GenomeNet

Database: PDB
Entry: 1WKP
LinkDB: 1WKP
Original site: 1WKP 
HEADER    SIGNALING PROTEIN                       01-JUN-04   1WKP              
TITLE     FLOWERING LOCUS T (FT) FROM ARABIDOPSIS THALIANA                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: FLOWERING LOCUS T PROTEIN;                                 
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ARABIDOPSIS THALIANA;                           
SOURCE   3 ORGANISM_COMMON: THALE CRESS;                                        
SOURCE   4 ORGANISM_TAXID: 3702;                                                
SOURCE   5 GENE: FT;                                                            
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);                                
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET-28A                                   
KEYWDS    CIS-PEPTIDE, PEBP, SIGNALING PROTEIN                                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.MILLER,M.J.BANFIELD,V.J.WINTER,R.L.BRADY                            
REVDAT   7   10-NOV-21 1WKP    1       REMARK SEQADV                            
REVDAT   6   13-JUL-11 1WKP    1       VERSN                                    
REVDAT   5   06-OCT-10 1WKP    1       REMARK                                   
REVDAT   4   09-JUN-09 1WKP    1       REVDAT                                   
REVDAT   3   24-FEB-09 1WKP    1       VERSN                                    
REVDAT   2   20-JAN-09 1WKP    1       JRNL                                     
REVDAT   1   28-JUN-05 1WKP    0                                                
JRNL        AUTH   J.H.AHN,D.MILLER,V.J.WINTER,M.J.BANFIELD,J.H.LEE,S.Y.YOO,    
JRNL        AUTH 2 S.R.HENZ,R.L.BRADY,D.WEIGEL                                  
JRNL        TITL   A DIVERGENT EXTERNAL LOOP CONFERS ANTAGONISTIC ACTIVITY ON   
JRNL        TITL 2 FLORAL REGULATORS FT AND TFL1.                               
JRNL        REF    EMBO J.                       V.  25   605 2006              
JRNL        REFN                   ISSN 0261-4189                               
JRNL        PMID   16424903                                                     
JRNL        DOI    10.1038/SJ.EMBOJ.7600950                                     
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.1.24                                        
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) : 2.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 93.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 20788                          
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) : 0.184                           
REMARK   3   R VALUE            (WORKING SET) : 0.181                           
REMARK   3   FREE R VALUE                     : 0.226                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1104                            
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) : 2.60                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.67                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1043                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2240                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 55                           
REMARK   3   BIN FREE R VALUE                    : 0.2910                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5202                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 15                                      
REMARK   3   SOLVENT ATOMS            : 195                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 22.07                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.72000                                             
REMARK   3    B22 (A**2) : 0.30000                                              
REMARK   3    B33 (A**2) : -0.49000                                             
REMARK   3    B12 (A**2) : -1.01000                                             
REMARK   3    B13 (A**2) : -0.87000                                             
REMARK   3    B23 (A**2) : 4.13000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.312         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): NULL          
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL          
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.937                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.908                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  5350 ; 0.012 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  7318 ; 1.400 ; 1.944       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   645 ; 4.901 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   813 ; 0.095 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4208 ; 0.005 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  2074 ; 0.198 ; 0.200       
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):   279 ; 0.144 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    58 ; 0.228 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     7 ; 0.305 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  3249 ; 0.438 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  5328 ; 0.840 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2101 ; 1.265 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1990 ; 2.115 ; 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 : 6                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : A B C D                         
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 15                              
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A     10       A      12      1                      
REMARK   3           1     B     10       B      12      1                      
REMARK   3           1     C     10       C      12      1                      
REMARK   3           1     D     10       D      12      1                      
REMARK   3           2     A    119       A     123      1                      
REMARK   3           2     B    119       B     123      1                      
REMARK   3           2     C    119       C     123      1                      
REMARK   3           2     D    119       D     123      1                      
REMARK   3           3     A    141       A     164      1                      
REMARK   3           3     B    141       B     164      1                      
REMARK   3           3     C    141       C     164      1                      
REMARK   3           3     D    141       D     164      1                      
REMARK   3           4     A     14       A      20      1                      
REMARK   3           4     B     14       B      20      1                      
REMARK   3           4     C     14       C      20      1                      
REMARK   3           4     D     14       D      20      1                      
REMARK   3           5     A    107       A     109      1                      
REMARK   3           5     B    107       B     109      1                      
REMARK   3           5     C    107       C     109      1                      
REMARK   3           5     D    107       D     109      1                      
REMARK   3           6     A      6       A       9      6                      
REMARK   3           6     B      6       B       9      6                      
REMARK   3           6     C      6       C       9      6                      
REMARK   3           6     D      6       D       9      6                      
REMARK   3           7     A     64       A      78      1                      
REMARK   3           7     B     64       B      78      1                      
REMARK   3           7     C     64       C      78      1                      
REMARK   3           7     D     64       D      78      1                      
REMARK   3           8     A     92       A     102      1                      
REMARK   3           8     B     92       B     102      1                      
REMARK   3           8     C     92       C     102      1                      
REMARK   3           8     D     92       D     102      1                      
REMARK   3           9     A    165       A     167      6                      
REMARK   3           9     B    165       B     167      6                      
REMARK   3           9     C    165       C     167      6                      
REMARK   3           9     D    165       D     167      6                      
REMARK   3          10     A     45       A      61      1                      
REMARK   3          10     B     45       B      61      1                      
REMARK   3          10     C     45       C      61      1                      
REMARK   3          10     D     45       D      61      1                      
REMARK   3          11     A     27       A      43      1                      
REMARK   3          11     B     27       B      43      1                      
REMARK   3          11     C     27       C      43      1                      
REMARK   3          11     D     27       D      43      1                      
REMARK   3          12     A     80       A      82      1                      
REMARK   3          12     B     80       B      82      1                      
REMARK   3          12     C     80       C      82      1                      
REMARK   3          12     D     80       D      82      1                      
REMARK   3          13     A     84       A      90      1                      
REMARK   3          13     B     84       B      90      1                      
REMARK   3          13     C     84       C      90      1                      
REMARK   3          13     D     84       D      90      1                      
REMARK   3          14     A     12       A      14      3                      
REMARK   3          14     B     12       B      14      3                      
REMARK   3          14     C     12       C      14      3                      
REMARK   3          14     D     12       D      14      3                      
REMARK   3          15     A     23       A      25      1                      
REMARK   3          15     B     23       B      25      1                      
REMARK   3          15     C     23       C      25      1                      
REMARK   3          15     D     23       D      25      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   1    A    (A):    920 ;  0.08 ;  0.05           
REMARK   3   TIGHT POSITIONAL   1    B    (A):    920 ;  0.09 ;  0.05           
REMARK   3   TIGHT POSITIONAL   1    C    (A):    920 ;  0.09 ;  0.05           
REMARK   3   TIGHT POSITIONAL   1    D    (A):    920 ;  0.09 ;  0.05           
REMARK   3   LOOSE POSITIONAL   1    A    (A):     69 ;  0.70 ;  5.00           
REMARK   3   LOOSE POSITIONAL   1    B    (A):     69 ;  0.95 ;  5.00           
REMARK   3   LOOSE POSITIONAL   1    C    (A):     69 ;  0.72 ;  5.00           
REMARK   3   LOOSE POSITIONAL   1    D    (A):     69 ;  0.80 ;  5.00           
REMARK   3   TIGHT THERMAL      1    A (A**2):    920 ;  0.08 ;  0.50           
REMARK   3   TIGHT THERMAL      1    B (A**2):    920 ;  0.08 ;  0.50           
REMARK   3   TIGHT THERMAL      1    C (A**2):    920 ;  0.08 ;  0.50           
REMARK   3   TIGHT THERMAL      1    D (A**2):    920 ;  0.09 ;  0.50           
REMARK   3   LOOSE THERMAL      1    A (A**2):     69 ;  2.58 ; 10.00           
REMARK   3   LOOSE THERMAL      1    B (A**2):     69 ;  2.65 ; 10.00           
REMARK   3   LOOSE THERMAL      1    C (A**2):     69 ;  2.00 ; 10.00           
REMARK   3   LOOSE THERMAL      1    D (A**2):     69 ;  3.04 ; 10.00           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 2                                  
REMARK   3     CHAIN NAMES                    : A B                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 5                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A    125       A     129      1                      
REMARK   3           1     B    125       B     129      1                      
REMARK   3           2     A     83       A      83      1                      
REMARK   3           2     B     83       B      83      1                      
REMARK   3           3     A    103       A     106      1                      
REMARK   3           3     B    103       B     106      1                      
REMARK   3           4     A    131       A     137      1                      
REMARK   3           4     B    131       B     137      1                      
REMARK   3           5     A    130       A     130      5                      
REMARK   3           5     B    130       B     130      5                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   2    A    (A):    137 ;  0.03 ;  0.05           
REMARK   3   MEDIUM POSITIONAL  2    A    (A):      4 ;  0.09 ;  0.50           
REMARK   3   LOOSE POSITIONAL   2    A    (A):      7 ;  0.60 ;  5.00           
REMARK   3   TIGHT THERMAL      2    A (A**2):    137 ;  0.08 ;  0.50           
REMARK   3   MEDIUM THERMAL     2    A (A**2):      4 ;  0.28 ;  2.00           
REMARK   3   LOOSE THERMAL      2    A (A**2):      7 ;  3.16 ; 10.00           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 3                                  
REMARK   3     CHAIN NAMES                    : C D                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 4                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     C    125       C     137      1                      
REMARK   3           1     D    125       D     137      1                      
REMARK   3           2     C    139       C     140      1                      
REMARK   3           2     D    139       D     140      1                      
REMARK   3           3     C     83       C      83      1                      
REMARK   3           3     D     83       D      83      1                      
REMARK   3           4     C    103       C     105      2                      
REMARK   3           4     D    103       D     105      2                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   3    C    (A):    148 ;  0.19 ;  0.05           
REMARK   3   MEDIUM POSITIONAL  3    C    (A):     13 ;  0.10 ;  0.50           
REMARK   3   TIGHT THERMAL      3    C (A**2):    148 ;  0.07 ;  0.50           
REMARK   3   MEDIUM THERMAL     3    C (A**2):     13 ;  0.50 ;  2.00           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 4                                  
REMARK   3     CHAIN NAMES                    : A C D                           
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A    111       A     116      5                      
REMARK   3           1     C    111       C     116      5                      
REMARK   3           1     D    111       D     116      5                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  4    A    (A):     24 ;  0.16 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  4    C    (A):     24 ;  0.18 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  4    D    (A):     24 ;  0.06 ;  0.50           
REMARK   3   LOOSE POSITIONAL   4    A    (A):     12 ;  0.59 ;  5.00           
REMARK   3   LOOSE POSITIONAL   4    C    (A):     12 ;  0.55 ;  5.00           
REMARK   3   LOOSE POSITIONAL   4    D    (A):     12 ;  0.40 ;  5.00           
REMARK   3   MEDIUM THERMAL     4    A (A**2):     24 ;  0.70 ;  2.00           
REMARK   3   MEDIUM THERMAL     4    C (A**2):     24 ;  0.39 ;  2.00           
REMARK   3   MEDIUM THERMAL     4    D (A**2):     24 ;  0.63 ;  2.00           
REMARK   3   LOOSE THERMAL      4    A (A**2):     12 ;  0.74 ; 10.00           
REMARK   3   LOOSE THERMAL      4    C (A**2):     12 ;  0.39 ; 10.00           
REMARK   3   LOOSE THERMAL      4    D (A**2):     12 ;  0.73 ; 10.00           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 5                                  
REMARK   3     CHAIN NAMES                    : A B                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 2                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A     20       A      22      4                      
REMARK   3           1     B     20       B      22      4                      
REMARK   3           2     A     23       A      27      1                      
REMARK   3           2     B     23       B      27      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   5    A    (A):     40 ;  0.02 ;  0.05           
REMARK   3   MEDIUM POSITIONAL  5    A    (A):     26 ;  0.10 ;  0.50           
REMARK   3   TIGHT THERMAL      5    A (A**2):     40 ;  0.04 ;  0.50           
REMARK   3   MEDIUM THERMAL     5    A (A**2):     26 ;  0.14 ;  2.00           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 6                                  
REMARK   3     CHAIN NAMES                    : C D                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 2                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     C     20       C      22      4                      
REMARK   3           1     D     20       D      22      4                      
REMARK   3           2     C     23       C      27      1                      
REMARK   3           2     D     23       D      27      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   6    C    (A):     40 ;  0.02 ;  0.05           
REMARK   3   MEDIUM POSITIONAL  6    C    (A):     26 ;  0.04 ;  0.50           
REMARK   3   TIGHT THERMAL      6    C (A**2):     40 ;  0.05 ;  0.50           
REMARK   3   MEDIUM THERMAL     6    C (A**2):     26 ;  0.32 ;  2.00           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 4                                          
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     6        A   167                          
REMARK   3    ORIGIN FOR THE GROUP (A):  74.4977  10.8268  62.5845              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0387 T22:   0.0752                                     
REMARK   3      T33:   0.0206 T12:  -0.0082                                     
REMARK   3      T13:   0.0001 T23:  -0.0011                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.3031 L22:   4.5032                                     
REMARK   3      L33:   3.0139 L12:   0.2030                                     
REMARK   3      L13:   0.2261 L23:  -0.0831                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0288 S12:  -0.0556 S13:   0.0374                       
REMARK   3      S21:   0.1161 S22:  -0.0989 S23:  -0.1668                       
REMARK   3      S31:   0.0093 S32:   0.0659 S33:   0.0701                       
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 :   B     6        B   167                          
REMARK   3    ORIGIN FOR THE GROUP (A):  37.2278  38.4376  34.2762              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0437 T22:   0.0268                                     
REMARK   3      T33:   0.0549 T12:   0.0038                                     
REMARK   3      T13:  -0.0005 T23:   0.0130                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.5304 L22:   2.8529                                     
REMARK   3      L33:   3.8291 L12:   0.2617                                     
REMARK   3      L13:   0.2837 L23:   0.5241                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0077 S12:   0.0718 S13:   0.0602                       
REMARK   3      S21:   0.0559 S22:  -0.0145 S23:   0.0305                       
REMARK   3      S31:   0.0190 S32:  -0.1487 S33:   0.0222                       
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 :   C     6        C   167                          
REMARK   3    ORIGIN FOR THE GROUP (A):  47.7738  56.2162  13.7807              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0644 T22:   0.0463                                     
REMARK   3      T33:   0.0070 T12:   0.0038                                     
REMARK   3      T13:   0.0063 T23:  -0.0073                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.8997 L22:   3.6784                                     
REMARK   3      L33:   3.2149 L12:   0.5384                                     
REMARK   3      L13:   0.0932 L23:  -0.5194                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0153 S12:  -0.1325 S13:   0.1089                       
REMARK   3      S21:   0.0987 S22:   0.0025 S23:   0.0018                       
REMARK   3      S31:  -0.2360 S32:   0.0783 S33:   0.0128                       
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 :   D     6        D   167                          
REMARK   3    ORIGIN FOR THE GROUP (A):  63.9718  25.5440  39.7898              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0480 T22:   0.0226                                     
REMARK   3      T33:   0.0511 T12:   0.0109                                     
REMARK   3      T13:   0.0044 T23:   0.0105                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.4938 L22:   2.7746                                     
REMARK   3      L33:   4.1934 L12:   0.0643                                     
REMARK   3      L13:   0.6462 L23:  -0.4329                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0861 S12:   0.0712 S13:  -0.1606                       
REMARK   3      S21:  -0.1675 S22:  -0.0743 S23:   0.0431                       
REMARK   3      S31:   0.2049 S32:   0.0878 S33:  -0.0118                       
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: NULL                                      
REMARK   4                                                                      
REMARK   4 1WKP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 10-JUN-04.                  
REMARK 100 THE DEPOSITION ID IS D_1000023682.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 07-MAY-03                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.1                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SRS                                
REMARK 200  BEAMLINE                       : PX14.2                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.488                              
REMARK 200  MONOCHROMATOR                  : MIRRORS                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 21870                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 93.2                               
REMARK 200  DATA REDUNDANCY                : 2.200                              
REMARK 200  R MERGE                    (I) : 0.07600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.0500                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.72                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 66.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.17000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.800                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: ARABIDOPSIS THALIANA TERMINAL FLOWER 1 (TFL1)        
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 51.44                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.53                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.14M AMMONIUM SULFATE, 38% W/V PEG      
REMARK 280  5000 MME, 0.1M MES, PH 7.1, VAPOR DIFFUSION, SITTING DROP,          
REMARK 280  TEMPERATURE 291K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,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                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6                                        
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 300 REMARK: MONOMER IS BIOLOGICAL UNIT                                   
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 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 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 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
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: D                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 5                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1870 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 15520 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -18.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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 350                                                                      
REMARK 350 BIOMOLECULE: 6                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2010 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 15740 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -27.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, D                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A    -2                                                      
REMARK 465     SER A    -1                                                      
REMARK 465     HIS A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     SER A     2                                                      
REMARK 465     ILE A     3                                                      
REMARK 465     ASN A     4                                                      
REMARK 465     ILE A     5                                                      
REMARK 465     GLY B    -2                                                      
REMARK 465     SER B    -1                                                      
REMARK 465     HIS B     0                                                      
REMARK 465     MET B     1                                                      
REMARK 465     SER B     2                                                      
REMARK 465     ILE B     3                                                      
REMARK 465     ASN B     4                                                      
REMARK 465     ILE B     5                                                      
REMARK 465     SER B   168                                                      
REMARK 465     GLY C    -2                                                      
REMARK 465     SER C    -1                                                      
REMARK 465     HIS C     0                                                      
REMARK 465     MET C     1                                                      
REMARK 465     SER C     2                                                      
REMARK 465     ILE C     3                                                      
REMARK 465     ASN C     4                                                      
REMARK 465     ILE C     5                                                      
REMARK 465     SER C   168                                                      
REMARK 465     GLY D    -2                                                      
REMARK 465     SER D    -1                                                      
REMARK 465     HIS D     0                                                      
REMARK 465     MET D     1                                                      
REMARK 465     SER D     2                                                      
REMARK 465     ILE D     3                                                      
REMARK 465     ASN D     4                                                      
REMARK 465     ILE D     5                                                      
REMARK 465     SER D   168                                                      
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     ARG A   6    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     SER A 168    O                                                   
REMARK 470     ARG B   6    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG C   6    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG D   6    CG   CD   NE   CZ   NH1  NH2                        
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   OG   SER A   107     OD2  ASP C    20     1646     2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    TYR A 162   CG    TYR A 162   CD2    -0.082                       
REMARK 500    TYR A 162   CE1   TYR A 162   CZ     -0.095                       
REMARK 500    TYR A 162   CZ    TYR A 162   CE2    -0.087                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ASP B  73   CB  -  CG  -  OD2 ANGL. DEV. =   5.4 DEGREES          
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    THR A  97     -116.96   -106.25                                   
REMARK 500    THR B  97     -116.36   -106.62                                   
REMARK 500    THR C  97     -119.52   -106.30                                   
REMARK 500    THR D  97     -116.37   -107.49                                   
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 SO4 A 1001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 1002                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1003                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1KN3   RELATED DB: PDB                                   
REMARK 900 MURINE PEBP-2 (PHOSPHATIDYLETHANOLAMINE-BINDING PROTEIN-2)           
REMARK 900 RELATED ID: 1BD9   RELATED DB: PDB                                   
REMARK 900 HUMAN PHOSPATIDYLETHANOLAMINE-BINDING PROTEIN (HPEBP)                
REMARK 900 RELATED ID: 1BEH   RELATED DB: PDB                                   
REMARK 900 HUMAN PEBP IN COMPLEX WITH CACODYLATE                                
REMARK 900 RELATED ID: 1A44   RELATED DB: PDB                                   
REMARK 900 BOVINE PHOSPATIDYLETHANOLAMINE-BINDING PROTEIN (BPEBP)               
REMARK 900 RELATED ID: 1QOU   RELATED DB: PDB                                   
REMARK 900 ANTIRRHINUM CENTRORADIALIS (CEN) PROTEIN                             
REMARK 900 RELATED ID: 1FJJ   RELATED DB: PDB                                   
REMARK 900 E. COLI YBHB PROTEIN                                                 
REMARK 900 RELATED ID: 1FUX   RELATED DB: PDB                                   
REMARK 900 E. COLI YBCL PROTEIN                                                 
REMARK 900 RELATED ID: 1WKO   RELATED DB: PDB                                   
REMARK 900 TERMINAL FLOWER 1 PROTEIN                                            
DBREF  1WKP A    1   168  UNP    Q9SXZ2   FT_ARATH         1    168             
DBREF  1WKP B    1   168  UNP    Q9SXZ2   FT_ARATH         1    168             
DBREF  1WKP C    1   168  UNP    Q9SXZ2   FT_ARATH         1    168             
DBREF  1WKP D    1   168  UNP    Q9SXZ2   FT_ARATH         1    168             
SEQADV 1WKP GLY A   -2  UNP  Q9SXZ2              CLONING ARTIFACT               
SEQADV 1WKP SER A   -1  UNP  Q9SXZ2              CLONING ARTIFACT               
SEQADV 1WKP HIS A    0  UNP  Q9SXZ2              CLONING ARTIFACT               
SEQADV 1WKP ASN A   42  UNP  Q9SXZ2    ASP    42 ENGINEERED MUTATION            
SEQADV 1WKP SER A  107  UNP  Q9SXZ2    CYS   107 ENGINEERED MUTATION            
SEQADV 1WKP SER A  164  UNP  Q9SXZ2    CYS   164 ENGINEERED MUTATION            
SEQADV 1WKP GLY B   -2  UNP  Q9SXZ2              CLONING ARTIFACT               
SEQADV 1WKP SER B   -1  UNP  Q9SXZ2              CLONING ARTIFACT               
SEQADV 1WKP HIS B    0  UNP  Q9SXZ2              CLONING ARTIFACT               
SEQADV 1WKP ASN B   42  UNP  Q9SXZ2    ASP    42 ENGINEERED MUTATION            
SEQADV 1WKP SER B  107  UNP  Q9SXZ2    CYS   107 ENGINEERED MUTATION            
SEQADV 1WKP SER B  164  UNP  Q9SXZ2    CYS   164 ENGINEERED MUTATION            
SEQADV 1WKP GLY C   -2  UNP  Q9SXZ2              CLONING ARTIFACT               
SEQADV 1WKP SER C   -1  UNP  Q9SXZ2              CLONING ARTIFACT               
SEQADV 1WKP HIS C    0  UNP  Q9SXZ2              CLONING ARTIFACT               
SEQADV 1WKP ASN C   42  UNP  Q9SXZ2    ASP    42 ENGINEERED MUTATION            
SEQADV 1WKP SER C  107  UNP  Q9SXZ2    CYS   107 ENGINEERED MUTATION            
SEQADV 1WKP SER C  164  UNP  Q9SXZ2    CYS   164 ENGINEERED MUTATION            
SEQADV 1WKP GLY D   -2  UNP  Q9SXZ2              CLONING ARTIFACT               
SEQADV 1WKP SER D   -1  UNP  Q9SXZ2              CLONING ARTIFACT               
SEQADV 1WKP HIS D    0  UNP  Q9SXZ2              CLONING ARTIFACT               
SEQADV 1WKP ASN D   42  UNP  Q9SXZ2    ASP    42 ENGINEERED MUTATION            
SEQADV 1WKP SER D  107  UNP  Q9SXZ2    CYS   107 ENGINEERED MUTATION            
SEQADV 1WKP SER D  164  UNP  Q9SXZ2    CYS   164 ENGINEERED MUTATION            
SEQRES   1 A  171  GLY SER HIS MET SER ILE ASN ILE ARG ASP PRO LEU ILE          
SEQRES   2 A  171  VAL SER ARG VAL VAL GLY ASP VAL LEU ASP PRO PHE ASN          
SEQRES   3 A  171  ARG SER ILE THR LEU LYS VAL THR TYR GLY GLN ARG GLU          
SEQRES   4 A  171  VAL THR ASN GLY LEU ASN LEU ARG PRO SER GLN VAL GLN          
SEQRES   5 A  171  ASN LYS PRO ARG VAL GLU ILE GLY GLY GLU ASP LEU ARG          
SEQRES   6 A  171  ASN PHE TYR THR LEU VAL MET VAL ASP PRO ASP VAL PRO          
SEQRES   7 A  171  SER PRO SER ASN PRO HIS LEU ARG GLU TYR LEU HIS TRP          
SEQRES   8 A  171  LEU VAL THR ASP ILE PRO ALA THR THR GLY THR THR PHE          
SEQRES   9 A  171  GLY ASN GLU ILE VAL SER TYR GLU ASN PRO SER PRO THR          
SEQRES  10 A  171  ALA GLY ILE HIS ARG VAL VAL PHE ILE LEU PHE ARG GLN          
SEQRES  11 A  171  LEU GLY ARG GLN THR VAL TYR ALA PRO GLY TRP ARG GLN          
SEQRES  12 A  171  ASN PHE ASN THR ARG GLU PHE ALA GLU ILE TYR ASN LEU          
SEQRES  13 A  171  GLY LEU PRO VAL ALA ALA VAL PHE TYR ASN SER GLN ARG          
SEQRES  14 A  171  GLU SER                                                      
SEQRES   1 B  171  GLY SER HIS MET SER ILE ASN ILE ARG ASP PRO LEU ILE          
SEQRES   2 B  171  VAL SER ARG VAL VAL GLY ASP VAL LEU ASP PRO PHE ASN          
SEQRES   3 B  171  ARG SER ILE THR LEU LYS VAL THR TYR GLY GLN ARG GLU          
SEQRES   4 B  171  VAL THR ASN GLY LEU ASN LEU ARG PRO SER GLN VAL GLN          
SEQRES   5 B  171  ASN LYS PRO ARG VAL GLU ILE GLY GLY GLU ASP LEU ARG          
SEQRES   6 B  171  ASN PHE TYR THR LEU VAL MET VAL ASP PRO ASP VAL PRO          
SEQRES   7 B  171  SER PRO SER ASN PRO HIS LEU ARG GLU TYR LEU HIS TRP          
SEQRES   8 B  171  LEU VAL THR ASP ILE PRO ALA THR THR GLY THR THR PHE          
SEQRES   9 B  171  GLY ASN GLU ILE VAL SER TYR GLU ASN PRO SER PRO THR          
SEQRES  10 B  171  ALA GLY ILE HIS ARG VAL VAL PHE ILE LEU PHE ARG GLN          
SEQRES  11 B  171  LEU GLY ARG GLN THR VAL TYR ALA PRO GLY TRP ARG GLN          
SEQRES  12 B  171  ASN PHE ASN THR ARG GLU PHE ALA GLU ILE TYR ASN LEU          
SEQRES  13 B  171  GLY LEU PRO VAL ALA ALA VAL PHE TYR ASN SER GLN ARG          
SEQRES  14 B  171  GLU SER                                                      
SEQRES   1 C  171  GLY SER HIS MET SER ILE ASN ILE ARG ASP PRO LEU ILE          
SEQRES   2 C  171  VAL SER ARG VAL VAL GLY ASP VAL LEU ASP PRO PHE ASN          
SEQRES   3 C  171  ARG SER ILE THR LEU LYS VAL THR TYR GLY GLN ARG GLU          
SEQRES   4 C  171  VAL THR ASN GLY LEU ASN LEU ARG PRO SER GLN VAL GLN          
SEQRES   5 C  171  ASN LYS PRO ARG VAL GLU ILE GLY GLY GLU ASP LEU ARG          
SEQRES   6 C  171  ASN PHE TYR THR LEU VAL MET VAL ASP PRO ASP VAL PRO          
SEQRES   7 C  171  SER PRO SER ASN PRO HIS LEU ARG GLU TYR LEU HIS TRP          
SEQRES   8 C  171  LEU VAL THR ASP ILE PRO ALA THR THR GLY THR THR PHE          
SEQRES   9 C  171  GLY ASN GLU ILE VAL SER TYR GLU ASN PRO SER PRO THR          
SEQRES  10 C  171  ALA GLY ILE HIS ARG VAL VAL PHE ILE LEU PHE ARG GLN          
SEQRES  11 C  171  LEU GLY ARG GLN THR VAL TYR ALA PRO GLY TRP ARG GLN          
SEQRES  12 C  171  ASN PHE ASN THR ARG GLU PHE ALA GLU ILE TYR ASN LEU          
SEQRES  13 C  171  GLY LEU PRO VAL ALA ALA VAL PHE TYR ASN SER GLN ARG          
SEQRES  14 C  171  GLU SER                                                      
SEQRES   1 D  171  GLY SER HIS MET SER ILE ASN ILE ARG ASP PRO LEU ILE          
SEQRES   2 D  171  VAL SER ARG VAL VAL GLY ASP VAL LEU ASP PRO PHE ASN          
SEQRES   3 D  171  ARG SER ILE THR LEU LYS VAL THR TYR GLY GLN ARG GLU          
SEQRES   4 D  171  VAL THR ASN GLY LEU ASN LEU ARG PRO SER GLN VAL GLN          
SEQRES   5 D  171  ASN LYS PRO ARG VAL GLU ILE GLY GLY GLU ASP LEU ARG          
SEQRES   6 D  171  ASN PHE TYR THR LEU VAL MET VAL ASP PRO ASP VAL PRO          
SEQRES   7 D  171  SER PRO SER ASN PRO HIS LEU ARG GLU TYR LEU HIS TRP          
SEQRES   8 D  171  LEU VAL THR ASP ILE PRO ALA THR THR GLY THR THR PHE          
SEQRES   9 D  171  GLY ASN GLU ILE VAL SER TYR GLU ASN PRO SER PRO THR          
SEQRES  10 D  171  ALA GLY ILE HIS ARG VAL VAL PHE ILE LEU PHE ARG GLN          
SEQRES  11 D  171  LEU GLY ARG GLN THR VAL TYR ALA PRO GLY TRP ARG GLN          
SEQRES  12 D  171  ASN PHE ASN THR ARG GLU PHE ALA GLU ILE TYR ASN LEU          
SEQRES  13 D  171  GLY LEU PRO VAL ALA ALA VAL PHE TYR ASN SER GLN ARG          
SEQRES  14 D  171  GLU SER                                                      
HET    SO4  A1001       5                                                       
HET    SO4  A1003       5                                                       
HET    SO4  B1002       5                                                       
HETNAM     SO4 SULFATE ION                                                      
FORMUL   5  SO4    3(O4 S 2-)                                                   
FORMUL   8  HOH   *195(H2 O)                                                    
HELIX    1   1 ASP A    7  SER A   12  1                                   6    
HELIX    2   2 ARG A   13  VAL A   18  1                                   6    
HELIX    3   3 ARG A   44  VAL A   48  5                                   5    
HELIX    4   4 GLY A   98  GLY A  102  5                                   5    
HELIX    5   5 ASN A  143  TYR A  151  1                                   9    
HELIX    6   6 ASP B    7  SER B   12  1                                   6    
HELIX    7   7 ARG B   13  VAL B   18  1                                   6    
HELIX    8   8 ARG B   44  VAL B   48  5                                   5    
HELIX    9   9 GLY B   98  GLY B  102  5                                   5    
HELIX   10  10 ASN B  143  TYR B  151  1                                   9    
HELIX   11  11 ASP C    7  SER C   12  1                                   6    
HELIX   12  12 ARG C   13  VAL C   18  1                                   6    
HELIX   13  13 GLY C   98  GLY C  102  5                                   5    
HELIX   14  14 ASN C  143  TYR C  151  1                                   9    
HELIX   15  15 ASP D    7  SER D   12  1                                   6    
HELIX   16  16 ARG D   13  VAL D   18  1                                   6    
HELIX   17  17 ARG D   44  VAL D   48  5                                   5    
HELIX   18  18 GLY D   98  GLY D  102  5                                   5    
HELIX   19  19 ASN D  143  TYR D  151  1                                   9    
SHEET    1   A 3 ARG A  35  GLU A  36  0                                        
SHEET    2   A 3 LEU A  28  TYR A  32 -1  N  TYR A  32   O  ARG A  35           
SHEET    3   A 3 ARG A  53  ILE A  56 -1  O  ARG A  53   N  THR A  31           
SHEET    1   B 6 LEU A  41  ASN A  42  0                                        
SHEET    2   B 6 ALA A 158  SER A 164  1  O  ASN A 163   N  LEU A  41           
SHEET    3   B 6 HIS A 118  ARG A 126 -1  N  VAL A 120   O  TYR A 162           
SHEET    4   B 6 PHE A  64  ASP A  71 -1  N  VAL A  68   O  ILE A 123           
SHEET    5   B 6 TYR A  85  PRO A  94 -1  O  VAL A  90   N  LEU A  67           
SHEET    6   B 6 ASN A 103  VAL A 106 -1  O  ASN A 103   N  THR A  91           
SHEET    1   C 3 ARG B  35  GLU B  36  0                                        
SHEET    2   C 3 LEU B  28  TYR B  32 -1  N  TYR B  32   O  ARG B  35           
SHEET    3   C 3 ARG B  53  ILE B  56 -1  O  ARG B  53   N  THR B  31           
SHEET    1   D 6 LEU B  41  ASN B  42  0                                        
SHEET    2   D 6 ALA B 158  SER B 164  1  O  ASN B 163   N  LEU B  41           
SHEET    3   D 6 HIS B 118  ARG B 126 -1  N  VAL B 120   O  TYR B 162           
SHEET    4   D 6 PHE B  64  ASP B  71 -1  N  VAL B  68   O  ILE B 123           
SHEET    5   D 6 TYR B  85  PRO B  94 -1  O  ILE B  93   N  TYR B  65           
SHEET    6   D 6 ASN B 103  VAL B 106 -1  O  ASN B 103   N  THR B  91           
SHEET    1   E 3 ARG C  35  GLU C  36  0                                        
SHEET    2   E 3 LEU C  28  TYR C  32 -1  N  TYR C  32   O  ARG C  35           
SHEET    3   E 3 ARG C  53  ILE C  56 -1  O  ARG C  53   N  THR C  31           
SHEET    1   F 6 LEU C  41  LEU C  43  0                                        
SHEET    2   F 6 ALA C 158  SER C 164  1  O  ASN C 163   N  LEU C  41           
SHEET    3   F 6 HIS C 118  ARG C 126 -1  N  VAL C 120   O  TYR C 162           
SHEET    4   F 6 PHE C  64  ASP C  71 -1  N  VAL C  70   O  VAL C 121           
SHEET    5   F 6 TYR C  85  PRO C  94 -1  O  VAL C  90   N  LEU C  67           
SHEET    6   F 6 ASN C 103  VAL C 106 -1  O  ASN C 103   N  THR C  91           
SHEET    1   G 3 ARG D  35  GLU D  36  0                                        
SHEET    2   G 3 LEU D  28  TYR D  32 -1  N  TYR D  32   O  ARG D  35           
SHEET    3   G 3 ARG D  53  ILE D  56 -1  O  ARG D  53   N  THR D  31           
SHEET    1   H 6 LEU D  41  LEU D  43  0                                        
SHEET    2   H 6 ALA D 158  SER D 164  1  O  ASN D 163   N  LEU D  41           
SHEET    3   H 6 HIS D 118  ARG D 126 -1  N  VAL D 120   O  TYR D 162           
SHEET    4   H 6 PHE D  64  ASP D  71 -1  N  VAL D  68   O  ILE D 123           
SHEET    5   H 6 TYR D  85  PRO D  94 -1  O  VAL D  90   N  LEU D  67           
SHEET    6   H 6 ASN D 103  VAL D 106 -1  O  ASN D 103   N  THR D  91           
CISPEP   1 VAL A   74    PRO A   75          0        -3.19                     
CISPEP   2 ARG A   83    GLU A   84          0        -4.02                     
CISPEP   3 VAL B   74    PRO B   75          0        -2.65                     
CISPEP   4 ARG B   83    GLU B   84          0        -1.76                     
CISPEP   5 VAL C   74    PRO C   75          0        -1.27                     
CISPEP   6 ARG C   83    GLU C   84          0        -8.74                     
CISPEP   7 VAL D   74    PRO D   75          0        -0.75                     
CISPEP   8 ARG D   83    GLU D   84          0        -9.13                     
SITE     1 AC1  8 THR A  27  LEU A  28  LYS A  29  THR D  27                    
SITE     2 AC1  8 LEU D  28  LYS D  29  HOH D 170  HOH D 175                    
SITE     1 AC2  8 THR B  27  LEU B  28  LYS B  29  THR C  27                    
SITE     2 AC2  8 LEU C  28  LYS C  29  HOH C 174  HOH C 175                    
SITE     1 AC3  6 ALA A 115  GLY A 116  ARG A 166  THR B 114                    
SITE     2 AC3  6 ALA B 115  ARG B 166                                          
CRYST1   53.973   61.542   66.841  75.15  72.18  70.55 P 1           4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.018528 -0.006544 -0.004902        0.00000                         
SCALE2      0.000000  0.017233 -0.003009        0.00000                         
SCALE3      0.000000  0.000000  0.015952        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system