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Database: PDB
Entry: 2J44
LinkDB: 2J44
Original site: 2J44 
HEADER    CARBOHYDRATE-BINDING MODULE             24-AUG-06   2J44              
TITLE     ALPHA-GLUCAN BINDING BY A STREPTOCOCCAL VIRULENCE FACTOR              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ALKALINE AMYLOPULLULANASE;                                 
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: CARBOHYDRATE-BINDING MODULE, RESIDUES                      
COMPND   5  135-312,314,316-353;                                                
COMPND   6 SYNONYM: SPNDX;                                                      
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 OTHER_DETAILS: TANDEM FAMILY 41 CARBOHYDRATE BINDING                 
COMPND   9  MODULES                                                             
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: STREPTOCOCCUS PNEUMONIAE;                       
SOURCE   3 ORGANISM_TAXID: 1313;                                                
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)                                  
KEYWDS    VIRULENCE, PULLULANASE, GLYCOGEN BINDING, STREPTOCOCCUS               
KEYWDS   2 PNEUMONIAE, CARBOHYDRATE-BINDING MODULE                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.LAMMERTS VAN BUEREN,M.HIGGINS,D.WANG,R.D.BURKE,                     
AUTHOR   2 A.B.BORASTON                                                         
REVDAT   3   24-FEB-09 2J44    1       VERSN                                    
REVDAT   2   29-APR-08 2J44    1       VERSN  JRNL   REMARK                     
REVDAT   1   11-DEC-06 2J44    0                                                
JRNL        AUTH   A.LAMMERTS VAN BUEREN,M.HIGGINS,D.WANG,R.D.BURKE,            
JRNL        AUTH 2 A.B.BORASTON                                                 
JRNL        TITL   IDENTIFICATION AND STRUCTURAL BASIS OF BINDING TO            
JRNL        TITL 2 HOST LUNG GLYCOGEN BY STREPTOCOCCAL VIRULENCE                
JRNL        TITL 3 FACTORS.                                                     
JRNL        REF    NAT.STRUCT.MOL.BIOL.          V.  14    76 2007              
JRNL        REFN                   ISSN 1545-9993                               
JRNL        PMID   17187076                                                     
JRNL        DOI    10.1038/NSMB1187                                             
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.1  ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.1.24                                        
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 15070                          
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) : 0.225                           
REMARK   3   R VALUE            (WORKING SET) : 0.221                           
REMARK   3   FREE R VALUE                     : 0.304                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 802                             
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.10                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.15                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1083                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2380                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 69                           
REMARK   3   BIN FREE R VALUE                    : 0.3370                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1801                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 82                                      
REMARK   3   SOLVENT ATOMS            : 187                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 49.09                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.99000                                             
REMARK   3    B22 (A**2) : 0.41000                                              
REMARK   3    B33 (A**2) : 0.58000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.243         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.170         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.484         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.945                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.910                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1937 ; 0.011 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2635 ; 1.554 ; 1.989       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   218 ; 8.558 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   284 ; 0.118 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1453 ; 0.005 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   952 ; 0.234 ; 0.200       
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):   164 ; 0.209 ; 0.200       
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):    25 ; 0.329 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    15 ; 0.170 ; 0.200       
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):  1083 ; 1.058 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1745 ; 1.890 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   854 ; 2.437 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   889 ; 3.816 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
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          
REMARK   3  RIDING POSITIONS.                                                   
REMARK   4                                                                      
REMARK   4 2J44 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 25-AUG-06.                  
REMARK 100 THE PDBE ID CODE IS EBI-29835.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 113.0                              
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU                             
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 15873                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 19.510                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.9                               
REMARK 200  DATA REDUNDANCY                : 4.400                              
REMARK 200  R MERGE                    (I) : 0.07000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.3000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.17                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.31                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.37000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.100                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: SPYD                                                  
REMARK 200 STARTING MODEL: PDB ENTRY 2J43                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS  (%): 46.84                                      
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.33                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X+1/2,Y+1/2,-Z                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       25.27750            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       44.56200            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       25.27750            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       44.56200            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY.  THE REMARK MAY ALSO PROVIDE INFORMATION ON              
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 GENERATING THE BIOMOLECULE                                           
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE:  1                                                      
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PQS                                                   
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 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    GLN A   113  -  O    HOH A  2105              1.97            
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  60   CB  -  CG  -  OD2 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    ASP A 126   CB  -  CG  -  OD2 ANGL. DEV. =   6.9 DEGREES          
REMARK 500    ASP A 209   CB  -  CG  -  OD2 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 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    ASN A   8       68.47     79.64                                   
REMARK 500    ASP A  31     -130.90     66.01                                   
REMARK 500    ASP A  32       39.33    -78.96                                   
REMARK 500    ASN A  39       64.31     63.95                                   
REMARK 500    ASN A 128       79.35    103.75                                   
REMARK 500    TYR A 129      -64.13     93.96                                   
REMARK 500    SER A 145       87.97   -169.44                                   
REMARK 500    ALA A 146     -119.04    160.96                                   
REMARK 500    GLN A 147       86.83     65.83                                   
REMARK 500    TRP A 148      135.03    -35.87                                   
REMARK 500    PRO A 149       59.92   -109.30                                   
REMARK 500    ASN A 169      154.28     88.31                                   
REMARK 500    GLU A 170     -153.47     56.71                                   
REMARK 500    ILE A 189      -61.04     53.54                                   
REMARK 500    THR A 197     -110.83    -91.59                                   
REMARK 500    ASP A 198       32.06      5.34                                   
REMARK 500    HIS A 202      -88.16   -134.97                                   
REMARK 500    SER A 203      -33.80    107.51                                   
REMARK 500    ASP A 209     -123.73     48.41                                   
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 ASP A  126     GLY A  127                  144.63                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    TYR A 129        21.2      L          L   OUTSIDE RANGE           
REMARK 500    ASP A 186        23.8      L          L   OUTSIDE RANGE           
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 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                              ZN A1224  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 202   NE2                                                    
REMARK 620 2 ASP A 198   OD2  82.9                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A1225  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 222   ND1                                                    
REMARK 620 2 HOH A2177   O   110.9                                              
REMARK 620 3 HOH A2178   O   100.4 130.8                                        
REMARK 620 4 ASP A  60   OD2 111.6 103.4  98.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A1226  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 153   OD1                                                    
REMARK 620 2 HOH A2179   O    89.0                                              
REMARK 620 N                    1                                               
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC A1227                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC A1228                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC A1232                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC A1229                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC A1230                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC A1231                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC A1233                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN A1224                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN A1225                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN A1226                 
DBREF  2J44 A    7   184  UNP    Q97SQ7   Q97SQ7_STRPN   135    312             
DBREF  2J44 A  185   185  UNP    Q97SQ7   Q97SQ7_STRPN   314    314             
DBREF  2J44 A  186   223  UNP    Q97SQ7   Q97SQ7_STRPN   316    353             
SEQRES   1 A  217  ASP ASN TYR PHE ARG ILE HIS VAL LYS LYS LEU PRO GLU          
SEQRES   2 A  217  GLU ASN LYS ASP ALA GLN GLY LEU TRP THR TRP ASP ASP          
SEQRES   3 A  217  VAL GLU LYS PRO SER GLU ASN TRP PRO ASN GLY ALA LEU          
SEQRES   4 A  217  SER PHE LYS ASP ALA LYS LYS ASP ASP TYR GLY TYR TYR          
SEQRES   5 A  217  LEU ASP VAL LYS LEU LYS GLY GLU GLN ALA LYS LYS ILE          
SEQRES   6 A  217  SER PHE LEU ILE ASN ASN THR ALA GLY LYS ASN LEU THR          
SEQRES   7 A  217  GLY ASP LYS SER VAL GLU LYS LEU VAL PRO LYS MET ASN          
SEQRES   8 A  217  GLU ALA TRP LEU ASP GLN ASP TYR LYS VAL PHE SER TYR          
SEQRES   9 A  217  GLU PRO GLN PRO ALA GLY THR VAL ARG VAL ASN TYR TYR          
SEQRES  10 A  217  ARG THR ASP GLY ASN TYR ASP LYS LYS SER LEU TRP TYR          
SEQRES  11 A  217  TRP GLY ASP VAL LYS ASN PRO SER SER ALA GLN TRP PRO          
SEQRES  12 A  217  ASP GLY THR ASP PHE THR ALA THR GLY LYS TYR GLY ARG          
SEQRES  13 A  217  TYR ILE ASP ILE PRO LEU ASN GLU ALA ALA ARG GLU PHE          
SEQRES  14 A  217  GLY PHE LEU LEU LEU ASP GLU SER LYS GLY ASP VAL LYS          
SEQRES  15 A  217  ILE ARG LYS GLU ASN TYR LYS PHE THR ASP LEU LYS ASN          
SEQRES  16 A  217  HIS SER GLN ILE PHE LEU LYS ASP ASP ASP GLU SER ILE          
SEQRES  17 A  217  TYR THR ASN PRO TYR TYR VAL HIS ASP                          
HET    GLC  A1227      11                                                       
HET    GLC  A1228      11                                                       
HET    GLC  A1232      12                                                       
HET    GLC  A1229      11                                                       
HET    GLC  A1230      11                                                       
HET    GLC  A1231      11                                                       
HET    GLC  A1233      12                                                       
HET     ZN  A1224       1                                                       
HET     ZN  A1225       1                                                       
HET     ZN  A1226       1                                                       
HETNAM     GLC ALPHA-D-GLUCOSE                                                  
HETNAM      ZN ZINC ION                                                         
FORMUL   2  GLC    7(C6 H12 O6)                                                 
FORMUL   4   ZN    3(ZN 2+)                                                     
FORMUL   7  HOH   *187(H2 O1)                                                   
HELIX    1   1 ASN A   21  ASP A   23  5                                   3    
HELIX    2   2 LYS A   48  ALA A   50  5                                   3    
SHEET    1  AA 5 LYS A  51  LYS A  52  0                                        
SHEET    2  AA 5 TYR A  57  LYS A  62 -1  O  TYR A  58   N  LYS A  51           
SHEET    3  AA 5 TYR A   9  VAL A  14 -1  O  PHE A  10   N  VAL A  61           
SHEET    4  AA 5 GLU A  98  LEU A 101  1  O  ALA A  99   N  HIS A  13           
SHEET    5  AA 5 VAL A 107  PHE A 108 -1  O  PHE A 108   N  TRP A 100           
SHEET    1  AB 4 LEU A  45  SER A  46  0                                        
SHEET    2  AB 4 GLN A  25  ASP A  31 -1  O  LEU A  27   N  LEU A  45           
SHEET    3  AB 4 LYS A  70  ASN A  77 -1  O  SER A  72   N  TRP A  30           
SHEET    4  AB 4 LYS A  87  GLU A  90 -1  O  LYS A  87   N  PHE A  73           
SHEET    1  AC 4 ALA A 156  GLY A 158  0                                        
SHEET    2  AC 4 GLY A 161  PRO A 167 -1  O  GLY A 161   N  GLY A 158           
SHEET    3  AC 4 THR A 117  TYR A 123 -1  O  VAL A 118   N  ILE A 166           
SHEET    4  AC 4 GLN A 204  LYS A 208  1  O  ILE A 205   N  ASN A 121           
SHEET    1  AD 4 THR A 152  ASP A 153  0                                        
SHEET    2  AD 4 LYS A 132  TRP A 137 -1  O  LEU A 134   N  THR A 152           
SHEET    3  AD 4 PHE A 175  ASP A 181 -1  O  GLY A 176   N  TRP A 137           
SHEET    4  AD 4 TYR A 194  PHE A 196 -1  O  TYR A 194   N  PHE A 177           
LINK        ZN    ZN A1224                 NE2 HIS A 202     1555   1555  2.35  
LINK        ZN    ZN A1224                 OD2 ASP A 198     1555   1555  2.33  
LINK        ZN    ZN A1225                 ND1 HIS A 222     1555   4444  2.26  
LINK        ZN    ZN A1225                 OD2 ASP A  60     1555   1555  1.90  
LINK        ZN    ZN A1225                 O   HOH A2178     1555   1555  2.61  
LINK        ZN    ZN A1225                 O   HOH A2177     1555   1555  2.24  
LINK        ZN    ZN A1226                 O   HOH A2179     1555   1555  2.23  
LINK        ZN    ZN A1226                 OD1 ASP A 153     1555   1555  2.19  
LINK         C1  GLC A1227                 O4  GLC A1232     1555   1555  1.45  
LINK         O4  GLC A1227                 C1  GLC A1228     1555   1555  1.44  
LINK         C1  GLC A1229                 O4  GLC A1233     1555   1555  1.44  
LINK         O4  GLC A1229                 C1  GLC A1230     1555   1555  1.44  
LINK         O4  GLC A1230                 C1  GLC A1231     1555   1555  1.45  
CISPEP   1 TRP A   40    PRO A   41          0        -4.47                     
CISPEP   2 GLY A   65    GLU A   66          0        -0.01                     
CISPEP   3 GLU A   66    GLN A   67          0        -1.19                     
CISPEP   4 ALA A   79    GLY A   80          0       -16.79                     
CISPEP   5 GLY A  127    ASN A  128          0        -0.48                     
CISPEP   6 ASN A  128    TYR A  129          0         1.08                     
CISPEP   7 ASP A  130    LYS A  131          0        26.98                     
CISPEP   8 SER A  145    ALA A  146          0         2.38                     
CISPEP   9 TRP A  148    PRO A  149          0        -0.26                     
CISPEP  10 ASP A  150    GLY A  151          0        15.92                     
SITE     1 AC1  4 TRP A 148  LYS A 188  GLC A1228  GLC A1232                    
SITE     1 AC2  6 TRP A 135  TRP A 137  ASN A 193  GLC A1227                    
SITE     2 AC2  6 HOH A2180  HOH A2182                                          
SITE     1 AC3  2 THR A 155  GLC A1227                                          
SITE     1 AC4  5 TRP A  40  GLC A1230  GLC A1233  HOH A2183                    
SITE     2 AC4  5 HOH A2184                                                     
SITE     1 AC5 10 TRP A  28  TRP A  30  LEU A  74  ASP A  86                    
SITE     2 AC5 10 GLC A1229  GLC A1231  HOH A2183  HOH A2184                    
SITE     3 AC5 10 HOH A2185  HOH A2186                                          
SITE     1 AC6  4 TRP A  30  GLY A  80  LYS A  81  GLC A1230                    
SITE     1 AC7  1 GLC A1229                                                     
SITE     1 AC8  3 ASP A   7  ASP A 198  HIS A 202                               
SITE     1 AC9  4 ASP A  60  HIS A 222  HOH A2177  HOH A2178                    
SITE     1 BC1  4 GLY A 151  ASP A 153  GLU A 182  HOH A2179                    
CRYST1   50.555   89.124   59.997  90.00  90.00  90.00 P 21 21 2     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      0.019780  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011220  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.016667        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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