GenomeNet

Database: PDB
Entry: 6MZW
LinkDB: 6MZW
Original site: 6MZW 
HEADER    TRANSFERASE/TRANSFERASE INHIBITOR       05-NOV-18   6MZW              
TITLE     TAS-120 COVALENT COMPLEX WITH FGFR1                                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: FIBROBLAST GROWTH FACTOR RECEPTOR 1;                       
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: FGFR-1,BASIC FIBROBLAST GROWTH FACTOR RECEPTOR 1,BFGF-R-1,  
COMPND   5 FMS-LIKE TYROSINE KINASE 2,FLT-2,N-SAM,PROTO-ONCOGENE C-FGR;         
COMPND   6 EC: 2.7.10.1;                                                        
COMPND   7 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: FGFR1, BFGFR, CEK, FGFBR, FLG, FLT2, HBGFR;                    
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    FGFR1, TAS-120, INHIBITOR, COMPLEX, COVALENT, TRANSFERASE,            
KEYWDS   2 TRANSFERASE-TRANSFERASE INHIBITOR COMPLEX                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.KALYUKINA,C.J.SQUIRE                                                
REVDAT   3   06-MAR-19 6MZW    1       JRNL                                     
REVDAT   2   30-JAN-19 6MZW    1       JRNL                                     
REVDAT   1   16-JAN-19 6MZW    0                                                
JRNL        AUTH   M.KALYUKINA,Y.YOSAATMADJA,M.J.MIDDLEDITCH,A.V.PATTERSON,     
JRNL        AUTH 2 J.B.SMAILL,C.J.SQUIRE                                        
JRNL        TITL   TAS-120 CANCER TARGET BINDING: DEFINING REACTIVITY AND       
JRNL        TITL 2 REVEALING THE FIRST FIBROBLAST GROWTH FACTOR RECEPTOR 1      
JRNL        TITL 3 (FGFR1) IRREVERSIBLE STRUCTURE.                              
JRNL        REF    CHEMMEDCHEM                   V.  14   494 2019              
JRNL        REFN                   ESSN 1860-7187                               
JRNL        PMID   30600916                                                     
JRNL        DOI    10.1002/CMDC.201800719                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0230                                      
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) : 2.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 47.63                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 30946                          
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) : 0.244                           
REMARK   3   R VALUE            (WORKING SET) : 0.241                           
REMARK   3   FREE R VALUE                     : 0.297                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1579                            
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) : 2.20                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.26                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2280                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.92                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.4250                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 102                          
REMARK   3   BIN FREE R VALUE                    : 0.4530                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3991                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 67                                      
REMARK   3   SOLVENT ATOMS            : 48                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 49.23                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.11000                                              
REMARK   3    B22 (A**2) : -0.22000                                             
REMARK   3    B33 (A**2) : 0.09000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.01000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.288         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.243         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.269         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 11.726        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.937                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.899                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4168 ; 0.008 ; 0.014       
REMARK   3   BOND LENGTHS OTHERS               (A):  3697 ; 0.002 ; 0.017       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5679 ; 1.085 ; 1.675       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  8574 ; 0.854 ; 1.655       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   537 ; 6.581 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   168 ;32.417 ;22.202       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   634 ;14.273 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    21 ;19.615 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   553 ; 0.052 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4684 ; 0.004 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   738 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  2166 ; 3.115 ; 5.267       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  2165 ; 3.115 ; 5.266       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2697 ; 4.891 ; 7.875       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  2698 ; 4.891 ; 7.877       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2002 ; 3.320 ; 5.390       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  1999 ; 3.317 ; 5.387       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  2977 ; 5.092 ; 7.981       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  4607 ; 7.358 ;60.217       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  4607 ; 7.357 ;60.216       
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: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 6MZW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-NOV-18.                  
REMARK 100 THE DEPOSITION ID IS D_1000237930.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-FEB-18                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : AUSTRALIAN SYNCHROTRON             
REMARK 200  BEAMLINE                       : MX2                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9537                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 32531                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 100.000                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 6.900                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.3000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.27                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.90                               
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: PHASER                                                
REMARK 200 STARTING MODEL: 5UR1                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 45.59                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.26                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: MPEG 5000, AMMONIUM SULFATE, SODIUM      
REMARK 280  CACODYLATE, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K         
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000      104.45950            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       24.49050            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000      104.45950            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       24.49050            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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     GLY A   455                                                      
REMARK 465     ALA A   456                                                      
REMARK 465     MET A   457                                                      
REMARK 465     SER A   458                                                      
REMARK 465     GLY A   459                                                      
REMARK 465     VAL A   460                                                      
REMARK 465     SER A   461                                                      
REMARK 465     GLU A   462                                                      
REMARK 465     TYR A   463                                                      
REMARK 465     HIS A   589                                                      
REMARK 465     ASN A   590                                                      
REMARK 465     ALA A   645                                                      
REMARK 465     ARG A   646                                                      
REMARK 465     ASP A   647                                                      
REMARK 465     ILE A   648                                                      
REMARK 465     HIS A   649                                                      
REMARK 465     HIS A   650                                                      
REMARK 465     ILE A   651                                                      
REMARK 465     ASP A   652                                                      
REMARK 465     TYR A   653                                                      
REMARK 465     TYR A   654                                                      
REMARK 465     LYS A   655                                                      
REMARK 465     LYS A   656                                                      
REMARK 465     THR A   657                                                      
REMARK 465     THR A   658                                                      
REMARK 465     ASN A   659                                                      
REMARK 465     GLY A   660                                                      
REMARK 465     ARG A   661                                                      
REMARK 465     LEU A   662                                                      
REMARK 465     GLY B   455                                                      
REMARK 465     ALA B   456                                                      
REMARK 465     MET B   457                                                      
REMARK 465     SER B   458                                                      
REMARK 465     GLY B   459                                                      
REMARK 465     VAL B   460                                                      
REMARK 465     SER B   461                                                      
REMARK 465     GLU B   462                                                      
REMARK 465     GLU B   486                                                      
REMARK 465     GLY B   487                                                      
REMARK 465     CYS B   488                                                      
REMARK 465     PHE B   489                                                      
REMARK 465     GLY B   490                                                      
REMARK 465     LYS B   502                                                      
REMARK 465     ASP B   503                                                      
REMARK 465     PRO B   579                                                      
REMARK 465     GLY B   580                                                      
REMARK 465     LEU B   581                                                      
REMARK 465     GLU B   582                                                      
REMARK 465     TYR B   583                                                      
REMARK 465     SER B   584                                                      
REMARK 465     TYR B   585                                                      
REMARK 465     ASN B   586                                                      
REMARK 465     PRO B   587                                                      
REMARK 465     SER B   588                                                      
REMARK 465     HIS B   589                                                      
REMARK 465     ASN B   590                                                      
REMARK 465     PRO B   591                                                      
REMARK 465     GLU B   592                                                      
REMARK 465     GLU B   593                                                      
REMARK 465     GLY B   643                                                      
REMARK 465     LEU B   644                                                      
REMARK 465     ALA B   645                                                      
REMARK 465     ARG B   646                                                      
REMARK 465     ASP B   647                                                      
REMARK 465     ILE B   648                                                      
REMARK 465     HIS B   649                                                      
REMARK 465     HIS B   650                                                      
REMARK 465     ILE B   651                                                      
REMARK 465     ASP B   652                                                      
REMARK 465     TYR B   653                                                      
REMARK 465     TYR B   654                                                      
REMARK 465     LYS B   655                                                      
REMARK 465     LYS B   656                                                      
REMARK 465     THR B   657                                                      
REMARK 465     THR B   658                                                      
REMARK 465     ASN B   659                                                      
REMARK 465     GLY B   660                                                      
REMARK 465     ARG B   661                                                      
REMARK 465     LEU B   662                                                      
REMARK 465     ASN B   763                                                      
REMARK 465     GLN B   764                                                      
REMARK 465     GLU B   765                                                      
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 464    CG   CD   OE1  OE2                                  
REMARK 470     LEU A 465    CG   CD1  CD2                                       
REMARK 470     GLU A 467    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 486    CG   CD   OE1  OE2                                  
REMARK 470     GLN A 491    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 502    CG   CD   CE   NZ                                   
REMARK 470     ARG A 507    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 510    CG   CD   CE   NZ                                   
REMARK 470     LYS A 517    CG   CD   CE   NZ                                   
REMARK 470     SER A 518    OG                                                  
REMARK 470     ASP A 519    CG   OD1  OD2                                       
REMARK 470     THR A 521    OG1  CG2                                            
REMARK 470     GLU A 522    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 523    CG   CD   CE   NZ                                   
REMARK 470     LEU A 525    CG   CD1  CD2                                       
REMARK 470     MET A 534    CG   SD   CE                                        
REMARK 470     LYS A 540    CG   CD   CE   NZ                                   
REMARK 470     LYS A 542    CG   CD   CE   NZ                                   
REMARK 470     ASP A 554    CG   OD1  OD2                                       
REMARK 470     LEU A 581    CG   CD1  CD2                                       
REMARK 470     GLU A 582    CG   CD   OE1  OE2                                  
REMARK 470     TYR A 583    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     SER A 584    OG                                                  
REMARK 470     ARG A 627    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     PHE A 673    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ASP A 674    CG   OD1  OD2                                       
REMARK 470     ARG A 675    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     VAL A 706    CG1  CG2                                            
REMARK 470     GLU A 707    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 708    CG   CD   OE1  OE2                                  
REMARK 470     LEU A 709    CG   CD1  CD2                                       
REMARK 470     PHE A 710    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LYS A 711    CG   CD   CE   NZ                                   
REMARK 470     LYS A 714    CG   CD   CE   NZ                                   
REMARK 470     ASN A 724    CG   OD1  ND2                                       
REMARK 470     MET A 731    CG   SD   CE                                        
REMARK 470     LYS A 748    CG   CD   CE   NZ                                   
REMARK 470     ARG A 756    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN A 764    CG   CD   OE1  NE2                                  
REMARK 470     GLU A 765    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 464    CG   CD   OE1  OE2                                  
REMARK 470     ARG B 470    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B 477    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 482    CG   CD   CE   NZ                                   
REMARK 470     LEU B 484    CG   CD1  CD2                                       
REMARK 470     GLU B 496    CG   CD   OE1  OE2                                  
REMARK 470     ILE B 498    CG1  CG2  CD1                                       
REMARK 470     ASP B 501    CG   OD1  OD2                                       
REMARK 470     ARG B 507    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     THR B 509    OG1  CG2                                            
REMARK 470     LYS B 517    CD   CE   NZ                                        
REMARK 470     ASP B 519    CG   OD1  OD2                                       
REMARK 470     GLU B 522    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 523    CG   CD   CE   NZ                                   
REMARK 470     LEU B 525    CG   CD1  CD2                                       
REMARK 470     LYS B 540    CG   CD   CE   NZ                                   
REMARK 470     ASP B 554    CG   OD1  OD2                                       
REMARK 470     GLN B 594    CG   CD   OE1  NE2                                  
REMARK 470     ARG B 609    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 618    CG   CD   CE   NZ                                   
REMARK 470     ARG B 627    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B 633    CG   CD   OE1  OE2                                  
REMARK 470     ASP B 634    CG   OD1  OD2                                       
REMARK 470     VAL B 636    CG1  CG2                                            
REMARK 470     ASP B 641    CG   OD1  OD2                                       
REMARK 470     PHE B 673    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     GLN B 680    CG   CD   OE1  NE2                                  
REMARK 470     VAL B 706    CG1  CG2                                            
REMARK 470     GLU B 707    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 708    CG   CD   OE1  OE2                                  
REMARK 470     PHE B 710    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LYS B 711    CG   CD   CE   NZ                                   
REMARK 470     LEU B 713    CG   CD1  CD2                                       
REMARK 470     LYS B 714    CG   CD   CE   NZ                                   
REMARK 470     ASN B 724    CG   OD1  ND2                                       
REMARK 470     ASN B 727    CG   OD1  ND2                                       
REMARK 470     GLU B 728    CG   CD   OE1  OE2                                  
REMARK 470     MET B 731    CG   SD   CE                                        
REMARK 470     GLN B 743    CG   CD   OE1  NE2                                  
REMARK 470     LYS B 748    CG   CD   CE   NZ                                   
REMARK 470     GLN B 749    CG   CD   OE1  NE2                                  
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    ASP A 554       30.49    -84.96                                   
REMARK 500    ARG A 622       -8.47     83.74                                   
REMARK 500    ASP A 623       49.97   -153.09                                   
REMARK 500    ARG B 622       -7.56     82.90                                   
REMARK 500    ASP B 623       77.38   -161.33                                   
REMARK 500    TYR B 701       63.94     38.19                                   
REMARK 500    ASN B 724       63.75     64.50                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    ARG A 475         0.09    SIDE CHAIN                              
REMARK 500    ARG A 570         0.10    SIDE CHAIN                              
REMARK 500    ARG A 744         0.12    SIDE CHAIN                              
REMARK 500    ARG B 475         0.12    SIDE CHAIN                              
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 TZ0 A 801                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 802                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue TZ0 B 801                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 6MZQ   RELATED DB: PDB                                   
REMARK 900 REVERSIBLE MODE OF TAS120 BINDING TO FGFR1                           
DBREF  6MZW A  459   765  UNP    P11362   FGFR1_HUMAN    368    674             
DBREF  6MZW B  459   765  UNP    P11362   FGFR1_HUMAN    368    674             
SEQADV 6MZW GLY A  455  UNP  P11362              EXPRESSION TAG                 
SEQADV 6MZW ALA A  456  UNP  P11362              EXPRESSION TAG                 
SEQADV 6MZW MET A  457  UNP  P11362              EXPRESSION TAG                 
SEQADV 6MZW SER A  458  UNP  P11362              EXPRESSION TAG                 
SEQADV 6MZW SER A  584  UNP  P11362    CYS   493 CONFLICT                       
SEQADV 6MZW GLY B  455  UNP  P11362              EXPRESSION TAG                 
SEQADV 6MZW ALA B  456  UNP  P11362              EXPRESSION TAG                 
SEQADV 6MZW MET B  457  UNP  P11362              EXPRESSION TAG                 
SEQADV 6MZW SER B  458  UNP  P11362              EXPRESSION TAG                 
SEQADV 6MZW SER B  584  UNP  P11362    CYS   493 CONFLICT                       
SEQRES   1 A  311  GLY ALA MET SER GLY VAL SER GLU TYR GLU LEU PRO GLU          
SEQRES   2 A  311  ASP PRO ARG TRP GLU LEU PRO ARG ASP ARG LEU VAL LEU          
SEQRES   3 A  311  GLY LYS PRO LEU GLY GLU GLY CYS PHE GLY GLN VAL VAL          
SEQRES   4 A  311  LEU ALA GLU ALA ILE GLY LEU ASP LYS ASP LYS PRO ASN          
SEQRES   5 A  311  ARG VAL THR LYS VAL ALA VAL LYS MET LEU LYS SER ASP          
SEQRES   6 A  311  ALA THR GLU LYS ASP LEU SER ASP LEU ILE SER GLU MET          
SEQRES   7 A  311  GLU MET MET LYS MET ILE GLY LYS HIS LYS ASN ILE ILE          
SEQRES   8 A  311  ASN LEU LEU GLY ALA CYS THR GLN ASP GLY PRO LEU TYR          
SEQRES   9 A  311  VAL ILE VAL GLU TYR ALA SER LYS GLY ASN LEU ARG GLU          
SEQRES  10 A  311  TYR LEU GLN ALA ARG ARG PRO PRO GLY LEU GLU TYR SER          
SEQRES  11 A  311  TYR ASN PRO SER HIS ASN PRO GLU GLU GLN LEU SER SER          
SEQRES  12 A  311  LYS ASP LEU VAL SER CYS ALA TYR GLN VAL ALA ARG GLY          
SEQRES  13 A  311  MET GLU TYR LEU ALA SER LYS LYS CYS ILE HIS ARG ASP          
SEQRES  14 A  311  LEU ALA ALA ARG ASN VAL LEU VAL THR GLU ASP ASN VAL          
SEQRES  15 A  311  MET LYS ILE ALA ASP PHE GLY LEU ALA ARG ASP ILE HIS          
SEQRES  16 A  311  HIS ILE ASP TYR TYR LYS LYS THR THR ASN GLY ARG LEU          
SEQRES  17 A  311  PRO VAL LYS TRP MET ALA PRO GLU ALA LEU PHE ASP ARG          
SEQRES  18 A  311  ILE TYR THR HIS GLN SER ASP VAL TRP SER PHE GLY VAL          
SEQRES  19 A  311  LEU LEU TRP GLU ILE PHE THR LEU GLY GLY SER PRO TYR          
SEQRES  20 A  311  PRO GLY VAL PRO VAL GLU GLU LEU PHE LYS LEU LEU LYS          
SEQRES  21 A  311  GLU GLY HIS ARG MET ASP LYS PRO SER ASN CYS THR ASN          
SEQRES  22 A  311  GLU LEU TYR MET MET MET ARG ASP CYS TRP HIS ALA VAL          
SEQRES  23 A  311  PRO SER GLN ARG PRO THR PHE LYS GLN LEU VAL GLU ASP          
SEQRES  24 A  311  LEU ASP ARG ILE VAL ALA LEU THR SER ASN GLN GLU              
SEQRES   1 B  311  GLY ALA MET SER GLY VAL SER GLU TYR GLU LEU PRO GLU          
SEQRES   2 B  311  ASP PRO ARG TRP GLU LEU PRO ARG ASP ARG LEU VAL LEU          
SEQRES   3 B  311  GLY LYS PRO LEU GLY GLU GLY CYS PHE GLY GLN VAL VAL          
SEQRES   4 B  311  LEU ALA GLU ALA ILE GLY LEU ASP LYS ASP LYS PRO ASN          
SEQRES   5 B  311  ARG VAL THR LYS VAL ALA VAL LYS MET LEU LYS SER ASP          
SEQRES   6 B  311  ALA THR GLU LYS ASP LEU SER ASP LEU ILE SER GLU MET          
SEQRES   7 B  311  GLU MET MET LYS MET ILE GLY LYS HIS LYS ASN ILE ILE          
SEQRES   8 B  311  ASN LEU LEU GLY ALA CYS THR GLN ASP GLY PRO LEU TYR          
SEQRES   9 B  311  VAL ILE VAL GLU TYR ALA SER LYS GLY ASN LEU ARG GLU          
SEQRES  10 B  311  TYR LEU GLN ALA ARG ARG PRO PRO GLY LEU GLU TYR SER          
SEQRES  11 B  311  TYR ASN PRO SER HIS ASN PRO GLU GLU GLN LEU SER SER          
SEQRES  12 B  311  LYS ASP LEU VAL SER CYS ALA TYR GLN VAL ALA ARG GLY          
SEQRES  13 B  311  MET GLU TYR LEU ALA SER LYS LYS CYS ILE HIS ARG ASP          
SEQRES  14 B  311  LEU ALA ALA ARG ASN VAL LEU VAL THR GLU ASP ASN VAL          
SEQRES  15 B  311  MET LYS ILE ALA ASP PHE GLY LEU ALA ARG ASP ILE HIS          
SEQRES  16 B  311  HIS ILE ASP TYR TYR LYS LYS THR THR ASN GLY ARG LEU          
SEQRES  17 B  311  PRO VAL LYS TRP MET ALA PRO GLU ALA LEU PHE ASP ARG          
SEQRES  18 B  311  ILE TYR THR HIS GLN SER ASP VAL TRP SER PHE GLY VAL          
SEQRES  19 B  311  LEU LEU TRP GLU ILE PHE THR LEU GLY GLY SER PRO TYR          
SEQRES  20 B  311  PRO GLY VAL PRO VAL GLU GLU LEU PHE LYS LEU LEU LYS          
SEQRES  21 B  311  GLU GLY HIS ARG MET ASP LYS PRO SER ASN CYS THR ASN          
SEQRES  22 B  311  GLU LEU TYR MET MET MET ARG ASP CYS TRP HIS ALA VAL          
SEQRES  23 B  311  PRO SER GLN ARG PRO THR PHE LYS GLN LEU VAL GLU ASP          
SEQRES  24 B  311  LEU ASP ARG ILE VAL ALA LEU THR SER ASN GLN GLU              
HET    TZ0  A 801      31                                                       
HET    SO4  A 802       5                                                       
HET    TZ0  B 801      31                                                       
HETNAM     TZ0 1-[(3S)-3-{4-AMINO-3-[(3,5-DIMETHOXYPHENYL)ETHYNYL]-1H-          
HETNAM   2 TZ0  PYRAZOLO[3,4-D]PYRIMIDIN-1-YL}PYRROLIDIN-1-YL]PROP-2-           
HETNAM   3 TZ0  EN-1-ONE                                                        
HETNAM     SO4 SULFATE ION                                                      
FORMUL   3  TZ0    2(C22 H22 N6 O3)                                             
FORMUL   4  SO4    O4 S 2-                                                      
FORMUL   6  HOH   *48(H2 O)                                                     
HELIX    1 AA1 PRO A  474  ASP A  476  5                                   3    
HELIX    2 AA2 LYS A  523  GLY A  539  1                                  17    
HELIX    3 AA3 ASN A  568  ALA A  575  1                                   8    
HELIX    4 AA4 SER A  596  LYS A  617  1                                  22    
HELIX    5 AA5 ALA A  625  ARG A  627  5                                   3    
HELIX    6 AA6 PRO A  663  MET A  667  5                                   5    
HELIX    7 AA7 ALA A  668  ARG A  675  1                                   8    
HELIX    8 AA8 THR A  678  THR A  695  1                                  18    
HELIX    9 AA9 PRO A  705  GLU A  715  1                                  11    
HELIX   10 AB1 THR A  726  TRP A  737  1                                  12    
HELIX   11 AB2 VAL A  740  ARG A  744  5                                   5    
HELIX   12 AB3 THR A  746  THR A  761  1                                  16    
HELIX   13 AB4 PRO B  474  ASP B  476  5                                   3    
HELIX   14 AB5 THR B  521  GLY B  539  1                                  19    
HELIX   15 AB6 ASN B  568  ALA B  575  1                                   8    
HELIX   16 AB7 SER B  596  LYS B  617  1                                  22    
HELIX   17 AB8 ALA B  625  ARG B  627  5                                   3    
HELIX   18 AB9 PRO B  663  MET B  667  5                                   5    
HELIX   19 AC1 ALA B  668  ASP B  674  1                                   7    
HELIX   20 AC2 THR B  678  THR B  695  1                                  18    
HELIX   21 AC3 PRO B  705  GLU B  715  1                                  11    
HELIX   22 AC4 THR B  726  TRP B  737  1                                  12    
HELIX   23 AC5 VAL B  740  ARG B  744  5                                   5    
HELIX   24 AC6 THR B  746  LEU B  760  1                                  15    
SHEET    1 AA1 5 LEU A 478  PRO A 483  0                                        
SHEET    2 AA1 5 VAL A 492  ILE A 498 -1  O  LEU A 494   N  GLY A 481           
SHEET    3 AA1 5 VAL A 508  LYS A 514 -1  O  THR A 509   N  ALA A 497           
SHEET    4 AA1 5 TYR A 558  GLU A 562 -1  O  VAL A 561   N  ALA A 512           
SHEET    5 AA1 5 LEU A 547  CYS A 551 -1  N  LEU A 548   O  ILE A 560           
SHEET    1 AA2 2 VAL A 629  VAL A 631  0                                        
SHEET    2 AA2 2 MET A 637  ILE A 639 -1  O  LYS A 638   N  LEU A 630           
SHEET    1 AA3 5 LEU B 478  PRO B 483  0                                        
SHEET    2 AA3 5 VAL B 492  ILE B 498 -1  O  GLU B 496   N  VAL B 479           
SHEET    3 AA3 5 VAL B 508  LYS B 514 -1  O  VAL B 511   N  ALA B 495           
SHEET    4 AA3 5 TYR B 558  GLU B 562 -1  O  VAL B 561   N  ALA B 512           
SHEET    5 AA3 5 LEU B 547  CYS B 551 -1  N  LEU B 548   O  ILE B 560           
SHEET    1 AA4 2 VAL B 629  VAL B 631  0                                        
SHEET    2 AA4 2 MET B 637  ILE B 639 -1  O  LYS B 638   N  LEU B 630           
LINK         SG  CYS A 488                 C0V TZ0 A 801     1555   1555  1.80  
SITE     1 AC1 15 LEU A 484  GLY A 485  CYS A 488  PHE A 489                    
SITE     2 AC1 15 VAL A 492  ALA A 512  LYS A 514  GLU A 531                    
SITE     3 AC1 15 MET A 535  ILE A 545  GLU A 562  ALA A 564                    
SITE     4 AC1 15 ALA A 640  ASP A 641  PHE A 642                               
SITE     1 AC2  3 GLY A 539  LYS A 540  LYS A 618                               
SITE     1 AC3  9 LEU B 484  ALA B 512  LYS B 514  GLU B 531                    
SITE     2 AC3  9 MET B 535  GLU B 562  ALA B 564  LEU B 630                    
SITE     3 AC3  9 ASP B 641                                                     
CRYST1  208.919   48.981   65.119  90.00 106.19  90.00 C 1 2 1       8          
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      0.004787  0.000000  0.001389        0.00000                         
SCALE2      0.000000  0.020416  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.015990        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system