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Database: PDB
Entry: 4AQ3
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Original site: 4AQ3 
HEADER    APOPTOSIS                               12-APR-12   4AQ3              
TITLE     HUMAN BCL-2 WITH PHENYLACYLSULFONAMIDE INHIBITOR                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: APOPTOSIS REGULATOR BCL-2, BCL-2-LIKE PROTEIN 1;           
COMPND   3 CHAIN: A, B, C, D, E, F;                                             
COMPND   4 FRAGMENT: RESIDUES 1-33 AND 92-207 OF P10415 AND RESIDUES 29-44 OF   
COMPND   5  Q07817;                                                             
COMPND   6 SYNONYM: BCL2-L-1, APOPTOSIS REGULATOR BCL-X;                        
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 OTHER_DETAILS: APOPTOSIS REGULATOR BCL-2 WITH PUTATIVE FLEXIBLE      
COMPND   9  LOOP REPLACED WITH A PORTION OF APOPTOSIS REGULATOR BCL-X PROTEIN   
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    APOPTOSIS, CHIMERA                                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.A.BERTRAND,M.FASOLINI,M.MODUGNO                                     
REVDAT   2   21-NOV-12 4AQ3    1       SEQADV                                   
REVDAT   1   06-JUN-12 4AQ3    0                                                
JRNL        AUTH   H.L.PEREZ,P.BANFI,J.A.BERTRAND,Z.W.CAI,J.W.GREBINSKI,K.KIM,  
JRNL        AUTH 2 J.LIPPY,M.MODUGNO,J.NAGLICH,R.J.SCHMIDT,A.TEBBEN,P.VIANELLO, 
JRNL        AUTH 3 D.D.WEI,L.ZHANG,A.GALVANI,L.J.LOMBARDO,R.M.BORZILLERI        
JRNL        TITL   IDENTIFICATION OF A PHENYLACYLSULFONAMIDE SERIES OF DUAL     
JRNL        TITL 2 BCL-2/BCL-XL ANTAGONISTS.                                    
JRNL        REF    BIOORG.MED.CHEM.LETT.         V.  22  3946 2012              
JRNL        REFN                   ISSN 0960-894X                               
JRNL        PMID   22608961                                                     
JRNL        DOI    10.1016/J.BMCL.2012.04.103                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.6.0117                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 100.00                         
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NONE                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.75                          
REMARK   3   NUMBER OF REFLECTIONS             : 55094                          
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) : 0.20300                         
REMARK   3   R VALUE            (WORKING SET) : 0.20072                         
REMARK   3   FREE R VALUE                     : 0.24494                         
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.0                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 2926                            
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) : 2.400                        
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.462                        
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3637                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 87.19                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.317                        
REMARK   3   BIN FREE R VALUE SET COUNT          : 174                          
REMARK   3   BIN FREE R VALUE                    : 0.409                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6778                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 318                                     
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 57.235                         
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.31                                                 
REMARK   3    B22 (A**2) : 0.31                                                 
REMARK   3    B33 (A**2) : -0.46                                                
REMARK   3    B12 (A**2) : 0.15                                                 
REMARK   3    B13 (A**2) : 0.00                                                 
REMARK   3    B23 (A**2) : 0.00                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.255         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.216         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.161         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 12.963        
REMARK   3                                                                      
REMARK   3  CORRELATION COEFFICIENTS.                                           
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.948                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.925                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  7311 ; 0.013 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  9916 ; 1.884 ; 1.961       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   802 ; 6.870 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   403 ;35.705 ;22.581       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1108 ;19.747 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    72 ;22.373 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   952 ; 0.111 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  5854 ; 0.011 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
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):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED 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 : 1                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : A B C D E F                     
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 2                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A     10       A      30      4                      
REMARK   3           1     B     10       B      30      4                      
REMARK   3           1     C     10       C      30      4                      
REMARK   3           1     D     10       D      30      4                      
REMARK   3           1     E     10       E      30      4                      
REMARK   3           1     F     10       F      30      4                      
REMARK   3           2     A     52       A     157      4                      
REMARK   3           2     B     52       B     157      4                      
REMARK   3           2     C     52       C     157      4                      
REMARK   3           2     D     52       D     157      4                      
REMARK   3           2     E     52       E     157      4                      
REMARK   3           2     F     52       F     157      4                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  1    A    (A):   1059 ;  0.32 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  1    B    (A):   1059 ;  0.27 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  1    C    (A):   1059 ;  0.35 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  1    D    (A):   1059 ;  0.32 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  1    E    (A):   1059 ;  0.34 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  1    F    (A):   1059 ;  0.34 ;  0.50           
REMARK   3   MEDIUM THERMAL     1    A (A**2):   1059 ;  5.65 ;  2.00           
REMARK   3   MEDIUM THERMAL     1    B (A**2):   1059 ;  4.56 ;  2.00           
REMARK   3   MEDIUM THERMAL     1    C (A**2):   1059 ;  5.89 ;  2.00           
REMARK   3   MEDIUM THERMAL     1    D (A**2):   1059 ;  5.63 ;  2.00           
REMARK   3   MEDIUM THERMAL     1    E (A**2):   1059 ;  6.70 ;  2.00           
REMARK   3   MEDIUM THERMAL     1    F (A**2):   1059 ;  6.01 ;  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    -2        A   166                          
REMARK   3    ORIGIN FOR THE GROUP (A): -13.8902  14.2160 -10.2099              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0879 T22:   0.0672                                     
REMARK   3      T33:   0.0304 T12:   0.0178                                     
REMARK   3      T13:   0.0018 T23:  -0.0228                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2077 L22:   1.5279                                     
REMARK   3      L33:   1.2490 L12:  -0.2539                                     
REMARK   3      L13:   0.5596 L23:   0.1709                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0469 S12:  -0.0035 S13:   0.1670                       
REMARK   3      S21:  -0.0266 S22:  -0.0463 S23:   0.0156                       
REMARK   3      S31:  -0.0903 S32:   0.0446 S33:   0.0932                       
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    -2        B   166                          
REMARK   3    ORIGIN FOR THE GROUP (A): -42.2120  17.9809 -44.6444              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0952 T22:   0.0497                                     
REMARK   3      T33:   0.0425 T12:   0.0392                                     
REMARK   3      T13:   0.0241 T23:   0.0316                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1553 L22:   1.3696                                     
REMARK   3      L33:   1.4854 L12:  -0.5062                                     
REMARK   3      L13:  -0.3255 L23:   0.4285                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0857 S12:   0.0387 S13:  -0.0572                       
REMARK   3      S21:   0.1530 S22:   0.0795 S23:  -0.0099                       
REMARK   3      S31:   0.0978 S32:   0.0241 S33:   0.0062                       
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    -2        C   166                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -7.4064 -21.1416 -11.6370              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0892 T22:   0.0697                                     
REMARK   3      T33:   0.0204 T12:  -0.0171                                     
REMARK   3      T13:   0.0052 T23:  -0.0071                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6481 L22:   3.1235                                     
REMARK   3      L33:   1.5524 L12:   0.0372                                     
REMARK   3      L13:  -0.0388 L23:   0.5744                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1068 S12:   0.0135 S13:  -0.0601                       
REMARK   3      S21:  -0.0108 S22:  -0.1555 S23:   0.1084                       
REMARK   3      S31:   0.0810 S32:  -0.1644 S33:   0.0487                       
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    -2        D   166                          
REMARK   3    ORIGIN FOR THE GROUP (A): -10.3502  16.4464 -44.0337              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0482 T22:   0.0678                                     
REMARK   3      T33:   0.1338 T12:  -0.0170                                     
REMARK   3      T13:  -0.0565 T23:   0.0405                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.3229 L22:   1.5146                                     
REMARK   3      L33:   2.2469 L12:  -1.5719                                     
REMARK   3      L13:   0.5386 L23:  -0.0427                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1976 S12:   0.3195 S13:   0.3311                       
REMARK   3      S21:   0.0809 S22:  -0.0081 S23:   0.0013                       
REMARK   3      S31:  -0.1798 S32:   0.1513 S33:   0.2057                       
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 :   E    -2        E   166                          
REMARK   3    ORIGIN FOR THE GROUP (A): -45.9430  15.6412  -9.4843              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0503 T22:   0.0458                                     
REMARK   3      T33:   0.0997 T12:   0.0004                                     
REMARK   3      T13:   0.0182 T23:   0.0426                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.7431 L22:   1.7409                                     
REMARK   3      L33:   1.5761 L12:  -1.4547                                     
REMARK   3      L13:  -0.6513 L23:   0.5865                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2777 S12:   0.1166 S13:  -0.3711                       
REMARK   3      S21:  -0.0197 S22:   0.1402 S23:   0.3679                       
REMARK   3      S31:   0.0917 S32:   0.0948 S33:   0.1375                       
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 :   F    -2        F   166                          
REMARK   3    ORIGIN FOR THE GROUP (A): -50.3924  50.2935  -8.9127              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0554 T22:   0.0534                                     
REMARK   3      T33:   0.0843 T12:  -0.0098                                     
REMARK   3      T13:  -0.0019 T23:   0.0471                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5204 L22:   2.2972                                     
REMARK   3      L33:   1.2614 L12:  -0.6744                                     
REMARK   3      L13:   0.5222 L23:   0.1825                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1009 S12:   0.1569 S13:   0.1134                       
REMARK   3      S21:  -0.1511 S22:  -0.1342 S23:  -0.1282                       
REMARK   3      S31:  -0.0221 S32:   0.1521 S33:   0.0333                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3   POSITIONS.                                                         
REMARK   4                                                                      
REMARK   4 4AQ3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 12-APR-12.                  
REMARK 100 THE PDBE ID CODE IS EBI-52041.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 17-FEB-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID23-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.07200                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD (QUANTUM 315)                  
REMARK 200  DETECTOR MANUFACTURER          : ADSC                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 58071                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.40                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.00                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.0                                
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.8                               
REMARK 200  DATA REDUNDANCY                : 3.4                                
REMARK 200  R MERGE                    (I) : 0.08                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 14.20                              
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.49                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 88.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.7                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.58                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.80                               
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: INTERNAL STRUCTURE                                   
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 47                                        
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.3                      
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32                             
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                                                                      
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       68.21200            
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       34.10600            
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 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 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 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 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 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: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E                                     
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: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: F                                     
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     ALA A     2                                                      
REMARK 465     HIS A     3                                                      
REMARK 465     ALA A     4                                                      
REMARK 465     GLY A     5                                                      
REMARK 465     ARG A     6                                                      
REMARK 465     THR A     7                                                      
REMARK 465     GLY A     8                                                      
REMARK 465     ALA A    32                                                      
REMARK 465     GLY A    33                                                      
REMARK 465     ASP A    34                                                      
REMARK 465     ASP A    35                                                      
REMARK 465     VAL A    36                                                      
REMARK 465     GLU A    37                                                      
REMARK 465     GLU A    38                                                      
REMARK 465     ASN A    39                                                      
REMARK 465     ARG A    40                                                      
REMARK 465     THR A    41                                                      
REMARK 465     GLU A    42                                                      
REMARK 465     ALA A    43                                                      
REMARK 465     PRO A    44                                                      
REMARK 465     GLU A    45                                                      
REMARK 465     GLY A    46                                                      
REMARK 465     THR A    47                                                      
REMARK 465     GLU A    48                                                      
REMARK 465     SER A    49                                                      
REMARK 465     GLU A    50                                                      
REMARK 465     PRO A   163                                                      
REMARK 465     SER A   164                                                      
REMARK 465     MET A   165                                                      
REMARK 465     ARG A   166                                                      
REMARK 465     GLY B    -2                                                      
REMARK 465     SER B    -1                                                      
REMARK 465     HIS B     0                                                      
REMARK 465     MET B     1                                                      
REMARK 465     ALA B     2                                                      
REMARK 465     HIS B     3                                                      
REMARK 465     ALA B     4                                                      
REMARK 465     GLY B     5                                                      
REMARK 465     ARG B     6                                                      
REMARK 465     THR B     7                                                      
REMARK 465     GLY B     8                                                      
REMARK 465     ALA B    32                                                      
REMARK 465     GLY B    33                                                      
REMARK 465     ASP B    34                                                      
REMARK 465     ASP B    35                                                      
REMARK 465     VAL B    36                                                      
REMARK 465     GLU B    37                                                      
REMARK 465     GLU B    38                                                      
REMARK 465     ASN B    39                                                      
REMARK 465     ARG B    40                                                      
REMARK 465     THR B    41                                                      
REMARK 465     GLU B    42                                                      
REMARK 465     ALA B    43                                                      
REMARK 465     PRO B    44                                                      
REMARK 465     GLU B    45                                                      
REMARK 465     GLY B    46                                                      
REMARK 465     THR B    47                                                      
REMARK 465     GLU B    48                                                      
REMARK 465     SER B    49                                                      
REMARK 465     GLU B    50                                                      
REMARK 465     PRO B   163                                                      
REMARK 465     SER B   164                                                      
REMARK 465     MET B   165                                                      
REMARK 465     ARG B   166                                                      
REMARK 465     GLY C    -2                                                      
REMARK 465     SER C    -1                                                      
REMARK 465     HIS C     0                                                      
REMARK 465     MET C     1                                                      
REMARK 465     ALA C     2                                                      
REMARK 465     HIS C     3                                                      
REMARK 465     ALA C     4                                                      
REMARK 465     GLY C     5                                                      
REMARK 465     ARG C     6                                                      
REMARK 465     THR C     7                                                      
REMARK 465     GLY C     8                                                      
REMARK 465     ALA C    32                                                      
REMARK 465     GLY C    33                                                      
REMARK 465     ASP C    34                                                      
REMARK 465     ASP C    35                                                      
REMARK 465     VAL C    36                                                      
REMARK 465     GLU C    37                                                      
REMARK 465     GLU C    38                                                      
REMARK 465     ASN C    39                                                      
REMARK 465     ARG C    40                                                      
REMARK 465     THR C    41                                                      
REMARK 465     GLU C    42                                                      
REMARK 465     ALA C    43                                                      
REMARK 465     PRO C    44                                                      
REMARK 465     GLU C    45                                                      
REMARK 465     GLY C    46                                                      
REMARK 465     THR C    47                                                      
REMARK 465     GLU C    48                                                      
REMARK 465     SER C    49                                                      
REMARK 465     GLU C    50                                                      
REMARK 465     PRO C   163                                                      
REMARK 465     SER C   164                                                      
REMARK 465     MET C   165                                                      
REMARK 465     ARG C   166                                                      
REMARK 465     GLY D    -2                                                      
REMARK 465     SER D    -1                                                      
REMARK 465     HIS D     0                                                      
REMARK 465     MET D     1                                                      
REMARK 465     ALA D     2                                                      
REMARK 465     HIS D     3                                                      
REMARK 465     ALA D     4                                                      
REMARK 465     GLY D     5                                                      
REMARK 465     ARG D     6                                                      
REMARK 465     THR D     7                                                      
REMARK 465     GLY D     8                                                      
REMARK 465     ALA D    32                                                      
REMARK 465     GLY D    33                                                      
REMARK 465     ASP D    34                                                      
REMARK 465     ASP D    35                                                      
REMARK 465     VAL D    36                                                      
REMARK 465     GLU D    37                                                      
REMARK 465     GLU D    38                                                      
REMARK 465     ASN D    39                                                      
REMARK 465     ARG D    40                                                      
REMARK 465     THR D    41                                                      
REMARK 465     GLU D    42                                                      
REMARK 465     ALA D    43                                                      
REMARK 465     PRO D    44                                                      
REMARK 465     GLU D    45                                                      
REMARK 465     GLY D    46                                                      
REMARK 465     THR D    47                                                      
REMARK 465     GLU D    48                                                      
REMARK 465     PRO D   163                                                      
REMARK 465     SER D   164                                                      
REMARK 465     MET D   165                                                      
REMARK 465     ARG D   166                                                      
REMARK 465     GLY E    -2                                                      
REMARK 465     SER E    -1                                                      
REMARK 465     HIS E     0                                                      
REMARK 465     MET E     1                                                      
REMARK 465     ALA E     2                                                      
REMARK 465     HIS E     3                                                      
REMARK 465     ALA E     4                                                      
REMARK 465     GLY E     5                                                      
REMARK 465     ARG E     6                                                      
REMARK 465     THR E     7                                                      
REMARK 465     GLY E     8                                                      
REMARK 465     TYR E     9                                                      
REMARK 465     GLY E    33                                                      
REMARK 465     ASP E    34                                                      
REMARK 465     ASP E    35                                                      
REMARK 465     VAL E    36                                                      
REMARK 465     GLU E    37                                                      
REMARK 465     GLU E    38                                                      
REMARK 465     ASN E    39                                                      
REMARK 465     ARG E    40                                                      
REMARK 465     THR E    41                                                      
REMARK 465     GLU E    42                                                      
REMARK 465     ALA E    43                                                      
REMARK 465     PRO E    44                                                      
REMARK 465     GLU E    45                                                      
REMARK 465     GLY E    46                                                      
REMARK 465     THR E    47                                                      
REMARK 465     GLU E    48                                                      
REMARK 465     SER E    49                                                      
REMARK 465     GLU E    50                                                      
REMARK 465     PRO E   163                                                      
REMARK 465     SER E   164                                                      
REMARK 465     MET E   165                                                      
REMARK 465     ARG E   166                                                      
REMARK 465     GLY F    -2                                                      
REMARK 465     SER F    -1                                                      
REMARK 465     HIS F     0                                                      
REMARK 465     MET F     1                                                      
REMARK 465     ALA F     2                                                      
REMARK 465     HIS F     3                                                      
REMARK 465     ALA F     4                                                      
REMARK 465     GLY F     5                                                      
REMARK 465     ARG F     6                                                      
REMARK 465     THR F     7                                                      
REMARK 465     GLY F     8                                                      
REMARK 465     GLY F    33                                                      
REMARK 465     ASP F    34                                                      
REMARK 465     ASP F    35                                                      
REMARK 465     VAL F    36                                                      
REMARK 465     GLU F    37                                                      
REMARK 465     GLU F    38                                                      
REMARK 465     ASN F    39                                                      
REMARK 465     ARG F    40                                                      
REMARK 465     THR F    41                                                      
REMARK 465     GLU F    42                                                      
REMARK 465     ALA F    43                                                      
REMARK 465     PRO F    44                                                      
REMARK 465     GLU F    45                                                      
REMARK 465     GLY F    46                                                      
REMARK 465     THR F    47                                                      
REMARK 465     GLU F    48                                                      
REMARK 465     SER F    49                                                      
REMARK 465     PRO F   163                                                      
REMARK 465     SER F   164                                                      
REMARK 465     MET F   165                                                      
REMARK 465     ARG F   166                                                      
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   OH   TYR A    18     OE2  GLU A   111              2.13            
REMARK 500   OE1  GLU A    94     NH2  ARG A    98              2.17            
REMARK 500   OH   TYR C     9     OD1  ASP C   155              2.09            
REMARK 500   OH   TYR C    18     OE2  GLU C   111              1.94            
REMARK 500   OH   TYR D    18     OE2  GLU D   111              2.18            
REMARK 500   OH   TYR E    18     OE2  GLU E   111              2.01            
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    TRP A 147   CD2   TRP A 147   CE2     0.073                       
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    ARG C  66   NE  -  CZ  -  NH2 ANGL. DEV. =   3.2 DEGREES          
REMARK 500    ASP D  61   CB  -  CG  -  OD1 ANGL. DEV. =   5.7 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    GLU A 159       27.14    -66.75                                   
REMARK 500    LEU A 160      -63.50   -121.11                                   
REMARK 500    GLN B  25      -42.56    -27.51                                   
REMARK 500    GLN C  25      -38.39    -33.03                                   
REMARK 500    GLU D  50      -47.94     68.94                                   
REMARK 500    TYR D 161     -164.24    103.64                                   
REMARK 500    HIS E  79       71.18     36.33                                   
REMARK 500    ASP F  31       89.14    -63.24                                   
REMARK 500    ASP F  99       24.38    -79.10                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 TYR D    9     ASP D   10                  143.78                    
REMARK 500 TYR F    9     ASP F   10                 -144.50                    
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 398 A1163                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 398 B1163                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 398 C1163                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 398 D1163                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 398 E1163                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 398 F1163                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1BXL   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF BCL-XL/BAK PEPTIDE COMPLEX, NMR,                       
REMARK 900  MINIMIZED AVERAGE STRUCTURE                                         
REMARK 900 RELATED ID: 1G5J   RELATED DB: PDB                                   
REMARK 900  COMPLEX OF BCL-XL WITH PEPTIDE FROM BAD                             
REMARK 900 RELATED ID: 1G5M   RELATED DB: PDB                                   
REMARK 900  HUMAN BCL-2, ISOFORM 1                                              
REMARK 900 RELATED ID: 1GJH   RELATED DB: PDB                                   
REMARK 900  HUMAN BCL-2, ISOFORM 2                                              
REMARK 900 RELATED ID: 1LXL   RELATED DB: PDB                                   
REMARK 900  NMR STRUCTURE OF BCL-XL, AN INHIBITOR OF PROGRAMMED                 
REMARK 900  CELL DEATH, MINIMIZED AVERAGE STRUCTURE                             
REMARK 900 RELATED ID: 1MAZ   RELATED DB: PDB                                   
REMARK 900  X-RAY STRUCTURE OF BCL-XL, AN INHIBITOR OF                          
REMARK 900  PROGRAMMED CELL DEATH                                               
REMARK 900 RELATED ID: 1R2D   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF HUMAN BCL-XL AT 1.95 ANGSTROMS                         
REMARK 900 RELATED ID: 1R2E   RELATED DB: PDB                                   
REMARK 900  HUMAN BCL-XL CONTAINING A GLU TO LEU MUTATION AT                    
REMARK 900  POSITION 92                                                         
REMARK 900 RELATED ID: 1R2G   RELATED DB: PDB                                   
REMARK 900  HUMAN BCL-XL CONTAINING A PHE TO TRP MUTATION AT                    
REMARK 900  POSITION 97                                                         
REMARK 900 RELATED ID: 1R2H   RELATED DB: PDB                                   
REMARK 900  HUMAN BCL-XL CONTAINING AN ALA TO LEU MUTATION AT                   
REMARK 900  POSITION142                                                         
REMARK 900 RELATED ID: 1R2I   RELATED DB: PDB                                   
REMARK 900  HUMAN BCL-XL CONTAINING A PHE TO LEU MUTATION AT                    
REMARK 900  POSITION146                                                         
REMARK 900 RELATED ID: 1YSG   RELATED DB: PDB                                   
REMARK 900  SOLUTION STRUCTURE OF THE ANTI-APOPTOTIC PROTEIN BCL-               
REMARK 900  XL INCOMPLEX WITH "SAR BY NMR" LIGANDS                              
REMARK 900 RELATED ID: 1YSI   RELATED DB: PDB                                   
REMARK 900  SOLUTION STRUCTURE OF THE ANTI-APOPTOTIC PROTEIN BCL-               
REMARK 900  XL INCOMPLEX WITH AN ACYL-SULFONAMIDE-BASED LIGAND                  
REMARK 900 RELATED ID: 1YSN   RELATED DB: PDB                                   
REMARK 900  SOLUTION STRUCTURE OF THE ANTI-APOPTOTIC PROTEIN BCL-               
REMARK 900  XLCOMPLEXED WITH AN ACYL-SULFONAMIDE-BASED LIGAND                   
REMARK 900 RELATED ID: 1YSW   RELATED DB: PDB                                   
REMARK 900  SOLUTION STRUCTURE OF THE ANTI-APOPTOTIC PROTEIN BCL-               
REMARK 900  2COMPLEXED WITH AN ACYL-SULFONAMIDE-BASED LIGAND                    
REMARK 900 RELATED ID: 2B48   RELATED DB: PDB                                   
REMARK 900  BCL-XL 3D DOMAIN SWAPPED DIMER                                      
REMARK 900 RELATED ID: 2W3L   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF CHIMAERIC BCL2-XL AND PHENYL                   
REMARK 900  TETRAHYDROISOQUINOLINE AMIDE COMPLEX                                
REMARK 900 RELATED ID: 2XA0   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF BCL-2 IN COMPLEX WITH A BAX                    
REMARK 900  BH3 PEPTIDE                                                         
REMARK 900 RELATED ID: 2YJ1   RELATED DB: PDB                                   
REMARK 900  PUMA BH3 FOLDAMER IN COMPLEX WITH BCL-XL                            
REMARK 900 RELATED ID: 4A1U   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF ALPHA-BETA-FOLDAMER 2C IN COMPLEX              
REMARK 900   WITH BCL-XL                                                        
REMARK 900 RELATED ID: 4A1W   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF ALPHA-BETA FOLDAMER 4C IN COMPLEX              
REMARK 900   WITH BCL-XL                                                        
DBREF  4AQ3 A    1    33  UNP    P10415   BCL2_HUMAN       1     33             
DBREF  4AQ3 A   35    50  UNP    Q07817   BCLX_HUMAN      29     44             
DBREF  4AQ3 A   51   166  UNP    P10415   BCL2_HUMAN      92    207             
DBREF  4AQ3 B    1    33  UNP    P10415   BCL2_HUMAN       1     33             
DBREF  4AQ3 B   35    50  UNP    Q07817   BCLX_HUMAN      29     44             
DBREF  4AQ3 B   51   166  UNP    P10415   BCL2_HUMAN      92    207             
DBREF  4AQ3 C    1    33  UNP    P10415   BCL2_HUMAN       1     33             
DBREF  4AQ3 C   35    50  UNP    Q07817   BCLX_HUMAN      29     44             
DBREF  4AQ3 C   51   166  UNP    P10415   BCL2_HUMAN      92    207             
DBREF  4AQ3 D    1    33  UNP    P10415   BCL2_HUMAN       1     33             
DBREF  4AQ3 D   35    50  UNP    Q07817   BCLX_HUMAN      29     44             
DBREF  4AQ3 D   51   166  UNP    P10415   BCL2_HUMAN      92    207             
DBREF  4AQ3 E    1    33  UNP    P10415   BCL2_HUMAN       1     33             
DBREF  4AQ3 E   35    50  UNP    Q07817   BCLX_HUMAN      29     44             
DBREF  4AQ3 E   51   166  UNP    P10415   BCL2_HUMAN      92    207             
DBREF  4AQ3 F    1    33  UNP    P10415   BCL2_HUMAN       1     33             
DBREF  4AQ3 F   35    50  UNP    Q07817   BCLX_HUMAN      29     44             
DBREF  4AQ3 F   51   166  UNP    P10415   BCL2_HUMAN      92    207             
SEQADV 4AQ3 GLY A   -2  UNP  P10415              EXPRESSION TAG                 
SEQADV 4AQ3 SER A   -1  UNP  P10415              EXPRESSION TAG                 
SEQADV 4AQ3 HIS A    0  UNP  P10415              EXPRESSION TAG                 
SEQADV 4AQ3 ASP A   34  UNP  P10415              EXPRESSION TAG                 
SEQADV 4AQ3 ALA A   55  UNP  P10415    THR    96 VARIANT                        
SEQADV 4AQ3 GLY A   69  UNP  P10415    ARG   110 VARIANT                        
SEQADV 4AQ3 GLY B   -2  UNP  P10415              EXPRESSION TAG                 
SEQADV 4AQ3 SER B   -1  UNP  P10415              EXPRESSION TAG                 
SEQADV 4AQ3 HIS B    0  UNP  P10415              EXPRESSION TAG                 
SEQADV 4AQ3 ASP B   34  UNP  P10415              EXPRESSION TAG                 
SEQADV 4AQ3 ALA B   55  UNP  P10415    THR    96 VARIANT                        
SEQADV 4AQ3 GLY B   69  UNP  P10415    ARG   110 VARIANT                        
SEQADV 4AQ3 GLY C   -2  UNP  P10415              EXPRESSION TAG                 
SEQADV 4AQ3 SER C   -1  UNP  P10415              EXPRESSION TAG                 
SEQADV 4AQ3 HIS C    0  UNP  P10415              EXPRESSION TAG                 
SEQADV 4AQ3 ASP C   34  UNP  P10415              EXPRESSION TAG                 
SEQADV 4AQ3 ALA C   55  UNP  P10415    THR    96 VARIANT                        
SEQADV 4AQ3 GLY C   69  UNP  P10415    ARG   110 VARIANT                        
SEQADV 4AQ3 GLY D   -2  UNP  P10415              EXPRESSION TAG                 
SEQADV 4AQ3 SER D   -1  UNP  P10415              EXPRESSION TAG                 
SEQADV 4AQ3 HIS D    0  UNP  P10415              EXPRESSION TAG                 
SEQADV 4AQ3 ASP D   34  UNP  P10415              EXPRESSION TAG                 
SEQADV 4AQ3 ALA D   55  UNP  P10415    THR    96 VARIANT                        
SEQADV 4AQ3 GLY D   69  UNP  P10415    ARG   110 VARIANT                        
SEQADV 4AQ3 GLY E   -2  UNP  P10415              EXPRESSION TAG                 
SEQADV 4AQ3 SER E   -1  UNP  P10415              EXPRESSION TAG                 
SEQADV 4AQ3 HIS E    0  UNP  P10415              EXPRESSION TAG                 
SEQADV 4AQ3 ASP E   34  UNP  P10415              EXPRESSION TAG                 
SEQADV 4AQ3 ALA E   55  UNP  P10415    THR    96 VARIANT                        
SEQADV 4AQ3 GLY E   69  UNP  P10415    ARG   110 VARIANT                        
SEQADV 4AQ3 GLY F   -2  UNP  P10415              EXPRESSION TAG                 
SEQADV 4AQ3 SER F   -1  UNP  P10415              EXPRESSION TAG                 
SEQADV 4AQ3 HIS F    0  UNP  P10415              EXPRESSION TAG                 
SEQADV 4AQ3 ASP F   34  UNP  P10415              EXPRESSION TAG                 
SEQADV 4AQ3 ALA F   55  UNP  P10415    THR    96 VARIANT                        
SEQADV 4AQ3 GLY F   69  UNP  P10415    ARG   110 VARIANT                        
SEQRES   1 A  169  GLY SER HIS MET ALA HIS ALA GLY ARG THR GLY TYR ASP          
SEQRES   2 A  169  ASN ARG GLU ILE VAL MET LYS TYR ILE HIS TYR LYS LEU          
SEQRES   3 A  169  SER GLN ARG GLY TYR GLU TRP ASP ALA GLY ASP ASP VAL          
SEQRES   4 A  169  GLU GLU ASN ARG THR GLU ALA PRO GLU GLY THR GLU SER          
SEQRES   5 A  169  GLU VAL VAL HIS LEU ALA LEU ARG GLN ALA GLY ASP ASP          
SEQRES   6 A  169  PHE SER ARG ARG TYR ARG GLY ASP PHE ALA GLU MET SER          
SEQRES   7 A  169  SER GLN LEU HIS LEU THR PRO PHE THR ALA ARG GLY ARG          
SEQRES   8 A  169  PHE ALA THR VAL VAL GLU GLU LEU PHE ARG ASP GLY VAL          
SEQRES   9 A  169  ASN TRP GLY ARG ILE VAL ALA PHE PHE GLU PHE GLY GLY          
SEQRES  10 A  169  VAL MET CYS VAL GLU SER VAL ASN ARG GLU MET SER PRO          
SEQRES  11 A  169  LEU VAL ASP ASN ILE ALA LEU TRP MET THR GLU TYR LEU          
SEQRES  12 A  169  ASN ARG HIS LEU HIS THR TRP ILE GLN ASP ASN GLY GLY          
SEQRES  13 A  169  TRP ASP ALA PHE VAL GLU LEU TYR GLY PRO SER MET ARG          
SEQRES   1 B  169  GLY SER HIS MET ALA HIS ALA GLY ARG THR GLY TYR ASP          
SEQRES   2 B  169  ASN ARG GLU ILE VAL MET LYS TYR ILE HIS TYR LYS LEU          
SEQRES   3 B  169  SER GLN ARG GLY TYR GLU TRP ASP ALA GLY ASP ASP VAL          
SEQRES   4 B  169  GLU GLU ASN ARG THR GLU ALA PRO GLU GLY THR GLU SER          
SEQRES   5 B  169  GLU VAL VAL HIS LEU ALA LEU ARG GLN ALA GLY ASP ASP          
SEQRES   6 B  169  PHE SER ARG ARG TYR ARG GLY ASP PHE ALA GLU MET SER          
SEQRES   7 B  169  SER GLN LEU HIS LEU THR PRO PHE THR ALA ARG GLY ARG          
SEQRES   8 B  169  PHE ALA THR VAL VAL GLU GLU LEU PHE ARG ASP GLY VAL          
SEQRES   9 B  169  ASN TRP GLY ARG ILE VAL ALA PHE PHE GLU PHE GLY GLY          
SEQRES  10 B  169  VAL MET CYS VAL GLU SER VAL ASN ARG GLU MET SER PRO          
SEQRES  11 B  169  LEU VAL ASP ASN ILE ALA LEU TRP MET THR GLU TYR LEU          
SEQRES  12 B  169  ASN ARG HIS LEU HIS THR TRP ILE GLN ASP ASN GLY GLY          
SEQRES  13 B  169  TRP ASP ALA PHE VAL GLU LEU TYR GLY PRO SER MET ARG          
SEQRES   1 C  169  GLY SER HIS MET ALA HIS ALA GLY ARG THR GLY TYR ASP          
SEQRES   2 C  169  ASN ARG GLU ILE VAL MET LYS TYR ILE HIS TYR LYS LEU          
SEQRES   3 C  169  SER GLN ARG GLY TYR GLU TRP ASP ALA GLY ASP ASP VAL          
SEQRES   4 C  169  GLU GLU ASN ARG THR GLU ALA PRO GLU GLY THR GLU SER          
SEQRES   5 C  169  GLU VAL VAL HIS LEU ALA LEU ARG GLN ALA GLY ASP ASP          
SEQRES   6 C  169  PHE SER ARG ARG TYR ARG GLY ASP PHE ALA GLU MET SER          
SEQRES   7 C  169  SER GLN LEU HIS LEU THR PRO PHE THR ALA ARG GLY ARG          
SEQRES   8 C  169  PHE ALA THR VAL VAL GLU GLU LEU PHE ARG ASP GLY VAL          
SEQRES   9 C  169  ASN TRP GLY ARG ILE VAL ALA PHE PHE GLU PHE GLY GLY          
SEQRES  10 C  169  VAL MET CYS VAL GLU SER VAL ASN ARG GLU MET SER PRO          
SEQRES  11 C  169  LEU VAL ASP ASN ILE ALA LEU TRP MET THR GLU TYR LEU          
SEQRES  12 C  169  ASN ARG HIS LEU HIS THR TRP ILE GLN ASP ASN GLY GLY          
SEQRES  13 C  169  TRP ASP ALA PHE VAL GLU LEU TYR GLY PRO SER MET ARG          
SEQRES   1 D  169  GLY SER HIS MET ALA HIS ALA GLY ARG THR GLY TYR ASP          
SEQRES   2 D  169  ASN ARG GLU ILE VAL MET LYS TYR ILE HIS TYR LYS LEU          
SEQRES   3 D  169  SER GLN ARG GLY TYR GLU TRP ASP ALA GLY ASP ASP VAL          
SEQRES   4 D  169  GLU GLU ASN ARG THR GLU ALA PRO GLU GLY THR GLU SER          
SEQRES   5 D  169  GLU VAL VAL HIS LEU ALA LEU ARG GLN ALA GLY ASP ASP          
SEQRES   6 D  169  PHE SER ARG ARG TYR ARG GLY ASP PHE ALA GLU MET SER          
SEQRES   7 D  169  SER GLN LEU HIS LEU THR PRO PHE THR ALA ARG GLY ARG          
SEQRES   8 D  169  PHE ALA THR VAL VAL GLU GLU LEU PHE ARG ASP GLY VAL          
SEQRES   9 D  169  ASN TRP GLY ARG ILE VAL ALA PHE PHE GLU PHE GLY GLY          
SEQRES  10 D  169  VAL MET CYS VAL GLU SER VAL ASN ARG GLU MET SER PRO          
SEQRES  11 D  169  LEU VAL ASP ASN ILE ALA LEU TRP MET THR GLU TYR LEU          
SEQRES  12 D  169  ASN ARG HIS LEU HIS THR TRP ILE GLN ASP ASN GLY GLY          
SEQRES  13 D  169  TRP ASP ALA PHE VAL GLU LEU TYR GLY PRO SER MET ARG          
SEQRES   1 E  169  GLY SER HIS MET ALA HIS ALA GLY ARG THR GLY TYR ASP          
SEQRES   2 E  169  ASN ARG GLU ILE VAL MET LYS TYR ILE HIS TYR LYS LEU          
SEQRES   3 E  169  SER GLN ARG GLY TYR GLU TRP ASP ALA GLY ASP ASP VAL          
SEQRES   4 E  169  GLU GLU ASN ARG THR GLU ALA PRO GLU GLY THR GLU SER          
SEQRES   5 E  169  GLU VAL VAL HIS LEU ALA LEU ARG GLN ALA GLY ASP ASP          
SEQRES   6 E  169  PHE SER ARG ARG TYR ARG GLY ASP PHE ALA GLU MET SER          
SEQRES   7 E  169  SER GLN LEU HIS LEU THR PRO PHE THR ALA ARG GLY ARG          
SEQRES   8 E  169  PHE ALA THR VAL VAL GLU GLU LEU PHE ARG ASP GLY VAL          
SEQRES   9 E  169  ASN TRP GLY ARG ILE VAL ALA PHE PHE GLU PHE GLY GLY          
SEQRES  10 E  169  VAL MET CYS VAL GLU SER VAL ASN ARG GLU MET SER PRO          
SEQRES  11 E  169  LEU VAL ASP ASN ILE ALA LEU TRP MET THR GLU TYR LEU          
SEQRES  12 E  169  ASN ARG HIS LEU HIS THR TRP ILE GLN ASP ASN GLY GLY          
SEQRES  13 E  169  TRP ASP ALA PHE VAL GLU LEU TYR GLY PRO SER MET ARG          
SEQRES   1 F  169  GLY SER HIS MET ALA HIS ALA GLY ARG THR GLY TYR ASP          
SEQRES   2 F  169  ASN ARG GLU ILE VAL MET LYS TYR ILE HIS TYR LYS LEU          
SEQRES   3 F  169  SER GLN ARG GLY TYR GLU TRP ASP ALA GLY ASP ASP VAL          
SEQRES   4 F  169  GLU GLU ASN ARG THR GLU ALA PRO GLU GLY THR GLU SER          
SEQRES   5 F  169  GLU VAL VAL HIS LEU ALA LEU ARG GLN ALA GLY ASP ASP          
SEQRES   6 F  169  PHE SER ARG ARG TYR ARG GLY ASP PHE ALA GLU MET SER          
SEQRES   7 F  169  SER GLN LEU HIS LEU THR PRO PHE THR ALA ARG GLY ARG          
SEQRES   8 F  169  PHE ALA THR VAL VAL GLU GLU LEU PHE ARG ASP GLY VAL          
SEQRES   9 F  169  ASN TRP GLY ARG ILE VAL ALA PHE PHE GLU PHE GLY GLY          
SEQRES  10 F  169  VAL MET CYS VAL GLU SER VAL ASN ARG GLU MET SER PRO          
SEQRES  11 F  169  LEU VAL ASP ASN ILE ALA LEU TRP MET THR GLU TYR LEU          
SEQRES  12 F  169  ASN ARG HIS LEU HIS THR TRP ILE GLN ASP ASN GLY GLY          
SEQRES  13 F  169  TRP ASP ALA PHE VAL GLU LEU TYR GLY PRO SER MET ARG          
HET    398  A1163      53                                                       
HET    398  B1163      53                                                       
HET    398  C1163      53                                                       
HET    398  D1163      53                                                       
HET    398  E1163      53                                                       
HET    398  F1163      53                                                       
HETNAM     398 N,N-DIBUTYL-4-CHLORANYL-1-[2-(3,4-DIHYDRO-1H-                    
HETNAM   2 398  ISOQUINOLIN-2-YLCARBONYL)-4-[(7-                                
HETNAM   3 398  IODANYLNAPHTHALEN-2-YL)SULFONYLCARBAMOYL]PHENYL]-5-METHYL-      
HETNAM   4 398  PYRAZOLE-3-CARBOXAMIDE                                          
FORMUL   7  398    6(C40 H41 CL I N5 O5 S)                                      
HELIX    1   1 ASP A   10  ARG A   26  1                                  17    
HELIX    2   2 VAL A   51  TYR A   67  1                                  17    
HELIX    3   3 TYR A   67  LEU A   78  1                                  12    
HELIX    4   4 THR A   84  PHE A   97  1                                  14    
HELIX    5   5 ASN A  102  ARG A  123  1                                  22    
HELIX    6   6 PRO A  127  LEU A  144  1                                  18    
HELIX    7   7 LEU A  144  ASN A  151  1                                   8    
HELIX    8   8 GLY A  152  GLU A  159  1                                   8    
HELIX    9   9 ASP B   10  ARG B   26  1                                  17    
HELIX   10  10 VAL B   51  TYR B   67  1                                  17    
HELIX   11  11 TYR B   67  LEU B   78  1                                  12    
HELIX   12  12 THR B   84  PHE B   97  1                                  14    
HELIX   13  13 ASN B  102  ARG B  123  1                                  22    
HELIX   14  14 PRO B  127  HIS B  143  1                                  17    
HELIX   15  15 LEU B  144  ASN B  151  1                                   8    
HELIX   16  16 GLY B  152  GLY B  162  1                                  11    
HELIX   17  17 ASP C   10  ARG C   26  1                                  17    
HELIX   18  18 VAL C   51  TYR C   67  1                                  17    
HELIX   19  19 TYR C   67  LEU C   78  1                                  12    
HELIX   20  20 THR C   84  ARG C   98  1                                  15    
HELIX   21  21 ASN C  102  ARG C  123  1                                  22    
HELIX   22  22 PRO C  127  LEU C  144  1                                  18    
HELIX   23  23 LEU C  144  ASN C  151  1                                   8    
HELIX   24  24 GLY C  153  GLY C  162  1                                  10    
HELIX   25  25 ASP D   10  GLN D   25  1                                  16    
HELIX   26  26 GLU D   50  TYR D   67  1                                  18    
HELIX   27  27 TYR D   67  GLN D   77  1                                  11    
HELIX   28  28 THR D   84  PHE D   97  1                                  14    
HELIX   29  29 ASN D  102  ARG D  123  1                                  22    
HELIX   30  30 PRO D  127  LEU D  144  1                                  18    
HELIX   31  31 LEU D  144  ASN D  151  1                                   8    
HELIX   32  32 GLY D  152  LEU D  160  1                                   9    
HELIX   33  33 ASP E   10  ARG E   26  1                                  17    
HELIX   34  34 VAL E   51  TYR E   67  1                                  17    
HELIX   35  35 TYR E   67  GLN E   77  1                                  11    
HELIX   36  36 THR E   84  ARG E   98  1                                  15    
HELIX   37  37 ASN E  102  ARG E  123  1                                  22    
HELIX   38  38 SER E  126  LEU E  144  1                                  19    
HELIX   39  39 LEU E  144  ASN E  151  1                                   8    
HELIX   40  40 GLY E  152  GLY E  162  1                                  11    
HELIX   41  41 ASP F   10  GLN F   25  1                                  16    
HELIX   42  42 GLU F   50  TYR F   67  1                                  18    
HELIX   43  43 TYR F   67  SER F   76  1                                  10    
HELIX   44  44 THR F   84  PHE F   97  1                                  14    
HELIX   45  45 ASN F  102  ARG F  123  1                                  22    
HELIX   46  46 PRO F  127  LEU F  144  1                                  18    
HELIX   47  47 LEU F  144  ASN F  151  1                                   8    
HELIX   48  48 GLY F  152  GLY F  162  1                                  11    
CISPEP   1 TYR F  161    GLY F  162          0       -29.13                     
SITE     1 AC1 10 TYR A  67  ASP A  70  MET A  74  GLU A  95                    
SITE     2 AC1 10 LEU A  96  ARG A 105  GLN E  58  LEU E 160                    
SITE     3 AC1 10 TYR E 161  GLY E 162                                          
SITE     1 AC2 15 PHE B  63  TYR B  67  ASP B  70  PHE B  71                    
SITE     2 AC2 15 MET B  74  VAL B  92  GLU B  95  GLY B 104                    
SITE     3 AC2 15 ALA B 108  PHE B 112  TYR B 161  GLN D  58                    
SITE     4 AC2 15 TYR D 161  GLY D 162  PRO E  82                               
SITE     1 AC3 11 PHE C  63  TYR C  67  ASP C  70  MET C  74                    
SITE     2 AC3 11 GLU C  95  LEU C  96  TYR C 161  PRO D  82                    
SITE     3 AC3 11 GLN F  58  TYR F 161  GLY F 162                               
SITE     1 AC4 11 PRO A  82  GLN B  58  LEU B 160  TYR B 161                    
SITE     2 AC4 11 GLY B 162  PHE D  63  TYR D  67  ASP D  70                    
SITE     3 AC4 11 MET D  74  GLU D  95  ALA D 108                               
SITE     1 AC5 11 GLN A  58  LEU A 160  TYR A 161  GLY A 162                    
SITE     2 AC5 11 PHE E  63  TYR E  67  ASP E  70  MET E  74                    
SITE     3 AC5 11 VAL E  92  GLU E  95  ALA E 108                               
SITE     1 AC6 11 PHE B  83  GLN C  58  LEU C 160  TYR C 161                    
SITE     2 AC6 11 GLY C 162  PHE F  63  TYR F  67  ASP F  70                    
SITE     3 AC6 11 VAL F  92  GLU F  95  ALA F 108                               
CRYST1  115.214  115.214  102.318  90.00  90.00 120.00 P 32         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      0.008680  0.005011  0.000000        0.00000                         
SCALE2      0.000000  0.010022  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009773        0.00000                         
MTRIX1   1  1.000000  0.000000  0.000000        0.00000    1                    
MTRIX2   1  0.000000  1.000000  0.000000        0.00000    1                    
MTRIX3   1  0.000000  0.000000  1.000000        0.00000    1                    
MTRIX1   2 -0.999896 -0.002574 -0.014206      -56.68136    1                    
MTRIX2   2  0.004890 -0.986189 -0.165554       24.74994    1                    
MTRIX3   2 -0.013583 -0.165606  0.986098       36.21980    1                    
MTRIX1   3 -0.501065  0.860651 -0.090629       -0.46102    1                    
MTRIX2   3 -0.833152 -0.508062 -0.218473       -5.25083    1                    
MTRIX3   3 -0.234074 -0.033961  0.971625       -1.35637    1                    
MTRIX1   4  0.998112 -0.011743  0.060290       -0.82415    1                    
MTRIX2   4  0.011612  0.999929  0.002517       -1.77654    1                    
MTRIX3   4 -0.060316 -0.001812  0.998178       33.11996    1                    
MTRIX1   5 -0.999594 -0.006045  0.027859      -59.37437    1                    
MTRIX2   5  0.002596 -0.992501 -0.122213       28.60782    1                    
MTRIX3   5  0.028389 -0.122091  0.992113        2.53127    1                    
MTRIX1   6  0.477377 -0.870284  0.121313       54.98487    1                    
MTRIX2   6  0.870083  0.487455  0.073092       34.36977    1                    
MTRIX3   6 -0.122745  0.070660  0.989920      -11.18358    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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