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Database: PDB
Entry: 5ITW
LinkDB: 5ITW
Original site: 5ITW 
HEADER    OXIDOREDUCTASE                          17-MAR-16   5ITW              
TITLE     CRYSTAL STRUCTURE OF BACILLUS SUBTILIS BACC DIHYDROANTICAPSIN 7-      
TITLE    2 DEHYDROGENASE                                                        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: DIHYDROANTICAPSIN 7-DEHYDROGENASE;                         
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 SYNONYM: BACILYSIN BIOSYNTHESIS OXIDOREDUCTASE BACC;                 
COMPND   5 EC: 1.1.1.385;                                                       
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 OTHER_DETAILS: SULFATE IONS ARE MODELLED                             
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS (STRAIN 168);                 
SOURCE   3 ORGANISM_TAXID: 224308;                                              
SOURCE   4 STRAIN: 168;                                                         
SOURCE   5 GENE: BACC, YWFD, BSU37720, IPA-82D;                                 
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET22B                                    
KEYWDS    OXIDOREDUCTASE, SHORT-CHAIN DEHYDROGENASES/REDUCTASES, ROSSMANN FOLD, 
KEYWDS   2 NAD(P) BINDING DOMAIN                                                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.PERINBAM,H.BALARAM,T.N.G.ROW,B.GOPAL                                
REVDAT   2   06-DEC-17 5ITW    1       JRNL                                     
REVDAT   1   22-FEB-17 5ITW    0                                                
JRNL        AUTH   K.PERINBAM,H.BALARAM,T.N.GURU ROW,B.GOPAL                    
JRNL        TITL   PROBING THE INFLUENCE OF NON-COVALENT CONTACT NETWORKS       
JRNL        TITL 2 IDENTIFIED BY CHARGE DENSITY ANALYSIS ON THE OXIDOREDUCTASE  
JRNL        TITL 3 BACC.                                                        
JRNL        REF    PROTEIN ENG. DES. SEL.        V.  30   265 2017              
JRNL        REFN                   ESSN 1741-0134                               
JRNL        PMID   28158843                                                     
JRNL        DOI    10.1093/PROTEIN/GZX006                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.19 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0049                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.19                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 32.95                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 290778                         
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) : 0.139                           
REMARK   3   R VALUE            (WORKING SET) : 0.138                           
REMARK   3   FREE R VALUE                     : 0.163                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 15057                           
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) : 1.19                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.22                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 20267                        
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 94.40                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3520                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 1097                         
REMARK   3   BIN FREE R VALUE                    : 0.3390                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 7576                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 40                                      
REMARK   3   SOLVENT ATOMS            : 987                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 10.10                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 18.26                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.58000                                             
REMARK   3    B22 (A**2) : 0.55000                                              
REMARK   3    B33 (A**2) : -0.19000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.59000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.034         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.034         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.030         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.581         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.980                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.974                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  7962 ; 0.012 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  7703 ; 0.008 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 10848 ; 1.583 ; 1.962       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 17740 ; 1.388 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1073 ; 5.762 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   315 ;40.828 ;26.571       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1367 ;11.610 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    15 ;12.687 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1287 ; 0.101 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  9268 ; 0.008 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  1675 ; 0.006 ; 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):  4212 ; 2.130 ; 1.530       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  4211 ; 2.109 ; 1.530       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  5301 ; 2.619 ; 2.305       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  5302 ; 2.623 ; 2.305       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3750 ; 3.825 ; 1.899       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  3719 ; 3.773 ; 1.881       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  5496 ; 4.346 ; 2.687       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2): 10002 ; 5.125 ;14.596       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  9442 ; 4.437 ;13.669       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2): 15665 ; 3.520 ; 3.000       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):   298 ;36.519 ; 5.000       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2): 16221 ;15.650 ; 5.000       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NCS TYPE: LOCAL                                                    
REMARK   3   NUMBER OF DIFFERENT NCS PAIRS  : 6                                 
REMARK   3  GROUP  CHAIN1    RANGE     CHAIN2     RANGE    COUNT RMS  WEIGHT    
REMARK   3    1     A     1    255       B     1    255   15973  0.10  0.05     
REMARK   3    2     A     1    255       C     1    255   15739  0.11  0.05     
REMARK   3    3     A     1    255       D     1    255   15671  0.09  0.05     
REMARK   3    4     B     1    255       C     1    255   15630  0.09  0.05     
REMARK   3    5     B     1    255       D     1    255   15531  0.08  0.05     
REMARK   3    6     C     1    255       D     1    255   15315  0.09  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   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 5ITW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 23-MAR-16.                  
REMARK 100 THE DEPOSITION ID IS D_1000219392.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 12-SEP-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : BM14                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.95372                            
REMARK 200  MONOCHROMATOR                  : BAND PASS 1.9X10-4 FOR A SI(111)   
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 225 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : IMOSFLM 7.2.0                      
REMARK 200  DATA SCALING SOFTWARE          : SCALA 3.3.21                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 305981                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.187                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 32.950                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY                : 4.100                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.07100                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.2000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.19                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.25                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.80                               
REMARK 200  R MERGE FOR SHELL          (I) : 1.06700                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.500                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER 2.5.6                                          
REMARK 200 STARTING MODEL: 3AWD                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 45.40                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.25                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M AMMONIUM SULFATE, 0.1M BIS-TRIS     
REMARK 280  PH6.5, 25% W/V POLYETHYLENE GLYCOL 3350, 10% GLYCEROL               
REMARK 280  CRYOPROTECTANT, 0.05M TRIS, 0.25M NACL, MICROBATCH, TEMPERATURE     
REMARK 280  291.15K                                                             
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       43.60000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 15020 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 33540 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -244.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLU B  45    CG   CD   OE1  OE2                                  
REMARK 470     ARG B  49    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B  50    CD   CE   NZ                                        
REMARK 470     GLU C  45    CG   CD   OE1  OE2                                  
REMARK 470     HIS C  78    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LEU C 191    CD1  CD2                                            
REMARK 470     LYS C 194    NZ                                                  
REMARK 470     GLU C 198    CD   OE1  OE2                                       
REMARK 470     LEU C 204    CG   CD1  CD2                                       
REMARK 470     HIS D  78    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LYS D 194    CG   CD   CE   NZ                                   
REMARK 470     GLU D 198    CD   OE1  OE2                                       
REMARK 470     GLU D 201    CG   CD   OE1  OE2                                  
REMARK 470     THR D 203    CG2                                                 
REMARK 470     LEU D 204    CD1                                                 
REMARK 470     GLU D 205    CG   CD   OE1  OE2                                  
REMARK 470     GLU D 206    CG   CD   OE1  OE2                                  
REMARK 470     LYS D 209    CG   CD   CE   NZ                                   
REMARK 470     GLU D 210    CG   CD   OE1  OE2                                  
REMARK 470     LYS D 211    CD   CE   NZ                                        
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   672     O    HOH A   699              1.43            
REMARK 500   O    HOH B   579     O    HOH B   654              1.90            
REMARK 500   O    HOH A   610     O    HOH A   672              1.90            
REMARK 500   O    HOH A   494     O    HOH A   639              1.94            
REMARK 500   O    HOH C   606     O    HOH D   553              1.95            
REMARK 500   O    HOH C   564     O    HOH C   585              1.96            
REMARK 500   O    HOH A   402     O    HOH A   677              1.99            
REMARK 500   O    HOH B   591     O    HOH B   665              1.99            
REMARK 500   O    HOH B   518     O    HOH B   654              2.02            
REMARK 500   O    HOH A   652     O    HOH B   619              2.05            
REMARK 500   O    HOH A   459     O    HOH A   620              2.08            
REMARK 500   O    HOH D   553     O    HOH D   563              2.10            
REMARK 500   OH   TYR C    21     OE2  GLU C    51              2.13            
REMARK 500   O    HOH A   612     O    HOH D   524              2.13            
REMARK 500   OH   TYR D    21     OE2  GLU D    51              2.16            
REMARK 500   NZ   LYS A   122     O    HOH A   401              2.17            
REMARK 500   O    HOH B   651     O    HOH B   667              2.19            
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    MET A   3   CG  -  SD  -  CE  ANGL. DEV. = -18.8 DEGREES          
REMARK 500    MET B   1   CG  -  SD  -  CE  ANGL. DEV. =  -9.6 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    LEU A 114      -56.54   -121.93                                   
REMARK 500    CYS A 140     -135.61    -92.92                                   
REMARK 500    CYS A 140     -136.59    -92.92                                   
REMARK 500    ASP A 249       17.84   -142.48                                   
REMARK 500    LEU B 114      -56.34   -122.12                                   
REMARK 500    CYS B 140     -134.56    -94.06                                   
REMARK 500    ASP B 249       17.70   -142.59                                   
REMARK 500    LEU C 114      -54.82   -120.39                                   
REMARK 500    CYS C 140     -136.05    -92.64                                   
REMARK 500    ASP C 249       17.70   -140.61                                   
REMARK 500    LEU D 114      -52.96   -123.89                                   
REMARK 500    CYS D 140     -136.15    -92.94                                   
REMARK 500    ASP D 249       17.37   -140.81                                   
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 C 629        DISTANCE =  6.40 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 C 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 C 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 C 303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 D 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 D 302                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5ITV   RELATED DB: PDB                                   
DBREF  5ITW A    3   255  UNP    P39640   BACC_BACSU       1    253             
DBREF  5ITW B    3   255  UNP    P39640   BACC_BACSU       1    253             
DBREF  5ITW C    3   255  UNP    P39640   BACC_BACSU       1    253             
DBREF  5ITW D    3   255  UNP    P39640   BACC_BACSU       1    253             
SEQADV 5ITW MET A    1  UNP  P39640              EXPRESSION TAG                 
SEQADV 5ITW ILE A    2  UNP  P39640              EXPRESSION TAG                 
SEQADV 5ITW MET B    1  UNP  P39640              EXPRESSION TAG                 
SEQADV 5ITW ILE B    2  UNP  P39640              EXPRESSION TAG                 
SEQADV 5ITW MET C    1  UNP  P39640              EXPRESSION TAG                 
SEQADV 5ITW ILE C    2  UNP  P39640              EXPRESSION TAG                 
SEQADV 5ITW MET D    1  UNP  P39640              EXPRESSION TAG                 
SEQADV 5ITW ILE D    2  UNP  P39640              EXPRESSION TAG                 
SEQRES   1 A  255  MET ILE MET ASN LEU THR ASP LYS THR VAL LEU ILE THR          
SEQRES   2 A  255  GLY GLY ALA SER GLY ILE GLY TYR ALA ALA VAL GLN ALA          
SEQRES   3 A  255  PHE LEU GLY GLN GLN ALA ASN VAL VAL VAL ALA ASP ILE          
SEQRES   4 A  255  ASP GLU ALA GLN GLY GLU ALA MET VAL ARG LYS GLU ASN          
SEQRES   5 A  255  ASN ASP ARG LEU HIS PHE VAL GLN THR ASP ILE THR ASP          
SEQRES   6 A  255  GLU ALA ALA CYS GLN HIS ALA VAL GLU SER ALA VAL HIS          
SEQRES   7 A  255  THR PHE GLY GLY LEU ASP VAL LEU ILE ASN ASN ALA GLY          
SEQRES   8 A  255  ILE GLU ILE VAL ALA PRO ILE HIS GLU MET GLU LEU SER          
SEQRES   9 A  255  ASP TRP ASN LYS VAL LEU GLN VAL ASN LEU THR GLY MET          
SEQRES  10 A  255  PHE LEU MET SER LYS HIS ALA LEU LYS HIS MET LEU ALA          
SEQRES  11 A  255  ALA GLY LYS GLY ASN ILE ILE ASN THR CYS SER VAL GLY          
SEQRES  12 A  255  GLY LEU VAL ALA TRP PRO ASP ILE PRO ALA TYR ASN ALA          
SEQRES  13 A  255  SER LYS GLY GLY VAL LEU GLN LEU THR LYS SER MET ALA          
SEQRES  14 A  255  VAL ASP TYR ALA LYS HIS GLN ILE ARG VAL ASN CYS VAL          
SEQRES  15 A  255  CYS PRO GLY ILE ILE ASP THR PRO LEU ASN GLU LYS SER          
SEQRES  16 A  255  PHE LEU GLU ASN ASN GLU GLY THR LEU GLU GLU ILE LYS          
SEQRES  17 A  255  LYS GLU LYS ALA LYS VAL ASN PRO LEU LEU ARG LEU GLY          
SEQRES  18 A  255  LYS PRO GLU GLU ILE ALA ASN VAL MET LEU PHE LEU ALA          
SEQRES  19 A  255  SER ASP LEU SER SER TYR MET THR GLY SER ALA ILE THR          
SEQRES  20 A  255  ALA ASP GLY GLY TYR THR ALA GLN                              
SEQRES   1 B  255  MET ILE MET ASN LEU THR ASP LYS THR VAL LEU ILE THR          
SEQRES   2 B  255  GLY GLY ALA SER GLY ILE GLY TYR ALA ALA VAL GLN ALA          
SEQRES   3 B  255  PHE LEU GLY GLN GLN ALA ASN VAL VAL VAL ALA ASP ILE          
SEQRES   4 B  255  ASP GLU ALA GLN GLY GLU ALA MET VAL ARG LYS GLU ASN          
SEQRES   5 B  255  ASN ASP ARG LEU HIS PHE VAL GLN THR ASP ILE THR ASP          
SEQRES   6 B  255  GLU ALA ALA CYS GLN HIS ALA VAL GLU SER ALA VAL HIS          
SEQRES   7 B  255  THR PHE GLY GLY LEU ASP VAL LEU ILE ASN ASN ALA GLY          
SEQRES   8 B  255  ILE GLU ILE VAL ALA PRO ILE HIS GLU MET GLU LEU SER          
SEQRES   9 B  255  ASP TRP ASN LYS VAL LEU GLN VAL ASN LEU THR GLY MET          
SEQRES  10 B  255  PHE LEU MET SER LYS HIS ALA LEU LYS HIS MET LEU ALA          
SEQRES  11 B  255  ALA GLY LYS GLY ASN ILE ILE ASN THR CYS SER VAL GLY          
SEQRES  12 B  255  GLY LEU VAL ALA TRP PRO ASP ILE PRO ALA TYR ASN ALA          
SEQRES  13 B  255  SER LYS GLY GLY VAL LEU GLN LEU THR LYS SER MET ALA          
SEQRES  14 B  255  VAL ASP TYR ALA LYS HIS GLN ILE ARG VAL ASN CYS VAL          
SEQRES  15 B  255  CYS PRO GLY ILE ILE ASP THR PRO LEU ASN GLU LYS SER          
SEQRES  16 B  255  PHE LEU GLU ASN ASN GLU GLY THR LEU GLU GLU ILE LYS          
SEQRES  17 B  255  LYS GLU LYS ALA LYS VAL ASN PRO LEU LEU ARG LEU GLY          
SEQRES  18 B  255  LYS PRO GLU GLU ILE ALA ASN VAL MET LEU PHE LEU ALA          
SEQRES  19 B  255  SER ASP LEU SER SER TYR MET THR GLY SER ALA ILE THR          
SEQRES  20 B  255  ALA ASP GLY GLY TYR THR ALA GLN                              
SEQRES   1 C  255  MET ILE MET ASN LEU THR ASP LYS THR VAL LEU ILE THR          
SEQRES   2 C  255  GLY GLY ALA SER GLY ILE GLY TYR ALA ALA VAL GLN ALA          
SEQRES   3 C  255  PHE LEU GLY GLN GLN ALA ASN VAL VAL VAL ALA ASP ILE          
SEQRES   4 C  255  ASP GLU ALA GLN GLY GLU ALA MET VAL ARG LYS GLU ASN          
SEQRES   5 C  255  ASN ASP ARG LEU HIS PHE VAL GLN THR ASP ILE THR ASP          
SEQRES   6 C  255  GLU ALA ALA CYS GLN HIS ALA VAL GLU SER ALA VAL HIS          
SEQRES   7 C  255  THR PHE GLY GLY LEU ASP VAL LEU ILE ASN ASN ALA GLY          
SEQRES   8 C  255  ILE GLU ILE VAL ALA PRO ILE HIS GLU MET GLU LEU SER          
SEQRES   9 C  255  ASP TRP ASN LYS VAL LEU GLN VAL ASN LEU THR GLY MET          
SEQRES  10 C  255  PHE LEU MET SER LYS HIS ALA LEU LYS HIS MET LEU ALA          
SEQRES  11 C  255  ALA GLY LYS GLY ASN ILE ILE ASN THR CYS SER VAL GLY          
SEQRES  12 C  255  GLY LEU VAL ALA TRP PRO ASP ILE PRO ALA TYR ASN ALA          
SEQRES  13 C  255  SER LYS GLY GLY VAL LEU GLN LEU THR LYS SER MET ALA          
SEQRES  14 C  255  VAL ASP TYR ALA LYS HIS GLN ILE ARG VAL ASN CYS VAL          
SEQRES  15 C  255  CYS PRO GLY ILE ILE ASP THR PRO LEU ASN GLU LYS SER          
SEQRES  16 C  255  PHE LEU GLU ASN ASN GLU GLY THR LEU GLU GLU ILE LYS          
SEQRES  17 C  255  LYS GLU LYS ALA LYS VAL ASN PRO LEU LEU ARG LEU GLY          
SEQRES  18 C  255  LYS PRO GLU GLU ILE ALA ASN VAL MET LEU PHE LEU ALA          
SEQRES  19 C  255  SER ASP LEU SER SER TYR MET THR GLY SER ALA ILE THR          
SEQRES  20 C  255  ALA ASP GLY GLY TYR THR ALA GLN                              
SEQRES   1 D  255  MET ILE MET ASN LEU THR ASP LYS THR VAL LEU ILE THR          
SEQRES   2 D  255  GLY GLY ALA SER GLY ILE GLY TYR ALA ALA VAL GLN ALA          
SEQRES   3 D  255  PHE LEU GLY GLN GLN ALA ASN VAL VAL VAL ALA ASP ILE          
SEQRES   4 D  255  ASP GLU ALA GLN GLY GLU ALA MET VAL ARG LYS GLU ASN          
SEQRES   5 D  255  ASN ASP ARG LEU HIS PHE VAL GLN THR ASP ILE THR ASP          
SEQRES   6 D  255  GLU ALA ALA CYS GLN HIS ALA VAL GLU SER ALA VAL HIS          
SEQRES   7 D  255  THR PHE GLY GLY LEU ASP VAL LEU ILE ASN ASN ALA GLY          
SEQRES   8 D  255  ILE GLU ILE VAL ALA PRO ILE HIS GLU MET GLU LEU SER          
SEQRES   9 D  255  ASP TRP ASN LYS VAL LEU GLN VAL ASN LEU THR GLY MET          
SEQRES  10 D  255  PHE LEU MET SER LYS HIS ALA LEU LYS HIS MET LEU ALA          
SEQRES  11 D  255  ALA GLY LYS GLY ASN ILE ILE ASN THR CYS SER VAL GLY          
SEQRES  12 D  255  GLY LEU VAL ALA TRP PRO ASP ILE PRO ALA TYR ASN ALA          
SEQRES  13 D  255  SER LYS GLY GLY VAL LEU GLN LEU THR LYS SER MET ALA          
SEQRES  14 D  255  VAL ASP TYR ALA LYS HIS GLN ILE ARG VAL ASN CYS VAL          
SEQRES  15 D  255  CYS PRO GLY ILE ILE ASP THR PRO LEU ASN GLU LYS SER          
SEQRES  16 D  255  PHE LEU GLU ASN ASN GLU GLY THR LEU GLU GLU ILE LYS          
SEQRES  17 D  255  LYS GLU LYS ALA LYS VAL ASN PRO LEU LEU ARG LEU GLY          
SEQRES  18 D  255  LYS PRO GLU GLU ILE ALA ASN VAL MET LEU PHE LEU ALA          
SEQRES  19 D  255  SER ASP LEU SER SER TYR MET THR GLY SER ALA ILE THR          
SEQRES  20 D  255  ALA ASP GLY GLY TYR THR ALA GLN                              
HET    SO4  A 301       5                                                       
HET    SO4  A 302       5                                                       
HET    SO4  B 301       5                                                       
HET    SO4  C 301       5                                                       
HET    SO4  C 302       5                                                       
HET    SO4  C 303       5                                                       
HET    SO4  D 301       5                                                       
HET    SO4  D 302       5                                                       
HETNAM     SO4 SULFATE ION                                                      
FORMUL   5  SO4    8(O4 S 2-)                                                   
FORMUL  13  HOH   *987(H2 O)                                                    
HELIX    1 AA1 SER A   17  GLN A   30  1                                  14    
HELIX    2 AA2 ASP A   40  ASN A   52  1                                  13    
HELIX    3 AA3 ASP A   65  GLY A   81  1                                  17    
HELIX    4 AA4 PRO A   97  MET A  101  5                                   5    
HELIX    5 AA5 GLU A  102  LEU A  114  1                                  13    
HELIX    6 AA6 LEU A  114  GLY A  132  1                                  19    
HELIX    7 AA7 SER A  141  LEU A  145  5                                   5    
HELIX    8 AA8 ILE A  151  ALA A  173  1                                  23    
HELIX    9 AA9 THR A  189  ASN A  200  1                                  12    
HELIX   10 AB1 THR A  203  LYS A  213  1                                  11    
HELIX   11 AB2 LYS A  222  SER A  235  1                                  14    
HELIX   12 AB3 ASP A  236  SER A  239  5                                   4    
HELIX   13 AB4 GLY A  251  GLN A  255  5                                   5    
HELIX   14 AB5 SER B   17  GLN B   30  1                                  14    
HELIX   15 AB6 ASP B   40  ASN B   52  1                                  13    
HELIX   16 AB7 ASP B   65  GLY B   81  1                                  17    
HELIX   17 AB8 GLU B  102  LEU B  114  1                                  13    
HELIX   18 AB9 LEU B  114  GLY B  132  1                                  19    
HELIX   19 AC1 SER B  141  LEU B  145  5                                   5    
HELIX   20 AC2 ILE B  151  ALA B  173  1                                  23    
HELIX   21 AC3 THR B  189  ASN B  200  1                                  12    
HELIX   22 AC4 THR B  203  VAL B  214  1                                  12    
HELIX   23 AC5 LYS B  222  SER B  235  1                                  14    
HELIX   24 AC6 ASP B  236  SER B  239  5                                   4    
HELIX   25 AC7 GLY B  251  GLN B  255  5                                   5    
HELIX   26 AC8 SER C   17  GLN C   30  1                                  14    
HELIX   27 AC9 ASP C   40  ASN C   52  1                                  13    
HELIX   28 AD1 ASP C   65  GLY C   81  1                                  17    
HELIX   29 AD2 PRO C   97  MET C  101  5                                   5    
HELIX   30 AD3 GLU C  102  LEU C  114  1                                  13    
HELIX   31 AD4 LEU C  114  GLY C  132  1                                  19    
HELIX   32 AD5 SER C  141  LEU C  145  5                                   5    
HELIX   33 AD6 ILE C  151  ALA C  173  1                                  23    
HELIX   34 AD7 THR C  189  ASN C  200  1                                  12    
HELIX   35 AD8 THR C  203  LYS C  213  1                                  11    
HELIX   36 AD9 LYS C  222  SER C  235  1                                  14    
HELIX   37 AE1 ASP C  236  SER C  239  5                                   4    
HELIX   38 AE2 GLY C  251  GLN C  255  5                                   5    
HELIX   39 AE3 SER D   17  GLN D   30  1                                  14    
HELIX   40 AE4 ASP D   40  ASN D   52  1                                  13    
HELIX   41 AE5 ASP D   65  GLY D   81  1                                  17    
HELIX   42 AE6 PRO D   97  MET D  101  5                                   5    
HELIX   43 AE7 GLU D  102  LEU D  114  1                                  13    
HELIX   44 AE8 LEU D  114  GLY D  132  1                                  19    
HELIX   45 AE9 SER D  141  LEU D  145  5                                   5    
HELIX   46 AF1 ILE D  151  ALA D  173  1                                  23    
HELIX   47 AF2 THR D  189  ASN D  200  1                                  12    
HELIX   48 AF3 THR D  203  LYS D  213  1                                  11    
HELIX   49 AF4 LYS D  222  SER D  235  1                                  14    
HELIX   50 AF5 ASP D  236  SER D  239  5                                   4    
HELIX   51 AF6 GLY D  251  GLN D  255  5                                   5    
SHEET    1 AA1 7 LEU A  56  GLN A  60  0                                        
SHEET    2 AA1 7 ASN A  33  ASP A  38  1  N  VAL A  36   O  VAL A  59           
SHEET    3 AA1 7 THR A   9  THR A  13  1  N  ILE A  12   O  VAL A  35           
SHEET    4 AA1 7 VAL A  85  ASN A  88  1  O  ILE A  87   N  LEU A  11           
SHEET    5 AA1 7 GLY A 134  THR A 139  1  O  ILE A 137   N  LEU A  86           
SHEET    6 AA1 7 ILE A 177  PRO A 184  1  O  ARG A 178   N  ILE A 136           
SHEET    7 AA1 7 ALA A 245  ALA A 248  1  O  ILE A 246   N  CYS A 183           
SHEET    1 AA2 7 LEU B  56  GLN B  60  0                                        
SHEET    2 AA2 7 ASN B  33  ASP B  38  1  N  VAL B  36   O  VAL B  59           
SHEET    3 AA2 7 THR B   9  THR B  13  1  N  VAL B  10   O  ASN B  33           
SHEET    4 AA2 7 VAL B  85  ASN B  88  1  O  ILE B  87   N  LEU B  11           
SHEET    5 AA2 7 GLY B 134  THR B 139  1  O  ILE B 137   N  LEU B  86           
SHEET    6 AA2 7 ILE B 177  PRO B 184  1  O  ARG B 178   N  ILE B 136           
SHEET    7 AA2 7 ALA B 245  ALA B 248  1  O  ILE B 246   N  CYS B 183           
SHEET    1 AA3 7 LEU C  56  GLN C  60  0                                        
SHEET    2 AA3 7 ASN C  33  ASP C  38  1  N  VAL C  36   O  VAL C  59           
SHEET    3 AA3 7 THR C   9  THR C  13  1  N  VAL C  10   O  ASN C  33           
SHEET    4 AA3 7 VAL C  85  ASN C  88  1  O  ILE C  87   N  LEU C  11           
SHEET    5 AA3 7 GLY C 134  THR C 139  1  O  ILE C 137   N  LEU C  86           
SHEET    6 AA3 7 ILE C 177  PRO C 184  1  O  ARG C 178   N  ILE C 136           
SHEET    7 AA3 7 ALA C 245  ALA C 248  1  O  ILE C 246   N  CYS C 183           
SHEET    1 AA4 7 LEU D  56  GLN D  60  0                                        
SHEET    2 AA4 7 ASN D  33  ASP D  38  1  N  VAL D  36   O  VAL D  59           
SHEET    3 AA4 7 THR D   9  THR D  13  1  N  VAL D  10   O  ASN D  33           
SHEET    4 AA4 7 VAL D  85  ASN D  88  1  O  ILE D  87   N  LEU D  11           
SHEET    5 AA4 7 GLY D 134  THR D 139  1  O  ILE D 137   N  LEU D  86           
SHEET    6 AA4 7 ILE D 177  PRO D 184  1  O  ARG D 178   N  ILE D 136           
SHEET    7 AA4 7 ALA D 245  ALA D 248  1  O  ILE D 246   N  CYS D 183           
SITE     1 AC1  9 MET A   1  ILE A   2  HOH A 414  HOH A 471                    
SITE     2 AC1  9 HOH A 504  HOH A 535  MET B   1  GLN B  30                    
SITE     3 AC1  9 HOH B 458                                                     
SITE     1 AC2 10 SER A  17  GLY A  18  ILE A  19  GLY A  20                    
SITE     2 AC2 10 ASN A  89  HOH A 404  HOH A 408  HOH A 416                    
SITE     3 AC2 10 HOH A 427  HOH A 473                                          
SITE     1 AC3  7 MET A   1  GLN A  30  MET B   1  ILE B   2                    
SITE     2 AC3  7 HOH B 458  HOH B 471  HOH B 493                               
SITE     1 AC4 11 SER C  17  GLY C  18  ILE C  19  GLY C  20                    
SITE     2 AC4 11 ASN C  89  HOH C 416  HOH C 421  HOH C 424                    
SITE     3 AC4 11 HOH C 431  HOH C 436  HOH C 516                               
SITE     1 AC5  4 MET C   1  GLN C  30  MET D   1  ILE D   2                    
SITE     1 AC6  4 MET C   1  ILE C   2  MET D   1  GLN D  30                    
SITE     1 AC7  8 SER D  17  GLY D  18  ILE D  19  GLY D  20                    
SITE     2 AC7  8 ASN D  89  HOH D 401  HOH D 404  HOH D 407                    
SITE     1 AC8 10 ASN B 107  LEU B 110  THR B 115  HOH B 410                    
SITE     2 AC8 10 ASN D 107  LEU D 110  THR D 115  HOH D 403                    
SITE     3 AC8 10 HOH D 411  HOH D 446                                          
CRYST1   72.520   87.200   78.290  90.00 101.08  90.00 P 1 21 1      8          
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      0.013789  0.000000  0.002700        0.00000                         
SCALE2      0.000000  0.011468  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013016        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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