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Database: PDB
Entry: 5NRH
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Original site: 5NRH 
HEADER    LIGASE                                  23-APR-17   5NRH              
TITLE     CRYSTAL STRUCTURE OF BURKHOLDERIA PSEUDOMALLEI D-ALANINE-D-ALANINE    
TITLE    2 LIGASE IN COMPLEX WITH AMP                                           
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: 28450;                                               
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 5NRH    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.    1.30 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 : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 70.08                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 133936                         
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) : 0.148                           
REMARK   3   R VALUE            (WORKING SET) : 0.146                           
REMARK   3   FREE R VALUE                     : 0.190                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 7097                            
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) : 1.30                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.33                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 9734                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 95.93                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2320                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 482                          
REMARK   3   BIN FREE R VALUE                    : 0.2670                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4672                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 69                                      
REMARK   3   SOLVENT ATOMS            : 785                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 24.76                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.98000                                             
REMARK   3    B22 (A**2) : 0.64000                                              
REMARK   3    B33 (A**2) : 0.33000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 1.52000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.052         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.053         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.042         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.286         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.978                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.965                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  5124 ; 0.022 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  4908 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  6976 ; 2.247 ; 1.989       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 11383 ; 1.444 ; 3.003       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   648 ; 7.711 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   233 ;30.341 ;23.348       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   859 ;13.802 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    45 ;20.523 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   789 ; 0.184 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  5695 ; 0.012 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  1060 ; 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):  2518 ; 3.726 ; 2.225       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  2517 ; 3.716 ; 2.222       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3154 ; 4.581 ; 3.357       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  3155 ; 4.583 ; 3.359       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2606 ; 5.385 ; 2.425       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  2607 ; 5.386 ; 2.425       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  3807 ; 6.253 ; 3.543       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  5971 ; 7.277 ;28.885       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  5972 ; 7.276 ;28.887       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2): 10032 ; 4.711 ; 3.000       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):   497 ;42.426 ; 5.000       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2): 10205 ;19.534 ; 5.000       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NCS TYPE: LOCAL                                                    
REMARK   3   NUMBER OF DIFFERENT NCS PAIRS  : 1                                 
REMARK   3  GROUP  CHAIN1    RANGE     CHAIN2     RANGE    COUNT RMS  WEIGHT    
REMARK   3    1     A     4    311       B     4    311   18826  0.13  0.05     
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.00                                          
REMARK   3   ION PROBE RADIUS   : 0.70                                          
REMARK   3   SHRINKAGE RADIUS   : 0.70                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5NRH 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_1200004599.                                   
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 : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 141049                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 70.080                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.6                               
REMARK 200  DATA REDUNDANCY                : 4.800                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 15.0000                            
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: 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   (%): 45.20                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.24                     
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       30.57500            
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     SER A     2                                                      
REMARK 465     MET B     1                                                      
REMARK 465     SER B     2                                                      
REMARK 465     GLY B     3                                                      
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     ASN A  224   CB   CG   OD1  ND2                                  
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   O    HOH A   834     O    HOH A  1081              2.10            
REMARK 500   O    HOH A  1246     O    HOH B  1096              2.13            
REMARK 500   O    HOH B   887     O    HOH B  1069              2.17            
REMARK 500   OE1  GLU A   152     O    HOH A   801              2.18            
REMARK 500   O    HOH A  1126     O    HOH A  1144              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   NE2  HIS A   218     O    HOH A  1246     2647     2.15            
REMARK 500   ND2  ASN B   224     O    HOH B  1037     2756     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    GLU A 239   CD    GLU A 239   OE1     0.126                       
REMARK 500    GLU A 239   CD    GLU A 239   OE2     0.068                       
REMARK 500    LEU B  15   C     LEU B  15   O       0.134                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG A  38   NE  -  CZ  -  NH1 ANGL. DEV. =   3.6 DEGREES          
REMARK 500    ARG A  52   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.5 DEGREES          
REMARK 500    ARG A  52   NE  -  CZ  -  NH2 ANGL. DEV. =   3.6 DEGREES          
REMARK 500    ASP A 103   CB  -  CG  -  OD1 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    SER A 151   CA  -  C   -  N   ANGL. DEV. =  16.7 DEGREES          
REMARK 500    GLU A 152   C   -  N   -  CA  ANGL. DEV. =  16.4 DEGREES          
REMARK 500    ASP A 165   CB  -  CG  -  OD1 ANGL. DEV. =   6.8 DEGREES          
REMARK 500    ASN A 224   CB  -  CA  -  C   ANGL. DEV. =  14.1 DEGREES          
REMARK 500    PHE A 250   CB  -  CA  -  C   ANGL. DEV. = -12.4 DEGREES          
REMARK 500    PHE A 250   N   -  CA  -  CB  ANGL. DEV. = -10.9 DEGREES          
REMARK 500    ASP A 251   CB  -  CG  -  OD1 ANGL. DEV. =   8.9 DEGREES          
REMARK 500    ASP A 251   CB  -  CG  -  OD2 ANGL. DEV. =  -5.8 DEGREES          
REMARK 500    ASP A 284   CB  -  CG  -  OD1 ANGL. DEV. =   6.5 DEGREES          
REMARK 500    ASP A 284   CB  -  CG  -  OD2 ANGL. DEV. =  -5.4 DEGREES          
REMARK 500    ARG B  38   NE  -  CZ  -  NH1 ANGL. DEV. =   3.5 DEGREES          
REMARK 500    ARG B  38   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.8 DEGREES          
REMARK 500    ILE B  42   CG1 -  CB  -  CG2 ANGL. DEV. = -14.6 DEGREES          
REMARK 500    PRO B  53   C   -  N   -  CA  ANGL. DEV. =   9.5 DEGREES          
REMARK 500    ARG B 106   NE  -  CZ  -  NH1 ANGL. DEV. =   4.5 DEGREES          
REMARK 500    ARG B 106   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.9 DEGREES          
REMARK 500    ARG B 133   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES          
REMARK 500    ARG B 244   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.8 DEGREES          
REMARK 500    ASP B 251   CB  -  CG  -  OD1 ANGL. DEV. =   9.5 DEGREES          
REMARK 500    ASP B 251   CB  -  CG  -  OD2 ANGL. DEV. =  -6.4 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    SER A 151      146.49    148.09                                   
REMARK 500    GLU A 152     -161.29   -167.11                                   
REMARK 500    SER A 155      -66.60     69.67                                   
REMARK 500    ALA A 199     -136.21     49.86                                   
REMARK 500    ASP A 257       61.73    -67.61                                   
REMARK 500    ASP A 257      -27.30     53.04                                   
REMARK 500    TRP A 258      116.03   -172.46                                   
REMARK 500    ALA B 199     -133.86     52.72                                   
REMARK 500    ASP B 257      -40.39     72.31                                   
REMARK 500    MET B 282       33.13   -140.21                                   
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 ALA A  150     SER A  151                  107.46                    
REMARK 500 SER A  151     GLU A  152                   50.97                    
REMARK 500 THR A  256     ASP A  257                 -129.28                    
REMARK 500 THR A  256     ASP A  257                  112.83                    
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         11.44                                           
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 A1253        DISTANCE =  5.83 ANGSTROMS                       
REMARK 525    HOH A1254        DISTANCE =  5.87 ANGSTROMS                       
REMARK 525    HOH A1255        DISTANCE =  5.91 ANGSTROMS                       
REMARK 525    HOH A1256        DISTANCE =  6.11 ANGSTROMS                       
REMARK 525    HOH A1257        DISTANCE =  6.20 ANGSTROMS                       
REMARK 525    HOH A1258        DISTANCE =  6.24 ANGSTROMS                       
REMARK 525    HOH A1259        DISTANCE =  6.38 ANGSTROMS                       
REMARK 525    HOH A1260        DISTANCE =  6.82 ANGSTROMS                       
REMARK 525    HOH A1261        DISTANCE =  6.88 ANGSTROMS                       
REMARK 525    HOH A1262        DISTANCE =  7.08 ANGSTROMS                       
REMARK 525    HOH A1263        DISTANCE =  7.28 ANGSTROMS                       
REMARK 525    HOH A1264        DISTANCE =  7.29 ANGSTROMS                       
REMARK 525    HOH A1265        DISTANCE =  8.16 ANGSTROMS                       
REMARK 525    HOH B1111        DISTANCE =  5.93 ANGSTROMS                       
REMARK 525    HOH B1112        DISTANCE =  5.98 ANGSTROMS                       
REMARK 525    HOH B1113        DISTANCE =  6.80 ANGSTROMS                       
REMARK 525    HOH B1114        DISTANCE =  6.84 ANGSTROMS                       
REMARK 525    HOH B1115        DISTANCE =  6.92 ANGSTROMS                       
REMARK 525    HOH B1116        DISTANCE =  6.93 ANGSTROMS                       
REMARK 525    HOH B1117        DISTANCE =  7.47 ANGSTROMS                       
REMARK 525    HOH B1118        DISTANCE =  7.87 ANGSTROMS                       
REMARK 525    HOH B1119        DISTANCE =  8.77 ANGSTROMS                       
REMARK 525    HOH B1120        DISTANCE =  9.20 ANGSTROMS                       
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 701  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A 809   O                                                      
REMARK 620 2 HOH A 947   O    88.4                                              
REMARK 620 3 HOH A1070   O   164.8  88.4                                        
REMARK 620 4 HOH A1094   O    82.8 164.8  96.8                                  
REMARK 620 5 HOH A1170   O    79.8  75.2  85.1  91.1                            
REMARK 620 6 HOH A 809   O    42.8 103.8 152.0  77.9 122.2                      
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 700                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 701                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 702                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 703                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 704                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 705                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue AMP B 700                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 701                 
DBREF  5NRH A    1   312  UNP    A3NZL3   DDL_BURP0        1    312             
DBREF  5NRH 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 700      23                                                       
HET     MG  A 701       1                                                       
HET    SO4  A 702       5                                                       
HET    EDO  A 703       4                                                       
HET    EDO  A 704       4                                                       
HET    EDO  A 705       4                                                       
HET    AMP  B 700      23                                                       
HET    SO4  B 701       5                                                       
HETNAM     AMP ADENOSINE MONOPHOSPHATE                                          
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     SO4 SULFATE ION                                                      
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   3  AMP    2(C10 H14 N5 O7 P)                                           
FORMUL   4   MG    MG 2+                                                        
FORMUL   5  SO4    2(O4 S 2-)                                                   
FORMUL   6  EDO    3(C2 H6 O2)                                                  
FORMUL  11  HOH   *785(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  GLY A  115  1                                  13    
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  PHE B    9  5                                   5    
HELIX   16 AB7 GLU B   22  ALA B   40  1                                  19    
HELIX   17 AB8 ALA B   55  GLU B   60  1                                   6    
HELIX   18 AB9 GLY B   71  GLU B   75  5                                   5    
HELIX   19 AC1 GLY B   77  TYR B   86  1                                  10    
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 GLU B  152  VAL B  156  5                                   5    
HELIX   24 AC6 SER B  163  ASP B  165  5                                   3    
HELIX   25 AC7 ALA B  166  LYS B  176  1                                  11    
HELIX   26 AC8 ASP B  216  ILE B  222  1                                   7    
HELIX   27 AC9 ASP B  235  VAL B  252  1                                  18    
HELIX   28 AD1 SER B  286  VAL B  295  1                                  10    
HELIX   29 AD2 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  LEU A 274   N  ASP A 262           
SHEET    1 AA4 4 ASP B  43  PHE B  47  0                                        
SHEET    2 AA4 4 LYS B  11  LEU B  15  1  N  VAL B  12   O  ASP B  43           
SHEET    3 AA4 4 ARG B  64  ASN B  67  1  O  PHE B  66   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  VAL B 161   N  LEU B 145           
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 GLY B 189  ALA B 198 -1  N  GLU B 192   O  ILE B 208           
SHEET    4 AA6 5 TRP B 258  ASP B 266 -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        MG    MG A 701                 O  BHOH A 809     1555   1555  2.17  
LINK        MG    MG A 701                 O   HOH A 947     1555   1555  1.99  
LINK        MG    MG A 701                 O   HOH A1070     1555   1555  1.94  
LINK        MG    MG A 701                 O   HOH A1094     1555   1555  2.20  
LINK        MG    MG A 701                 O   HOH A1170     1555   1555  2.04  
LINK        MG    MG A 701                 O  AHOH A 809     1555   1555  2.94  
CISPEP   1 VAL A  143    PRO A  144          0        -2.66                     
CISPEP   2 SER A  151    GLU A  152          0        15.18                     
CISPEP   3 ILE A  230    PRO A  231          0         3.49                     
CISPEP   4 VAL B  143    PRO B  144          0        -0.38                     
CISPEP   5 ILE B  230    PRO B  231          0        -5.62                     
SITE     1 AC1 15 LYS A 104  PHE A 146  LYS A 148  GLU A 184                    
SITE     2 AC1 15 LYS A 185  SER A 186  ILE A 187  GLU A 192                    
SITE     3 AC1 15 PHE A 214  TYR A 215  GLU A 275  HOH A 804                    
SITE     4 AC1 15 HOH A 842  HOH A 920  HOH A 951                               
SITE     1 AC2  6 HIS A  70  HOH A 809  HOH A 947  HOH A1070                    
SITE     2 AC2  6 HOH A1094  HOH A1170                                          
SITE     1 AC3  7 ARG A 293  GLY A 298  TYR A 299  HOH A 818                    
SITE     2 AC3  7 HOH A 819  HOH A1003  ARG B 293                               
SITE     1 AC4  4 GLU A  24  ARG A  31  HOH A 826  HOH A 949                    
SITE     1 AC5  4 LEU A 201  ASP A 202  VAL A 295  HOH A 856                    
SITE     1 AC6  8 ALA A 219  LYS A 220  ALA A 223  ASN A 224                    
SITE     2 AC6  8 ASP A 225  THR A 226  TYR A 228  HOH A 973                    
SITE     1 AC7 16 LYS B 104  PHE B 146  LYS B 148  SER B 155                    
SITE     2 AC7 16 GLU B 184  LYS B 185  SER B 186  ILE B 187                    
SITE     3 AC7 16 GLU B 192  PHE B 214  TYR B 215  LEU B 274                    
SITE     4 AC7 16 GLU B 275  HOH B 852  HOH B 912  HOH B 949                    
SITE     1 AC8  8 HIS B  70  TYR B 221  ARG B 260  ASN B 277                    
SITE     2 AC8  8 PRO B 280  GLY B 281  HOH B 827  HOH B 950                    
CRYST1   69.648   61.150   70.079  90.00  90.17  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      0.014358  0.000000  0.000043        0.00000                         
SCALE2      0.000000  0.016353  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.014270        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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