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Database: PDB
Entry: 3E7X
LinkDB: 3E7X
Original site: 3E7X 
HEADER    LIGASE                                  19-AUG-08   3E7X              
TITLE     CRYSTAL STRUCTURE OF DLTA: IMPLICATIONS FOR THE REACTION              
TITLE    2 MECHANISM OF NON-RIBOSOMAL PEPTIDE SYNTHETASE (NRPS)                 
TITLE    3 ADENYLATION DOMAINS                                                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: D-ALANINE--POLY(PHOSPHORIBITOL) LIGASE SUBUNIT 1;          
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: DLTA PROTEIN, D-ALANINE-ACTIVATING ENZYME, DAE, D-          
COMPND   5 ALANINE-D-ALANYL CARRIER PROTEIN LIGASE, DCL;                        
COMPND   6 EC: 6.1.1.13;                                                        
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS;                              
SOURCE   3 ORGANISM_TAXID: 1423;                                                
SOURCE   4 GENE: DLTA;                                                          
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: M15;                                       
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PQE60                                     
KEYWDS    DLTA, NON-RIBOSOMAL PEPTIDE SYNTHETASE, NRPS, ADENYLATION             
KEYWDS   2 DOMAIN, D-ALANYLATION, D-ALANINE-DALANYL, AMP, CYTOPLASM,            
KEYWDS   3 LIGASE                                                               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    H.YONUS,P.NEUMANN,S.ZIMMERMANN,J.J.MAY,M.A.MARAHIEL,                  
AUTHOR   2 M.T.STUBBS                                                           
REVDAT   2   30-DEC-08 3E7X    1       JRNL   VERSN                             
REVDAT   1   09-SEP-08 3E7X    0                                                
JRNL        AUTH   H.YONUS,P.NEUMANN,S.ZIMMERMANN,J.J.MAY,                      
JRNL        AUTH 2 M.A.MARAHIEL,M.T.STUBBS                                      
JRNL        TITL   CRYSTAL STRUCTURE OF DLTA. IMPLICATIONS FOR THE              
JRNL        TITL 2 REACTION MECHANISM OF NON-RIBOSOMAL PEPTIDE                  
JRNL        TITL 3 SYNTHETASE ADENYLATION DOMAINS                               
JRNL        REF    J.BIOL.CHEM.                  V. 283 32484 2008              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   18784082                                                     
JRNL        DOI    10.1074/JBC.M800557200                                       
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.1                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,             
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.92                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 2190991.000                    
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 97.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 15932                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.179                           
REMARK   3   FREE R VALUE                     : 0.238                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 6.500                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1037                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.007                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.60                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.64                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.30                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 755                          
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2550                       
REMARK   3   BIN FREE R VALUE                    : 0.3280                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 6.60                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 53                           
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.045                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4035                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 23                                      
REMARK   3   SOLVENT ATOMS            : 211                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 34.72                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 39.41                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.18000                                             
REMARK   3    B22 (A**2) : -3.63000                                             
REMARK   3    B33 (A**2) : 4.81000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.26                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.43                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 3.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.38                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.54                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.006                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.30                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 23.50                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.84                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : GROUP                                     
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.34                                                 
REMARK   3   BSOL        : 49.51                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  3  : AMP.PARAM                                      
REMARK   3  PARAMETER FILE  4  : ION.PARAM                                      
REMARK   3  PARAMETER FILE  5  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : AMP.TOP                                        
REMARK   3  TOPOLOGY FILE  3   : ION.TOP                                        
REMARK   3  TOPOLOGY FILE  4   : NULL                                           
REMARK   3  TOPOLOGY FILE  5   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3E7X COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 26-AUG-08.                  
REMARK 100 THE RCSB ID CODE IS RCSB048987.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-APR-05                          
REMARK 200  TEMPERATURE           (KELVIN) : 180                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : BESSY                              
REMARK 200  BEAMLINE                       : 14.1                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.91438                            
REMARK 200  MONOCHROMATOR                  : GRAPHITE                           
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MAR CCD 165 MM                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XSCALE                             
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 15976                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.5                               
REMARK 200  DATA REDUNDANCY                : 3.010                              
REMARK 200  R MERGE                    (I) : 0.04700                            
REMARK 200  R SYM                      (I) : 0.05800                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 19.4900                            
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) : 2.68                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.89                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.21800                            
REMARK 200  R SYM FOR SHELL            (I) : 0.26900                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 5.300                              
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: PDB CODE 3E7W                                        
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 44.86                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.23                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG 1000, PH 6.5, VAPOR              
REMARK 280  DIFFUSION, SITTING DROP, TEMPERATURE 293K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       22.88250            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       60.73550            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       45.69450            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       60.73550            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       22.88250            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       45.69450            
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 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     HIS A   509                                                      
REMARK 465     HIS A   510                                                      
REMARK 465     HIS A   511                                                      
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    TYR A  14       71.86   -119.79                                   
REMARK 500    GLN A  23       73.03     52.80                                   
REMARK 500    HIS A  60      -94.43   -118.91                                   
REMARK 500    ALA A 106       -7.18    -32.83                                   
REMARK 500    LEU A 109     -160.56    -59.97                                   
REMARK 500    SER A 110     -157.84   -137.93                                   
REMARK 500    ASP A 112       61.60     67.42                                   
REMARK 500    ALA A 113      -97.40   -104.04                                   
REMARK 500    GLN A 117       75.01   -102.80                                   
REMARK 500    LEU A 127       -0.91    -56.72                                   
REMARK 500    GLU A 130     -116.59    -95.90                                   
REMARK 500    SER A 133      113.46   -162.61                                   
REMARK 500    GLN A 136      -35.92    -33.89                                   
REMARK 500    TRP A 139      139.47    -36.91                                   
REMARK 500    GLU A 142     -122.32     48.38                                   
REMARK 500    PRO A 223      -37.09    -39.58                                   
REMARK 500    LEU A 259       79.08   -118.89                                   
REMARK 500    THR A 299       68.84     63.43                                   
REMARK 500    VAL A 300      -76.68     73.15                                   
REMARK 500    PRO A 325      -39.30    -28.06                                   
REMARK 500    ILE A 331       77.64   -119.59                                   
REMARK 500    ASP A 398     -158.87   -105.08                                   
REMARK 500    ASN A 434      -71.61    -70.75                                   
REMARK 500    HIS A 449     -141.51   -113.79                                   
REMARK 500    PHE A 451      170.04    -57.72                                   
REMARK 500    GLU A 452      -91.52    -98.08                                   
REMARK 500    LYS A 453     -176.47    -67.17                                   
REMARK 500    PHE A 455        2.49    -64.06                                   
REMARK 500    ILE A 492      153.03    -43.01                                   
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 AMP A 512                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1AMU   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1MD9   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2DLS   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1BA3   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1PG4   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1HQB   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3E7W   RELATED DB: PDB                                   
DBREF  3E7X A    1   503  UNP    P39581   DLTA_BACSU       1    503             
SEQADV 3E7X ARG A  504  UNP  P39581              EXPRESSION TAG                 
SEQADV 3E7X SER A  505  UNP  P39581              EXPRESSION TAG                 
SEQADV 3E7X HIS A  506  UNP  P39581              EXPRESSION TAG                 
SEQADV 3E7X HIS A  507  UNP  P39581              EXPRESSION TAG                 
SEQADV 3E7X HIS A  508  UNP  P39581              EXPRESSION TAG                 
SEQADV 3E7X HIS A  509  UNP  P39581              EXPRESSION TAG                 
SEQADV 3E7X HIS A  510  UNP  P39581              EXPRESSION TAG                 
SEQADV 3E7X HIS A  511  UNP  P39581              EXPRESSION TAG                 
SEQRES   1 A  511  MET LYS LEU LEU HIS ALA ILE GLN THR HIS ALA GLU THR          
SEQRES   2 A  511  TYR PRO GLN THR ASP ALA PHE ARG SER GLN GLY GLN SER          
SEQRES   3 A  511  LEU THR TYR GLN GLU LEU TRP GLU GLN SER ASP ARG ALA          
SEQRES   4 A  511  ALA ALA ALA ILE GLN LYS ARG ILE SER GLY GLU LYS LYS          
SEQRES   5 A  511  SER PRO ILE LEU VAL TYR GLY HIS MET GLU PRO HIS MET          
SEQRES   6 A  511  ILE VAL SER PHE LEU GLY SER VAL LYS ALA GLY HIS PRO          
SEQRES   7 A  511  TYR ILE PRO VAL ASP LEU SER ILE PRO SER GLU ARG ILE          
SEQRES   8 A  511  ALA LYS ILE ILE GLU SER SER GLY ALA GLU LEU LEU ILE          
SEQRES   9 A  511  HIS ALA ALA GLY LEU SER ILE ASP ALA VAL GLY GLN GLN          
SEQRES  10 A  511  ILE GLN THR VAL SER ALA GLU GLU LEU LEU GLU ASN GLU          
SEQRES  11 A  511  GLY GLY SER VAL SER GLN ASP GLN TRP VAL LYS GLU HIS          
SEQRES  12 A  511  GLU THR PHE TYR ILE ILE TYR THR SER GLY SER THR GLY          
SEQRES  13 A  511  ASN PRO LYS GLY VAL GLN ILE SER ALA ALA ASN LEU GLN          
SEQRES  14 A  511  SER PHE THR ASP TRP ILE CYS ALA ASP PHE PRO VAL SER          
SEQRES  15 A  511  GLY GLY LYS ILE PHE LEU ASN GLN ALA PRO PHE SER PHE          
SEQRES  16 A  511  ASP LEU SER VAL MET ASP LEU TYR PRO CYS LEU GLN SER          
SEQRES  17 A  511  GLY GLY THR LEU HIS CYS VAL THR LYS ASP ALA VAL ASN          
SEQRES  18 A  511  LYS PRO LYS VAL LEU PHE GLU GLU LEU LYS LYS SER GLY          
SEQRES  19 A  511  LEU ASN VAL TRP THR SER THR PRO SER PHE VAL GLN MET          
SEQRES  20 A  511  CYS LEU MET ASP PRO GLY PHE SER GLN ASP LEU LEU PRO          
SEQRES  21 A  511  HIS ALA ASP THR PHE MET PHE CYS GLY GLU VAL LEU PRO          
SEQRES  22 A  511  VAL SER VAL ALA LYS ALA LEU LEU GLU ARG PHE PRO LYS          
SEQRES  23 A  511  ALA LYS ILE PHE ASN THR TYR GLY PRO THR GLU ALA THR          
SEQRES  24 A  511  VAL ALA VAL THR SER VAL GLU ILE THR ASN ASP VAL ILE          
SEQRES  25 A  511  SER ARG SER GLU SER LEU PRO VAL GLY PHE ALA LYS PRO          
SEQRES  26 A  511  ASP MET ASN ILE PHE ILE MET ASP GLU GLU GLY GLN PRO          
SEQRES  27 A  511  LEU PRO GLU GLY GLU LYS GLY GLU ILE VAL ILE ALA GLY          
SEQRES  28 A  511  PRO SER VAL SER ARG GLY TYR LEU GLY GLU PRO GLU LEU          
SEQRES  29 A  511  THR GLU LYS ALA PHE PHE SER HIS GLU GLY GLN TRP ALA          
SEQRES  30 A  511  TYR ARG THR GLY ASP ALA GLY PHE ILE GLN ASP GLY GLN          
SEQRES  31 A  511  ILE PHE CYS GLN GLY ARG LEU ASP PHE GLN ILE LYS LEU          
SEQRES  32 A  511  HIS GLY TYR ARG MET GLU LEU GLU GLU ILE GLU PHE HIS          
SEQRES  33 A  511  VAL ARG GLN SER GLN TYR VAL ARG SER ALA VAL VAL ILE          
SEQRES  34 A  511  PRO TYR GLN PRO ASN GLY THR VAL GLU TYR LEU ILE ALA          
SEQRES  35 A  511  ALA ILE VAL PRO GLU GLU HIS GLU PHE GLU LYS GLU PHE          
SEQRES  36 A  511  GLN LEU THR SER ALA ILE LYS LYS GLU LEU ALA ALA SER          
SEQRES  37 A  511  LEU PRO ALA TYR MET ILE PRO ARG LYS PHE ILE TYR GLN          
SEQRES  38 A  511  ASP HIS ILE GLN MET THR ALA ASN GLY LYS ILE ASP ARG          
SEQRES  39 A  511  LYS ARG ILE GLY GLU GLU VAL LEU VAL ARG SER HIS HIS          
SEQRES  40 A  511  HIS HIS HIS HIS                                              
HET    AMP  A 512      23                                                       
HETNAM     AMP ADENOSINE MONOPHOSPHATE                                          
FORMUL   2  AMP    C10 H14 N5 O7 P                                              
FORMUL   3  HOH   *211(H2 O)                                                    
HELIX    1   1 LYS A    2  TYR A   14  1                                  13    
HELIX    2   2 TYR A   29  GLN A   44  1                                  16    
HELIX    3   3 GLU A   62  ALA A   75  1                                  14    
HELIX    4   4 PRO A   87  GLY A   99  1                                  13    
HELIX    5   5 ALA A  123  LEU A  127  1                                   5    
HELIX    6   6 ALA A  165  PHE A  179  1                                  15    
HELIX    7   7 ASP A  196  SER A  208  1                                  13    
HELIX    8   8 THR A  216  ASN A  221  1                                   6    
HELIX    9   9 LYS A  222  GLY A  234  1                                  13    
HELIX   10  10 THR A  241  LEU A  249  1                                   9    
HELIX   11  11 PRO A  273  PHE A  284  1                                  12    
HELIX   12  12 PRO A  295  THR A  299  5                                   5    
HELIX   13  13 THR A  308  ARG A  314  1                                   7    
HELIX   14  14 GLU A  361  ALA A  368  1                                   8    
HELIX   15  15 LEU A  410  GLN A  419  1                                  10    
HELIX   16  16 LYS A  453  LEU A  469  1                                  17    
HELIX   17  17 PRO A  470  ILE A  474  5                                   5    
HELIX   18  18 THR A  487  LYS A  491  5                                   5    
HELIX   19  19 ASP A  493  SER A  505  1                                  13    
SHEET    1   A 4 GLN A  25  THR A  28  0                                        
SHEET    2   A 4 ASP A  18  SER A  22 -1  N  ALA A  19   O  LEU A  27           
SHEET    3   A 4 THR A 211  CYS A 214  1  O  LEU A 212   N  ARG A  21           
SHEET    4   A 4 ILE A 186  ASN A 189  1  N  PHE A 187   O  HIS A 213           
SHEET    1   B 4 TYR A  79  ASP A  83  0                                        
SHEET    2   B 4 ILE A  55  GLY A  59  1  N  VAL A  57   O  VAL A  82           
SHEET    3   B 4 LEU A 102  HIS A 105  1  O  ILE A 104   N  TYR A  58           
SHEET    4   B 4 THR A 120  SER A 122  1  O  VAL A 121   N  HIS A 105           
SHEET    1   C 2 THR A 145  THR A 151  0                                        
SHEET    2   C 2 LYS A 159  SER A 164 -1  O  ILE A 163   N  PHE A 146           
SHEET    1   D 5 VAL A 237  SER A 240  0                                        
SHEET    2   D 5 THR A 264  PHE A 267  1  O  MET A 266   N  TRP A 238           
SHEET    3   D 5 LYS A 288  ASN A 291  1  O  LYS A 288   N  PHE A 265           
SHEET    4   D 5 THR A 303  ILE A 307 -1  O  VAL A 305   N  ASN A 291           
SHEET    5   D 5 PHE A 322  ALA A 323 -1  O  PHE A 322   N  SER A 304           
SHEET    1   E 4 ASN A 328  MET A 332  0                                        
SHEET    2   E 4 GLY A 345  ALA A 350 -1  O  ALA A 350   N  ASN A 328           
SHEET    3   E 4 GLN A 375  GLN A 387 -1  O  GLY A 384   N  GLY A 345           
SHEET    4   E 4 PHE A 369  HIS A 372 -1  N  PHE A 370   O  ALA A 377           
SHEET    1   F 4 ASN A 328  MET A 332  0                                        
SHEET    2   F 4 GLY A 345  ALA A 350 -1  O  ALA A 350   N  ASN A 328           
SHEET    3   F 4 GLN A 375  GLN A 387 -1  O  GLY A 384   N  GLY A 345           
SHEET    4   F 4 GLN A 390  ARG A 396 -1  O  GLY A 395   N  ALA A 383           
SHEET    1   G 2 GLN A 400  LEU A 403  0                                        
SHEET    2   G 2 TYR A 406  GLU A 409 -1  O  MET A 408   N  ILE A 401           
SHEET    1   H 3 VAL A 423  TYR A 431  0                                        
SHEET    2   H 3 TYR A 439  PRO A 446 -1  O  ILE A 441   N  ILE A 429           
SHEET    3   H 3 LYS A 477  TYR A 480  1  O  LYS A 477   N  ALA A 442           
SITE     1 AC1 16 GLY A 269  GLU A 270  ASN A 291  THR A 292                    
SITE     2 AC1 16 TYR A 293  GLY A 294  PRO A 295  THR A 296                    
SITE     3 AC1 16 ASP A 382  ARG A 396  LYS A 402  ARG A 407                    
SITE     4 AC1 16 HOH A 515  HOH A 529  HOH A 658  HOH A 718                    
CRYST1   45.765   91.389  121.471  90.00  90.00  90.00 P 21 21 21    4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.021851  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010942  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008232        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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