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Database: PDB
Entry: 5ITV
LinkDB: 5ITV
Original site: 5ITV 
HEADER    OXIDOREDUCTASE                          17-MAR-16   5ITV              
TITLE     CRYSTAL STRUCTURE OF BACILLUS SUBTILIS BACC DIHYDROANTICAPSIN 7-      
TITLE    2 DEHYDROGENASE IN COMPLEX WITH NADH                                   
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                                                      
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 5ITV    1       JRNL                                     
REVDAT   1   22-FEB-17 5ITV    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.    2.26 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) : 2.26                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 38.10                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 43846                          
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) : 0.208                           
REMARK   3   R VALUE            (WORKING SET) : 0.207                           
REMARK   3   FREE R VALUE                     : 0.221                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.800                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2205                            
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) : 2.26                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.32                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3189                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.08                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2800                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 174                          
REMARK   3   BIN FREE R VALUE                    : 0.3270                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 7391                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 176                                     
REMARK   3   SOLVENT ATOMS            : 131                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 16.30                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 25.39                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.28000                                             
REMARK   3    B22 (A**2) : 0.22000                                              
REMARK   3    B33 (A**2) : 0.85000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.10000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.366         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.213         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.160         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.622         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.927                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.925                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  7708 ; 0.006 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  7400 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 10480 ; 1.125 ; 1.983       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 17016 ; 0.771 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   987 ; 5.129 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   309 ;39.555 ;26.408       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1295 ;12.707 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    16 ;20.331 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1238 ; 0.060 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  8756 ; 0.004 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  1644 ; 0.002 ; 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):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  3962 ; 1.125 ; 2.404       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4945 ; 1.976 ; 3.599       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  4946 ; 1.976 ; 3.599       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3745 ; 1.303 ; 2.719       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  3746 ; 1.303 ; 2.719       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  5536 ; 2.270 ; 3.998       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2): 32374 ; 4.812 ;22.866       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2): 32328 ; 4.807 ;22.871       
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   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   15706  0.03  0.05     
REMARK   3    2     A     1    255       C     1    255   15726  0.02  0.05     
REMARK   3    3     A     1    255       D     1    255   13715  0.02  0.05     
REMARK   3    4     B     1    255       C     1    255   15707  0.03  0.05     
REMARK   3    5     B     1    255       D     1    255   13679  0.03  0.05     
REMARK   3    6     C     1    255       D     1    255   13709  0.02  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: NULL                                      
REMARK   4                                                                      
REMARK   4 5ITV 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_1000219415.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-OCT-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) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU MICROMAX-007 HF             
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54180                            
REMARK 200  MONOCHROMATOR                  : VARIMAX HF                         
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MAR SCANNER 345 MM PLATE           
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   : 46073                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.260                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 38.100                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 3.900                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.08000                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.26                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.38                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.32500                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.800                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER 2.5.7                                          
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 46.51                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.30                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M AMMONIUM SULFATE, 0.1M BIS-TRIS,    
REMARK 280  PH 6.5, 25% W/V POLYETHYLENE GLYCOL 3350, 10% V/V GLYCEROL,         
REMARK 280  MICROBATCH, TEMPERATURE 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       44.04000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3                                                 
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 17660 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 31970 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -117.0 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 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     PRO D   190                                                      
REMARK 465     LEU D   191                                                      
REMARK 465     ASN D   192                                                      
REMARK 465     GLU D   193                                                      
REMARK 465     LYS D   194                                                      
REMARK 465     SER D   195                                                      
REMARK 465     PHE D   196                                                      
REMARK 465     LEU D   197                                                      
REMARK 465     GLU D   198                                                      
REMARK 465     ASN D   199                                                      
REMARK 465     ASN D   200                                                      
REMARK 465     GLU D   201                                                      
REMARK 465     GLY D   202                                                      
REMARK 465     THR D   203                                                      
REMARK 465     LEU D   204                                                      
REMARK 465     GLU D   205                                                      
REMARK 465     GLU D   206                                                      
REMARK 465     ILE D   207                                                      
REMARK 465     LYS D   208                                                      
REMARK 465     LYS D   209                                                      
REMARK 465     GLU D   210                                                      
REMARK 465     LYS D   211                                                      
REMARK 465     ALA D   212                                                      
REMARK 465     LYS D   213                                                      
REMARK 465     VAL D   214                                                      
REMARK 465     ASN D   215                                                      
REMARK 465     PRO D   216                                                      
REMARK 465     LEU D   217                                                      
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     LYS A  50    CD   CE   NZ                                        
REMARK 470     LEU A 191    CG   CD1  CD2                                       
REMARK 470     LYS B  50    CE   NZ                                             
REMARK 470     ASP B  54    CG   OD1  OD2                                       
REMARK 470     LEU B 191    CG   CD1  CD2                                       
REMARK 470     LYS B 213    CE   NZ                                             
REMARK 470     LYS C  50    CE   NZ                                             
REMARK 470     LEU C 191    CG   CD1  CD2                                       
REMARK 470     GLU C 205    CD   OE1  OE2                                       
REMARK 470     LYS D  50    CG   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   O1N  NAI C   301     O    HOH C   401              2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   OE1  GLN B    31     NE2  GLN C    31     1556     1.93            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG A 178   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.4 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ALA A  96      137.45   -170.02                                   
REMARK 500    LEU A 114      -56.84   -120.28                                   
REMARK 500    CYS A 140     -134.44    -89.92                                   
REMARK 500    ALA B  96      136.97   -170.03                                   
REMARK 500    CYS B 140     -134.24    -89.70                                   
REMARK 500    SER B 238       30.69    -95.18                                   
REMARK 500    LEU C 114      -56.59   -120.04                                   
REMARK 500    CYS C 140     -134.28    -90.97                                   
REMARK 500    SER C 238       30.53    -95.25                                   
REMARK 500    CYS D 140     -133.60    -89.97                                   
REMARK 500    SER D 238       30.59    -95.24                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NAI A 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NAI B 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NAI C 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NAI D 301                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5ITW   RELATED DB: PDB                                   
DBREF  5ITV A    3   255  UNP    P39640   BACC_BACSU       1    253             
DBREF  5ITV B    3   255  UNP    P39640   BACC_BACSU       1    253             
DBREF  5ITV C    3   255  UNP    P39640   BACC_BACSU       1    253             
DBREF  5ITV D    3   255  UNP    P39640   BACC_BACSU       1    253             
SEQADV 5ITV MET A    1  UNP  P39640              EXPRESSION TAG                 
SEQADV 5ITV ILE A    2  UNP  P39640              EXPRESSION TAG                 
SEQADV 5ITV MET B    1  UNP  P39640              EXPRESSION TAG                 
SEQADV 5ITV ILE B    2  UNP  P39640              EXPRESSION TAG                 
SEQADV 5ITV MET C    1  UNP  P39640              EXPRESSION TAG                 
SEQADV 5ITV ILE C    2  UNP  P39640              EXPRESSION TAG                 
SEQADV 5ITV MET D    1  UNP  P39640              EXPRESSION TAG                 
SEQADV 5ITV 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    NAI  A 301      44                                                       
HET    NAI  B 301      44                                                       
HET    NAI  C 301      44                                                       
HET    NAI  D 301      44                                                       
HETNAM     NAI 1,4-DIHYDRONICOTINAMIDE ADENINE DINUCLEOTIDE                     
HETSYN     NAI NADH                                                             
FORMUL   5  NAI    4(C21 H29 N7 O14 P2)                                         
FORMUL   9  HOH   *131(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 GLU A  102  LEU A  114  1                                  13    
HELIX    5 AA5 LEU A  114  GLY A  132  1                                  19    
HELIX    6 AA6 SER A  141  LEU A  145  5                                   5    
HELIX    7 AA7 ILE A  151  ALA A  173  1                                  23    
HELIX    8 AA8 THR A  189  ASN A  200  1                                  12    
HELIX    9 AA9 THR A  203  VAL A  214  1                                  12    
HELIX   10 AB1 LYS A  222  SER A  235  1                                  14    
HELIX   11 AB2 ASP A  236  SER A  239  5                                   4    
HELIX   12 AB3 GLY A  251  GLN A  255  5                                   5    
HELIX   13 AB4 SER B   17  GLN B   30  1                                  14    
HELIX   14 AB5 ASP B   40  ASN B   52  1                                  13    
HELIX   15 AB6 ASP B   65  GLY B   81  1                                  17    
HELIX   16 AB7 GLU B  102  LEU B  114  1                                  13    
HELIX   17 AB8 LEU B  114  GLY B  132  1                                  19    
HELIX   18 AB9 SER B  141  LEU B  145  5                                   5    
HELIX   19 AC1 ILE B  151  ALA B  173  1                                  23    
HELIX   20 AC2 THR B  189  ASN B  200  1                                  12    
HELIX   21 AC3 THR B  203  ALA B  212  1                                  10    
HELIX   22 AC4 LYS B  222  SER B  235  1                                  14    
HELIX   23 AC5 ASP B  236  SER B  239  5                                   4    
HELIX   24 AC6 GLY B  251  GLN B  255  5                                   5    
HELIX   25 AC7 SER C   17  GLN C   30  1                                  14    
HELIX   26 AC8 ASP C   40  ASN C   52  1                                  13    
HELIX   27 AC9 ASP C   65  GLY C   81  1                                  17    
HELIX   28 AD1 GLU C  102  LEU C  114  1                                  13    
HELIX   29 AD2 LEU C  114  GLY C  132  1                                  19    
HELIX   30 AD3 SER C  141  LEU C  145  5                                   5    
HELIX   31 AD4 ILE C  151  ALA C  173  1                                  23    
HELIX   32 AD5 THR C  189  ASN C  200  1                                  12    
HELIX   33 AD6 THR C  203  VAL C  214  1                                  12    
HELIX   34 AD7 LYS C  222  SER C  235  1                                  14    
HELIX   35 AD8 ASP C  236  SER C  239  5                                   4    
HELIX   36 AD9 GLY C  251  GLN C  255  5                                   5    
HELIX   37 AE1 SER D   17  GLN D   30  1                                  14    
HELIX   38 AE2 ASP D   40  ASN D   52  1                                  13    
HELIX   39 AE3 ASP D   65  GLY D   81  1                                  17    
HELIX   40 AE4 GLU D  102  LEU D  114  1                                  13    
HELIX   41 AE5 LEU D  114  GLY D  132  1                                  19    
HELIX   42 AE6 SER D  141  LEU D  145  5                                   5    
HELIX   43 AE7 ILE D  151  ALA D  173  1                                  23    
HELIX   44 AE8 LYS D  222  SER D  235  1                                  14    
HELIX   45 AE9 ASP D  236  SER D  239  5                                   4    
HELIX   46 AF1 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  HIS A  57           
SHEET    3 AA1 7 THR A   9  THR A  13  1  N  VAL A  10   O  ASN A  33           
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  HIS B  57           
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  HIS C  57           
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  HIS D  57           
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 25 GLY A  14  SER A  17  GLY A  18  ILE A  19                    
SITE     2 AC1 25 ASP A  38  ILE A  39  THR A  61  ASP A  62                    
SITE     3 AC1 25 ILE A  63  ASN A  89  ALA A  90  GLY A  91                    
SITE     4 AC1 25 THR A 139  CYS A 140  SER A 141  TYR A 154                    
SITE     5 AC1 25 LYS A 158  PRO A 184  GLY A 185  ILE A 186                    
SITE     6 AC1 25 ILE A 187  THR A 189  LEU A 191  ASN A 192                    
SITE     7 AC1 25 HOH A 410                                                     
SITE     1 AC2 24 GLY B  14  SER B  17  GLY B  18  ILE B  19                    
SITE     2 AC2 24 ASP B  38  ILE B  39  THR B  61  ASP B  62                    
SITE     3 AC2 24 ILE B  63  ASN B  89  GLY B  91  THR B 139                    
SITE     4 AC2 24 CYS B 140  SER B 141  TYR B 154  LYS B 158                    
SITE     5 AC2 24 PRO B 184  GLY B 185  ILE B 186  ILE B 187                    
SITE     6 AC2 24 THR B 189  LEU B 191  ASN B 192  HOH B 426                    
SITE     1 AC3 25 GLY C  14  SER C  17  GLY C  18  ILE C  19                    
SITE     2 AC3 25 ASP C  38  ILE C  39  THR C  61  ASP C  62                    
SITE     3 AC3 25 ILE C  63  ASN C  89  ALA C  90  GLY C  91                    
SITE     4 AC3 25 THR C 139  CYS C 140  SER C 141  TYR C 154                    
SITE     5 AC3 25 LYS C 158  PRO C 184  GLY C 185  ILE C 186                    
SITE     6 AC3 25 ILE C 187  THR C 189  LEU C 191  ASN C 192                    
SITE     7 AC3 25 HOH C 401                                                     
SITE     1 AC4 19 GLY D  14  SER D  17  GLY D  18  ILE D  19                    
SITE     2 AC4 19 ASP D  38  ILE D  39  THR D  61  ASP D  62                    
SITE     3 AC4 19 ILE D  63  ASN D  89  THR D 139  CYS D 140                    
SITE     4 AC4 19 SER D 141  TYR D 154  LYS D 158  PRO D 184                    
SITE     5 AC4 19 GLY D 185  ILE D 187  HOH D 409                               
CRYST1   74.750   88.080   78.610  90.00 106.44  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      0.013378  0.000000  0.003947        0.00000                         
SCALE2      0.000000  0.011353  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013263        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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