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Database: PDB
Entry: 2RKZ
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HEADER    CELL ADHESION                           18-OCT-07   2RKZ              
TITLE     CRYSTAL STRUCTURE OF THE SECOND AND THIRD FIBRONECTIN F1 MODULES IN   
TITLE    2 COMPLEX WITH A FRAGMENT OF STAPHYLOCOCCUS AUREUS FNBPA-1             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: FIBRONECTIN;                                               
COMPND   3 CHAIN: A, B, C, D, E, F;                                             
COMPND   4 FRAGMENT: UNP RESIDUES 93-182;                                       
COMPND   5 SYNONYM: FN,COLD-INSOLUBLE GLOBULIN,CIG;                             
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: PEPTIDE FROM FIBRONECTIN-BINDING PROTEIN A;                
COMPND   9 CHAIN: M, N, O, P, Q, R;                                             
COMPND  10 FRAGMENT: UNP RESIDUES 529-549;                                      
COMPND  11 SYNONYM: FNBPA;                                                      
COMPND  12 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: FN1;                                                           
SOURCE   6 EXPRESSION_SYSTEM: PICHIA PASTORIS;                                  
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 4922;                                       
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: GS115;                                     
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 SYNTHETIC: YES;                                                      
SOURCE  11 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS (STRAIN NCTC 8325);       
SOURCE  12 ORGANISM_TAXID: 93061;                                               
SOURCE  13 OTHER_DETAILS: PEPTIDE SYNTHESIS                                     
KEYWDS    FIBRRONECTIN, 2F13F1, BETA ZIPPER, STAPHYLOCOCCUS AUREUS, ACUTE       
KEYWDS   2 PHASE, ALTERNATIVE SPLICING, CELL ADHESION, EXTRACELLULAR MATRIX,    
KEYWDS   3 GLYCOPROTEIN, HEPARIN-BINDING, PHOSPHORYLATION, PYRROLIDONE          
KEYWDS   4 CARBOXYLIC ACID, SECRETED, SULFATION, CELL WALL, PEPTIDOGLYCAN-      
KEYWDS   5 ANCHOR, VIRULENCE                                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    R.J.BINGHAM                                                           
REVDAT   5   19-JUN-19 2RKZ    1       COMPND SOURCE REMARK DBREF               
REVDAT   5 2                   1       SEQADV SEQRES SHEET  LINK                
REVDAT   5 3                   1       SITE   ATOM                              
REVDAT   4   24-FEB-09 2RKZ    1       VERSN                                    
REVDAT   3   16-SEP-08 2RKZ    1       REMARK                                   
REVDAT   2   09-SEP-08 2RKZ    1       JRNL                                     
REVDAT   1   05-AUG-08 2RKZ    0                                                
JRNL        AUTH   R.J.BINGHAM,N.A.MEENAN,U.SCHWARZ-LINEK,J.P.TURKENBURG,       
JRNL        AUTH 2 E.F.GARMAN,J.R.POTTS                                         
JRNL        TITL   CRYSTAL STRUCTURES OF FIBRONECTIN-BINDING SITES FROM         
JRNL        TITL 2 STAPHYLOCOCCUS AUREUS FNBPA IN COMPLEX WITH FIBRONECTIN      
JRNL        TITL 3 DOMAINS                                                      
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 105 12254 2008              
JRNL        REFN                   ISSN 0027-8424                               
JRNL        PMID   18713862                                                     
JRNL        DOI    10.1073/PNAS.0803556105                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.4.0013                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 25.58                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 58424                          
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) : 0.200                           
REMARK   3   R VALUE            (WORKING SET) : 0.197                           
REMARK   3   FREE R VALUE                     : 0.261                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3086                            
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) : 2.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.05                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 4326                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.0                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2350                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 218                          
REMARK   3   BIN FREE R VALUE                    : 0.2860                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5057                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 24                                      
REMARK   3   SOLVENT ATOMS            : 822                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 19.10                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 24.36                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 3.64000                                              
REMARK   3    B22 (A**2) : -2.17000                                             
REMARK   3    B33 (A**2) : -1.49000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.13000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.166         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.169         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.132         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.723         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.942                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.888                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  5230 ; 0.014 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  7079 ; 1.423 ; 1.946       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   639 ;23.122 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   254 ;31.418 ;23.740       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   878 ;16.566 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    42 ;18.765 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   731 ; 0.028 ; 0.020       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4018 ; 0.006 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   338 ; 0.310 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):   730 ; 0.338 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   162 ; 0.228 ; 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):     9 ; 0.288 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     9 ; 0.350 ; 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):  3156 ; 3.106 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  5075 ; 4.349 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2074 ; 6.619 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1998 ; 9.292 ; 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 : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : 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: NULL                                      
REMARK   4                                                                      
REMARK   4 2RKZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 23-OCT-07.                  
REMARK 100 THE DEPOSITION ID IS D_1000044986.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 25-JUL-06                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID29                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97620                            
REMARK 200  MONOCHROMATOR                  : SI 111 CHANNEL                     
REMARK 200  OPTICS                         : LIQUID NITROGEN COOLED CHANNEL     
REMARK 200                                   -CUT SILICON MONOCHROMATOR AND A   
REMARK 200                                   CYLINDRICAL GRAZING INCIDENCE      
REMARK 200                                   MIRROR                             
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 58424                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 26.038                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 3.700                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 3.600                              
REMARK 200  R MERGE                    (I) : 0.10000                            
REMARK 200  R SYM                      (I) : 0.10000                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.11                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.27200                            
REMARK 200  R SYM FOR SHELL            (I) : 0.27200                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.200                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: A PREVIOUS LOWER RESOLUTION STRUCTURE                
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 60.05                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.08                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.8M SUCCINIC ACID, PH7.0, VAPOR         
REMARK 280  DIFFUSION, SITTING DROP, TEMPERATURE 291K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       54.86000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6                                        
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2270 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 6500 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -3.2 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, M                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2270 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 6470 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -4.1 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, N                                  
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 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2170 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 6730 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -3.5 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, O                                  
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: 4                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1950 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 6790 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -4.8 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, P                                  
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: 5                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1800 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 6320 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -6.6 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, Q                                  
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: 6                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1910 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 6550 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -6.3 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: F, R                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     ALA A    62                                                      
REMARK 465     ALA B    62                                                      
REMARK 465     GLU D   128                                                      
REMARK 465     THR D   129                                                      
REMARK 465     GLY D   130                                                      
REMARK 465     GLY D   131                                                      
REMARK 465     ALA E    62                                                      
REMARK 465     HIS E   127                                                      
REMARK 465     GLU E   128                                                      
REMARK 465     THR E   129                                                      
REMARK 465     GLY E   130                                                      
REMARK 465     GLY E   131                                                      
REMARK 465     TYR E   132                                                      
REMARK 465     MET E   133                                                      
REMARK 465     ILE E   151                                                      
REMARK 465     ALA F    62                                                      
REMARK 465     TYR M   547                                                      
REMARK 465     ASP M   548                                                      
REMARK 465     SER M   549                                                      
REMARK 465     NH2 M   550                                                      
REMARK 465     ACE N   528                                                      
REMARK 465     ASP N   548                                                      
REMARK 465     SER N   549                                                      
REMARK 465     NH2 N   550                                                      
REMARK 465     ACE O   528                                                      
REMARK 465     SER O   549                                                      
REMARK 465     NH2 O   550                                                      
REMARK 465     ACE P   528                                                      
REMARK 465     ACE Q   528                                                      
REMARK 465     SER Q   549                                                      
REMARK 465     NH2 Q   550                                                      
REMARK 465     ACE R   528                                                      
REMARK 465     ASP R   548                                                      
REMARK 465     SER R   549                                                      
REMARK 465     NH2 R   550                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLU C 128    CG   CD   OE1  OE2                                  
REMARK 470     LYS M 537    CG   CD   CE   NZ                                   
REMARK 470     GLU P 529    CG   CD   OE1  OE2                                  
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   OD1  ASN C   108     O    HOH C   301              2.09            
REMARK 500   O    HOH A   315     O    HOH A   379              2.14            
REMARK 500   O    HOH B   384     O    HOH B   419              2.15            
REMARK 500   ND2  ASN O   538     O    HOH O   601              2.16            
REMARK 500   O    HOH B   414     O    HOH M   623              2.17            
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 A   377     O    HOH B   351     1556     2.08            
REMARK 500   O    HOH A   348     O    HOH D   239     2545     2.16            
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    ARG A  99       21.29   -151.52                                   
REMARK 500    LYS A 143       17.53   -145.05                                   
REMARK 500    ARG B  99       22.27   -144.35                                   
REMARK 500    LYS B 143       19.65   -146.53                                   
REMARK 500    LYS C 143       19.65   -149.95                                   
REMARK 500    LYS D 143       20.78   -141.09                                   
REMARK 500    LYS E  85      107.90   -161.74                                   
REMARK 500    ASP E  86       37.20     77.03                                   
REMARK 500    SER F  87       -1.99     82.06                                   
REMARK 500    GLU F 128      -50.45    -24.50                                   
REMARK 500    THR F 129      -30.27   -150.18                                   
REMARK 500    LYS F 143       18.15   -145.75                                   
REMARK 500    ASP Q 536      122.10    -25.09                                   
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 GLU N  529     THR N  530                  138.19                    
REMARK 500 TYR Q  535     ASP Q  536                  148.62                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 417        DISTANCE =  5.93 ANGSTROMS                       
REMARK 525    HOH A 418        DISTANCE =  6.35 ANGSTROMS                       
REMARK 525    HOH A 419        DISTANCE =  6.44 ANGSTROMS                       
REMARK 525    HOH B 433        DISTANCE =  6.35 ANGSTROMS                       
REMARK 525    HOH B 434        DISTANCE =  7.48 ANGSTROMS                       
REMARK 525    HOH D 299        DISTANCE =  7.52 ANGSTROMS                       
REMARK 525    HOH D 300        DISTANCE =  8.07 ANGSTROMS                       
REMARK 525    HOH E 277        DISTANCE =  5.81 ANGSTROMS                       
REMARK 525    HOH F 289        DISTANCE =  6.80 ANGSTROMS                       
REMARK 525    HOH F 290        DISTANCE =  7.04 ANGSTROMS                       
REMARK 525    HOH O 640        DISTANCE =  5.86 ANGSTROMS                       
REMARK 525    HOH O 641        DISTANCE =  6.13 ANGSTROMS                       
REMARK 525    HOH P 630        DISTANCE =  6.18 ANGSTROMS                       
REMARK 525    HOH P 631        DISTANCE =  6.55 ANGSTROMS                       
REMARK 525    HOH P 632        DISTANCE =  7.50 ANGSTROMS                       
REMARK 525    HOH Q 622        DISTANCE =  5.84 ANGSTROMS                       
REMARK 525    HOH Q 623        DISTANCE =  6.86 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SIN B 1                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SIN B 2                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SIN B 3                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACE M 528                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NH2 P 550                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2RKY   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2RL0   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3CAL   RELATED DB: PDB                                   
DBREF  2RKZ A   62   151  UNP    P02751   FINC_HUMAN      93    182             
DBREF  2RKZ B   62   151  UNP    P02751   FINC_HUMAN      93    182             
DBREF  2RKZ C   62   151  UNP    P02751   FINC_HUMAN      93    182             
DBREF  2RKZ D   62   151  UNP    P02751   FINC_HUMAN      93    182             
DBREF  2RKZ E   62   151  UNP    P02751   FINC_HUMAN      93    182             
DBREF  2RKZ F   62   151  UNP    P02751   FINC_HUMAN      93    182             
DBREF  2RKZ M  529   549  UNP    P14738   FNBA_STAA8     529    549             
DBREF  2RKZ N  529   549  UNP    P14738   FNBA_STAA8     529    549             
DBREF  2RKZ O  529   549  UNP    P14738   FNBA_STAA8     529    549             
DBREF  2RKZ P  529   549  UNP    P14738   FNBA_STAA8     529    549             
DBREF  2RKZ Q  529   549  UNP    P14738   FNBA_STAA8     529    549             
DBREF  2RKZ R  529   549  UNP    P14738   FNBA_STAA8     529    549             
SEQADV 2RKZ ACE M  528  UNP  P14738              ACETYLATION                    
SEQADV 2RKZ NH2 M  550  UNP  P14738              AMIDATION                      
SEQADV 2RKZ ACE N  528  UNP  P14738              ACETYLATION                    
SEQADV 2RKZ NH2 N  550  UNP  P14738              AMIDATION                      
SEQADV 2RKZ ACE O  528  UNP  P14738              ACETYLATION                    
SEQADV 2RKZ NH2 O  550  UNP  P14738              AMIDATION                      
SEQADV 2RKZ ACE P  528  UNP  P14738              ACETYLATION                    
SEQADV 2RKZ NH2 P  550  UNP  P14738              AMIDATION                      
SEQADV 2RKZ ACE Q  528  UNP  P14738              ACETYLATION                    
SEQADV 2RKZ NH2 Q  550  UNP  P14738              AMIDATION                      
SEQADV 2RKZ ACE R  528  UNP  P14738              ACETYLATION                    
SEQADV 2RKZ NH2 R  550  UNP  P14738              AMIDATION                      
SEQRES   1 A   90  ALA GLU GLU THR CYS PHE ASP LYS TYR THR GLY ASN THR          
SEQRES   2 A   90  TYR ARG VAL GLY ASP THR TYR GLU ARG PRO LYS ASP SER          
SEQRES   3 A   90  MET ILE TRP ASP CYS THR CYS ILE GLY ALA GLY ARG GLY          
SEQRES   4 A   90  ARG ILE SER CYS THR ILE ALA ASN ARG CYS HIS GLU GLY          
SEQRES   5 A   90  GLY GLN SER TYR LYS ILE GLY ASP THR TRP ARG ARG PRO          
SEQRES   6 A   90  HIS GLU THR GLY GLY TYR MET LEU GLU CYS VAL CYS LEU          
SEQRES   7 A   90  GLY ASN GLY LYS GLY GLU TRP THR CYS LYS PRO ILE              
SEQRES   1 B   90  ALA GLU GLU THR CYS PHE ASP LYS TYR THR GLY ASN THR          
SEQRES   2 B   90  TYR ARG VAL GLY ASP THR TYR GLU ARG PRO LYS ASP SER          
SEQRES   3 B   90  MET ILE TRP ASP CYS THR CYS ILE GLY ALA GLY ARG GLY          
SEQRES   4 B   90  ARG ILE SER CYS THR ILE ALA ASN ARG CYS HIS GLU GLY          
SEQRES   5 B   90  GLY GLN SER TYR LYS ILE GLY ASP THR TRP ARG ARG PRO          
SEQRES   6 B   90  HIS GLU THR GLY GLY TYR MET LEU GLU CYS VAL CYS LEU          
SEQRES   7 B   90  GLY ASN GLY LYS GLY GLU TRP THR CYS LYS PRO ILE              
SEQRES   1 C   90  ALA GLU GLU THR CYS PHE ASP LYS TYR THR GLY ASN THR          
SEQRES   2 C   90  TYR ARG VAL GLY ASP THR TYR GLU ARG PRO LYS ASP SER          
SEQRES   3 C   90  MET ILE TRP ASP CYS THR CYS ILE GLY ALA GLY ARG GLY          
SEQRES   4 C   90  ARG ILE SER CYS THR ILE ALA ASN ARG CYS HIS GLU GLY          
SEQRES   5 C   90  GLY GLN SER TYR LYS ILE GLY ASP THR TRP ARG ARG PRO          
SEQRES   6 C   90  HIS GLU THR GLY GLY TYR MET LEU GLU CYS VAL CYS LEU          
SEQRES   7 C   90  GLY ASN GLY LYS GLY GLU TRP THR CYS LYS PRO ILE              
SEQRES   1 D   90  ALA GLU GLU THR CYS PHE ASP LYS TYR THR GLY ASN THR          
SEQRES   2 D   90  TYR ARG VAL GLY ASP THR TYR GLU ARG PRO LYS ASP SER          
SEQRES   3 D   90  MET ILE TRP ASP CYS THR CYS ILE GLY ALA GLY ARG GLY          
SEQRES   4 D   90  ARG ILE SER CYS THR ILE ALA ASN ARG CYS HIS GLU GLY          
SEQRES   5 D   90  GLY GLN SER TYR LYS ILE GLY ASP THR TRP ARG ARG PRO          
SEQRES   6 D   90  HIS GLU THR GLY GLY TYR MET LEU GLU CYS VAL CYS LEU          
SEQRES   7 D   90  GLY ASN GLY LYS GLY GLU TRP THR CYS LYS PRO ILE              
SEQRES   1 E   90  ALA GLU GLU THR CYS PHE ASP LYS TYR THR GLY ASN THR          
SEQRES   2 E   90  TYR ARG VAL GLY ASP THR TYR GLU ARG PRO LYS ASP SER          
SEQRES   3 E   90  MET ILE TRP ASP CYS THR CYS ILE GLY ALA GLY ARG GLY          
SEQRES   4 E   90  ARG ILE SER CYS THR ILE ALA ASN ARG CYS HIS GLU GLY          
SEQRES   5 E   90  GLY GLN SER TYR LYS ILE GLY ASP THR TRP ARG ARG PRO          
SEQRES   6 E   90  HIS GLU THR GLY GLY TYR MET LEU GLU CYS VAL CYS LEU          
SEQRES   7 E   90  GLY ASN GLY LYS GLY GLU TRP THR CYS LYS PRO ILE              
SEQRES   1 F   90  ALA GLU GLU THR CYS PHE ASP LYS TYR THR GLY ASN THR          
SEQRES   2 F   90  TYR ARG VAL GLY ASP THR TYR GLU ARG PRO LYS ASP SER          
SEQRES   3 F   90  MET ILE TRP ASP CYS THR CYS ILE GLY ALA GLY ARG GLY          
SEQRES   4 F   90  ARG ILE SER CYS THR ILE ALA ASN ARG CYS HIS GLU GLY          
SEQRES   5 F   90  GLY GLN SER TYR LYS ILE GLY ASP THR TRP ARG ARG PRO          
SEQRES   6 F   90  HIS GLU THR GLY GLY TYR MET LEU GLU CYS VAL CYS LEU          
SEQRES   7 F   90  GLY ASN GLY LYS GLY GLU TRP THR CYS LYS PRO ILE              
SEQRES   1 M   23  ACE GLU THR LEU THR GLY GLN TYR ASP LYS ASN LEU VAL          
SEQRES   2 M   23  THR THR VAL GLU GLU GLU TYR ASP SER NH2                      
SEQRES   1 N   23  ACE GLU THR LEU THR GLY GLN TYR ASP LYS ASN LEU VAL          
SEQRES   2 N   23  THR THR VAL GLU GLU GLU TYR ASP SER NH2                      
SEQRES   1 O   23  ACE GLU THR LEU THR GLY GLN TYR ASP LYS ASN LEU VAL          
SEQRES   2 O   23  THR THR VAL GLU GLU GLU TYR ASP SER NH2                      
SEQRES   1 P   23  ACE GLU THR LEU THR GLY GLN TYR ASP LYS ASN LEU VAL          
SEQRES   2 P   23  THR THR VAL GLU GLU GLU TYR ASP SER NH2                      
SEQRES   1 Q   23  ACE GLU THR LEU THR GLY GLN TYR ASP LYS ASN LEU VAL          
SEQRES   2 Q   23  THR THR VAL GLU GLU GLU TYR ASP SER NH2                      
SEQRES   1 R   23  ACE GLU THR LEU THR GLY GLN TYR ASP LYS ASN LEU VAL          
SEQRES   2 R   23  THR THR VAL GLU GLU GLU TYR ASP SER NH2                      
HET    ACE  M 528       3                                                       
HET    NH2  P 550       1                                                       
HET    SIN  A 201       8                                                       
HET    SIN  B 201       8                                                       
HET    SIN  C 201       8                                                       
HETNAM     ACE ACETYL GROUP                                                     
HETNAM     NH2 AMINO GROUP                                                      
HETNAM     SIN SUCCINIC ACID                                                    
FORMUL   7  ACE    C2 H4 O                                                      
FORMUL  10  NH2    H2 N                                                         
FORMUL  13  SIN    3(C4 H6 O4)                                                  
FORMUL  16  HOH   *822(H2 O)                                                    
SHEET    1   A 2 THR A  65  ASP A  68  0                                        
SHEET    2   A 2 ASN A  73  ARG A  76 -1  O  TYR A  75   N  CYS A  66           
SHEET    1   B 4 THR A  80  LYS A  85  0                                        
SHEET    2   B 4 MET A  88  GLY A  96 -1  O  CYS A  92   N  TYR A  81           
SHEET    3   B 4 ARG A 101  THR A 105 -1  O  SER A 103   N  THR A  93           
SHEET    4   B 4 THR M 542  GLU M 545 -1  O  GLU M 545   N  ILE A 102           
SHEET    1   C 4 ARG A 109  GLU A 112  0                                        
SHEET    2   C 4 GLN A 115  LYS A 118 -1  O  TYR A 117   N  CYS A 110           
SHEET    3   C 4 GLU D  63  ASP D  68 -1  O  GLU D  63   N  SER A 116           
SHEET    4   C 4 ASN D  73  ARG D  76 -1  O  TYR D  75   N  CYS D  66           
SHEET    1   D 4 THR A 122  PRO A 126  0                                        
SHEET    2   D 4 MET A 133  GLY A 140 -1  O  CYS A 136   N  TRP A 123           
SHEET    3   D 4 GLU A 145  PRO A 150 -1  O  LYS A 149   N  GLU A 135           
SHEET    4   D 4 LEU M 531  GLY M 533 -1  O  LEU M 531   N  CYS A 148           
SHEET    1   E 2 THR B  65  PHE B  67  0                                        
SHEET    2   E 2 THR B  74  ARG B  76 -1  O  TYR B  75   N  CYS B  66           
SHEET    1   F 4 THR B  80  LYS B  85  0                                        
SHEET    2   F 4 MET B  88  GLY B  96 -1  O  CYS B  92   N  TYR B  81           
SHEET    3   F 4 ARG B 101  THR B 105 -1  O  ARG B 101   N  ILE B  95           
SHEET    4   F 4 THR N 542  GLU N 545 -1  O  VAL N 543   N  CYS B 104           
SHEET    1   G 2 ARG B 109  GLU B 112  0                                        
SHEET    2   G 2 GLN B 115  LYS B 118 -1  O  TYR B 117   N  CYS B 110           
SHEET    1   H 4 THR B 122  PRO B 126  0                                        
SHEET    2   H 4 MET B 133  GLY B 140 -1  O  CYS B 136   N  TRP B 123           
SHEET    3   H 4 GLU B 145  PRO B 150 -1  O  LYS B 149   N  GLU B 135           
SHEET    4   H 4 LEU N 531  GLY N 533 -1  O  LEU N 531   N  CYS B 148           
SHEET    1   I 2 THR C  65  ASP C  68  0                                        
SHEET    2   I 2 ASN C  73  ARG C  76 -1  O  TYR C  75   N  CYS C  66           
SHEET    1   J 8 THR C  80  LYS C  85  0                                        
SHEET    2   J 8 MET C  88  GLY C  96 -1  O  TRP C  90   N  ARG C  83           
SHEET    3   J 8 ARG C 101  THR C 105 -1  O  THR C 105   N  ASP C  91           
SHEET    4   J 8 THR O 542  GLU O 546 -1  O  GLU O 545   N  ILE C 102           
SHEET    5   J 8 THR P 542  GLU P 546 -1  O  THR P 542   N  GLU O 546           
SHEET    6   J 8 ARG D 101  THR D 105 -1  N  ILE D 102   O  GLU P 545           
SHEET    7   J 8 MET D  88  GLY D  96 -1  N  ASP D  91   O  THR D 105           
SHEET    8   J 8 THR D  80  LYS D  85 -1  N  TYR D  81   O  CYS D  92           
SHEET    1   K 2 ARG C 109  GLU C 112  0                                        
SHEET    2   K 2 GLN C 115  LYS C 118 -1  O  TYR C 117   N  CYS C 110           
SHEET    1   L 4 THR C 122  PRO C 126  0                                        
SHEET    2   L 4 MET C 133  GLY C 140 -1  O  CYS C 136   N  TRP C 123           
SHEET    3   L 4 GLU C 145  PRO C 150 -1  O  LYS C 149   N  GLU C 135           
SHEET    4   L 4 LEU O 531  GLY O 533 -1  O  GLY O 533   N  TRP C 146           
SHEET    1   M 2 ARG D 109  GLU D 112  0                                        
SHEET    2   M 2 GLN D 115  LYS D 118 -1  O  TYR D 117   N  CYS D 110           
SHEET    1   N 4 THR D 122  ARG D 125  0                                        
SHEET    2   N 4 LEU D 134  GLY D 140 -1  O  CYS D 136   N  TRP D 123           
SHEET    3   N 4 GLU D 145  PRO D 150 -1  O  GLU D 145   N  GLY D 140           
SHEET    4   N 4 LEU P 531  GLY P 533 -1  O  LEU P 531   N  CYS D 148           
SHEET    1   O 2 THR E  65  ASP E  68  0                                        
SHEET    2   O 2 ASN E  73  ARG E  76 -1  O  TYR E  75   N  CYS E  66           
SHEET    1   P 8 THR E  80  LYS E  85  0                                        
SHEET    2   P 8 MET E  88  GLY E  96 -1  O  CYS E  92   N  TYR E  81           
SHEET    3   P 8 ARG E 101  THR E 105 -1  O  ARG E 101   N  ILE E  95           
SHEET    4   P 8 THR Q 542  GLU Q 546 -1  O  VAL Q 543   N  CYS E 104           
SHEET    5   P 8 THR R 542  GLU R 546 -1  O  THR R 542   N  GLU Q 546           
SHEET    6   P 8 ARG F 101  THR F 105 -1  N  ILE F 102   O  GLU R 545           
SHEET    7   P 8 MET F  88  GLY F  96 -1  N  ILE F  95   O  ARG F 101           
SHEET    8   P 8 THR F  80  LYS F  85 -1  N  TYR F  81   O  CYS F  92           
SHEET    1   Q 2 ARG E 109  GLU E 112  0                                        
SHEET    2   Q 2 GLN E 115  LYS E 118 -1  O  TYR E 117   N  CYS E 110           
SHEET    1   R 4 THR E 122  ARG E 124  0                                        
SHEET    2   R 4 GLU E 135  GLY E 140 -1  O  CYS E 136   N  TRP E 123           
SHEET    3   R 4 GLU E 145  LYS E 149 -1  O  LYS E 149   N  GLU E 135           
SHEET    4   R 4 LEU Q 531  GLY Q 533 -1  O  GLY Q 533   N  TRP E 146           
SHEET    1   S 2 THR F  65  PHE F  67  0                                        
SHEET    2   S 2 THR F  74  ARG F  76 -1  O  TYR F  75   N  CYS F  66           
SHEET    1   T 2 ARG F 109  GLU F 112  0                                        
SHEET    2   T 2 GLN F 115  LYS F 118 -1  O  TYR F 117   N  CYS F 110           
SHEET    1   U 4 THR F 122  PRO F 126  0                                        
SHEET    2   U 4 MET F 133  GLY F 140 -1  O  CYS F 136   N  TRP F 123           
SHEET    3   U 4 GLU F 145  PRO F 150 -1  O  GLU F 145   N  GLY F 140           
SHEET    4   U 4 LEU R 531  GLY R 533 -1  O  LEU R 531   N  CYS F 148           
SSBOND   1 CYS A   66    CYS A   94                          1555   1555  2.01  
SSBOND   2 CYS A   92    CYS A  104                          1555   1555  2.07  
SSBOND   3 CYS A  110    CYS A  138                          1555   1555  2.00  
SSBOND   4 CYS A  136    CYS A  148                          1555   1555  2.11  
SSBOND   5 CYS B   66    CYS B   94                          1555   1555  2.03  
SSBOND   6 CYS B   92    CYS B  104                          1555   1555  2.10  
SSBOND   7 CYS B  110    CYS B  138                          1555   1555  2.05  
SSBOND   8 CYS B  136    CYS B  148                          1555   1555  2.07  
SSBOND   9 CYS C   66    CYS C   94                          1555   1555  2.03  
SSBOND  10 CYS C   92    CYS C  104                          1555   1555  2.05  
SSBOND  11 CYS C  110    CYS C  138                          1555   1555  2.06  
SSBOND  12 CYS C  136    CYS C  148                          1555   1555  2.04  
SSBOND  13 CYS D   66    CYS D   94                          1555   1555  2.07  
SSBOND  14 CYS D   92    CYS D  104                          1555   1555  2.09  
SSBOND  15 CYS D  110    CYS D  138                          1555   1555  2.06  
SSBOND  16 CYS D  136    CYS D  148                          1555   1555  2.03  
SSBOND  17 CYS E   66    CYS E   94                          1555   1555  2.02  
SSBOND  18 CYS E   92    CYS E  104                          1555   1555  2.07  
SSBOND  19 CYS E  110    CYS E  138                          1555   1555  2.03  
SSBOND  20 CYS E  136    CYS E  148                          1555   1555  2.04  
SSBOND  21 CYS F   66    CYS F   94                          1555   1555  2.00  
SSBOND  22 CYS F   92    CYS F  104                          1555   1555  2.06  
SSBOND  23 CYS F  110    CYS F  138                          1555   1555  2.06  
SSBOND  24 CYS F  136    CYS F  148                          1555   1555  2.05  
LINK         N   GLU M 529                 C   ACE M 528     1555   1555  1.34  
LINK         C   SER P 549                 N   NH2 P 550     1555   1555  1.33  
SITE     1 AC1  7 ARG B 125  HIS B 127  GLU B 128  THR B 129                    
SITE     2 AC1  7 HOH B 346  HOH B 356  LEU N 531                               
SITE     1 AC2  3 ARG C 125  HIS C 127  GLU C 128                               
SITE     1 AC3  7 ARG A 125  HIS A 127  GLU A 128  THR A 129                    
SITE     2 AC3  7 HOH A 318  HOH A 350  LEU M 531                               
SITE     1 AC4  6 PRO A 150  GLY B  78  THR B  93  GLU M 529                    
SITE     2 AC4  6 HOH M 603  HOH M 609                                          
SITE     1 AC5  4 LYS O 537  TYR P 547  ASP P 548  SER P 549                    
CRYST1   59.590  109.720   71.470  90.00  96.94  90.00 P 1 21 1     12          
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      0.016781  0.000000  0.002043        0.00000                         
SCALE2      0.000000  0.009114  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.014095        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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