28                                   
REMARK 500    ARG A 523      -71.79    -50.59                                   
REMARK 500    THR A 535     -166.09   -128.47                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     OLC A  801                                                       
REMARK 610     OLC A  802                                                       
REMARK 610     OLC A  803                                                       
REMARK 610     OLC A  804                                                       
REMARK 610     OLC A  805                                                       
REMARK 610     OLC A  807                                                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 801                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 802                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 803                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 804                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 805                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 806                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 807                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 808                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5XAM   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5XAN   RELATED DB: PDB                                   
DBREF  5XAP A   28   768  UNP    Q9RTE3   Q9RTE3_DEIRA    28    768             
SEQADV 5XAP MET A   27  UNP  Q9RTE3              EXPRESSION TAG                 
SEQADV 5XAP CYS A  143  UNP  Q9RTE3    ILE   143 ENGINEERED MUTATION            
SEQADV 5XAP CYS A  268  UNP  Q9RTE3    LEU   268 ENGINEERED MUTATION            
SEQADV 5XAP HIS A  769  UNP  Q9RTE3              EXPRESSION TAG                 
SEQADV 5XAP HIS A  770  UNP  Q9RTE3              EXPRESSION TAG                 
SEQADV 5XAP HIS A  771  UNP  Q9RTE3              EXPRESSION TAG                 
SEQADV 5XAP HIS A  772  UNP  Q9RTE3              EXPRESSION TAG                 
SEQADV 5XAP HIS A  773  UNP  Q9RTE3              EXPRESSION TAG                 
SEQADV 5XAP HIS A  774  UNP  Q9RTE3              EXPRESSION TAG                 
SEQADV 5XAP HIS A  775  UNP  Q9RTE3              EXPRESSION TAG                 
SEQADV 5XAP HIS A  776  UNP  Q9RTE3              EXPRESSION TAG                 
SEQRES   1 A  750  MET SER ARG PRO ASN PRO TRP THR ALA LEU LEU LEU LEU          
SEQRES   2 A  750  LEU THR LEU LEU GLY SER LEU LEU TYR ILE TRP ARG PRO          
SEQRES   3 A  750  TRP GLU HIS LYS ASN ASP PRO TRP SER LEU TRP ASN ASP          
SEQRES   4 A  750  GLN TYR GLN PHE MET THR LEU GLY LEU ASP LEU LYS GLY          
SEQRES   5 A  750  GLY LEU ARG ILE GLU LEU ALA PRO GLU SER GLY THR ALA          
SEQRES   6 A  750  THR ARG ASP GLU LEU ASP ARG VAL LYS THR VAL ILE GLU          
SEQRES   7 A  750  ASN ARG ILE ASN ALA LEU GLY VAL ALA GLU PRO THR VAL          
SEQRES   8 A  750  THR VAL SER GLY GLY LYS ARG VAL VAL VAL GLU ILE PRO          
SEQRES   9 A  750  GLY ALA THR PRO ALA VAL GLN ASP ARG ALA ARG SER CYS          
SEQRES  10 A  750  ILE GLN GLN THR ALA ARG LEU GLU PHE ARG ILE VAL ASN          
SEQRES  11 A  750  SER ASP ALA LYS PRO ASP PRO ALA VAL ARG GLU LYS ASN          
SEQRES  12 A  750  PRO ARG SER SER GLY TYR THR LEU ALA GLN LEU GLY PRO          
SEQRES  13 A  750  VAL VAL ALA THR GLY GLU THR ILE ALA ASP ALA THR SER          
SEQRES  14 A  750  GLY THR ASP GLN ARG SER GLY GLN TRP VAL VAL ASN PHE          
SEQRES  15 A  750  LYS THR THR ASP ALA GLY ALA LYS THR PHE GLY ASP PHE          
SEQRES  16 A  750  THR GLY LYS ASN VAL ASN ARG LEU MET ALA VAL VAL LEU          
SEQRES  17 A  750  ASP ASP GLN ILE GLN SER VAL ALA THR ILE ASN GLN ARG          
SEQRES  18 A  750  LEU PHE ARG ASP ILE GLN ILE SER GLY ASN PHE THR PRO          
SEQRES  19 A  750  GLU GLU ALA SER GLN LEU ALA CYS VAL LEU LYS SER GLY          
SEQRES  20 A  750  ALA LEU PRO ILE LYS ILE VAL THR ALA ALA GLU ARG SER          
SEQRES  21 A  750  ILE GLY PRO SER LEU GLY ALA ASP ALA ILE ARG SER GLY          
SEQRES  22 A  750  ALA ILE ALA ALA LEU VAL GLY ILE GLY LEU VAL PHE VAL          
SEQRES  23 A  750  MET LEU PHE ALA TYR TYR GLY LEU TRP PHE GLY LEU VAL          
SEQRES  24 A  750  GLY ALA LEU GLY LEU LEU PHE SER SER ILE ILE ILE LEU          
SEQRES  25 A  750  GLY ILE LEU GLY GLY PHE GLY ALA THR LEU THR LEU PRO          
SEQRES  26 A  750  GLY ILE ALA GLY LEU VAL LEU THR ILE GLY ALA ALA VAL          
SEQRES  27 A  750  ASP GLY ASN VAL ILE SER PHE GLU ARG ILE LYS GLU GLU          
SEQRES  28 A  750  LEU ALA ARG GLY LYS GLY ILE LYS ASN ALA ILE GLY ALA          
SEQRES  29 A  750  GLY TYR GLU HIS SER THR ALA ALA ILE LEU ASP VAL ASN          
SEQRES  30 A  750  ALA SER HIS LEU LEU SER ALA LEU ALA LEU TYR ASN TYR          
SEQRES  31 A  750  SER THR GLY ALA VAL LYS GLY PHE ALA VAL THR LEU ILE          
SEQRES  32 A  750  ILE GLY VAL ILE ALA SER THR PHE SER ASN LEU VAL PHE          
SEQRES  33 A  750  ALA LYS TRP PHE MET GLN TRP LEU ALA GLN ARG ARG PRO          
SEQRES  34 A  750  ASN MET SER ALA PRO GLN TRP ILE LYS HIS THR HIS PHE          
SEQRES  35 A  750  ASP PHE MET LYS PRO ALA LYS VAL ILE THR THR LEU SER          
SEQRES  36 A  750  VAL LEU LEU ALA LEU ALA GLY ALA ALA LEU VAL ALA THR          
SEQRES  37 A  750  ARG GLY LEU ASN TYR GLY VAL ASP PHE ALA PRO GLY THR          
SEQRES  38 A  750  THR LEU THR ALA ARG VAL ASP ARG GLN VAL THR THR GLU          
SEQRES  39 A  750  GLN LEU ARG ASN SER VAL ILE GLY ALA GLY VAL SER LYS          
SEQRES  40 A  750  VAL THR GLY GLN SER ALA THR ILE GLN ARG ASP THR THR          
SEQRES  41 A  750  PRO GLY GLN GLN GLY GLN ASN PHE THR VAL LYS VAL PRO          
SEQRES  42 A  750  GLU LEU ASN ASP ALA GLU VAL LYS GLN ILE GLY ALA ALA          
SEQRES  43 A  750  ILE GLY LYS LEU PRO GLN GLY GLN VAL LEU ALA SER GLU          
SEQRES  44 A  750  THR VAL GLY PRO ALA VAL GLY LYS GLU LEU THR GLN LYS          
SEQRES  45 A  750  THR ILE TYR ALA VAL LEU LEU GLY LEU GLY LEU ILE LEU          
SEQRES  46 A  750  VAL TYR VAL GLY PHE ARG PHE ASP PHE ILE MET GLY LEU          
SEQRES  47 A  750  GLY SER ILE ILE ALA ALA ILE HIS ASP VAL ALA ILE ALA          
SEQRES  48 A  750  MET GLY LEU PHE SER LEU LEU GLY LEU GLU PHE THR VAL          
SEQRES  49 A  750  ALA SER VAL ALA ALA LEU LEU THR LEU ILE GLY TYR SER          
SEQRES  50 A  750  LEU ASN ASP SER ILE ILE VAL SER ASP ARG ILE ARG GLU          
SEQRES  51 A  750  ASN MET LYS THR MET ARG GLY HIS SER TYR ARG GLU ILE          
SEQRES  52 A  750  VAL ASN ALA ALA ILE ASN GLN THR LEU SER ARG THR VAL          
SEQRES  53 A  750  MET THR SER VAL SER THR MET LEU PRO LEU ILE SER LEU          
SEQRES  54 A  750  LEU ILE PHE GLY GLY PRO VAL LEU ARG ASP PHE SER LEU          
SEQRES  55 A  750  ILE LEU LEU VAL GLY ILE LEU VAL GLY THR TYR SER SER          
SEQRES  56 A  750  ILE TYR ILE VAL ALA PRO LEU VAL VAL TYR PHE GLU GLU          
SEQRES  57 A  750  TRP ARG ASP LYS ASN ARG ALA ALA LYS PRO VAL THR ASN          
SEQRES  58 A  750  SER HIS HIS HIS HIS HIS HIS HIS HIS                          
HET    OLC  A 801      20                                                       
HET    OLC  A 802      20                                                       
HET    OLC  A 803      20                                                       
HET    OLC  A 804       8                                                       
HET    OLC  A 805      17                                                       
HET    OLC  A 806      25                                                       
HET    OLC  A 807      15                                                       
HET    PEG  A 808       7                                                       
HETNAM     OLC (2R)-2,3-DIHYDROXYPROPYL (9Z)-OCTADEC-9-ENOATE                   
HETNAM     PEG DI(HYDROXYETHYL)ETHER                                            
HETSYN     OLC 1-OLEOYL-R-GLYCEROL                                              
FORMUL   2  OLC    7(C21 H40 O4)                                                
FORMUL   9  PEG    C4 H10 O3                                                    
FORMUL  10  HOH   *52(H2 O)                                                     
HELIX    1 AA1 ASN A   31  ARG A   51  1                                  21    
HELIX    2 AA2 PRO A   52  LYS A   56  5                                   5    
HELIX    3 AA3 GLY A   73  GLY A   78  1                                   6    
HELIX    4 AA4 THR A   92  LEU A  110  1                                  19    
HELIX    5 AA5 THR A  133  GLN A  146  1                                  14    
HELIX    6 AA6 ASP A  162  ASN A  169  1                                   8    
HELIX    7 AA7 THR A  176  LEU A  180  5                                   5    
HELIX    8 AA8 THR A  211  GLY A  223  1                                  13    
HELIX    9 AA9 THR A  259  GLY A  273  1                                  15    
HELIX   10 AB1 GLY A  288  PHE A  344  1                                  57    
HELIX   11 AB2 THR A  349  ALA A  363  1                                  15    
HELIX   12 AB3 VAL A  364  ARG A  380  1                                  17    
HELIX   13 AB4 GLY A  383  TYR A  416  1                                  34    
HELIX   14 AB5 THR A  418  ARG A  454  1                                  37    
HELIX   15 AB6 PRO A  473  ARG A  495  1                                  23    
HELIX   16 AB7 THR A  518  GLY A  528  1                                  11    
HELIX   17 AB8 ASN A  562  LEU A  576  1                                  15    
HELIX   18 AB9 GLY A  588  PHE A  618  1                                  31    
HELIX   19 AC1 ASP A  619  GLY A  645  1                                  27    
HELIX   20 AC2 THR A  649  MET A  681  1                                  33    
HELIX   21 AC3 SER A  685  THR A  697  1                                  13    
HELIX   22 AC4 THR A  697  GLY A  719  1                                  23    
HELIX   23 AC5 GLY A  720  ILE A  744  1                                  25    
HELIX   24 AC6 ILE A  744  ARG A  760  1                                  17    
SHEET    1 AA1 2 TRP A  63  ASN A  64  0                                        
SHEET    2 AA1 2 TYR A  67  GLN A  68 -1  O  TYR A  67   N  ASN A  64           
SHEET    1 AA2 2 THR A  71  LEU A  72  0                                        
SHEET    2 AA2 2 THR A 347  LEU A 348  1  O  LEU A 348   N  THR A  71           
SHEET    1 AA3 8 THR A 116  SER A 120  0                                        
SHEET    2 AA3 8 ARG A 124  PRO A 130 -1  O  VAL A 126   N  THR A 118           
SHEET    3 AA3 8 GLY A  79  PRO A  86 -1  N  LEU A  84   O  VAL A 125           
SHEET    4 AA3 8 ILE A 279  ILE A 287 -1  O  ARG A 285   N  ARG A  81           
SHEET    5 AA3 8 GLN A 580  VAL A 587 -1  O  SER A 584   N  SER A 286           
SHEET    6 AA3 8 GLY A 506  VAL A 513 -1  N  ARG A 512   O  GLN A 580           
SHEET    7 AA3 8 GLN A 552  VAL A 558 -1  O  GLN A 552   N  VAL A 513           
SHEET    8 AA3 8 THR A 540  ARG A 543 -1  N  GLN A 542   O  THR A 555           
SHEET    1 AA4 4 ALA A 185  THR A 186  0                                        
SHEET    2 AA4 4 LEU A 150  ILE A 154 -1  N  PHE A 152   O  ALA A 185           
SHEET    3 AA4 4 LEU A 229  LEU A 234 -1  O  VAL A 233   N  GLU A 151           
SHEET    4 AA4 4 GLN A 237  THR A 243 -1  O  ALA A 242   N  MET A 230           
SHEET    1 AA5 3 ILE A 190  THR A 197  0                                        
SHEET    2 AA5 3 TRP A 204  THR A 210 -1  O  VAL A 205   N  GLY A 196           
SHEET    3 AA5 3 ASP A 251  PHE A 258 -1  O  ILE A 252   N  PHE A 208           
SHEET    1 AA6 2 ASN A 498  TYR A 499  0                                        
SHEET    2 AA6 2 GLU A 647  PHE A 648  1  O  PHE A 648   N  ASN A 498           
SSBOND   1 CYS A  143    CYS A  268                          1555   1555  2.05  
SITE     1 AC1  7 PRO A  32  ALA A  35  VAL A 305  ILE A 335                    
SITE     2 AC1  7 PHE A 442  TRP A 445  PHE A 718                               
SITE     1 AC2  6 LEU A  47  TRP A  53  PHE A 315  ALA A 316                    
SITE     2 AC2  6 GLY A 319  PRO A 460                                          
SITE     1 AC3  4 PHE A 468  ASP A 469  PRO A 473  TYR A 743                    
SITE     1 AC4  4 ASN A 415  LYS A 475  THR A 479  TYR A 751                    
SITE     1 AC5  7 TYR A 416  LYS A 472  VAL A 476  TYR A 601                    
SITE     2 AC5  7 LEU A 604  LEU A 605  GLY A 608                               
SITE     1 AC6  9 LEU A  40  THR A  41  SER A  45  TYR A  48                    
SITE     2 AC6  9 GLY A 339  GLY A 343  PHE A 344  GLY A 345                    
SITE     3 AC6  9 ASN A 759                                                     
SITE     1 AC7  8 TRP A  63  ILE A 296  ALA A 303  SER A 334                    
SITE     2 AC7  8 ILE A 337  ILE A 353  LEU A 356  ILE A 360                    
SITE     1 AC8  1 TYR A 317                                                     
CRYST1  208.265   69.807   66.169  90.00  94.86  90.00 C 1 2 1       4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.004802  0.000000  0.000408        0.00000                         
SCALE2      0.000000  0.014325  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.015167        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system