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Database: PDB
Entry: 2OQC
LinkDB: 2OQC
Original site: 2OQC 
HEADER    HYDROLASE                               31-JAN-07   2OQC              
TITLE     CRYSTAL STRUCTURE OF PENICILLIN V ACYLASE FROM BACILLUS SUBTILIS      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PENICILLIN V ACYLASE;                                      
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 EC: 3.5.1.11;                                                        
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS;                              
SOURCE   3 ORGANISM_TAXID: 1423;                                                
SOURCE   4 STRAIN: IG20;                                                        
SOURCE   5 GENE: YXEI;                                                          
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: PET26B                                    
KEYWDS    NTN-HYDROLASE, PENICILLIN V ACYLASE, CONJUGATED BILE ACID HYDROLASE,  
KEYWDS   2 CHOLOYLGLYCINE HYDROLASE, BACILLUS SUBTILIS, HYDROLASE               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.G.SURESH,P.RATHINASWAMY,A.V.PUNDLE,A.A.PRABHUNE,H.SIVARAMAN,        
AUTHOR   2 J.A.BRANNIGAN,G.G.DODSON                                             
REVDAT   4   16-APR-14 2OQC    1       REMARK                                   
REVDAT   3   13-JUL-11 2OQC    1       VERSN                                    
REVDAT   2   24-FEB-09 2OQC    1       VERSN                                    
REVDAT   1   15-JAN-08 2OQC    0                                                
JRNL        AUTH   C.G.SURESH,P.RATHINASWAMY,A.V.PUNDLE,A.A.PRABHUNE,           
JRNL        AUTH 2 H.SIVARAMAN,J.A.BRANNIGAN,G.G.DODSON                         
JRNL        TITL   CRYSTAL STRUCTURE OF PENICILLIN V ACYLASE FROM BACILLUS      
JRNL        TITL 2 SUBTILIS                                                     
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   P.RATHINASWAMY,A.V.PUNDLE,A.A.PRABHUNE,H.SIVARAMAN,          
REMARK   1  AUTH 2 J.A.BRANNIGAN,G.G.DODSON,C.G.SURESH                          
REMARK   1  TITL   CLONING, PURIFICATION, CRYSTALLIZATION AND PRELIMINARY       
REMARK   1  TITL 2 STRUCTURAL STUDIES OF PENICILLIN V ACYLASE FROM BACILLUS     
REMARK   1  TITL 3 SUBTILIS                                                     
REMARK   1  REF    ACTA CRYSTALLOGR.,SECT.F      V.  61   680 2005              
REMARK   1  REFN                   ESSN 1744-3091                               
REMARK   1  PMID   16511127                                                     
REMARK   1  DOI    10.1107/S1744309105017987                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 31859                          
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) : 0.158                           
REMARK   3   R VALUE            (WORKING SET) : 0.155                           
REMARK   3   FREE R VALUE                     : 0.218                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1705                            
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) : 2.50                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.56                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2269                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 96.24                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1770                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 109                          
REMARK   3   BIN FREE R VALUE                    : 0.2520                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5082                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 420                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 40.76                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 40.76                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.01000                                              
REMARK   3    B22 (A**2) : -3.35000                                             
REMARK   3    B33 (A**2) : 3.34000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.296         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.231         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.143         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.252         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.961                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.928                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  5198 ; 0.030 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  7056 ; 2.341 ; 1.950       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   626 ; 7.424 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   256 ;40.708 ;24.219       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   868 ;19.579 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    30 ;22.909 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   784 ; 0.182 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3972 ; 0.011 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  2492 ; 0.263 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  3510 ; 0.322 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   399 ; 0.227 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):   201 ; 0.296 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    85 ; 0.396 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  3246 ; 1.627 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  5102 ; 2.604 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2239 ; 4.238 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1954 ; 6.476 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : 1                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : A B                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A      1       A     329      4                      
REMARK   3           1     B      1       B     329      4                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  1    A    (A):   2541 ;  0.12 ;  0.50           
REMARK   3   MEDIUM THERMAL     1    A (A**2):   2541 ;  2.24 ;  2.00           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 2OQC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 05-FEB-07.                  
REMARK 100 THE RCSB ID CODE IS RCSB041456.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 07-SEP-02                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.2                                
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                             
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : OSMIC MIRROR                       
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 31859                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.497                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.56                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: PDB ENTRY 2PVA                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 61.90                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.23                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 4M SODIUM FORMATE IN 100MM TRIS-HCL      
REMARK 280  BUFFER, PH 8.2, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       28.00150            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       28.00150            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       55.48150            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000      153.97800            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       55.48150            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000      153.97800            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       28.00150            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       55.48150            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000      153.97800            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       28.00150            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       55.48150            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000      153.97800            
REMARK 290   SMTRY3   8  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: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 16730 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 45610 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -69.0 KCAL/MOL                        
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   BIOMT1   2 -1.000000  0.000000  0.000000      221.92600            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       84.00450            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000      221.92600            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       84.00450            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000      221.92600            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       84.00450            
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     SER A   199                                                      
REMARK 465     LYS A   200                                                      
REMARK 465     GLU A   201                                                      
REMARK 465     MET A   202                                                      
REMARK 465     GLY A   203                                                      
REMARK 465     GLY A   204                                                      
REMARK 465     LEU A   205                                                      
REMARK 465     ALA A   206                                                      
REMARK 465     LEU A   207                                                      
REMARK 465     SER A   208                                                      
REMARK 465     SER B   199                                                      
REMARK 465     LYS B   200                                                      
REMARK 465     GLU B   201                                                      
REMARK 465     MET B   202                                                      
REMARK 465     GLY B   203                                                      
REMARK 465     GLY B   204                                                      
REMARK 465     LEU B   205                                                      
REMARK 465     ALA B   206                                                      
REMARK 465     LEU B   207                                                      
REMARK 465     SER B   208                                                      
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   332     O    HOH A   538              1.41            
REMARK 500   OG1  THR A    18     O    HOH A   332              1.95            
REMARK 500   NE   ARG B   159     O    HOH B   492              2.12            
REMARK 500   O    HOH B   407     O    HOH B   492              2.15            
REMARK 500   O    HOH A   387     O    HOH A   508              2.16            
REMARK 500   OH   TYR A   275     O    HOH A   512              2.16            
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   O    HOH B   441     O    HOH B   475     4556     1.12            
REMARK 500   NE2  HIS B   306     O    HOH B   390     4556     1.65            
REMARK 500   O    HOH B   509     O    HOH B   536     4556     1.65            
REMARK 500   O    GLU B   307     O    HOH B   468     4556     1.86            
REMARK 500   O    HOH B   368     O    HOH B   390     4556     1.89            
REMARK 500   N    GLU B   307     O    HOH B   468     4556     1.89            
REMARK 500   O    HOH B   395     O    HOH B   464     2755     1.91            
REMARK 500   O    HOH B   487     O    HOH B   497     3756     1.94            
REMARK 500   O    HOH B   388     O    HOH B   446     4556     1.98            
REMARK 500   O    HOH A   457     O    HOH B   484     3756     2.06            
REMARK 500   O    HOH A   484     O    HOH B   457     3756     2.15            
REMARK 500   O    HIS B   306     O    HOH B   366     4556     2.16            
REMARK 500   O    HOH A   487     O    HOH A   497     3756     2.16            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    GLU A   7   CG    GLU A   7   CD      0.099                       
REMARK 500    GLU A  28   CD    GLU A  28   OE1     0.072                       
REMARK 500    GLU A  28   CD    GLU A  28   OE2     0.102                       
REMARK 500    GLU A  41   C     ALA A  43   N       0.212                       
REMARK 500    ILE A  64   C     LEU A  66   N       0.205                       
REMARK 500    TYR A  82   CD1   TYR A  82   CE1     0.109                       
REMARK 500    TYR A  82   CE2   TYR A  82   CD2     0.099                       
REMARK 500    TRP A 144   CZ3   TRP A 144   CH2     0.097                       
REMARK 500    SER A 147   CB    SER A 147   OG     -0.110                       
REMARK 500    GLU A 237   CG    GLU A 237   CD      0.122                       
REMARK 500    GLU A 237   CD    GLU A 237   OE2     0.081                       
REMARK 500    GLU A 269   CG    GLU A 269   CD      0.127                       
REMARK 500    GLU B  41   C     ALA B  43   N       0.228                       
REMARK 500    ILE B  64   C     LEU B  66   N       0.160                       
REMARK 500    TYR B  89   CD1   TYR B  89   CE1     0.100                       
REMARK 500    GLN B 187   CB    GLN B 187   CG      0.192                       
REMARK 500    GLN B 187   CG    GLN B 187   CD      0.140                       
REMARK 500    GLU B 237   CG    GLU B 237   CD      0.106                       
REMARK 500    GLU B 237   CD    GLU B 237   OE2     0.069                       
REMARK 500    GLU B 269   CG    GLU B 269   CD      0.095                       
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  34   NE  -  CZ  -  NH1 ANGL. DEV. =   4.7 DEGREES          
REMARK 500    ARG A  34   NE  -  CZ  -  NH2 ANGL. DEV. =  -7.1 DEGREES          
REMARK 500    ARG A  46   NE  -  CZ  -  NH1 ANGL. DEV. =   7.5 DEGREES          
REMARK 500    ILE A  64   O   -  C   -  N   ANGL. DEV. = -21.9 DEGREES          
REMARK 500    LEU A  66   C   -  N   -  CA  ANGL. DEV. =  17.1 DEGREES          
REMARK 500    ARG A 124   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES          
REMARK 500    ARG A 124   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.3 DEGREES          
REMARK 500    LEU A 146   CA  -  CB  -  CG  ANGL. DEV. =  20.8 DEGREES          
REMARK 500    LEU A 146   CB  -  CG  -  CD2 ANGL. DEV. =  11.0 DEGREES          
REMARK 500    ARG A 152   NE  -  CZ  -  NH1 ANGL. DEV. =   3.5 DEGREES          
REMARK 500    LEU A 154   CA  -  CB  -  CG  ANGL. DEV. =  15.1 DEGREES          
REMARK 500    ARG B  11   NE  -  CZ  -  NH1 ANGL. DEV. =   3.7 DEGREES          
REMARK 500    ARG B  11   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.1 DEGREES          
REMARK 500    LYS B  12   CD  -  CE  -  NZ  ANGL. DEV. = -18.2 DEGREES          
REMARK 500    ARG B  17   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.4 DEGREES          
REMARK 500    ARG B  34   NE  -  CZ  -  NH1 ANGL. DEV. =   6.1 DEGREES          
REMARK 500    ARG B  34   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.2 DEGREES          
REMARK 500    GLU B  41   O   -  C   -  N   ANGL. DEV. =  -9.9 DEGREES          
REMARK 500    ARG B  46   NE  -  CZ  -  NH1 ANGL. DEV. =   3.6 DEGREES          
REMARK 500    ILE B  64   CA  -  C   -  N   ANGL. DEV. = -13.7 DEGREES          
REMARK 500    LEU B  76   CB  -  CG  -  CD2 ANGL. DEV. =  10.3 DEGREES          
REMARK 500    LEU B 146   CA  -  CB  -  CG  ANGL. DEV. =  16.5 DEGREES          
REMARK 500    SER B 147   N   -  CA  -  CB  ANGL. DEV. =  -9.2 DEGREES          
REMARK 500    LEU B 214   CB  -  CG  -  CD2 ANGL. DEV. = -12.6 DEGREES          
REMARK 500    ASP B 244   CB  -  CG  -  OD1 ANGL. DEV. =   5.8 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    PHE A  83       53.76   -149.37                                   
REMARK 500    ARG A  94     -161.68    -66.02                                   
REMARK 500    HIS A 103        1.97    -67.58                                   
REMARK 500    THR A 174     -106.68   -116.86                                   
REMARK 500    ASN A 175     -140.82   -129.06                                   
REMARK 500    PRO A 177     -155.50    -75.08                                   
REMARK 500    LEU A 197      -80.60     -2.67                                   
REMARK 500    ASN A 296      109.79   -160.88                                   
REMARK 500    CYS A 311      136.93    -34.99                                   
REMARK 500    PHE B  83       54.37   -143.16                                   
REMARK 500    ARG B  94     -161.35    -57.28                                   
REMARK 500    HIS B 103        9.98    -69.34                                   
REMARK 500    THR B 174     -108.29   -117.22                                   
REMARK 500    ASN B 175     -145.46   -130.34                                   
REMARK 500    PRO B 177     -158.44    -79.99                                   
REMARK 500    LEU B 197      -67.46    -29.74                                   
REMARK 500    CYS B 311      151.00    -34.73                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 GLN A  196     LEU A  197                  144.33                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY                                       
REMARK 500                                                                      
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY                       
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER                 
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;                     
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;                            
REMARK 500 I=INSERTION CODE).                                                   
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        ANGLE                                           
REMARK 500    GLU A  41         10.14                                           
REMARK 500    ILE A  64         27.30                                           
REMARK 500    ILE B  64         16.96                                           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN                            
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE                   
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    SER B  74        23.0      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  2OQC A    1   329  UNP    Q2HPP6   Q2HPP6_BACSU     2    328             
DBREF  2OQC B    1   329  UNP    Q2HPP6   Q2HPP6_BACSU     2    328             
SEQRES   1 A  327  CYS THR SER LEU THR LEU GLU THR ALA ASP ARG LYS HIS          
SEQRES   2 A  327  VAL LEU ALA ARG THR MET ASP PHE ALA PHE GLN LEU GLY          
SEQRES   3 A  327  THR GLU VAL ILE LEU TYR PRO ARG ARG TYR SER TRP ASN          
SEQRES   4 A  327  SER GLU ALA ASP GLY ARG ALA HIS GLN THR GLN TYR ALA          
SEQRES   5 A  327  PHE ILE GLY MET GLY ARG LYS LEU GLY ASN ILE LEU PHE          
SEQRES   6 A  327  ALA ASP GLY ILE ASN GLU SER GLY LEU SER CYS ALA ALA          
SEQRES   7 A  327  LEU TYR PHE PRO GLY TYR ALA GLU TYR GLU LYS THR ILE          
SEQRES   8 A  327  ARG GLU ASP THR VAL HIS ILE VAL PRO HIS GLU PHE VAL          
SEQRES   9 A  327  THR TRP VAL LEU SER VAL CYS GLN SER LEU GLU ASP VAL          
SEQRES  10 A  327  LYS GLU LYS ILE ARG SER LEU THR ILE VAL GLU LYS LYS          
SEQRES  11 A  327  LEU ASP LEU LEU ASP THR VAL LEU PRO LEU HIS TRP ILE          
SEQRES  12 A  327  LEU SER ASP ARG THR GLY ARG ASN LEU THR ILE GLU PRO          
SEQRES  13 A  327  ARG ALA ASP GLY LEU LYS VAL TYR ASP ASN GLN PRO GLY          
SEQRES  14 A  327  VAL MET THR ASN SER PRO ASP PHE ILE TRP HIS VAL THR          
SEQRES  15 A  327  ASN LEU GLN GLN TYR THR GLY ILE ARG PRO LYS GLN LEU          
SEQRES  16 A  327  GLU SER LYS GLU MET GLY GLY LEU ALA LEU SER ALA PHE          
SEQRES  17 A  327  GLY GLN GLY LEU GLY THR VAL GLY LEU PRO GLY ASP TYR          
SEQRES  18 A  327  THR PRO PRO SER ARG PHE VAL ARG ALA VAL TYR LEU LYS          
SEQRES  19 A  327  GLU HIS LEU GLU PRO ALA ALA ASP GLU THR LYS GLY VAL          
SEQRES  20 A  327  THR ALA ALA PHE GLN ILE LEU ALA ASN MET THR ILE PRO          
SEQRES  21 A  327  LYS GLY ALA VAL ILE THR GLU GLU ASP GLU ILE HIS TYR          
SEQRES  22 A  327  THR GLN TYR THR SER VAL MET CYS ASN GLU THR GLY ASN          
SEQRES  23 A  327  TYR TYR PHE HIS HIS TYR ASP ASN ARG GLN ILE GLN LYS          
SEQRES  24 A  327  VAL ASN LEU PHE HIS GLU ASP LEU ASP CYS LEU GLU PRO          
SEQRES  25 A  327  LYS VAL PHE SER ALA LYS ALA GLU GLU SER ILE HIS GLU          
SEQRES  26 A  327  LEU ASN                                                      
SEQRES   1 B  327  CYS THR SER LEU THR LEU GLU THR ALA ASP ARG LYS HIS          
SEQRES   2 B  327  VAL LEU ALA ARG THR MET ASP PHE ALA PHE GLN LEU GLY          
SEQRES   3 B  327  THR GLU VAL ILE LEU TYR PRO ARG ARG TYR SER TRP ASN          
SEQRES   4 B  327  SER GLU ALA ASP GLY ARG ALA HIS GLN THR GLN TYR ALA          
SEQRES   5 B  327  PHE ILE GLY MET GLY ARG LYS LEU GLY ASN ILE LEU PHE          
SEQRES   6 B  327  ALA ASP GLY ILE ASN GLU SER GLY LEU SER CYS ALA ALA          
SEQRES   7 B  327  LEU TYR PHE PRO GLY TYR ALA GLU TYR GLU LYS THR ILE          
SEQRES   8 B  327  ARG GLU ASP THR VAL HIS ILE VAL PRO HIS GLU PHE VAL          
SEQRES   9 B  327  THR TRP VAL LEU SER VAL CYS GLN SER LEU GLU ASP VAL          
SEQRES  10 B  327  LYS GLU LYS ILE ARG SER LEU THR ILE VAL GLU LYS LYS          
SEQRES  11 B  327  LEU ASP LEU LEU ASP THR VAL LEU PRO LEU HIS TRP ILE          
SEQRES  12 B  327  LEU SER ASP ARG THR GLY ARG ASN LEU THR ILE GLU PRO          
SEQRES  13 B  327  ARG ALA ASP GLY LEU LYS VAL TYR ASP ASN GLN PRO GLY          
SEQRES  14 B  327  VAL MET THR ASN SER PRO ASP PHE ILE TRP HIS VAL THR          
SEQRES  15 B  327  ASN LEU GLN GLN TYR THR GLY ILE ARG PRO LYS GLN LEU          
SEQRES  16 B  327  GLU SER LYS GLU MET GLY GLY LEU ALA LEU SER ALA PHE          
SEQRES  17 B  327  GLY GLN GLY LEU GLY THR VAL GLY LEU PRO GLY ASP TYR          
SEQRES  18 B  327  THR PRO PRO SER ARG PHE VAL ARG ALA VAL TYR LEU LYS          
SEQRES  19 B  327  GLU HIS LEU GLU PRO ALA ALA ASP GLU THR LYS GLY VAL          
SEQRES  20 B  327  THR ALA ALA PHE GLN ILE LEU ALA ASN MET THR ILE PRO          
SEQRES  21 B  327  LYS GLY ALA VAL ILE THR GLU GLU ASP GLU ILE HIS TYR          
SEQRES  22 B  327  THR GLN TYR THR SER VAL MET CYS ASN GLU THR GLY ASN          
SEQRES  23 B  327  TYR TYR PHE HIS HIS TYR ASP ASN ARG GLN ILE GLN LYS          
SEQRES  24 B  327  VAL ASN LEU PHE HIS GLU ASP LEU ASP CYS LEU GLU PRO          
SEQRES  25 B  327  LYS VAL PHE SER ALA LYS ALA GLU GLU SER ILE HIS GLU          
SEQRES  26 B  327  LEU ASN                                                      
FORMUL   3  HOH   *420(H2 O)                                                    
HELIX    1   1 VAL A  101  HIS A  103  5                                   3    
HELIX    2   2 GLU A  104  CYS A  113  1                                  10    
HELIX    3   3 SER A  115  ILE A  123  1                                   9    
HELIX    4   4 LEU A  133  ASP A  137  5                                   5    
HELIX    5   5 ASP A  178  LEU A  186  1                                   9    
HELIX    6   6 GLN A  187  THR A  190  5                                   4    
HELIX    7   7 GLY A  213  VAL A  217  5                                   5    
HELIX    8   8 THR A  224  HIS A  238  1                                  15    
HELIX    9   9 ASP A  244  ASN A  258  1                                  15    
HELIX   10  10 PHE A  305  GLU A  307  5                                   3    
HELIX   11  11 VAL B  101  HIS B  103  5                                   3    
HELIX   12  12 GLU B  104  CYS B  113  1                                  10    
HELIX   13  13 SER B  115  ILE B  123  1                                   9    
HELIX   14  14 LEU B  133  ASP B  137  5                                   5    
HELIX   15  15 ASP B  178  GLN B  187  1                                  10    
HELIX   16  16 GLN B  188  THR B  190  5                                   3    
HELIX   17  17 GLY B  213  VAL B  217  5                                   5    
HELIX   18  18 THR B  224  HIS B  238  1                                  15    
HELIX   19  19 ASP B  244  ALA B  257  1                                  14    
HELIX   20  20 ASN B  258  THR B  260  5                                   3    
HELIX   21  21 PHE B  305  GLU B  307  5                                   3    
SHEET    1   A 6 VAL A 172  MET A 173  0                                        
SHEET    2   A 6 SER A   3  GLU A   7 -1  N  SER A   3   O  MET A 173           
SHEET    3   A 6 HIS A  13  PHE A  21 -1  O  ALA A  16   N  LEU A   4           
SHEET    4   A 6 TYR A 275  CYS A 283 -1  O  GLN A 277   N  MET A  19           
SHEET    5   A 6 ASN A 288  HIS A 293 -1  O  TYR A 290   N  VAL A 281           
SHEET    6   A 6 ASN A 296  ASN A 303 -1  O  VAL A 302   N  TYR A 289           
SHEET    1   B 7 ILE A  64  PHE A  67  0                                        
SHEET    2   B 7 PHE A  54  LYS A  60 -1  N  ARG A  59   O  LEU A  66           
SHEET    3   B 7 ASP A  69  ASN A  72 -1  O  ILE A  71   N  ILE A  55           
SHEET    4   B 7 SER A  77  TYR A  82 -1  O  CYS A  78   N  GLY A  70           
SHEET    5   B 7 LEU A 142  SER A 147 -1  O  SER A 147   N  SER A  77           
SHEET    6   B 7 ASN A 153  ARG A 159 -1  O  LEU A 154   N  LEU A 146           
SHEET    7   B 7 GLY A 162  ASP A 167 -1  O  TYR A 166   N  THR A 155           
SHEET    1   C 4 ILE A  64  PHE A  67  0                                        
SHEET    2   C 4 PHE A  54  LYS A  60 -1  N  ARG A  59   O  LEU A  66           
SHEET    3   C 4 GLU A  28  TYR A  32 -1  N  TYR A  32   O  PHE A  54           
SHEET    4   C 4 LYS A 315  PHE A 317 -1  O  PHE A 317   N  VAL A  29           
SHEET    1   D 2 SER A  37  ASN A  39  0                                        
SHEET    2   D 2 ALA A  47  GLN A  49 -1  O  HIS A  48   N  TRP A  38           
SHEET    1   E 2 VAL A  98  ILE A 100  0                                        
SHEET    2   E 2 LEU A 126  ILE A 128  1  O  THR A 127   N  VAL A  98           
SHEET    1   F 6 VAL B 172  MET B 173  0                                        
SHEET    2   F 6 SER B   3  GLU B   7 -1  N  SER B   3   O  MET B 173           
SHEET    3   F 6 HIS B  13  PHE B  21 -1  O  ALA B  16   N  LEU B   4           
SHEET    4   F 6 TYR B 275  CYS B 283 -1  O  GLN B 277   N  MET B  19           
SHEET    5   F 6 ASN B 288  HIS B 293 -1  O  TYR B 290   N  VAL B 281           
SHEET    6   F 6 ASN B 296  ASN B 303 -1  O  GLN B 300   N  PHE B 291           
SHEET    1   G 7 ILE B  64  PHE B  67  0                                        
SHEET    2   G 7 PHE B  54  LYS B  60 -1  N  ARG B  59   O  LEU B  66           
SHEET    3   G 7 ASP B  69  ASN B  72 -1  O  ILE B  71   N  ILE B  55           
SHEET    4   G 7 SER B  77  TYR B  82 -1  O  CYS B  78   N  GLY B  70           
SHEET    5   G 7 LEU B 142  SER B 147 -1  O  SER B 147   N  SER B  77           
SHEET    6   G 7 ASN B 153  ARG B 159 -1  O  LEU B 154   N  LEU B 146           
SHEET    7   G 7 GLY B 162  ASP B 167 -1  O  LYS B 164   N  GLU B 157           
SHEET    1   H 4 ILE B  64  PHE B  67  0                                        
SHEET    2   H 4 PHE B  54  LYS B  60 -1  N  ARG B  59   O  LEU B  66           
SHEET    3   H 4 GLU B  28  TYR B  32 -1  N  GLU B  28   O  GLY B  58           
SHEET    4   H 4 LYS B 315  PHE B 317 -1  O  PHE B 317   N  VAL B  29           
SHEET    1   I 2 SER B  37  ASN B  39  0                                        
SHEET    2   I 2 ALA B  47  GLN B  49 -1  O  HIS B  48   N  TRP B  38           
SHEET    1   J 2 VAL B  98  ILE B 100  0                                        
SHEET    2   J 2 LEU B 126  ILE B 128  1  O  THR B 127   N  ILE B 100           
CISPEP   1 SER A  176    PRO A  177          0        -5.50                     
CISPEP   2 SER B  176    PRO B  177          0        -1.60                     
CRYST1  110.963  307.956   56.003  90.00  90.00  90.00 C 2 2 21     16          
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      0.009012  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.003247  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.017856        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system