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Database: PDB
Entry: 5BPH
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HEADER    LIGASE                                  28-MAY-15   5BPH              
TITLE     CRYSTAL STRUCTURE OF AMP COMPLEXED D-ALANINE-D-ALANINE LIGASE(DDL)    
TITLE    2 FROM YERSINIA PESTIS                                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: D-ALANINE--D-ALANINE LIGASE;                               
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 SYNONYM: D-ALA-D-ALA LIGASE,D-ALANYLALANINE SYNTHETASE;              
COMPND   5 EC: 6.3.2.4;                                                         
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: YERSINIA PESTIS;                                
SOURCE   3 ORGANISM_TAXID: 632;                                                 
SOURCE   4 GENE: DDL, DDLB, YPO0557, Y3624, YP_3627;                            
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    D-ALANINE-D-ALANINE LIGASE (DDL), DRUG TARGET; BACTERIAL CELL WALL    
KEYWDS   2 SYNTHESIS, LIGASE                                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    H.T.TRAN,L.W.KANG,M.K.HONG                                            
REVDAT   1   02-MAR-16 5BPH    0                                                
JRNL        AUTH   H.T.TRAN,M.K.HONG,H.P.NGO,K.H.HUYNH,Y.J.AHN,Z.WANG,L.W.KANG  
JRNL        TITL   STRUCTURE OF D-ALANINE-D-ALANINE LIGASE FROM YERSINIA        
JRNL        TITL 2 PESTIS: NUCLEOTIDE PHOSPHATE RECOGNITION BY THE SERINE LOOP. 
JRNL        REF    ACTA CRYSTALLOGR D STRUCT     V.  72    12 2016              
JRNL        REF  2 BIOL                                                         
JRNL        REFN                   ISSN 2059-7983                               
JRNL        PMID   26894530                                                     
JRNL        DOI    10.1107/S2059798315021671                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.7.0032                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 34.96                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 145553                         
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 + TEST SET) : 0.179                           
REMARK   3   R VALUE            (WORKING SET) : 0.177                           
REMARK   3   FREE R VALUE                     : 0.209                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 7688                            
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) : 1.70                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.75                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 10221                        
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 96.02                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2560                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 522                          
REMARK   3   BIN FREE R VALUE                    : 0.3070                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 9296                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 163                                     
REMARK   3   SOLVENT ATOMS            : 730                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 30.53                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.00000                                              
REMARK   3    B22 (A**2) : 0.00000                                              
REMARK   3    B33 (A**2) : 0.00000                                              
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 OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.096         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.096         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.066         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.019         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.966                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.957                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  9654 ; 0.022 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  9205 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 13067 ; 2.179 ; 1.997       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 21233 ; 0.942 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1214 ; 6.285 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   391 ;35.586 ;25.013       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1598 ;13.411 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    36 ;16.416 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1491 ; 0.130 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 10822 ; 0.011 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  2046 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  4880 ; 2.816 ; 2.745       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  4877 ; 2.814 ; 2.745       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  6082 ; 3.713 ; 4.106       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  6083 ; 3.713 ; 4.106       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  4774 ; 4.289 ; 3.271       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  4775 ; 4.288 ; 3.271       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  6986 ; 6.252 ; 4.724       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2): 11265 ; 7.744 ;23.649       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2): 11216 ; 7.744 ;23.594       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 5BPH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 04-JUN-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000210321.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 28-MAY-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : PAL/PLS                            
REMARK 200  BEAMLINE                       : 5C (4A)                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.997                              
REMARK 200  MONOCHROMATOR                  : DCM SI (111) CRYSTAL               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : NULL                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.700                              
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     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 14.80                              
REMARK 200  R MERGE                    (I) : 0.07000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 50.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
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: NULL                         
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: ORTHORHOMBIC SHAPED CRYSTAL                                  
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 53.33                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.64                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M SODIUM ACETATE, 0.1 M BIS-TRIS     
REMARK 280  PH 7.0, 29% PEG 8000, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE    
REMARK 280  287K                                                                
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       31.29250            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      105.38450            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       53.03550            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      105.38450            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       31.29250            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       53.03550            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, D                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, C                                  
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 B     1                                                      
REMARK 465     GLY D   149                                                      
REMARK 465     TYR D   216                                                      
REMARK 465     LEU D   217                                                      
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   N    MET A     1     O    HOH A   501              2.19            
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    GLN A 105   CD    GLN A 105   NE2     0.158                       
REMARK 500    GLY B 185   N     GLY B 185   CA      0.135                       
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    ASP A  69   CB  -  CG  -  OD1 ANGL. DEV. =   5.6 DEGREES          
REMARK 500    MET A  89   CG  -  SD  -  CE  ANGL. DEV. = -30.2 DEGREES          
REMARK 500    GLN A 105   CA  -  CB  -  CG  ANGL. DEV. =  14.2 DEGREES          
REMARK 500    ASP A 261   CB  -  CG  -  OD1 ANGL. DEV. =   6.5 DEGREES          
REMARK 500    GLY B 185   N   -  CA  -  C   ANGL. DEV. = -17.8 DEGREES          
REMARK 500    ARG B 255   NE  -  CZ  -  NH1 ANGL. DEV. =   3.6 DEGREES          
REMARK 500    MET B 259   CA  -  CB  -  CG  ANGL. DEV. =  18.3 DEGREES          
REMARK 500    ARG C  16   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES          
REMARK 500    ASP C  96   CB  -  CG  -  OD1 ANGL. DEV. =   5.6 DEGREES          
REMARK 500    MET D  89   CG  -  SD  -  CE  ANGL. DEV. = -31.1 DEGREES          
REMARK 500    ARG D 255   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.8 DEGREES          
REMARK 500    ASP D 261   CB  -  CG  -  OD1 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    ARG D 300   NE  -  CZ  -  NH1 ANGL. DEV. =   4.0 DEGREES          
REMARK 500    ARG D 300   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.7 DEGREES          
REMARK 500    MET D 303   CG  -  SD  -  CE  ANGL. DEV. = -28.0 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    ASP A 249       30.91     70.03                                   
REMARK 500    GLU B 148      123.20   -178.27                                   
REMARK 500    SER B 150     -130.78   -131.05                                   
REMARK 500    VAL B 208      -54.52     66.71                                   
REMARK 500    ASP B 211     -169.15   -125.34                                   
REMARK 500    SER D 151     -139.04    -64.86                                   
REMARK 500    TYR D 212      -50.05    149.44                                   
REMARK 500    LEU D 269      -60.35   -102.91                                   
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 SER B  184     GLY B  185                 -145.15                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA A 402  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A  68   O                                                      
REMARK 620 2 SER A  91   O    79.4                                              
REMARK 620 3 THR A  94   OG1 151.4  73.1                                        
REMARK 620 4 THR A 273   OG1  85.1 118.5 100.8                                  
REMARK 620 5 HOH A 575   O   113.3 155.4  95.2  84.4                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA B 402  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU B  68   O                                                      
REMARK 620 2 SER B  91   O    79.3                                              
REMARK 620 3 THR B  94   OG1 152.1  75.2                                        
REMARK 620 4 THR B 273   OG1  82.0 114.8  98.5                                  
REMARK 620 5 HOH B 566   O   110.6 158.1  97.2  86.5                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA C 402  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU C  68   O                                                      
REMARK 620 2 SER C  91   O    80.1                                              
REMARK 620 3 THR C  94   OG1 153.3  74.9                                        
REMARK 620 4 THR C 273   OG1  85.3 117.3  97.9                                  
REMARK 620 5 HOH C 551   O   111.4 157.8  95.2  83.4                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA D 402  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU D  68   O                                                      
REMARK 620 2 SER D  91   O    80.3                                              
REMARK 620 3 THR D  94   OG1 152.2  74.4                                        
REMARK 620 4 THR D 273   OG1  83.9 118.5  98.1                                  
REMARK 620 5 HOH D 558   O   113.7 156.4  94.1  83.0                            
REMARK 620 N                    1     2     3     4                             
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 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 402                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT A 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 405                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 406                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue AMP B 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NA B 402                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT B 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT B 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 405                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue AMP C 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NA C 402                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT C 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 405                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue AMP D 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NA D 402                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT D 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL D 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL D 405                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT D 406                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5BPF   RELATED DB: PDB                                   
DBREF  5BPH A    1   306  UNP    Q8ZIE7   DDL_YERPE        1    306             
DBREF  5BPH B    1   306  UNP    Q8ZIE7   DDL_YERPE        1    306             
DBREF  5BPH C    1   306  UNP    Q8ZIE7   DDL_YERPE        1    306             
DBREF  5BPH D    1   306  UNP    Q8ZIE7   DDL_YERPE        1    306             
SEQRES   1 A  306  MET ALA GLU LYS VAL ALA VAL LEU LEU GLY GLY THR SER          
SEQRES   2 A  306  ALA GLU ARG GLU VAL SER LEU LEU SER GLY GLN ALA VAL          
SEQRES   3 A  306  LEU ALA GLY LEU LYS GLU ALA GLY ILE ASP ALA TYR GLY          
SEQRES   4 A  306  VAL ASP THR LYS ASP PHE PRO VAL THR GLN LEU LYS GLU          
SEQRES   5 A  306  GLN GLY PHE ASP LYS VAL PHE ILE ALA LEU HIS GLY ARG          
SEQRES   6 A  306  GLY GLY GLU ASP GLY THR LEU GLN GLY VAL LEU GLU PHE          
SEQRES   7 A  306  LEU GLN LEU PRO TYR THR GLY SER GLY VAL MET ALA SER          
SEQRES   8 A  306  ALA LEU THR MET ASP LYS LEU ARG THR LYS LEU VAL TRP          
SEQRES   9 A  306  GLN ALA LEU GLY LEU PRO ILE SER PRO TYR VAL ALA LEU          
SEQRES  10 A  306  ASN ARG GLN GLN PHE GLU THR LEU SER PRO GLU GLU LEU          
SEQRES  11 A  306  VAL ALA CYS VAL ALA LYS LEU GLY LEU PRO LEU ILE VAL          
SEQRES  12 A  306  LYS PRO SER HIS GLU GLY SER SER VAL GLY MET SER LYS          
SEQRES  13 A  306  VAL ASP HIS ALA SER GLU LEU GLN LYS ALA LEU VAL GLU          
SEQRES  14 A  306  ALA PHE GLN HIS ASP SER ASP VAL LEU ILE GLU LYS TRP          
SEQRES  15 A  306  LEU SER GLY PRO GLU PHE THR VAL ALA ILE LEU GLY ASP          
SEQRES  16 A  306  GLU VAL LEU PRO SER ILE ARG ILE GLN PRO PRO GLY VAL          
SEQRES  17 A  306  PHE TYR ASP TYR ASP ALA LYS TYR LEU SER ASP LYS THR          
SEQRES  18 A  306  GLN TYR PHE CYS PRO SER GLY LEU SER ASP GLU SER GLU          
SEQRES  19 A  306  GLN GLN LEU ALA ALA LEU ALA LEU GLN ALA TYR HIS ALA          
SEQRES  20 A  306  LEU ASP CYS SER GLY TRP GLY ARG VAL ASP VAL MET GLN          
SEQRES  21 A  306  ASP ARG ASP GLY HIS PHE TYR LEU LEU GLU VAL ASN THR          
SEQRES  22 A  306  SER PRO GLY MET THR SER HIS SER LEU VAL PRO MET ALA          
SEQRES  23 A  306  ALA ARG GLN TYR GLY LEU SER PHE SER GLN LEU VAL ALA          
SEQRES  24 A  306  ARG ILE LEU MET LEU ALA ASP                                  
SEQRES   1 B  306  MET ALA GLU LYS VAL ALA VAL LEU LEU GLY GLY THR SER          
SEQRES   2 B  306  ALA GLU ARG GLU VAL SER LEU LEU SER GLY GLN ALA VAL          
SEQRES   3 B  306  LEU ALA GLY LEU LYS GLU ALA GLY ILE ASP ALA TYR GLY          
SEQRES   4 B  306  VAL ASP THR LYS ASP PHE PRO VAL THR GLN LEU LYS GLU          
SEQRES   5 B  306  GLN GLY PHE ASP LYS VAL PHE ILE ALA LEU HIS GLY ARG          
SEQRES   6 B  306  GLY GLY GLU ASP GLY THR LEU GLN GLY VAL LEU GLU PHE          
SEQRES   7 B  306  LEU GLN LEU PRO TYR THR GLY SER GLY VAL MET ALA SER          
SEQRES   8 B  306  ALA LEU THR MET ASP LYS LEU ARG THR LYS LEU VAL TRP          
SEQRES   9 B  306  GLN ALA LEU GLY LEU PRO ILE SER PRO TYR VAL ALA LEU          
SEQRES  10 B  306  ASN ARG GLN GLN PHE GLU THR LEU SER PRO GLU GLU LEU          
SEQRES  11 B  306  VAL ALA CYS VAL ALA LYS LEU GLY LEU PRO LEU ILE VAL          
SEQRES  12 B  306  LYS PRO SER HIS GLU GLY SER SER VAL GLY MET SER LYS          
SEQRES  13 B  306  VAL ASP HIS ALA SER GLU LEU GLN LYS ALA LEU VAL GLU          
SEQRES  14 B  306  ALA PHE GLN HIS ASP SER ASP VAL LEU ILE GLU LYS TRP          
SEQRES  15 B  306  LEU SER GLY PRO GLU PHE THR VAL ALA ILE LEU GLY ASP          
SEQRES  16 B  306  GLU VAL LEU PRO SER ILE ARG ILE GLN PRO PRO GLY VAL          
SEQRES  17 B  306  PHE TYR ASP TYR ASP ALA LYS TYR LEU SER ASP LYS THR          
SEQRES  18 B  306  GLN TYR PHE CYS PRO SER GLY LEU SER ASP GLU SER GLU          
SEQRES  19 B  306  GLN GLN LEU ALA ALA LEU ALA LEU GLN ALA TYR HIS ALA          
SEQRES  20 B  306  LEU ASP CYS SER GLY TRP GLY ARG VAL ASP VAL MET GLN          
SEQRES  21 B  306  ASP ARG ASP GLY HIS PHE TYR LEU LEU GLU VAL ASN THR          
SEQRES  22 B  306  SER PRO GLY MET THR SER HIS SER LEU VAL PRO MET ALA          
SEQRES  23 B  306  ALA ARG GLN TYR GLY LEU SER PHE SER GLN LEU VAL ALA          
SEQRES  24 B  306  ARG ILE LEU MET LEU ALA ASP                                  
SEQRES   1 C  306  MET ALA GLU LYS VAL ALA VAL LEU LEU GLY GLY THR SER          
SEQRES   2 C  306  ALA GLU ARG GLU VAL SER LEU LEU SER GLY GLN ALA VAL          
SEQRES   3 C  306  LEU ALA GLY LEU LYS GLU ALA GLY ILE ASP ALA TYR GLY          
SEQRES   4 C  306  VAL ASP THR LYS ASP PHE PRO VAL THR GLN LEU LYS GLU          
SEQRES   5 C  306  GLN GLY PHE ASP LYS VAL PHE ILE ALA LEU HIS GLY ARG          
SEQRES   6 C  306  GLY GLY GLU ASP GLY THR LEU GLN GLY VAL LEU GLU PHE          
SEQRES   7 C  306  LEU GLN LEU PRO TYR THR GLY SER GLY VAL MET ALA SER          
SEQRES   8 C  306  ALA LEU THR MET ASP LYS LEU ARG THR LYS LEU VAL TRP          
SEQRES   9 C  306  GLN ALA LEU GLY LEU PRO ILE SER PRO TYR VAL ALA LEU          
SEQRES  10 C  306  ASN ARG GLN GLN PHE GLU THR LEU SER PRO GLU GLU LEU          
SEQRES  11 C  306  VAL ALA CYS VAL ALA LYS LEU GLY LEU PRO LEU ILE VAL          
SEQRES  12 C  306  LYS PRO SER HIS GLU GLY SER SER VAL GLY MET SER LYS          
SEQRES  13 C  306  VAL ASP HIS ALA SER GLU LEU GLN LYS ALA LEU VAL GLU          
SEQRES  14 C  306  ALA PHE GLN HIS ASP SER ASP VAL LEU ILE GLU LYS TRP          
SEQRES  15 C  306  LEU SER GLY PRO GLU PHE THR VAL ALA ILE LEU GLY ASP          
SEQRES  16 C  306  GLU VAL LEU PRO SER ILE ARG ILE GLN PRO PRO GLY VAL          
SEQRES  17 C  306  PHE TYR ASP TYR ASP ALA LYS TYR LEU SER ASP LYS THR          
SEQRES  18 C  306  GLN TYR PHE CYS PRO SER GLY LEU SER ASP GLU SER GLU          
SEQRES  19 C  306  GLN GLN LEU ALA ALA LEU ALA LEU GLN ALA TYR HIS ALA          
SEQRES  20 C  306  LEU ASP CYS SER GLY TRP GLY ARG VAL ASP VAL MET GLN          
SEQRES  21 C  306  ASP ARG ASP GLY HIS PHE TYR LEU LEU GLU VAL ASN THR          
SEQRES  22 C  306  SER PRO GLY MET THR SER HIS SER LEU VAL PRO MET ALA          
SEQRES  23 C  306  ALA ARG GLN TYR GLY LEU SER PHE SER GLN LEU VAL ALA          
SEQRES  24 C  306  ARG ILE LEU MET LEU ALA ASP                                  
SEQRES   1 D  306  MET ALA GLU LYS VAL ALA VAL LEU LEU GLY GLY THR SER          
SEQRES   2 D  306  ALA GLU ARG GLU VAL SER LEU LEU SER GLY GLN ALA VAL          
SEQRES   3 D  306  LEU ALA GLY LEU LYS GLU ALA GLY ILE ASP ALA TYR GLY          
SEQRES   4 D  306  VAL ASP THR LYS ASP PHE PRO VAL THR GLN LEU LYS GLU          
SEQRES   5 D  306  GLN GLY PHE ASP LYS VAL PHE ILE ALA LEU HIS GLY ARG          
SEQRES   6 D  306  GLY GLY GLU ASP GLY THR LEU GLN GLY VAL LEU GLU PHE          
SEQRES   7 D  306  LEU GLN LEU PRO TYR THR GLY SER GLY VAL MET ALA SER          
SEQRES   8 D  306  ALA LEU THR MET ASP LYS LEU ARG THR LYS LEU VAL TRP          
SEQRES   9 D  306  GLN ALA LEU GLY LEU PRO ILE SER PRO TYR VAL ALA LEU          
SEQRES  10 D  306  ASN ARG GLN GLN PHE GLU THR LEU SER PRO GLU GLU LEU          
SEQRES  11 D  306  VAL ALA CYS VAL ALA LYS LEU GLY LEU PRO LEU ILE VAL          
SEQRES  12 D  306  LYS PRO SER HIS GLU GLY SER SER VAL GLY MET SER LYS          
SEQRES  13 D  306  VAL ASP HIS ALA SER GLU LEU GLN LYS ALA LEU VAL GLU          
SEQRES  14 D  306  ALA PHE GLN HIS ASP SER ASP VAL LEU ILE GLU LYS TRP          
SEQRES  15 D  306  LEU SER GLY PRO GLU PHE THR VAL ALA ILE LEU GLY ASP          
SEQRES  16 D  306  GLU VAL LEU PRO SER ILE ARG ILE GLN PRO PRO GLY VAL          
SEQRES  17 D  306  PHE TYR ASP TYR ASP ALA LYS TYR LEU SER ASP LYS THR          
SEQRES  18 D  306  GLN TYR PHE CYS PRO SER GLY LEU SER ASP GLU SER GLU          
SEQRES  19 D  306  GLN GLN LEU ALA ALA LEU ALA LEU GLN ALA TYR HIS ALA          
SEQRES  20 D  306  LEU ASP CYS SER GLY TRP GLY ARG VAL ASP VAL MET GLN          
SEQRES  21 D  306  ASP ARG ASP GLY HIS PHE TYR LEU LEU GLU VAL ASN THR          
SEQRES  22 D  306  SER PRO GLY MET THR SER HIS SER LEU VAL PRO MET ALA          
SEQRES  23 D  306  ALA ARG GLN TYR GLY LEU SER PHE SER GLN LEU VAL ALA          
SEQRES  24 D  306  ARG ILE LEU MET LEU ALA ASP                                  
HET    AMP  A 401      23                                                       
HET     NA  A 402       1                                                       
HET    ACT  A 403       4                                                       
HET    GOL  A 404       6                                                       
HET    GOL  A 405       6                                                       
HET     NA  A 406       1                                                       
HET    AMP  B 401      23                                                       
HET     NA  B 402       1                                                       
HET    ACT  B 403       4                                                       
HET    ACT  B 404       4                                                       
HET    GOL  B 405       6                                                       
HET    AMP  C 401      23                                                       
HET     NA  C 402       1                                                       
HET    ACT  C 403       4                                                       
HET    GOL  C 404       6                                                       
HET    GOL  C 405       6                                                       
HET    AMP  D 401      23                                                       
HET     NA  D 402       1                                                       
HET    ACT  D 403       4                                                       
HET    GOL  D 404       6                                                       
HET    GOL  D 405       6                                                       
HET    ACT  D 406       4                                                       
HETNAM     AMP ADENOSINE MONOPHOSPHATE                                          
HETNAM      NA SODIUM ION                                                       
HETNAM     ACT ACETATE ION                                                      
HETNAM     GOL GLYCEROL                                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   5  AMP    4(C10 H14 N5 O7 P)                                           
FORMUL   6   NA    5(NA 1+)                                                     
FORMUL   7  ACT    6(C2 H3 O2 1-)                                               
FORMUL   8  GOL    7(C3 H8 O3)                                                  
FORMUL  27  HOH   *730(H2 O)                                                    
HELIX    1 AA1 GLU A   15  ALA A   33  1                                  19    
HELIX    2 AA2 PRO A   46  LEU A   50  5                                   5    
HELIX    3 AA3 GLY A   70  GLN A   80  1                                  11    
HELIX    4 AA4 GLY A   87  THR A   94  1                                   8    
HELIX    5 AA5 ASP A   96  LEU A  107  1                                  12    
HELIX    6 AA6 ARG A  119  LEU A  125  1                                   7    
HELIX    7 AA7 SER A  126  ALA A  135  1                                  10    
HELIX    8 AA8 LYS A  136  GLY A  138  5                                   3    
HELIX    9 AA9 HIS A  159  SER A  161  5                                   3    
HELIX   10 AB1 GLU A  162  GLN A  172  1                                  11    
HELIX   11 AB2 ASP A  211  LEU A  217  1                                   7    
HELIX   12 AB3 SER A  230  LEU A  248  1                                  19    
HELIX   13 AB4 SER A  281  GLY A  291  1                                  11    
HELIX   14 AB5 SER A  293  LEU A  304  1                                  12    
HELIX   15 AB6 GLU B   15  ALA B   33  1                                  19    
HELIX   16 AB7 PRO B   46  LEU B   50  5                                   5    
HELIX   17 AB8 GLY B   70  GLN B   80  1                                  11    
HELIX   18 AB9 GLY B   87  THR B   94  1                                   8    
HELIX   19 AC1 ASP B   96  LEU B  107  1                                  12    
HELIX   20 AC2 ARG B  119  LEU B  125  1                                   7    
HELIX   21 AC3 SER B  126  ALA B  135  1                                  10    
HELIX   22 AC4 LYS B  136  GLY B  138  5                                   3    
HELIX   23 AC5 HIS B  159  SER B  161  5                                   3    
HELIX   24 AC6 GLU B  162  GLN B  172  1                                  11    
HELIX   25 AC7 ASP B  211  LEU B  217  1                                   7    
HELIX   26 AC8 SER B  230  LEU B  248  1                                  19    
HELIX   27 AC9 SER B  281  TYR B  290  1                                  10    
HELIX   28 AD1 SER B  293  LEU B  304  1                                  12    
HELIX   29 AD2 GLU C   15  ALA C   33  1                                  19    
HELIX   30 AD3 PRO C   46  LEU C   50  5                                   5    
HELIX   31 AD4 GLY C   70  GLN C   80  1                                  11    
HELIX   32 AD5 GLY C   87  THR C   94  1                                   8    
HELIX   33 AD6 ASP C   96  LEU C  107  1                                  12    
HELIX   34 AD7 ARG C  119  LEU C  125  1                                   7    
HELIX   35 AD8 SER C  126  ALA C  135  1                                  10    
HELIX   36 AD9 LYS C  136  GLY C  138  5                                   3    
HELIX   37 AE1 HIS C  159  SER C  161  5                                   3    
HELIX   38 AE2 GLU C  162  GLN C  172  1                                  11    
HELIX   39 AE3 ASP C  211  LEU C  217  1                                   7    
HELIX   40 AE4 SER C  230  LEU C  248  1                                  19    
HELIX   41 AE5 SER C  281  GLY C  291  1                                  11    
HELIX   42 AE6 SER C  293  LEU C  304  1                                  12    
HELIX   43 AE7 GLU D   15  ALA D   33  1                                  19    
HELIX   44 AE8 PRO D   46  LEU D   50  5                                   5    
HELIX   45 AE9 GLY D   70  GLN D   80  1                                  11    
HELIX   46 AF1 GLY D   87  THR D   94  1                                   8    
HELIX   47 AF2 ASP D   96  LEU D  107  1                                  12    
HELIX   48 AF3 ARG D  119  LEU D  125  1                                   7    
HELIX   49 AF4 SER D  126  VAL D  134  1                                   9    
HELIX   50 AF5 ALA D  135  GLY D  138  5                                   4    
HELIX   51 AF6 HIS D  159  SER D  161  5                                   3    
HELIX   52 AF7 GLU D  162  GLN D  172  1                                  11    
HELIX   53 AF8 SER D  230  LEU D  248  1                                  19    
HELIX   54 AF9 SER D  281  GLY D  291  1                                  11    
HELIX   55 AG1 SER D  293  LEU D  304  1                                  12    
SHEET    1 AA1 3 ASP A  36  ASP A  41  0                                        
SHEET    2 AA1 3 LYS A   4  LEU A   9  1  N  VAL A   7   O  VAL A  40           
SHEET    3 AA1 3 LYS A  57  ILE A  60  1  O  PHE A  59   N  ALA A   6           
SHEET    1 AA2 4 TYR A 114  ASN A 118  0                                        
SHEET    2 AA2 4 ASP A 176  LYS A 181 -1  O  ILE A 179   N  VAL A 115           
SHEET    3 AA2 4 LEU A 141  PRO A 145 -1  N  ILE A 142   O  GLU A 180           
SHEET    4 AA2 4 SER A 155  VAL A 157 -1  O  VAL A 157   N  LEU A 141           
SHEET    1 AA3 4 GLU A 196  VAL A 197  0                                        
SHEET    2 AA3 4 GLU A 187  LEU A 193 -1  N  LEU A 193   O  GLU A 196           
SHEET    3 AA3 4 ILE A 201  GLN A 204 -1  O  ILE A 203   N  GLU A 187           
SHEET    4 AA3 4 GLN A 222  PHE A 224 -1  O  GLN A 222   N  GLN A 204           
SHEET    1 AA4 4 GLU A 196  VAL A 197  0                                        
SHEET    2 AA4 4 GLU A 187  LEU A 193 -1  N  LEU A 193   O  GLU A 196           
SHEET    3 AA4 4 TRP A 253  GLN A 260 -1  O  VAL A 258   N  PHE A 188           
SHEET    4 AA4 4 PHE A 266  ASN A 272 -1  O  LEU A 269   N  ASP A 257           
SHEET    1 AA5 3 ALA B  37  ASP B  41  0                                        
SHEET    2 AA5 3 VAL B   5  LEU B   9  1  N  VAL B   7   O  TYR B  38           
SHEET    3 AA5 3 LYS B  57  ILE B  60  1  O  PHE B  59   N  ALA B   6           
SHEET    1 AA6 4 TYR B 114  ASN B 118  0                                        
SHEET    2 AA6 4 ASP B 176  LYS B 181 -1  O  VAL B 177   N  LEU B 117           
SHEET    3 AA6 4 LEU B 141  PRO B 145 -1  N  ILE B 142   O  GLU B 180           
SHEET    4 AA6 4 SER B 155  VAL B 157 -1  O  VAL B 157   N  LEU B 141           
SHEET    1 AA7 4 GLU B 196  VAL B 197  0                                        
SHEET    2 AA7 4 GLU B 187  LEU B 193 -1  N  LEU B 193   O  GLU B 196           
SHEET    3 AA7 4 ILE B 201  GLN B 204 -1  O  ILE B 203   N  GLU B 187           
SHEET    4 AA7 4 GLN B 222  PHE B 224 -1  O  GLN B 222   N  GLN B 204           
SHEET    1 AA8 4 GLU B 196  VAL B 197  0                                        
SHEET    2 AA8 4 GLU B 187  LEU B 193 -1  N  LEU B 193   O  GLU B 196           
SHEET    3 AA8 4 TRP B 253  GLN B 260 -1  O  VAL B 258   N  PHE B 188           
SHEET    4 AA8 4 PHE B 266  ASN B 272 -1  O  ASN B 272   N  ARG B 255           
SHEET    1 AA9 3 ASP C  36  ASP C  41  0                                        
SHEET    2 AA9 3 LYS C   4  LEU C   9  1  N  VAL C   7   O  TYR C  38           
SHEET    3 AA9 3 LYS C  57  ILE C  60  1  O  PHE C  59   N  ALA C   6           
SHEET    1 AB1 4 TYR C 114  ASN C 118  0                                        
SHEET    2 AB1 4 ASP C 176  LYS C 181 -1  O  VAL C 177   N  LEU C 117           
SHEET    3 AB1 4 LEU C 141  PRO C 145 -1  N  LYS C 144   O  LEU C 178           
SHEET    4 AB1 4 SER C 155  VAL C 157 -1  O  VAL C 157   N  LEU C 141           
SHEET    1 AB2 4 GLU C 196  VAL C 197  0                                        
SHEET    2 AB2 4 GLU C 187  LEU C 193 -1  N  LEU C 193   O  GLU C 196           
SHEET    3 AB2 4 ILE C 201  GLN C 204 -1  O  ILE C 203   N  GLU C 187           
SHEET    4 AB2 4 GLN C 222  PHE C 224 -1  O  GLN C 222   N  GLN C 204           
SHEET    1 AB3 4 GLU C 196  VAL C 197  0                                        
SHEET    2 AB3 4 GLU C 187  LEU C 193 -1  N  LEU C 193   O  GLU C 196           
SHEET    3 AB3 4 TRP C 253  GLN C 260 -1  O  VAL C 258   N  PHE C 188           
SHEET    4 AB3 4 PHE C 266  ASN C 272 -1  O  ASN C 272   N  ARG C 255           
SHEET    1 AB4 3 ASP D  36  ASP D  41  0                                        
SHEET    2 AB4 3 LYS D   4  LEU D   9  1  N  VAL D   7   O  TYR D  38           
SHEET    3 AB4 3 LYS D  57  ILE D  60  1  O  PHE D  59   N  ALA D   6           
SHEET    1 AB5 4 TYR D 114  ASN D 118  0                                        
SHEET    2 AB5 4 ASP D 176  LYS D 181 -1  O  ILE D 179   N  VAL D 115           
SHEET    3 AB5 4 LEU D 141  PRO D 145 -1  N  LYS D 144   O  LEU D 178           
SHEET    4 AB5 4 SER D 155  VAL D 157 -1  O  SER D 155   N  VAL D 143           
SHEET    1 AB6 4 GLU D 196  VAL D 197  0                                        
SHEET    2 AB6 4 GLU D 187  LEU D 193 -1  N  LEU D 193   O  GLU D 196           
SHEET    3 AB6 4 ILE D 201  GLN D 204 -1  O  ILE D 203   N  GLU D 187           
SHEET    4 AB6 4 GLN D 222  PHE D 224 -1  O  PHE D 224   N  ARG D 202           
SHEET    1 AB7 4 GLU D 196  VAL D 197  0                                        
SHEET    2 AB7 4 GLU D 187  LEU D 193 -1  N  LEU D 193   O  GLU D 196           
SHEET    3 AB7 4 TRP D 253  GLN D 260 -1  O  VAL D 258   N  PHE D 188           
SHEET    4 AB7 4 PHE D 266  ASN D 272 -1  O  ASN D 272   N  ARG D 255           
LINK         O   GLU A  68                NA    NA A 402     1555   1555  2.33  
LINK         O   SER A  91                NA    NA A 402     1555   1555  2.45  
LINK         OG1 THR A  94                NA    NA A 402     1555   1555  2.33  
LINK         OG1 THR A 273                NA    NA A 402     1555   1555  2.32  
LINK         O   GLU B  68                NA    NA B 402     1555   1555  2.31  
LINK         O   SER B  91                NA    NA B 402     1555   1555  2.47  
LINK         OG1 THR B  94                NA    NA B 402     1555   1555  2.28  
LINK         OG1 THR B 273                NA    NA B 402     1555   1555  2.38  
LINK         O   GLU C  68                NA    NA C 402     1555   1555  2.30  
LINK         O   SER C  91                NA    NA C 402     1555   1555  2.43  
LINK         OG1 THR C  94                NA    NA C 402     1555   1555  2.31  
LINK         OG1 THR C 273                NA    NA C 402     1555   1555  2.35  
LINK         O   GLU D  68                NA    NA D 402     1555   1555  2.31  
LINK         O   SER D  91                NA    NA D 402     1555   1555  2.41  
LINK         OG1 THR D  94                NA    NA D 402     1555   1555  2.35  
LINK         OG1 THR D 273                NA    NA D 402     1555   1555  2.33  
LINK        NA    NA A 402                 O   HOH A 575     1555   1555  2.33  
LINK        NA    NA A 406                 O   HOH B 687     1555   1555  3.10  
LINK        NA    NA B 402                 O   HOH B 566     1555   1555  2.34  
LINK        NA    NA C 402                 O   HOH C 551     1555   1555  2.32  
LINK        NA    NA D 402                 O   HOH D 558     1555   1555  2.35  
CISPEP   1 LEU A  139    PRO A  140          0        -0.97                     
CISPEP   2 GLY A  185    PRO A  186          0         7.96                     
CISPEP   3 CYS A  225    PRO A  226          0         5.36                     
CISPEP   4 LEU B  139    PRO B  140          0         0.63                     
CISPEP   5 CYS B  225    PRO B  226          0         4.62                     
CISPEP   6 LEU C  139    PRO C  140          0        -7.69                     
CISPEP   7 GLY C  185    PRO C  186          0        14.03                     
CISPEP   8 CYS C  225    PRO C  226          0         3.97                     
CISPEP   9 LEU D  139    PRO D  140          0         1.90                     
CISPEP  10 GLY D  185    PRO D  186          0        10.26                     
CISPEP  11 CYS D  225    PRO D  226          0         5.22                     
SITE     1 AC1 16 LYS A  97  ILE A 142  LYS A 144  MET A 154                    
SITE     2 AC1 16 GLU A 180  LYS A 181  TRP A 182  LEU A 183                    
SITE     3 AC1 16 GLU A 187  PHE A 209  TYR A 210  MET A 259                    
SITE     4 AC1 16 GLU A 270  HOH A 524  HOH A 598  HOH A 601                    
SITE     1 AC2  6 GLU A  68  SER A  91  THR A  94  MET A  95                    
SITE     2 AC2  6 THR A 273  HOH A 575                                          
SITE     1 AC3  6 GLY A 276  SER A 281  LEU A 282  HOH A 508                    
SITE     2 AC3  6 HOH A 560  HOH A 566                                          
SITE     1 AC4  5 LEU A  76  GLU A  77  GLN A  80  LEU A  81                    
SITE     2 AC4  5 ASP A 306                                                     
SITE     1 AC5  6 LEU A 107  HIS A 246  ALA A 247  HOH A 502                    
SITE     2 AC5  6 ALA D 116  ASN D 118                                          
SITE     1 AC6  2 HIS A 280  HIS B 265                                          
SITE     1 AC7 19 LYS B  97  ILE B 142  LYS B 144  MET B 154                    
SITE     2 AC7 19 GLU B 180  LYS B 181  TRP B 182  LEU B 183                    
SITE     3 AC7 19 GLU B 187  VAL B 208  PHE B 209  TYR B 210                    
SITE     4 AC7 19 MET B 259  GLU B 270  HOH B 514  HOH B 516                    
SITE     5 AC7 19 HOH B 527  HOH B 531  HOH B 537                               
SITE     1 AC8  6 GLU B  68  SER B  91  THR B  94  MET B  95                    
SITE     2 AC8  6 THR B 273  HOH B 566                                          
SITE     1 AC9  8 LYS B 215  TYR B 216  ARG B 255  ASN B 272                    
SITE     2 AC9  8 PRO B 275  GLY B 276  ACT B 404  HOH B 572                    
SITE     1 AD1  7 LYS B 215  TYR B 216  GLY B 276  SER B 281                    
SITE     2 AD1  7 LEU B 282  ACT B 403  HOH B 555                               
SITE     1 AD2  5 GLY B  11  THR B  12  THR B  42  GLY B  66                    
SITE     2 AD2  5 HOH B 618                                                     
SITE     1 AD3 15 LYS C  97  ILE C 142  LYS C 144  GLU C 180                    
SITE     2 AD3 15 LYS C 181  TRP C 182  LEU C 183  GLU C 187                    
SITE     3 AD3 15 PHE C 209  TYR C 210  MET C 259  GLU C 270                    
SITE     4 AD3 15 HOH C 503  HOH C 518  HOH C 542                               
SITE     1 AD4  6 GLU C  68  SER C  91  THR C  94  MET C  95                    
SITE     2 AD4  6 THR C 273  HOH C 551                                          
SITE     1 AD5  7 TYR C 210  GLY C 276  SER C 281  LEU C 282                    
SITE     2 AD5  7 HOH C 501  HOH C 514  HOH C 533                               
SITE     1 AD6  7 PRO C  82  TYR C  83  GLY C  85  SER C  86                    
SITE     2 AD6  7 GLY C  87  SER C 251  ASP C 306                               
SITE     1 AD7  7 GLY C  11  THR C  12  THR C  42  ARG C  65                    
SITE     2 AD7  7 GLY C  66  HOH C 531  HOH C 534                               
SITE     1 AD8 16 LYS D  97  ILE D 142  LYS D 144  GLU D 180                    
SITE     2 AD8 16 LYS D 181  TRP D 182  LEU D 183  GLU D 187                    
SITE     3 AD8 16 PHE D 209  TYR D 210  MET D 259  LEU D 269                    
SITE     4 AD8 16 GLU D 270  HOH D 538  HOH D 576  HOH D 584                    
SITE     1 AD9  6 GLU D  68  SER D  91  THR D  94  MET D  95                    
SITE     2 AD9  6 THR D 273  HOH D 558                                          
SITE     1 AE1  6 ARG D 255  GLY D 276  SER D 281  LEU D 282                    
SITE     2 AE1  6 ACT D 406  HOH D 548                                          
SITE     1 AE2  8 PRO D  82  TYR D  83  GLY D  85  SER D  86                    
SITE     2 AE2  8 GLY D  87  SER D 251  ASP D 306  HOH D 506                    
SITE     1 AE3  6 LEU D  76  GLU D  77  GLN D  80  LEU D  81                    
SITE     2 AE3  6 ASP D 306  HOH D 516                                          
SITE     1 AE4  6 LYS D 215  ARG D 255  ASN D 272  GLY D 276                    
SITE     2 AE4  6 ACT D 403  HOH D 518                                          
CRYST1   62.585  106.071  210.769  90.00  90.00  90.00 P 21 21 21   16          
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      0.015978  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009428  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004745        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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