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Database: PDB
Entry: 3FN9
LinkDB: 3FN9
Original site: 3FN9 
HEADER    HYDROLASE                               23-DEC-08   3FN9              
TITLE     CRYSTAL STRUCTURE OF PUTATIVE BETA-GALACTOSIDASE FROM BACTEROIDES     
TITLE    2 FRAGILIS                                                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PUTATIVE BETA-GALACTOSIDASE;                               
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 FRAGMENT: UNP RESIDUES 23-703;                                       
COMPND   5 EC: 3.2.1.23;                                                        
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BACTEROIDES FRAGILIS;                           
SOURCE   3 ORGANISM_TAXID: 272559;                                              
SOURCE   4 STRAIN: NCTC 9343;                                                   
SOURCE   5 ATCC: 25285;                                                         
SOURCE   6 GENE: BF0029;                                                        
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: BC-PSGX4(BC)                              
KEYWDS    STRUCTURAL GENOMICS, PUTATIVE BETA-GALACTOSIDASE, GLYCOSIDASE,        
KEYWDS   2 HYDROLASE, PSI-2, PROTEIN STRUCTURE INITIATIVE, NEW YORK SGX         
KEYWDS   3 RESEARCH CENTER FOR STRUCTURAL GENOMICS, NYSGXRC                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    U.A.RAMAGOPAL,R.TORO,S.K.BURLEY,S.C.ALMO,NEW YORK SGX RESEARCH CENTER 
AUTHOR   2 FOR STRUCTURAL GENOMICS (NYSGXRC)                                    
REVDAT   2   13-JUL-11 3FN9    1       VERSN                                    
REVDAT   1   13-JAN-09 3FN9    0                                                
JRNL        AUTH   U.A.RAMAGOPAL,R.TORO,S.K.BURLEY,S.C.ALMO                     
JRNL        TITL   STRUCTURE OF PUTATIVE BETA-GALACTOSIDASE FROM BACTEROIDES    
JRNL        TITL 2 FRAGILIS                                                     
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0066                                      
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) : 2.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 49.39                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 89140                          
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) : 0.204                           
REMARK   3   R VALUE            (WORKING SET) : 0.201                           
REMARK   3   FREE R VALUE                     : 0.270                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 4414                            
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) : 2.70                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.77                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 6173                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.25                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2920                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 319                          
REMARK   3   BIN FREE R VALUE                    : 0.4200                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 21641                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 7                                       
REMARK   3   SOLVENT ATOMS            : 92                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 39.46                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -3.05000                                             
REMARK   3    B22 (A**2) : 4.43000                                              
REMARK   3    B33 (A**2) : -1.38000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.376         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.274         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 13.560        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.937                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.884                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 22245 ; 0.011 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 30232 ; 1.363 ; 1.928       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  2679 ; 6.583 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  1112 ;36.316 ;24.137       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  3598 ;18.753 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):   115 ;19.862 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  3160 ; 0.088 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 17306 ; 0.006 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
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): 13307 ; 1.297 ; 2.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 21447 ; 2.209 ; 3.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  8938 ; 1.488 ; 2.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  8785 ; 2.285 ; 3.000       
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 C D B                         
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A     22       A     686      4                      
REMARK   3           1     C     22       C     686      4                      
REMARK   3           1     D     22       D     686      4                      
REMARK   3           1     B     22       B     686      4                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  1    A    (A):   5336 ; 0.370 ; 0.500           
REMARK   3   MEDIUM POSITIONAL  1    B    (A):   5336 ; 0.330 ; 0.500           
REMARK   3   MEDIUM POSITIONAL  1    C    (A):   5336 ; 0.360 ; 0.500           
REMARK   3   MEDIUM POSITIONAL  1    D    (A):   5336 ; 0.380 ; 0.500           
REMARK   3   MEDIUM THERMAL     1    A (A**2):   5336 ; 2.370 ; 2.000           
REMARK   3   MEDIUM THERMAL     1    B (A**2):   5336 ; 3.700 ; 2.000           
REMARK   3   MEDIUM THERMAL     1    C (A**2):   5336 ; 2.310 ; 2.000           
REMARK   3   MEDIUM THERMAL     1    D (A**2):   5336 ; 3.560 ; 2.000           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
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: 1. HYDROGENS HAVE BEEN ADDED IN THE       
REMARK   3  RIDING POSITIONS. 2. U VALUES: REFINED INDIVIDUALLY                 
REMARK   4                                                                      
REMARK   4 3FN9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-DEC-08.                  
REMARK 100 THE RCSB ID CODE IS RCSB050799.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 14-JUL-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X29A                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : NULL                               
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9790                             
REMARK 200  MONOCHROMATOR                  : SI(111)                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 89259                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 10.300                             
REMARK 200  R MERGE                    (I) : 0.14600                            
REMARK 200  R SYM                      (I) : 0.10300                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 16.8440                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.80                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 10.10                              
REMARK 200  R MERGE FOR SHELL          (I) : 0.83300                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SAD                                            
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: SHELXD, PHENIX                                        
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 51.53                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.54                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M BIS-TRIS PH 6.5, 25% PEG 3350,      
REMARK 280  0.2M MGCL2, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K         
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       54.72650            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      110.59600            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       66.53300            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      110.59600            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       54.72650            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       66.53300            
REMARK 290   SMTRY3   4  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: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4360 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 48940 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -1.7 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, D, 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: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4350 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 48700 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -1.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, A                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 11220 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 95120 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -23.8 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, D, 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 APPLY THE FOLLOWING TO CHAINS: A, D, C                               
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000      -54.72650            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000      133.06600            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000      110.59600            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A    20                                                      
REMARK 465     SER A    21                                                      
REMARK 465     SER A   694                                                      
REMARK 465     TYR A   695                                                      
REMARK 465     GLU A   696                                                      
REMARK 465     ASN A   697                                                      
REMARK 465     LYS A   698                                                      
REMARK 465     ASN A   699                                                      
REMARK 465     GLU A   700                                                      
REMARK 465     HIS A   701                                                      
REMARK 465     SER A   702                                                      
REMARK 465     GLY A   703                                                      
REMARK 465     GLU A   704                                                      
REMARK 465     GLY A   705                                                      
REMARK 465     HIS A   706                                                      
REMARK 465     HIS A   707                                                      
REMARK 465     HIS A   708                                                      
REMARK 465     HIS A   709                                                      
REMARK 465     HIS A   710                                                      
REMARK 465     HIS A   711                                                      
REMARK 465     MET B    20                                                      
REMARK 465     SER B    21                                                      
REMARK 465     SER B   694                                                      
REMARK 465     TYR B   695                                                      
REMARK 465     GLU B   696                                                      
REMARK 465     ASN B   697                                                      
REMARK 465     LYS B   698                                                      
REMARK 465     ASN B   699                                                      
REMARK 465     GLU B   700                                                      
REMARK 465     HIS B   701                                                      
REMARK 465     SER B   702                                                      
REMARK 465     GLY B   703                                                      
REMARK 465     GLU B   704                                                      
REMARK 465     GLY B   705                                                      
REMARK 465     HIS B   706                                                      
REMARK 465     HIS B   707                                                      
REMARK 465     HIS B   708                                                      
REMARK 465     HIS B   709                                                      
REMARK 465     HIS B   710                                                      
REMARK 465     HIS B   711                                                      
REMARK 465     MET C    20                                                      
REMARK 465     SER C    21                                                      
REMARK 465     TYR C   695                                                      
REMARK 465     GLU C   696                                                      
REMARK 465     ASN C   697                                                      
REMARK 465     LYS C   698                                                      
REMARK 465     ASN C   699                                                      
REMARK 465     GLU C   700                                                      
REMARK 465     HIS C   701                                                      
REMARK 465     SER C   702                                                      
REMARK 465     GLY C   703                                                      
REMARK 465     GLU C   704                                                      
REMARK 465     GLY C   705                                                      
REMARK 465     HIS C   706                                                      
REMARK 465     HIS C   707                                                      
REMARK 465     HIS C   708                                                      
REMARK 465     HIS C   709                                                      
REMARK 465     HIS C   710                                                      
REMARK 465     HIS C   711                                                      
REMARK 465     MET D    20                                                      
REMARK 465     SER D    21                                                      
REMARK 465     LYS D   688                                                      
REMARK 465     ASN D   689                                                      
REMARK 465     ARG D   690                                                      
REMARK 465     GLU D   691                                                      
REMARK 465     ILE D   692                                                      
REMARK 465     ASP D   693                                                      
REMARK 465     SER D   694                                                      
REMARK 465     TYR D   695                                                      
REMARK 465     GLU D   696                                                      
REMARK 465     ASN D   697                                                      
REMARK 465     LYS D   698                                                      
REMARK 465     ASN D   699                                                      
REMARK 465     GLU D   700                                                      
REMARK 465     HIS D   701                                                      
REMARK 465     SER D   702                                                      
REMARK 465     GLY D   703                                                      
REMARK 465     GLU D   704                                                      
REMARK 465     GLY D   705                                                      
REMARK 465     HIS D   706                                                      
REMARK 465     HIS D   707                                                      
REMARK 465     HIS D   708                                                      
REMARK 465     HIS D   709                                                      
REMARK 465     HIS D   710                                                      
REMARK 465     HIS D   711                                                      
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 525    CG   CD   CE   NZ                                   
REMARK 470     LYS A 662    CD   CE   NZ                                        
REMARK 470     LYS A 672    CG   CD   CE   NZ                                   
REMARK 470     LYS B  54    CD   CE   NZ                                        
REMARK 470     LYS B 271    CG   CD   CE   NZ                                   
REMARK 470     VAL B 632    CG1  CG2                                            
REMARK 470     SER B 670    OG                                                  
REMARK 470     LYS B 672    CE   NZ                                             
REMARK 470     GLU B 675    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 679    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 688    CE   NZ                                             
REMARK 470     ARG B 690    NH1  NH2                                            
REMARK 470     ASP B 693    CG   OD1  OD2                                       
REMARK 470     LYS C 262    CG   CD   CE   NZ                                   
REMARK 470     LYS C 672    CG   CD   CE   NZ                                   
REMARK 470     LYS C 674    CG   CD   CE   NZ                                   
REMARK 470     LYS D 525    CG   CD   CE   NZ                                   
REMARK 470     THR D 671    OG1  CG2                                            
REMARK 470     LYS D 672    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   OE1  GLN C   608     NH2  ARG C   614              2.11            
REMARK 500   OE2  GLU A   538     OH   TYR A   624              2.13            
REMARK 500   OE2  GLU C   538     OH   TYR C   624              2.15            
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    PRO D  90   C   -  N   -  CA  ANGL. DEV. =   9.1 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  41      150.89    -47.78                                   
REMARK 500    GLN A  72      141.17   -170.08                                   
REMARK 500    SER A  75       84.68   -169.22                                   
REMARK 500    ILE A 132      -13.43   -140.74                                   
REMARK 500    THR A 134        4.61    -63.54                                   
REMARK 500    ASP A 200       64.40     60.80                                   
REMARK 500    ASP A 272       78.90   -152.41                                   
REMARK 500    ASP A 285       32.93     76.12                                   
REMARK 500    ARG A 323      112.02   -167.89                                   
REMARK 500    GLN A 361     -166.36   -119.89                                   
REMARK 500    PRO A 381       40.67    -78.65                                   
REMARK 500    ASN A 384      -57.45     81.38                                   
REMARK 500    TYR A 421      -98.74   -124.72                                   
REMARK 500    ASP A 442       63.94   -176.64                                   
REMARK 500    PRO A 443        2.65    -63.58                                   
REMARK 500    ASP A 457       41.55    -94.10                                   
REMARK 500    TYR A 472       57.69   -114.78                                   
REMARK 500    TRP A 475      -52.67   -125.07                                   
REMARK 500    GLU A 477      118.63   -164.89                                   
REMARK 500    LYS A 478     -163.44     59.01                                   
REMARK 500    GLU A 503      132.20   -173.04                                   
REMARK 500    LEU A 510      -31.53    -38.59                                   
REMARK 500    THR A 514      160.40    175.37                                   
REMARK 500    ASN A 522      133.89    -31.47                                   
REMARK 500    PRO A 526       30.61    -94.47                                   
REMARK 500    TYR A 528       71.07   -100.99                                   
REMARK 500    TRP A 598      -50.16   -124.20                                   
REMARK 500    ASN A 611       58.11    -99.90                                   
REMARK 500    GLU A 638      140.30    -36.29                                   
REMARK 500    ASP A 648       -0.24    -57.45                                   
REMARK 500    SER A 685       95.64   -169.44                                   
REMARK 500    ASN A 689       87.42    173.84                                   
REMARK 500    ILE A 692       36.16    -73.38                                   
REMARK 500    LYS B  36       94.19   -169.03                                   
REMARK 500    MET B  67      -67.08    -90.23                                   
REMARK 500    SER B  75       73.19   -163.37                                   
REMARK 500    ALA B 107      -31.06   -130.25                                   
REMARK 500    TYR B 167      129.78    -37.83                                   
REMARK 500    ASP B 200       70.43     48.90                                   
REMARK 500    LYS B 237      108.86    -40.83                                   
REMARK 500    PHE B 245      160.20    177.73                                   
REMARK 500    ASP B 272       77.21    178.71                                   
REMARK 500    ASN B 312       58.90     25.96                                   
REMARK 500    ARG B 323      119.73   -163.44                                   
REMARK 500    GLN B 325       32.99    -98.89                                   
REMARK 500    ASN B 384      -55.69     76.93                                   
REMARK 500    GLU B 419       71.67     52.93                                   
REMARK 500    TYR B 421     -111.61   -132.72                                   
REMARK 500    ASP B 442       72.28   -156.31                                   
REMARK 500    ASP B 457       41.64    -71.48                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     119 RAMACHANDRAN OUTLIERS.                        
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 CL A 802                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 807                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 805                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL D 803                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL D 804                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL D 806                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: NYSGXRC-11098J   RELATED DB: TARGETDB                    
DBREF  3FN9 A   23   703  UNP    Q5LJ68   Q5LJ68_BACFN    23    703             
DBREF  3FN9 B   23   703  UNP    Q5LJ68   Q5LJ68_BACFN    23    703             
DBREF  3FN9 C   23   703  UNP    Q5LJ68   Q5LJ68_BACFN    23    703             
DBREF  3FN9 D   23   703  UNP    Q5LJ68   Q5LJ68_BACFN    23    703             
SEQADV 3FN9 MET A   20  UNP  Q5LJ68              EXPRESSION TAG                 
SEQADV 3FN9 SER A   21  UNP  Q5LJ68              EXPRESSION TAG                 
SEQADV 3FN9 LEU A   22  UNP  Q5LJ68              EXPRESSION TAG                 
SEQADV 3FN9 GLU A  704  UNP  Q5LJ68              EXPRESSION TAG                 
SEQADV 3FN9 GLY A  705  UNP  Q5LJ68              EXPRESSION TAG                 
SEQADV 3FN9 HIS A  706  UNP  Q5LJ68              EXPRESSION TAG                 
SEQADV 3FN9 HIS A  707  UNP  Q5LJ68              EXPRESSION TAG                 
SEQADV 3FN9 HIS A  708  UNP  Q5LJ68              EXPRESSION TAG                 
SEQADV 3FN9 HIS A  709  UNP  Q5LJ68              EXPRESSION TAG                 
SEQADV 3FN9 HIS A  710  UNP  Q5LJ68              EXPRESSION TAG                 
SEQADV 3FN9 HIS A  711  UNP  Q5LJ68              EXPRESSION TAG                 
SEQADV 3FN9 MET B   20  UNP  Q5LJ68              EXPRESSION TAG                 
SEQADV 3FN9 SER B   21  UNP  Q5LJ68              EXPRESSION TAG                 
SEQADV 3FN9 LEU B   22  UNP  Q5LJ68              EXPRESSION TAG                 
SEQADV 3FN9 GLU B  704  UNP  Q5LJ68              EXPRESSION TAG                 
SEQADV 3FN9 GLY B  705  UNP  Q5LJ68              EXPRESSION TAG                 
SEQADV 3FN9 HIS B  706  UNP  Q5LJ68              EXPRESSION TAG                 
SEQADV 3FN9 HIS B  707  UNP  Q5LJ68              EXPRESSION TAG                 
SEQADV 3FN9 HIS B  708  UNP  Q5LJ68              EXPRESSION TAG                 
SEQADV 3FN9 HIS B  709  UNP  Q5LJ68              EXPRESSION TAG                 
SEQADV 3FN9 HIS B  710  UNP  Q5LJ68              EXPRESSION TAG                 
SEQADV 3FN9 HIS B  711  UNP  Q5LJ68              EXPRESSION TAG                 
SEQADV 3FN9 MET C   20  UNP  Q5LJ68              EXPRESSION TAG                 
SEQADV 3FN9 SER C   21  UNP  Q5LJ68              EXPRESSION TAG                 
SEQADV 3FN9 LEU C   22  UNP  Q5LJ68              EXPRESSION TAG                 
SEQADV 3FN9 GLU C  704  UNP  Q5LJ68              EXPRESSION TAG                 
SEQADV 3FN9 GLY C  705  UNP  Q5LJ68              EXPRESSION TAG                 
SEQADV 3FN9 HIS C  706  UNP  Q5LJ68              EXPRESSION TAG                 
SEQADV 3FN9 HIS C  707  UNP  Q5LJ68              EXPRESSION TAG                 
SEQADV 3FN9 HIS C  708  UNP  Q5LJ68              EXPRESSION TAG                 
SEQADV 3FN9 HIS C  709  UNP  Q5LJ68              EXPRESSION TAG                 
SEQADV 3FN9 HIS C  710  UNP  Q5LJ68              EXPRESSION TAG                 
SEQADV 3FN9 HIS C  711  UNP  Q5LJ68              EXPRESSION TAG                 
SEQADV 3FN9 MET D   20  UNP  Q5LJ68              EXPRESSION TAG                 
SEQADV 3FN9 SER D   21  UNP  Q5LJ68              EXPRESSION TAG                 
SEQADV 3FN9 LEU D   22  UNP  Q5LJ68              EXPRESSION TAG                 
SEQADV 3FN9 GLU D  704  UNP  Q5LJ68              EXPRESSION TAG                 
SEQADV 3FN9 GLY D  705  UNP  Q5LJ68              EXPRESSION TAG                 
SEQADV 3FN9 HIS D  706  UNP  Q5LJ68              EXPRESSION TAG                 
SEQADV 3FN9 HIS D  707  UNP  Q5LJ68              EXPRESSION TAG                 
SEQADV 3FN9 HIS D  708  UNP  Q5LJ68              EXPRESSION TAG                 
SEQADV 3FN9 HIS D  709  UNP  Q5LJ68              EXPRESSION TAG                 
SEQADV 3FN9 HIS D  710  UNP  Q5LJ68              EXPRESSION TAG                 
SEQADV 3FN9 HIS D  711  UNP  Q5LJ68              EXPRESSION TAG                 
SEQRES   1 A  692  MET SER LEU ALA ARG GLN VAL THR ALA PHE ASN THR GLY          
SEQRES   2 A  692  TRP GLN PHE LYS LYS GLY PRO PHE ALA THR ASP PRO MET          
SEQRES   3 A  692  ARG ALA ALA SER GLN TRP ASP GLY LYS TRP GLU THR VAL          
SEQRES   4 A  692  GLU ILE PRO HIS THR TRP ASN ALA MET ASP MET GLN VAL          
SEQRES   5 A  692  GLN SER GLY SER PHE TYR GLU GLY ALA GLY TYR TYR ARG          
SEQRES   6 A  692  LYS THR GLN PHE PHE PRO HIS ASP LEU GLU GLY LYS ARG          
SEQRES   7 A  692  VAL PHE LEU ARG PHE GLU GLY VAL GLY ALA CYS ALA GLU          
SEQRES   8 A  692  VAL TYR VAL ASN GLY LYS LEU ALA GLY THR HIS LYS GLY          
SEQRES   9 A  692  GLY TYR SER ALA PHE ALA CYS GLU ILE GLY THR ALA LEU          
SEQRES  10 A  692  LYS LEU GLY ALA GLU ASN GLU ILE ILE VAL LYS ALA ASP          
SEQRES  11 A  692  ASN LYS ALA ARG PRO ASP VAL ILE PRO VAL ASN GLN ASN          
SEQRES  12 A  692  LEU PHE GLY VAL TYR GLY GLY ILE TYR ARG PRO VAL TRP          
SEQRES  13 A  692  LEU ILE VAL THR GLU GLN ASN ASN ILE THR VAL THR ASP          
SEQRES  14 A  692  CYS ALA SER PRO GLY VAL TYR ILE THR GLN LYS ASP VAL          
SEQRES  15 A  692  SER LYS LYS SER ALA ASP ILE THR VAL LYS VAL LYS LEU          
SEQRES  16 A  692  ASP ASN ALA GLY LEU GLN PRO ALA ALA VAL THR LEU GLU          
SEQRES  17 A  692  ASN THR ILE TYR THR GLN GLU GLY GLN LYS VAL GLY THR          
SEQRES  18 A  692  HIS SER ARG SER PHE ASP LEU SER PRO GLN GLY THR GLN          
SEQRES  19 A  692  THR TYR LEU SER THR PHE LYS LEU LYS ASN PRO HIS LEU          
SEQRES  20 A  692  TRP GLN GLY ARG LYS ASP PRO TYR LEU TYR LYS VAL VAL          
SEQRES  21 A  692  CYS ARG LEU MET ALA ASP GLY LYS VAL ILE ASP GLU VAL          
SEQRES  22 A  692  VAL GLN PRO LEU GLY VAL ARG LYS TYR GLU ILE VAL ALA          
SEQRES  23 A  692  GLY LYS GLY PHE PHE LEU ASN GLY GLU LYS TYR SER MET          
SEQRES  24 A  692  TYR GLY VAL THR ARG HIS GLN ASP TRP TRP GLY LEU GLY          
SEQRES  25 A  692  SER ALA LEU LYS ASN GLU HIS HIS ASP PHE ASP LEU ALA          
SEQRES  26 A  692  ALA ILE MET ASP VAL GLY ALA THR THR VAL ARG PHE ALA          
SEQRES  27 A  692  HIS TYR GLN GLN SER ASP TYR LEU TYR SER ARG CYS ASP          
SEQRES  28 A  692  THR LEU GLY LEU ILE ILE TRP ALA GLU ILE PRO CYS VAL          
SEQRES  29 A  692  ASN ARG VAL THR GLY TYR GLU THR GLU ASN ALA GLN SER          
SEQRES  30 A  692  GLN LEU ARG GLU LEU ILE ARG GLN SER PHE ASN HIS PRO          
SEQRES  31 A  692  SER ILE TYR VAL TRP GLY LEU HIS ASN GLU VAL TYR GLN          
SEQRES  32 A  692  PRO HIS GLU TYR THR ALA ALA LEU THR ARG SER LEU HIS          
SEQRES  33 A  692  ASP LEU ALA LYS THR GLU ASP PRO ASP ARG TYR THR VAL          
SEQRES  34 A  692  SER VAL ASN GLY TYR GLY HIS MET ASP HIS PRO VAL ASN          
SEQRES  35 A  692  LEU ASN ALA ASP ILE GLN GLY MET ASN ARG TYR PHE GLY          
SEQRES  36 A  692  TRP TYR GLU LYS LYS ILE GLN ASP ILE LYS PRO TRP VAL          
SEQRES  37 A  692  GLU GLN LEU GLU LYS ASP TYR PRO TYR GLN LYS LEU MET          
SEQRES  38 A  692  LEU THR GLU TYR GLY ALA ASP ALA ASN LEU ALA HIS GLN          
SEQRES  39 A  692  THR GLU TYR LEU GLY ASP ALA LEU ASN TRP GLY LYS PRO          
SEQRES  40 A  692  PHE TYR PRO GLU THR PHE GLN THR LYS THR HIS GLU TYR          
SEQRES  41 A  692  GLN TRP SER ILE ILE LYS ASP HIS PRO TYR ILE ILE ALA          
SEQRES  42 A  692  SER TYR LEU TRP ASN MET PHE ASP PHE ALA VAL PRO MET          
SEQRES  43 A  692  TRP THR ARG GLY GLY VAL PRO ALA ARG ASN MET LYS GLY          
SEQRES  44 A  692  LEU ILE THR PHE ASP ARG LYS THR LYS LYS ASP SER TYR          
SEQRES  45 A  692  PHE TRP TYR LYS ALA ASN TRP SER GLU GLU PRO VAL LEU          
SEQRES  46 A  692  TYR LEU THR GLN ARG ARG ASN ALA ASP ARG GLU LYS ARG          
SEQRES  47 A  692  THR THR ALA VAL THR VAL TYR SER ASN ILE GLY THR PRO          
SEQRES  48 A  692  LYS VAL TYR LEU ASN GLY GLN GLU LEU SER GLY ILE ARG          
SEQRES  49 A  692  ASN GLY TYR THR ASP VAL HIS TYR VAL PHE ASP ASN VAL          
SEQRES  50 A  692  SER LEU ALA ASP GLY LYS ASN ILE LEU LYS ALA VAL VAL          
SEQRES  51 A  692  SER THR LYS GLY LYS GLU TYR THR ASP GLU ILE GLU TRP          
SEQRES  52 A  692  ASN TYR SER GLY GLU LYS ASN ARG GLU ILE ASP SER TYR          
SEQRES  53 A  692  GLU ASN LYS ASN GLU HIS SER GLY GLU GLY HIS HIS HIS          
SEQRES  54 A  692  HIS HIS HIS                                                  
SEQRES   1 B  692  MET SER LEU ALA ARG GLN VAL THR ALA PHE ASN THR GLY          
SEQRES   2 B  692  TRP GLN PHE LYS LYS GLY PRO PHE ALA THR ASP PRO MET          
SEQRES   3 B  692  ARG ALA ALA SER GLN TRP ASP GLY LYS TRP GLU THR VAL          
SEQRES   4 B  692  GLU ILE PRO HIS THR TRP ASN ALA MET ASP MET GLN VAL          
SEQRES   5 B  692  GLN SER GLY SER PHE TYR GLU GLY ALA GLY TYR TYR ARG          
SEQRES   6 B  692  LYS THR GLN PHE PHE PRO HIS ASP LEU GLU GLY LYS ARG          
SEQRES   7 B  692  VAL PHE LEU ARG PHE GLU GLY VAL GLY ALA CYS ALA GLU          
SEQRES   8 B  692  VAL TYR VAL ASN GLY LYS LEU ALA GLY THR HIS LYS GLY          
SEQRES   9 B  692  GLY TYR SER ALA PHE ALA CYS GLU ILE GLY THR ALA LEU          
SEQRES  10 B  692  LYS LEU GLY ALA GLU ASN GLU ILE ILE VAL LYS ALA ASP          
SEQRES  11 B  692  ASN LYS ALA ARG PRO ASP VAL ILE PRO VAL ASN GLN ASN          
SEQRES  12 B  692  LEU PHE GLY VAL TYR GLY GLY ILE TYR ARG PRO VAL TRP          
SEQRES  13 B  692  LEU ILE VAL THR GLU GLN ASN ASN ILE THR VAL THR ASP          
SEQRES  14 B  692  CYS ALA SER PRO GLY VAL TYR ILE THR GLN LYS ASP VAL          
SEQRES  15 B  692  SER LYS LYS SER ALA ASP ILE THR VAL LYS VAL LYS LEU          
SEQRES  16 B  692  ASP ASN ALA GLY LEU GLN PRO ALA ALA VAL THR LEU GLU          
SEQRES  17 B  692  ASN THR ILE TYR THR GLN GLU GLY GLN LYS VAL GLY THR          
SEQRES  18 B  692  HIS SER ARG SER PHE ASP LEU SER PRO GLN GLY THR GLN          
SEQRES  19 B  692  THR TYR LEU SER THR PHE LYS LEU LYS ASN PRO HIS LEU          
SEQRES  20 B  692  TRP GLN GLY ARG LYS ASP PRO TYR LEU TYR LYS VAL VAL          
SEQRES  21 B  692  CYS ARG LEU MET ALA ASP GLY LYS VAL ILE ASP GLU VAL          
SEQRES  22 B  692  VAL GLN PRO LEU GLY VAL ARG LYS TYR GLU ILE VAL ALA          
SEQRES  23 B  692  GLY LYS GLY PHE PHE LEU ASN GLY GLU LYS TYR SER MET          
SEQRES  24 B  692  TYR GLY VAL THR ARG HIS GLN ASP TRP TRP GLY LEU GLY          
SEQRES  25 B  692  SER ALA LEU LYS ASN GLU HIS HIS ASP PHE ASP LEU ALA          
SEQRES  26 B  692  ALA ILE MET ASP VAL GLY ALA THR THR VAL ARG PHE ALA          
SEQRES  27 B  692  HIS TYR GLN GLN SER ASP TYR LEU TYR SER ARG CYS ASP          
SEQRES  28 B  692  THR LEU GLY LEU ILE ILE TRP ALA GLU ILE PRO CYS VAL          
SEQRES  29 B  692  ASN ARG VAL THR GLY TYR GLU THR GLU ASN ALA GLN SER          
SEQRES  30 B  692  GLN LEU ARG GLU LEU ILE ARG GLN SER PHE ASN HIS PRO          
SEQRES  31 B  692  SER ILE TYR VAL TRP GLY LEU HIS ASN GLU VAL TYR GLN          
SEQRES  32 B  692  PRO HIS GLU TYR THR ALA ALA LEU THR ARG SER LEU HIS          
SEQRES  33 B  692  ASP LEU ALA LYS THR GLU ASP PRO ASP ARG TYR THR VAL          
SEQRES  34 B  692  SER VAL ASN GLY TYR GLY HIS MET ASP HIS PRO VAL ASN          
SEQRES  35 B  692  LEU ASN ALA ASP ILE GLN GLY MET ASN ARG TYR PHE GLY          
SEQRES  36 B  692  TRP TYR GLU LYS LYS ILE GLN ASP ILE LYS PRO TRP VAL          
SEQRES  37 B  692  GLU GLN LEU GLU LYS ASP TYR PRO TYR GLN LYS LEU MET          
SEQRES  38 B  692  LEU THR GLU TYR GLY ALA ASP ALA ASN LEU ALA HIS GLN          
SEQRES  39 B  692  THR GLU TYR LEU GLY ASP ALA LEU ASN TRP GLY LYS PRO          
SEQRES  40 B  692  PHE TYR PRO GLU THR PHE GLN THR LYS THR HIS GLU TYR          
SEQRES  41 B  692  GLN TRP SER ILE ILE LYS ASP HIS PRO TYR ILE ILE ALA          
SEQRES  42 B  692  SER TYR LEU TRP ASN MET PHE ASP PHE ALA VAL PRO MET          
SEQRES  43 B  692  TRP THR ARG GLY GLY VAL PRO ALA ARG ASN MET LYS GLY          
SEQRES  44 B  692  LEU ILE THR PHE ASP ARG LYS THR LYS LYS ASP SER TYR          
SEQRES  45 B  692  PHE TRP TYR LYS ALA ASN TRP SER GLU GLU PRO VAL LEU          
SEQRES  46 B  692  TYR LEU THR GLN ARG ARG ASN ALA ASP ARG GLU LYS ARG          
SEQRES  47 B  692  THR THR ALA VAL THR VAL TYR SER ASN ILE GLY THR PRO          
SEQRES  48 B  692  LYS VAL TYR LEU ASN GLY GLN GLU LEU SER GLY ILE ARG          
SEQRES  49 B  692  ASN GLY TYR THR ASP VAL HIS TYR VAL PHE ASP ASN VAL          
SEQRES  50 B  692  SER LEU ALA ASP GLY LYS ASN ILE LEU LYS ALA VAL VAL          
SEQRES  51 B  692  SER THR LYS GLY LYS GLU TYR THR ASP GLU ILE GLU TRP          
SEQRES  52 B  692  ASN TYR SER GLY GLU LYS ASN ARG GLU ILE ASP SER TYR          
SEQRES  53 B  692  GLU ASN LYS ASN GLU HIS SER GLY GLU GLY HIS HIS HIS          
SEQRES  54 B  692  HIS HIS HIS                                                  
SEQRES   1 C  692  MET SER LEU ALA ARG GLN VAL THR ALA PHE ASN THR GLY          
SEQRES   2 C  692  TRP GLN PHE LYS LYS GLY PRO PHE ALA THR ASP PRO MET          
SEQRES   3 C  692  ARG ALA ALA SER GLN TRP ASP GLY LYS TRP GLU THR VAL          
SEQRES   4 C  692  GLU ILE PRO HIS THR TRP ASN ALA MET ASP MET GLN VAL          
SEQRES   5 C  692  GLN SER GLY SER PHE TYR GLU GLY ALA GLY TYR TYR ARG          
SEQRES   6 C  692  LYS THR GLN PHE PHE PRO HIS ASP LEU GLU GLY LYS ARG          
SEQRES   7 C  692  VAL PHE LEU ARG PHE GLU GLY VAL GLY ALA CYS ALA GLU          
SEQRES   8 C  692  VAL TYR VAL ASN GLY LYS LEU ALA GLY THR HIS LYS GLY          
SEQRES   9 C  692  GLY TYR SER ALA PHE ALA CYS GLU ILE GLY THR ALA LEU          
SEQRES  10 C  692  LYS LEU GLY ALA GLU ASN GLU ILE ILE VAL LYS ALA ASP          
SEQRES  11 C  692  ASN LYS ALA ARG PRO ASP VAL ILE PRO VAL ASN GLN ASN          
SEQRES  12 C  692  LEU PHE GLY VAL TYR GLY GLY ILE TYR ARG PRO VAL TRP          
SEQRES  13 C  692  LEU ILE VAL THR GLU GLN ASN ASN ILE THR VAL THR ASP          
SEQRES  14 C  692  CYS ALA SER PRO GLY VAL TYR ILE THR GLN LYS ASP VAL          
SEQRES  15 C  692  SER LYS LYS SER ALA ASP ILE THR VAL LYS VAL LYS LEU          
SEQRES  16 C  692  ASP ASN ALA GLY LEU GLN PRO ALA ALA VAL THR LEU GLU          
SEQRES  17 C  692  ASN THR ILE TYR THR GLN GLU GLY GLN LYS VAL GLY THR          
SEQRES  18 C  692  HIS SER ARG SER PHE ASP LEU SER PRO GLN GLY THR GLN          
SEQRES  19 C  692  THR TYR LEU SER THR PHE LYS LEU LYS ASN PRO HIS LEU          
SEQRES  20 C  692  TRP GLN GLY ARG LYS ASP PRO TYR LEU TYR LYS VAL VAL          
SEQRES  21 C  692  CYS ARG LEU MET ALA ASP GLY LYS VAL ILE ASP GLU VAL          
SEQRES  22 C  692  VAL GLN PRO LEU GLY VAL ARG LYS TYR GLU ILE VAL ALA          
SEQRES  23 C  692  GLY LYS GLY PHE PHE LEU ASN GLY GLU LYS TYR SER MET          
SEQRES  24 C  692  TYR GLY VAL THR ARG HIS GLN ASP TRP TRP GLY LEU GLY          
SEQRES  25 C  692  SER ALA LEU LYS ASN GLU HIS HIS ASP PHE ASP LEU ALA          
SEQRES  26 C  692  ALA ILE MET ASP VAL GLY ALA THR THR VAL ARG PHE ALA          
SEQRES  27 C  692  HIS TYR GLN GLN SER ASP TYR LEU TYR SER ARG CYS ASP          
SEQRES  28 C  692  THR LEU GLY LEU ILE ILE TRP ALA GLU ILE PRO CYS VAL          
SEQRES  29 C  692  ASN ARG VAL THR GLY TYR GLU THR GLU ASN ALA GLN SER          
SEQRES  30 C  692  GLN LEU ARG GLU LEU ILE ARG GLN SER PHE ASN HIS PRO          
SEQRES  31 C  692  SER ILE TYR VAL TRP GLY LEU HIS ASN GLU VAL TYR GLN          
SEQRES  32 C  692  PRO HIS GLU TYR THR ALA ALA LEU THR ARG SER LEU HIS          
SEQRES  33 C  692  ASP LEU ALA LYS THR GLU ASP PRO ASP ARG TYR THR VAL          
SEQRES  34 C  692  SER VAL ASN GLY TYR GLY HIS MET ASP HIS PRO VAL ASN          
SEQRES  35 C  692  LEU ASN ALA ASP ILE GLN GLY MET ASN ARG TYR PHE GLY          
SEQRES  36 C  692  TRP TYR GLU LYS LYS ILE GLN ASP ILE LYS PRO TRP VAL          
SEQRES  37 C  692  GLU GLN LEU GLU LYS ASP TYR PRO TYR GLN LYS LEU MET          
SEQRES  38 C  692  LEU THR GLU TYR GLY ALA ASP ALA ASN LEU ALA HIS GLN          
SEQRES  39 C  692  THR GLU TYR LEU GLY ASP ALA LEU ASN TRP GLY LYS PRO          
SEQRES  40 C  692  PHE TYR PRO GLU THR PHE GLN THR LYS THR HIS GLU TYR          
SEQRES  41 C  692  GLN TRP SER ILE ILE LYS ASP HIS PRO TYR ILE ILE ALA          
SEQRES  42 C  692  SER TYR LEU TRP ASN MET PHE ASP PHE ALA VAL PRO MET          
SEQRES  43 C  692  TRP THR ARG GLY GLY VAL PRO ALA ARG ASN MET LYS GLY          
SEQRES  44 C  692  LEU ILE THR PHE ASP ARG LYS THR LYS LYS ASP SER TYR          
SEQRES  45 C  692  PHE TRP TYR LYS ALA ASN TRP SER GLU GLU PRO VAL LEU          
SEQRES  46 C  692  TYR LEU THR GLN ARG ARG ASN ALA ASP ARG GLU LYS ARG          
SEQRES  47 C  692  THR THR ALA VAL THR VAL TYR SER ASN ILE GLY THR PRO          
SEQRES  48 C  692  LYS VAL TYR LEU ASN GLY GLN GLU LEU SER GLY ILE ARG          
SEQRES  49 C  692  ASN GLY TYR THR ASP VAL HIS TYR VAL PHE ASP ASN VAL          
SEQRES  50 C  692  SER LEU ALA ASP GLY LYS ASN ILE LEU LYS ALA VAL VAL          
SEQRES  51 C  692  SER THR LYS GLY LYS GLU TYR THR ASP GLU ILE GLU TRP          
SEQRES  52 C  692  ASN TYR SER GLY GLU LYS ASN ARG GLU ILE ASP SER TYR          
SEQRES  53 C  692  GLU ASN LYS ASN GLU HIS SER GLY GLU GLY HIS HIS HIS          
SEQRES  54 C  692  HIS HIS HIS                                                  
SEQRES   1 D  692  MET SER LEU ALA ARG GLN VAL THR ALA PHE ASN THR GLY          
SEQRES   2 D  692  TRP GLN PHE LYS LYS GLY PRO PHE ALA THR ASP PRO MET          
SEQRES   3 D  692  ARG ALA ALA SER GLN TRP ASP GLY LYS TRP GLU THR VAL          
SEQRES   4 D  692  GLU ILE PRO HIS THR TRP ASN ALA MET ASP MET GLN VAL          
SEQRES   5 D  692  GLN SER GLY SER PHE TYR GLU GLY ALA GLY TYR TYR ARG          
SEQRES   6 D  692  LYS THR GLN PHE PHE PRO HIS ASP LEU GLU GLY LYS ARG          
SEQRES   7 D  692  VAL PHE LEU ARG PHE GLU GLY VAL GLY ALA CYS ALA GLU          
SEQRES   8 D  692  VAL TYR VAL ASN GLY LYS LEU ALA GLY THR HIS LYS GLY          
SEQRES   9 D  692  GLY TYR SER ALA PHE ALA CYS GLU ILE GLY THR ALA LEU          
SEQRES  10 D  692  LYS LEU GLY ALA GLU ASN GLU ILE ILE VAL LYS ALA ASP          
SEQRES  11 D  692  ASN LYS ALA ARG PRO ASP VAL ILE PRO VAL ASN GLN ASN          
SEQRES  12 D  692  LEU PHE GLY VAL TYR GLY GLY ILE TYR ARG PRO VAL TRP          
SEQRES  13 D  692  LEU ILE VAL THR GLU GLN ASN ASN ILE THR VAL THR ASP          
SEQRES  14 D  692  CYS ALA SER PRO GLY VAL TYR ILE THR GLN LYS ASP VAL          
SEQRES  15 D  692  SER LYS LYS SER ALA ASP ILE THR VAL LYS VAL LYS LEU          
SEQRES  16 D  692  ASP ASN ALA GLY LEU GLN PRO ALA ALA VAL THR LEU GLU          
SEQRES  17 D  692  ASN THR ILE TYR THR GLN GLU GLY GLN LYS VAL GLY THR          
SEQRES  18 D  692  HIS SER ARG SER PHE ASP LEU SER PRO GLN GLY THR GLN          
SEQRES  19 D  692  THR TYR LEU SER THR PHE LYS LEU LYS ASN PRO HIS LEU          
SEQRES  20 D  692  TRP GLN GLY ARG LYS ASP PRO TYR LEU TYR LYS VAL VAL          
SEQRES  21 D  692  CYS ARG LEU MET ALA ASP GLY LYS VAL ILE ASP GLU VAL          
SEQRES  22 D  692  VAL GLN PRO LEU GLY VAL ARG LYS TYR GLU ILE VAL ALA          
SEQRES  23 D  692  GLY LYS GLY PHE PHE LEU ASN GLY GLU LYS TYR SER MET          
SEQRES  24 D  692  TYR GLY VAL THR ARG HIS GLN ASP TRP TRP GLY LEU GLY          
SEQRES  25 D  692  SER ALA LEU LYS ASN GLU HIS HIS ASP PHE ASP LEU ALA          
SEQRES  26 D  692  ALA ILE MET ASP VAL GLY ALA THR THR VAL ARG PHE ALA          
SEQRES  27 D  692  HIS TYR GLN GLN SER ASP TYR LEU TYR SER ARG CYS ASP          
SEQRES  28 D  692  THR LEU GLY LEU ILE ILE TRP ALA GLU ILE PRO CYS VAL          
SEQRES  29 D  692  ASN ARG VAL THR GLY TYR GLU THR GLU ASN ALA GLN SER          
SEQRES  30 D  692  GLN LEU ARG GLU LEU ILE ARG GLN SER PHE ASN HIS PRO          
SEQRES  31 D  692  SER ILE TYR VAL TRP GLY LEU HIS ASN GLU VAL TYR GLN          
SEQRES  32 D  692  PRO HIS GLU TYR THR ALA ALA LEU THR ARG SER LEU HIS          
SEQRES  33 D  692  ASP LEU ALA LYS THR GLU ASP PRO ASP ARG TYR THR VAL          
SEQRES  34 D  692  SER VAL ASN GLY TYR GLY HIS MET ASP HIS PRO VAL ASN          
SEQRES  35 D  692  LEU ASN ALA ASP ILE GLN GLY MET ASN ARG TYR PHE GLY          
SEQRES  36 D  692  TRP TYR GLU LYS LYS ILE GLN ASP ILE LYS PRO TRP VAL          
SEQRES  37 D  692  GLU GLN LEU GLU LYS ASP TYR PRO TYR GLN LYS LEU MET          
SEQRES  38 D  692  LEU THR GLU TYR GLY ALA ASP ALA ASN LEU ALA HIS GLN          
SEQRES  39 D  692  THR GLU TYR LEU GLY ASP ALA LEU ASN TRP GLY LYS PRO          
SEQRES  40 D  692  PHE TYR PRO GLU THR PHE GLN THR LYS THR HIS GLU TYR          
SEQRES  41 D  692  GLN TRP SER ILE ILE LYS ASP HIS PRO TYR ILE ILE ALA          
SEQRES  42 D  692  SER TYR LEU TRP ASN MET PHE ASP PHE ALA VAL PRO MET          
SEQRES  43 D  692  TRP THR ARG GLY GLY VAL PRO ALA ARG ASN MET LYS GLY          
SEQRES  44 D  692  LEU ILE THR PHE ASP ARG LYS THR LYS LYS ASP SER TYR          
SEQRES  45 D  692  PHE TRP TYR LYS ALA ASN TRP SER GLU GLU PRO VAL LEU          
SEQRES  46 D  692  TYR LEU THR GLN ARG ARG ASN ALA ASP ARG GLU LYS ARG          
SEQRES  47 D  692  THR THR ALA VAL THR VAL TYR SER ASN ILE GLY THR PRO          
SEQRES  48 D  692  LYS VAL TYR LEU ASN GLY GLN GLU LEU SER GLY ILE ARG          
SEQRES  49 D  692  ASN GLY TYR THR ASP VAL HIS TYR VAL PHE ASP ASN VAL          
SEQRES  50 D  692  SER LEU ALA ASP GLY LYS ASN ILE LEU LYS ALA VAL VAL          
SEQRES  51 D  692  SER THR LYS GLY LYS GLU TYR THR ASP GLU ILE GLU TRP          
SEQRES  52 D  692  ASN TYR SER GLY GLU LYS ASN ARG GLU ILE ASP SER TYR          
SEQRES  53 D  692  GLU ASN LYS ASN GLU HIS SER GLY GLU GLY HIS HIS HIS          
SEQRES  54 D  692  HIS HIS HIS                                                  
HET     CL  A 801       1                                                       
HET     CL  A 802       1                                                       
HET     CL  A 807       1                                                       
HET     CL  C 805       1                                                       
HET     CL  D 803       1                                                       
HET     CL  D 804       1                                                       
HET     CL  D 806       1                                                       
HETNAM      CL CHLORIDE ION                                                     
FORMUL   5   CL    7(CL 1-)                                                     
FORMUL  12  HOH   *92(H2 O)                                                     
HELIX    1   1 ASP A   43  GLY A   53  1                                  11    
HELIX    2   2 PRO A   90  GLU A   94  5                                   5    
HELIX    3   3 GLY A  133  LEU A  136  5                                   4    
HELIX    4   4 LYS A  335  GLY A  350  1                                  16    
HELIX    5   5 SER A  362  GLY A  373  1                                  12    
HELIX    6   6 GLU A  390  PHE A  406  1                                  17    
HELIX    7   7 PRO A  423  ASP A  442  1                                  20    
HELIX    8   8 LYS A  479  GLN A  481  5                                   3    
HELIX    9   9 ASP A  482  TYR A  494  1                                  13    
HELIX   10  10 PRO A  529  HIS A  547  1                                  19    
HELIX   11  11 LYS A  588  SER A  599  1                                  12    
HELIX   12  12 ASP B   43  ASP B   52  1                                  10    
HELIX   13  13 PRO B   90  GLU B   94  5                                   5    
HELIX   14  14 GLY B  133  LEU B  136  5                                   4    
HELIX   15  15 GLN B  268  ASP B  272  5                                   5    
HELIX   16  16 LYS B  335  GLY B  350  1                                  16    
HELIX   17  17 SER B  362  GLY B  373  1                                  12    
HELIX   18  18 GLU B  390  SER B  405  1                                  16    
HELIX   19  19 PRO B  423  ASP B  442  1                                  20    
HELIX   20  20 LYS B  479  GLN B  481  5                                   3    
HELIX   21  21 ASP B  482  TYR B  494  1                                  13    
HELIX   22  22 PRO B  529  ASP B  546  1                                  18    
HELIX   23  23 LYS B  588  SER B  599  1                                  12    
HELIX   24  24 ASP C   43  ASP C   52  1                                  10    
HELIX   25  25 PRO C   90  GLU C   94  5                                   5    
HELIX   26  26 GLY C  133  LEU C  136  5                                   4    
HELIX   27  27 LYS C  335  GLY C  350  1                                  16    
HELIX   28  28 SER C  362  GLY C  373  1                                  12    
HELIX   29  29 GLU C  390  PHE C  406  1                                  17    
HELIX   30  30 PRO C  423  ASP C  442  1                                  20    
HELIX   31  31 LYS C  479  GLN C  481  5                                   3    
HELIX   32  32 ASP C  482  TYR C  494  1                                  13    
HELIX   33  33 PRO C  529  HIS C  547  1                                  19    
HELIX   34  34 LYS C  588  SER C  599  1                                  12    
HELIX   35  35 ASP D   43  GLY D   53  1                                  11    
HELIX   36  36 PRO D   90  GLU D   94  5                                   5    
HELIX   37  37 GLY D  133  LEU D  136  5                                   4    
HELIX   38  38 LYS D  335  VAL D  349  1                                  15    
HELIX   39  39 SER D  362  GLY D  373  1                                  12    
HELIX   40  40 GLU D  390  PHE D  406  1                                  17    
HELIX   41  41 PRO D  423  ASP D  442  1                                  20    
HELIX   42  42 LYS D  479  GLN D  481  5                                   3    
HELIX   43  43 ASP D  482  TYR D  494  1                                  13    
HELIX   44  44 PRO D  529  ASP D  546  1                                  18    
HELIX   45  45 LYS D  588  SER D  599  1                                  12    
SHEET    1   A 4 GLN A  25  ALA A  28  0                                        
SHEET    2   A 4 VAL A 174  THR A 179 -1  O  VAL A 178   N  GLN A  25           
SHEET    3   A 4 ARG A  97  PHE A 102 -1  N  PHE A  99   O  ILE A 177           
SHEET    4   A 4 PHE A 128  GLU A 131 -1  O  PHE A 128   N  PHE A 102           
SHEET    1   B 6 GLU A  56  THR A  57  0                                        
SHEET    2   B 6 GLN A  34  LYS A  37 -1  N  PHE A  35   O  GLU A  56           
SHEET    3   B 6 ALA A  80  PHE A  89 -1  O  ARG A  84   N  GLN A  34           
SHEET    4   B 6 ALA A 140  ASP A 149 -1  O  ILE A 144   N  LYS A  85           
SHEET    5   B 6 CYS A 108  VAL A 113 -1  N  TYR A 112   O  ILE A 145           
SHEET    6   B 6 LYS A 116  LYS A 122 -1  O  HIS A 121   N  ALA A 109           
SHEET    1   C 3 ASN A 182  ILE A 184  0                                        
SHEET    2   C 3 SER A 205  ASN A 216 -1  O  ASP A 215   N  ASN A 183           
SHEET    3   C 3 VAL A 194  LYS A 199 -1  N  TYR A 195   O  LYS A 211           
SHEET    1   D 3 ASN A 182  ILE A 184  0                                        
SHEET    2   D 3 SER A 205  ASN A 216 -1  O  ASP A 215   N  ASN A 183           
SHEET    3   D 3 GLN A 253  LYS A 262 -1  O  PHE A 259   N  ILE A 208           
SHEET    1   E 8 VAL A 288  LEU A 296  0                                        
SHEET    2   E 8 TYR A 276  MET A 283 -1  N  VAL A 278   O  GLN A 294           
SHEET    3   E 8 ALA A 222  TYR A 231 -1  N  THR A 229   O  VAL A 279           
SHEET    4   E 8 LYS A 237  LEU A 247 -1  O  LEU A 247   N  ALA A 222           
SHEET    5   E 8 LYS D 237  LEU D 247  1  O  SER D 244   N  SER A 242           
SHEET    6   E 8 ALA D 222  TYR D 231 -1  N  ALA D 222   O  LEU D 247           
SHEET    7   E 8 TYR D 276  ALA D 284 -1  O  MET D 283   N  THR D 225           
SHEET    8   E 8 LYS D 287  LEU D 296 -1  O  ILE D 289   N  LEU D 282           
SHEET    1   F 3 TYR A 301  VAL A 304  0                                        
SHEET    2   F 3 GLY A 308  LEU A 311 -1  O  PHE A 310   N  GLU A 302           
SHEET    3   F 3 GLU A 314  LYS A 315 -1  O  GLU A 314   N  LEU A 311           
SHEET    1   G 9 TYR A 319  THR A 322  0                                        
SHEET    2   G 9 THR A 353  PHE A 356  1  O  ARG A 355   N  VAL A 321           
SHEET    3   G 9 ILE A 375  GLU A 379  1  O  TRP A 377   N  VAL A 354           
SHEET    4   G 9 ILE A 411  ASN A 418  1  O  GLY A 415   N  ALA A 378           
SHEET    5   G 9 TYR A 446  ASN A 451  1  O  VAL A 448   N  LEU A 416           
SHEET    6   G 9 ILE A 466  ASN A 470  1  O  ASN A 470   N  ASN A 451           
SHEET    7   G 9 LEU A 499  GLU A 503  1  O  MET A 500   N  MET A 469           
SHEET    8   G 9 ALA A 552  LEU A 555  1  O  TYR A 554   N  LEU A 501           
SHEET    9   G 9 TYR A 319  THR A 322  1  N  GLY A 320   O  LEU A 555           
SHEET    1   H 2 PHE A 561  ARG A 568  0                                        
SHEET    2   H 2 VAL A 571  ASN A 575 -1  O  ASN A 575   N  PHE A 561           
SHEET    1   I 4 LEU A 604  LEU A 606  0                                        
SHEET    2   I 4 THR A 618  SER A 625 -1  O  TYR A 624   N  TYR A 605           
SHEET    3   I 4 HIS A 650  SER A 657 -1  O  VAL A 656   N  THR A 619           
SHEET    4   I 4 ARG A 643  ASN A 644 -1  N  ARG A 643   O  VAL A 652           
SHEET    1   J 5 ASP A 613  ARG A 614  0                                        
SHEET    2   J 5 LYS A 674  TYR A 684  1  O  ASN A 683   N  ARG A 614           
SHEET    3   J 5 GLY A 661  THR A 671 -1  N  THR A 671   O  LYS A 674           
SHEET    4   J 5 LYS A 631  LEU A 634 -1  N  LYS A 631   O  VAL A 668           
SHEET    5   J 5 GLN A 637  GLU A 638 -1  O  GLN A 637   N  LEU A 634           
SHEET    1   K 4 GLN B  25  ALA B  28  0                                        
SHEET    2   K 4 VAL B 174  THR B 179 -1  O  LEU B 176   N  THR B  27           
SHEET    3   K 4 ARG B  97  PHE B 102 -1  N  ARG B  97   O  THR B 179           
SHEET    4   K 4 PHE B 128  GLU B 131 -1  O  PHE B 128   N  PHE B 102           
SHEET    1   L 6 GLU B  56  VAL B  58  0                                        
SHEET    2   L 6 TRP B  33  LYS B  37 -1  N  PHE B  35   O  GLU B  56           
SHEET    3   L 6 ALA B  80  PHE B  89 -1  O  ARG B  84   N  GLN B  34           
SHEET    4   L 6 ALA B 140  ASP B 149 -1  O  ASN B 142   N  GLN B  87           
SHEET    5   L 6 CYS B 108  VAL B 113 -1  N  TYR B 112   O  ILE B 145           
SHEET    6   L 6 LEU B 117  LYS B 122 -1  O  ALA B 118   N  VAL B 111           
SHEET    1   M 3 ASN B 182  ILE B 184  0                                        
SHEET    2   M 3 SER B 205  ASN B 216 -1  O  ASP B 215   N  ASN B 183           
SHEET    3   M 3 VAL B 194  LYS B 199 -1  N  TYR B 195   O  LYS B 211           
SHEET    1   N 3 ASN B 182  ILE B 184  0                                        
SHEET    2   N 3 SER B 205  ASN B 216 -1  O  ASP B 215   N  ASN B 183           
SHEET    3   N 3 GLN B 253  LYS B 262 -1  O  GLN B 253   N  LEU B 214           
SHEET    1   O 4 LYS B 237  LEU B 247  0                                        
SHEET    2   O 4 ALA B 222  TYR B 231 -1  N  ALA B 222   O  LEU B 247           
SHEET    3   O 4 TYR B 276  ALA B 284 -1  O  MET B 283   N  THR B 225           
SHEET    4   O 4 LYS B 287  LEU B 296 -1  O  GLN B 294   N  VAL B 278           
SHEET    1   P 3 TYR B 301  VAL B 304  0                                        
SHEET    2   P 3 GLY B 308  LEU B 311 -1  O  PHE B 310   N  GLU B 302           
SHEET    3   P 3 GLU B 314  LYS B 315 -1  O  GLU B 314   N  LEU B 311           
SHEET    1   Q 9 TYR B 319  THR B 322  0                                        
SHEET    2   Q 9 THR B 353  PHE B 356  1  O  ARG B 355   N  VAL B 321           
SHEET    3   Q 9 ILE B 375  GLU B 379  1  O  TRP B 377   N  VAL B 354           
SHEET    4   Q 9 ILE B 411  ASN B 418  1  O  GLY B 415   N  ALA B 378           
SHEET    5   Q 9 TYR B 446  ASN B 451  1  O  VAL B 450   N  HIS B 417           
SHEET    6   Q 9 ILE B 466  ASN B 470  1  O  ASN B 470   N  ASN B 451           
SHEET    7   Q 9 LEU B 499  GLU B 503  1  O  MET B 500   N  MET B 469           
SHEET    8   Q 9 ALA B 552  LEU B 555  1  O  ALA B 552   N  LEU B 501           
SHEET    9   Q 9 TYR B 319  THR B 322  1  N  GLY B 320   O  LEU B 555           
SHEET    1   R 2 PHE B 561  ARG B 568  0                                        
SHEET    2   R 2 VAL B 571  ASN B 575 -1  O  ASN B 575   N  PHE B 561           
SHEET    1   S 4 LEU B 604  LEU B 606  0                                        
SHEET    2   S 4 THR B 618  SER B 625 -1  O  TYR B 624   N  TYR B 605           
SHEET    3   S 4 HIS B 650  SER B 657 -1  O  PHE B 653   N  VAL B 621           
SHEET    4   S 4 ARG B 643  ASN B 644 -1  N  ARG B 643   O  VAL B 652           
SHEET    1   T 4 GLN B 637  GLU B 638  0                                        
SHEET    2   T 4 LYS B 631  LEU B 634 -1  O  LEU B 634   N  GLN B 637           
SHEET    3   T 4 GLY B 661  THR B 671 -1  O  VAL B 668   N  LYS B 631           
SHEET    4   T 4 LYS B 674  TYR B 684 -1  O  ASP B 678   N  ALA B 667           
SHEET    1   U 4 GLN C  25  ALA C  28  0                                        
SHEET    2   U 4 VAL C 174  THR C 179 -1  O  LEU C 176   N  THR C  27           
SHEET    3   U 4 ARG C  97  PHE C 102 -1  N  ARG C  97   O  THR C 179           
SHEET    4   U 4 PHE C 128  GLU C 131 -1  O  PHE C 128   N  PHE C 102           
SHEET    1   V 6 GLU C  56  VAL C  58  0                                        
SHEET    2   V 6 TRP C  33  LYS C  37 -1  N  PHE C  35   O  GLU C  56           
SHEET    3   V 6 ALA C  80  PHE C  89 -1  O  ARG C  84   N  GLN C  34           
SHEET    4   V 6 ALA C 140  ASP C 149 -1  O  ILE C 144   N  LYS C  85           
SHEET    5   V 6 CYS C 108  VAL C 113 -1  N  CYS C 108   O  ASP C 149           
SHEET    6   V 6 LYS C 116  LYS C 122 -1  O  HIS C 121   N  ALA C 109           
SHEET    1   W 3 ASN C 182  ILE C 184  0                                        
SHEET    2   W 3 SER C 205  ASN C 216 -1  O  ASP C 215   N  ASN C 183           
SHEET    3   W 3 VAL C 194  SER C 202 -1  N  TYR C 195   O  LYS C 211           
SHEET    1   X 3 ASN C 182  ILE C 184  0                                        
SHEET    2   X 3 SER C 205  ASN C 216 -1  O  ASP C 215   N  ASN C 183           
SHEET    3   X 3 GLN C 253  LYS C 262 -1  O  GLN C 253   N  LEU C 214           
SHEET    1   Y 4 LYS C 237  LEU C 247  0                                        
SHEET    2   Y 4 ALA C 222  TYR C 231 -1  N  ALA C 222   O  LEU C 247           
SHEET    3   Y 4 TYR C 276  ALA C 284 -1  O  LYS C 277   N  TYR C 231           
SHEET    4   Y 4 LYS C 287  LEU C 296 -1  O  LEU C 296   N  TYR C 276           
SHEET    1   Z 2 TRP C 267  GLN C 268  0                                        
SHEET    2   Z 2 ASP C 272  PRO C 273 -1  O  ASP C 272   N  GLN C 268           
SHEET    1  AA 3 TYR C 301  VAL C 304  0                                        
SHEET    2  AA 3 GLY C 308  LEU C 311 -1  O  PHE C 310   N  GLU C 302           
SHEET    3  AA 3 GLU C 314  LYS C 315 -1  O  GLU C 314   N  LEU C 311           
SHEET    1  AB 9 TYR C 319  THR C 322  0                                        
SHEET    2  AB 9 THR C 353  PHE C 356  1  O  ARG C 355   N  VAL C 321           
SHEET    3  AB 9 ILE C 375  GLU C 379  1  O  TRP C 377   N  VAL C 354           
SHEET    4  AB 9 ILE C 411  ASN C 418  1  O  GLY C 415   N  ALA C 378           
SHEET    5  AB 9 TYR C 446  ASN C 451  1  O  VAL C 448   N  LEU C 416           
SHEET    6  AB 9 ILE C 466  MET C 469  1  O  GLY C 468   N  SER C 449           
SHEET    7  AB 9 LEU C 499  LEU C 501  1  O  MET C 500   N  MET C 469           
SHEET    8  AB 9 ILE C 550  TYR C 554  1  O  TYR C 554   N  LEU C 501           
SHEET    9  AB 9 TYR C 319  THR C 322  1  N  GLY C 320   O  SER C 553           
SHEET    1  AC 2 PHE C 561  ARG C 568  0                                        
SHEET    2  AC 2 VAL C 571  ASN C 575 -1  O  ASN C 575   N  PHE C 561           
SHEET    1  AD 4 LEU C 604  LEU C 606  0                                        
SHEET    2  AD 4 THR C 618  SER C 625 -1  O  TYR C 624   N  TYR C 605           
SHEET    3  AD 4 HIS C 650  SER C 657 -1  O  VAL C 656   N  THR C 619           
SHEET    4  AD 4 ARG C 643  ASN C 644 -1  N  ARG C 643   O  VAL C 652           
SHEET    1  AE 4 GLN C 637  GLU C 638  0                                        
SHEET    2  AE 4 LYS C 631  LEU C 634 -1  N  LEU C 634   O  GLN C 637           
SHEET    3  AE 4 GLY C 661  SER C 670 -1  O  LYS C 666   N  TYR C 633           
SHEET    4  AE 4 GLU C 675  TYR C 684 -1  O  TYR C 676   N  VAL C 669           
SHEET    1  AF 4 GLN D  25  ALA D  28  0                                        
SHEET    2  AF 4 VAL D 174  THR D 179 -1  O  LEU D 176   N  THR D  27           
SHEET    3  AF 4 ARG D  97  PHE D 102 -1  N  ARG D  97   O  THR D 179           
SHEET    4  AF 4 PHE D 128  GLU D 131 -1  O  PHE D 128   N  PHE D 102           
SHEET    1  AG 6 GLU D  56  VAL D  58  0                                        
SHEET    2  AG 6 TRP D  33  LYS D  37 -1  N  PHE D  35   O  GLU D  56           
SHEET    3  AG 6 ALA D  80  PHE D  89 -1  O  ARG D  84   N  GLN D  34           
SHEET    4  AG 6 ALA D 140  ASP D 149 -1  O  ILE D 144   N  LYS D  85           
SHEET    5  AG 6 CYS D 108  VAL D 113 -1  N  TYR D 112   O  ILE D 145           
SHEET    6  AG 6 LYS D 116  LYS D 122 -1  O  ALA D 118   N  VAL D 111           
SHEET    1  AH 3 ASN D 182  ILE D 184  0                                        
SHEET    2  AH 3 SER D 205  ASN D 216 -1  O  ASP D 215   N  ASN D 183           
SHEET    3  AH 3 VAL D 194  LYS D 199 -1  N  THR D 197   O  THR D 209           
SHEET    1  AI 3 ASN D 182  ILE D 184  0                                        
SHEET    2  AI 3 SER D 205  ASN D 216 -1  O  ASP D 215   N  ASN D 183           
SHEET    3  AI 3 GLN D 253  LYS D 262 -1  O  GLN D 253   N  LEU D 214           
SHEET    1  AJ 3 TYR D 301  VAL D 304  0                                        
SHEET    2  AJ 3 GLY D 308  LEU D 311 -1  O  GLY D 308   N  VAL D 304           
SHEET    3  AJ 3 GLU D 314  LYS D 315 -1  O  GLU D 314   N  LEU D 311           
SHEET    1  AK 9 TYR D 319  THR D 322  0                                        
SHEET    2  AK 9 THR D 353  ARG D 355  1  O  ARG D 355   N  VAL D 321           
SHEET    3  AK 9 ILE D 375  GLU D 379  1  O  TRP D 377   N  VAL D 354           
SHEET    4  AK 9 ILE D 411  ASN D 418  1  O  GLY D 415   N  ALA D 378           
SHEET    5  AK 9 TYR D 446  ASN D 451  1  O  VAL D 448   N  LEU D 416           
SHEET    6  AK 9 ILE D 466  ASN D 470  1  O  GLY D 468   N  SER D 449           
SHEET    7  AK 9 LEU D 499  GLU D 503  1  O  MET D 500   N  MET D 469           
SHEET    8  AK 9 ILE D 550  TYR D 554  1  O  TYR D 554   N  LEU D 501           
SHEET    9  AK 9 TYR D 319  THR D 322  1  N  GLY D 320   O  SER D 553           
SHEET    1  AL 2 PHE D 561  ARG D 568  0                                        
SHEET    2  AL 2 VAL D 571  ASN D 575 -1  O  ASN D 575   N  PHE D 561           
SHEET    1  AM 4 LEU D 604  LEU D 606  0                                        
SHEET    2  AM 4 THR D 618  SER D 625 -1  O  TYR D 624   N  TYR D 605           
SHEET    3  AM 4 HIS D 650  SER D 657 -1  O  PHE D 653   N  VAL D 621           
SHEET    4  AM 4 ARG D 643  ASN D 644 -1  N  ARG D 643   O  VAL D 652           
SHEET    1  AN 4 GLN D 637  GLU D 638  0                                        
SHEET    2  AN 4 LYS D 631  LEU D 634 -1  N  LEU D 634   O  GLN D 637           
SHEET    3  AN 4 LEU D 665  THR D 671 -1  O  LYS D 666   N  TYR D 633           
SHEET    4  AN 4 LYS D 674  ILE D 680 -1  O  ASP D 678   N  ALA D 667           
SHEET    1  AO 2 GLY D 661  LYS D 662  0                                        
SHEET    2  AO 2 ASN D 683  TYR D 684 -1  O  TYR D 684   N  GLY D 661           
CISPEP   1 GLY A   38    PRO A   39          0         2.85                     
CISPEP   2 ILE A   60    PRO A   61          0         4.41                     
CISPEP   3 GLY A  106    ALA A  107          0        -1.70                     
CISPEP   4 ILE A  157    PRO A  158          0        -2.41                     
CISPEP   5 ALA A  357    HIS A  358          0        -0.46                     
CISPEP   6 GLN A  422    PRO A  423          0        -2.25                     
CISPEP   7 TRP A  556    ASN A  557          0         0.83                     
CISPEP   8 ASP A  654    ASN A  655          0        15.46                     
CISPEP   9 GLY B   38    PRO B   39          0        -2.66                     
CISPEP  10 ILE B   60    PRO B   61          0         6.81                     
CISPEP  11 GLY B  106    ALA B  107          0        -1.86                     
CISPEP  12 ILE B  157    PRO B  158          0        -3.55                     
CISPEP  13 ALA B  357    HIS B  358          0        -4.21                     
CISPEP  14 GLN B  422    PRO B  423          0        -6.65                     
CISPEP  15 TRP B  556    ASN B  557          0         8.62                     
CISPEP  16 ASP B  654    ASN B  655          0         0.95                     
CISPEP  17 GLY C   38    PRO C   39          0         1.42                     
CISPEP  18 ILE C   60    PRO C   61          0        -0.55                     
CISPEP  19 GLY C  106    ALA C  107          0        -1.01                     
CISPEP  20 ILE C  157    PRO C  158          0        -3.98                     
CISPEP  21 ALA C  357    HIS C  358          0        -7.08                     
CISPEP  22 GLN C  422    PRO C  423          0        -4.24                     
CISPEP  23 TRP C  556    ASN C  557          0         7.53                     
CISPEP  24 GLY D   38    PRO D   39          0         1.34                     
CISPEP  25 ILE D   60    PRO D   61          0         2.76                     
CISPEP  26 GLY D  106    ALA D  107          0        -4.34                     
CISPEP  27 ILE D  157    PRO D  158          0        -3.55                     
CISPEP  28 ALA D  357    HIS D  358          0        -5.29                     
CISPEP  29 GLN D  422    PRO D  423          0        -0.17                     
CISPEP  30 TRP D  556    ASN D  557          0         3.00                     
SITE     1 AC1  1 THR A  42                                                     
SITE     1 AC2  3 ASP A 200  VAL A 201  LYS A 300                               
SITE     1 AC3  1 ASP C 200                                                     
SITE     1 AC4  2 ASP D 200  LYS D 300                                          
SITE     1 AC5  1 TYR D 231                                                     
SITE     1 AC6  2 THR D  42  ARG D  46                                          
CRYST1  109.453  133.066  221.192  90.00  90.00  90.00 P 21 21 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      0.009136  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007515  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004521        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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