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Database: PDB
Entry: 5NRI
LinkDB: 5NRI
Original site: 5NRI 
HEADER    LIGASE                                  23-APR-17   5NRI              
TITLE     CRYSTAL STRUCTURE OF BURKHOLDERIA PSEUDOMALLEI D-ALANINE-D-ALANINE    
TITLE    2 LIGASE IN COMPLEX WITH AMP AND D-ALA-D-ALA                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: D-ALANINE--D-ALANINE LIGASE;                               
COMPND   3 CHAIN: A, B;                                                         
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: BURKHOLDERIA PSEUDOMALLEI;                      
SOURCE   3 ORGANISM_TAXID: 357348;                                              
SOURCE   4 GENE: DDL, BURPS1106A_3548;                                          
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008                                      
KEYWDS    LIGASE, COMPLEX                                                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    L.DIAZ-SAEZ,W.N.HUNTER                                                
REVDAT   1   30-MAY-18 5NRI    0                                                
JRNL        AUTH   L.DIAZ-SAEZ,W.N.HUNTER                                       
JRNL        TITL   CHARACTERISATION OF BURKHOLDERIA PSEUDOMALLEI                
JRNL        TITL 2 D-ALANINE-D-ALANINE LIGASE                                   
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0158                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 69.97                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 86139                          
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) : 0.136                           
REMARK   3   R VALUE            (WORKING SET) : 0.133                           
REMARK   3   FREE R VALUE                     : 0.208                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 4448                            
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) : 1.50                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.54                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 6411                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.11                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2180                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 351                          
REMARK   3   BIN FREE R VALUE                    : 0.3110                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4678                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 115                                     
REMARK   3   SOLVENT ATOMS            : 789                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 26.00                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.69000                                             
REMARK   3    B22 (A**2) : 0.86000                                              
REMARK   3    B33 (A**2) : 0.85000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -1.40000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.084         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.083         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.070         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.339         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.981                         
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):  5073 ; 0.027 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  4847 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  6878 ; 2.583 ; 1.991       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 11224 ; 1.432 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   627 ; 7.129 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   227 ;31.011 ;23.480       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   832 ;14.824 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    42 ;19.851 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   772 ; 0.174 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  5607 ; 0.014 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  1042 ; 0.005 ; 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):  2500 ; 5.652 ; 2.280       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  2499 ; 5.652 ; 2.421       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3118 ; 6.758 ; 3.439       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  3119 ; 6.758 ;21.193       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2573 ; 6.683 ; 2.611       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  2573 ; 6.679 ; 2.611       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  3752 ; 7.680 ; 3.778       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  5917 ; 8.435 ;30.113       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  5918 ; 8.435 ;30.117       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  9919 ; 4.984 ; 3.000       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):   512 ;39.121 ; 5.000       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2): 10098 ;21.439 ; 5.000       
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 5NRI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 24-APR-17.                  
REMARK 100 THE DEPOSITION ID IS D_1200004600.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 04-FEB-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 80                                 
REMARK 200  PH                             : 5.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I04-1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.917410                           
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS3 S 6M              
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 90609                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 69.970                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.6                               
REMARK 200  DATA REDUNDANCY                : 3.100                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.5000                            
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: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: SEE PUBLICATION                                      
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 44.87                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.23                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.05 TO 0.3 M LI2SO4, 0.1 M BIS-TRIS     
REMARK 280  PH 5.5 AND 15-30% (W/V) PEG 3350, RATIO PROTEIN:RESERVOIR 1:1,      
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       30.56650            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     MET B     1                                                      
REMARK 465     SER B     2                                                      
REMARK 465     GLY B     3                                                      
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    DAL A   403     O    HOH A   501              1.80            
REMARK 500   O    HOH A   684     O    HOH A   778              1.99            
REMARK 500   O    HOH A   532     O    HOH A   611              2.02            
REMARK 500   CE1  HIS A    70     O    HOH A   505              2.10            
REMARK 500   O    GLY B   190     O    HOH B   501              2.19            
REMARK 500   O    HOH B   575     O    HOH B   672              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   OE2  GLU B    24     CD   GLU B   188     2756     2.15            
REMARK 500   O    HOH A   703     O    HOH B   502     1556     2.17            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    SER A 151   CB    SER A 151   OG      0.079                       
REMARK 500    ARG A 244   CZ    ARG A 244   NH2    -0.078                       
REMARK 500    ASP A 251   CB    ASP A 251   CG      0.129                       
REMARK 500    GLU A 275   CD    GLU A 275   OE2     0.079                       
REMARK 500    GLU B  75   CG    GLU B  75   CD      0.111                       
REMARK 500    LEU B 229   C     LEU B 229   O       0.116                       
REMARK 500    GLU B 275   CG    GLU B 275   CD     -0.125                       
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   5   CB  -  CG  -  OD1 ANGL. DEV. =   6.1 DEGREES          
REMARK 500    ARG A  31   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.6 DEGREES          
REMARK 500    ARG A  38   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES          
REMARK 500    ARG A  52   NE  -  CZ  -  NH1 ANGL. DEV. =  -5.3 DEGREES          
REMARK 500    ARG A  52   NE  -  CZ  -  NH2 ANGL. DEV. =   4.4 DEGREES          
REMARK 500    TYR A  86   CB  -  CG  -  CD2 ANGL. DEV. =   4.6 DEGREES          
REMARK 500    VAL A 143   CG1 -  CB  -  CG2 ANGL. DEV. = -10.1 DEGREES          
REMARK 500    ASP A 165   CB  -  CG  -  OD1 ANGL. DEV. =   8.2 DEGREES          
REMARK 500    GLU A 239   OE1 -  CD  -  OE2 ANGL. DEV. =   7.5 DEGREES          
REMARK 500    ARG A 244   NE  -  CZ  -  NH1 ANGL. DEV. =   5.0 DEGREES          
REMARK 500    ARG A 244   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.5 DEGREES          
REMARK 500    PHE A 250   CB  -  CG  -  CD1 ANGL. DEV. =  -4.6 DEGREES          
REMARK 500    ASP A 251   CB  -  CG  -  OD1 ANGL. DEV. =  11.3 DEGREES          
REMARK 500    ASP A 251   CB  -  CG  -  OD2 ANGL. DEV. =   5.8 DEGREES          
REMARK 500    ASP A 251   CB  -  CG  -  OD2 ANGL. DEV. =  -6.0 DEGREES          
REMARK 500    THR A 256   CB  -  CA  -  C   ANGL. DEV. =  18.7 DEGREES          
REMARK 500    ARG A 293   NE  -  CZ  -  NH1 ANGL. DEV. =   5.2 DEGREES          
REMARK 500    LEU A 309   CB  -  CG  -  CD1 ANGL. DEV. = -10.3 DEGREES          
REMARK 500    ARG B  52   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.1 DEGREES          
REMARK 500    ASP B 103   CB  -  CG  -  OD1 ANGL. DEV. =   7.0 DEGREES          
REMARK 500    ARG B 106   NE  -  CZ  -  NH2 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    ARG B 133   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES          
REMARK 500    TYR B 193   CB  -  CG  -  CD2 ANGL. DEV. =  -5.0 DEGREES          
REMARK 500    TYR B 193   CB  -  CG  -  CD1 ANGL. DEV. =   3.8 DEGREES          
REMARK 500    LEU B 234   CB  -  CG  -  CD2 ANGL. DEV. =  10.3 DEGREES          
REMARK 500    ASP B 251   CB  -  CG  -  OD1 ANGL. DEV. =   6.0 DEGREES          
REMARK 500    ASP B 257   CB  -  CG  -  OD1 ANGL. DEV. =   6.3 DEGREES          
REMARK 500    ASP B 262   CB  -  CG  -  OD2 ANGL. DEV. =  -6.5 DEGREES          
REMARK 500    LEU B 265   CB  -  CG  -  CD1 ANGL. DEV. =  12.1 DEGREES          
REMARK 500    ASP B 266   CB  -  CG  -  OD1 ANGL. DEV. =   5.4 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    ALA A 199     -137.27     56.76                                   
REMARK 500    ASP A 257       71.01    -65.45                                   
REMARK 500    ALA A 279       57.83   -142.06                                   
REMARK 500    ALA B 199     -134.51     56.06                                   
REMARK 500    ASP B 257      -36.36     76.05                                   
REMARK 500    TRP B 258      119.24   -161.83                                   
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 THR A  256     ASP A  257                 -134.92                    
REMARK 500 ILE B    4     ASP B    5                 -139.86                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY                                       
REMARK 500                                                                      
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY                       
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER                 
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;                     
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;                            
REMARK 500 I=INSERTION CODE).                                                   
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        ANGLE                                           
REMARK 500    GLY A 190         11.49                                           
REMARK 500    THR A 256         10.32                                           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 945        DISTANCE =  6.07 ANGSTROMS                       
REMARK 525    HOH A 946        DISTANCE =  6.83 ANGSTROMS                       
REMARK 525    HOH A 947        DISTANCE =  6.86 ANGSTROMS                       
REMARK 525    HOH A 948        DISTANCE =  6.91 ANGSTROMS                       
REMARK 525    HOH A 949        DISTANCE =  7.06 ANGSTROMS                       
REMARK 525    HOH A 950        DISTANCE =  7.07 ANGSTROMS                       
REMARK 525    HOH A 951        DISTANCE =  7.13 ANGSTROMS                       
REMARK 525    HOH A 952        DISTANCE =  7.19 ANGSTROMS                       
REMARK 525    HOH A 953        DISTANCE =  7.24 ANGSTROMS                       
REMARK 525    HOH A 954        DISTANCE =  7.44 ANGSTROMS                       
REMARK 525    HOH A 955        DISTANCE =  7.86 ANGSTROMS                       
REMARK 525    HOH A 956        DISTANCE =  8.06 ANGSTROMS                       
REMARK 525    HOH A 957        DISTANCE =  8.36 ANGSTROMS                       
REMARK 525    HOH A 958        DISTANCE =  8.63 ANGSTROMS                       
REMARK 525    HOH A 959        DISTANCE =  8.78 ANGSTROMS                       
REMARK 525    HOH A 960        DISTANCE =  9.32 ANGSTROMS                       
REMARK 525    HOH A 961        DISTANCE =  9.58 ANGSTROMS                       
REMARK 525    HOH A 962        DISTANCE = 10.49 ANGSTROMS                       
REMARK 525    HOH A 963        DISTANCE = 10.88 ANGSTROMS                       
REMARK 525    HOH A 964        DISTANCE = 10.96 ANGSTROMS                       
REMARK 525    HOH A 965        DISTANCE = 11.85 ANGSTROMS                       
REMARK 525    HOH A 966        DISTANCE = 12.01 ANGSTROMS                       
REMARK 525    HOH A 967        DISTANCE = 12.96 ANGSTROMS                       
REMARK 525    HOH A 968        DISTANCE = 15.52 ANGSTROMS                       
REMARK 525    HOH A 969        DISTANCE = 16.87 ANGSTROMS                       
REMARK 525    HOH B 813        DISTANCE =  6.25 ANGSTROMS                       
REMARK 525    HOH B 814        DISTANCE =  6.35 ANGSTROMS                       
REMARK 525    HOH B 815        DISTANCE =  6.64 ANGSTROMS                       
REMARK 525    HOH B 816        DISTANCE =  6.71 ANGSTROMS                       
REMARK 525    HOH B 817        DISTANCE =  6.99 ANGSTROMS                       
REMARK 525    HOH B 818        DISTANCE =  7.16 ANGSTROMS                       
REMARK 525    HOH B 819        DISTANCE =  7.35 ANGSTROMS                       
REMARK 525    HOH B 820        DISTANCE = 10.11 ANGSTROMS                       
REMARK 615                                                                      
REMARK 615 ZERO OCCUPANCY ATOM                                                  
REMARK 615 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 615 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 615 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 615 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 615   M RES C  SSEQI                                                     
REMARK 615     DAL A   403                                                      
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                              MG A 404  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A 501   O                                                      
REMARK 620 2 HOH A 642   O   162.8                                              
REMARK 620 3 HOH A 683   O    93.7  74.2                                        
REMARK 620 4 HOH A 712   O    89.6  92.5 141.5                                  
REMARK 620 5 HOH A 850   O    80.6  83.0  62.4  80.4                            
REMARK 620 6 HOH A 505   O    85.1  98.9  60.5 157.8 119.7                      
REMARK 620 N                    1     2     3     4     5                       
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 MG A 404                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 405                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 406                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 407                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 408                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue AMP B 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 405                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PGE B 406                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 407                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 408                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 409                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide DAL A 402 and DAL A    
REMARK 800  403                                                                 
DBREF  5NRI A    1   312  UNP    A3NZL3   DDL_BURP0        1    312             
DBREF  5NRI B    1   312  UNP    A3NZL3   DDL_BURP0        1    312             
SEQRES   1 A  312  MET SER GLY ILE ASP PRO LYS ARG PHE GLY LYS VAL ALA          
SEQRES   2 A  312  VAL LEU LEU GLY GLY ASP SER ALA GLU ARG GLU VAL SER          
SEQRES   3 A  312  LEU ASN SER GLY ARG LEU VAL LEU GLN GLY LEU ARG ASP          
SEQRES   4 A  312  ALA GLY ILE ASP ALA HIS PRO PHE ASP PRO ALA GLN ARG          
SEQRES   5 A  312  PRO LEU ALA ALA LEU LYS ASP GLU GLY PHE VAL ARG ALA          
SEQRES   6 A  312  PHE ASN ALA LEU HIS GLY GLY TYR GLY GLU ASN GLY GLN          
SEQRES   7 A  312  ILE GLN GLY ALA LEU ASP PHE TYR GLY ILE ARG TYR THR          
SEQRES   8 A  312  GLY SER GLY VAL LEU GLY SER ALA LEU GLY LEU ASP LYS          
SEQRES   9 A  312  PHE ARG THR LYS LEU VAL TRP GLN GLN THR GLY ILE PRO          
SEQRES  10 A  312  THR PRO PRO PHE GLU THR VAL MET ARG GLY ASP ASP TYR          
SEQRES  11 A  312  ALA ALA ARG ALA GLN ASP ILE VAL ALA LYS LEU GLY VAL          
SEQRES  12 A  312  PRO LEU PHE VAL LYS PRO ALA SER GLU GLY SER SER VAL          
SEQRES  13 A  312  ALA VAL GLU LYS VAL LYS SER ALA ASP ALA LEU PRO ALA          
SEQRES  14 A  312  ALA LEU GLU GLU ALA ALA LYS HIS ASP LYS ILE VAL ILE          
SEQRES  15 A  312  VAL GLU LYS SER ILE GLU GLY GLY GLY GLU TYR THR ALA          
SEQRES  16 A  312  CYS ILE ALA ALA ASP LEU ASP LEU PRO LEU ILE ARG ILE          
SEQRES  17 A  312  VAL PRO ALA GLY GLU PHE TYR ASP TYR HIS ALA LYS TYR          
SEQRES  18 A  312  ILE ALA ASN ASP THR GLN TYR LEU ILE PRO CYS GLY LEU          
SEQRES  19 A  312  ASP ALA ALA LYS GLU ALA GLU PHE LYS ARG ILE ALA ARG          
SEQRES  20 A  312  ARG ALA PHE ASP VAL LEU GLY CYS THR ASP TRP GLY ARG          
SEQRES  21 A  312  ALA ASP PHE MET LEU ASP ALA ALA GLY ASN PRO TYR PHE          
SEQRES  22 A  312  LEU GLU VAL ASN THR ALA PRO GLY MET THR ASP HIS SER          
SEQRES  23 A  312  LEU PRO PRO LYS ALA ALA ARG ALA VAL GLY ILE GLY TYR          
SEQRES  24 A  312  SER GLU LEU VAL VAL LYS VAL LEU SER LEU THR LEU ASP          
SEQRES   1 B  312  MET SER GLY ILE ASP PRO LYS ARG PHE GLY LYS VAL ALA          
SEQRES   2 B  312  VAL LEU LEU GLY GLY ASP SER ALA GLU ARG GLU VAL SER          
SEQRES   3 B  312  LEU ASN SER GLY ARG LEU VAL LEU GLN GLY LEU ARG ASP          
SEQRES   4 B  312  ALA GLY ILE ASP ALA HIS PRO PHE ASP PRO ALA GLN ARG          
SEQRES   5 B  312  PRO LEU ALA ALA LEU LYS ASP GLU GLY PHE VAL ARG ALA          
SEQRES   6 B  312  PHE ASN ALA LEU HIS GLY GLY TYR GLY GLU ASN GLY GLN          
SEQRES   7 B  312  ILE GLN GLY ALA LEU ASP PHE TYR GLY ILE ARG TYR THR          
SEQRES   8 B  312  GLY SER GLY VAL LEU GLY SER ALA LEU GLY LEU ASP LYS          
SEQRES   9 B  312  PHE ARG THR LYS LEU VAL TRP GLN GLN THR GLY ILE PRO          
SEQRES  10 B  312  THR PRO PRO PHE GLU THR VAL MET ARG GLY ASP ASP TYR          
SEQRES  11 B  312  ALA ALA ARG ALA GLN ASP ILE VAL ALA LYS LEU GLY VAL          
SEQRES  12 B  312  PRO LEU PHE VAL LYS PRO ALA SER GLU GLY SER SER VAL          
SEQRES  13 B  312  ALA VAL GLU LYS VAL LYS SER ALA ASP ALA LEU PRO ALA          
SEQRES  14 B  312  ALA LEU GLU GLU ALA ALA LYS HIS ASP LYS ILE VAL ILE          
SEQRES  15 B  312  VAL GLU LYS SER ILE GLU GLY GLY GLY GLU TYR THR ALA          
SEQRES  16 B  312  CYS ILE ALA ALA ASP LEU ASP LEU PRO LEU ILE ARG ILE          
SEQRES  17 B  312  VAL PRO ALA GLY GLU PHE TYR ASP TYR HIS ALA LYS TYR          
SEQRES  18 B  312  ILE ALA ASN ASP THR GLN TYR LEU ILE PRO CYS GLY LEU          
SEQRES  19 B  312  ASP ALA ALA LYS GLU ALA GLU PHE LYS ARG ILE ALA ARG          
SEQRES  20 B  312  ARG ALA PHE ASP VAL LEU GLY CYS THR ASP TRP GLY ARG          
SEQRES  21 B  312  ALA ASP PHE MET LEU ASP ALA ALA GLY ASN PRO TYR PHE          
SEQRES  22 B  312  LEU GLU VAL ASN THR ALA PRO GLY MET THR ASP HIS SER          
SEQRES  23 B  312  LEU PRO PRO LYS ALA ALA ARG ALA VAL GLY ILE GLY TYR          
SEQRES  24 B  312  SER GLU LEU VAL VAL LYS VAL LEU SER LEU THR LEU ASP          
HET    AMP  A 401      23                                                       
HET    DAL  A 402       6                                                       
HET    DAL  A 403       5                                                       
HET     MG  A 404       1                                                       
HET    SO4  A 405       5                                                       
HET    EDO  A 406       4                                                       
HET    EDO  A 407       4                                                       
HET    EDO  A 408       4                                                       
HET    SO4  B 401       5                                                       
HET    EDO  B 402       4                                                       
HET    EDO  B 403       4                                                       
HET    AMP  B 404      23                                                       
HET    SO4  B 405       5                                                       
HET    PGE  B 406      10                                                       
HET    EDO  B 407       4                                                       
HET    EDO  B 408       4                                                       
HET    EDO  B 409       4                                                       
HETNAM     AMP ADENOSINE MONOPHOSPHATE                                          
HETNAM     DAL D-ALANINE                                                        
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     SO4 SULFATE ION                                                      
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETNAM     PGE TRIETHYLENE GLYCOL                                               
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   3  AMP    2(C10 H14 N5 O7 P)                                           
FORMUL   4  DAL    2(C3 H7 N O2)                                                
FORMUL   6   MG    MG 2+                                                        
FORMUL   7  SO4    3(O4 S 2-)                                                   
FORMUL   8  EDO    8(C2 H6 O2)                                                  
FORMUL  16  PGE    C6 H14 O4                                                    
FORMUL  20  HOH   *789(H2 O)                                                    
HELIX    1 AA1 ASP A    5  PHE A    9  5                                   5    
HELIX    2 AA2 GLU A   22  ALA A   40  1                                  19    
HELIX    3 AA3 ALA A   55  GLU A   60  1                                   6    
HELIX    4 AA4 GLY A   71  GLU A   75  5                                   5    
HELIX    5 AA5 GLY A   77  TYR A   86  1                                  10    
HELIX    6 AA6 GLY A   94  LEU A  102  1                                   9    
HELIX    7 AA7 ASP A  103  THR A  114  1                                  12    
HELIX    8 AA8 ASP A  129  GLY A  142  1                                  14    
HELIX    9 AA9 SER A  163  ASP A  165  5                                   3    
HELIX   10 AB1 ALA A  166  ASP A  178  1                                  13    
HELIX   11 AB2 ASP A  216  ILE A  222  1                                   7    
HELIX   12 AB3 ASP A  235  LEU A  253  1                                  19    
HELIX   13 AB4 SER A  286  ALA A  294  1                                   9    
HELIX   14 AB5 GLY A  298  LEU A  309  1                                  12    
HELIX   15 AB6 ASP B    5  GLY B   10  5                                   6    
HELIX   16 AB7 GLU B   22  ALA B   40  1                                  19    
HELIX   17 AB8 ALA B   55  GLY B   61  1                                   7    
HELIX   18 AB9 GLY B   71  GLU B   75  5                                   5    
HELIX   19 AC1 GLY B   77  GLY B   87  1                                  11    
HELIX   20 AC2 GLY B   94  ASP B  103  1                                  10    
HELIX   21 AC3 ASP B  103  THR B  114  1                                  12    
HELIX   22 AC4 ASP B  129  GLY B  142  1                                  14    
HELIX   23 AC5 SER B  163  ASP B  165  5                                   3    
HELIX   24 AC6 ALA B  166  LYS B  176  1                                  11    
HELIX   25 AC7 ASP B  216  ILE B  222  1                                   7    
HELIX   26 AC8 ASP B  235  VAL B  252  1                                  18    
HELIX   27 AC9 SER B  286  VAL B  295  1                                  10    
HELIX   28 AD1 GLY B  298  LEU B  309  1                                  12    
SHEET    1 AA1 4 ASP A  43  PHE A  47  0                                        
SHEET    2 AA1 4 LYS A  11  LEU A  15  1  N  VAL A  12   O  ASP A  43           
SHEET    3 AA1 4 ARG A  64  ASN A  67  1  O  PHE A  66   N  ALA A  13           
SHEET    4 AA1 4 ARG A  89  TYR A  90  1  O  ARG A  89   N  ALA A  65           
SHEET    1 AA2 4 PHE A 121  MET A 125  0                                        
SHEET    2 AA2 4 ILE A 180  LYS A 185 -1  O  VAL A 183   N  GLU A 122           
SHEET    3 AA2 4 LEU A 145  PRO A 149 -1  N  LYS A 148   O  ILE A 182           
SHEET    4 AA2 4 GLU A 159  VAL A 161 -1  O  VAL A 161   N  LEU A 145           
SHEET    1 AA3 5 GLN A 227  LEU A 229  0                                        
SHEET    2 AA3 5 ILE A 206  VAL A 209 -1  N  ARG A 207   O  LEU A 229           
SHEET    3 AA3 5 GLY A 189  ALA A 198 -1  N  GLU A 192   O  ILE A 208           
SHEET    4 AA3 5 TRP A 258  ASP A 266 -1  O  GLY A 259   N  ILE A 197           
SHEET    5 AA3 5 PRO A 271  ASN A 277 -1  O  ASN A 277   N  ARG A 260           
SHEET    1 AA4 4 ALA B  44  PHE B  47  0                                        
SHEET    2 AA4 4 LYS B  11  LEU B  15  1  N  VAL B  14   O  PHE B  47           
SHEET    3 AA4 4 PHE B  62  ASN B  67  1  O  ARG B  64   N  ALA B  13           
SHEET    4 AA4 4 ARG B  89  TYR B  90  1  O  ARG B  89   N  ALA B  65           
SHEET    1 AA5 4 PHE B 121  MET B 125  0                                        
SHEET    2 AA5 4 ILE B 180  LYS B 185 -1  O  VAL B 183   N  GLU B 122           
SHEET    3 AA5 4 LEU B 145  PRO B 149 -1  N  PHE B 146   O  GLU B 184           
SHEET    4 AA5 4 GLU B 159  VAL B 161 -1  O  GLU B 159   N  VAL B 147           
SHEET    1 AA6 5 GLN B 227  LEU B 229  0                                        
SHEET    2 AA6 5 ILE B 206  VAL B 209 -1  N  VAL B 209   O  GLN B 227           
SHEET    3 AA6 5 GLU B 192  ALA B 198 -1  N  GLU B 192   O  ILE B 208           
SHEET    4 AA6 5 TRP B 258  LEU B 265 -1  O  GLY B 259   N  ILE B 197           
SHEET    5 AA6 5 PRO B 271  ASN B 277 -1  O  LEU B 274   N  ASP B 262           
LINK         N   DAL A 402                 C   DAL A 403     1555   1555  1.37  
LINK        MG    MG A 404                 O   HOH A 501     1555   1555  1.95  
LINK        MG    MG A 404                 O   HOH A 642     1555   1555  1.92  
LINK        MG    MG A 404                 O   HOH A 683     1555   1555  2.53  
LINK        MG    MG A 404                 O   HOH A 712     1555   1555  1.73  
LINK        MG    MG A 404                 O   HOH A 850     1555   1555  1.90  
LINK        MG    MG A 404                 O   HOH A 505     1555   1555  2.85  
CISPEP   1 SER A    2    GLY A    3          0        -9.55                     
CISPEP   2 VAL A  143    PRO A  144          0         2.06                     
CISPEP   3 GLU A  152    GLY A  153          0        -5.78                     
CISPEP   4 GLU A  152    GLY A  153          0       -18.14                     
CISPEP   5 ILE A  230    PRO A  231          0         5.72                     
CISPEP   6 VAL B  143    PRO B  144          0         6.94                     
CISPEP   7 ILE B  230    PRO B  231          0        -6.61                     
SITE     1 AC1 16 LYS A 104  PRO A 119  PHE A 146  LYS A 148                    
SITE     2 AC1 16 GLU A 184  LYS A 185  SER A 186  ILE A 187                    
SITE     3 AC1 16 GLU A 192  PHE A 214  TYR A 215  GLU A 275                    
SITE     4 AC1 16 HOH A 602  HOH A 635  HOH A 648  HOH A 665                    
SITE     1 AC2  7 HIS A  70  HOH A 501  HOH A 505  HOH A 642                    
SITE     2 AC2  7 HOH A 683  HOH A 712  HOH A 850                               
SITE     1 AC3  9 ARG A 293  GLY A 298  TYR A 299  HOH A 570                    
SITE     2 AC3  9 HOH A 593  HOH A 616  HOH A 639  HOH A 756                    
SITE     3 AC3  9 ARG B 293                                                     
SITE     1 AC4  6 GLN A 112  PHE A 121  HOH A 510  HOH A 625                    
SITE     2 AC4  6 HOH A 659  GLN B 113                                          
SITE     1 AC5  2 HIS A  45  HOH A 528                                          
SITE     1 AC6  2 ARG A 126  LYS A 179                                          
SITE     1 AC7  7 ARG A 293  HOH A 630  HOH A 942  LYS B 290                    
SITE     2 AC7  7 HOH B 532  HOH B 605  HOH B 630                               
SITE     1 AC8  5 ALA B 240  ARG B 244  EDO B 403  HOH B 506                    
SITE     2 AC8  5 HOH B 609                                                     
SITE     1 AC9  6 ALA B 236  ALA B 237  EDO B 402  HOH B 515                    
SITE     2 AC9  6 HOH B 520  HOH B 543                                          
SITE     1 AD1 17 LYS B 104  PHE B 146  LYS B 148  SER B 155                    
SITE     2 AD1 17 VAL B 158  GLU B 184  LYS B 185  SER B 186                    
SITE     3 AD1 17 ILE B 187  GLU B 192  PHE B 214  TYR B 215                    
SITE     4 AD1 17 LEU B 274  GLU B 275  HOH B 531  HOH B 565                    
SITE     5 AD1 17 HOH B 644                                                     
SITE     1 AD2 10 HIS B  70  TYR B 221  ARG B 260  ASN B 277                    
SITE     2 AD2 10 PRO B 280  GLY B 281  HOH B 559  HOH B 569                    
SITE     3 AD2 10 HOH B 608  HOH B 664                                          
SITE     1 AD3  9 ARG B 293  GLY B 298  TYR B 299  SER B 300                    
SITE     2 AD3  9 GLU B 301  HOH B 502  HOH B 516  HOH B 526                    
SITE     3 AD3  9 HOH B 578                                                     
SITE     1 AD4  2 GLN A 112  GLN B 113                                          
SITE     1 AD5  3 ARG B 207  HOH B 631  HOH B 682                               
SITE     1 AD6  8 VAL B  25  SER B  29  ALA B  68  LEU B  69                    
SITE     2 AD6  8 HIS B  70  ALA B 279  PRO B 280  HOH B 545                    
SITE     1 AD7  7 HIS A  70  ARG A 260  ASN A 277  GLY A 281                    
SITE     2 AD7  7 SER A 286  LEU A 287  HOH A 523                               
CRYST1   69.642   61.133   69.972  90.00  90.31  90.00 P 1 21 1      4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.014359  0.000000  0.000078        0.00000                         
SCALE2      0.000000  0.016358  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.014292        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system