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Database: PDB
Entry: 3CAL
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Original site: 3CAL 
HEADER    CELL ADHESION                           20-FEB-08   3CAL              
TITLE     CRYSTAL STRUCTURE OF THE SECOND AND THIRD FIBRONECTIN F1 MODULES IN   
TITLE    2 COMPLEX WITH A FRAGMENT OF STAPHYLOCOCCUS AUREUS FNBPA-5             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: FIBRONECTIN;                                               
COMPND   3 CHAIN: A, C;                                                         
COMPND   4 FRAGMENT: UNP RESIDUES 93-182, SECOND AND THIRD F1 MODULES;          
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: B, D;                                                         
COMPND  10 FRAGMENT: UNP RESIDUES 655-672;                                      
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_COMMON: FUNGI;                                     
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 4922;                                       
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: GS115;                                     
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 SYNTHETIC: YES;                                                      
SOURCE  12 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS (STRAIN NCTC 8325);       
SOURCE  13 ORGANISM_TAXID: 93061;                                               
SOURCE  14 OTHER_DETAILS: PEPTIDE SYNTHESIS                                     
KEYWDS    FIBRONECTIN, 2F13F1, BETA ZIPPER, STAPHYLOCOCCUS AUREUS, ACUTE PHASE, 
KEYWDS   2 ALTERNATIVE SPLICING, CELL ADHESION, EXTRACELLULAR MATRIX,           
KEYWDS   3 GLYCOPROTEIN, HEPARIN-BINDING, PHOSPHOPROTEIN, POLYMORPHISM,         
KEYWDS   4 PYRROLIDONE CARBOXYLIC ACID, SECRETED, SULFATION, CELL WALL,         
KEYWDS   5 PEPTIDOGLYCAN-ANCHOR, VIRULENCE                                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    R.J.BINGHAM                                                           
REVDAT   5   19-JUN-19 3CAL    1       COMPND SOURCE REMARK DBREF               
REVDAT   5 2                   1       SEQADV SEQRES SHEET  LINK                
REVDAT   5 3                   1       ATOM                                     
REVDAT   4   24-FEB-09 3CAL    1       VERSN                                    
REVDAT   3   16-SEP-08 3CAL    1       REMARK                                   
REVDAT   2   09-SEP-08 3CAL    1       JRNL                                     
REVDAT   1   05-AUG-08 3CAL    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.    1.70 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) : 1.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 36.59                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 19459                          
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) : 0.179                           
REMARK   3   R VALUE            (WORKING SET) : 0.177                           
REMARK   3   FREE R VALUE                     : 0.217                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1051                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.70                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.74                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1421                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 95.62                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2300                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 109                          
REMARK   3   BIN FREE R VALUE                    : 0.3080                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1622                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 204                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 16.70                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 20.14                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.79000                                              
REMARK   3    B22 (A**2) : -0.75000                                             
REMARK   3    B33 (A**2) : -0.13000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.51000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.121         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.117         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.079         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.332         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.956                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.934                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1684 ; 0.014 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2278 ; 1.428 ; 1.937       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   211 ; 6.095 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    73 ;31.103 ;22.877       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   281 ;13.072 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    14 ;14.806 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   238 ; 0.006 ; 0.020       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1272 ; 0.008 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   107 ; 0.249 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):   236 ; 0.318 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):    42 ; 0.171 ; 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):     2 ; 0.191 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     5 ; 0.390 ; 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):  1046 ; 1.034 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1678 ; 1.792 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   638 ; 2.536 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   598 ; 4.036 ; 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   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3CAL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 22-FEB-08.                  
REMARK 100 THE DEPOSITION ID IS D_1000046546.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 04-FEB-08                          
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                       : ID14-4                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97900                            
REMARK 200  MONOCHROMATOR                  : SI 111 CHANNEL                     
REMARK 200  OPTICS                         : MIRRORS                            
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   : 19459                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 36.588                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 3.700                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.3                               
REMARK 200  DATA REDUNDANCY                : 3.800                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.05100                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 20.7000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.79                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.80                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.32100                            
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: PDB ENTRY 2RKZ                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 39.90                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.05                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.95M 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       36.71900            
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                                                    
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: 2070 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 6160 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -5.2 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
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: 2220 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 6110 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -7.4 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     THR A   129                                                      
REMARK 465     NH2 B   673                                                      
REMARK 465     ALA C    62                                                      
REMARK 465     THR C   129                                                      
REMARK 465     GLY C   130                                                      
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 A  63    CD   OE1  OE2                                       
REMARK 470     GLU A 128    CG   CD   OE1  OE2                                  
REMARK 470     ARG C  99    NE   CZ   NH1  NH2                                  
REMARK 470     LYS C 118    CD   CE   NZ                                        
REMARK 470     GLU C 135    CG   CD   OE1  OE2                                  
REMARK 470     ILE C 151    CG1  CD1                                            
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH C   266     O    HOH D   228              2.09            
REMARK 500   O    GLU C   135     O    HOH C   274              2.13            
REMARK 500   O    HOH A   184     O    HOH C   267              2.18            
REMARK 500   OD1  ASN C   108     O    HOH C   267              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   OE1  GLU C    63     O    HOH A   175     2656     2.10            
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    LYS A 143       31.19   -151.50                                   
REMARK 500    LYS C 143       29.57   -152.57                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2RKY   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2RKZ   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2RL0   RELATED DB: PDB                                   
DBREF  3CAL A   62   151  UNP    P02751   FINC_HUMAN      93    182             
DBREF  3CAL B  655   672  UNP    P14738   FNBA_STAA8     655    672             
DBREF  3CAL C   62   151  UNP    P02751   FINC_HUMAN      93    182             
DBREF  3CAL D  655   672  UNP    P14738   FNBA_STAA8     655    672             
SEQADV 3CAL ACE B  654  UNP  P14738              ACETYLATION                    
SEQADV 3CAL NH2 B  673  UNP  P14738              AMIDATION                      
SEQADV 3CAL ACE D  654  UNP  P14738              ACETYLATION                    
SEQADV 3CAL NH2 D  673  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   20  ACE LYS GLY ILE VAL THR GLY ALA VAL SER ASP HIS THR          
SEQRES   2 B   20  THR VAL GLU ASP THR LYS NH2                                  
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   20  ACE LYS GLY ILE VAL THR GLY ALA VAL SER ASP HIS THR          
SEQRES   2 D   20  THR VAL GLU ASP THR LYS NH2                                  
HET    ACE  B 654       3                                                       
HET    ACE  D 654       3                                                       
HET    NH2  D 673       1                                                       
HETNAM     ACE ACETYL GROUP                                                     
HETNAM     NH2 AMINO GROUP                                                      
FORMUL   2  ACE    2(C2 H4 O)                                                   
FORMUL   4  NH2    H2 N                                                         
FORMUL   5  HOH   *204(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  TRP A  90   N  ARG A  83           
SHEET    3   B 4 ARG A 101  THR A 105 -1  O  THR A 105   N  ASP A  91           
SHEET    4   B 4 THR B 666  GLU B 669 -1  O  GLU B 669   N  ILE A 102           
SHEET    1   C 2 ARG A 109  GLU A 112  0                                        
SHEET    2   C 2 GLN A 115  LYS A 118 -1  O  TYR A 117   N  CYS A 110           
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 VAL B 658  GLY B 660 -1  O  VAL B 658   N  CYS A 148           
SHEET    1   E 2 THR C  65  PHE C  67  0                                        
SHEET    2   E 2 THR C  74  ARG C  76 -1  O  TYR C  75   N  CYS C  66           
SHEET    1   F 4 THR C  80  LYS C  85  0                                        
SHEET    2   F 4 MET C  88  GLY C  96 -1  O  TRP C  90   N  ARG C  83           
SHEET    3   F 4 ARG C 101  THR C 105 -1  O  ARG C 101   N  ILE C  95           
SHEET    4   F 4 THR D 666  GLU D 669 -1  O  THR D 667   N  CYS C 104           
SHEET    1   G 2 ARG C 109  GLU C 112  0                                        
SHEET    2   G 2 GLN C 115  LYS C 118 -1  O  TYR C 117   N  CYS C 110           
SHEET    1   H 4 THR C 122  PRO C 126  0                                        
SHEET    2   H 4 MET C 133  GLY C 140 -1  O  LEU C 134   N  ARG C 125           
SHEET    3   H 4 GLU C 145  PRO C 150 -1  O  LYS C 149   N  GLU C 135           
SHEET    4   H 4 VAL D 658  GLY D 660 -1  O  VAL D 658   N  CYS C 148           
SSBOND   1 CYS A   66    CYS A   94                          1555   1555  2.01  
SSBOND   2 CYS A   92    CYS A  104                          1555   1555  2.01  
SSBOND   3 CYS A  110    CYS A  138                          1555   1555  2.05  
SSBOND   4 CYS A  136    CYS A  148                          1555   1555  2.03  
SSBOND   5 CYS C   66    CYS C   94                          1555   1555  2.04  
SSBOND   6 CYS C   92    CYS C  104                          1555   1555  2.07  
SSBOND   7 CYS C  110    CYS C  138                          1555   1555  2.06  
SSBOND   8 CYS C  136    CYS C  148                          1555   1555  2.05  
LINK         C   ACE B 654                 N   LYS B 655     1555   1555  1.33  
LINK         C   ACE D 654                 N   LYS D 655     1555   1555  1.33  
LINK         N   NH2 D 673                 C   LYS D 672     1555   1555  1.34  
CISPEP   1 GLY A  130    GLY A  131          0        -5.35                     
CRYST1   36.495   73.438   36.742  90.00  95.05  90.00 P 1 21 1      4          
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      0.027401  0.000000  0.002422        0.00000                         
SCALE2      0.000000  0.013617  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.027323        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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