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Database: PDB
Entry: 4QBV
LinkDB: 4QBV
Original site: 4QBV 
HEADER    PROTEIN BINDING                         08-MAY-14   4QBV              
TITLE     CRYSTAL STRUCTURE OF C117T MUTANT OF HUMAN ACIDIC FIBROBLAST GROWTH   
TITLE    2 FACTOR IN SODIUM CITRATE BUFFER                                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: FIBROBLAST GROWTH FACTOR 1;                                
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: UNP RESIDUES 16-155;                                       
COMPND   5 SYNONYM: FGF-1, ACIDIC FIBROBLAST GROWTH FACTOR, AFGF, ENDOTHELIAL   
COMPND   6 CELL GROWTH FACTOR, ECGF, HEPARIN-BINDING GROWTH FACTOR 1, HBGF-1;   
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: FGF1, FGFA;                                                    
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET21A(+)                                 
KEYWDS    BETA-TREFOIL, GROWTH FACTOR, FGFR BINDING, HEPARIN BINDING, PROTEIN   
KEYWDS   2 BINDING                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.BLABER,X.XIA                                                        
REVDAT   1   11-MAR-15 4QBV    0                                                
JRNL        AUTH   X.XIA,L.M.LONGO,M.BLABER                                     
JRNL        TITL   MUTATION CHOICE TO ELIMINATE BURIED FREE CYSTEINES IN        
JRNL        TITL 2 PROTEIN THERAPEUTICS.                                        
JRNL        REF    J.PHARM.SCI.                  V. 104   566 2015              
JRNL        REFN                   ISSN 0022-3549                               
JRNL        PMID   25312595                                                     
JRNL        DOI    10.1002/JPS.24188                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.8.4_1496)                   
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 35.38                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 59183                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.150                           
REMARK   3   R VALUE            (WORKING SET) : 0.149                           
REMARK   3   FREE R VALUE                     : 0.168                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 3.380                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2000                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 35.3844 -  3.6077    0.99     4305   150  0.1484 0.1668        
REMARK   3     2  3.6077 -  2.8640    1.00     4151   146  0.1440 0.1701        
REMARK   3     3  2.8640 -  2.5021    1.00     4146   145  0.1490 0.1452        
REMARK   3     4  2.5021 -  2.2733    1.00     4149   144  0.1468 0.1460        
REMARK   3     5  2.2733 -  2.1104    1.00     4103   144  0.1440 0.1650        
REMARK   3     6  2.1104 -  1.9860    1.00     4095   143  0.1420 0.1566        
REMARK   3     7  1.9860 -  1.8865    1.00     4101   144  0.1513 0.1963        
REMARK   3     8  1.8865 -  1.8044    1.00     4102   144  0.1487 0.1718        
REMARK   3     9  1.8044 -  1.7350    1.00     4067   142  0.1527 0.1988        
REMARK   3    10  1.7350 -  1.6751    1.00     4079   142  0.1561 0.1708        
REMARK   3    11  1.6751 -  1.6227    1.00     4067   142  0.1592 0.1818        
REMARK   3    12  1.6227 -  1.5763    1.00     4078   143  0.1605 0.1795        
REMARK   3    13  1.5763 -  1.5348    1.00     4035   141  0.1649 0.1715        
REMARK   3    14  1.5348 -  1.4970    0.91     3705   130  0.1752 0.2149        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.110            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 16.060           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.017           2415                                  
REMARK   3   ANGLE     :  1.434           3276                                  
REMARK   3   CHIRALITY :  0.066            336                                  
REMARK   3   PLANARITY :  0.007            431                                  
REMARK   3   DIHEDRAL  : 15.770            944                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4QBV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-MAY-14.                  
REMARK 100 THE RCSB ID CODE IS RCSB085858.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 16-APR-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 22-BM                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97911                            
REMARK 200  MONOCHROMATOR                  : ROSENBAUM-ROCK DOUBLE-CRYSTAL      
REMARK 200                                   SI(220)                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 225 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 59183                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.497                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHENIX (PHASER MR)                                    
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 55.44                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.76                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.9 M SODIUM CITRATE, 0.1 M IMIDAZOLE,   
REMARK 280  PH 8.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K             
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       52.98300            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       52.98300            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       36.58750            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       47.51650            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       36.58750            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       47.51650            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       52.98300            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       36.58750            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       47.51650            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       52.98300            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       36.58750            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       47.51650            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     HIS A     1A                                                     
REMARK 465     HIS A     1B                                                     
REMARK 465     SER A   138                                                      
REMARK 465     SER A   139                                                      
REMARK 465     ASP A   140                                                      
REMARK 465     HIS B     1A                                                     
REMARK 465     HIS B     1B                                                     
REMARK 465     SER B   138                                                      
REMARK 465     SER B   139                                                      
REMARK 465     ASP B   140                                                      
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   H    PHE A   108     HG1  THR A   123              1.20            
REMARK 500   HG   SER A    17     O    HOH A   486              1.53            
REMARK 500   HE   ARG A   122     OD2  ASP B    68              1.55            
REMARK 500  HE22  GLN B    63     O    HOH B   442              1.56            
REMARK 500   O    HOH A   333     O    HOH A   340              2.02            
REMARK 500   O    HOH A   350     O    HOH A   381              2.09            
REMARK 500   NE2  GLN B    63     O    HOH B   442              2.10            
REMARK 500   O    HOH B   377     O    HOH B   383              2.11            
REMARK 500   O    HOH B   420     O    HOH B   433              2.11            
REMARK 500   O    HOH B   463     O    HOH B   469              2.13            
REMARK 500   O    HOH A   465     O    HOH A   476              2.13            
REMARK 500   O    HOH B   467     O    HOH B   469              2.15            
REMARK 500   O    HOH B   472     O    HOH B   473              2.16            
REMARK 500   O    HOH A   476     O    HOH A   479              2.17            
REMARK 500   O    HOH A   488     O    HOH A   494              2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH A   449     O    HOH A   449     4557     2.04            
REMARK 500   O    HOH A   453     O    HOH B   434     6554     2.09            
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    GLU A  49     -104.62    -97.26                                   
REMARK 500    HIS A  93      -50.46   -157.98                                   
REMARK 500    GLU B  49     -106.49   -103.46                                   
REMARK 500    HIS B  93      -51.85   -155.28                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FLC A 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FLC B 201                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2AFG   RELATED DB: PDB                                   
REMARK 900 WILD-TYPE HUMAN FGF-1                                                
REMARK 900 RELATED ID: 1JQZ   RELATED DB: PDB                                   
REMARK 900 WILD-TYPE HUMAN FGF-1 WITH 6XHISTAG                                  
REMARK 900 RELATED ID: 1RG8   RELATED DB: PDB                                   
REMARK 900 WILD-TYPE HUMAN FGF-1                                                
REMARK 900 RELATED ID: 4Q91   RELATED DB: PDB                                   
REMARK 900 FGF-1 MUTANT C16A/K12V/C117V/P134V                                   
REMARK 900 RELATED ID: 4Q9G   RELATED DB: PDB                                   
REMARK 900 FGF-1 MUTANT C16S/K12V/C117V/P134V                                   
REMARK 900 RELATED ID: 4Q9P   RELATED DB: PDB                                   
REMARK 900 FGF-1 MUTANT C16T/K12V/C117V/P134V                                   
REMARK 900 RELATED ID: 4QAL   RELATED DB: PDB                                   
REMARK 900 FGF-1 MUTANT C117A                                                   
REMARK 900 RELATED ID: 4QBC   RELATED DB: PDB                                   
REMARK 900 FGF-1 MUTANT C117T IN FORMATE BUFFER                                 
REMARK 900 RELATED ID: 1JY0   RELATED DB: PDB                                   
REMARK 900 FGF-1 MUTANT C117V                                                   
REMARK 900 RELATED ID: 3FJH   RELATED DB: PDB                                   
REMARK 900 FGF-1 MUTANT C83A                                                    
REMARK 900 RELATED ID: 3FJF   RELATED DB: PDB                                   
REMARK 900 FGF-1 MUTANT C83T                                                    
REMARK 900 RELATED ID: 3FJE   RELATED DB: PDB                                   
REMARK 900 FGF-1 MUTANT C83S                                                    
REMARK 900 RELATED ID: 3FJK   RELATED DB: PDB                                   
REMARK 900 FGF-1 MUTANT C83V                                                    
DBREF  4QBV A    1G  140  UNP    P05230   FGF1_HUMAN      16    155             
DBREF  4QBV B    1G  140  UNP    P05230   FGF1_HUMAN      16    155             
SEQADV 4QBV HIS A    1A UNP  P05230              EXPRESSION TAG                 
SEQADV 4QBV HIS A    1B UNP  P05230              EXPRESSION TAG                 
SEQADV 4QBV HIS A    1C UNP  P05230              EXPRESSION TAG                 
SEQADV 4QBV HIS A    1D UNP  P05230              EXPRESSION TAG                 
SEQADV 4QBV HIS A    1E UNP  P05230              EXPRESSION TAG                 
SEQADV 4QBV HIS A    1F UNP  P05230              EXPRESSION TAG                 
SEQADV 4QBV THR A  117  UNP  P05230    CYS   132 ENGINEERED MUTATION            
SEQADV 4QBV HIS B    1A UNP  P05230              EXPRESSION TAG                 
SEQADV 4QBV HIS B    1B UNP  P05230              EXPRESSION TAG                 
SEQADV 4QBV HIS B    1C UNP  P05230              EXPRESSION TAG                 
SEQADV 4QBV HIS B    1D UNP  P05230              EXPRESSION TAG                 
SEQADV 4QBV HIS B    1E UNP  P05230              EXPRESSION TAG                 
SEQADV 4QBV HIS B    1F UNP  P05230              EXPRESSION TAG                 
SEQADV 4QBV THR B  117  UNP  P05230    CYS   132 ENGINEERED MUTATION            
SEQRES   1 A  146  HIS HIS HIS HIS HIS HIS PHE ASN LEU PRO PRO GLY ASN          
SEQRES   2 A  146  TYR LYS LYS PRO LYS LEU LEU TYR CYS SER ASN GLY GLY          
SEQRES   3 A  146  HIS PHE LEU ARG ILE LEU PRO ASP GLY THR VAL ASP GLY          
SEQRES   4 A  146  THR ARG ASP ARG SER ASP GLN HIS ILE GLN LEU GLN LEU          
SEQRES   5 A  146  SER ALA GLU SER VAL GLY GLU VAL TYR ILE LYS SER THR          
SEQRES   6 A  146  GLU THR GLY GLN TYR LEU ALA MET ASP THR ASP GLY LEU          
SEQRES   7 A  146  LEU TYR GLY SER GLN THR PRO ASN GLU GLU CYS LEU PHE          
SEQRES   8 A  146  LEU GLU ARG LEU GLU GLU ASN HIS TYR ASN THR TYR ILE          
SEQRES   9 A  146  SER LYS LYS HIS ALA GLU LYS ASN TRP PHE VAL GLY LEU          
SEQRES  10 A  146  LYS LYS ASN GLY SER THR LYS ARG GLY PRO ARG THR HIS          
SEQRES  11 A  146  TYR GLY GLN LYS ALA ILE LEU PHE LEU PRO LEU PRO VAL          
SEQRES  12 A  146  SER SER ASP                                                  
SEQRES   1 B  146  HIS HIS HIS HIS HIS HIS PHE ASN LEU PRO PRO GLY ASN          
SEQRES   2 B  146  TYR LYS LYS PRO LYS LEU LEU TYR CYS SER ASN GLY GLY          
SEQRES   3 B  146  HIS PHE LEU ARG ILE LEU PRO ASP GLY THR VAL ASP GLY          
SEQRES   4 B  146  THR ARG ASP ARG SER ASP GLN HIS ILE GLN LEU GLN LEU          
SEQRES   5 B  146  SER ALA GLU SER VAL GLY GLU VAL TYR ILE LYS SER THR          
SEQRES   6 B  146  GLU THR GLY GLN TYR LEU ALA MET ASP THR ASP GLY LEU          
SEQRES   7 B  146  LEU TYR GLY SER GLN THR PRO ASN GLU GLU CYS LEU PHE          
SEQRES   8 B  146  LEU GLU ARG LEU GLU GLU ASN HIS TYR ASN THR TYR ILE          
SEQRES   9 B  146  SER LYS LYS HIS ALA GLU LYS ASN TRP PHE VAL GLY LEU          
SEQRES  10 B  146  LYS LYS ASN GLY SER THR LYS ARG GLY PRO ARG THR HIS          
SEQRES  11 B  146  TYR GLY GLN LYS ALA ILE LEU PHE LEU PRO LEU PRO VAL          
SEQRES  12 B  146  SER SER ASP                                                  
HET    FLC  A 201      18                                                       
HET    FLC  B 201      18                                                       
HETNAM     FLC CITRATE ANION                                                    
FORMUL   3  FLC    2(C6 H5 O7 3-)                                               
FORMUL   5  HOH   *413(H2 O)                                                    
HELIX    1   1 ASN A   80  CYS A   83  5                                   4    
HELIX    2   2 HIS A  102  ASN A  106  5                                   5    
HELIX    3   3 ARG A  119  THR A  123  5                                   5    
HELIX    4   4 ASP B   39  ILE B   42  5                                   4    
HELIX    5   5 ASN B   80  CYS B   83  5                                   4    
HELIX    6   6 HIS B  102  ASN B  106  5                                   5    
HELIX    7   7 ARG B  119  THR B  123  5                                   5    
SHEET    1   A 4 VAL A  31  THR A  34  0                                        
SHEET    2   A 4 HIS A  21  ILE A  25 -1  N  PHE A  22   O  THR A  34           
SHEET    3   A 4 LYS A  12  CYS A  16 -1  N  CYS A  16   O  HIS A  21           
SHEET    4   A 4 PHE A 132  PRO A 136 -1  O  LEU A 135   N  LEU A  13           
SHEET    1   B 4 LEU A  44  ALA A  48  0                                        
SHEET    2   B 4 GLU A  53  SER A  58 -1  O  LYS A  57   N  GLN A  45           
SHEET    3   B 4 PHE A  85  GLU A  90 -1  O  PHE A  85   N  VAL A  54           
SHEET    4   B 4 TYR A  94  SER A  99 -1  O  ILE A  98   N  LEU A  86           
SHEET    1   C 2 TYR A  64  MET A  67  0                                        
SHEET    2   C 2 LEU A  73  SER A  76 -1  O  SER A  76   N  TYR A  64           
SHEET    1   D 4 VAL B  31  THR B  34  0                                        
SHEET    2   D 4 HIS B  21  ILE B  25 -1  N  PHE B  22   O  THR B  34           
SHEET    3   D 4 LYS B  12  CYS B  16 -1  N  CYS B  16   O  HIS B  21           
SHEET    4   D 4 PHE B 132  PRO B 136 -1  O  LEU B 133   N  TYR B  15           
SHEET    1   E 4 LEU B  44  ALA B  48  0                                        
SHEET    2   E 4 GLU B  53  SER B  58 -1  O  LYS B  57   N  GLN B  45           
SHEET    3   E 4 PHE B  85  GLU B  90 -1  O  PHE B  85   N  VAL B  54           
SHEET    4   E 4 TYR B  94  SER B  99 -1  O  ILE B  98   N  LEU B  86           
SHEET    1   F 2 TYR B  64  MET B  67  0                                        
SHEET    2   F 2 LEU B  73  SER B  76 -1  O  SER B  76   N  TYR B  64           
SITE     1 AC1 14 ASN A  18  LYS A 112  LYS A 113  LYS A 118                    
SITE     2 AC1 14 GLN A 127  LYS A 128  ALA A 129  HOH A 375                    
SITE     3 AC1 14 HOH A 384  HOH A 388  HOH A 400  HOH A 459                    
SITE     4 AC1 14 HOH A 482  ASP B  70                                          
SITE     1 AC2 10 ASN B  18  LYS B 112  LYS B 113  LYS B 118                    
SITE     2 AC2 10 GLN B 127  LYS B 128  ALA B 129  HOH B 409                    
SITE     3 AC2 10 HOH B 450  HOH B 491                                          
CRYST1   73.175   95.033  105.966  90.00  90.00  90.00 C 2 2 21     16          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.013666  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010523  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009437        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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