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Database: PDB
Entry: 2XYN
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HEADER    TRANSFERASE                             18-NOV-10   2XYN              
TITLE     HUMAN ABL2 IN COMPLEX WITH AURORA KINASE INHIBITOR VX-680             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TYROSINE-PROTEIN KINASE ABL2;                              
COMPND   3 CHAIN: A, B, C;                                                      
COMPND   4 FRAGMENT: RESIDUES 243-510;                                          
COMPND   5 SYNONYM: ABELSON MURINE LEUKEMIA VIRAL ONCOGENE HOMOLOG 2, ABELSON-  
COMPND   6 RELATED GENE PROTEIN, TYROSINE-PROTEIN KINASE ARG, ABL2;             
COMPND   7 EC: 2.7.10.2;                                                        
COMPND   8 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;                                  
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 7111;                                       
SOURCE   7 EXPRESSION_SYSTEM_CELL_LINE: HIGH FIVE;                              
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PFB-LIC-BSE                               
KEYWDS    CELL ADHESION, STRUCTURAL GENOMICS CONSORTIUM, SGC, TRANSFERASE       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    E.SALAH,E.UGOCHUKWU,J.M.ELKINS,A.J.BARR,B.SHRESTHA,P.SAVITSKY,        
AUTHOR   2 P.MAHAJAN,J.R.C.MUNIZ,W.W.YUE,A.CHAIKUAD,F.VON DELFT,C.BOUNTRA,      
AUTHOR   3 C.H.ARROWSMITH,J.WEIGELT,A.EDWARDS,S.KNAPP,STRUCTURAL GENOMICS       
AUTHOR   4 CONSORTIUM (SGC)                                                     
REVDAT   7   03-APR-19 2XYN    1       SOURCE                                   
REVDAT   6   30-JAN-19 2XYN    1       REMARK                                   
REVDAT   5   24-JAN-18 2XYN    1       JRNL                                     
REVDAT   4   29-APR-15 2XYN    1       REMARK VERSN                             
REVDAT   3   20-APR-11 2XYN    1       JRNL                                     
REVDAT   2   30-MAR-11 2XYN    1       JRNL                                     
REVDAT   1   01-DEC-10 2XYN    0                                                
SPRSDE     01-DEC-10 2XYN      3NSV                                             
JRNL        AUTH   E.SALAH,E.UGOCHUKWU,A.J.BARR,F.VON DELFT,S.KNAPP,J.M.ELKINS  
JRNL        TITL   CRYSTAL STRUCTURES OF ABL-RELATED GENE (ABL2) IN COMPLEX     
JRNL        TITL 2 WITH IMATINIB, TOZASERTIB (VX-680), AND A TYPE I INHIBITOR   
JRNL        TITL 3 OF THE TRIAZOLE CARBOTHIOAMIDE CLASS.                        
JRNL        REF    J.MED.CHEM.                   V.  54  2359 2011              
JRNL        REFN                   ISSN 0022-2623                               
JRNL        PMID   21417343                                                     
JRNL        DOI    10.1021/JM101506N                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.81 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0110                                      
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) : 2.81                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 147.66                         
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 39462                          
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) : 0.248                           
REMARK   3   R VALUE            (WORKING SET) : 0.246                           
REMARK   3   FREE R VALUE                     : 0.284                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2086                            
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) : 2.81                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.88                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2888                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.97                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.4110                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 152                          
REMARK   3   BIN FREE R VALUE                    : 0.4460                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5838                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 234                                     
REMARK   3   SOLVENT ATOMS            : 13                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 94.26                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.93000                                              
REMARK   3    B22 (A**2) : 1.93000                                              
REMARK   3    B33 (A**2) : -2.89000                                             
REMARK   3    B12 (A**2) : 0.96000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.446         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.319         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.268         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 27.882        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.919                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.886                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  6260 ; 0.011 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  3950 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  8569 ; 1.345 ; 1.987       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  9428 ; 0.966 ; 3.006       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   786 ; 5.301 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   223 ;35.716 ;23.363       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   824 ;15.891 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    23 ;14.323 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   924 ; 0.070 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  7099 ; 0.005 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  1277 ; 0.002 ; 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):  3940 ; 0.390 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  1588 ; 0.105 ; 1.500       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  6222 ; 0.727 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2320 ; 1.163 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2326 ; 1.954 ; 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 : 3                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : A B C                           
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 2                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A    367       A     425      2                      
REMARK   3           1     B    367       B     425      2                      
REMARK   3           1     C    367       C     425      2                      
REMARK   3           2     A    438       A     543      2                      
REMARK   3           2     B    438       B     543      2                      
REMARK   3           2     C    438       C     543      2                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   1    A    (A):    967 ;  0.05 ;  0.05           
REMARK   3   TIGHT POSITIONAL   1    B    (A):    967 ;  0.04 ;  0.05           
REMARK   3   TIGHT POSITIONAL   1    C    (A):    967 ;  0.04 ;  0.05           
REMARK   3   MEDIUM POSITIONAL  1    A    (A):    895 ;  0.05 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  1    B    (A):    895 ;  0.04 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  1    C    (A):    895 ;  0.06 ;  0.50           
REMARK   3   TIGHT THERMAL      1    A (A**2):    967 ;  0.08 ;  0.50           
REMARK   3   TIGHT THERMAL      1    B (A**2):    967 ;  0.08 ;  0.50           
REMARK   3   TIGHT THERMAL      1    C (A**2):    967 ;  0.09 ;  0.50           
REMARK   3   MEDIUM THERMAL     1    A (A**2):    895 ;  0.10 ;  2.00           
REMARK   3   MEDIUM THERMAL     1    B (A**2):    895 ;  0.08 ;  2.00           
REMARK   3   MEDIUM THERMAL     1    C (A**2):    895 ;  0.08 ;  2.00           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 2                                  
REMARK   3     CHAIN NAMES                    : A B C                           
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A    281       A     366      6                      
REMARK   3           1     B    281       B     366      6                      
REMARK   3           1     C    281       C     366      6                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   LOOSE POSITIONAL   2    A    (A):    813 ;  0.43 ;  5.00           
REMARK   3   LOOSE POSITIONAL   2    B    (A):    813 ;  0.55 ;  5.00           
REMARK   3   LOOSE POSITIONAL   2    C    (A):    813 ;  0.52 ;  5.00           
REMARK   3   LOOSE THERMAL      2    A (A**2):    813 ;  1.12 ; 10.00           
REMARK   3   LOOSE THERMAL      2    B (A**2):    813 ;  1.61 ; 10.00           
REMARK   3   LOOSE THERMAL      2    C (A**2):    813 ;  1.51 ; 10.00           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 3                                  
REMARK   3     CHAIN NAMES                    : A B C                           
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A    547       A     547      4                      
REMARK   3           1     B    547       B     547      4                      
REMARK   3           1     C    547       C     547      4                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  3    A    (A):     56 ;  0.16 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  3    B    (A):     56 ;  0.29 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  3    C    (A):     56 ;  0.30 ;  0.50           
REMARK   3   MEDIUM THERMAL     3    A (A**2):     56 ;  0.72 ;  2.00           
REMARK   3   MEDIUM THERMAL     3    B (A**2):     56 ;  1.74 ;  2.00           
REMARK   3   MEDIUM THERMAL     3    C (A**2):     56 ;  2.25 ;  2.00           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 6                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   280        A   366                          
REMARK   3    ORIGIN FOR THE GROUP (A): -50.1277  57.9243 -10.7312              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8533 T22:   1.0845                                     
REMARK   3      T33:   0.5553 T12:  -0.6463                                     
REMARK   3      T13:  -0.1674 T23:  -0.0648                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.2297 L22:   4.8368                                     
REMARK   3      L33:   3.9751 L12:   0.1007                                     
REMARK   3      L13:   0.0540 L23:  -0.7003                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.5310 S12:   1.4727 S13:   0.4108                       
REMARK   3      S21:  -0.5102 S22:   0.3472 S23:  -1.0781                       
REMARK   3      S31:  -0.6235 S32:   1.3334 S33:   0.1839                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   367        A   543                          
REMARK   3    ORIGIN FOR THE GROUP (A): -73.0787  50.2875  -5.2077              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6386 T22:   0.2160                                     
REMARK   3      T33:   0.0363 T12:  -0.1984                                     
REMARK   3      T13:  -0.0301 T23:  -0.0409                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.1243 L22:   2.7784                                     
REMARK   3      L33:   3.4080 L12:   0.0802                                     
REMARK   3      L13:   1.1977 L23:   0.2974                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4553 S12:   0.0421 S13:   0.0731                       
REMARK   3      S21:   0.5171 S22:   0.2196 S23:  -0.1760                       
REMARK   3      S31:  -0.5807 S32:   0.0502 S33:   0.2358                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   280        B   366                          
REMARK   3    ORIGIN FOR THE GROUP (A): -90.1252  -1.9395 -15.7052              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.1388 T22:   0.3677                                     
REMARK   3      T33:   0.3720 T12:  -0.4177                                     
REMARK   3      T13:   0.0236 T23:  -0.0308                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.7581 L22:   9.8304                                     
REMARK   3      L33:   3.5131 L12:  -0.1910                                     
REMARK   3      L13:  -1.6710 L23:   1.1113                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1697 S12:  -0.7612 S13:  -0.3937                       
REMARK   3      S21:   1.9830 S22:  -0.7241 S23:   0.3549                       
REMARK   3      S31:   0.8373 S32:  -0.1470 S33:   0.5544                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   367        B   543                          
REMARK   3    ORIGIN FOR THE GROUP (A): -94.0388  22.6984 -21.3663              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4551 T22:   0.3667                                     
REMARK   3      T33:   0.4010 T12:  -0.1134                                     
REMARK   3      T13:   0.0669 T23:  -0.1719                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9274 L22:   9.6996                                     
REMARK   3      L33:   2.6905 L12:  -0.9516                                     
REMARK   3      L13:  -0.4414 L23:   3.7548                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4291 S12:   0.0131 S13:   0.0899                       
REMARK   3      S21:   0.1401 S22:  -1.0245 S23:   1.0321                       
REMARK   3      S31:   0.0837 S32:  -0.8417 S33:   0.5953                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C   273        C   366                          
REMARK   3    ORIGIN FOR THE GROUP (A): -54.6337  18.4470 -36.6739              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7719 T22:   0.4167                                     
REMARK   3      T33:   1.9446 T12:  -0.2055                                     
REMARK   3      T13:   0.2147 T23:   0.0453                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.5108 L22:   5.5396                                     
REMARK   3      L33:   5.3592 L12:  -1.1070                                     
REMARK   3      L13:   0.4412 L23:  -0.3464                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0907 S12:   0.4825 S13:   0.7228                       
REMARK   3      S21:  -0.5562 S22:   0.2170 S23:  -1.8051                       
REMARK   3      S31:  -0.5123 S32:   0.8308 S33:  -0.1264                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C   367        C   545                          
REMARK   3    ORIGIN FOR THE GROUP (A): -63.8705  15.2661 -14.0184              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9051 T22:   0.2141                                     
REMARK   3      T33:   1.3947 T12:  -0.1079                                     
REMARK   3      T13:  -0.5239 T23:  -0.0239                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.7856 L22:   3.4230                                     
REMARK   3      L33:   3.8626 L12:  -1.3003                                     
REMARK   3      L13:  -0.1224 L23:   1.1285                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0155 S12:  -0.3625 S13:   0.5187                       
REMARK   3      S21:   1.0415 S22:   0.1311 S23:  -1.8911                       
REMARK   3      S31:   0.1470 S32:   0.4661 S33:  -0.1157                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS.ATOM RECORD CONTAINS SUM OF TLS AND RESIDUAL B            
REMARK   3  FACTORS.ANISOU RECORD CONTAINS SUM OF TLS AND RESIDUAL U FACTORS    
REMARK   4                                                                      
REMARK   4 2XYN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 18-NOV-10.                  
REMARK 100 THE DEPOSITION ID IS D_1290046258.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 16-APR-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7                                  
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I03                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9782                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC CCD                           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 41549                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.810                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 41.140                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 7.300                              
REMARK 200  R MERGE                    (I) : 0.10000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.8000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.81                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.96                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 1.02000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.900                              
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 3HMI                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 70.69                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.20                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.8M SODIUM SUCCINATE, PH 7, VAPOUR      
REMARK 280  DIFFUSION, SITTING DROP, TEMPERATURE 277K, VAPOR DIFFUSION,         
REMARK 280  SITTING DROP                                                        
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+1/3                                           
REMARK 290       6555   -X,-X+Y,-Z+2/3                                          
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       67.10067            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       33.55033            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  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        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       33.55033            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       67.10067            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3                                                 
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: 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 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
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: C                                     
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     MET A   255                                                      
REMARK 465     GLY A   256                                                      
REMARK 465     HIS A   257                                                      
REMARK 465     HIS A   258                                                      
REMARK 465     HIS A   259                                                      
REMARK 465     HIS A   260                                                      
REMARK 465     HIS A   261                                                      
REMARK 465     HIS A   262                                                      
REMARK 465     SER A   263                                                      
REMARK 465     SER A   264                                                      
REMARK 465     GLY A   265                                                      
REMARK 465     VAL A   266                                                      
REMARK 465     ASP A   267                                                      
REMARK 465     LEU A   268                                                      
REMARK 465     GLY A   269                                                      
REMARK 465     THR A   270                                                      
REMARK 465     GLU A   271                                                      
REMARK 465     ASN A   272                                                      
REMARK 465     LEU A   273                                                      
REMARK 465     TYR A   274                                                      
REMARK 465     PHE A   275                                                      
REMARK 465     GLN A   276                                                      
REMARK 465     SER A   277                                                      
REMARK 465     MET A   278                                                      
REMARK 465     ASP A   279                                                      
REMARK 465     LYS A   320                                                      
REMARK 465     GLU A   321                                                      
REMARK 465     SER A   546                                                      
REMARK 465     MET B   255                                                      
REMARK 465     GLY B   256                                                      
REMARK 465     HIS B   257                                                      
REMARK 465     HIS B   258                                                      
REMARK 465     HIS B   259                                                      
REMARK 465     HIS B   260                                                      
REMARK 465     HIS B   261                                                      
REMARK 465     HIS B   262                                                      
REMARK 465     SER B   263                                                      
REMARK 465     SER B   264                                                      
REMARK 465     GLY B   265                                                      
REMARK 465     VAL B   266                                                      
REMARK 465     ASP B   267                                                      
REMARK 465     LEU B   268                                                      
REMARK 465     GLY B   269                                                      
REMARK 465     THR B   270                                                      
REMARK 465     GLU B   271                                                      
REMARK 465     ASN B   272                                                      
REMARK 465     LEU B   273                                                      
REMARK 465     TYR B   274                                                      
REMARK 465     PHE B   275                                                      
REMARK 465     GLN B   276                                                      
REMARK 465     SER B   277                                                      
REMARK 465     MET B   278                                                      
REMARK 465     ASP B   279                                                      
REMARK 465     LYS B   320                                                      
REMARK 465     GLU B   321                                                      
REMARK 465     SER B   546                                                      
REMARK 465     MET C   255                                                      
REMARK 465     GLY C   256                                                      
REMARK 465     HIS C   257                                                      
REMARK 465     HIS C   258                                                      
REMARK 465     HIS C   259                                                      
REMARK 465     HIS C   260                                                      
REMARK 465     HIS C   261                                                      
REMARK 465     HIS C   262                                                      
REMARK 465     SER C   263                                                      
REMARK 465     SER C   264                                                      
REMARK 465     GLY C   265                                                      
REMARK 465     VAL C   266                                                      
REMARK 465     ASP C   267                                                      
REMARK 465     LEU C   268                                                      
REMARK 465     GLY C   269                                                      
REMARK 465     THR C   270                                                      
REMARK 465     GLU C   271                                                      
REMARK 465     ASN C   272                                                      
REMARK 465     LEU C   273                                                      
REMARK 465     TYR C   274                                                      
REMARK 465     PHE C   275                                                      
REMARK 465     GLN C   276                                                      
REMARK 465     SER C   277                                                      
REMARK 465     MET C   278                                                      
REMARK 465     ASP C   279                                                      
REMARK 465     LYS C   280                                                      
REMARK 465     GLU C   321                                                      
REMARK 465     ASP C   322                                                      
REMARK 465     ASP C   545                                                      
REMARK 465     SER C   546                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS A 280    CE   NZ                                             
REMARK 470     MET A 283    CG   SD   CE                                        
REMARK 470     GLU A 284    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 291    CG   CD   CE   NZ                                   
REMARK 470     LYS A 293    CD   CE   NZ                                        
REMARK 470     GLN A 298    CD   OE1  NE2                                       
REMARK 470     TYR A 303    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LYS A 308    CG   CD   CE   NZ                                   
REMARK 470     LYS A 309    CG   CD   CE   NZ                                   
REMARK 470     TYR A 310    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LYS A 317    NZ                                                  
REMARK 470     LEU A 319    CD1  CD2                                            
REMARK 470     ASP A 322    CG   OD1  OD2                                       
REMARK 470     THR A 323    OG1  CG2                                            
REMARK 470     MET A 324    CG   SD   CE                                        
REMARK 470     VAL A 326    CG1  CG2                                            
REMARK 470     GLU A 327    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 328    CG   CD   OE1  OE2                                  
REMARK 470     LEU A 330    CD1  CD2                                            
REMARK 470     LYS A 331    CD   CE   NZ                                        
REMARK 470     GLU A 332    OE2                                                 
REMARK 470     LEU A 353    CG   CD1  CD2                                       
REMARK 470     GLU A 354    CG   CD   OE1  OE2                                  
REMARK 470     ILE A 359    CD1                                                 
REMARK 470     VAL A 360    CG1  CG2                                            
REMARK 470     GLU A 379    CD   OE1  OE2                                       
REMARK 470     VAL A 384    CG1  CG2                                            
REMARK 470     LYS A 402    CD   CE   NZ                                        
REMARK 470     LYS A 403    NZ                                                  
REMARK 470     ILE A 406    CD1                                                 
REMARK 470     LYS A 424    NZ                                                  
REMARK 470     MET A 434    CE                                                  
REMARK 470     LYS A 446    CG   CD   CE   NZ                                   
REMARK 470     ILE A 464    CD1                                                 
REMARK 470     GLU A 505    CD   OE1  OE2                                       
REMARK 470     GLU A 516    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 523    CE   NZ                                             
REMARK 470     GLN A 537    CD   OE1  NE2                                       
REMARK 470     HIS A 544    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LYS B 280    CE   NZ                                             
REMARK 470     GLU B 284    CD   OE1  OE2                                       
REMARK 470     HIS B 292    ND1  CD2  CE1  NE2                                  
REMARK 470     LYS B 293    CE   NZ                                             
REMARK 470     LYS B 308    CG   CD   CE   NZ                                   
REMARK 470     LYS B 317    NZ                                                  
REMARK 470     ASP B 322    CG   OD1  OD2                                       
REMARK 470     THR B 323    OG1  CG2                                            
REMARK 470     MET B 324    CG   SD   CE                                        
REMARK 470     GLU B 325    CD   OE1  OE2                                       
REMARK 470     VAL B 326    CG1  CG2                                            
REMARK 470     GLU B 327    OE1  OE2                                            
REMARK 470     GLU B 328    CG   CD   OE1  OE2                                  
REMARK 470     LEU B 330    CG   CD1  CD2                                       
REMARK 470     GLU B 332    CD   OE1  OE2                                       
REMARK 470     LYS B 337    CG   CD   CE   NZ                                   
REMARK 470     GLU B 338    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 340    CG   CD   CE   NZ                                   
REMARK 470     GLU B 354    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 402    CG   CD   CE   NZ                                   
REMARK 470     LYS B 403    CG   CD   CE   NZ                                   
REMARK 470     PHE B 405    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ILE B 406    CD1                                                 
REMARK 470     HIS B 442    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LYS B 446    CG   CD   CE   NZ                                   
REMARK 470     ILE B 449    CD1                                                 
REMARK 470     ILE B 464    CG1  CG2  CD1                                       
REMARK 470     MET B 483    CE                                                  
REMARK 470     LYS B 500    CE   NZ                                             
REMARK 470     GLU B 508    CD   OE1  OE2                                       
REMARK 470     LYS B 513    CG   CD   CE   NZ                                   
REMARK 470     GLU B 516    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 523    CE   NZ                                             
REMARK 470     GLN B 537    CG   CD   OE1  NE2                                  
REMARK 470     GLU C 282    CG   CD   OE1  OE2                                  
REMARK 470     MET C 283    CG   SD   CE                                        
REMARK 470     GLU C 284    CD   OE1  OE2                                       
REMARK 470     ARG C 285    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP C 287    OD1  OD2                                            
REMARK 470     ILE C 288    CG1  CG2  CD1                                       
REMARK 470     THR C 289    OG1  CG2                                            
REMARK 470     LYS C 291    CD   CE   NZ                                        
REMARK 470     LYS C 293    NZ                                                  
REMARK 470     VAL C 304    CG1  CG2                                            
REMARK 470     VAL C 306    CG1  CG2                                            
REMARK 470     LYS C 308    CG   CD   CE   NZ                                   
REMARK 470     LYS C 309    CG   CD   CE   NZ                                   
REMARK 470     TYR C 310    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LEU C 312    CG   CD1  CD2                                       
REMARK 470     VAL C 314    CG1  CG2                                            
REMARK 470     LEU C 319    CG   CD1  CD2                                       
REMARK 470     LYS C 320    CG   CD   CE   NZ                                   
REMARK 470     THR C 323    OG1  CG2                                            
REMARK 470     MET C 324    CG   SD   CE                                        
REMARK 470     GLU C 325    CG   CD   OE1  OE2                                  
REMARK 470     VAL C 326    CG1  CG2                                            
REMARK 470     GLU C 327    CG   CD   OE1  OE2                                  
REMARK 470     GLU C 328    CD   OE1  OE2                                       
REMARK 470     PHE C 329    CD1  CD2  CE1  CE2  CZ                              
REMARK 470     LEU C 330    CG   CD1  CD2                                       
REMARK 470     LYS C 331    CG   CD   CE   NZ                                   
REMARK 470     GLU C 332    CG   CD   OE1  OE2                                  
REMARK 470     VAL C 335    CG1  CG2                                            
REMARK 470     MET C 336    CG   SD   CE                                        
REMARK 470     LYS C 337    CG   CD   CE   NZ                                   
REMARK 470     ILE C 339    CG1  CG2  CD1                                       
REMARK 470     LYS C 340    CE   NZ                                             
REMARK 470     ASN C 343    OD1  ND2                                            
REMARK 470     LEU C 347    CG   CD1  CD2                                       
REMARK 470     LEU C 348    CG   CD1  CD2                                       
REMARK 470     VAL C 350    CG1  CG2                                            
REMARK 470     LEU C 353    CG   CD1  CD2                                       
REMARK 470     GLU C 354    CD   OE1  OE2                                       
REMARK 470     PHE C 357    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ILE C 359    CD1                                                 
REMARK 470     GLU C 375    CG   CD   OE1  OE2                                  
REMARK 470     GLU C 379    CG   CD   OE1  OE2                                  
REMARK 470     GLU C 380    CG   CD   OE1  OE2                                  
REMARK 470     VAL C 381    CG1  CG2                                            
REMARK 470     THR C 382    OG1  CG2                                            
REMARK 470     VAL C 384    CG1  CG2                                            
REMARK 470     LEU C 387    CG   CD1  CD2                                       
REMARK 470     THR C 391    OG1  CG2                                            
REMARK 470     SER C 395    OG                                                  
REMARK 470     MET C 397    CG   SD   CE                                        
REMARK 470     GLU C 398    CG   CD   OE1  OE2                                  
REMARK 470     LYS C 402    CG   CD   CE   NZ                                   
REMARK 470     LYS C 403    CD   CE   NZ                                        
REMARK 470     PHE C 405    CD1  CD2  CE1  CE2  CZ                              
REMARK 470     ILE C 406    CD1                                                 
REMARK 470     ARG C 408    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU C 419    CG   CD   OE1  OE2                                  
REMARK 470     VAL C 422    CG1  CG2                                            
REMARK 470     LYS C 424    NZ                                                  
REMARK 470     LEU C 430    CD1  CD2                                            
REMARK 470     SER C 431    OG                                                  
REMARK 470     ARG C 432    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU C 433    CG   CD1  CD2                                       
REMARK 470     ASP C 437    OD1  OD2                                            
REMARK 470     THR C 440    OG1  CG2                                            
REMARK 470     HIS C 442    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LYS C 446    CG   CD   CE   NZ                                   
REMARK 470     PHE C 447    CD1  CD2  CE1  CE2  CZ                              
REMARK 470     ILE C 464    CG1  CG2  CD1                                       
REMARK 470     LYS C 465    CG   CD   CE   NZ                                   
REMARK 470     SER C 466    OG                                                  
REMARK 470     VAL C 468    CG1  CG2                                            
REMARK 470     PHE C 471    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     VAL C 473    CG1  CG2                                            
REMARK 470     LEU C 475    CD1  CD2                                            
REMARK 470     ILE C 489    CG1  CD1                                            
REMARK 470     ASP C 496    OD1  OD2                                            
REMARK 470     GLU C 499    CG   CD   OE1  OE2                                  
REMARK 470     LYS C 500    CG   CD   CE   NZ                                   
REMARK 470     ARG C 503    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU C 505    OE1  OE2                                            
REMARK 470     GLU C 508    CG   CD   OE1  OE2                                  
REMARK 470     LYS C 513    CG   CD   CE   NZ                                   
REMARK 470     GLU C 516    CG   CD   OE1  OE2                                  
REMARK 470     LYS C 523    CE   NZ                                             
REMARK 470     TRP C 524    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP C 524    CZ3  CH2                                            
REMARK 470     PRO C 530    CG   CD                                             
REMARK 470     SER C 531    OG                                                  
REMARK 470     PHE C 532    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     GLU C 534    CD   OE1  OE2                                       
REMARK 470     THR C 535    OG1  CG2                                            
REMARK 470     GLN C 537    CG   CD   OE1  NE2                                  
REMARK 470     PHE C 539    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     GLU C 540    OE1  OE2                                            
REMARK 470     MET C 542    CG   SD   CE                                        
REMARK 470     PHE C 543    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     HIS C 544    CG   ND1  CD2  CE1  NE2                             
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   NZ   LYS B   450     OG   SER C   492              2.06            
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 291      -65.75    -90.47                                   
REMARK 500    MET A 324       62.36    -53.79                                   
REMARK 500    ASP A 409       45.26   -149.99                                   
REMARK 500    ASP A 427       77.47     61.28                                   
REMARK 500    HIS A 544      -74.57    -85.79                                   
REMARK 500    LYS B 291      -62.42   -100.23                                   
REMARK 500    THR B 352       34.84   -143.12                                   
REMARK 500    ASP B 409       45.62   -153.24                                   
REMARK 500    ASP B 427       76.57     62.00                                   
REMARK 500    PHE B 428       37.01    -98.40                                   
REMARK 500    HIS B 544        1.35    -62.50                                   
REMARK 500    LYS C 291     -116.23    -93.57                                   
REMARK 500    LYS C 340      115.91   -165.28                                   
REMARK 500    ASN C 343       34.46    -99.72                                   
REMARK 500    ASP C 409       45.06   -150.50                                   
REMARK 500    ASP C 427       72.00     57.60                                   
REMARK 500    PHE C 428       30.83    -90.09                                   
REMARK 500    ASN C 460       29.03     48.03                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 600                                                                      
REMARK 600 HETEROGEN                                                            
REMARK 600                                                                      
REMARK 600 CYCLOPROPANECARBOXYLIC ACID                                          
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA A   1  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ILE A 449   O                                                      
REMARK 620 2 THR A 452   O    88.7                                              
REMARK 620 3 HOH A2004   O   108.6 109.6                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA A 549  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A2006   O                                                      
REMARK 620 2 ARG A 519   O   119.3                                              
REMARK 620 N                    1                                               
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 1                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE VX6 A 547                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 548                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 549                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE VX6 B 547                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE VX6 B 548                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE VX6 B 549                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE VX6 C 547                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE VX6 C 548                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE VX6 C 549                 
DBREF  2XYN A  279   546  UNP    P42684   ABL2_HUMAN     243    510             
DBREF  2XYN B  279   546  UNP    P42684   ABL2_HUMAN     243    510             
DBREF  2XYN C  279   546  UNP    P42684   ABL2_HUMAN     243    510             
SEQADV 2XYN MET A  255  UNP  P42684              EXPRESSION TAG                 
SEQADV 2XYN GLY A  256  UNP  P42684              EXPRESSION TAG                 
SEQADV 2XYN HIS A  257  UNP  P42684              EXPRESSION TAG                 
SEQADV 2XYN HIS A  258  UNP  P42684              EXPRESSION TAG                 
SEQADV 2XYN HIS A  259  UNP  P42684              EXPRESSION TAG                 
SEQADV 2XYN HIS A  260  UNP  P42684              EXPRESSION TAG                 
SEQADV 2XYN HIS A  261  UNP  P42684              EXPRESSION TAG                 
SEQADV 2XYN HIS A  262  UNP  P42684              EXPRESSION TAG                 
SEQADV 2XYN SER A  263  UNP  P42684              EXPRESSION TAG                 
SEQADV 2XYN SER A  264  UNP  P42684              EXPRESSION TAG                 
SEQADV 2XYN GLY A  265  UNP  P42684              EXPRESSION TAG                 
SEQADV 2XYN VAL A  266  UNP  P42684              EXPRESSION TAG                 
SEQADV 2XYN ASP A  267  UNP  P42684              EXPRESSION TAG                 
SEQADV 2XYN LEU A  268  UNP  P42684              EXPRESSION TAG                 
SEQADV 2XYN GLY A  269  UNP  P42684              EXPRESSION TAG                 
SEQADV 2XYN THR A  270  UNP  P42684              EXPRESSION TAG                 
SEQADV 2XYN GLU A  271  UNP  P42684              EXPRESSION TAG                 
SEQADV 2XYN ASN A  272  UNP  P42684              EXPRESSION TAG                 
SEQADV 2XYN LEU A  273  UNP  P42684              EXPRESSION TAG                 
SEQADV 2XYN TYR A  274  UNP  P42684              EXPRESSION TAG                 
SEQADV 2XYN PHE A  275  UNP  P42684              EXPRESSION TAG                 
SEQADV 2XYN GLN A  276  UNP  P42684              EXPRESSION TAG                 
SEQADV 2XYN SER A  277  UNP  P42684              EXPRESSION TAG                 
SEQADV 2XYN MET A  278  UNP  P42684              EXPRESSION TAG                 
SEQADV 2XYN MET B  255  UNP  P42684              EXPRESSION TAG                 
SEQADV 2XYN GLY B  256  UNP  P42684              EXPRESSION TAG                 
SEQADV 2XYN HIS B  257  UNP  P42684              EXPRESSION TAG                 
SEQADV 2XYN HIS B  258  UNP  P42684              EXPRESSION TAG                 
SEQADV 2XYN HIS B  259  UNP  P42684              EXPRESSION TAG                 
SEQADV 2XYN HIS B  260  UNP  P42684              EXPRESSION TAG                 
SEQADV 2XYN HIS B  261  UNP  P42684              EXPRESSION TAG                 
SEQADV 2XYN HIS B  262  UNP  P42684              EXPRESSION TAG                 
SEQADV 2XYN SER B  263  UNP  P42684              EXPRESSION TAG                 
SEQADV 2XYN SER B  264  UNP  P42684              EXPRESSION TAG                 
SEQADV 2XYN GLY B  265  UNP  P42684              EXPRESSION TAG                 
SEQADV 2XYN VAL B  266  UNP  P42684              EXPRESSION TAG                 
SEQADV 2XYN ASP B  267  UNP  P42684              EXPRESSION TAG                 
SEQADV 2XYN LEU B  268  UNP  P42684              EXPRESSION TAG                 
SEQADV 2XYN GLY B  269  UNP  P42684              EXPRESSION TAG                 
SEQADV 2XYN THR B  270  UNP  P42684              EXPRESSION TAG                 
SEQADV 2XYN GLU B  271  UNP  P42684              EXPRESSION TAG                 
SEQADV 2XYN ASN B  272  UNP  P42684              EXPRESSION TAG                 
SEQADV 2XYN LEU B  273  UNP  P42684              EXPRESSION TAG                 
SEQADV 2XYN TYR B  274  UNP  P42684              EXPRESSION TAG                 
SEQADV 2XYN PHE B  275  UNP  P42684              EXPRESSION TAG                 
SEQADV 2XYN GLN B  276  UNP  P42684              EXPRESSION TAG                 
SEQADV 2XYN SER B  277  UNP  P42684              EXPRESSION TAG                 
SEQADV 2XYN MET B  278  UNP  P42684              EXPRESSION TAG                 
SEQADV 2XYN MET C  255  UNP  P42684              EXPRESSION TAG                 
SEQADV 2XYN GLY C  256  UNP  P42684              EXPRESSION TAG                 
SEQADV 2XYN HIS C  257  UNP  P42684              EXPRESSION TAG                 
SEQADV 2XYN HIS C  258  UNP  P42684              EXPRESSION TAG                 
SEQADV 2XYN HIS C  259  UNP  P42684              EXPRESSION TAG                 
SEQADV 2XYN HIS C  260  UNP  P42684              EXPRESSION TAG                 
SEQADV 2XYN HIS C  261  UNP  P42684              EXPRESSION TAG                 
SEQADV 2XYN HIS C  262  UNP  P42684              EXPRESSION TAG                 
SEQADV 2XYN SER C  263  UNP  P42684              EXPRESSION TAG                 
SEQADV 2XYN SER C  264  UNP  P42684              EXPRESSION TAG                 
SEQADV 2XYN GLY C  265  UNP  P42684              EXPRESSION TAG                 
SEQADV 2XYN VAL C  266  UNP  P42684              EXPRESSION TAG                 
SEQADV 2XYN ASP C  267  UNP  P42684              EXPRESSION TAG                 
SEQADV 2XYN LEU C  268  UNP  P42684              EXPRESSION TAG                 
SEQADV 2XYN GLY C  269  UNP  P42684              EXPRESSION TAG                 
SEQADV 2XYN THR C  270  UNP  P42684              EXPRESSION TAG                 
SEQADV 2XYN GLU C  271  UNP  P42684              EXPRESSION TAG                 
SEQADV 2XYN ASN C  272  UNP  P42684              EXPRESSION TAG                 
SEQADV 2XYN LEU C  273  UNP  P42684              EXPRESSION TAG                 
SEQADV 2XYN TYR C  274  UNP  P42684              EXPRESSION TAG                 
SEQADV 2XYN PHE C  275  UNP  P42684              EXPRESSION TAG                 
SEQADV 2XYN GLN C  276  UNP  P42684              EXPRESSION TAG                 
SEQADV 2XYN SER C  277  UNP  P42684              EXPRESSION TAG                 
SEQADV 2XYN MET C  278  UNP  P42684              EXPRESSION TAG                 
SEQRES   1 A  292  MET GLY HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP          
SEQRES   2 A  292  LEU GLY THR GLU ASN LEU TYR PHE GLN SER MET ASP LYS          
SEQRES   3 A  292  TRP GLU MET GLU ARG THR ASP ILE THR MET LYS HIS LYS          
SEQRES   4 A  292  LEU GLY GLY GLY GLN TYR GLY GLU VAL TYR VAL GLY VAL          
SEQRES   5 A  292  TRP LYS LYS TYR SER LEU THR VAL ALA VAL LYS THR LEU          
SEQRES   6 A  292  LYS GLU ASP THR MET GLU VAL GLU GLU PHE LEU LYS GLU          
SEQRES   7 A  292  ALA ALA VAL MET LYS GLU ILE LYS HIS PRO ASN LEU VAL          
SEQRES   8 A  292  GLN LEU LEU GLY VAL CYS THR LEU GLU PRO PRO PHE TYR          
SEQRES   9 A  292  ILE VAL THR GLU TYR MET PRO TYR GLY ASN LEU LEU ASP          
SEQRES  10 A  292  TYR LEU ARG GLU CYS ASN ARG GLU GLU VAL THR ALA VAL          
SEQRES  11 A  292  VAL LEU LEU TYR MET ALA THR GLN ILE SER SER ALA MET          
SEQRES  12 A  292  GLU TYR LEU GLU LYS LYS ASN PHE ILE HIS ARG ASP LEU          
SEQRES  13 A  292  ALA ALA ARG ASN CYS LEU VAL GLY GLU ASN HIS VAL VAL          
SEQRES  14 A  292  LYS VAL ALA ASP PHE GLY LEU SER ARG LEU MET THR GLY          
SEQRES  15 A  292  ASP THR TYR THR ALA HIS ALA GLY ALA LYS PHE PRO ILE          
SEQRES  16 A  292  LYS TRP THR ALA PRO GLU SER LEU ALA TYR ASN THR PHE          
SEQRES  17 A  292  SER ILE LYS SER ASP VAL TRP ALA PHE GLY VAL LEU LEU          
SEQRES  18 A  292  TRP GLU ILE ALA THR TYR GLY MET SER PRO TYR PRO GLY          
SEQRES  19 A  292  ILE ASP LEU SER GLN VAL TYR ASP LEU LEU GLU LYS GLY          
SEQRES  20 A  292  TYR ARG MET GLU GLN PRO GLU GLY CYS PRO PRO LYS VAL          
SEQRES  21 A  292  TYR GLU LEU MET ARG ALA CYS TRP LYS TRP SER PRO ALA          
SEQRES  22 A  292  ASP ARG PRO SER PHE ALA GLU THR HIS GLN ALA PHE GLU          
SEQRES  23 A  292  THR MET PHE HIS ASP SER                                      
SEQRES   1 B  292  MET GLY HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP          
SEQRES   2 B  292  LEU GLY THR GLU ASN LEU TYR PHE GLN SER MET ASP LYS          
SEQRES   3 B  292  TRP GLU MET GLU ARG THR ASP ILE THR MET LYS HIS LYS          
SEQRES   4 B  292  LEU GLY GLY GLY GLN TYR GLY GLU VAL TYR VAL GLY VAL          
SEQRES   5 B  292  TRP LYS LYS TYR SER LEU THR VAL ALA VAL LYS THR LEU          
SEQRES   6 B  292  LYS GLU ASP THR MET GLU VAL GLU GLU PHE LEU LYS GLU          
SEQRES   7 B  292  ALA ALA VAL MET LYS GLU ILE LYS HIS PRO ASN LEU VAL          
SEQRES   8 B  292  GLN LEU LEU GLY VAL CYS THR LEU GLU PRO PRO PHE TYR          
SEQRES   9 B  292  ILE VAL THR GLU TYR MET PRO TYR GLY ASN LEU LEU ASP          
SEQRES  10 B  292  TYR LEU ARG GLU CYS ASN ARG GLU GLU VAL THR ALA VAL          
SEQRES  11 B  292  VAL LEU LEU TYR MET ALA THR GLN ILE SER SER ALA MET          
SEQRES  12 B  292  GLU TYR LEU GLU LYS LYS ASN PHE ILE HIS ARG ASP LEU          
SEQRES  13 B  292  ALA ALA ARG ASN CYS LEU VAL GLY GLU ASN HIS VAL VAL          
SEQRES  14 B  292  LYS VAL ALA ASP PHE GLY LEU SER ARG LEU MET THR GLY          
SEQRES  15 B  292  ASP THR TYR THR ALA HIS ALA GLY ALA LYS PHE PRO ILE          
SEQRES  16 B  292  LYS TRP THR ALA PRO GLU SER LEU ALA TYR ASN THR PHE          
SEQRES  17 B  292  SER ILE LYS SER ASP VAL TRP ALA PHE GLY VAL LEU LEU          
SEQRES  18 B  292  TRP GLU ILE ALA THR TYR GLY MET SER PRO TYR PRO GLY          
SEQRES  19 B  292  ILE ASP LEU SER GLN VAL TYR ASP LEU LEU GLU LYS GLY          
SEQRES  20 B  292  TYR ARG MET GLU GLN PRO GLU GLY CYS PRO PRO LYS VAL          
SEQRES  21 B  292  TYR GLU LEU MET ARG ALA CYS TRP LYS TRP SER PRO ALA          
SEQRES  22 B  292  ASP ARG PRO SER PHE ALA GLU THR HIS GLN ALA PHE GLU          
SEQRES  23 B  292  THR MET PHE HIS ASP SER                                      
SEQRES   1 C  292  MET GLY HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP          
SEQRES   2 C  292  LEU GLY THR GLU ASN LEU TYR PHE GLN SER MET ASP LYS          
SEQRES   3 C  292  TRP GLU MET GLU ARG THR ASP ILE THR MET LYS HIS LYS          
SEQRES   4 C  292  LEU GLY GLY GLY GLN TYR GLY GLU VAL TYR VAL GLY VAL          
SEQRES   5 C  292  TRP LYS LYS TYR SER LEU THR VAL ALA VAL LYS THR LEU          
SEQRES   6 C  292  LYS GLU ASP THR MET GLU VAL GLU GLU PHE LEU LYS GLU          
SEQRES   7 C  292  ALA ALA VAL MET LYS GLU ILE LYS HIS PRO ASN LEU VAL          
SEQRES   8 C  292  GLN LEU LEU GLY VAL CYS THR LEU GLU PRO PRO PHE TYR          
SEQRES   9 C  292  ILE VAL THR GLU TYR MET PRO TYR GLY ASN LEU LEU ASP          
SEQRES  10 C  292  TYR LEU ARG GLU CYS ASN ARG GLU GLU VAL THR ALA VAL          
SEQRES  11 C  292  VAL LEU LEU TYR MET ALA THR GLN ILE SER SER ALA MET          
SEQRES  12 C  292  GLU TYR LEU GLU LYS LYS ASN PHE ILE HIS ARG ASP LEU          
SEQRES  13 C  292  ALA ALA ARG ASN CYS LEU VAL GLY GLU ASN HIS VAL VAL          
SEQRES  14 C  292  LYS VAL ALA ASP PHE GLY LEU SER ARG LEU MET THR GLY          
SEQRES  15 C  292  ASP THR TYR THR ALA HIS ALA GLY ALA LYS PHE PRO ILE          
SEQRES  16 C  292  LYS TRP THR ALA PRO GLU SER LEU ALA TYR ASN THR PHE          
SEQRES  17 C  292  SER ILE LYS SER ASP VAL TRP ALA PHE GLY VAL LEU LEU          
SEQRES  18 C  292  TRP GLU ILE ALA THR TYR GLY MET SER PRO TYR PRO GLY          
SEQRES  19 C  292  ILE ASP LEU SER GLN VAL TYR ASP LEU LEU GLU LYS GLY          
SEQRES  20 C  292  TYR ARG MET GLU GLN PRO GLU GLY CYS PRO PRO LYS VAL          
SEQRES  21 C  292  TYR GLU LEU MET ARG ALA CYS TRP LYS TRP SER PRO ALA          
SEQRES  22 C  292  ASP ARG PRO SER PHE ALA GLU THR HIS GLN ALA PHE GLU          
SEQRES  23 C  292  THR MET PHE HIS ASP SER                                      
HET     NA  A   1       1                                                       
HET    VX6  A 547      33                                                       
HET     CL  A 548       1                                                       
HET     NA  A 549       1                                                       
HET    VX6  B 547      33                                                       
HET    VX6  B 548      33                                                       
HET    VX6  B 549      33                                                       
HET    VX6  C 547      33                                                       
HET    VX6  C 548      33                                                       
HET    VX6  C 549      33                                                       
HETNAM      NA SODIUM ION                                                       
HETNAM     VX6 CYCLOPROPANECARBOXYLIC ACID {4-[4-(4-METHYL-PIPERAZIN-           
HETNAM   2 VX6  1-YL)-6-(5-METHYL-2H-PYRAZOL-3-YLAMINO)-PYRIMIDIN-2-            
HETNAM   3 VX6  YLSULFANYL]-PHENYL}-AMIDE                                       
HETNAM      CL CHLORIDE ION                                                     
FORMUL   4   NA    2(NA 1+)                                                     
FORMUL   5  VX6    7(C23 H28 N8 O S)                                            
FORMUL   6   CL    CL 1-                                                        
FORMUL  14  HOH   *13(H2 O)                                                     
HELIX    1   1 GLU A  284  THR A  286  5                                   3    
HELIX    2   2 GLU A  325  GLU A  338  1                                  14    
HELIX    3   3 ASN A  368  CYS A  376  1                                   9    
HELIX    4   4 THR A  382  LYS A  403  1                                  22    
HELIX    5   5 ALA A  411  ARG A  413  5                                   3    
HELIX    6   6 GLU A  419  HIS A  421  5                                   3    
HELIX    7   7 PRO A  448  THR A  452  5                                   5    
HELIX    8   8 ALA A  453  ASN A  460  1                                   8    
HELIX    9   9 SER A  463  THR A  480  1                                  18    
HELIX   10  10 ASP A  490  SER A  492  5                                   3    
HELIX   11  11 GLN A  493  LYS A  500  1                                   8    
HELIX   12  12 PRO A  511  TRP A  522  1                                  12    
HELIX   13  13 SER A  525  ARG A  529  5                                   5    
HELIX   14  14 SER A  531  ASP A  545  1                                  15    
HELIX   15  15 GLY B  296  GLY B  300  5                                   5    
HELIX   16  16 LYS B  309  SER B  311  5                                   3    
HELIX   17  17 GLU B  325  LYS B  337  1                                  13    
HELIX   18  18 LEU B  369  CYS B  376  1                                   8    
HELIX   19  19 THR B  382  LYS B  403  1                                  22    
HELIX   20  20 ALA B  411  ARG B  413  5                                   3    
HELIX   21  21 GLU B  419  HIS B  421  5                                   3    
HELIX   22  22 PRO B  448  THR B  452  5                                   5    
HELIX   23  23 ALA B  453  ASN B  460  1                                   8    
HELIX   24  24 ILE B  464  THR B  480  1                                  17    
HELIX   25  25 ASP B  490  SER B  492  5                                   3    
HELIX   26  26 GLN B  493  LYS B  500  1                                   8    
HELIX   27  27 PRO B  511  TRP B  522  1                                  12    
HELIX   28  28 SER B  525  ARG B  529  5                                   5    
HELIX   29  29 SER B  531  HIS B  544  1                                  14    
HELIX   30  30 GLU C  284  THR C  286  5                                   3    
HELIX   31  31 GLY C  295  GLN C  298  5                                   4    
HELIX   32  32 GLU C  325  ILE C  339  1                                  15    
HELIX   33  33 LEU C  369  CYS C  376  1                                   8    
HELIX   34  34 THR C  382  LYS C  403  1                                  22    
HELIX   35  35 ALA C  411  ARG C  413  5                                   3    
HELIX   36  36 GLU C  419  HIS C  421  5                                   3    
HELIX   37  37 PRO C  448  THR C  452  5                                   5    
HELIX   38  38 ALA C  453  ASN C  460  1                                   8    
HELIX   39  39 SER C  463  THR C  480  1                                  18    
HELIX   40  40 ASP C  490  SER C  492  5                                   3    
HELIX   41  41 GLN C  493  LYS C  500  1                                   8    
HELIX   42  42 PRO C  511  TRP C  522  1                                  12    
HELIX   43  43 SER C  525  ARG C  529  5                                   5    
HELIX   44  44 SER C  531  HIS C  544  1                                  14    
SHEET    1  AA 5 ILE A 288  LYS A 293  0                                        
SHEET    2  AA 5 GLU A 301  TRP A 307 -1  O  VAL A 304   N  LYS A 291           
SHEET    3  AA 5 LEU A 312  THR A 318 -1  O  LEU A 312   N  TRP A 307           
SHEET    4  AA 5 TYR A 358  GLU A 362 -1  O  ILE A 359   N  LYS A 317           
SHEET    5  AA 5 LEU A 347  CYS A 351 -1  N  LEU A 348   O  VAL A 360           
SHEET    1  AB 2 PHE A 405  ILE A 406  0                                        
SHEET    2  AB 2 ARG A 432  LEU A 433 -1  O  ARG A 432   N  ILE A 406           
SHEET    1  AC 2 CYS A 415  VAL A 417  0                                        
SHEET    2  AC 2 VAL A 423  VAL A 425 -1  O  LYS A 424   N  LEU A 416           
SHEET    1  AD 2 TYR A 439  THR A 440  0                                        
SHEET    2  AD 2 THR A 461  PHE A 462 -1  O  PHE A 462   N  TYR A 439           
SHEET    1  BA 5 ILE B 288  LEU B 294  0                                        
SHEET    2  BA 5 VAL B 302  TRP B 307 -1  O  VAL B 302   N  LEU B 294           
SHEET    3  BA 5 LEU B 312  LYS B 317 -1  O  LEU B 312   N  TRP B 307           
SHEET    4  BA 5 TYR B 358  GLU B 362 -1  O  ILE B 359   N  LYS B 317           
SHEET    5  BA 5 LEU B 347  CYS B 351 -1  N  LEU B 348   O  VAL B 360           
SHEET    1  BB 3 GLY B 367  ASN B 368  0                                        
SHEET    2  BB 3 CYS B 415  VAL B 417 -1  N  VAL B 417   O  GLY B 367           
SHEET    3  BB 3 VAL B 423  VAL B 425 -1  O  LYS B 424   N  LEU B 416           
SHEET    1  BC 2 PHE B 405  ILE B 406  0                                        
SHEET    2  BC 2 ARG B 432  LEU B 433 -1  O  ARG B 432   N  ILE B 406           
SHEET    1  BD 2 THR B 438  THR B 440  0                                        
SHEET    2  BD 2 THR B 461  SER B 463 -1  O  PHE B 462   N  TYR B 439           
SHEET    1  CA 5 ILE C 288  LEU C 294  0                                        
SHEET    2  CA 5 GLU C 301  TRP C 307 -1  O  VAL C 302   N  LEU C 294           
SHEET    3  CA 5 LEU C 312  THR C 318 -1  O  LEU C 312   N  TRP C 307           
SHEET    4  CA 5 TYR C 358  GLU C 362 -1  O  ILE C 359   N  LYS C 317           
SHEET    5  CA 5 LEU C 347  CYS C 351 -1  N  LEU C 348   O  VAL C 360           
SHEET    1  CB 3 GLY C 367  ASN C 368  0                                        
SHEET    2  CB 3 CYS C 415  VAL C 417 -1  N  VAL C 417   O  GLY C 367           
SHEET    3  CB 3 VAL C 423  VAL C 425 -1  O  LYS C 424   N  LEU C 416           
SHEET    1  CC 2 PHE C 405  ILE C 406  0                                        
SHEET    2  CC 2 ARG C 432  LEU C 433 -1  O  ARG C 432   N  ILE C 406           
SHEET    1  CD 2 TYR C 439  THR C 440  0                                        
SHEET    2  CD 2 THR C 461  PHE C 462 -1  O  PHE C 462   N  TYR C 439           
LINK        NA    NA A   1                 O   ILE A 449     1555   1555  2.64  
LINK        NA    NA A   1                 O   THR A 452     1555   1555  2.63  
LINK        NA    NA A   1                 O   HOH A2004     1555   1555  2.72  
LINK        NA    NA A 549                 O   HOH A2006     1555   1555  2.47  
LINK        NA    NA A 549                 O   ARG A 519     1555   1555  2.86  
CISPEP   1 PRO A  355    PRO A  356          0        -0.76                     
CISPEP   2 PRO B  355    PRO B  356          0        -2.36                     
CISPEP   3 PRO C  355    PRO C  356          0        -3.50                     
SITE     1 AC1  4 ILE A 449  THR A 452  LEU A 498  HOH A2004                    
SITE     1 AC2 12 TYR A 299  VAL A 302  ALA A 315  LYS A 317                    
SITE     2 AC2 12 THR A 361  GLU A 362  TYR A 363  MET A 364                    
SITE     3 AC2 12 PRO A 365  GLY A 367  LEU A 416  ASP A 427                    
SITE     1 AC3  6 LEU A 294  GLY A 295  GLY A 297  GLN A 298                    
SITE     2 AC3  6 TYR A 299  GLY A 300                                          
SITE     1 AC4  4 ARG A 503  ARG A 519  TRP A 522  HOH A2006                    
SITE     1 AC5 11 LEU B 294  TYR B 299  THR B 361  GLU B 362                    
SITE     2 AC5 11 TYR B 363  MET B 364  PRO B 365  GLY B 367                    
SITE     3 AC5 11 LEU B 416  ASP B 427  ARG C 374                               
SITE     1 AC6 11 LYS A 280  TRP A 281  TRP A 307  TYR A 310                    
SITE     2 AC6 11 LEU A 312  LEU A 348  THR B 352  LEU B 353                    
SITE     3 AC6 11 GLU B 354  PRO B 355  PHE B 357                               
SITE     1 AC7  9 ASP B 437  THR B 438  TYR B 459  THR B 461                    
SITE     2 AC7  9 SER B 463  LYS B 465  ALA B 527  HOH B2007                    
SITE     3 AC7  9 VX6 C 548                                                     
SITE     1 AC8 13 LEU C 294  TYR C 299  VAL C 302  ALA C 315                    
SITE     2 AC8 13 THR C 361  GLU C 362  TYR C 363  MET C 364                    
SITE     3 AC8 13 PRO C 365  TYR C 366  GLY C 367  LEU C 416                    
SITE     4 AC8 13 ASP C 427                                                     
SITE     1 AC9  6 SER B 525  VX6 B 549  THR C 352  LEU C 353                    
SITE     2 AC9  6 GLU C 354  PRO C 355                                          
SITE     1 BC1  7 MET B 483  ALA C 445  LYS C 446  PHE C 447                    
SITE     2 BC1  7 ILE C 449  SER C 492  TYR C 495                               
CRYST1  170.500  170.500  100.651  90.00  90.00 120.00 P 32 2 1     18          
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      0.005865  0.003386  0.000000        0.00000                         
SCALE2      0.000000  0.006772  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009935        0.00000                         
MTRIX1   1  0.445430 -0.893760 -0.052820      -17.04952    1                    
MTRIX2   1 -0.895160 -0.445690 -0.007380      -20.43198    1                    
MTRIX3   1 -0.016940  0.050570 -0.998580      -30.23569    1                    
MTRIX1   2  0.236630  0.859110  0.453800      -86.93401    1                    
MTRIX2   2 -0.211440  0.501400 -0.838980      -29.52684    1                    
MTRIX3   2 -0.948320  0.102580  0.300290      -86.71567    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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